|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
306-829 |
2.93e-139 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 422.94 E-value: 2.93e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 306 LEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRA------LSIPPNIDVLLCEQEVVADET-PAVQ 378
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELepdsgeVSIPKGLRIGYLPQEPPLDDDlTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 379 AVLRADTKRLKLLEEERRLQGQLEQGDDtAAERLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRM 458
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAEPDE-DLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 459 RVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQRLHYYRGNYMTFkk 538
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAY-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 539 mYQQKQKELLKQyekqekklkelkaggksTKQAEKQTKE--------------ALTRKQQKCRRKNQDE-ESQEAPellk 603
Cdd:COG0488 238 -LEQRAERLEQE-----------------AAAYAKQQKKiakeeefirrfrakARKAKQAQSRIKALEKlEREEPP---- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 604 rPKEYTVRFTFPDPPPLSPPVLGLHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMR 683
Cdd:COG0488 296 -RRDKTVEIRFPPPERLGKKVLELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 684 KNHRLKIGFFNQQYaEQLRMEETPTEYLQRGF-NLPYQDARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPD 762
Cdd:COG0488 374 LGETVKIGYFDQHQ-EELDPDKTVLDELRDGApGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPN 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 69354671 763 VLILDEPTNNLDIESIDALGEAINEYKGAVIVVSHDARLITETNCQLWVVEEQSVSQIDGDFEDYKR 829
Cdd:COG0488 453 VLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
264-829 |
1.86e-135 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 420.04 E-value: 1.86e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 264 QMEYERQVASLKAANAAENDFSVSQAEMSSRQAmlenASDIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKT 343
Cdd:PLN03073 142 EVQYQAHVAEMEAAKAGMPGVYVNHDGNGGGPA----IKDIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKT 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 344 TLLKHIANRALS-IPPNIDVLLCEQEVVADETPAVQAVLRADTKRLKLLEEERRL--------------QGQLEQGD--- 405
Cdd:PLN03073 218 TFLRYMAMHAIDgIPKNCQILHVEQEVVGDDTTALQCVLNTDIERTQLLEEEAQLvaqqrelefetetgKGKGANKDgvd 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 406 -DTAAERLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDL 484
Cdd:PLN03073 298 kDAVSQRLEEIYKRLELIDAYTAEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 485 NAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQRLHYYRGNYMTFKKMYQQKQKELLKQYEKQEKKLKELKA- 563
Cdd:PLN03073 378 HAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAf 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 564 ------GGKSTKQAEKQTKeALTRKQQKCRRKNQDEESQEAPELLKRPKEYTVRFTfpdppplsppvlglhGVTFGYQGQ 637
Cdd:PLN03073 458 idkfryNAKRASLVQSRIK-ALDRLGHVDAVVNDPDYKFEFPTPDDRPGPPIISFS---------------DASFGYPGG 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 638 KPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRLKIGFFNQQYAEQLRMEETPTEYLQRGF-N 716
Cdd:PLN03073 522 PLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFpG 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 717 LPYQDARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKGAVIVVS 796
Cdd:PLN03073 602 VPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVS 681
|
570 580 590
....*....|....*....|....*....|...
gi 69354671 797 HDARLITETNCQLWVVEEQSVSQIDGDFEDYKR 829
Cdd:PLN03073 682 HDEHLISGSVDELWVVSEGKVTPFHGTFHDYKK 714
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
318-829 |
1.06e-79 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 270.12 E-value: 1.06e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 318 LFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANR------ALSIPPNIDVLLCEQEVVADETPAVQAVLRADTKRLKLl 391
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEisadggSYTFPGNWQLAWVNQETPALPQPALEYVIDGDREYRQL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 392 eeERRLQGQLEQGDDTAaerLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPT 471
Cdd:PRK10636 95 --EAQLHDANERNDGHA---IATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 472 LLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQRLHYYRGNYMTFKK-----------MY 540
Cdd:PRK10636 170 LLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVqratrlaqqqaMY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 541 QQKQKEL--LKQYEKQEKklkelkagGKSTKQaekqtkealtrKQQKCRRKNQDEESQEAPELLKRPkeytVRFTFPDPP 618
Cdd:PRK10636 250 ESQQERVahLQSYIDRFR--------AKATKA-----------KQAQSRIKMLERMELIAPAHVDNP----FHFSFRAPE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 619 PLSPPVLGLHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRLKIGFFNQQYA 698
Cdd:PRK10636 307 SLPNPLLKMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 699 EQLRMEETPTEYLQR-GFNLPYQDARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIES 777
Cdd:PRK10636 386 EFLRADESPLQHLARlAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 69354671 778 IDALGEAINEYKGAVIVVSHDARLITETNCQLWVVEEQSVSQIDGDFEDYKR 829
Cdd:PRK10636 466 RQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQ 517
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
316-827 |
2.22e-60 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 213.99 E-value: 2.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 316 KELFVNADLYIVAGRRYGLVGPNGKGKTTLLKhIANRAL-------SIPPNIDVLLCEQEVVADETPAV-QAVLRADTKR 387
Cdd:PRK15064 14 KPLFENISVKFGGGNRYGLIGANGCGKSTFMK-ILGGDLepsagnvSLDPNERLGKLRQDQFAFEEFTVlDTVIMGHTEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 388 LKLLEEERRLQGQLEQGDD---TAAErLEKVYEELRATGAAAAEAKarrILAGLGFDPEMQNRPTQKFSGGWRMRVSLAR 464
Cdd:PRK15064 93 WEVKQERDRIYALPEMSEEdgmKVAD-LEVKFAEMDGYTAEARAGE---LLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 465 ALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQRLHYYRGNYMTFKKMYQQKQ 544
Cdd:PRK15064 169 ALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMTAATQAR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 545 KELLKQYEKqekklkelkaggKSTKQAEKQT------------KEALTRKQQKcrRKNQDEE----SQEAPELlkrpkey 608
Cdd:PRK15064 249 ERLLADNAK------------KKAQIAELQSfvsrfsanaskaKQATSRAKQI--DKIKLEEvkpsSRQNPFI------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 609 tvrfTFPDPPPLSPPVLGLHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRL 688
Cdd:PRK15064 308 ----RFEQDKKLHRNALEVENLTKGF-DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 689 KIGFFNQQYAEQLRMEETPTEYL----QRGFNlpYQDARKCLGR--FGLESHAHTIQICklSGGQKARVVFAELACREPD 762
Cdd:PRK15064 383 NIGYYAQDHAYDFENDLTLFDWMsqwrQEGDD--EQAVRGTLGRllFSQDDIKKSVKVL--SGGEKGRMLFGKLMMQKPN 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 69354671 763 VLILDEPTNNLDIESIDALGEAINEYKGAVIVVSHDARLITETNCQLWVVEEQSVSQIDGDFEDY 827
Cdd:PRK15064 459 VLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEY 523
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
315-837 |
3.26e-49 |
|
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: 182.83 E-value: 3.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 315 GKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIA------NRALSIPPNIDVLLCEQEVVADETPAVQ-------AVL 381
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAgvdkdfNGEARPQPGIKVGYLPQEPQLDPTKTVRenveegvAEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 382 RADTKRL---------------KLLEEERRLQGQLEQGDDTAAER-LEKVYEELRAtgaaaaeakarrilaglgfdPEmQ 445
Cdd:TIGR03719 97 KDALDRFneisakyaepdadfdKLAAEQAELQEIIDAADAWDLDSqLEIAMDALRC--------------------PP-W 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 446 NRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQR 525
Cdd:TIGR03719 156 DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 526 LHYYRGNYMTFkkmYQQKQKELLKQyekqekklkelkagGKSTKQAEKQTKEAL--TRKQQKCRRKNQDEESQEAPELLK 603
Cdd:TIGR03719 236 GIPWEGNYSSW---LEQKQKRLEQE--------------EKEESARQKTLKRELewVRQSPKGRQAKSKARLARYEELLS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 604 rpKEYTVRFTFPDPPPLSPPVLG-----LHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPT 678
Cdd:TIGR03719 299 --QEFQKRNETAEIYIPPGPRLGdkvieAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 679 HGEMRKNHRLKIGffnqqYAEQLRMEETP-----------TEYLQRG-FNLPyqdARKCLGRFGLESHAHTIQICKLSGG 746
Cdd:TIGR03719 376 SGTIEIGETVKLA-----YVDQSRDALDPnktvweeisggLDIIKLGkREIP---SRAYVGRFNFKGSDQQKKVGQLSGG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 747 QKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKGAVIVVSHDA----RLITetncQLWVVEEQS-VSQID 821
Cdd:TIGR03719 448 ERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRwfldRIAT----HILAFEGDShVEWFE 523
|
570
....*....|....*.
gi 69354671 822 GDFEDYKREVLEALGE 837
Cdd:TIGR03719 524 GNFSEYEEDKKRRLGE 539
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
304-525 |
6.50e-47 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 163.77 E-value: 6.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVllceqevvadetpavqavlra 383
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 384 dTKRLKLleeerrlqGQLEQgddtaaerlekvyeelratgaaaaeakarrilaglgfdpemqnrptqkFSGGWRMRVSLA 463
Cdd:cd03221 60 -GSTVKI--------GYFEQ------------------------------------------------LSGGEKMRLALA 82
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 69354671 464 RALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQR 525
Cdd:cd03221 83 KLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
318-813 |
1.20e-46 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 177.06 E-value: 1.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 318 LFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANralsippniDVLLCEQEVVAdETPAVQAVLRADTKR---------- 387
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG---------EVLLDDGRIIY-EQDLIVARLQQDPPRnvegtvydfv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 388 -------LKLLEEERRLQGQLEQG-DDTAAERLEKVYEELRATGAAAAEAKARRILAGLGFDPEMqnrPTQKFSGGWRMR 459
Cdd:PRK11147 88 aegieeqAEYLKRYHDISHLVETDpSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDA---ALSSLSGGWLRK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 460 VSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQRLHYYRGNYmtfkKM 539
Cdd:PRK11147 165 AALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNY----DQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 540 YQQKQKELLKQyekqekklkelkaggKSTKQAEKQTK----EALTRKQQKCRR----------KNQDEESQEapellKRP 605
Cdd:PRK11147 241 YLLEKEEALRV---------------EELQNAEFDRKlaqeEVWIRQGIKARRtrnegrvralKALRRERSE-----RRE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 606 KEYTVRFTFPDPPPLSPPVLGLHGVTFGYQGqKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKN 685
Cdd:PRK11147 301 VMGTAKMQVEEASRSGKIVFEMENVNYQIDG-KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 686 HRLKIGFFNqQYAEQLRMEETPTEYLQRGfnlpYQD------ARKCLGRFG--LESHAHTIQICK-LSGGQKARVVFAEL 756
Cdd:PRK11147 380 TKLEVAYFD-QHRAELDPEKTVMDNLAEG----KQEvmvngrPRHVLGYLQdfLFHPKRAMTPVKaLSGGERNRLLLARL 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 69354671 757 ACREPDVLILDEPTNNLDIESIDALGEAINEYKGAVIVVSHDARLITETNCQLWVVE 813
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFE 511
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
627-815 |
2.03e-40 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 145.28 E-value: 2.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRLKIGFFNQqyaeqlrmeet 706
Cdd:cd03221 3 LENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 707 pteylqrgfnlpyqdarkclgrfgleshahtiqickLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAIN 786
Cdd:cd03221 71 ------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALK 114
|
170 180
....*....|....*....|....*....
gi 69354671 787 EYKGAVIVVSHDARLITETNCQLWVVEEQ 815
Cdd:cd03221 115 EYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
333-837 |
1.20e-38 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 151.81 E-value: 1.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 333 GLVGPNGKGKTTLLKHIA------NRALSIPPNIDVLLCEQEVVADETPAV-----QAVlrADTKRL------------- 388
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAgvdkefEGEARPAPGIKVGYLPQEPQLDPEKTVrenveEGV--AEVKAAldrfneiyaayae 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 389 ------KLLEEERRLQGQLEQGD----DTaaeRLEKVYEELRAtgaaaaeakarrilaglgfdPEMqNRPTQKFSGGWRM 458
Cdd:PRK11819 115 pdadfdALAAEQGELQEIIDAADawdlDS---QLEIAMDALRC--------------------PPW-DAKVTKLSGGERR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 459 RVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQRLHYYRGNYMTFkk 538
Cdd:PRK11819 171 RVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSW-- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 539 mYQQKQKELLKQyekqekklkelkagGKSTKQAEKQTKEAL--TRKQQKCRR-KN----------QDEESQEAPELL--- 602
Cdd:PRK11819 249 -LEQKAKRLAQE--------------EKQEAARQKALKRELewVRQSPKARQaKSkarlaryeelLSEEYQKRNETNeif 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 603 ----KRpkeytvrftfpdpppLSPPVLGLHGVTFGYqGQKPLFKNLDF-----GIdmdsrICIVGPNGVGKSTLLLLLTG 673
Cdd:PRK11819 314 ippgPR---------------LGDKVIEAENLSKSF-GDRLLIDDLSFslppgGI-----VGIIGPNGAGKSTLFKMITG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 674 KLTPTHGEMRKNHRLKIGffnqqYAEQLR--MEETPT---------EYLQRG-FNLPyqdARKCLGRFGLESHAHTIQIC 741
Cdd:PRK11819 373 QEQPDSGTIKIGETVKLA-----YVDQSRdaLDPNKTvweeisgglDIIKVGnREIP---SRAYVGRFNFKGGDQQKKVG 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 742 KLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKGAVIVVSHDA----RLIT-----ETNCQlwvv 812
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRwfldRIAThilafEGDSQ---- 520
|
570 580
....*....|....*....|....*
gi 69354671 813 eeqsVSQIDGDFEDYKREVLEALGE 837
Cdd:PRK11819 521 ----VEWFEGNFQEYEEDKKRRLGA 541
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
284-533 |
6.84e-37 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 145.98 E-value: 6.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 284 FSVSQAEMSSRQAmlenasdIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRalsippnidvl 363
Cdd:COG0488 303 IRFPPPERLGKKV-------LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGE----------- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 364 lceqevvadetpavqavLRADTKRLKL---------------LEEERRlqgqleqgddtaaerlekVYEELRATGAAAAE 428
Cdd:COG0488 365 -----------------LEPDSGTVKLgetvkigyfdqhqeeLDPDKT------------------VLDELRDGAPGGTE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 429 AKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQ 508
Cdd:COG0488 410 QEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDR 489
|
250 260
....*....|....*....|....*
gi 69354671 509 GFLDDVCTDIIHLDAQRLHYYRGNY 533
Cdd:COG0488 490 YFLDRVATRILEFEDGGVREYPGGY 514
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
304-526 |
1.10e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 117.22 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANraLsIPPNI-DVLLCEQEVvaDETPAVQavLR 382
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALAD--L-DPPTSgEIYLDGKPL--SAMPPPE--WR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 383 adtKRLKLLEEERRLqgqleqGDDTAAERLEKVYEelrATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSL 462
Cdd:COG4619 74 ---RQVAYVPQEPAL------WGGTVRDNLPFPFQ---LRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 463 ARALFMEPTLLMLDEPTNHLDLN---AVI-WLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQRL 526
Cdd:COG4619 142 IRALLLQPDVLLLDEPTSALDPEntrRVEeLLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
305-525 |
1.11e-25 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 103.86 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 305 KLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANraLSIPPNIDVLLCEQEVvadetpavqavlrad 384
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAG--LLKPTSGEILIDGKDI--------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 385 tkRLKLLEEERRLQGQLEQgddtaaerlekvyeelratgaaaaeakarrilaglgfdpemqnrptqkFSGGWRMRVSLAR 464
Cdd:cd00267 64 --AKLPLEELRRRIGYVPQ------------------------------------------------LSGGQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 69354671 465 ALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK---TLLIVSHDQGFLDDVCTDIIHLDAQR 525
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
304-528 |
1.13e-24 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 103.78 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNidvllcEQEVVADETPAVQAVLRA 383
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAG---LLKPD------SGSILIDGEDVRKEPREA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 384 DtKRLKLLEEERRLQGQLeqgddTAAERLEkVYEELRATGAAAAEAKARRILAGLGFDPEMqNRPTQKFSGGWRMRVSLA 463
Cdd:COG4555 73 R-RQIGVLPDERGLYDRL-----TVRENIR-YFAELYGLFDEELKKRIEELIELLGLEEFL-DRRVGELSTGMKKKVALA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 464 RALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR---KTLLIVSHDQGFLDDVCTDIIHLDAQRLHY 528
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRALKkegKTVLFSSHIMQEVEALCDRVVILHKGKVVA 212
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
624-805 |
1.08e-23 |
|
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: 99.86 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 624 VLGLHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKS---------TLLLlltgkltptHGEMRKNHRlKIGFFN 694
Cdd:COG4133 2 MLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTtllrilaglLPPS---------AGEVLWNGE-PIRDAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 695 QQYAEQLRM---------EETPTEYLQ-----RGFNLPYQDARKCLGRFGLESHAHTiQICKLSGGQKARVVFAELACRE 760
Cdd:COG4133 71 EDYRRRLAYlghadglkpELTVRENLRfwaalYGLRADREAIDEALEAVGLAGLADL-PVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 69354671 761 PDVLILDEPTNNLDIESIDALGEAINEYK---GAVIVVSHDARLITET 805
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAA 197
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
321-526 |
1.22e-23 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 98.62 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIANraLSIPPNIDVLLCEQEVVADETPAVqavlradtKRLKLLEEERRLQGQ 400
Cdd:cd03230 18 DISLTVEKGEIYGLLGPNGAGKTTLIKIILG--LLKPDSGEIKVLGKDIKKEPEEVK--------RRIGYLPEEPSLYEN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 401 LeqgddTAAERLekvyeelratgaaaaeakarrilaglgfdpemqnrptqKFSGGWRMRVSLARALFMEPTLLMLDEPTN 480
Cdd:cd03230 88 L-----TVRENL--------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 69354671 481 HLDLNAVIWLNNYLQGWR---KTLLIVSHDQGFLDDVCTDIIHLDAQRL 526
Cdd:cd03230 125 GLDPESRREFWELLRELKkegKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
624-798 |
1.49e-23 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 100.55 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 624 VLGLHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKS------------TllllltgkltptHGEMR------KN 685
Cdd:COG1121 6 AIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKStllkailgllppT------------SGTVRlfgkppRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 686 HRLKIGFFNQQYAEQLRMEETPTE------YLQRGFNLPY-----QDARKCLGRFGLESHAHTiQICKLSGGQKARVVFA 754
Cdd:COG1121 73 ARRRIGYVPQRAEVDWDFPITVRDvvlmgrYGRRGLFRRPsradrEAVDEALERVGLEDLADR-PIGELSGGQQQRVLLA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 69354671 755 ELACREPDVLILDEPTNNLDIESIDALGEAINEYKG---AVIVVSHD 798
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHD 198
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
627-804 |
8.83e-23 |
|
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: 97.22 E-value: 8.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMR------KNHRLKIGFFNQQY--- 697
Cdd:cd03235 2 VEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRRsid 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 698 -------AEQLRMeetpTEYLQRGFNLPYQDARKC-----LGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLI 765
Cdd:cd03235 81 rdfpisvRDVVLM----GLYGHKGLFRRLSKADKAkvdeaLERVGLSELADR-QIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 69354671 766 LDEPTNNLDIESIDALGEAINEYKG---AVIVVSHDARLITE 804
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLE 197
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
321-480 |
9.09e-23 |
|
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: 95.41 E-value: 9.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVADETPAVQavlradtKRLKLLEEERRLQGQ 400
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIA--GLLSPTEGTILLDGQDLTDDERKSLR-------KEIGYVFQDPQLFPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 401 LeqgddTAAERLeKVYEELRATGAAAAEAKARRILAGLG---FDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDE 477
Cdd:pfam00005 74 L-----TVRENL-RLGLLLKGLSKREKDARAEEALEKLGlgdLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
...
gi 69354671 478 PTN 480
Cdd:pfam00005 148 PTA 150
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
321-526 |
1.03e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 97.83 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIANraLSIPPNIDVLLCEQEVVADEtpavQAVLRadtkRLKLLEEERRLQGQ 400
Cdd:COG1131 18 GVSLTVEPGEIFGLLGPNGAGKTTTIRMLLG--LLRPTSGEVRVLGEDVARDP----AEVRR----RIGYVPQEPALYPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 401 LeqgddTAAERLEkVYEELRATGAAAAEAKARRILAGLGFDpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTN 480
Cdd:COG1131 88 L-----TVRENLR-FFARLYGLPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 69354671 481 HLDLNAVIWLNNYLQGWR---KTLLIVSHDqgfLDDV---CTDIIHLDAQRL 526
Cdd:COG1131 161 GLDPEARRELWELLRELAaegKTVLLSTHY---LEEAerlCDRVAIIDKGRI 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
304-834 |
4.02e-22 |
|
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: 101.13 E-value: 4.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFV--NADLYIVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNIDVllcEQEVVADETPAVQAVL 381
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAvdGVSLTIAPGETVALVGESGSGKSTLALALMG---LLPHGGRI---SGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 382 RADTKRLKLLEEE-------RRLQGQ----LEQGDDTAAERLEKVYEelratgaaaaeakarrILAGLGFDPEMQNRPTQ 450
Cdd:COG1123 79 ALRGRRIGMVFQDpmtqlnpVTVGDQiaeaLENLGLSRAEARARVLE----------------LLEAVGLERRLDRYPHQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 451 kFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDL---NAVIWLNNYLQGWR-KTLLIVSHDQGFLDDVCTDIIHLDAQRL 526
Cdd:COG1123 143 -LSGGQRQRVAIAMALALDPDLLIADEPTTALDVttqAEILDLLRELQRERgTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 527 hyyrgnymtfkkmyqqkqkellkqyekqekklkelkaggkstkQAEKQTKEALTRKQQkcrrknqdeesqeapeLLKRPK 606
Cdd:COG1123 222 -------------------------------------------VEDGPPEEILAAPQA----------------LAAVPR 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 607 EYTVRFTFPDPPPLSPPVLGLHGVTFGYQGQKP-LFKNLDfGIDMD----SRICIVGPNGVGKS---------------- 665
Cdd:COG1123 243 LGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGKgGVRAVD-DVSLTlrrgETLGLVGESGSGKStlarlllgllrptsgs 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 666 --TLLLLLTGKLTPTHGEMRK-------------NHRLKIGffnQQYAEQLRM--EETPTEYLQRgfnlpyqdARKCLGR 728
Cdd:COG1123 322 ilFDGKDLTKLSRRSLRELRRrvqmvfqdpysslNPRMTVG---DIIAEPLRLhgLLSRAERRER--------VAELLER 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 729 FGLESHA-----HTiqickLSGGQKARVVFAE-LACrEPDVLILDEPTNNLDIeSI-----DALGEAINEYKGAVIVVSH 797
Cdd:COG1123 391 VGLPPDLadrypHE-----LSGGQRQRVAIARaLAL-EPKLLILDEPTSALDV-SVqaqilNLLRDLQRELGLTYLFISH 463
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 69354671 798 D---ARLITEtncQLWV------VEEQSVSQI-DGDFEDYKREVLEA 834
Cdd:COG1123 464 DlavVRYIAD---RVAVmydgriVEDGPTEEVfANPQHPYTRALLAA 507
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
627-804 |
9.94e-22 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 94.71 E-value: 9.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKS------------TLlllltgkltpthGEMR----------- 683
Cdd:COG1122 3 LENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKStllrllngllkpTS------------GEVLvdgkditkknl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 684 KNHRLKIGF-FnqQYAE-QLRMeetPTEY-------LQRGfnLPYQDARK----CLGRFGLESHAHTiQICKLSGGQKAR 750
Cdd:COG1122 71 RELRRKVGLvF--QNPDdQLFA---PTVEedvafgpENLG--LPREEIRErveeALELVGLEHLADR-PPHELSGGQKQR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 751 VVFAE-LACrEPDVLILDEPTNNLDIESIDALGEAINEYKGA---VIVVSHDARLITE 804
Cdd:COG1122 143 VAIAGvLAM-EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgktVIIVTHDLDLVAE 199
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
627-798 |
1.64e-21 |
|
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: 93.69 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGY-QGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMR-----------KNHRLKIGF-F 693
Cdd:cd03225 2 LKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLvdgkdltklslKELRRKVGLvF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 694 nqQYAE-QLRMEeTPTEYL---QRGFNLPYQDARK----CLGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLI 765
Cdd:cd03225 82 --QNPDdQFFGP-TVEEEVafgLENLGLPEEEIEErveeALELVGLEGLRDR-SPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 69354671 766 LDEPTNNLDIESIDALGEAINEYKGA---VIVVSHD 798
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEgktIIIVTHD 193
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
627-814 |
3.03e-21 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 92.57 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRknhrlkigFFNQQY----AEQLR 702
Cdd:COG4619 3 LEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIY--------LDGKPLsampPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 703 M------------EETPTEYLQRGFNL-----PYQDARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLI 765
Cdd:COG4619 74 RqvayvpqepalwGGTVRDNLPFPFQLrerkfDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 69354671 766 LDEPTNNLDIESIDALGEAINEYK----GAVIVVSHDARLITETNCQLWVVEE 814
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
304-528 |
3.04e-21 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 93.17 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSIS-AHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVADETPAV-QAV- 380
Cdd:COG1122 1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLN--GLLKPTSGEVLVDGKDITKKNLRELrRKVg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 381 ---------LRADT---------KRLKLLEEERRlqgqleqgddtaaERLEKVyeelratgaaaaeakarriLAGLGFDp 442
Cdd:COG1122 79 lvfqnpddqLFAPTveedvafgpENLGLPREEIR-------------ERVEEA-------------------LELVGLE- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 443 EMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR---KTLLIVSHDQGFLDDVCTDII 519
Cdd:COG1122 126 HLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNkegKTVIIVTHDLDLVAELADRVI 205
|
....*....
gi 69354671 520 HLDAQRLHY 528
Cdd:COG1122 206 VLDDGRIVA 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
304-525 |
7.02e-21 |
|
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: 91.77 E-value: 7.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLkhianRALS--IPPNI-DVLLCEQEVVADETPAVQAV 380
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLL-----RILAglLPPSAgEVLWNGEPIRDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 381 L----RADTKR-LKLLEE---ERRLQGqLEQGDDTAAERLEKVYeelratgaaaaeakarriLAGLgfdpemQNRPTQKF 452
Cdd:COG4133 78 AylghADGLKPeLTVRENlrfWAALYG-LRADREAIDEALEAVG------------------LAGL------ADLPVRQL 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 69354671 453 SGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK---TLLIVSHDQGFLDDVctDIIHLDAQR 525
Cdd:COG4133 133 SAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLArggAVLLTTHQPLELAAA--RVLDLGDFK 206
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
304-528 |
7.47e-21 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 92.46 E-value: 7.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANraLsIPP---NIDVLLCE-------------Q 367
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILG--L-LPPtsgTVRLFGKPprrarrrigyvpqR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 368 EVVADETPA-VQAV----LRADTKRLKLLEEERRlqgqleqgdDTAAERLEKVyeelratgaaaaeakarrilaGLGfdp 442
Cdd:COG1121 84 AEVDWDFPItVRDVvlmgRYGRRGLFRRPSRADR---------EAVDEALERV---------------------GLE--- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 443 EMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR---KTLLIVSHDQGFLDDVCTDII 519
Cdd:COG1121 131 DLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRregKTILVVTHDLGAVREYFDRVL 210
|
....*....
gi 69354671 520 HLDAQRLHY 528
Cdd:COG1121 211 LLNRGLVAH 219
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
303-526 |
1.26e-20 |
|
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: 92.18 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 303 DIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNidvllcEQEVVADETPAVQAVLR 382
Cdd:TIGR03873 1 GLRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAG---ALRPD------AGTVDLAGVDLHGLSRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 383 ADTKRLKLLEEERRLQGQLEQGDDTAAERLEkvYEELRATGAAAAEAKARRILAGLGFDpEMQNRPTQKFSGGWRMRVSL 462
Cdd:TIGR03873 72 ARARRVALVEQDSDTAVPLTVRDVVALGRIP--HRSLWAGDSPHDAAVVDRALARTELS-HLADRDMSTLSGGERQRVHV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 69354671 463 ARALFMEPTLLMLDEPTNHLDLNA---VIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQRL 526
Cdd:TIGR03873 149 ARALAQEPKLLLLDEPTNHLDVRAqleTLALVRELAATGVTVVAALHDLNLAASYCDHVVVLDGGRV 215
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
309-525 |
4.25e-20 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 89.45 E-value: 4.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 309 FSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVADET-------------P 375
Cdd:cd03225 7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLN--GLLGPTSGEVLVDGKDLTKLSLkelrrkvglvfqnP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 376 AVQAVlrADTkrlklLEEE-----RRLQgqleQGDDTAAERLEKVYEELratgaaaaeakarrilaGLGfdpEMQNRPTQ 450
Cdd:cd03225 85 DDQFF--GPT-----VEEEvafglENLG----LPEEEIEERVEEALELV-----------------GLE---GLRDRSPF 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 451 KFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR---KTLLIVSHDQGFLDDVCTDIIHLDAQR 525
Cdd:cd03225 134 TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKaegKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
627-798 |
7.12e-20 |
|
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: 87.88 E-value: 7.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLlllltgkltpthgemrknhrLKI--GFFNQQyAEQLRME 704
Cdd:cd03214 2 VENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTL--------------------LKTlaGLLKPS-SGEILLD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 705 ETPTEYLQrgfnlPYQDARK------CLGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDI--- 775
Cdd:cd03214 60 GKDLASLS-----PKELARKiayvpqALELLGLAHLADR-PFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIahq 133
|
170 180
....*....|....*....|....
gi 69354671 776 -ESIDALGEAINEYKGAVIVVSHD 798
Cdd:cd03214 134 iELLELLRRLARERGKTVVMVLHD 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
304-507 |
1.30e-19 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 89.33 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNI-DVLLCEQE-------------- 368
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAG---LLKPSSgEVLLDGRDlaslsrrelarria 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 369 VVADETPAV------QAVLRADTKRLKLLeeerrlqGQLEQGDDTAAER-LEKVyeelratgaaaaeakarrilaGLGfd 441
Cdd:COG1120 79 YVPQEPPAPfgltvrELVALGRYPHLGLF-------GRPSAEDREAVEEaLERT---------------------GLE-- 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 442 pEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR----KTLLIVSHD 507
Cdd:COG1120 129 -HLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLArergRTVVMVLHD 197
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
309-526 |
2.00e-19 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 88.71 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 309 FSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLkhianRALS--IPPNidvllcEQEVVADETPAVQAVLRADTK 386
Cdd:COG1124 11 YGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLL-----RALAglERPW------SGEVTFDGRPVTRRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 387 RL------------------KLLEEERRLQGQLEQgDDTAAERLEKVyeelratgaaaaeakarrilaglGFDPEMQNR- 447
Cdd:COG1124 80 RVqmvfqdpyaslhprhtvdRILAEPLRIHGLPDR-EERIAELLEQV-----------------------GLPPSFLDRy 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 448 PTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLN--AVIWlnNYLQGWRK----TLLIVSHDQGFLDDVCTDIIHL 521
Cdd:COG1124 136 PHQ-LSGGQRQRVAIARALILEPELLLLDEPTSALDVSvqAEIL--NLLKDLREerglTYLFVSHDLAVVAHLCDRVAVM 212
|
....*
gi 69354671 522 DAQRL 526
Cdd:COG1124 213 QNGRI 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
624-798 |
2.77e-19 |
|
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: 88.18 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 624 VLGLHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMR---KN-HRL-------KIGF 692
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgRDlASLsrrelarRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 693 FNQQY--AEQLRMEE------TPteYLQRGFNLPYQD---ARKCLGRFGLESHAHTiQICKLSGGQKARVVFAELACREP 761
Cdd:COG1120 80 VPQEPpaPFGLTVRElvalgrYP--HLGLFGRPSAEDreaVEEALERTGLEHLADR-PVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 69354671 762 DVLILDEPTNNLDI----ESIDALGEAINEYKGAVIVVSHD 798
Cdd:COG1120 157 PLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHD 197
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
305-507 |
2.90e-19 |
|
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: 85.95 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 305 KLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnRALSiPPNIDVLLCEQevvadetpavqavlraD 384
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLA-GLLK-PSSGEILLDGK----------------D 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 385 TKRLKLLEEERRLqGQLEQgddtAAERLEkvyeelratgaaaaeakarriLAGLGfdpemqNRPTQKFSGGWRMRVSLAR 464
Cdd:cd03214 63 LASLSPKELARKI-AYVPQ----ALELLG---------------------LAHLA------DRPFNELSGGERQRVLLAR 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 69354671 465 ALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR----KTLLIVSHD 507
Cdd:cd03214 111 ALAQEPPILLLDEPTSHLDIAHQIELLELLRRLArergKTVVMVLHD 157
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
627-804 |
5.27e-19 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 86.16 E-value: 5.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEM--------RKNHRLKIGFFNQQYA 698
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngkpikAKERRKSIGYVMQDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 699 EQLRMEETPTEYLQRGFNLP--YQDARKCLGRFGL----ESHAHTiqickLSGGQKARVVFAELACREPDVLILDEPTNN 772
Cdd:cd03226 82 YQLFTDSVREELLLGLKELDagNEQAETVLKDLDLyalkERHPLS-----LSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190
....*....|....*....|....*....|....*
gi 69354671 773 LDIESIDALGEAINEYKG---AVIVVSHDARLITE 804
Cdd:cd03226 157 LDYKNMERVGELIRELAAqgkAVIVITHDYEFLAK 191
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
292-533 |
1.57e-18 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 89.95 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 292 SSRQ----------AMLENAsdIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRalsIPP--- 358
Cdd:PRK15064 300 SSRQnpfirfeqdkKLHRNA--LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGE---LEPdsg 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 359 ------NIDVLLCEQEVVADetpavqavlradtkrlklLEEERRL---QGQLEQ-GDDTAAERlekvyeelratgaaaae 428
Cdd:PRK15064 375 tvkwseNANIGYYAQDHAYD------------------FENDLTLfdwMSQWRQeGDDEQAVR----------------- 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 429 akarRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQ 508
Cdd:PRK15064 420 ----GTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDR 495
|
250 260
....*....|....*....|....*
gi 69354671 509 GFLDDVCTDIIHLDAQRLHYYRGNY 533
Cdd:PRK15064 496 EFVSSLATRIIEITPDGVVDFSGTY 520
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
627-802 |
3.22e-18 |
|
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: 82.29 E-value: 3.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLlllltgkltpthgemrknhrLK-IGFFNQQYAEQLRMEE 705
Cdd:cd00267 2 IENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTL--------------------LRaIAGLLKPTSGEILIDG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 706 TPTEylqrgfNLPYQDARKCLG-RFGLeshahtiqicklSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEA 784
Cdd:cd00267 61 KDIA------KLPLEELRRRIGyVPQL------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEL 122
|
170 180
....*....|....*....|.
gi 69354671 785 INEYKG---AVIVVSHDARLI 802
Cdd:cd00267 123 LRELAEegrTVIIVTHDPELA 143
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
627-837 |
5.67e-18 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 84.14 E-value: 5.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYqGQKPLFKNLDFGIDmDSRI-CIVGPNGVGKSTLLLLLTGKLTPTHGEMRKN----------HRLKIGFFNQ 695
Cdd:COG4555 4 VENLSKKY-GKVPALKDVSFTAK-DGEItGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDgedvrkepreARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 696 QYAEQLRMeeTPTEYLQ---RGFNLPYQDARK----CLGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDE 768
Cdd:COG4555 82 ERGLYDRL--TVRENIRyfaELYGLFDEELKKrieeLIELLGLEEFLDR-RVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 769 PTNNLDIESIDALGEAINEYKG---AVIVVSHDARLITETnC-------QLWVVEEQSVSQID--GDFEDYKREVLEALG 836
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEAL-CdrvvilhKGKVVAQGSLDELReeIGEENLEDAFVALIG 237
|
.
gi 69354671 837 E 837
Cdd:COG4555 238 S 238
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
304-526 |
5.76e-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: 83.04 E-value: 5.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVADETPAvqavlra 383
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIIL--GLIKPDSGEITFDGKSYQKNIEAL------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 384 dtKRLKLLEEERRLQGQLeqgddTAAERLEkvyeeLRATGAAAAEAKARRILAGLGFDpEMQNRPTQKFSGGWRMRVSLA 463
Cdd:cd03268 72 --RRIGALIEAPGFYPNL-----TARENLR-----LLARLLGIRKKRIDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 69354671 464 RALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK---TLLIVSHDQGFLDDVCTDIIHLDAQRL 526
Cdd:cd03268 139 LALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDqgiTVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
305-529 |
6.85e-17 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 80.27 E-value: 6.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 305 KLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIA---------------------NRA------LSIP 357
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILgllkptsgsirvfgkplekerKRIgyvpqrRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 358 PN--IDVLlceqEVVAdetpavqavLRADTKRlklleeerRLQGQLEQGDDTAAER-LEKVyeelratgaaaaeakarri 434
Cdd:cd03235 81 RDfpISVR----DVVL---------MGLYGHK--------GLFRRLSKADKAKVDEaLERV------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 435 laGLGfdpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR---KTLLIVSHDQGFL 511
Cdd:cd03235 121 --GLS---ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRregMTILVVTHDLGLV 195
|
250
....*....|....*...
gi 69354671 512 DDVCTDIIHLDaQRLHYY 529
Cdd:cd03235 196 LEYFDRVLLLN-RTVVAS 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
304-523 |
6.85e-17 |
|
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: 79.15 E-value: 6.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVvadetpavqavlra 383
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIA--GLEEPDSGSILIDGEDL-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 384 DTKRLKLLEEERRL-----QGQLEQgddtaaeRLEkVYEelratgaaaaeakarRILAGLgfdpemqnrptqkfSGGWRM 458
Cdd:cd03229 65 TDLEDELPPLRRRIgmvfqDFALFP-------HLT-VLE---------------NIALGL--------------SGGQQQ 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 69354671 459 RVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR----KTLLIVSHDQGFLDDVCTDIIHLDA 523
Cdd:cd03229 108 RVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQaqlgITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
633-809 |
2.48e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.04 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 633 GYQGQkPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRLKIGFFNQQYAEQ----LRMEETPT 708
Cdd:NF040873 1 GYGGR-PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPdslpLTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 709 --EYLQRGFNLPY-QDAR----KCLGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDAL 781
Cdd:NF040873 80 mgRWARRGLWRRLtRDDRaavdDALERVGLADLAGR-QLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI 158
|
170 180 190
....*....|....*....|....*....|.
gi 69354671 782 GEAINEYKG---AVIVVSHDARLITETNCQL 809
Cdd:NF040873 159 IALLAEEHArgaTVVVVTHDLELVRRADPCV 189
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
323-528 |
2.75e-16 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 78.56 E-value: 2.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 323 DLYIVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNIDVLLCEQEVVADETPAVQAVL------RADTKRLKLLEEER- 395
Cdd:cd03266 25 SFTVKPGEVTGLLGPNGAGKTTTLRMLAG---LLEPDAGFATVDGFDVVKEPAEARRRLgfvsdsTGLYDRLTARENLEy 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 396 --RLQGQleQGDDTAAeRLEKVYEELRATgaaaaeakarrilaglgfdpEMQNRPTQKFSGGWRMRVSLARALFMEPTLL 473
Cdd:cd03266 102 faGLYGL--KGDELTA-RLEELADRLGME--------------------ELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 474 MLDEPTNHLDLNAVIWLNNYLQGWR---KTLLIVSHDQGFLDDVCTDIIHLDAQRLHY 528
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQLRalgKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
304-508 |
5.11e-16 |
|
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: 77.56 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQeVVADETPavqavlra 383
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIA--GLERPDSGEILIDGR-DVTGVPP-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 384 dtkrlklleeERRLQGQLEQGDD-----TAAE------RLEKVYEElratgaaAAEAKARRILAGLGFDPEMQNRPTQkF 452
Cdd:cd03259 70 ----------ERRNIGMVFQDYAlfphlTVAEniafglKLRGVPKA-------EIRARVRELLELVGLEGLLNRYPHE-L 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 453 SGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK----TLLIVSHDQ 508
Cdd:cd03259 132 SGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelgiTTIYVTHDQ 191
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
304-526 |
5.15e-16 |
|
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: 77.93 E-value: 5.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNA----DLYIVAGRRYGLVGPNGKGKTTLLKHIANraLSIPPNIDVLLCEQEVvadetpavqa 379
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKAlddvSFSIKKGETLGLVGESGSGKSTLARAILG--LLKPTSGSIIFDGKDL---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 380 vLRADTKRLKLLEEE---------------RRLQGQLE-----QGDDTAAERLEKVYEELratgaaaaeakarriLAGLG 439
Cdd:cd03257 70 -LKLSRRLRKIRRKEiqmvfqdpmsslnprMTIGEQIAeplriHGKLSKKEARKEAVLLL---------------LVGVG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 440 FDPEMQNR-PTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------LNAVIWLNNYLQgwrKTLLIVSHDQGFL 511
Cdd:cd03257 134 LPEEVLNRyPHE-LSGGQRQRVAIARALALNPKLLIADEPTSALDvsvqaqiLDLLKKLQEELG---LTLLFITHDLGVV 209
|
250
....*....|....*
gi 69354671 512 DDVCTDIIHLDAQRL 526
Cdd:cd03257 210 AKIADRVAVMYAGKI 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
627-798 |
5.40e-16 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 78.18 E-value: 5.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGE-------MRKNH---RLKIGFFNQQ 696
Cdd:COG1131 3 VRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEvrvlgedVARDPaevRRRIGYVPQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 697 YAeqLRMEETPTEYLQ---RGFNLPYQDARK----CLGRFGLESHAHTiQICKLSGGQKARVvfaELAC---REPDVLIL 766
Cdd:COG1131 82 PA--LYPDLTVRENLRffaRLYGLPRKEARErideLLELFGLTDAADR-KVGTLSGGMKQRL---GLALallHDPELLIL 155
|
170 180 190
....*....|....*....|....*....|....*
gi 69354671 767 DEPTNNLDIESIDALGEAINEYKG---AVIVVSHD 798
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAegkTVLLSTHY 190
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
324-526 |
9.66e-16 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 77.24 E-value: 9.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 324 LYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLceqevvaDETPAVQ---AVLRadtKRLKLLEEERRL-QG 399
Cdd:cd03245 25 LTIRAGEKVAIIGRVGSGKSTLLKLLA--GLYKPTSGSVLL-------DGTDIRQldpADLR---RNIGYVPQDVTLfYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 400 QLEQ--------GDDtaaERLEKVYEelratgaaaaeakarriLAGL---------GFDPEMQNRpTQKFSGGWRMRVSL 462
Cdd:cd03245 93 TLRDnitlgaplADD---ERILRAAE-----------------LAGVtdfvnkhpnGLDLQIGER-GRGLSGGQRQAVAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 69354671 463 ARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR--KTLLIVSHDQGFLdDVCTDIIHLDAQRL 526
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLgdKTLIIITHRPSLL-DLVDRIIVMDSGRI 216
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
641-771 |
2.32e-15 |
|
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: 73.84 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 641 FKNLDFGIDMDSRICIVGPNGVGKS-----------TLLLLLTGKLTPTHGEMRKNHRLKIGFFNQQyaEQLRMEETPTE 709
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKStllkliagllsPTEGTILLDGQDLTDDERKSLRKEIGYVFQD--PQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 69354671 710 YLQRGFNLPYQDARKC-------LGRFGLESHAHTI---QICKLSGGQKARVVFAELACREPDVLILDEPTN 771
Cdd:pfam00005 79 NLRLGLLLKGLSKREKdaraeeaLEKLGLGDLADRPvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
624-798 |
8.27e-15 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 75.09 E-value: 8.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 624 VLGLHGVTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKS---------------TLLLLLTGKLTPTHGEMRKnHRL 688
Cdd:COG3638 2 MLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKStllrclnglveptsgEILVDGQDVTALRGRALRR-LRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 689 KIGFFNQQYA--EQL---------RMEETPTeyLQRGFNLPYQD----ARKCLGRFGLESHAHtiQIC-KLSGGQKARVV 752
Cdd:COG3638 81 RIGMIFQQFNlvPRLsvltnvlagRLGRTST--WRSLLGLFPPEdrerALEALERVGLADKAY--QRAdQLSGGQQQRVA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 69354671 753 FAELACREPDVLILDEPTNNLDIES----IDALGEAINEYKGAVIVVSHD 798
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTarqvMDLLRRIAREDGITVVVNLHQ 206
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
629-801 |
1.28e-14 |
|
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: 73.68 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 629 GVTFGYQGQK---PLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMR---------KNHRL------KI 690
Cdd:cd03255 5 NLSKTYGGGGekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgtdisklSEKELaafrrrHI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 691 GFFNQQYA--------EQLRMeetPTEYLQRGFNLPYQDARKCLGRFGLESHAHTiQICKLSGGQKARVVFAE-LACrEP 761
Cdd:cd03255 85 GFVFQSFNllpdltalENVEL---PLLLAGVPKKERRERAEELLERVGLGDRLNH-YPSELSGGQQQRVAIARaLAN-DP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 69354671 762 DVLILDEPTNNLDIES----IDALGEaINEYKG-AVIVVSHDARL 801
Cdd:cd03255 160 KIILADEPTGNLDSETgkevMELLRE-LNKEAGtTIVVVTHDPEL 203
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
627-802 |
1.40e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 77.68 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRLKIGFFNQ----------- 695
Cdd:PRK11147 6 IHGAWLSF-SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQdpprnvegtvy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 696 --------QYAEQLR--------MEETPTEYL-------------QRGFNLpyqDAR--KCLGRFGLESHAhtiQICKLS 744
Cdd:PRK11147 85 dfvaegieEQAEYLKryhdishlVETDPSEKNlnelaklqeqldhHNLWQL---ENRinEVLAQLGLDPDA---ALSSLS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 745 GGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKGAVIVVSHDARLI 802
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFI 216
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
627-798 |
2.32e-14 |
|
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: 71.66 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLlllltgkltpthgemrknhrLKI--GFFNQQYAEQLRME 704
Cdd:cd03230 3 VRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTL--------------------IKIilGLLKPDSGEIKVLG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 705 ETPTEYlqrgfnlpYQDARKCLG----RFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDA 780
Cdd:cd03230 62 KDIKKE--------PEEVKRRIGylpeEPSLYENLTVRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRRE 133
|
170 180
....*....|....*....|.
gi 69354671 781 LGEAINEYK---GAVIVVSHD 798
Cdd:cd03230 134 FWELLRELKkegKTILLSSHI 154
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
627-826 |
2.45e-14 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 76.72 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNH-----------RLKIGFFNQ 695
Cdd:COG4988 339 LEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswRRQIAWVPQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 696 Q-Y------AEQLRM---EETPTE---------------YLQRGFNLPyqdarkcLGRFGLeshahtiqicKLSGGQKAR 750
Cdd:COG4988 419 NpYlfagtiRENLRLgrpDASDEEleaaleaagldefvaALPDGLDTP-------LGEGGR----------GLSGGQAQR 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 751 VVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKG--AVIVVSHDARLITETNcQLWVVEEQSVSQIdGDFED 826
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITHRLALLAQAD-RILVLDDGRIVEQ-GTHEE 557
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
272-526 |
3.35e-14 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 76.34 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 272 ASLKAANAAEN-----DFSVSQAEMSSRQAMLENASDIKLEKFSISAH-GKELFVNADLYIVAGRRYGLVGPNGKGKTTL 345
Cdd:COG4988 300 ARANGIAAAEKifallDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 346 LK-------------HIANRALS-IPP-----------------------NIdvLLCEQEvvADETpAVQAVLRadtkRL 388
Cdd:COG4988 380 LNlllgflppysgsiLINGVDLSdLDPaswrrqiawvpqnpylfagtireNL--RLGRPD--ASDE-ELEAALE----AA 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 389 KLLEEERRLQGQLeqgdDTA-AERlekvyeelratgaaaaeakarrilaGLGFdpemqnrptqkfSGGWRMRVSLARALF 467
Cdd:COG4988 451 GLDEFVAALPDGL----DTPlGEG-------------------------GRGL------------SGGQAQRLALARALL 489
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 69354671 468 MEPTLLMLDEPTNHLDLN--AVIW--LNNYLQGwrKTLLIVSHDQGFLDDvCTDIIHLDAQRL 526
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAEteAEILqaLRRLAKG--RTVILITHRLALLAQ-ADRILVLDDGRI 549
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
627-814 |
5.47e-14 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 70.49 E-value: 5.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYQGQ-KPLFKNLDFGIDMDSRICIVGPNGVGKSTLlllltgkltpthgemrknhrLKI--GFFnQQYAEQLRM 703
Cdd:cd03228 3 FKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTL--------------------LKLllRLY-DPTSGEILI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 704 EETPTEylqrgfNLPYQDARKclgRFGL---ESH--AHTIQ--IckLSGGQKARVVFAELACREPDVLILDEPTNNLDIE 776
Cdd:cd03228 62 DGVDLR------DLDLESLRK---NIAYvpqDPFlfSGTIRenI--LSGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 69354671 777 SIDALGEAINEYKG--AVIVVSHdaRLITETNC-QLWVVEE 814
Cdd:cd03228 131 TEALILEALRALAKgkTVIVIAH--RLSTIRDAdRIIVLDD 169
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
304-528 |
6.83e-14 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 71.46 E-value: 6.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRrYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVADETPAVQAV--- 380
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILA--TLTPPSSGTIRIDGQDVLKQPQKLRRRIgyl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 381 -----LRADTKRLKLLEEERRLQGQLEQGDDTAAER-LEKVyeelratgaaaaeakarrilaGLGfdpEMQNRPTQKFSG 454
Cdd:cd03264 78 pqefgVYPNFTVREFLDYIAWLKGIPSKEVKARVDEvLELV---------------------NLG---DRAKKKIGSLSG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 69354671 455 GWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQ--GWRKTLLIVSHDQGFLDDVCTDIIHLDAQRLHY 528
Cdd:cd03264 134 GMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSelGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVF 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
624-820 |
1.00e-13 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 74.55 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 624 VLGLHGVTFGY-QGQKPLFKNLDFGIDMDSRICIVGPNGVGKS---TLLLLLTGKLTPTHGEMRKNHR-----------L 688
Cdd:COG1123 4 LLEVRDLSVRYpGGDVPAVDGVSLTIAPGETVALVGESGSGKStlaLALMGLLPHGGRISGEVLLDGRdllelsealrgR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 689 KIGFFNQQYAEQL---RMEETPTEYLQRGfNLPYQDARK----CLGRFGLESHAHTiQICKLSGGQKARVVFAELACREP 761
Cdd:COG1123 84 RIGMVFQDPMTQLnpvTVGDQIAEALENL-GLSRAEARArvleLLEAVGLERRLDR-YPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 69354671 762 DVLILDEPTNNLD----IESIDALGEAINEYKGAVIVVSHDARLITETNCQLWV------VEEQSVSQI 820
Cdd:COG1123 162 DLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVmddgriVEDGPPEEI 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
323-514 |
1.34e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 69.96 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 323 DLYIVAGRRYGLVGPNGKGKTTLLKHIA----------NRALSIPPnidVLLCEQEVVADETPA--VQAVLRADTKRLKL 390
Cdd:NF040873 12 DLTIPAGSLTAVVGPNGSGKSTLLKVLAgvlrptsgtvRRAGGARV---AYVPQRSEVPDSLPLtvRDLVAMGRWARRGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 391 LeeeRRLQGQLEQGDDTAAERLEkvyeelratgaaaaeakarriLAGLGfdpemqNRPTQKFSGGWRMRVSLARALFMEP 470
Cdd:NF040873 89 W---RRLTRDDRAAVDDALERVG---------------------LADLA------GRQLGELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 69354671 471 TLLMLDEPTNHLDLNAVIWLNNYLQGWR---KTLLIVSHDqgfLDDV 514
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHargATVVVVTHD---LELV 182
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
304-526 |
1.86e-13 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 70.61 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALsIPPNIDVLLCEQEVVADETPAVQAVLRa 383
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIV--GL-LRPDSGEVLIDGEDISGLSEAELYRLR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 384 dtKRLKLLEEerrlQGQL---------------EQGDDTAAERLEKVYEELRatgaaaaeakarriLAGLGfdPEMQNRP 448
Cdd:cd03261 77 --RRMGMLFQ----SGALfdsltvfenvafplrEHTRLSEEEIREIVLEKLE--------------AVGLR--GAEDLYP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 449 TQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------LNAVIWLNNYLQgwrKTLLIVSHDQGFLDDVCTDIIHL 521
Cdd:cd03261 135 AE-LSGGMKKRVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLKKELG---LTSIMVTHDLDTAFAIADRIAVL 210
|
....*
gi 69354671 522 DAQRL 526
Cdd:cd03261 211 YDGKI 215
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
627-801 |
2.54e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 70.07 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYQ---GQKPLFKNLDFGIDMDSRICIVGPNGVGKS------------------TLLLLLTGKLTPTHGEMRKN 685
Cdd:COG1136 7 LRNLTKSYGtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKStllnilggldrptsgevlIDGQDISSLSERELARLRRR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 686 HrlkIGF-FnQQY--------AEQLRMeetPTEYLQRGFNLPYQDARKCLGRFGLESHAHTiQICKLSGGQKARVVFAE- 755
Cdd:COG1136 87 H---IGFvF-QFFnllpeltaLENVAL---PLLLAGVSRKERRERARELLERVGLGDRLDH-RPSQLSGGQQQRVAIARa 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 69354671 756 LACRePDVLILDEPTNNLDIES----IDALGEAINEYKGAVIVVSHDARL 801
Cdd:COG1136 159 LVNR-PKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDPEL 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
303-526 |
2.54e-13 |
|
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: 73.71 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 303 DIKLEK--FSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIA-------------NRALS-IPP-----NID 361
Cdd:COG2274 473 DIELENvsFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLglyeptsgrilidGIDLRqIDPaslrrQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 362 VLLceQEVV------------ADETPAVQAVLRAdTKRLKLLEEERRLqgqlEQGDDTaaerleKVYEElratgaaaaea 429
Cdd:COG2274 553 VVL--QDVFlfsgtirenitlGDPDATDEEIIEA-ARLAGLHDFIEAL----PMGYDT------VVGEG----------- 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 430 karrilaGLGFdpemqnrptqkfSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLN--AVIW--LNNYLQGWrkTLLIVS 505
Cdd:COG2274 609 -------GSNL------------SGGQRQRLAIARALLRNPRILILDEATSALDAEteAIILenLRRLLKGR--TVIIIA 667
|
250 260
....*....|....*....|.
gi 69354671 506 HDQGFLDDvCTDIIHLDAQRL 526
Cdd:COG2274 668 HRLSTIRL-ADRIIVLDKGRI 687
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
333-529 |
2.59e-13 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 70.02 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 333 GLVGPNGKGKTTLLKHIAnrALSIPPNidvllceQEVVADETPAVqavlraDTKRLKLLEEERRLQGQLEQGDD-----T 407
Cdd:cd03297 27 GIFGASGAGKSTLLRCIA--GLEKPDG-------GTIVLNGTVLF------DSRKKINLPPQQRKIGLVFQQYAlfphlN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 408 AAERLEKVyeeLRATGAAAAEAKARRILAGLGFDPeMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAV 487
Cdd:cd03297 92 VRENLAFG---LKRKRNREDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 69354671 488 IWLNNYLQGWRKTL----LIVSHDQGFLDDVCTDIIHLDAQRLHYY 529
Cdd:cd03297 168 LQLLPELKQIKKNLnipvIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
321-521 |
2.66e-13 |
|
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: 69.83 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVvADETPAVQAVLRADT-----KRLKLLEE-- 393
Cdd:cd03255 22 GVSLSIEKGEFVAIVGPSGSGKSTLLNILG--GLDRPTSGEVRVDGTDI-SKLSEKELAAFRRRHigfvfQSFNLLPDlt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 394 --ERRLQGQLEQGDDtAAERLEKVYEELRatgaaaaeakarriLAGLGfdpEMQNRPTQKFSGGWRMRVSLARALFMEPT 471
Cdd:cd03255 99 alENVELPLLLAGVP-KKERRERAEELLE--------------RVGLG---DRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 69354671 472 LLMLDEPTNHLDL-NAVIWLN-----NYLQGwrKTLLIVSHDQgFLDDVCTDIIHL 521
Cdd:cd03255 161 IILADEPTGNLDSeTGKEVMEllrelNKEAG--TTIVVVTHDP-ELAEYADRIIEL 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
625-804 |
2.73e-13 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 70.29 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 625 LGLHGVTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKS---------------TLLLLLTGKLTPTHGEMRKnHRLK 689
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKStllrclnglveptsgSVLIDGTDINKLKGKALRQ-LRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 690 IGFFNQQYA--EQL---------RMEETPTeyLQRGFNLPY----QDARKCLGRFGLESHAHTiQICKLSGGQKARVVFA 754
Cdd:cd03256 80 IGMIFQQFNliERLsvlenvlsgRLGRRST--WRSLFGLFPkeekQRALAALERVGLLDKAYQ-RADQLSGGQQQRVAIA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 69354671 755 ELACREPDVLILDEPTNNLDIES----IDALgEAINEYKG-AVIVVSHDARLITE 804
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASsrqvMDLL-KRINREEGiTVIVSLHQVDLARE 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
302-526 |
3.35e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 70.16 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 302 SDIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIanRALSIPPNIDVLLCEQEVVADetpavqavl 381
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI--NLLEQPEAGTIRVGDITIDTA--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 382 RADTKRLKLLEEERRLQGQLEQGDDTAAER--LEKVYEE---LRATGAAAAEAKARRILAGLGFDPEMQNRPtQKFSGGW 456
Cdd:PRK11264 71 RSLSQQKGLIRQLRQHVGFVFQNFNLFPHRtvLENIIEGpviVKGEPKEEATARARELLAKVGLAGKETSYP-RRLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 69354671 457 RMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGW---RKTLLIVSHDQGFLDDVCTDIIHLDAQRL 526
Cdd:PRK11264 150 QQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLaqeKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
306-604 |
4.84e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 72.68 E-value: 4.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 306 LEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKhianralsippnidvLLCEQevvadetpavqavLRADT 385
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLK---------------LMLGQ-------------LQADS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 386 KRL----KL-----------LEEERRLQGQLEQGDDT----AAERlekvyeelratgaaaaeakarRILAGLG---FDPE 443
Cdd:PRK11147 374 GRIhcgtKLevayfdqhraeLDPEKTVMDNLAEGKQEvmvnGRPR---------------------HVLGYLQdflFHPK 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 444 MQNRPTQKFSGGWRMRVSLARaLFMEPT-LLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTD-IIHL 521
Cdd:PRK11147 433 RAMTPVKALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTEcWIFE 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 522 DAQRLHYYRGNYmtFKKMYQQKQKELLKQyekqekklkelkAGGKSTKQAEKQTKEALTRKQQKCRRKNQDEESQeAPEL 601
Cdd:PRK11147 512 GNGKIGRYVGGY--HDARQQQAQYLALKQ------------PAVKKKEEAAAPKAETVKRSSKKLSYKLQRELEQ-LPQL 576
|
...
gi 69354671 602 LKR 604
Cdd:PRK11147 577 LED 579
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
627-802 |
1.34e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 67.77 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGE----------MRKN----HRLKIGF 692
Cdd:COG2884 4 FENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQvlvngqdlsrLKRReipyLRRRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 693 FNQQY------------AEQLRMEETPTEYLQRgfnlpyqDARKCLGRFGLESHAHT--IQickLSGGQKARVVFAelac 758
Cdd:COG2884 84 VFQDFrllpdrtvyenvALPLRVTGKSRKEIRR-------RVREVLDLVGLSDKAKAlpHE---LSGGEQQRVAIA---- 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 69354671 759 R----EPDVLILDEPTNNLDIES----IDALgEAINEYKGAVIVVSHDARLI 802
Cdd:COG2884 150 RalvnRPELLLADEPTGNLDPETsweiMELL-EEINRRGTTVLIATHDLELV 200
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
321-527 |
1.42e-12 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 67.76 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLkHIAnrALSIPPNI-DVLLCEQEVvADETPAVQAVLRADT-----KRLKLLEE- 393
Cdd:COG1136 26 GVSLSIEAGEFVAIVGPSGSGKSTLL-NIL--GGLDRPTSgEVLIDGQDI-SSLSERELARLRRRHigfvfQFFNLLPEl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 394 ---E-----RRLQGQleqgddTAAERLEKVYEelratgaaaaeakarrILAGLGFDPEMQNRPTQkFSGGWRMRVSLARA 465
Cdd:COG1136 102 talEnvalpLLLAGV------SRKERRERARE----------------LLERVGLGDRLDHRPSQ-LSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 69354671 466 LFMEPTLLMLDEPTNHLD-------LNAVIWLNnylQGWRKTLLIVSHDQgFLDDVCTDIIHLDAQRLH 527
Cdd:COG1136 159 LVNRPKLILADEPTGNLDsktgeevLELLRELN---RELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
288-526 |
1.79e-12 |
|
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: 70.95 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 288 QAEMSSRQAMLENASDIKLEK--FSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnRALsiPP------- 358
Cdd:COG4987 318 AVTEPAEPAPAPGGPSLELEDvsFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLL-RFL--DPqsgsitl 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 359 -NIDVLLCEQE-------VVADETPAVQAVLRADtkrLKLleeerrlqGQLEQGDDTAAERLEKVY-EELratgaaaaea 429
Cdd:COG4987 395 gGVDLRDLDEDdlrrriaVVPQRPHLFDTTLREN---LRL--------ARPDATDEELWAALERVGlGDW---------- 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 430 karriLAGL--GFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-LNAVIWLNNYLQGWR-KTLLIVS 505
Cdd:COG4987 454 -----LAALpdGLDTWLGEGGRR-LSGGERRRLALARALLRDAPILLLDEPTEGLDaATEQALLADLLEALAgRTVLLIT 527
|
250 260
....*....|....*....|.
gi 69354671 506 HDQGFLDDVCTdIIHLDAQRL 526
Cdd:COG4987 528 HRLAGLERMDR-ILVLEDGRI 547
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
632-821 |
1.82e-12 |
|
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: 67.32 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 632 FGYQGQKPLFK-NLDFGIDmDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRL---------------KIGFFNQ 695
Cdd:cd03297 4 VDIEKRLPDFTlKIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrKIGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 696 QYA--EQLRMEETPTEYLQRGFNLPYQD-ARKCLGRFGLES--HAHTIQickLSGGQKARVVFAELACREPDVLILDEPT 770
Cdd:cd03297 83 QYAlfPHLNVRENLAFGLKRKRNREDRIsVDELLDLLGLDHllNRYPAQ---LSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 771 NNLDIES----IDALGEAINEYKGAVIVVSHD---ARLITETncqLWVVEEQSVSQID 821
Cdd:cd03297 160 SALDRALrlqlLPELKQIKKNLNIPVIFVTHDlseAEYLADR---IVVMEDGRLQYIG 214
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
267-507 |
1.97e-12 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 70.47 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 267 YERQVASLKAANAAENDfSVSQAEMSSRQAMLENASDIKLEKFSISAH---GKELFVNADLYIVAGRRYGLVGPNGKGKT 343
Cdd:TIGR02868 297 LTRVRAAAERIVEVLDA-AGPVAEGSAPAAGAVGLGKPTLELRDLSAGypgAPPVLDGVSLDLPPGERVAILGPSGSGKS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 344 TLLKHIAnRALSiPPNIDVLLceqevvaDETPAVQAVLRADTKRLKLLEEERRL----------QGQLEQGDDTAAERLE 413
Cdd:TIGR02868 376 TLLATLA-GLLD-PLQGEVTL-------DGVPVSSLDQDEVRRRVSVCAQDAHLfdttvrenlrLARPDATDEELWAALE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 414 KVyeelratgaaaaeaKARRILAGL--GFDPEMQNRpTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNA----V 487
Cdd:TIGR02868 447 RV--------------GLADWLRALpdGLDTVLGEG-GARLSGGERQRLALARALLADAPILLLDEPTEHLDAETadelL 511
|
250 260
....*....|....*....|
gi 69354671 488 IWLNNYLQGwrKTLLIVSHD 507
Cdd:TIGR02868 512 EDLLAALSG--RTVVLITHH 529
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
321-483 |
2.00e-12 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 70.48 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLlkhiaNRALS--IPpnidvllCEQEVVADETPaVQAVLRADTKRLKlleeeRRLQ 398
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTL-----GLALLrlIP-------SEGEIRFDGQD-LDGLSRRALRPLR-----RRMQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 399 ----------------GQ-------LEQGDDTAAERLEKVYEelratgaaaaeakarrILAGLGFDPEMQNRPTQKFSGG 455
Cdd:COG4172 366 vvfqdpfgslsprmtvGQiiaeglrVHGPGLSAAERRARVAE----------------ALEEVGLDPAARHRYPHEFSGG 429
|
170 180
....*....|....*....|....*...
gi 69354671 456 WRMRVSLARALFMEPTLLMLDEPTNHLD 483
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
629-802 |
2.14e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.83 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 629 GVTFGyqgQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRLKIGFFNQQYAEQLRMEETPT 708
Cdd:PRK09544 11 SVSFG---QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLPLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 709 EYLQRGFNLPYQDARKCLGRFgleSHAHTIQ--ICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAIN 786
Cdd:PRK09544 88 RFLRLRPGTKKEDILPALKRV---QAGHLIDapMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLID 164
|
170 180
....*....|....*....|
gi 69354671 787 ----EYKGAVIVVSHDARLI 802
Cdd:PRK09544 165 qlrrELDCAVLMVSHDLHLV 184
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
627-798 |
2.49e-12 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 66.06 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNhrlkiGFFNQQYAEQLRMEET 706
Cdd:cd03229 3 LKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-----GEDLTDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 707 PTEYLqrgfnlpYQDarkclgrFGLESHAHTIQICK--LSGGQKARVVFAELACREPDVLILDEPTNNLDIE---SIDAL 781
Cdd:cd03229 77 RIGMV-------FQD-------FALFPHLTVLENIAlgLSGGQQQRVALARALAMDPDVLLLDEPTSALDPItrrEVRAL 142
|
170
....*....|....*...
gi 69354671 782 GEAINEYKG-AVIVVSHD 798
Cdd:cd03229 143 LKSLQAQLGiTVVLVTHD 160
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
297-484 |
4.09e-12 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 67.06 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 297 MLEnASDIklekfSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLkhianRALS--IPPNI-DVLLCEQEVvaDE 373
Cdd:COG4559 1 MLE-AENL-----SVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLL-----KLLTgeLTPSSgEVRLNGRPL--AA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 374 TPAVQ-----AVLRADTkRL----KLLEEER--RLQGQLEQGDDT--AAERLEKVyeelratgaaaaeakarrilaGLGf 440
Cdd:COG4559 68 WSPWElarrrAVLPQHS-SLafpfTVEEVVAlgRAPHGSSAAQDRqiVREALALV---------------------GLA- 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 69354671 441 dpEMQNRPTQKFSGGWRMRVSLARAL-------FMEPTLLMLDEPTNHLDL 484
Cdd:COG4559 125 --HLAGRSYQTLSGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSALDL 173
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
309-522 |
4.19e-12 |
|
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: 65.10 E-value: 4.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 309 FSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNidvllcEQEVVADETpavqavlraDTKRL 388
Cdd:cd03228 8 FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLR---LYDPT------SGEILIDGV---------DLRDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 389 KLlEEERRLQGQLEQG----DDTAAERLekvyeelratgaaaaeakarrilaglgfdpemqnrptqkFSGGWRMRVSLAR 464
Cdd:cd03228 70 DL-ESLRKNIAYVPQDpflfSGTIRENI---------------------------------------LSGGQRQRIAIAR 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 69354671 465 ALFMEPTLLMLDEPTNHLD--LNAVIW--LNNYLQGwrKTLLIVSHDqgfLDDV--CTDIIHLD 522
Cdd:cd03228 110 ALLRDPPILILDEATSALDpeTEALILeaLRALAKG--KTVIVIAHR---LSTIrdADRIIVLD 168
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
291-507 |
5.06e-12 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 67.04 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 291 MSSRQAMLEnASDIKLEkFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANraLSIPPNIDVLLCEQEVv 370
Cdd:COG1116 1 MSAAAPALE-LRGVSKR-FPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAG--LEKPTSGEVLVDGKPV- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 371 ADETPAVQAVLRADT---------------KRLKLLEEERRlqgqleqgdDTAAERLEKVyeelratgaaaaeakarril 435
Cdd:COG1116 76 TGPGPDRGVVFQEPAllpwltvldnvalglELRGVPKAERR---------ERARELLELV-------------------- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 69354671 436 aGL-GFdpeMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD------LNAviWLNNYLQGWRKTLLIVSHD 507
Cdd:COG1116 127 -GLaGF---EDAYPHQ-LSGGMRQRVAIARALANDPEVLLMDEPFGALDaltrerLQD--ELLRLWQETGKTVLFVTHD 198
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
636-805 |
5.18e-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: 65.84 E-value: 5.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 636 GQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRlKIGFFNQQYAEQ---------LRMEET 706
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT-PLAEQRDEPHENilylghlpgLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 707 PTEYLQ------RGFNLPYQDArkcLGRFGLESHAHTIqICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDA 780
Cdd:TIGR01189 90 ALENLHfwaaihGGAQRTIEDA---LAAVGLTGFEDLP-AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170 180
....*....|....*....|....*...
gi 69354671 781 LGEAINEY---KGAVIVVSHDARLITET 805
Cdd:TIGR01189 166 LAGLLRAHlarGGIVLLTTHQDLGLVEA 193
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
624-797 |
5.56e-12 |
|
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: 66.65 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 624 VLGLHGVTFGYQGqKPLFKNLDFGIDMDSRICIVGPNGVGKStllllltgkltpthGEMRKNH----------------- 686
Cdd:COG1119 3 LLELRNVTVRRGG-KTILDDISWTVKPGEHWAILGPNGAGKStlls-------litGDLPPTYgndvrlfgerrggedvw 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 687 --RLKIGFFNQQYAEQLRMEETPTEYLQRGF--------NLPYQD---ARKCLGRFGLESHAHTiQICKLSGGQKARVVF 753
Cdd:COG1119 75 elRKRIGLVSPALQLRFPRDETVLDVVLSGFfdsiglyrEPTDEQrerARELLELLGLAHLADR-PFGTLSQGEQRRVLI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 69354671 754 AelacR----EPDVLILDEPTNNLDIESIDALGEAINEYKG----AVIVVSH 797
Cdd:COG1119 154 A----RalvkDPELLILDEPTAGLDLGARELLLALLDKLAAegapTLVLVTH 201
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
625-806 |
5.62e-12 |
|
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: 64.93 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 625 LGLHGVTFGYQG-QKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRLkigfFNQQYAEQLRm 703
Cdd:cd03246 1 LEVENVSFRYPGaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAD----ISQWDPNELG- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 704 eetpteylQRGFNLPyQDARKCLGrfgleSHAHTIqickLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGE 783
Cdd:cd03246 76 --------DHVGYLP-QDDELFSG-----SIAENI----LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQ 137
|
170 180
....*....|....*....|....*.
gi 69354671 784 AINEYKGA---VIVVSHDARLITETN 806
Cdd:cd03246 138 AIAALKAAgatRIVIAHRPETLASAD 163
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
323-527 |
5.89e-12 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 66.30 E-value: 5.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 323 DLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVA-DETPavQAVLRAD-------------TkrL 388
Cdd:COG4181 32 SLEVEAGESVAIVGASGSGKSTLLGLLA--GLDRPTSGTVRLAGQDLFAlDEDA--RARLRARhvgfvfqsfqllpT--L 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 389 KLLE------EERrlqgqleqGDDTAAER----LEKVyeelratgaaaaeakarrilaGLGfdPEMQNRPTQkFSGGWRM 458
Cdd:COG4181 106 TALEnvmlplELA--------GRRDARARaralLERV---------------------GLG--HRLDHYPAQ-LSGGEQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 459 RVSLARALFMEPTLLMLDEPTNHLD-------------LNAViwlnnylQGwrKTLLIVSHDQGfLDDVCTDIIHLDAQR 525
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDaatgeqiidllfeLNRE-------RG--TTLVLVTHDPA-LAARCDRVLRLRAGR 223
|
..
gi 69354671 526 LH 527
Cdd:COG4181 224 LV 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
629-812 |
6.55e-12 |
|
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: 68.85 E-value: 6.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 629 GVTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRLKIGFFNQQYAEQLR------ 702
Cdd:TIGR02857 326 GVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAwvpqhp 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 703 --MEETPTEYLQrgFNLPYQDA--------RKCLGRF--GLESHAHTI---QICKLSGGQKARVVFAELACREPDVLILD 767
Cdd:TIGR02857 406 flFAGTIAENIR--LARPDASDaeirealeRAGLDEFvaALPQGLDTPigeGGAGLSGGQAQRLALARAFLRDAPLLLLD 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 69354671 768 EPTNNLDIESIDALGEAINEYKG--AVIVVSHDARLITETNcQLWVV 812
Cdd:TIGR02857 484 EPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLALAALAD-RIVVL 529
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
304-528 |
7.52e-12 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 65.59 E-value: 7.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHgkELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVADEtPAVQAVlra 383
Cdd:cd03298 1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIA--GFETPQSGRVLINGVDVTAAP-PADRPV--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 384 dtkrlKLLEEERRLQGQL--EQGDDTAAERLEKVYEElratgaaaAEAKARRILAGLGFDPEMQNRPTQkFSGGWRMRVS 461
Cdd:cd03298 73 -----SMLFQENNLFAHLtvEQNVGLGLSPGLKLTAE--------DRQAIEVALARVGLAGLEKRLPGE-LSGGERQRVA 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 69354671 462 LARALFMEPTLLMLDEPTNHLD---LNAVIWLNNYLQGWRK-TLLIVSHDQGFLDDVCTDIIHLDAQRLHY 528
Cdd:cd03298 139 LARVLVRDKPVLLLDEPFAALDpalRAEMLDLVLDLHAETKmTVLMVTHQPEDAKRLAQRVVFLDNGRIAA 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
323-528 |
7.66e-12 |
|
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: 65.82 E-value: 7.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 323 DLYIVAGRRYGLVGPNGKGKTTLLKHIAN---------RALSIPP---------NIDVLLCEQEVVADETPAVQAvlrad 384
Cdd:cd03267 41 SFTIEKGEIVGFIGPNGAGKTTTLKILSGllqptsgevRVAGLVPwkrrkkflrRIGVVFGQKTQLWWDLPVIDS----- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 385 tkrLKLLEEERRLQgqleqgDDTAAERLEKVYEELRATgaaaaeakarrilaglgfdpEMQNRPTQKFSGGWRMRVSLAR 464
Cdd:cd03267 116 ---FYLLAAIYDLP------PARFKKRLDELSELLDLE--------------------ELLDTPVRQLSLGQRMRAEIAA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 465 ALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK----TLLIVSHDQGFLDDVCTDIIHLDAQRLHY 528
Cdd:cd03267 167 ALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRergtTVLLTSHYMKDIEALARRVLVIDKGRLLY 234
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
304-507 |
8.82e-12 |
|
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: 65.66 E-value: 8.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIaNRALSIPPNI----DVLLCEQEVVADETPAVQa 379
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLL-NRLNDLIPGApdegEVLLDGKDIYDLDVDVLE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 380 vLR-----------------ADTKRLKLleeerRLQGqlEQGDDTAAERLEKVyeelratgaaaaeakarriLAGLGFDP 442
Cdd:cd03260 79 -LRrrvgmvfqkpnpfpgsiYDNVAYGL-----RLHG--IKLKEELDERVEEA-------------------LRKAALWD 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 69354671 443 EMQNRPTQ-KFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDL-------NAVIWLNNylqgwRKTLLIVSHD 507
Cdd:cd03260 132 EVKDRLHAlGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPistakieELIAELKK-----EYTIVIVTHN 199
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
625-802 |
9.18e-12 |
|
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: 68.64 E-value: 9.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 625 LGLHGVTFGYQGQ-KPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNH-----------RLKIGF 692
Cdd:COG4987 334 LELEDVSFRYPGAgRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldeddlRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 693 FNQQ-------YAEQLRM------EETPTEYLQRgfnlpyqdARkcLGRF------GLES----HAHTiqickLSGGQKA 749
Cdd:COG4987 414 VPQRphlfdttLRENLRLarpdatDEELWAALER--------VG--LGDWlaalpdGLDTwlgeGGRR-----LSGGERR 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 69354671 750 RVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEY-KG-AVIVVSHDARLI 802
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAlAGrTVLLITHRLAGL 533
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
630-834 |
1.25e-11 |
|
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: 65.59 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 630 VTFGYQGQ-KPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEM-----------RKNHRLKIGFFNQQY 697
Cdd:COG1124 9 VSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVtfdgrpvtrrrRKAFRRRVQMVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 698 AEQL----RMEETPTEYLqRGFNLPYQDAR--KCLGRFGLESHA-----HtiqicKLSGGQKARVVFAELACREPDVLIL 766
Cdd:COG1124 89 YASLhprhTVDRILAEPL-RIHGLPDREERiaELLEQVGLPPSFldrypH-----QLSGGQRQRVAIARALILEPELLLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 767 DEPTNNLDI----ESIDALGEAINEYKGAVIVVSHDARLITETnC-------QLWVVEEQSVSQIDGDFE-DYKREVLEA 834
Cdd:COG1124 163 DEPTSALDVsvqaEILNLLKDLREERGLTYLFVSHDLAVVAHL-CdrvavmqNGRIVEELTVADLLAGPKhPYTRELLAA 241
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
269-507 |
1.44e-11 |
|
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: 67.70 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 269 RQV-----ASLKAANAAENDFSV----SQAEMSSRQAMLENASDIKLEKFSISAHGKELFV-NADLYIVAGRRYGLVGPN 338
Cdd:TIGR02857 278 RQLgaqyhARADGVAAAEALFAVldaaPRPLAGKAPVTAAPASSLEFSGVSVAYPGRRPALrPVSFTVPPGERVALVGPS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 339 GKGKTTLLKHIANRalsIPPNIDVLLCEQEVVADETPAV----------QAVLRADTkrlklLEEERRLqGQLEQGDDTA 408
Cdd:TIGR02857 358 GAGKSTLLNLLLGF---VDPTEGSIAVNGVPLADADADSwrdqiawvpqHPFLFAGT-----IAENIRL-ARPDASDAEI 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 409 AERLEKVYeelratgaaaaeakARRILAGLgfdPEMQNRPTQK----FSGGWRMRVSLARALFMEPTLLMLDEPTNHLD- 483
Cdd:TIGR02857 429 REALERAG--------------LDEFVAAL---PQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDa 491
|
250 260
....*....|....*....|....*..
gi 69354671 484 -LNAVIW--LNNYLQGwrKTLLIVSHD 507
Cdd:TIGR02857 492 eTEAEVLeaLRALAQG--RTVLLVTHR 516
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
625-797 |
1.51e-11 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 64.61 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 625 LGLHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKN-------HRLKIGFF---- 693
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDgkpldiaARNRIGYLpeer 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 694 ----NQQYAEQLRmeetpteYLQRGFNLPYQDARK----CLGRFGLESHAHtIQICKLSGGQKARVVFAELACREPDVLI 765
Cdd:cd03269 80 glypKMKVIDQLV-------YLAQLKGLKKEEARRrideWLERLELSEYAN-KRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190
....*....|....*....|....*....|....*
gi 69354671 766 LDEPTNNLDIESIDALGEAINEYKGA---VIVVSH 797
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAgktVILSTH 186
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
328-521 |
1.60e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.38 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 328 AGRRYGLVGPNGKGKTTLLKHIanRALSIPPNIDVLLCEQEV--VADETPAVQAvlrADTKRLKLLEEerRLQGQLEQGD 405
Cdd:PRK10619 30 AGDVISIIGSSGSGKSTFLRCI--NFLEKPSEGSIVVNGQTInlVRDKDGQLKV---ADKNQLRLLRT--RLTMVFQHFN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 406 ----DTAAERLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNH 481
Cdd:PRK10619 103 lwshMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSA 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 69354671 482 LD---LNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHL 521
Cdd:PRK10619 183 LDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFL 225
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
630-812 |
1.65e-11 |
|
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: 64.94 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 630 VTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMR-----------KNHRLKIG------- 691
Cdd:cd03253 6 VTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqdirevtlDSLRRAIGvvpqdtv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 692 ------FFNQQYAeqlRMEETPTEYLQ---------RGFNLPYQDARKcLGRFGLeshahtiqicKLSGGQKARVVFAEL 756
Cdd:cd03253 86 lfndtiGYNIRYG---RPDATDEEVIEaakaaqihdKIMRFPDGYDTI-VGERGL----------KLSGGEKQRVAIARA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 757 ACREPDVLILDEPTNNLDIESIDALGEAINE-YKG-AVIVVSHdaRLITETNCQLWVV 812
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDvSKGrTTIVIAH--RLSTIVNADKIIV 207
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
296-484 |
1.71e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 65.18 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 296 AMLEnASDIklekfSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLkhianRALS--IPPNI-DVLLCEQEVvAD 372
Cdd:PRK13548 1 AMLE-ARNL-----SVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLL-----RALSgeLSPDSgEVRLNGRPL-AD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 373 ETPAVQAVLRA---------------DTKRLKLLeeerRLQGQLEQGDDTAAERLEKVYeelratgaaaaeakarriLAG 437
Cdd:PRK13548 69 WSPAELARRRAvlpqhsslsfpftveEVVAMGRA----PHGLSRAEDDALVAAALAQVD------------------LAH 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 69354671 438 LGfdpemqNRPTQKFSGGWRMRVSLARAL------FMEPTLLMLDEPTNHLDL 484
Cdd:PRK13548 127 LA------GRDYPQLSGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDL 173
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
304-522 |
1.90e-11 |
|
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: 64.47 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVADETPAVQavLRA 383
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCIN--LLEEPDSGTIIIDGLKLTDDKKNINE--LRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 384 DT----------KRLKLLEE----ERRLQGQ-LEQGDDTAAERLEKVyeelratgaaaaeakarrilaglGFDPEMQNRP 448
Cdd:cd03262 77 KVgmvfqqfnlfPHLTVLENitlaPIKVKGMsKAEAEERALELLEKV-----------------------GLADKADAYP 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 69354671 449 TQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD---LNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLD 522
Cdd:cd03262 134 AQ-LSGGQQQRVAIARALAMNPKVMLFDEPTSALDpelVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMD 209
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
302-507 |
2.05e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 65.04 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 302 SDIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANraLSIPPNIDVLLceqevvaDETPAVQAVL 381
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFAR--LLTPQSGTVFL-------GDKPISMLSS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 382 RADTKRLKLLEEE---------RRL-----------QGQLEQGDDtaaERLEKVYEELRATgaaaaeakarrilaglgfd 441
Cdd:PRK11231 72 RQLARRLALLPQHhltpegitvRELvaygrspwlslWGRLSAEDN---ARVNQAMEQTRIN------------------- 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 69354671 442 pEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR---KTLLIVSHD 507
Cdd:PRK11231 130 -HLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNtqgKTVVTVLHD 197
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
304-507 |
2.06e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.14 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTL----LKHIANRALSI--PPNIDVLLCEQEVVADETPAV 377
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLvrvvLGLVAPDEGVIkrNGKLRIGYVPQKLYLDTTLPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 378 QA----VLRADTKRLKLLEEERRLQgqleqgddtAAERLEKvyeelratgaaaaeakarrilaglgfdpemqnrPTQKFS 453
Cdd:PRK09544 85 TVnrflRLRPGTKKEDILPALKRVQ---------AGHLIDA---------------------------------PMQKLS 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 454 GGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTL----LIVSHD 507
Cdd:PRK09544 123 GGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcavLMVSHD 180
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
321-522 |
2.35e-11 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 64.38 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIANRalsIPPNI-DVLLCEQEVvADETP------------------------ 375
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGF---LRPTSgSVLFDGEDI-TGLPPheiarlgigrtfqiprlfpeltvl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 376 -----AVQAVLRADTKRLKLLEEERRLQGQleqgddtAAERLEKVyeelratgaaaaeakarrilaGLGfdpEMQNRPTQ 450
Cdd:cd03219 94 envmvAAQARTGSGLLLARARREEREARER-------AEELLERV---------------------GLA---DLADRPAG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 69354671 451 KFSGGWRMRVSLARALFMEPTLLMLDEPT---NHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLD 522
Cdd:cd03219 143 ELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLD 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
321-515 |
2.37e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 67.13 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIANralSIPPN---IDVLLCEQEVvaDET-PAVQAVLRAdTKRLKLLEEERR 396
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAG---VLEPTsgeVNVRVGDEWV--DMTkPGPDGRGRA-KRYIGILHQEYD 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 397 LQGQLEQGDD-TAAERLEKVYEelratgaaAAEAKARRILAGLGFDPE----MQNRPTQKFSGGWRMRVSLARALFMEPT 471
Cdd:TIGR03269 376 LYPHRTVLDNlTEAIGLELPDE--------LARMKAVITLKMVGFDEEkaeeILDKYPDELSEGERHRVALAQVLIKEPR 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 69354671 472 LLMLDEPTNHLD-----------LNAVIWLNnylqgwrKTLLIVSHDQGFLDDVC 515
Cdd:TIGR03269 448 IVILDEPTGTMDpitkvdvthsiLKAREEME-------QTFIIVSHDMDFVLDVC 495
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
306-519 |
2.44e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.21 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 306 LEKFSISAHGKE--LFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLCEQEVvADETPAVQAVLRA 383
Cdd:COG2401 31 LEAFGVELRVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQF-GREASLIDAIGRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 384 DTKrlklleeerrlqgqleqgdDTAAERLEKVyeelratgaaaaeakarrilaGLGfDPEMQNRPTQKFSGGWRMRVSLA 463
Cdd:COG2401 110 GDF-------------------KDAVELLNAV---------------------GLS-DAVLWLRRFKELSTGQKFRFRLA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 464 RALFMEPTLLMLDEPTNHLD-LNAVIWLNNYLQGWRK---TLLIVSHDQGFLDDVCTDII 519
Cdd:COG2401 149 LLLAERPKLLVIDEFCSHLDrQTAKRVARNLQKLARRagiTLVVATHHYDVIDDLQPDLL 208
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
321-507 |
2.45e-11 |
|
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: 64.03 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIANraLsIPPNIDVLLCEQEVVADETPAVQAVLRADTkrlkLLE----EERR 396
Cdd:cd03293 22 DISLSVEEGEFVALVGPSGCGKSTLLRIIAG--L-ERPTSGEVLVDGEPVTGPGPDRGYVFQQDA----LLPwltvLDNV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 397 LQGqLEQGDDTAAERLEKVYEELRatgaaaaeakarriLAGL-GFDpemQNRPTQkFSGGWRMRVSLARALFMEPTLLML 475
Cdd:cd03293 95 ALG-LELQGVPKAEARERAEELLE--------------LVGLsGFE---NAYPHQ-LSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 69354671 476 DEPTNHLDlnAVI------WLNNYLQGWRKTLLIVSHD 507
Cdd:cd03293 156 DEPFSALD--ALTreqlqeELLDIWRETGKTVLLVTHD 191
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
304-526 |
3.90e-11 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 63.85 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALsIPPNidvllcEQEVVADEtpavQAVLRA 383
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLII--GL-LRPD------SGEILVDG----QDITGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 384 DTKRLKLLEeeRRL-----QGQL---------------EQGDDTAAERLEKVYEELRatgaaaaeakarriLAGLgfdPE 443
Cdd:COG1127 73 SEKELYELR--RRIgmlfqGGALfdsltvfenvafplrEHTDLSEAEIRELVLEKLE--------------LVGL---PG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 444 MQNR-PTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD------LNAVIwlnNYLQGWRK-TLLIVSHDQGFLDDVC 515
Cdd:COG1127 134 AADKmPSE-LSGGMRKRVALARALALDPEILLYDEPTAGLDpitsavIDELI---RELRDELGlTSVVVTHDLDSAFAIA 209
|
250
....*....|.
gi 69354671 516 TDIIHLDAQRL 526
Cdd:COG1127 210 DRVAVLADGKI 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
328-521 |
4.34e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.27 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 328 AGRRYGLVGPNGKGKTT----LLKHIANRAlsippnidvllceqEVVADETPAVQavlradTKRLKLLEEERRLQG---- 399
Cdd:PRK15134 311 PGETLGLVGESGSGKSTtglaLLRLINSQG--------------EIWFDGQPLHN------LNRRQLLPVRHRIQVvfqd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 400 -------------------QLEQGDDTAAERLEKVYEelratgaaaaeakarrILAGLGFDPEMQNRPTQKFSGGWRMRV 460
Cdd:PRK15134 371 pnsslnprlnvlqiieeglRVHQPTLSAAQREQQVIA----------------VMEEVGLDPETRHRYPAEFSGGQRQRI 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 69354671 461 SLARALFMEPTLLMLDEPTNHLD--LNAVI--WLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHL 521
Cdd:PRK15134 435 AIARALILKPSLIILDEPTSSLDktVQAQIlaLLKSLQQKHQLAYLFISHDLHVVRALCHQVIVL 499
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
452-506 |
5.12e-11 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 62.23 E-value: 5.12e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 452 FSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK---TLLIVSH 506
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAagaTRIVIAH 154
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
314-522 |
5.70e-11 |
|
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: 62.66 E-value: 5.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 314 HGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANralsippnidvLLCEQ--EVVADETPAVQAVLRadtKRLKLL 391
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAG-----------LIKESsgSILLNGKPIKAKERR---KSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 392 EEErrLQGQLeqGDDTaaerlekVYEELR--ATGAAAAEAKARRILAGLGFDpEMQNRPTQKFSGGWRMRVSLARALFME 469
Cdd:cd03226 77 MQD--VDYQL--FTDS-------VREELLlgLKELDAGNEQAETVLKDLDLY-ALKERHPLSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 69354671 470 PTLLMLDEPTNHLD---LNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLD 522
Cdd:cd03226 145 KDLLIFDEPTSGLDyknMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
624-804 |
6.44e-11 |
|
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: 63.47 E-value: 6.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 624 VLGLHGVTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHG---------------EMRKnHRL 688
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGsillegtditklrgkKLRK-LRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 689 KIGFFNQQYA--EQL---------RMEETPTeyLQRGFNL----PYQDARKCLGRFGLESHAHTiQICKLSGGQKARVVF 753
Cdd:TIGR02315 80 RIGMIFQHYNliERLtvlenvlhgRLGYKPT--WRSLLGRfseeDKERALSALERVGLADKAYQ-RADQLSGGQQQRVAI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 69354671 754 AELACREPDVLILDEPTNNLDIES----IDALGEaINEYKGAVIVVS-HDARLITE 804
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTskqvMDYLKR-INKEDGITVIINlHQVDLAKK 211
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
625-798 |
7.38e-11 |
|
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: 65.46 E-value: 7.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 625 LGLHGVTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKN-----------HRLKIGFF 693
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDgvpvssldqdeVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 694 NQQ-------YAEQLRmeetpteyLQRGfNLPYQDARKCLGRFGLESH-------AHTI---QICKLSGGQKARVVFAEL 756
Cdd:TIGR02868 415 AQDahlfdttVRENLR--------LARP-DATDEELWAALERVGLADWlralpdgLDTVlgeGGARLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 69354671 757 ACREPDVLILDEPTNNLDIESIDALGEAIN--EYKGAVIVVSHD 798
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLLaaLSGRTVVLITHH 529
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
323-507 |
7.46e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 64.37 E-value: 7.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 323 DLYIVAGRRYGLVGPNGKGKTTLlkhiaNRALS--IPPNidvllcEQEVVADETPavqaVLRADTKRLKLLEeeRRLQ-- 398
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTL-----GRLLLrlEEPT------SGEILFDGQD----ITGLSGRELRPLR--RRMQmv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 399 --------------GQL------EQGDDTAAERLEKVYEelratgaaaaeakarrILAGLGFDPEMQNRPTQKFSGGWRM 458
Cdd:COG4608 101 fqdpyaslnprmtvGDIiaeplrIHGLASKAERRERVAE----------------LLELVGLRPEHADRYPHEFSGGQRQ 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 69354671 459 RVSLARALFMEPTLLMLDEPTNHLDLN--A-VIwlnNYLQGWRK----TLLIVSHD 507
Cdd:COG4608 165 RIGIARALALNPKLIVCDEPVSALDVSiqAqVL---NLLEDLQDelglTYLFISHD 217
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
629-802 |
7.87e-11 |
|
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: 62.91 E-value: 7.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 629 GVTFG-YQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGE--------------MRKNHRLKIGF- 692
Cdd:cd03257 8 SVSFPtGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSiifdgkdllklsrrLRKIRRKEIQMv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 693 -------FN------QQYAEQLR---------MEETPTEYLQRGFNLPyqdaRKCLGRFgleshAHtiqicKLSGGQKAR 750
Cdd:cd03257 88 fqdpmssLNprmtigEQIAEPLRihgklskkeARKEAVLLLLVGVGLP----EEVLNRY-----PH-----ELSGGQRQR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 69354671 751 VVFAE-LACrEPDVLILDEPTNNLDIES----IDALGEAINEYKGAVIVVSHDARLI 802
Cdd:cd03257 154 VAIARaLAL-NPKLLIADEPTSALDVSVqaqiLDLLKKLQEELGLTLLFITHDLGVV 209
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
304-521 |
9.25e-11 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 63.05 E-value: 9.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLCEQEVVA------------ 371
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEVTSGTILFKGQDLLElepderaraglf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 372 ------DETPAVQAV--LRAdtkrlkLLEEERRLQGQleqgDDTAAERLEKVYEELratgaaaaeakarriLAGLGFDPE 443
Cdd:TIGR01978 81 lafqypEEIPGVSNLefLRS------ALNARRSARGE----EPLDLLDFEKLLKEK---------------LALLDMDEE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 444 MQNRPTQK-FSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR---KTLLIVSHDQGFLDDVCTDII 519
Cdd:TIGR01978 136 FLNRSVNEgFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLRepdRSFLIITHYQRLLNYIKPDYV 215
|
..
gi 69354671 520 HL 521
Cdd:TIGR01978 216 HV 217
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
322-507 |
1.08e-10 |
|
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: 63.98 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 322 ADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPnidvllcEQEVVADETpavqaVLRADTKRLKLLEEERRL---- 397
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIA--GLTRPD-------EGEIVLNGR-----TLFDSRKGIFLPPEKRRIgyvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 398 -----------QGQLEQGDDTAAERLEKVYEElratgaaaaeakarRILAGLGFDPEMQnRPTQKFSGGWRMRVSLARAL 466
Cdd:TIGR02142 82 qearlfphlsvRGNLRYGMKRARPSERRISFE--------------RVIELLGIGHLLG-RLPGRLSGGEKQRVAIGRAL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 69354671 467 FMEPTLLMLDEPTNHLDL---NAVI-WLNNYLQGWRKTLLIVSHD 507
Cdd:TIGR02142 147 LSSPRLLLMDEPLAALDDprkYEILpYLERLHAEFGIPILYVSHS 191
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
627-837 |
1.12e-10 |
|
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: 65.24 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYQGQ-KPLFKNLDFGIDMDSRICIVGPNGVGKSTLlllltgkltpthgemrknhrLKI--GF---------FN 694
Cdd:COG2274 476 LENVSFRYPGDsPPVLDNISLTIKPGERVAIVGRSGSGKSTL--------------------LKLllGLyeptsgrilID 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 695 QQYAEQLRmeetPTEY-------LQRGF--------NL-------PYQDARKCLGRFGL----ESHA---HTiQI----C 741
Cdd:COG2274 536 GIDLRQID----PASLrrqigvvLQDVFlfsgtireNItlgdpdaTDEEIIEAARLAGLhdfiEALPmgyDT-VVgeggS 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 742 KLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKG--AVIVVSHdaRLITETNC-QLWVVEEQSVS 818
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAH--RLSTIRLAdRIIVLDKGRIV 688
|
250
....*....|....*....
gi 69354671 819 QiDGDFEdykrEVLEALGE 837
Cdd:COG2274 689 E-DGTHE----ELLARKGL 702
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
630-805 |
1.17e-10 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 62.04 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 630 VTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKN--------------HRLKIGFFNQ 695
Cdd:cd03292 6 VTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqdvsdlrgraipyLRRKIGVVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 696 QYaeqlRMEETPTEYLQRGFNL-----PYQDARK----CLGRFGLESHAHTIQIcKLSGGQKARVVFAELACREPDVLIL 766
Cdd:cd03292 86 DF----RLLPDRNVYENVAFALevtgvPPREIRKrvpaALELVGLSHKHRALPA-ELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 69354671 767 DEPTNNLDIES---IDALGEAINEYKGAVIVVSHDARLITET 805
Cdd:cd03292 161 DEPTGNLDPDTtweIMNLLKKINKAGTTVVVATHAKELVDTT 202
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
304-521 |
1.46e-10 |
|
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: 61.39 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLCEQEVvadetpavqavlra 383
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKGEDI-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 384 dtkrLKLLEEERRLQGqleqgddtaaerlekvyeelratgaaaaeakarrilAGLGFdpemQNRPT-------------- 449
Cdd:cd03217 67 ----TDLPPEERARLG------------------------------------IFLAF----QYPPEipgvknadflryvn 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 69354671 450 QKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR---KTLLIVSHDQGFLDDVCTDIIHL 521
Cdd:cd03217 103 EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLReegKSVLIITHYQRLLDYIKPDRVHV 177
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
328-484 |
1.47e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 63.45 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 328 AGRRYGLVGPNGKGKTTLlkhiaNRALSI--PPNIDVLLCEQEVVADETPAVQAVLRadtKRLKL--------LEEERRL 397
Cdd:PRK11308 40 RGKTLAVVGESGCGKSTL-----ARLLTMieTPTGGELYYQGQDLLKADPEAQKLLR---QKIQIvfqnpygsLNPRKKV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 398 QGQLEQ-----GDDTAAERLEKVYEelratgaaaaeakarrILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTL 472
Cdd:PRK11308 112 GQILEEpllinTSLSAAERREKALA----------------MMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDV 175
|
170
....*....|..
gi 69354671 473 LMLDEPTNHLDL 484
Cdd:PRK11308 176 VVADEPVSALDV 187
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
637-803 |
1.49e-10 |
|
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: 62.35 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 637 QKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEM----------RKNHRLKIGF-FNQQyaEQLRMEE 705
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvaglvpwkrRKKFLRRIGVvFGQK--TQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 706 TPTE---YLQRGFNLPYQDARKCLGRFG----LESHAHTiQICKLSGGQKARvvfAELAC---REPDVLILDEPTNNLDI 775
Cdd:cd03267 111 PVIDsfyLLAAIYDLPPARFKKRLDELSelldLEELLDT-PVRQLSLGQRMR---AEIAAallHEPEILFLDEPTIGLDV 186
|
170 180 190
....*....|....*....|....*....|..
gi 69354671 776 ESIDALGEAINEY----KGAVIVVSHDARLIT 803
Cdd:cd03267 187 VAQENIRNFLKEYnrerGTTVLLTSHYMKDIE 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
315-487 |
1.55e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 61.22 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 315 GKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVADETPAVQAVL----RADTK-RLK 389
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILA--GLLRPDSGEVRWNGTPLAEQRDEPHENILylghLPGLKpELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 390 LLEEERRLQGQLEQGDDTAAERLEKVYeelratgaaaaeakarriLAGLgfdpemQNRPTQKFSGGWRMRVSLARALFME 469
Cdd:TIGR01189 90 ALENLHFWAAIHGGAQRTIEDALAAVG------------------LTGF------EDLPAAQLSAGQQRRLALARLWLSR 145
|
170
....*....|....*...
gi 69354671 470 PTLLMLDEPTNHLDLNAV 487
Cdd:TIGR01189 146 RPLWILDEPTTALDKAGV 163
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
627-802 |
1.65e-10 |
|
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: 61.50 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRknhrlkigfFNQQYAEQLRMEET 706
Cdd:TIGR02673 4 FHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVR---------IAGEDVNRLRGRQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 707 PteYLQRGFNLPYQDARKCLGR------------------------------FGLESHAHTIQIcKLSGGQKARVVFAEL 756
Cdd:TIGR02673 75 P--LLRRRIGVVFQDFRLLPDRtvyenvalplevrgkkereiqrrvgaalrqVGLEHKADAFPE-QLSGGEQQRVAIARA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 69354671 757 ACREPDVLILDEPTNNLD---IESIDALGEAINEYKGAVIVVSHDARLI 802
Cdd:TIGR02673 152 IVNSPPLLLADEPTGNLDpdlSERILDLLKRLNKRGTTVIVATHDLSLV 200
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
739-797 |
1.70e-10 |
|
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: 60.25 E-value: 1.70e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 69354671 739 QIC-----KLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKGAVIVVSH 797
Cdd:cd03223 83 QLIypwddVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH 146
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
305-483 |
2.13e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 61.34 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 305 KLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANrALSippniDVLLCEQEVVADETpavqavlrad 384
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAG-TLS-----PAFSASGEVLLNGR---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 385 tkRLKLLEEERRLQGQLEQgDD--------------------TAAERLEKVYEELRAtgaaaaeakarrilAGLGfdpEM 444
Cdd:COG4136 67 --RLTALPAEQRRIGILFQ-DDllfphlsvgenlafalpptiGRAQRRARVEQALEE--------------AGLA---GF 126
|
170 180 190
....*....|....*....|....*....|....*....
gi 69354671 445 QNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 483
Cdd:COG4136 127 ADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
321-508 |
2.95e-10 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 62.86 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIA-------------NRALSIppNIDVllCEQEV--------------VADE 373
Cdd:COG1118 20 DVSLEIASGELVALLGPSGSGKTTLLRIIAgletpdsgrivlnGRDLFT--NLPP--RERRVgfvfqhyalfphmtVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 374 tpaVQAVLRAdtkrLKLLEEERRlqgqleqgdDTAAERLEKVYeelratgaaaaeakarriLAGLGfdpemqNR-PTQkF 452
Cdd:COG1118 96 ---IAFGLRV----RPPSKAEIR---------ARVEELLELVQ------------------LEGLA------DRyPSQ-L 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 69354671 453 SGGWRMRVSLARALFMEPTLLMLDEPTNHLDlNAV-----IWLNNYLQGWRKTLLIVSHDQ 508
Cdd:COG1118 135 SGGQRQRVALARALAVEPEVLLLDEPFGALD-AKVrkelrRWLRRLHDELGGTTVFVTHDQ 194
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
625-776 |
4.74e-10 |
|
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: 60.28 E-value: 4.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 625 LGLHGVTFGYQGQKPLFK-NLDFGIDMdsrICIVGPNGVGKSTLLLLLTGKLTPTHG----------EMRKNHRLKIGFF 693
Cdd:cd03264 1 LQLENLTKRYGKKRALDGvSLTLGPGM---YGLLGPNGAGKTTLMRILATLTPPSSGtiridgqdvlKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 694 NQQ--YAEQLRMEETpTEYLQR--GFNLPYQDARKC--LGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILD 767
Cdd:cd03264 78 PQEfgVYPNFTVREF-LDYIAWlkGIPSKEVKARVDevLELVNLGDRAKK-KIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
....*....
gi 69354671 768 EPTNNLDIE 776
Cdd:cd03264 156 EPTAGLDPE 164
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
315-487 |
4.87e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 59.89 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 315 GKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVADETPAVQAVL-RADTKRLKLLEE 393
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIA--GLLPPAAGTIKLDGGDIDDPDVAEACHYLgHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 394 E-----RRLQGQLEQGDDTAAERLEkvyeelratgaaaaeakarriLAGLGfdpemqNRPTQKFSGGWRMRVSLARALFM 468
Cdd:PRK13539 92 EnlefwAAFLGGEELDIAAALEAVG---------------------LAPLA------HLPFGYLSAGQKRRVALARLLVS 144
|
170
....*....|....*....
gi 69354671 469 EPTLLMLDEPTNHLDLNAV 487
Cdd:PRK13539 145 NRPIWILDEPTAALDAAAV 163
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
304-506 |
5.21e-10 |
|
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: 60.87 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRalsIPP--NIDVLLCEQE------------- 368
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGD---LPPtyGNDVRLFGERrggedvwelrkri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 369 -VVadeTPAVQAVLRADTKRLKLLeeerrLQG---------QLEQGDDTAAERLekvyeelratgaaaaeakarriLAGL 438
Cdd:COG1119 81 gLV---SPALQLRFPRDETVLDVV-----LSGffdsiglyrEPTDEQRERAREL----------------------LELL 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 69354671 439 GFDpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK----TLLIVSH 506
Cdd:COG1119 131 GLA-HLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegapTLVLVTH 201
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
636-797 |
5.31e-10 |
|
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: 59.92 E-value: 5.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 636 GQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGE-------MRKNH--RLKIG-------FFNQQYA- 698
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEitfdgksYQKNIeaLRRIGalieapgFYPNLTAr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 699 EQLRmeetpteYLQRGFNLPYQDARKCLGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESI 778
Cdd:cd03268 91 ENLR-------LLARLLGIRKKRIDEVLDVVGLKDSAKK-KVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGI 162
|
170 180
....*....|....*....|..
gi 69354671 779 DALGEAI---NEYKGAVIVVSH 797
Cdd:cd03268 163 KELRELIlslRDQGITVLISSH 184
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
630-830 |
6.26e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 62.82 E-value: 6.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 630 VTFGY--QGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEM--------RKNHRL---KIGFFNQq 696
Cdd:TIGR00958 484 VSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVlldgvplvQYDHHYlhrQVALVGQ- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 697 yaEQLRMEETPTEYLQRGFNLPYQDARKCLGRfglESHAHTIqICK---------------LSGGQKARVVFAELACREP 761
Cdd:TIGR00958 563 --EPVLFSGSVRENIAYGLTDTPDEEIMAAAK---AANAHDF-IMEfpngydtevgekgsqLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 762 DVLILDEPTNNLDIESIDALGEAINEYKGAVIVVSHdaRLITETNC-QLWVVEEQSVSQIDGDFEDYKRE 830
Cdd:TIGR00958 637 RVLILDEATSALDAECEQLLQESRSRASRTVLLIAH--RLSTVERAdQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
304-527 |
6.47e-10 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 60.07 E-value: 6.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSIS-AHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnraLSIPPNI-DVLLCEQEVV---ADETPAvq 378
Cdd:COG2884 2 IRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLY---GEERPTSgQVLVNGQDLSrlkRREIPY-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 379 avLRadtKRL-------KLLEEeR----------RLQGQleqgddTAAERLEKVYEelratgaaaaeakarrILAGLGFD 441
Cdd:COG2884 77 --LR---RRIgvvfqdfRLLPD-RtvyenvalplRVTGK------SRKEIRRRVRE----------------VLDLVGLS 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 442 PEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------------LNAViwlnnylqGwrKTLLIVSHDQ 508
Cdd:COG2884 129 DKAKALPHE-LSGGEQQRVAIARALVNRPELLLADEPTGNLDpetsweimelleeINRR--------G--TTVLIATHDL 197
|
250
....*....|....*....
gi 69354671 509 GFLDDVCTDIIHLDAQRLH 527
Cdd:COG2884 198 ELVDRMPKRVLELEDGRLV 216
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
306-507 |
6.83e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.46 E-value: 6.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 306 LEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPnidvllcEQEVVADETPAVQAvlRADT 385
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLA--GLETPS-------AGELLAGTAPLAEA--REDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 386 KrlkLLEEERRLQ---------GQLEQGD--DTAAERLEKVyeelratgaaaaeakarrilaglGFDPEMQNRPTqKFSG 454
Cdd:PRK11247 84 R---LMFQDARLLpwkkvidnvGLGLKGQwrDAALQALAAV-----------------------GLADRANEWPA-ALSG 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 69354671 455 GWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQG-WRK---TLLIVSHD 507
Cdd:PRK11247 137 GQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESlWQQhgfTVLLVTHD 193
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
743-802 |
7.92e-10 |
|
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: 59.46 E-value: 7.92e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKG---AVIVVSHDARLI 802
Cdd:cd03217 105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREegkSVLIITHYQRLL 167
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
446-508 |
8.00e-10 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 60.04 E-value: 8.00e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 69354671 446 NRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK----TLLIVSHDQ 508
Cdd:cd03299 124 NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKefgvTVLHVTHDF 190
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
321-522 |
8.90e-10 |
|
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: 60.05 E-value: 8.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLK--------------------------HIANRALS-------IPPNIDVLlcEQ 367
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNlitgfyrptsgrilfdgrditglpphRIARLGIArtfqnprLFPELTVL--EN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 368 EVVADETPAVQAVLRADTKRLKLLEEERRLQgqleqgdDTAAERLEKVyeelratgaaaaeakarrilaGLGfdpEMQNR 447
Cdd:COG0411 100 VLVAAHARLGRGLLAALLRLPRARREEREAR-------ERAEELLERV---------------------GLA---DRADE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 448 PTQKFSGGWRMRVSLARALFMEPTLLMLDEPT---NH---LDLNAVI-WLNnylQGWRKTLLIVSHDQGFLDDVCTDIIH 520
Cdd:COG0411 149 PAGNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPeetEELAELIrRLR---DERGITILLIEHDMDLVMGLADRIVV 225
|
..
gi 69354671 521 LD 522
Cdd:COG0411 226 LD 227
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
742-815 |
9.40e-10 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 59.94 E-value: 9.40e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 69354671 742 KLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINE-YKG-AVIVVSHdaRLITETNCQLWVVEEQ 815
Cdd:cd03251 138 KLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERlMKNrTTFVIAH--RLSTIENADRIVVLED 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
333-479 |
9.49e-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: 59.37 E-value: 9.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 333 GLVGPNGKGKTTLLKHIANralSIPP-NIDVLLCEQEVvaDETPAVQAVLRAdtkrLKLLEEERRLQGQL---------- 401
Cdd:cd03224 30 ALLGRNGAGKTTLLKTIMG---LLPPrSGSIRFDGRDI--TGLPPHERARAG----IGYVPEGRRIFPELtveenlllga 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 69354671 402 -EQGDDTAAERLEKVYEELRatgaaaaeakarrILAglgfdpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPT 479
Cdd:cd03224 101 yARRRAKRKARLERVYELFP-------------RLK------ERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
304-528 |
1.08e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 59.38 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELfvNADLYIVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNI-DVLLCEQEVvADETPAVQAV-- 380
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAG---FLPPDSgRILWNGQDL-TALPPAERPVsm 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 381 --------------------LRADtkrLKLLEEERRlqgQLEQgddtAAERLEkvyeelratgaaaaeakarriLAGLGf 440
Cdd:COG3840 76 lfqennlfphltvaqniglgLRPG---LKLTAEQRA---QVEQ----ALERVG---------------------LAGLL- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 441 dpemQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------LNAVIWLNNYLQgwrKTLLIVSHDqgfLDD 513
Cdd:COG3840 124 ----DRLPGQ-LSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrqemLDLVDELCRERG---LTVLMVTHD---PED 192
|
250
....*....|....*...
gi 69354671 514 ---VCTDIIHLDAQRLHY 528
Cdd:COG3840 193 aarIADRVLLVADGRIAA 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
321-508 |
1.20e-09 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 59.66 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVADETPAVQ--------AVLRADTKRLKL-- 390
Cdd:cd03296 20 DVSLDIPSGELVALLGPSGSGKTTLLRLIA--GLERPDSGTILFGGEDATDVPVQERNvgfvfqhyALFRHMTVFDNVaf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 391 -LEEERRLQgqleqgDDTAAERLEKVYEELRATGaaaaeakarriLAGLGfdpemqNRPTQKFSGGWRMRVSLARALFME 469
Cdd:cd03296 98 gLRVKPRSE------RPPEAEIRAKVHELLKLVQ-----------LDWLA------DRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 69354671 470 PTLLMLDEPTNHLDLNAVIWLNNYLqgwRK-------TLLIVSHDQ 508
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWL---RRlhdelhvTTVFVTHDQ 197
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
636-798 |
1.80e-09 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 58.70 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 636 GQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMR-------------KNHRLKIGFFNQQYA--EQ 700
Cdd:cd03262 11 GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIidglkltddkkniNELRQKVGMVFQQFNlfPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 701 LRMEETPTEYLQRGFNLPYQDA----RKCLGRFGLESHAHTIQIcKLSGGQKARVVFAELACREPDVLILDEPTNNLDIE 776
Cdd:cd03262 91 LTVLENITLAPIKVKGMSKAEAeeraLELLEKVGLADKADAYPA-QLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPE 169
|
170 180
....*....|....*....|....*
gi 69354671 777 SIDALGEAINE--YKG-AVIVVSHD 798
Cdd:cd03262 170 LVGEVLDVMKDlaEEGmTMVVVTHE 194
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
323-526 |
1.87e-09 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 58.54 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 323 DLYIVAGRRYGLVGPNGKGKTTLLKHIANRAlsiPPNIDVLLCEQEVVADETPAVQavlradtKRLKLLEEERRLQGQLe 402
Cdd:cd03265 20 SFRVRRGEIFGLLGPNGAGKTTTIKMLTTLL---KPTSGRATVAGHDVVREPREVR-------RRIGIVFQDLSVDDEL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 403 qgddTAAERLEkVYEELRATGAAAAEAKARRILAGLGFdPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHL 482
Cdd:cd03265 89 ----TGWENLY-IHARLYGVPGAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 69354671 483 DLNAVIWLNNYLQGWRK----TLLIVSHDQGFLDDVCTDIIHLDAQRL 526
Cdd:cd03265 163 DPQTRAHVWEYIEKLKEefgmTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
304-485 |
1.91e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 60.63 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNIDVLLCEQEVVADETPAVQAVLRA 383
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAING---TLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 384 DTKRLKLLEEERRLQGQLEQG--------------DDTAAERlekvyeelratgaaaaeakarrILAGLGFDpEMQNRPT 449
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGrtphrsrfdtwtetDRAAVER----------------------AMERTGVA-QFADRPV 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 69354671 450 QKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLN 485
Cdd:PRK09536 138 TSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
321-505 |
2.10e-09 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 58.44 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIP-PNIDVLLCEQEVVADETPAVQAVLRADTKRLKLL--EEERRL 397
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGtTSGQILFNGQPRKPDQFQKCVAYVRQDDILLPGLtvRETLTY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 398 QGQLEQGDDTAAERLEKVYEELRATGaaaaeakarriLAglgfDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDE 477
Cdd:cd03234 105 TAILRLPRKSSDAIRKKRVEDVLLRD-----------LA----LTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190
....*....|....*....|....*....|..
gi 69354671 478 PTNHLD----LNAVIWLNNYLQgwRKTLLIVS 505
Cdd:cd03234 170 PTSGLDsftaLNLVSTLSQLAR--RNRIVILT 199
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
742-798 |
2.24e-09 |
|
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: 58.35 E-value: 2.24e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 69354671 742 KLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKG--AVIVVSHD 798
Cdd:cd03260 141 GLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
743-835 |
2.59e-09 |
|
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: 60.53 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYK---GAVIVVSHDARLITETNcQLWVVEeqsvsq 819
Cdd:COG4618 468 LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKargATVVVITHRPSLLAAVD-KLLVLR------ 540
|
90
....*....|....*...
gi 69354671 820 iDGDFEDY--KREVLEAL 835
Cdd:COG4618 541 -DGRVQAFgpRDEVLARL 557
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
743-803 |
2.78e-09 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 57.62 E-value: 2.78e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 69354671 743 LSGGQKA------RVVFAELACREPDVLILDEPTNNLDIESID-ALGEAINEYKGA----VIVVSHDARLIT 803
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLAEIIEERKSQknfqLIVITHDEELVD 187
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
321-508 |
3.09e-09 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 58.02 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVAdetpavqavLRADTKRLKLLEEERRLQGQ 400
Cdd:cd03300 18 GVSLDIKEGEFFTLLGPSGCGKTTLLRLIA--GFETPTSGEILLDGKDITN---------LPPHKRPVNTVFQNYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 401 LEQGDDTA----------AERLEKVYEELRatgaaaaeakarriLAGLGfdpEMQNRPTQKFSGGWRMRVSLARALFMEP 470
Cdd:cd03300 87 LTVFENIAfglrlkklpkAEIKERVAEALD--------------LVQLE---GYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 69354671 471 TLLMLDEPTNHLDLNAVIWLNNYLQGWRK----TLLIVSHDQ 508
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQ 191
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
314-525 |
3.51e-09 |
|
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: 57.83 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 314 HGKELFV--NADLYIVAGRRYGLVGPNGKGKTTLLKHI-AN--------RALSIPPNIDVLLC-EQEVVAdetpavqavL 381
Cdd:COG4778 20 GGKRLPVldGVSFSVAAGECVALTGPSGAGKSTLLKCIyGNylpdsgsiLVRHDGGWVDLAQAsPREILA---------L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 382 RADT-----------KRLKLLE-EERRLqgqLEQGDDtAAERLEKVyEELratgaaaaeakarriLAGLGFDPEMQNRPT 449
Cdd:COG4778 91 RRRTigyvsqflrviPRVSALDvVAEPL---LERGVD-REEARARA-REL---------------LARLNLPERLWDLPP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 69354671 450 QKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDL---NAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQR 525
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAanrAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
630-817 |
4.37e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 58.28 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 630 VTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEM--------RKNH---RLKIGFFNQQYA 698
Cdd:PRK13652 9 LCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlirgepitKENIrevRKFVGLVFQNPD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 699 EQLRmeeTPTEYLQRGF---NLPYQDA------RKCLGRFGLEsHAHTIQICKLSGGQKARVVFAELACREPDVLILDEP 769
Cdd:PRK13652 89 DQIF---SPTVEQDIAFgpiNLGLDEEtvahrvSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 69354671 770 TNNLDIESIDALGEAIN----EYKGAVIVVSHDARLITETNCQLWVVEEQSV 817
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNdlpeTYGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
630-798 |
5.22e-09 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 58.23 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 630 VTFGYQGQKPL----FKNLDFGIDMDSRICIVGPNGVGKST--------------LLLLLTGKLTPTHGEMRKNHRLKIG 691
Cdd:TIGR04521 6 VSYIYQPGTPFekkaLDDVSLTIEDGEFVAIIGHTGSGKSTliqhlngllkptsgTVTIDGRDITAKKKKKLKDLRKKVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 692 F-FnqQYAEQLRMEET--------PteylqRGFNLPYQDARKC----LGRFGLESHAHTIQICKLSGGQKARVVFAE-LA 757
Cdd:TIGR04521 86 LvF--QFPEHQLFEETvykdiafgP-----KNLGLSEEEAEERvkeaLELVGLDEEYLERSPFELSGGQMRRVAIAGvLA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 69354671 758 CrEPDVLILDEPTNNLDIESIDALGEAIN----EYKGAVIVVSHD 798
Cdd:TIGR04521 159 M-EPEVLILDEPTAGLDPKGRKEILDLFKrlhkEKGLTVILVTHS 202
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
334-522 |
6.41e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 57.33 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 334 LVGPNGKGKTTLLK-------------HIANRA--LSIPPNI-DVLLCEQEV--------VADETPAVQAVLRADTKRLK 389
Cdd:PRK11124 33 LLGPSGAGKSSLLRvlnllemprsgtlNIAGNHfdFSKTPSDkAIRELRRNVgmvfqqynLWPHLTVQQNLIEAPCRVLG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 390 LLEEErrlqgqleqgddtAAERLEKvyeelratgaaaaeakarrILAGLGFDPEMQNRPTQkFSGGWRMRVSLARALFME 469
Cdd:PRK11124 113 LSKDQ-------------ALARAEK-------------------LLERLRLKPYADRFPLH-LSGGQQQRVAIARALMME 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 69354671 470 PTLLMLDEPTNHLD---LNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLD 522
Cdd:PRK11124 160 PQVLLFDEPTAALDpeiTAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYME 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
304-483 |
6.41e-09 |
|
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: 57.58 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSIS-AHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIaNRaLSIPPNIDVLLCEQEVVADETPAVQAVlR 382
Cdd:cd03256 1 IEVENLSKTyPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCL-NG-LVEPTSGSVLIDGTDINKLKGKALRQL-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 383 ADT----------KRLKLLE----------------------EERRLqgqleqgddtAAERLEKVyeelratgaaaaeak 430
Cdd:cd03256 78 RQIgmifqqfnliERLSVLEnvlsgrlgrrstwrslfglfpkEEKQR----------ALAALERV--------------- 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 69354671 431 arrilaGLGfdpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 483
Cdd:cd03256 133 ------GLL---DKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLD 176
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
627-798 |
6.88e-09 |
|
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: 56.76 E-value: 6.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKN---------HRLKIGFFNQQY 697
Cdd:cd03259 3 LKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDgrdvtgvppERRNIGMVFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 698 A-------EQ-----LRMEETPTEYLQRgfnlpyqDARKCLGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLI 765
Cdd:cd03259 82 AlfphltvAEniafgLKLRGVPKAEIRA-------RVRELLELVGLEGLLNR-YPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 69354671 766 LDEPTNNLDIES----IDALGEAINEYKGAVIVVSHD 798
Cdd:cd03259 154 LDEPLSALDAKLreelREELKELQRELGITTIYVTHD 190
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
625-774 |
7.39e-09 |
|
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: 56.17 E-value: 7.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 625 LGLHGVTFGYQGQ-KPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEM----------RKNHRLKIGFF 693
Cdd:cd03247 1 LSINNVSFSYPEQeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEItldgvpvsdlEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 694 NQQyaeqlrmeetptEYLqrgFNlpyQDARKCLGRfgleshahtiqicKLSGGQKARVVFAELACREPDVLILDEPTNNL 773
Cdd:cd03247 81 NQR------------PYL---FD---TTLRNNLGR-------------RFSGGERQRLALARILLQDAPIVLLDEPTVGL 129
|
.
gi 69354671 774 D 774
Cdd:cd03247 130 D 130
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
304-526 |
7.72e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 57.33 E-value: 7.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLK-------------HIANRALSIPPNIDvllcEQEVV 370
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRvlnlletpdsgqlNIAGHQFDFSQKPS----EKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 371 AdetpavqavLRAD--------------TKRLKLLEEERRLQGQLEQgddTAAERLEKvyeelratgaaaaeakarrILA 436
Cdd:COG4161 79 L---------LRQKvgmvfqqynlwphlTVMENLIEAPCKVLGLSKE---QAREKAMK-------------------LLA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 437 GLGFDpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD---LNAVIWLNNYLQGWRKTLLIVSHDQGFLDD 513
Cdd:COG4161 128 RLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeiTAQVVEIIRELSQTGITQVIVTHEVEFARK 206
|
250
....*....|...
gi 69354671 514 VCTDIIHLDAQRL 526
Cdd:COG4161 207 VASQVVYMEKGRI 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
321-526 |
7.87e-09 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 56.82 E-value: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLkhianRALSippnidvLLceqevvadETPAVQAVLRADTKRLKLLEEERRLQGQ 400
Cdd:cd03258 23 DVSLSVPKGEIFGIIGRSGAGKSTLI-----RCIN-------GL--------ERPTSGSVLVDGTDLTLLSGKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 401 ------------------------LEQGDDTAAERLEKVYEELRatgaaaaeakarriLAGLGfDPEmQNRPTQkFSGGW 456
Cdd:cd03258 83 rigmifqhfnllssrtvfenvalpLEIAGVPKAEIEERVLELLE--------------LVGLE-DKA-DAYPAQ-LSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 69354671 457 RMRVSLARALFMEPTLLMLDEPTNHLD-------LNAVIWLNNYLqgwRKTLLIVSHDQGFLDDVCTDIIHLDAQRL 526
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDpettqsiLALLRDINREL---GLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
321-526 |
8.03e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.02 E-value: 8.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIaNRALSIP-------------PNIDVLLCEQE--VVADET---PAVQAvlr 382
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCI-NKLEEITsgdlivdglkvndPKVDERLIRQEagMVFQQFylfPHLTA--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 383 adtkrlklLEE----ERRLQGQLEQgddtAAERLEKvyeelratgaaaaeakarRILAGLGFDPEMQNRPTQkFSGGWRM 458
Cdd:PRK09493 95 --------LENvmfgPLRVRGASKE----EAEKQAR------------------ELLAKVGLAERAHHYPSE-LSGGQQQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 69354671 459 RVSLARALFMEPTLLMLDEPTNHLD---LNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQRL 526
Cdd:PRK09493 144 RVAIARALAVKPKLMLFDEPTSALDpelRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
321-508 |
9.93e-09 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 56.49 E-value: 9.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLcEQEVVADETPA---VQAVLR----------ADTKR 387
Cdd:cd03301 18 DLNLDIADGEFVVLLGPSGCGKTTTLRMIA--GLEEPTSGRIYI-GGRDVTDLPPKdrdIAMVFQnyalyphmtvYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 388 LKLleeerRLQGQLEqgdDTAAERLEKVYEELratgaaaaeakarrilaglGFDPEMQNRPTQkFSGGWRMRVSLARALF 467
Cdd:cd03301 95 FGL-----KLRKVPK---DEIDERVREVAELL-------------------QIEHLLDRKPKQ-LSGGQRQRVALGRAIV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 69354671 468 MEPTLLMLDEPTNHLD----LNAVIWLNNYLQGWRKTLLIVSHDQ 508
Cdd:cd03301 147 REPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQ 191
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
625-798 |
1.08e-08 |
|
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: 56.33 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 625 LGLHGVTFGYQGQKPLFKNLDfGIDMDSR----ICIVGPNGVGKSTLLLLLTGKLTPTHGEMR------KNHRLKIGFFN 694
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALE-DISLSVEegefVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvTGPGPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 695 QQYA-------EQ-----LRMEETPTEYLQRgfnlpyqDARKCLGRFGLESHAH--TIQickLSGGQKARVVFAE-LAcR 759
Cdd:cd03293 80 QQDAllpwltvLDnvalgLELQGVPKAEARE-------RAEELLELVGLSGFENayPHQ---LSGGMRQRVALARaLA-V 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 69354671 760 EPDVLILDEPTNNLDI---ESI-DALGEAINEYKGAVIVVSHD 798
Cdd:cd03293 149 DPDVLLLDEPFSALDAltrEQLqEELLDIWRETGKTVLLVTHD 191
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
627-798 |
1.15e-08 |
|
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: 56.36 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEM--------------RKNHRLKIGF 692
Cdd:cd03261 3 LRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlidgedisglseaeLYRLRRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 693 FNQQYA-------EQ-----LRMEETPTEYLQRGFnlpyqdARKCLGRFGLESHAH--TIQickLSGGQKARVVFAELAC 758
Cdd:cd03261 82 LFQSGAlfdsltvFEnvafpLREHTRLSEEEIREI------VLEKLEAVGLRGAEDlyPAE---LSGGMKKRVALARALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 69354671 759 REPDVLILDEPTNNLDIESIDALGEAINEYKGA----VIVVSHD 798
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElgltSIMVTHD 196
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
624-800 |
1.18e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.01 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 624 VLGLHGVTFGyQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKN-HRLKIGFFNQQYA---- 698
Cdd:PRK13543 11 LLAAHALAFS-RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDgKTATRGDRSRFMAylgh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 699 -EQLRMEETPTEYLQRGFNL----PYQDARKCLGRFGLESHAHTIqICKLSGGQKARVVFAELACREPDVLILDEPTNNL 773
Cdd:PRK13543 90 lPGLKADLSTLENLHFLCGLhgrrAKQMPGSALAIVGLAGYEDTL-VRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
170 180 190
....*....|....*....|....*....|
gi 69354671 774 DIESIDALGEAINEY---KGAVIVVSHDAR 800
Cdd:PRK13543 169 DLEGITLVNRMISAHlrgGGAALVTTHGAY 198
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
743-797 |
1.23e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 57.36 E-value: 1.23e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAI----NEYKGAVIVVSH 797
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIkelhKEYNMTIILVSH 203
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
321-514 |
1.33e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.40 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIanRALSIPPNIDV-LLCEQEVVADETPAVQAVLRADT------KRLKLLEE 393
Cdd:PRK13651 25 NVSVEINQGEFIAIIGQTGSGKTTFIEHL--NALLLPDTGTIeWIFKDEKNKKKTKEKEKVLEKLViqktrfKKIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 394 ERRLQG--------QL-EQG--------------DDTAAERLEKVYEELratgaaaaeakarrilagLGFDPEMQNRPTQ 450
Cdd:PRK13651 103 IRRRVGvvfqfaeyQLfEQTiekdiifgpvsmgvSKEEAKKRAAKYIEL------------------VGLDESYLQRSPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 69354671 451 KFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAV-----IWLNNYLQGwrKTLLIVSHDqgfLDDV 514
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVkeileIFDNLNKQG--KTIILVTHD---LDNV 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
625-798 |
1.34e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 56.56 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 625 LGLHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRLKIGFFNQQYAEQL--- 701
Cdd:PRK11231 3 LRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLall 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 702 -RMEETPT-----EYLQRGFNlPYQDArkcLGRFGLESHAHTIQ--------------ICKLSGGQKARVVFAELACREP 761
Cdd:PRK11231 82 pQHHLTPEgitvrELVAYGRS-PWLSL---WGRLSAEDNARVNQameqtrinhladrrLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 69354671 762 DVLILDEPTNNLDI----ESIDALGEAINEYKgAVIVVSHD 798
Cdd:PRK11231 158 PVVLLDEPTTYLDInhqvELMRLMRELNTQGK-TVVTVLHD 197
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
635-797 |
1.59e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 55.58 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 635 QGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRlKIGFFNQQYAEQL---------RMEE 705
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-PLDFQRDSIARGLlylghapgiKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 706 TPTEYLQrgFNLPYQDARKC---LGRFGLESHAHTIqICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALG 782
Cdd:cd03231 89 SVLENLR--FWHADHSDEQVeeaLARVGLNGFEDRP-VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
170
....*....|....*...
gi 69354671 783 EAINEY---KGAVIVVSH 797
Cdd:cd03231 166 EAMAGHcarGGMVVLTTH 183
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
321-508 |
1.61e-08 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 57.42 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIANraLSIPPNIDVLLcEQEVVADETPavqavlradtkrlklleEERRL--- 397
Cdd:COG3842 23 DVSLSIEPGEFVALLGPSGCGKTTLLRMIAG--FETPDSGRILL-DGRDVTGLPP-----------------EKRNVgmv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 398 -Q----------------GqLEQGDDTAAERLEKVYEELRatgaaaaeakarriLAGLGfdpEMQNRPTQKFSGGWRMRV 460
Cdd:COG3842 83 fQdyalfphltvaenvafG-LRMRGVPKAEIRARVAELLE--------------LVGLE---GLADRYPHQLSGGQQQRV 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 69354671 461 SLARALFMEPTLLMLDEPTNHLDLNA----VIWLNNYLQGWRKTLLIVSHDQ 508
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLreemREELRRLQRELGITFIYVTHDQ 196
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
326-513 |
1.71e-08 |
|
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: 55.49 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 326 IVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVllceqevvadetpAVQAVLRADTKRLKLLeeeRRLQGQLEQGD 405
Cdd:cd03292 24 ISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRV-------------NGQDVSDLRGRAIPYL---RRKIGVVFQDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 406 DTAAERleKVYE------ELRATGAAAAEAKARRILAGLGFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPT 479
Cdd:cd03292 88 RLLPDR--NVYEnvafalEVTGVPPREIRKRVPAALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 69354671 480 NHLDLNAVIWLNNYLQGWRK---TLLIVSHDQGFLDD 513
Cdd:cd03292 165 GNLDPDTTWEIMNLLKKINKagtTVVVATHAKELVDT 201
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
630-805 |
1.74e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 56.68 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 630 VTFGYQGQKPL-FKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMrknhrlkigFFNQQYAEQLRMEEtpt 708
Cdd:PRK13648 13 VSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI---------FYNNQAITDDNFEK--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 709 eyLQRGFNLPYQDA-RKCLGR-------FGLESHA------HTI--QICK--------------LSGGQKARVVFAELAC 758
Cdd:PRK13648 81 --LRKHIGIVFQNPdNQFVGSivkydvaFGLENHAvpydemHRRvsEALKqvdmleradyepnaLSGGQKQRVAIAGVLA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 69354671 759 REPDVLILDEPTNNLDIESIDALGEAINEYKG----AVIVVSHDarlITET 805
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSehniTIISITHD---LSEA 206
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
722-804 |
1.86e-08 |
|
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: 55.91 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 722 ARKCLGRFGLESHAHTIqICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGE---AINEYKGAVIVVSHD 798
Cdd:cd03219 124 AEELLERVGLADLADRP-AGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAElirELRERGITVLLVEHD 202
|
....*.
gi 69354671 799 ARLITE 804
Cdd:cd03219 203 MDVVMS 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
297-524 |
1.89e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 55.88 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 297 MLENASDIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRalsIPPNIDVLLCEQEVVADETPa 376
Cdd:PRK10247 1 MQENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASL---ISPTSGTLLFEGEDISTLKP- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 377 vqavlradtkrlkllEEERRlqgQLEQGDDTAAERLEKVYEEL----RATGAAAAEAKARRILAGLGFDPEMQNRPTQKF 452
Cdd:PRK10247 77 ---------------EIYRQ---QVSYCAQTPTLFGDTVYDNLifpwQIRNQQPDPAIFLDDLERFALPDTILTKNIAEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 453 SGGWRMRVSLARALFMEPTLLMLDEPTNHLD------LNAVIwlNNYLQGWRKTLLIVSHDQgflDDV--CTDIIHLDAQ 524
Cdd:PRK10247 139 SGGEKQRISLIRNLQFMPKVLLLDEITSALDesnkhnVNEII--HRYVREQNIAVLWVTHDK---DEInhADKVITLQPH 213
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
315-487 |
1.92e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 55.19 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 315 GKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLcEQEVVADETPAVQAVL------RADTKRL 388
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILA--GLSPPLAGRVLL-NGGPLDFQRDSIARGLlylghaPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 389 KLLEEERRLQGqlEQGDDTAAERLEKVYeelratgaaaaeakarriLAGLGfdpemqNRPTQKFSGGWRMRVSLARALFM 468
Cdd:cd03231 89 SVLENLRFWHA--DHSDEQVEEALARVG------------------LNGFE------DRPVAQLSAGQQRRVALARLLLS 142
|
170
....*....|....*....
gi 69354671 469 EPTLLMLDEPTNHLDLNAV 487
Cdd:cd03231 143 GRPLWILDEPTTALDKAGV 161
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
635-803 |
1.99e-08 |
|
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: 57.74 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 635 QGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMR-KNHRLK----------IGFFNQQ------- 696
Cdd:TIGR01842 328 GGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRlDGADLKqwdretfgkhIGYLPQDvelfpgt 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 697 YAEQL-RMEETPT--------------EYLQRgfnLP--YQDArkcLGRFGleshahtiqiCKLSGGQKARVVFAELACR 759
Cdd:TIGR01842 408 VAENIaRFGENADpekiieaaklagvhELILR---LPdgYDTV---IGPGG----------ATLSGGQRQRIALARALYG 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 69354671 760 EPDVLILDEPTNNLDIESIDALGEAINEYK---GAVIVVSHDARLIT 803
Cdd:TIGR01842 472 DPKLVVLDEPNSNLDEEGEQALANAIKALKargITVVVITHRPSLLG 518
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
312-483 |
2.11e-08 |
|
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: 54.86 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 312 SAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLceqevvaDETPavqavLRADTKRlkll 391
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLI-------NGRP-----LDKRSFR---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 392 eeerRLQGQLEQgDDTAAERLeKVYEELRatgaaaaeakarrILAGLgfdpemqnrptQKFSGGWRMRVSLARALFMEPT 471
Cdd:cd03213 82 ----KIIGYVPQ-DDILHPTL-TVRETLM-------------FAAKL-----------RGLSGGERKRVSIALELVSNPS 131
|
170
....*....|..
gi 69354671 472 LLMLDEPTNHLD 483
Cdd:cd03213 132 LLFLDEPTSGLD 143
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
741-803 |
2.56e-08 |
|
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: 55.29 E-value: 2.56e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 69354671 741 CKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKG--AVIVVSHDARLIT 803
Cdd:cd03245 139 RGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLD 203
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
627-801 |
2.62e-08 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 57.48 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKStllllltgkltpTHGEMR-----------KNHRLKIGFFNQ 695
Cdd:COG1132 342 FENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKStlvnlllrfydpTSGRILidgvdirdltlESLRRQIGVVPQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 696 QY-------AEQLRM--EETPTEYLQR--------GF--NLPYQ-DARkcLGRFGLeshahtiqicKLSGGQKARVVFAE 755
Cdd:COG1132 422 DTflfsgtiRENIRYgrPDATDEEVEEaakaaqahEFieALPDGyDTV--VGERGV----------NLSGGQRQRIAIAR 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 69354671 756 LACREPDVLILDEPTNNLDIESIDALGEAINEY-KGA-VIVVSHdaRL 801
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLmKGRtTIVIAH--RL 535
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
278-506 |
3.11e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 56.38 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 278 NAAENDFSVSQAEMSSRQAMLENAsdIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIP 357
Cdd:PRK13536 18 PIERKHQGISEAKASIPGSMSTVA--IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 358 PNIDVLlceqevvadetpAVQAVLRADTKRLKLleeerrlqGQLEQGDD-----TAAERLeKVYEELRATGAAAAEAKAR 432
Cdd:PRK13536 96 GKITVL------------GVPVPARARLARARI--------GVVPQFDNldlefTVRENL-LVFGRYFGMSTREIEAVIP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 69354671 433 RILAGLGFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNA--VIW--LNNYL-QGwrKTLLIVSH 506
Cdd:PRK13536 155 SLLEFARLESKADARVSD-LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHArhLIWerLRSLLaRG--KTILLTTH 230
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
321-507 |
3.16e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.21 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLkHIANrALSIPPNIDVLLCEQEVvADETPAVQAVLRadTKRLKLLEEERRLQGq 400
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLL-HLLG-GLDTPTSGDVIFNGQPM-SKLSSAAKAELR--NQKLGFIYQFHHLLP- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 401 leqgDDTAaerLEKVYEELR--ATGAAAAEAKARRILAGLGFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEP 478
Cdd:PRK11629 101 ----DFTA---LENVAMPLLigKKKPAEINSRALEMLAAVGLEHRANHRPSE-LSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190
....*....|....*....|....*....|....*
gi 69354671 479 TNHLDL-NAVIWLN-----NYLQGwrKTLLIVSHD 507
Cdd:PRK11629 173 TGNLDArNADSIFQllgelNRLQG--TAFLVVTHD 205
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
720-809 |
3.53e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.21 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 720 QDARKCLGRFGLESHAHTIQiCKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDA----LGEaINEYKG-AVIV 794
Cdd:PRK11629 124 SRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSifqlLGE-LNRLQGtAFLV 201
|
90
....*....|....*
gi 69354671 795 VSHDARLITETNCQL 809
Cdd:PRK11629 202 VTHDLQLAKRMSRQL 216
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
314-506 |
3.94e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 55.97 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 314 HGKELFVNA-DLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVvadetPAvqavlRADTKRLKLle 392
Cdd:PRK13537 17 YGDKLVVDGlSFHVQRGECFGLLGPNGAGKTTTLRMLL--GLTHPDAGSISLCGEPV-----PS-----RARHARQRV-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 393 eerrlqGQLEQGDD-----TAAERLeKVYEELRATGAAAAEAKARRILAglgFdPEMQNR---PTQKFSGGWRMRVSLAR 464
Cdd:PRK13537 83 ------GVVPQFDNldpdfTVRENL-LVFGRYFGLSAAAARALVPPLLE---F-AKLENKadaKVGELSGGMKRRLTLAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 69354671 465 ALFMEPTLLMLDEPTNHLDLNA--VIW--LNNYLQGwRKTLLIVSH 506
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQArhLMWerLRSLLAR-GKTILLTTH 196
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
743-802 |
4.17e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 55.07 E-value: 4.17e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKG---AVIVVSHDARLI 802
Cdd:COG0396 141 FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpdrGILIITHYQRIL 203
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
291-507 |
4.38e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 55.87 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 291 MSSRQAMLENASDIKLEkFSIsAHGKELF------------VNADLYivAGRRYGLVGPNGKGKTTLLKHIANRalsipp 358
Cdd:PRK15079 1 VTEGKKVLLEVADLKVH-FDI-KDGKQWFwqppktlkavdgVTLRLY--EGETLGVVGESGCGKSTFARAIIGL------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 359 nidVLLCEQEVV---ADETPAVQAVLRADTKRLKLLEEE--RRLQGQLEQGDdTAAERLEKVYEELRATGAAAAEAKarr 433
Cdd:PRK15079 71 ---VKATDGEVAwlgKDLLGMKDDEWRAVRSDIQMIFQDplASLNPRMTIGE-IIAEPLRTYHPKLSRQEVKDRVKA--- 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 434 ILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK----TLLIVSHD 507
Cdd:PRK15079 144 MMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemglSLIFIAHD 221
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
743-798 |
4.48e-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: 4.48e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 69354671 743 LSGG--QKarVVFA-ELAcREPDVLILDEPTNNLDIESIDALGEAINEYK---GAVIVVSHD 798
Cdd:cd03215 105 LSGGnqQK--VVLArWLA-RDPRVLILDEPTRGVDVGAKAEIYRLIRELAdagKAVLLISSE 163
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
453-514 |
4.55e-08 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 56.68 E-value: 4.55e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 69354671 453 SGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK---TLLIVSHDQGFLDDV 514
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArgaTVVVITHRPSLLAAV 533
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
333-518 |
4.67e-08 |
|
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: 54.43 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 333 GLVGPNGKGKTTLLKHIANRalsIPPNI-DVLLCEQEVVADetpavqavlradtkrlklLEEERRLQGQLEQGDD----- 406
Cdd:cd03263 32 GLLGHNGAGKTTTLKMLTGE---LRPTSgTAYINGYSIRTD------------------RKAARQSLGYCPQFDAlfdel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 407 TAAERLEkVYEELRATGAAAAEAKARRILAGLGFDPEmQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNA 486
Cdd:cd03263 91 TVREHLR-FYARLKGLPKSEIKEEVELLLRVLGLTDK-ANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 69354671 487 --VIWlnNYLQGWRK--TLLIVSHDQGFLDDVCTDI 518
Cdd:cd03263 169 rrAIW--DLILEVRKgrSIILTTHSMDEAEALCDRI 202
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
304-507 |
5.11e-08 |
|
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: 54.61 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSIS-AHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIaNRAlsIPPNIDVLLCEQEVVADETP------- 375
Cdd:cd03295 1 IEFENVTKRyGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI-NRL--IEPTSGEIFIDGEDIREQDPvelrrki 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 376 --AVQ--------AVLRADTKRLKLLEEERrlqgqleqgddtaAERLEKVYEelratgaaaaeakarrILAGLGFDP-EM 444
Cdd:cd03295 78 gyVIQqiglfphmTVEENIALVPKLLKWPK-------------EKIRERADE----------------LLALVGLDPaEF 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 445 QNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------LNAVIWLNNYLqgwRKTLLIVSHD 507
Cdd:cd03295 129 ADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDpitrdqlQEEFKRLQQEL---GKTIVFVTHD 195
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
297-525 |
5.21e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.99 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 297 MLENASDIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANraLSIPPNIDVLLCEQEVvadETPA 376
Cdd:PRK10253 1 MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSR--LMTPAHGHVWLDGEHI---QHYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 377 VQAVLRadtkRLKLLEeerrlQGQLEQGDDTAAE---RLEKVYEELRATGAAAAEAKARRILAGLGFDpEMQNRPTQKFS 453
Cdd:PRK10253 76 SKEVAR----RIGLLA-----QNATTPGDITVQElvaRGRYPHQPLFTRWRKEDEEAVTKAMQATGIT-HLADQSVDTLS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 454 GGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYL------QGWrkTLLIVSHDqgfLDDVCTDIIHLDAQR 525
Cdd:PRK10253 146 GGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLselnreKGY--TLAAVLHD---LNQACRYASHLIALR 218
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
630-803 |
5.71e-08 |
|
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: 54.54 E-value: 5.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 630 VTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEM-----------RKNHRLKIGF------ 692
Cdd:cd03254 8 VNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirdisRKSLRSMIGVvlqdtf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 693 -FNQQYAEQLRM--EETPTEYLQRgfnlpyqdARKCLG--RF------GLESH----AHTiqickLSGGQKARVVFAELA 757
Cdd:cd03254 88 lFSGTIMENIRLgrPNATDEEVIE--------AAKEAGahDFimklpnGYDTVlgenGGN-----LSQGERQLLAIARAM 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 69354671 758 CREPDVLILDEPTNNLDIESIDALGEAINE-YKG-AVIVVSHdaRLIT 803
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKlMKGrTSIIIAH--RLST 200
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
305-512 |
6.14e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 6.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 305 KLEKFSISAHGKELFVNADLyivagrryGLVGPNGKGKTTLLKHIANR----ALSIPPNIDVLLCEQEVVADETPAVQAV 380
Cdd:PRK13409 349 KLGDFSLEVEGGEIYEGEVI--------GIVGPNGIGKTTFAKLLAGVlkpdEGEVDPELKISYKPQYIKPDYDGTVEDL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 381 LRADTKRL--KLLEEE--RRLQgqleqgddtaaerLEKVYEelratgaaaaeakarrilaglgfdpemqnRPTQKFSGGW 456
Cdd:PRK13409 421 LRSITDDLgsSYYKSEiiKPLQ-------------LERLLD-----------------------------KNVKDLSGGE 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 457 RMRVSLARALFMEPTLLMLDEPTNHLD----LNAVIWLNNYLQGWRKTLLIVSHDQGFLD 512
Cdd:PRK13409 459 LQRVAIAACLSRDADLYLLDEPSAHLDveqrLAVAKAIRRIAEEREATALVVDHDIYMID 518
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
655-802 |
6.39e-08 |
|
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: 52.75 E-value: 6.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 655 CIVGPNGVGKSTllllltgkltpthgemrknhrlkigFFNQ-QYAEQLRM-EETPTEYLQRGFNLPYQDARKCLGRFGLe 732
Cdd:cd03227 25 IITGPNGSGKST-------------------------ILDAiGLALGGAQsATRRRSGVKAGCIVAAVSAELIFTRLQL- 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 69354671 733 shahtiqicklSGGQKARV----VFAELACREPDVLILDEPTNNLDIESIDALGEAINEY--KGA-VIVVSHDARLI 802
Cdd:cd03227 79 -----------SGGEKELSalalILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHlvKGAqVIVITHLPELA 144
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
743-798 |
6.50e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 54.78 E-value: 6.50e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 69354671 743 LSGGQKARV----VFAELACREPD--VLILDEPTNNLDI----ESIDALGEAINEYKGAVIVVSHD 798
Cdd:PRK13548 135 LSGGEQQRVqlarVLAQLWEPDGPprWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHD 200
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
743-798 |
7.48e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 55.09 E-value: 7.48e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLD----IESIDALGEaINEYKGAVIVVSHD 798
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIFDN-LNKQGKTIILVTHD 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
635-798 |
7.79e-08 |
|
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: 53.66 E-value: 7.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 635 QGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEM----------RKNHRLKIGF---FNQQYaEQL 701
Cdd:cd03263 12 KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingysirtdRKAARQSLGYcpqFDALF-DEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 702 rmeeTPTEYLQ-----RGfnLPYQDARKC----LGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPTNN 772
Cdd:cd03263 91 ----TVREHLRfyarlKG--LPKSEIKEEvellLRVLGLTDKANK-RARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
170 180
....*....|....*....|....*...
gi 69354671 773 LDIESIDALGEAINEYKG--AVIVVSHD 798
Cdd:cd03263 164 LDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
630-797 |
8.37e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 54.74 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 630 VTFGYQGQKPLFKNLDFGIDMD----SRICIVGPNGVGKSTLLLLLTGKLTPTHGEMR---------------KNHRLKI 690
Cdd:PRK13643 7 VNYTYQPNSPFASRALFDIDLEvkkgSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTvgdivvsstskqkeiKPVRKKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 691 GFFNQqYAEQLRMEETPTEYLQRG---FNLPYQDARKC----LGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDV 763
Cdd:PRK13643 87 GVVFQ-FPESQLFEETVLKDVAFGpqnFGIPKEKAEKIaaekLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEV 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 69354671 764 LILDEPTNNLDIES---IDALGEAINEYKGAVIVVSH 797
Cdd:PRK13643 166 LVLDEPTAGLDPKArieMMQLFESIHQSGQTVVLVTH 202
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
741-812 |
9.48e-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: 53.70 E-value: 9.48e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 69354671 741 CKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKGA--VIVVSHdaRLITETNCQLWVV 812
Cdd:cd03249 138 SQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGrtTIVIAH--RLSTIRNADLIAV 209
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
743-798 |
9.51e-08 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 54.67 E-value: 9.51e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 69354671 743 LSGGQKARVVFA-ELACrEPDVLILDEPTNNLDIeSIDA-----LGEAINEYKGAVIVVSHD 798
Cdd:COG0444 151 LSGGMRQRVMIArALAL-EPKLLIADEPTTALDV-TIQAqilnlLKDLQRELGLAILFITHD 210
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
627-835 |
9.97e-08 |
|
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: 55.64 E-value: 9.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYQGQK-PLFKNLDFGIDMDSRICIVGPNGVGKSTLLllltgkltpthgemrknhRLKIGFFNQQY-------- 697
Cdd:TIGR03375 466 FRNVSFAYPGQEtPALDNVSLTIRPGEKVAIIGRIGSGKSTLL------------------KLLLGLYQPTEgsvlldgv 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 698 -AEQLRMEEtpteyLQRGFNLPYQDAR-----------------------KCLGRFGLE----SHAH--TIQI----CKL 743
Cdd:TIGR03375 528 dIRQIDPAD-----LRRNIGYVPQDPRlfygtlrdnialgapyaddeeilRAAELAGVTefvrRHPDglDMQIgergRSL 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 744 SGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKG--AVIVVSHDA-------RLItetncqlwVVEE 814
Cdd:TIGR03375 603 SGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAgkTLVLVTHRTslldlvdRII--------VMDN 674
|
250 260
....*....|....*....|.
gi 69354671 815 QSVSqIDGDfedyKREVLEAL 835
Cdd:TIGR03375 675 GRIV-ADGP----KDQVLEAL 690
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
627-798 |
1.13e-07 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 53.94 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYQ---GQKPLFKNLDFGIDMDSRICIVGPNGVGKS-----------------TLlllltgkltptHGEMRKNH 686
Cdd:COG1116 10 LRGVSKRFPtggGGVTALDDVSLTVAAGEFVALVGPSGCGKStllrliaglekptsgevLV-----------DGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 687 RLKIGF-FnQQYA-------EQ-----LRMEETPT-EYLQRgfnlpyqdARKCLGRFGLESHAHtiqicK----LSGGQK 748
Cdd:COG1116 79 GPDRGVvF-QEPAllpwltvLDnvalgLELRGVPKaERRER--------ARELLELVGLAGFED-----AyphqLSGGMR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 69354671 749 ARVVFAE-LAcREPDVLILDEPTNNLDIESIDALGEAI----NEYKGAVIVVSHD 798
Cdd:COG1116 145 QRVAIARaLA-NDPEVLLMDEPFGALDALTRERLQDELlrlwQETGKTVLFVTHD 198
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
323-479 |
1.48e-07 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 53.06 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 323 DLYIVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNI-DVLLCEQEVVAdetpavqavLRADtKRLKL----LEEERRL 397
Cdd:COG0410 23 SLEVEEGEIVALLGRNGAGKTTLLKAISG---LLPPRSgSIRFDGEDITG---------LPPH-RIARLgigyVPEGRRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 398 QGQL------------EQGDDTAAERLEKVYE---ELRatgaaaaeakarrilaglgfdpEMQNRPTQKFSGGWRMRVSL 462
Cdd:COG0410 90 FPSLtveenlllgayaRRDRAEVRADLERVYElfpRLK----------------------ERRRQRAGTLSGGEQQMLAI 147
|
170
....*....|....*..
gi 69354671 463 ARALFMEPTLLMLDEPT 479
Cdd:COG0410 148 GRALMSRPKLLLLDEPS 164
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
438-506 |
1.56e-07 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 52.86 E-value: 1.56e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 69354671 438 LGFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGW--RKTLLIVSH 506
Cdd:cd03248 138 SGYDTEVGEKGSQ-LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAH 207
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
326-525 |
1.62e-07 |
|
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: 52.67 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 326 IVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNIDVLLCEQEVVADetpavqavlrADTKRLKLLEEERRLQGQLEQGD 405
Cdd:cd03269 23 VEKGEIFGLLGPNGAGKTTTIRMILG---IILPDSGEVLFDGKPLDI----------AARNRIGYLPEERGLYPKMKVID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 406 -------------DTAAERLEKVYEELratgaaaaeakarrilaGLGfdpEMQNRPTQKFSGGWRMRVSLARALFMEPTL 472
Cdd:cd03269 90 qlvylaqlkglkkEEARRRIDEWLERL-----------------ELS---EYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 69354671 473 LMLDEPTNHLD-LNAVIWLN--NYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQR 525
Cdd:cd03269 150 LILDEPFSGLDpVNVELLKDviRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
321-526 |
1.73e-07 |
|
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: 53.27 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLceqevvadetpAVQAVLRADTKRLKLLEEERRLQGQ 400
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLL--GLEKPAQGTVSF-----------RGQDLYQLDRKQRRAFRRDVQLVFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 401 LEQG----DDTAAERLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLD 476
Cdd:TIGR02769 96 DSPSavnpRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 69354671 477 EPTNHLD--LNAVI--WLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQRL 526
Cdd:TIGR02769 176 EAVSNLDmvLQAVIleLLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
446-508 |
1.74e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 54.32 E-value: 1.74e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 446 NR-PTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVI----WLNNYLQGWRKTLLIVSHDQ 508
Cdd:PRK10851 131 DRyPAQ-LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKelrrWLRQLHEELKFTSVFVTHDQ 197
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
630-814 |
1.84e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.59 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 630 VTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMR-----------KNHRLKIGFFNQQYA 698
Cdd:PRK13647 10 LHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvmgrevnaeneKWVRSKVGLVFQDPD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 699 EQL--------------RMEETPTEYLQRgfnlpYQDARKCLGRFGLESHA--HtiqickLSGGQKARVVFAELACREPD 762
Cdd:PRK13647 90 DQVfsstvwddvafgpvNMGLDKDEVERR-----VEEALKAVRMWDFRDKPpyH------LSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 69354671 763 VLILDEPTNNLDIESIDALGEAINEYKGA---VIVVSHDARLITETNCQLWVVEE 814
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQgktVIVATHDVDLAAEWADQVIVLKE 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
627-798 |
2.23e-07 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 52.26 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRL---------KIGFFNQQY 697
Cdd:cd03301 3 LENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDvtdlppkdrDIAMVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 698 AEQLRMeetpTEYLQRGFNLPYQDARKCLGRFGLESHAHTIQICK--------LSGGQKARVVFAELACREPDVLILDEP 769
Cdd:cd03301 82 ALYPHM----TVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHlldrkpkqLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190
....*....|....*....|....*....|...
gi 69354671 770 TNNLD----IESIDALGEAINEYKGAVIVVSHD 798
Cdd:cd03301 158 LSNLDaklrVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
307-515 |
2.26e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.97 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 307 EKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIanraLSIPPNIdvllcEQEVVADETPAVQAVLRADTK 386
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMV----VGIVPRD-----AGNIIIDDEDISLLPLHARAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 387 R-LKLLEEE----RRLQ------GQLEQGDDTAAERLEKVYEELRATGAAAaeakarrilaglgfdpEMQNRPTQKFSGG 455
Cdd:PRK10895 78 RgIGYLPQEasifRRLSvydnlmAVLQIRDDLSAEQREDRANELMEEFHIE----------------HLRDSMGQSLSGG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 69354671 456 WRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKT---LLIVSHDQGFLDDVC 515
Cdd:PRK10895 142 ERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSglgVLITDHNVRETLAVC 204
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
722-801 |
2.28e-07 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 52.44 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 722 ARKCLGRFGLES--HAHTIQickLSGGQKARVVFAELACREPDVLILDEPTNNLDIES----IDALgEAINEYKGA-VIV 794
Cdd:COG4181 127 ARALLERVGLGHrlDHYPAQ---LSGGEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLL-FELNRERGTtLVL 202
|
....*..
gi 69354671 795 VSHDARL 801
Cdd:COG4181 203 VTHDPAL 209
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
627-798 |
2.33e-07 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 52.71 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYQGQKPLFkNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMR-KNH----------------RLK 689
Cdd:COG4161 5 LKNINCFYGSHQALF-DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiAGHqfdfsqkpsekairllRQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 690 IGFFNQQYA--EQLRMEETPTEYLQRGFNLPYQDAR----KCLGRFGLESHAHTIQIcKLSGGQKARVVFAELACREPDV 763
Cdd:COG4161 84 VGMVFQQYNlwPHLTVMENLIEAPCKVLGLSKEQARekamKLLARLRLTDKADRFPL-HLSGGQQQRVAIARALMMEPQV 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 69354671 764 LILDEPTNNLDIESIDALGEAINEYKGAVI---VVSHD 798
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGItqvIVTHE 200
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
742-833 |
2.37e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 742 KLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKG----AVIVVSHDARLITETNcQLWVV---EE 814
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnenrITIIIAHRLSTIRYAN-TIFVLsnrER 657
|
90
....*....|....*....
gi 69354671 815 QSVSQIDGDFEDYKREVLE 833
Cdd:PTZ00265 658 GSTVDVDIIGEDPTKDNKE 676
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
305-519 |
2.60e-07 |
|
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: 54.41 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 305 KLEKFSISAHGKELFVNADLyivagrryGLVGPNGKGKTTLLKHIANR----ALSIPPNIDVLLCEQEVVADETPAVQAV 380
Cdd:COG1245 350 SYGGFSLEVEGGEIREGEVL--------GIVGPNGIGKTTFAKILAGVlkpdEGEVDEDLKISYKPQYISPDYDGTVEEF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 381 LRadtkrlklleeerrlqgqleqgdDTAAERLEKVYEElratgaaaaeakaRRILAGLGFDPEMQnRPTQKFSGGWRMRV 460
Cdd:COG1245 422 LR-----------------------SANTDDFGSSYYK-------------TEIIKPLGLEKLLD-KNVKDLSGGELQRV 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 69354671 461 SLARALFMEPTLLMLDEPTNHLD----LNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDII 519
Cdd:COG1245 465 AIAACLSRDADLYLLDEPSAHLDveqrLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
637-798 |
3.19e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.91 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 637 QKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMR---------------KNHRLKIGFFNQQYAEQL 701
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagyhitpetgnknlKKLRKKVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 702 rMEET---PTEYLQRGFNLPYQDAR----KCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLD 774
Cdd:PRK13641 99 -FENTvlkDVEFGPKNFGFSEDEAKekalKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180
....*....|....*....|....*..
gi 69354671 775 IESIDALGEAINEYKGA---VIVVSHD 798
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAghtVILVTHN 204
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
434-526 |
3.82e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 52.38 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 434 ILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLN---AVIWLNNYLQGWRKT-LLIVSHDQG 509
Cdd:PRK10419 134 MLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVlqaGVIRLLKKLQQQFGTaCLFITHDLR 213
|
90
....*....|....*..
gi 69354671 510 FLDDVCTDIIHLDAQRL 526
Cdd:PRK10419 214 LVERFCQRVMVMDNGQI 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
321-508 |
4.51e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 52.92 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVvaDETPAVQAVLRADTKRLKLLEE---ERRL 397
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLA--GFEQPTAGQIMLDGVDL--SHVPPYQRPINMMFQSYALFPHmtvEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 398 QGQLEQGDDTAAERLEKVYEELratgaaaaeakarrilaGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDE 477
Cdd:PRK11607 113 AFGLKQDKLPKAEIASRVNEML-----------------GLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190
....*....|....*....|....*....|....*
gi 69354671 478 PTNHLD--LNAVIWLN--NYLQGWRKTLLIVSHDQ 508
Cdd:PRK11607 176 PMGALDkkLRDRMQLEvvDILERVGVTCVMVTHDQ 210
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
315-516 |
4.56e-07 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 51.62 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 315 GKELFV--NADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALsiPPNIDVLLCEQEVVADetpAVQAVLRadtkrlKLLE 392
Cdd:TIGR02324 18 GVRLPVlkNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYL--PDSGRILVRHEGAWVD---LAQASPR------EVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 393 EERRLQGQLEQGDDtAAER---LEKVYEELRAT--GAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALF 467
Cdd:TIGR02324 87 VRRKTIGYVSQFLR-VIPRvsaLEVVAEPLLERgvPREAARARARELLARLNIPERLWHLPPATFSGGEQQRVNIARGFI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 69354671 468 MEPTLLMLDEPTNHLDLN---AVIWLNNYLQGWRKTLLIVSHDQGFLDDVCT 516
Cdd:TIGR02324 166 ADYPILLLDEPTASLDAAnrqVVVELIAEAKARGAALIGIFHDEEVRELVAD 217
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
324-507 |
4.95e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 52.05 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 324 LYIVAGRRYGLVGPNGKGKTTLLKHIanRALSIPPNIDVLLCEQEVvadeTPAVQAVLRA---------DTKRLKLLEEE 394
Cdd:PRK13647 26 LSIPEGSKTALLGPNGAGKSTLLLHL--NGIYLPQRGRVKVMGREV----NAENEKWVRSkvglvfqdpDDQVFSSTVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 395 RRLQGQLEQGDDtAAERLEKVYEELRATGAAaaeakarrilaglgfdpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLM 474
Cdd:PRK13647 100 DVAFGPVNMGLD-KDEVERRVEEALKAVRMW-----------------DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 69354671 475 LDEPTNHLD------LNAVIW-LNNylQGwrKTLLIVSHD 507
Cdd:PRK13647 162 LDEPMAYLDprgqetLMEILDrLHN--QG--KTVIVATHD 197
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
743-803 |
5.56e-07 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 51.32 E-value: 5.56e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEY--KGAVIVVSHdaRLIT 803
Cdd:cd03248 151 LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAH--RLST 211
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
743-802 |
5.68e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 53.27 E-value: 5.68e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINE--YKGAVIVVSHDARLI 802
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGHRSTLA 547
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
720-815 |
5.74e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 51.32 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 720 QDARKCLGRFGLESHAHTIQiCKLSGGQKARVVFAELACREPDVLILDEPTNNLDIES----IDALGEAINEYKGAVIVV 795
Cdd:PRK10584 125 NGAKALLEQLGLGKRLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgdkiADLLFSLNREHGTTLILV 203
|
90 100
....*....|....*....|
gi 69354671 796 SHDARLITETNCQLWVVEEQ 815
Cdd:PRK10584 204 THDLQLAARCDRRLRLVNGQ 223
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
333-507 |
6.37e-07 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 51.64 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 333 GLVGPNGKGKTTLLKHIANR-----ALSIPPNIDVLLCEQEVVADETPAVQAVLRADTKRLklleeerrlqgqleqgddt 407
Cdd:cd03237 29 GILGPNGIGKTTFIKMLAGVlkpdeGDIEIELDTVSYKPQYIKADYEGTVRDLLSSITKDF------------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 408 aaerLEKVYEElratgaaaaeakaRRILAGLGFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD---- 483
Cdd:cd03237 90 ----YTHPYFK-------------TEIAKPLQIEQILDREVPE-LSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqr 151
|
170 180
....*....|....*....|....
gi 69354671 484 LNAVIWLNNYLQGWRKTLLIVSHD 507
Cdd:cd03237 152 LMASKVIRRFAENNEKTAFVVEHD 175
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
321-507 |
6.46e-07 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 51.31 E-value: 6.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVA---DETPAVQ--AVLRADTKRLKLLEEER 395
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLIS--GLAQPTSGGVILEGKQITEpgpDRMVVFQnySLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 396 RLQGQLEQGddtaaERLEKVYEELRatgaaaaeakarriLAGLGfdpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLML 475
Cdd:TIGR01184 81 RVLPDLSKS-----ERRAIVEEHIA--------------LVGLT---EAADKRPGQLSGGMKQRVAIARALSIRPKVLLL 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 69354671 476 DEPTNHLDL----NAVIWLNNYLQGWRKTLLIVSHD 507
Cdd:TIGR01184 139 DEPFGALDAltrgNLQEELMQIWEEHRVTVLMVTHD 174
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
453-521 |
7.30e-07 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 51.34 E-value: 7.30e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 69354671 453 SGGWRMRVSLARALFMEPTLLMLDEPTNHLD---LNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHL 521
Cdd:COG4598 156 SGGQQQRAAIARALAMEPEVMLFDEPTSALDpelVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFL 227
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
743-814 |
7.36e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 52.71 E-value: 7.36e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKG--AVIVVSHdaRLIT-ETNCQLWVVEE 814
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH--RLSTiEKADEILVVED 553
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
442-529 |
7.80e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 52.03 E-value: 7.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 442 PEMQNRPT---QKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD--LNAVIW--LNNYLQGWRKTLLIVSHDQGFLDDV 514
Cdd:PRK09473 149 PEARKRMKmypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDvtVQAQIMtlLNELKREFNTAIIMITHDLGVVAGI 228
|
90
....*....|....*
gi 69354671 515 CTDIIHLDAQRLHYY 529
Cdd:PRK09473 229 CDKVLVMYAGRTMEY 243
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
634-797 |
8.40e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 50.64 E-value: 8.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 634 YQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRlkiGFFNQQYAEQ---------LRME 704
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG---DIDDPDVAEAchylghrnaMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 705 ETPTEYLQ--RGFNLPYQ-DARKCLGRFGLeSHAHTIQICKLSGGQKARVVFAEL-ACREPdVLILDEPTNNLDIESIDA 780
Cdd:PRK13539 88 LTVAENLEfwAAFLGGEElDIAAALEAVGL-APLAHLPFGYLSAGQKRRVALARLlVSNRP-IWILDEPTAALDAAAVAL 165
|
170 180
....*....|....*....|
gi 69354671 781 LGEAINEYK---GAVIVVSH 797
Cdd:PRK13539 166 FAELIRAHLaqgGIVIAATH 185
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
743-804 |
8.55e-07 |
|
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: 52.50 E-value: 8.55e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESI----DALGEAINEYKGAVIVVSHDARLITE 804
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIED 234
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
742-797 |
8.96e-07 |
|
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: 50.44 E-value: 8.96e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 69354671 742 KLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKG---AVIVVSH 797
Cdd:cd03266 136 GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlgkCILFSTH 194
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
309-506 |
8.97e-07 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 50.00 E-value: 8.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 309 FSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnRALSipPNidvllcEQEVVADETPAvqavlradtkrL 388
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLT-GDLK--PQ------QGEITLDGVPV-----------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 389 KLLEEERRLQGQLEQgddtaaerleKVYEelratgaaaaeakarrilaglgFDPEMQNRPTQKFSGGWRMRVSLARALFM 468
Cdd:cd03247 68 DLEKALSSLISVLNQ----------RPYL----------------------FDTTLRNNLGRRFSGGERQRLALARILLQ 115
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 69354671 469 EPTLLMLDEPTNHLD-LNAVIWLNNYLQGWR-KTLLIVSH 506
Cdd:cd03247 116 DAPIVLLDEPTVGLDpITERQLLSLIFEVLKdKTLIWITH 155
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
627-798 |
9.05e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 51.53 E-value: 9.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEM------------RKNHRLKIGFFN 694
Cdd:PRK13644 4 LENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidtgdfskLQGIRKLVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 695 QQYAEQL--RMEETPTEYLQRGFNLPYQDARK----CLGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDE 768
Cdd:PRK13644 84 QNPETQFvgRTVEEDLAFGPENLCLPPIEIRKrvdrALAEIGLEKYRHR-SPKTLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190
....*....|....*....|....*....|...
gi 69354671 769 PTNNLDIESIDALGEAINEY--KGAVIV-VSHD 798
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKLheKGKTIVyITHN 195
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
304-798 |
1.10e-06 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 52.11 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLkHIANRALSIPPN-----IDVLLCEQ----------- 367
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLM-HVLRGMDQYEPTsgriiYHVALCEKcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 368 -----------EVVADETPAVQAVLRADTKRLK--------LLEEERRLQGQLEQGDDTAAERLEKVYEELRATGAAaae 428
Cdd:TIGR03269 80 epcpvcggtlePEEVDFWNLSDKLRRRIRKRIAimlqrtfaLYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 429 akarrilaglgfdpEMQNRPT---QKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK----TL 501
Cdd:TIGR03269 157 --------------QLSHRIThiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasgiSM 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 502 LIVSHDQGFLDDVCTDIIHLDaqrlhyyrgnymtfkkmyqqkqkellkqyekqekklkelkaggKSTKQAEKQTKEALTR 581
Cdd:TIGR03269 223 VLTSHWPEVIEDLSDKAIWLE-------------------------------------------NGEIKEEGTPDEVVAV 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 582 KQQKCRRKNQDEESQEAPELLKRpKEYTVRFtfpdppplsppvlglhgvtfgYQGQKPLFKNLDfGIDMDSR----ICIV 657
Cdd:TIGR03269 260 FMEGVSEVEKECEVEVGEPIIKV-RNVSKRY---------------------ISVDRGVVKAVD-NVSLEVKegeiFGIV 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 658 GPNGVGKSTLLLLLTGKLTPTHGE-----------MRK-----NHRLK--IGFFNQQYAeqLRMEETPTEYLQR--GFNL 717
Cdd:TIGR03269 317 GTSGAGKTTLSKIIAGVLEPTSGEvnvrvgdewvdMTKpgpdgRGRAKryIGILHQEYD--LYPHRTVLDNLTEaiGLEL 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 718 PYQDARK----CLGRFGL-ESHAHTI---QICKLSGGQKARVVFAELACREPDVLILDEPTNNLD-------IESIDALG 782
Cdd:TIGR03269 395 PDELARMkaviTLKMVGFdEEKAEEIldkYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkvdvTHSILKAR 474
|
570
....*....|....*.
gi 69354671 783 EAINEykgAVIVVSHD 798
Cdd:TIGR03269 475 EEMEQ---TFIIVSHD 487
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
321-514 |
1.13e-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: 51.64 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIA--NRAlsippnidvllCEQEVVADETpavqaVLRADTKRLKLLEEERRL- 397
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAglERP-----------DSGRIRLGGE-----VLQDSARGIFLPPHRRRIg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 398 --------------QGQLEQG-----DDTAAERLEKVYEELratgaaaaeakarrilaGLGfdpEMQNRPTQKFSGGWRM 458
Cdd:COG4148 81 yvfqearlfphlsvRGNLLYGrkrapRAERRISFDEVVELL-----------------GIG---HLLDRRPATLSGGERQ 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 69354671 459 RVSLARALFMEPTLLMLDEPTNHLDL---NAVIwlnNYLQGWRKTL----LIVSHDqgfLDDV 514
Cdd:COG4148 141 RVAIGRALLSSPRLLLMDEPLAALDLarkAEIL---PYLERLRDELdipiLYVSHS---LDEV 197
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
624-774 |
1.24e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 51.34 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 624 VLGLHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMR----------KNHRLKIGFF 693
Cdd:PRK13537 7 PIDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsraRHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 694 NQqyAEQLRMEETPTEYLQ---RGFNLPYQDARKC---LGRFG-LESHAHTiQICKLSGGQKARVVFAELACREPDVLIL 766
Cdd:PRK13537 86 PQ--FDNLDPDFTVRENLLvfgRYFGLSAAAARALvppLLEFAkLENKADA-KVGELSGGMKRRLTLARALVNDPDVLVL 162
|
....*...
gi 69354671 767 DEPTNNLD 774
Cdd:PRK13537 163 DEPTTGLD 170
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
726-806 |
1.24e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 50.26 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 726 LGRFGLESHAHTIQIcKLSGGQKARVVFAELACREPDVLILDEPTNNLD---IESIDALGEAINEYKGAVIVVSHDARLI 802
Cdd:PRK10908 122 LDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
....
gi 69354671 803 TETN 806
Cdd:PRK10908 201 SRRS 204
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
625-798 |
1.25e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 50.83 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 625 LGLHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLllltgkltpthgemrknhRLKIGfFNQQYAEQLRME 704
Cdd:PRK11247 13 LLLNAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLL------------------RLLAG-LETPSAGELLAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 705 ETPTEYLQRGFNLPYQDAR------------------------KCLGRFGLESHAHTIQiCKLSGGQKARVVFAELACRE 760
Cdd:PRK11247 73 TAPLAEAREDTRLMFQDARllpwkkvidnvglglkgqwrdaalQALAAVGLADRANEWP-AALSGGQKQRVALARALIHR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 69354671 761 PDVLILDEPTNNLD----IESIDALGEAINEYKGAVIVVSHD 798
Cdd:PRK11247 152 PGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
451-506 |
1.32e-06 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 52.09 E-value: 1.32e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 69354671 451 KFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------LNAviwLNNYLQGwrKTLLIVSH 506
Cdd:COG1132 476 NLSGGQRQRIAIARALLKDPPILILDEATSALDtetealiQEA---LERLMKG--RTTIVIAH 533
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
317-483 |
1.39e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 50.68 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 317 ELFVNADLYIVAGRRYGLVGPNGKGKTTLLKhIANRALSIPPNI----DVLLCEQEV----VADETPAVQAVLRADTKRL 388
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLR-VFNRLIELYPEArvsgEVYLDGQDIfkmdVIELRRRVQMVFQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 389 KL-LEEERRLQGQLEQGDDTAAERLEKVYEELRATGAAAaeakarrilaglgfdpEMQNR---PTQKFSGGWRMRVSLAR 464
Cdd:PRK14247 96 NLsIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWD----------------EVKDRldaPAGKLSGGQQQRLCIAR 159
|
170
....*....|....*....
gi 69354671 465 ALFMEPTLLMLDEPTNHLD 483
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLD 178
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
627-798 |
1.47e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 50.40 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYQGQKPLFkNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMR-KNH----------------RLK 689
Cdd:PRK11124 5 LNGINCFYGAHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNiAGNhfdfsktpsdkairelRRN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 690 IGFFNQQY--------AEQLRmeETPTEYLQRGFNLPYQDARKCLGRFGLESHAHTIQIcKLSGGQKARVVFAELACREP 761
Cdd:PRK11124 84 VGMVFQQYnlwphltvQQNLI--EAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPL-HLSGGQQQRVAIARALMMEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 69354671 762 DVLILDEPTNNLDIESIDALGEAINEYKGAVI---VVSHD 798
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAETGItqvIVTHE 200
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
321-508 |
1.54e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 51.26 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVvadetpavqavlradTKR------LKLLEEE 394
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVA--GLEKPTEGQIFIDGEDV---------------THRsiqqrdICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 395 RRLQGQLEQGDD----------TAAERLEKVYEELRATGaaaaeakarriLAGlgfdpeMQNRPTQKFSGGWRMRVSLAR 464
Cdd:PRK11432 87 YALFPHMSLGENvgyglkmlgvPKEERKQRVKEALELVD-----------LAG------FEDRYVDQISGGQQQRVALAR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 69354671 465 ALFMEPTLLMLDEPTNHLDLNaviwLNNYL--------QGWRKTLLIVSHDQ 508
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLDAN----LRRSMrekirelqQQFNITSLYVTHDQ 197
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
627-774 |
1.60e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 50.98 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYQGqKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMR----------KNHRLKIGFFNQq 696
Cdd:PRK13536 44 LAGVSKSYGD-KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvparaRLARARIGVVPQ- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 697 yAEQLRMEETPTEYL---QRGFNLPYQDARKC---LGRFG-LESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEP 769
Cdd:PRK13536 122 -FDNLDLEFTVRENLlvfGRYFGMSTREIEAVipsLLEFArLESKADA-RVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
....*
gi 69354671 770 TNNLD 774
Cdd:PRK13536 200 TTGLD 204
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
329-520 |
1.63e-06 |
|
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: 50.44 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 329 GRRYGLVGPNGKGKTTLLKHIANRalsIPPNidvlLCEQevvaDETPAVQAVLRAdtKRLKLLEE--ERRLQGQLE---- 402
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGK---LKPN----LGKF----DDPPDWDEILDE--FRGSELQNyfTKLLEGDVKvivk 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 403 ---------QGDDTAAERLEKVYEelratgaaaaEAKARRILAGLGFDPEMqNRPTQKFSGGWRMRVSLARALFMEPTLL 473
Cdd:cd03236 93 pqyvdlipkAVKGKVGELLKKKDE----------RGKLDELVDQLELRHVL-DRNIDQLSGGELQRVAIAAALARDADFY 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 69354671 474 MLDEPTNHLD----LNAVIWLNNYLQGwRKTLLIVSHDQGFLdDVCTDIIH 520
Cdd:cd03236 162 FFDEPSSYLDikqrLNAARLIRELAED-DNYVLVVEHDLAVL-DYLSDYIH 210
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
634-800 |
1.85e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 50.05 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 634 YQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHrlKIGFFNQQY----AEQLRME----- 704
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG--KVLYFGKDIfqidAIKLRKEvgmvf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 705 --ETPTEYLQRGFNLPY-------QDARK-------CLGRFGLESHAH---TIQICKLSGGQKARVVFAELACREPDVLI 765
Cdd:PRK14246 97 qqPNPFPHLSIYDNIAYplkshgiKEKREikkiveeCLRKVGLWKEVYdrlNSPASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 69354671 766 LDEPTNNLDIESIDALGEAINEYKG--AVIVVSHDAR 800
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQ 213
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
720-797 |
1.89e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 50.62 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 720 QDARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKG---AVIVVS 796
Cdd:PRK13631 154 KLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnnkTVFVIT 233
|
.
gi 69354671 797 H 797
Cdd:PRK13631 234 H 234
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
742-838 |
1.98e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 50.85 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 742 KLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAI----NEYKGAVIVVSHDARLITETNCQLWVVEEQSV 817
Cdd:PRK10851 136 QLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLrqlhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
90 100
....*....|....*....|....*.
gi 69354671 818 SQIdGDFEDYKRE-----VLEALGEV 838
Cdd:PRK10851 216 EQA-GTPDQVWREpatrfVLEFMGEV 240
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
453-522 |
2.05e-06 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 49.99 E-value: 2.05e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 69354671 453 SGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------LNAVIWLNNylQGWrkTLLIVSHDQGFLDDVCTDIIHLD 522
Cdd:COG1126 138 SGGQQQRVAIARALAMEPKVMLFDEPTSALDpelvgevLDVMRDLAK--EGM--TMVVVTHEMGFAREVADRVVFMD 210
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
304-514 |
2.10e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.50 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFV-----NADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNI---DVLLCEQEVVADETP 375
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFAsralfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgDIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 376 AVQAVLRADTKRLKLLEEERRLQG----------QLEQGDDTAAERLEKVyeelratgaaaaeakarrilaglGFDPEMQ 445
Cdd:PRK13643 82 VRKKVGVVFQFPESQLFEETVLKDvafgpqnfgiPKEKAEKIAAEKLEMV-----------------------GLADEFW 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 69354671 446 NRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR---KTLLIVSHdqgFLDDV 514
Cdd:PRK13643 139 EKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHqsgQTVVLVTH---LMDDV 207
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
304-483 |
2.24e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 50.01 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRalsippnidvllceqeVVADETPAVQAVLRA 383
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL----------------ITGDKSAGSHIELLG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 384 DTkrlklLEEERRLQGqleqgdDTAAERLEKVYEELRATGAAAAEAKARRILAGLG-----------FDPEMQNRPTQ-- 450
Cdd:PRK09984 69 RT-----VQREGRLAR------DIRKSRANTGYIFQQFNLVNRLSVLENVLIGALGstpfwrtcfswFTREQKQRALQal 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 69354671 451 --------------KFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 483
Cdd:PRK09984 138 trvgmvhfahqrvsTLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
726-798 |
2.32e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 49.70 E-value: 2.32e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 69354671 726 LGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDI----ESIDALGEAINEYKGAVIVVSHD 798
Cdd:COG4604 120 IAYLDLEDLADR-YLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHD 195
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
630-798 |
2.37e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 49.98 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 630 VTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGemrknHRLKIGFFNQQYAEQ--------- 700
Cdd:PRK10253 13 LTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHG-----HVWLDGEHIQHYASKevarrigll 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 701 LRMEETP-----TEYLQRGfNLPYQ-----------DARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVL 764
Cdd:PRK10253 87 AQNATTPgditvQELVARG-RYPHQplftrwrkedeEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 69354671 765 ILDEPTNNLDI-ESIDALG--EAINEYKGAVI-VVSHD 798
Cdd:PRK10253 166 LLDEPTTWLDIsHQIDLLEllSELNREKGYTLaAVLHD 203
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
333-478 |
2.38e-06 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 49.46 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 333 GLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVADET-----------PAVQAVLRadtkrlKLLEEERrLQGQL 401
Cdd:cd03218 30 GLLGPNGAGKTTTFYMIV--GLVKPDSGKILLDGQDITKLPMhkrarlgigylPQEASIFR------KLTVEEN-ILAVL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 69354671 402 EQGDDTAAERLEKVyEELratgaaaaeakarriLAGLGFDPeMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEP 478
Cdd:cd03218 101 EIRGLSKKEREEKL-EEL---------------LEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
743-797 |
2.39e-06 |
|
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: 48.19 E-value: 2.39e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKG---AVIVVSH 797
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISH 140
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
309-483 |
2.75e-06 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 49.54 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 309 FSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKhianralSIPPNIDVllCEQEVVADETpavqavlraDTKRL 388
Cdd:cd03251 8 FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVN-------LIPRFYDV--DSGRILIDGH---------DVRDY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 389 KLlEEERRLQGQLEQG----DDTAAE-----RLEKVYEELRATGAAAAEAKARRILAGlGFDPEMQNRPTqKFSGGWRMR 459
Cdd:cd03251 70 TL-ASLRRQIGLVSQDvflfNDTVAEniaygRPGATREEVEEAARAANAHEFIMELPE-GYDTVIGERGV-KLSGGQRQR 146
|
170 180
....*....|....*....|....
gi 69354671 460 VSLARALFMEPTLLMLDEPTNHLD 483
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALD 170
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
742-844 |
2.96e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.01 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 742 KLSGGQKARVVFAELACREPDVLILDEPTNNLDI---ESIDALGEAIN-EYKGAVIVVSHDARLITETNCQLWVVEEQSV 817
Cdd:PRK13645 150 ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPkgeEDFINLFERLNkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
90 100
....*....|....*....|....*..
gi 69354671 818 SQIDGDFEDYKREvlEALGEVMVSRPR 844
Cdd:PRK13645 230 ISIGSPFEIFSNQ--ELLTKIEIDPPK 254
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
323-483 |
3.09e-06 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 50.05 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 323 DLYIVAGRRYGLVGPNGKGKTTLlkhianrALSI-----PPNI---DVLLCEQEVvadetpavqavlradtkrLKLLEEE 394
Cdd:COG0444 25 SFDVRRGETLGLVGESGSGKSTL-------ARAIlgllpPPGItsgEILFDGEDL------------------LKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 395 -RRLQG----------------------QLE-----QGDDTAAERLEKVYEELRatgaaaaeakarriLAGLGFDPEMQN 446
Cdd:COG0444 80 lRKIRGreiqmifqdpmtslnpvmtvgdQIAeplriHGGLSKAEARERAIELLE--------------RVGLPDPERRLD 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 69354671 447 R-PTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 483
Cdd:COG0444 146 RyPHE-LSGGMRQRVMIARALALEPKLLIADEPTTALD 182
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
636-776 |
3.12e-06 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 49.32 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 636 GQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMR-------------KNHRLKIGFFNQQYA--EQ 700
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIvdglkvndpkvdeRLIRQEAGMVFQQFYlfPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 701 LRMEET----PTEYLQRGFNLPYQDARKCLGRFGLESHAHTIQiCKLSGGQKARVVFAE-LACRePDVLILDEPTNNLDI 775
Cdd:PRK09493 92 LTALENvmfgPLRVRGASKEEAEKQARELLAKVGLAERAHHYP-SELSGGQQQRVAIARaLAVK-PKLMLFDEPTSALDP 169
|
.
gi 69354671 776 E 776
Cdd:PRK09493 170 E 170
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
326-507 |
3.21e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 49.55 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 326 IVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNIDVLLCEQeVVADETPAVQAVLRAdtkrlKLLEEERRLQG------ 399
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAG---LLPGSGSIQFAGQ-PLEAWSAAELARHRA-----YLSQQQTPPFAmpvfqy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 400 -QLEQGDDTAAERLEKVYEELRATgaaaaeakarrilagLGFDPEMqNRPTQKFSGGWRMRVSLA-------RALFMEPT 471
Cdd:PRK03695 90 lTLHQPDKTRTEAVASALNEVAEA---------------LGLDDKL-GRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQ 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 69354671 472 LLMLDEPTNHLDLNAVIWLNNYL-----QGwrKTLLIVSHD 507
Cdd:PRK03695 154 LLLLDEPMNSLDVAQQAALDRLLselcqQG--IAVVMSSHD 192
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
743-796 |
3.29e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 50.40 E-value: 3.29e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 69354671 743 LSGG--QKarVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEY--KG-AVIVVS 796
Cdd:COG1129 395 LSGGnqQK--VVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELaaEGkAVIVIS 451
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
304-507 |
3.54e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 49.31 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNIDVLLCEQEVVADETpAVQAVLRA 383
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAG---FVPYQHGSITLDGKPVEGPG-AERGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 384 DTKRLKLLEEERRLQGQLEQGDDTAAERLEKVYEELRATGaaaaeakarriLAGLGfdpemqNRPTQKFSGGWRMRVSLA 463
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVG-----------LEGAE------KRYIWQLSGGQRQRVGIA 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 69354671 464 RALFMEPTLLMLDEPTNHLD---------LNAVIWlnnylQGWRKTLLIVSHD 507
Cdd:PRK11248 141 RALAANPQLLLLDEPFGALDaftreqmqtLLLKLW-----QETGKQVLLITHD 188
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
306-802 |
3.73e-06 |
|
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: 50.55 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 306 LEKFSISAHGKELFVnadLY----IVAGRRYGLVGPNGKGKTTLLKhianrALS--IPPNidvlLCEqevvADETPAVQA 379
Cdd:COG1245 75 LEEDPVHRYGENGFR---LYglpvPKKGKVTGILGPNGIGKSTALK-----ILSgeLKPN----LGD----YDEEPSWDE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 380 VLradtKRL----------KLLEEE--------------RRLQGqleqgddTAAERLEKVYEElratgaaaaeAKARRIL 435
Cdd:COG1245 139 VL----KRFrgtelqdyfkKLANGEikvahkpqyvdlipKVFKG-------TVRELLEKVDER----------GKLDELA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 436 AGLGFDPEMqNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD----LNAVIWLNNYLQGwRKTLLIVSHDQGFL 511
Cdd:COG1245 198 EKLGLENIL-DRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIRELAEE-GKYVLVVEHDLAIL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 512 DDVcTDIIHLdaqrLHYYRGNYMTFKKMYQQKQ--KELLKQYEkqekklkelkaggkstkQAE--KQTKEALTRKQQKCR 587
Cdd:COG1245 276 DYL-ADYVHI----LYGEPGVYGVVSKPKSVRVgiNQYLDGYL-----------------PEEnvRIRDEPIEFEVHAPR 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 588 RKNQDEESQEAPELLKRPKEYTVRftfpdppplsppvlglhgVTFG--YQGQKplfknldfgidmdsrICIVGPNGVGKS 665
Cdd:COG1245 334 REKEEETLVEYPDLTKSYGGFSLE------------------VEGGeiREGEV---------------LGIVGPNGIGKT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 666 TLLLLLTGKLTPTHGEMRKNhrLKIGfFNQQYAEQlRMEETPTEYLQRGFNLPYQDAR---KCLGRFGLEsHAHTIQICK 742
Cdd:COG1245 381 TFAKILAGVLKPDEGEVDED--LKIS-YKPQYISP-DYDGTVEEFLRSANTDDFGSSYyktEIIKPLGLE-KLLDKNVKD 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAIN----EYKGAVIVVSHDARLI 802
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRrfaeNRGKTAMVVDHDIYLI 519
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
642-802 |
3.82e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 49.31 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 642 KNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEM----------RK---NHRLKIGFFNQQYAEQL---RMEE 705
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVlikgepikydKKsllEVRKTVGIVFQNPDDQLfapTVEE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 706 T----------PTEYLQRGFnlpyQDARKCLGRFGLESHA-HtiqicKLSGGQKARVVFAELACREPDVLILDEPTNNLD 774
Cdd:PRK13639 99 DvafgplnlglSKEEVEKRV----KEALKAVGMEGFENKPpH-----HLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
170 180 190
....*....|....*....|....*....|..
gi 69354671 775 ---IESIDALGEAINEyKGAVIVVS-HDARLI 802
Cdd:PRK13639 170 pmgASQIMKLLYDLNK-EGITIIIStHDVDLV 200
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
321-529 |
4.08e-06 |
|
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: 48.68 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNidvllcEQEVVADETPAvqAVLRA-----------DTKRLK 389
Cdd:cd03220 40 DVSFEVPRGERIGLIGRNGAGKSTLLRLLAG---IYPPD------SGTVTVRGRVS--SLLGLgggfnpeltgrENIYLN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 390 LleeerRLQGQLeqgDDTAAERLEKVYEelratgaaaaeakarriLAGLGfdpEMQNRPTQKFSGGWRMRVSLARALFME 469
Cdd:cd03220 109 G-----RLLGLS---RKEIDEKIDEIIE-----------------FSELG---DFIDLPVKTYSSGMKARLAFAIATALE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 69354671 470 PTLLMLDEPTNHLDLN----AVIWLNNYLQGwRKTLLIVSHDQGFLDDVCTDIIHLDAQRLHYY 529
Cdd:cd03220 161 PDILLIDEVLAVGDAAfqekCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
722-776 |
4.32e-06 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 48.84 E-value: 4.32e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 69354671 722 ARKCLGRFGLESHAHT--IQickLSGGQKARVVFAELACREPDVLILDEPTNNLDIE 776
Cdd:COG1126 117 AMELLERVGLADKADAypAQ---LSGGQQQRVAIARALAMEPKVMLFDEPTSALDPE 170
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
625-798 |
4.34e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 50.49 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 625 LGLHGVTFGYQ---GQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGE------------------MR 683
Cdd:PRK10535 5 LELKDIRRSYPsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdvatldadalaqLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 684 KNHrlkIGFFNQQY-------AEQlrMEETPTEYLQRGFNLPYQDARKCLGRFGLESHAHtIQICKLSGGQKARVVFAEL 756
Cdd:PRK10535 85 REH---FGFIFQRYhllshltAAQ--NVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVE-YQPSQLSGGQQQRVSIARA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 69354671 757 ACREPDVLILDEPTNNLDIES---IDALGEAINEYKGAVIVVSHD 798
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSgeeVMAILHQLRDRGHTVIIVTHD 203
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
271-486 |
4.50e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 50.19 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 271 VASLKAANAAendfsVSQAEMSSRQAMLENASDIKLEKFSI-SAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHI 349
Cdd:COG4178 335 LAGFEEALEA-----ADALPEAASRIETSEDGALALEDLTLrTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 350 A------NRALSIPPNIDVLLCEQEvvadetPAV------QAVLRADTKRlklleeerrlqgqlEQGDDTAAERLEKVYe 417
Cdd:COG4178 410 AglwpygSGRIARPAGARVLFLPQR------PYLplgtlrEALLYPATAE--------------AFSDAELREALEAVG- 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 69354671 418 elratgaaaaeakarriLAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNA 486
Cdd:COG4178 469 -----------------LGHLAERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEEN 520
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
315-527 |
6.02e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 48.33 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 315 GKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKhianralsippnidvLLCeqevvADETPAVQAVLRA--DTKRLKLLE 392
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLK---------------LIC-----GIERPSAGKIWFSghDITRLKNRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 393 EE--RRLQGQLEQGDDTAAERleKVYEE------LRATGAAAAEAKARRILAGLGFDPEMQNRPTQkFSGGWRMRVSLAR 464
Cdd:PRK10908 74 VPflRRQIGMIFQDHHLLMDR--TVYDNvaipliIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 69354671 465 ALFMEPTLLMLDEPTNHLD---LNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQRLH 527
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
720-798 |
7.98e-06 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 48.99 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 720 QDARKCLGRFGLESHAHTI--QickLSGGQKARVVFAE-LAcREPDVLILDEPTNNLDIESIDA----LGEAINEYKGAV 792
Cdd:COG1118 112 ARVEELLELVQLEGLADRYpsQ---LSGGQRQRVALARaLA-VEPEVLLLDEPFGALDAKVRKElrrwLRRLHDELGGTT 187
|
....*.
gi 69354671 793 IVVSHD 798
Cdd:COG1118 188 VFVTHD 193
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
624-798 |
8.18e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 48.47 E-value: 8.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 624 VLGLHGVTFGYQGQ-KPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNH-----------RLKIG 691
Cdd:PRK13635 5 IIRVEHISFRYPDAaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseetvwdvRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 692 FFNQQYAEQ-------------LRMEETP-TEYLQRgfnlpYQDArkcLGRFGLESHAHTiQICKLSGGQKARVVFAELA 757
Cdd:PRK13635 85 MVFQNPDNQfvgatvqddvafgLENIGVPrEEMVER-----VDQA---LRQVGMEDFLNR-EPHRLSGGQKQRVAIAGVL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 69354671 758 CREPDVLILDEPTNNLD----IESIDALGEAINEYKGAVIVVSHD 798
Cdd:PRK13635 156 ALQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITHD 200
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
333-478 |
9.09e-06 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 47.72 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 333 GLVGPNGKGKTTLLKHIANRalsIPPNI-DVLLCEQEVVADetPAVQavlRAdtkRLKL--LEEE----RRL------QG 399
Cdd:COG1137 33 GLLGPNGAGKTTTFYMIVGL---VKPDSgRIFLDGEDITHL--PMHK---RA---RLGIgyLPQEasifRKLtvedniLA 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 69354671 400 QLEQGDDTAAERLEKVyEELratgaaaaeakarriLAGLGFDpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEP 478
Cdd:COG1137 102 VLELRKLSKKEREERL-EEL---------------LEEFGIT-HLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
334-483 |
9.09e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 49.28 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 334 LVGPNGKGKTTLLKHIANRalsIPPNI----DVLLCEQEVVADETPAVQAVLRADTKRLKLL--EEERRLQGQLEQGDDT 407
Cdd:TIGR00955 56 VMGSSGAGKTTLMNALAFR---SPKGVkgsgSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLtvREHLMFQAHLRMPRRV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 408 AA----ERLEKVYEELRATGAAAAEAKARRILAGLgfdpemqnrptqkfSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 483
Cdd:TIGR00955 133 TKkekrERVDEVLQALGLRKCANTRIGVPGRVKGL--------------SGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
625-798 |
9.16e-06 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 48.56 E-value: 9.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 625 LGLHGVTFGYqGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLlllltgkltpthgemrknhrLKI--GFfnqqyaeqlr 702
Cdd:COG3842 6 LELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTL--------------------LRMiaGF---------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 703 meETPTE---YL-----------QRGFNLPYQD------------------------------ARKCLGRFGLESHAHTi 738
Cdd:COG3842 55 --ETPDSgriLLdgrdvtglppeKRNVGMVFQDyalfphltvaenvafglrmrgvpkaeirarVAELLELVGLEGLADR- 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 69354671 739 QICKLSGGQKARVVFAE-LACrEPDVLILDEPTNNLD----IESIDALGEAINEYKGAVIVVSHD 798
Cdd:COG3842 132 YPHQLSGGQQQRVALARaLAP-EPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHD 195
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
305-520 |
9.34e-06 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 47.75 E-value: 9.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 305 KLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLCEQEVVADETpavqavlrad 384
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEVTSGSILLDGEDILELSP---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 385 TKR-----------------------LKLLEEERRlqgqleQGDDTAAERLEKVYEELRAtgaaaaeakarrilagLGFD 441
Cdd:COG0396 72 DERaragiflafqypveipgvsvsnfLRTALNARR------GEELSAREFLKLLKEKMKE----------------LGLD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 442 PEMQNRP-TQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD---LNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTD 517
Cdd:COG0396 130 EDFLDRYvNEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDidaLRIVAEGVNKLRSPDRGILIITHYQRILDYIKPD 209
|
...
gi 69354671 518 IIH 520
Cdd:COG0396 210 FVH 212
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
320-507 |
9.42e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 48.00 E-value: 9.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 320 VNADLYivAGRRYGLVGPNGKGKTTLLKHIANRalsIPPnidvllceqevvadETPAVQAVLRADTKR--LKLLEEERRL 397
Cdd:PRK11701 25 VSFDLY--PGEVLGIVGESGSGKTTLLNALSAR---LAP--------------DAGEVHYRMRDGQLRdlYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 398 ---------------------------------QGQLEQGD--DTAAERLEKVyeELratgaaaaeakarrilaglgfDP 442
Cdd:PRK11701 86 llrtewgfvhqhprdglrmqvsaggnigerlmaVGARHYGDirATAGDWLERV--EI---------------------DA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 443 E-MQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTL----LIVSHD 507
Cdd:PRK11701 143 ArIDDLPTT-FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglavVIVTHD 211
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
742-818 |
9.58e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 48.14 E-value: 9.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 742 KLSGGQKARVVFAE-LACrEPDVLILDEPTNNLDI----ESIDALGEAINEYKGAVIVVSHDARLItETNCQLWV----- 811
Cdd:PRK10419 151 QLSGGQLQRVCLARaLAV-EPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLV-ERFCQRVMvmdng 228
|
....*....
gi 69354671 812 --VEEQSVS 818
Cdd:PRK10419 229 qiVETQPVG 237
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
434-507 |
9.60e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 48.31 E-value: 9.60e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 434 ILAGLGFDPeMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVI----WLNNYLQGWRKTLLIVSHD 507
Cdd:PRK13636 125 ALKRTGIEH-LKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSeimkLLVEMQKELGLTIIIATHD 201
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
334-507 |
1.07e-05 |
|
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: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 334 LVGPNGKGKTTLLKHIANralSIPPNI-DVLLCEQEVvadETP-AVQAV----------LRA-DTKRLKLleeerRLQGQ 400
Cdd:COG4525 38 ALGASGCGKTTLLNLIAG---FLAPSSgEITLDGVPV---TGPgADRGVvfqkdallpwLNVlDNVAFGL-----RLRGV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 401 leqgddTAAERLEKVYEELRatgaaaaeakarriLAGLGfdpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTN 480
Cdd:COG4525 107 ------PKAERRARAEELLA--------------LVGLA---DFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFG 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 69354671 481 HLD---------LNAVIWlnnylQGWRKTLLIVSHD 507
Cdd:COG4525 164 ALDaltreqmqeLLLDVW-----QRTGKGVFLITHS 194
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
726-804 |
1.11e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 47.96 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 726 LGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIES----IDALGEAINEYKgAVIVVSHDARL 801
Cdd:PRK15056 127 LARVDMVEFRHR-QIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTeariISLLRELRDEGK-TMLVSTHNLGS 204
|
...
gi 69354671 802 ITE 804
Cdd:PRK15056 205 VTE 207
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
453-547 |
1.11e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 49.07 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 453 SGGWRMRVSLARALFMEPTLLMLDEPTNHLDL---NAVIW-LNNYLQGwrKTLLIVSHDQGFLDDVctDIIHLDAQRLHY 528
Cdd:PRK11174 487 SVGQAQRLALARALLQPCQLLLLDEPTASLDAhseQLVMQaLNAASRR--QTTLMVTHQLEDLAQW--DQIWVMQDGQIV 562
|
90 100
....*....|....*....|....*.
gi 69354671 529 YRGNYMT-------FKKMYQQKQKEL 547
Cdd:PRK11174 563 QQGDYAElsqagglFATLLAHRQEEI 588
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
743-797 |
1.13e-05 |
|
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: 47.58 E-value: 1.13e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 743 LSGGQKARVVFAE-LACrEPDVLILDEPTNNLDIE---SIDALGEAINEYKG-AVIVVSH 797
Cdd:cd03258 141 LSGGQKQRVGIARaLAN-NPKVLLCDEATSALDPEttqSILALLRDINRELGlTIVLITH 199
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
743-798 |
1.19e-05 |
|
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: 48.91 E-value: 1.19e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 69354671 743 LSGGQKARVVFA-ELACrEPDVLILDEPTNNLDI----ESIDALGEAINEYKGAVIVVSHD 798
Cdd:COG4172 157 LSGGQRQRVMIAmALAN-EPDLLIADEPTTALDVtvqaQILDLLKDLQRELGMALLLITHD 216
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
743-803 |
1.21e-05 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 47.44 E-value: 1.21e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLDI----ESIDALGEAINEYKGAVIVVSH---DARLIT 803
Cdd:COG3840 130 LSGGQRQRVALARCLVRKRPILLLDEPFSALDPalrqEMLDLVDELCRERGLTVLMVTHdpeDAARIA 197
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
446-528 |
1.22e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 48.16 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 446 NRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNA--VIW--LNNYLQGWRKTLLIVSHDqgfLDDV---CTDI 518
Cdd:COG4586 149 DTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSkeAIRefLKEYNRERGTTILLTSHD---MDDIealCDRV 225
|
90
....*....|
gi 69354671 519 IHLDAQRLHY 528
Cdd:COG4586 226 IVIDHGRIIY 235
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
743-798 |
1.28e-05 |
|
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: 47.33 E-value: 1.28e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLDIES----IDALGEAINEYKGAVIVVSHD 798
Cdd:cd03299 130 LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHD 189
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
304-513 |
1.30e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 47.27 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGkeLFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNIDVLLCEQEVVADETPAvqavlra 383
Cdd:PRK10771 2 LKLTDITWLYHH--LPMRFDLTVERGERVAILGPSGAGKSTLLNLIAG---FLTPASGSLTLNGQDHTTTPPS------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 384 dtKR-LKLLEEERRLQGQL--EQ----GDD-----TAAERLEkvyeelratgaaaaeakARRILAGLGFDPEMQNRPTQk 451
Cdd:PRK10771 70 --RRpVSMLFQENNLFSHLtvAQniglGLNpglklNAAQREK-----------------LHAIARQMGIEDLLARLPGQ- 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 69354671 452 FSGGWRMRVSLARALFMEPTLLMLDEPTNHLD--LNAVI--WLNNYLQGWRKTLLIVSHDqgfLDD 513
Cdd:PRK10771 130 LSGGQRQRVALARCLVREQPILLLDEPFSALDpaLRQEMltLVSQVCQERQLTLLMVSHS---LED 192
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
644-796 |
1.31e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 47.70 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 644 LDFGIDMDSRICIVGPNGVGKSTLLLLLT-----GKLTPTHGEMRKNHRLKIGffnqQYAEQLRMEETPTEYLQRGFNL- 717
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSglitgDKSAGSHIELLGRTVQREG----RLARDIRKSRANTGYIFQQFNLv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 718 -----------------PY-------------QDARKCLGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILD 767
Cdd:PRK09984 99 nrlsvlenvligalgstPFwrtcfswftreqkQRALQALTRVGMVHFAHQ-RVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190
....*....|....*....|....*....|...
gi 69354671 768 EPTNNLDIES----IDALGEaINEYKGAVIVVS 796
Cdd:PRK09984 178 EPIASLDPESarivMDTLRD-INQNDGITVVVT 209
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
722-798 |
1.45e-05 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 47.44 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 722 ARKCLGRFGLESHAHTIQIcKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIdalGEAIN------EYKGAVIVV 795
Cdd:PRK11264 125 ARELLAKVGLAGKETSYPR-RLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELV---GEVLNtirqlaQEKRTMVIV 200
|
...
gi 69354671 796 SHD 798
Cdd:PRK11264 201 THE 203
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
633-803 |
1.57e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 47.02 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 633 GYQ-GQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEmrknhrlkIGFFNQQYA----EQLRME--- 704
Cdd:PRK10247 14 GYLaGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGT--------LLFEGEDIStlkpEIYRQQvsy 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 705 --ETPT---EYLQRGFNLPYQDARKC---------LGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPT 770
Cdd:PRK10247 86 caQTPTlfgDTVYDNLIFPWQIRNQQpdpaiflddLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 69354671 771 NNLDIESIDALGEAINEY----KGAVIVVSHDARLIT 803
Cdd:PRK10247 166 SALDESNKHNVNEIIHRYvreqNIAVLWVTHDKDEIN 202
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
630-774 |
1.66e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 47.71 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 630 VTFGYQGQKPL----FKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMR----------KNHRLK------ 689
Cdd:PRK13634 8 VEHRYQYKTPFerraLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTigervitagkKNKKLKplrkkv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 690 -IGFfnqQYAEQLRMEETPTEYLQRG---FNLPYQDA----RKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREP 761
Cdd:PRK13634 88 gIVF---QFPEHQLFEETVEKDICFGpmnFGVSEEDAkqkaREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEP 164
|
170
....*....|...
gi 69354671 762 DVLILDEPTNNLD 774
Cdd:PRK13634 165 EVLVLDEPTAGLD 177
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
334-506 |
1.68e-05 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 48.57 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 334 LVGPNGKGKTT---LLKHIANralsipPNidvllcEQEVVADETPAVQAVLRADTKRLKLLEEERRLQGQLEQgdDTAAE 410
Cdd:TIGR00958 512 LVGPSGSGKSTvaaLLQNLYQ------PT------GGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVR--ENIAY 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 411 RLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAviwl 490
Cdd:TIGR00958 578 GLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQ-LSGGQKQRIAIARALVRKPRVLILDEATSALDAEC---- 652
|
170 180
....*....|....*....|
gi 69354671 491 NNYLQGWRK----TLLIVSH 506
Cdd:TIGR00958 653 EQLLQESRSrasrTVLLIAH 672
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
636-798 |
1.70e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 47.27 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 636 GQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNH------RLKIGFFNQQYAEQLRMEETPTE 709
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvRDKDGQLKVADKNQLRLLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 710 YLQRGFNL-------------PYQ-------DAR----KCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLI 765
Cdd:PRK10619 96 MVFQHFNLwshmtvlenvmeaPIQvlglskqEAReravKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 69354671 766 LDEPTNNLDIESIDA---LGEAINEYKGAVIVVSHD 798
Cdd:PRK10619 176 FDEPTSALDPELVGEvlrIMQQLAEEGKTMVVVTHE 211
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
742-798 |
1.71e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 47.42 E-value: 1.71e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 69354671 742 KLSGGQKARVVFAELACREPDVLILDEPTNNLD----IESIDALGEAINEYKGAVIVVSHD 798
Cdd:PRK13650 140 RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD 200
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
721-798 |
2.34e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 47.41 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 721 DARKclgRFGLESHahtiqicKLSGGQKARVVFA-ELACRePDVLILDEPTNNLDIeSIDA-----LGEAINEYKGAVIV 794
Cdd:PRK09473 150 EARK---RMKMYPH-------EFSGGMRQRVMIAmALLCR-PKLLIADEPTTALDV-TVQAqimtlLNELKREFNTAIIM 217
|
....
gi 69354671 795 VSHD 798
Cdd:PRK09473 218 ITHD 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
329-802 |
2.46e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.88 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 329 GRRYGLVGPNGKGKTTLLKhianrALS--IPPNidvlLCEQEvvadETPAVQAVLRAdTKRLKLLEEERRL-QGQL---- 401
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVK-----ILSgeLIPN----LGDYE----EEPSWDEVLKR-FRGTELQNYFKKLyNGEIkvvh 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 402 ---------EQGDDTAAERLEKVYEElratgaaaaeAKARRILAGLGFDPEMqNRPTQKFSGGWRMRVSLARALFMEPTL 472
Cdd:PRK13409 165 kpqyvdlipKVFKGKVRELLKKVDER----------GKLDEVVERLGLENIL-DRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 473 LMLDEPTNHLD----LNAVIWLNNYLQGwrKTLLIVSHDQGFLDDVcTDIIHLdaqrlhyyrgnymtfkkMYQQKqkell 548
Cdd:PRK13409 234 YFFDEPTSYLDirqrLNVARLIRELAEG--KYVLVVEHDLAVLDYL-ADNVHI-----------------AYGEP----- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 549 kqyekqekklkelKAGGKSTKQaeKQTKEALtrkqqkcrrkNQ------DEES----QEAPELLKRPKEytvrftfpdpP 618
Cdd:PRK13409 289 -------------GAYGVVSKP--KGVRVGI----------NEylkgylPEENmrirPEPIEFEERPPR----------D 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 619 PLSPPVLglhgVTFGyqgqkPLFKNL-DFGIDMDSR-------ICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNhrLKI 690
Cdd:PRK13409 334 ESERETL----VEYP-----DLTKKLgDFSLEVEGGeiyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--LKI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 691 GFfNQQY--------AEQLRMEETP---TEYLQRGFNLPYQdarkcLGRFgLEShahtiQICKLSGGQKARVVFAelAC- 758
Cdd:PRK13409 403 SY-KPQYikpdydgtVEDLLRSITDdlgSSYYKSEIIKPLQ-----LERL-LDK-----NVKDLSGGELQRVAIA--ACl 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 69354671 759 -REPDVLILDEPTNNLDIESIDALGEAIN----EYKGAVIVVSHDARLI 802
Cdd:PRK13409 469 sRDADLYLLDEPSAHLDVEQRLAVAKAIRriaeEREATALVVDHDIYMI 517
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
299-507 |
2.65e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 46.58 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 299 ENASDI-KLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKhIANRAlsippnIDVLLCEQEVVADETPAV 377
Cdd:PRK14246 5 KSAEDVfNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLK-VLNRL------IEIYDSKIKVDGKVLYFG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 378 QAVLRADTKRLklleeeRRLQGQLEQGDDTAAERleKVYEELRATGAAAAEAKARRI-------LAGLGFDPEMQNR--- 447
Cdd:PRK14246 78 KDIFQIDAIKL------RKEVGMVFQQPNPFPHL--SIYDNIAYPLKSHGIKEKREIkkiveecLRKVGLWKEVYDRlns 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 69354671 448 PTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK--TLLIVSHD 507
Cdd:PRK14246 150 PASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
321-507 |
2.87e-05 |
|
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: 46.48 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIaNRaLSIPPNIDVLLCEQEVVADETPAVQAVLRadtKRLKLLEEERRLQGQ 400
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCI-NR-LIEPTSGKVLIDGQDIAAMSRKELRELRR---KKISMVFQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 401 LEQGDDTA----------AERLEKVYEELRatgaaaaeakarriLAGLGfdPEMQNRPTQkFSGGWRMRVSLARALFMEP 470
Cdd:cd03294 117 RTVLENVAfglevqgvprAEREERAAEALE--------------LVGLE--GWEHKYPDE-LSGGMQQRVGLARALAVDP 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 69354671 471 TLLMLDEPTNHLD-------LNAVIWLNNYLQgwrKTLLIVSHD 507
Cdd:cd03294 180 DILLMDEAFSALDplirremQDELLRLQAELQ---KTIVFITHD 220
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
323-508 |
2.88e-05 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 46.99 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 323 DLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALsIPPN-----IDvllceQEVVADETPAvqavlradtKR---------- 387
Cdd:COG3839 23 DLDIEDGEFLVLLGPSGCGKSTLLRMIA--GL-EDPTsgeilIG-----GRDVTDLPPK---------DRniamvfqsya 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 388 --------------LKLleeeRRLqgqleqgddTAAERLEKVYEelratgaaaaeakarrILAGLGFDPEMQNRPTQkFS 453
Cdd:COG3839 86 lyphmtvyeniafpLKL----RKV---------PKAEIDRRVRE----------------AAELLGLEDLLDRKPKQ-LS 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 69354671 454 GGWRMRVSLARALFMEPTLLMLDEPTNHLD-----------------LNAviwlnnylqgwrkTLLIVSHDQ 508
Cdd:COG3839 136 GGQRQRVALGRALVREPKVFLLDEPLSNLDaklrvemraeikrlhrrLGT-------------TTIYVTHDQ 194
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
722-774 |
2.89e-05 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 46.39 E-value: 2.89e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 69354671 722 ARKCLGRFGLEsHAHTIQICKLSGGQKARVVFAE-LACrEPDVLILDEPTNNLD 774
Cdd:COG4525 115 AEELLALVGLA-DFARRRIWQLSGGMRQRVGIARaLAA-DPRFLLMDEPFGALD 166
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
321-514 |
3.19e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 46.70 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIanRALSIPPNIDVLLCEQEVVADETpavQAVLRADTKRLKLLEE------- 393
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLIQNI--NALLKPTTGTVTVDDITITHKTK---DKYIRPVRKRIGMVFQfpesqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 394 ERRLQGQLEQGDDTAAERLEKVYEElratgaaaaeakARRILAGLGFDPE-MQNRPTQkFSGGWRMRVSLARALFMEPTL 472
Cdd:PRK13646 100 EDTVEREIIFGPKNFKMNLDEVKNY------------AHRLLMDLGFSRDvMSQSPFQ-MSGGQMRKIAIVSILAMNPDI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 69354671 473 LMLDEPTNHLDLNA---VIWLNNYLQ-GWRKTLLIVSHDqgfLDDV 514
Cdd:PRK13646 167 IVLDEPTAGLDPQSkrqVMRLLKSLQtDENKTIILVSHD---MNEV 209
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
742-797 |
3.20e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 46.44 E-value: 3.20e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 742 KLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKG--AVIVVSH 797
Cdd:PRK14247 146 KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
722-776 |
3.27e-05 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 46.33 E-value: 3.27e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 69354671 722 ARKCLGRFGLES--HAHTIQickLSGGQKARVVFAELACREPDVLILDEPTNNLDIE 776
Cdd:COG4598 135 AEALLAKVGLADkrDAYPAH---LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPE 188
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
320-529 |
3.31e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 46.23 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 320 VNADLYivAGRRYGLVGPNGKGKTTLLKHIANralSIPPNIDVLLCEQEVVAdetpavqavlradtkrlkLLEeerrLQG 399
Cdd:COG1134 45 VSFEVE--RGESVGIIGRNGAGKSTLLKLIAG---ILEPTSGRVEVNGRVSA------------------LLE----LGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 400 QLeQGDDTAAE--RL------------EKVYEElratgaaaaeakarrIL--AGLG--FDpemqnRPTQKFSGGWRMRVS 461
Cdd:COG1134 98 GF-HPELTGREniYLngrllglsrkeiDEKFDE---------------IVefAELGdfID-----QPVKTYSSGMRARLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 462 LARALFMEPTLLMLDEptnhldlnaVI-------------WLNNYLQGwRKTLLIVSHDQGFLDDVCTDIIHLDAQRLHY 528
Cdd:COG1134 157 FAVATAVDPDILLVDE---------VLavgdaafqkkclaRIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVM 226
|
.
gi 69354671 529 Y 529
Cdd:COG1134 227 D 227
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
742-844 |
3.43e-05 |
|
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: 46.34 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 742 KLSGGQKARVVFAELACREPDVLILDEPTNNLDI---ESIDALGEAINEYKG-AVIVVSHDARLITETNCQLWV------ 811
Cdd:TIGR02769 150 QLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMvlqAVILELLRKLQQAFGtAYLFITHDLRLVQSFCQRVAVmdkgqi 229
|
90 100 110
....*....|....*....|....*....|...
gi 69354671 812 VEEQSVSQIDGDFEDYKREVLEAlgeVMVSRPR 844
Cdd:TIGR02769 230 VEECDVAQLLSFKHPAGRNLQSA---VLPEHPV 259
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
743-797 |
3.43e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 46.37 E-value: 3.43e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKG--AVIVVSH 797
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTH 206
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
742-797 |
3.47e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 46.18 E-value: 3.47e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 69354671 742 KLSGGQKARVVFAelacR----EPDVLILDEPTNNLDIESIDALGEAINEYKG--AVIVVSH 797
Cdd:COG1117 154 GLSGGQQQRLCIA----RalavEPEVLLMDEPTSALDPISTAKIEELILELKKdyTIVIVTH 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
445-507 |
3.48e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 46.61 E-value: 3.48e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 69354671 445 QNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK---TLLIVSHD 507
Cdd:PRK13639 131 ENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKegiTIIISTHD 196
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
627-798 |
3.78e-05 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 46.14 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNH-----------RLKIGFFNQ 695
Cdd:cd03295 3 FENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelRRKIGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 696 QYA-------EQ-----LRMEETPTEYLQrgfnlpyQDARKCLGRFGLES------HAHtiqicKLSGGQKARVVFAELA 757
Cdd:cd03295 83 QIGlfphmtvEEnialvPKLLKWPKEKIR-------ERADELLALVGLDPaefadrYPH-----ELSGGQQQRVGVARAL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 69354671 758 CREPDVLILDEPTNNLDIESIDALGEA---INEYKGAVIV-VSHD 798
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEfkrLQQELGKTIVfVTHD 195
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
304-542 |
4.30e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.94 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRAlsippnidvllcEQEVVADEtpavqaVLRA 383
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRE------------DYEVTGGT------VEFK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 384 DTKRLKLLEEERRLQGQLEQGD--------------DTAAERLEKvYEELRATGAAAAEAKARRILAGLGFDPEMQNRPT 449
Cdd:PRK09580 64 GKDLLELSPEDRAGEGIFMAFQypveipgvsnqfflQTALNAVRS-YRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 450 Q-KFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAV-IWLN--NYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQR 525
Cdd:PRK09580 143 NvGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALkIVADgvNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQG 222
|
250
....*....|....*..
gi 69354671 526 LHYYRGNYMTFKKMYQQ 542
Cdd:PRK09580 223 RIVKSGDFTLVKQLEEQ 239
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
303-483 |
4.30e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 46.17 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 303 DIKLEKFSISAHGKELFVNADLY-----IVAGRRYGLVGPNGKGKTTLLKHIanRALSIPPNIDVLLCEQEVVADETPav 377
Cdd:PRK13634 2 DITFQKVEHRYQYKTPFERRALYdvnvsIPSGSYVAIIGHTGSGKSTLLQHL--NGLLQPTSGTVTIGERVITAGKKN-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 378 qavlradtKRLKLLeeeRRLQG--------QLEQgddtaaERLEK----------VYEElratgaaAAEAKARRILAGLG 439
Cdd:PRK13634 78 --------KKLKPL---RKKVGivfqfpehQLFE------ETVEKdicfgpmnfgVSEE-------DAKQKAREMIELVG 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 69354671 440 FDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 483
Cdd:PRK13634 134 LPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
624-798 |
4.59e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 45.99 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 624 VLGLHGVTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEM----------RK---NHRLKI 690
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysRKglmKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 691 GFFNQQYAEQLRMEET--PTEYLQRGFNLPYQDARK----CLGRFGLESHAHTIQICkLSGGQKARVVFAELACREPDVL 764
Cdd:PRK13636 85 GMVFQDPDNQLFSASVyqDVSFGAVNLKLPEDEVRKrvdnALKRTGIEHLKDKPTHC-LSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 69354671 765 ILDEPTNNLD----IESIDALGEAINEYKGAVIVVSHD 798
Cdd:PRK13636 164 VLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHD 201
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
327-483 |
5.10e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 45.95 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 327 VAGR--RYGLVGPNGKGKTTLLKHIaNRALSiPPNIDVLLCEQEVVADETPAVQAVL-----RADTKRLKLLEEERRLQG 399
Cdd:PRK13652 26 IAPRnsRIAVIGPNGAGKSTLFRHF-NGILK-PTSGSVLIRGEPITKENIREVRKFVglvfqNPDDQIFSPTVEQDIAFG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 400 QLEQGDD--TAAERLEKVyeelratgaaaaeakarriLAGLGFDpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDE 477
Cdd:PRK13652 104 PINLGLDeeTVAHRVSSA-------------------LHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
....*.
gi 69354671 478 PTNHLD 483
Cdd:PRK13652 164 PTAGLD 169
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
630-775 |
5.16e-05 |
|
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: 47.04 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 630 VTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNH-----------RLKIGFFNQQ-- 696
Cdd:TIGR01193 479 VSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslkdidrhtlRQFINYLPQEpy 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 697 -----YAEQLRM---EETPTEYLQRGFNLPY--QDARKCLGRFG--LESHAHTIqicklSGGQKARVVFAELACREPDVL 764
Cdd:TIGR01193 559 ifsgsILENLLLgakENVSQDEIWAACEIAEikDDIENMPLGYQteLSEEGSSI-----SGGQKQRIALARALLTDSKVL 633
|
170
....*....|.
gi 69354671 765 ILDEPTNNLDI 775
Cdd:TIGR01193 634 ILDESTSNLDT 644
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
296-508 |
5.44e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 46.48 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 296 AMLENASDIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVvaDETP 375
Cdd:PRK09452 7 QPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIA--GFETPDSGRIMLDGQDI--THVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 376 A----VQAVLR----------ADTKRLKLleeerRLQGQleqgddTAAERLEKVYEELRATGaaaaeakarriLAGLGfd 441
Cdd:PRK09452 83 AenrhVNTVFQsyalfphmtvFENVAFGL-----RMQKT------PAAEITPRVMEALRMVQ-----------LEEFA-- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 69354671 442 pemQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLI----VSHDQ 508
Cdd:PRK09452 139 ---QRKPHQ-LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGItfvfVTHDQ 205
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
654-803 |
5.65e-05 |
|
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: 45.48 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 654 ICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNhRLKIGFFNQQY-------AEQLRMEETPTEYLQRGFNlpyQDARKCL 726
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-LDTVSYKPQYIkadyegtVRDLLSSITKDFYTHPYFK---TEIAKPL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 727 GRFGLESHahtiQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEY----KGAVIVVSHDARLI 802
Cdd:cd03237 104 QIEQILDR----EVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVEHDIIMI 179
|
.
gi 69354671 803 T 803
Cdd:cd03237 180 D 180
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
434-507 |
5.90e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 45.16 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 434 ILAGLGFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------LNAVIWLNnylQGWRKTLLIVSH 506
Cdd:PRK10584 130 LLEQLGLGKRLDHLPAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGNLDrqtgdkiADLLFSLN---REHGTTLILVTH 205
|
.
gi 69354671 507 D 507
Cdd:PRK10584 206 D 206
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
434-507 |
6.42e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 46.64 E-value: 6.42e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 69354671 434 ILAGLGFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNA---VIWLNNYLQGWRKTLLIVSHD 507
Cdd:PRK10535 128 LLQRLGLEDRVEYQPSQ-LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSgeeVMAILHQLRDRGHTVIIVTHD 203
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
625-802 |
6.46e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 45.34 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 625 LGLHGVTFGYQGQKPLFknlDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMR---KNHR--------LKIGFF 693
Cdd:PRK10771 2 LKLTDITWLYHHLPMRF---DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTlngQDHTttppsrrpVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 694 NQQYAEQLRMEETPTEYLQRGFNL-PYQDA--RKCLGRFGLESHAHTIQiCKLSGGQKARVVFAELACREPDVLILDEPT 770
Cdd:PRK10771 79 ENNLFSHLTVAQNIGLGLNPGLKLnAAQREklHAIARQMGIEDLLARLP-GQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 69354671 771 NNLD----IESIDALGEAINEYKGAVIVVSH---DARLI 802
Cdd:PRK10771 158 SALDpalrQEMLTLVSQVCQERQLTLLMVSHsleDAARI 196
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
306-484 |
6.52e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 45.55 E-value: 6.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 306 LEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRalSIPPNIDVLLCEQEVVADETPAV-------- 377
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRH--QPPSEGEILLDAQPLESWSSKAFarkvaylp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 378 QAVLRADTKRLKLLEEERRLQGQLEQGDDTAAERlEKVYEElratgaaaaeakarriLAGLGFDPeMQNRPTQKFSGGWR 457
Cdd:PRK10575 92 QQLPAAEGMTVRELVAIGRYPWHGALGRFGAADR-EKVEEA----------------ISLVGLKP-LAHRLVDSLSGGER 153
|
170 180
....*....|....*....|....*..
gi 69354671 458 MRVSLARALFMEPTLLMLDEPTNHLDL 484
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
742-844 |
6.68e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.89 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 742 KLSGGQKARVVFA-ELACRePDVLILDEPTNNLDI----ESIDALGEAINEYKGAVIVVSHDARLITETNCQL------W 810
Cdd:PRK11022 153 QLSGGMSQRVMIAmAIACR-PKLLIADEPTTALDVtiqaQIIELLLELQQKENMALVLITHDLALVAEAAHKIivmyagQ 231
|
90 100 110
....*....|....*....|....*....|....*
gi 69354671 811 VVEEQSVSQI-DGDFEDYKREVLEALGEVMVSRPR 844
Cdd:PRK11022 232 VVETGKAHDIfRAPRHPYTQALLRALPEFAQDKAR 266
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
642-789 |
6.69e-05 |
|
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: 45.05 E-value: 6.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 642 KNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMR----------KNHRLKIGFFNQQYAeqLRMEETPTEYL 711
Cdd:cd03265 17 RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATvaghdvvrepREVRRRIGIVFQDLS--VDDELTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 712 Q---RGFNLPYQDARK----CLGRFGLESHAHTIqICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEA 784
Cdd:cd03265 95 YihaRLYGVPGAERRErideLLDFVGLLEAADRL-VKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEY 173
|
....*
gi 69354671 785 INEYK 789
Cdd:cd03265 174 IEKLK 178
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
642-798 |
7.06e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 45.85 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 642 KNLDFGIDMDSRICIVGPNGVGKSTLLllltgkltpthgEM----------------------RKNHRLKIGF-FNQQya 698
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTI------------KMltgilvptsgevrvlgyvpfkrRKEFARRIGVvFGQR-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 699 EQLRMEETPTE---YLQRGFNLPYQDARKCLGRF----GLESHAHTiQICKLSGGQKARvvfAELAC---REPDVLILDE 768
Cdd:COG4586 105 SQLWWDLPAIDsfrLLKAIYRIPDAEYKKRLDELvellDLGELLDT-PVRQLSLGQRMR---CELAAallHRPKILFLDE 180
|
170 180 190
....*....|....*....|....*....|....
gi 69354671 769 PTNNLDIESIDALGEAINEY---KGA-VIVVSHD 798
Cdd:COG4586 181 PTIGLDVVSKEAIREFLKEYnreRGTtILLTSHD 214
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
275-506 |
7.85e-05 |
|
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: 46.27 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 275 KAANAAENDFSVSQAEMSSRQAMLENA---SDIKLEKFSIS-AHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIA 350
Cdd:TIGR01193 442 RVANNRLNEVYLVDSEFINKKKRTELNnlnGDIVINDVSYSyGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLV 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 351 N------RALSIPP----NIDVLLCEQEVvaDETPAvQAVLRADTKRLKLLEEERRlqgQLEQGDDTAAERLEKVYEELR 420
Cdd:TIGR01193 522 GffqarsGEILLNGfslkDIDRHTLRQFI--NYLPQ-EPYIFSGSILENLLLGAKE---NVSQDEIWAACEIAEIKDDIE 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 421 ATGaaaaeakarrilagLGFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-LNAVIWLNNYLQGWRK 499
Cdd:TIGR01193 596 NMP--------------LGYQTELSEEGSS-ISGGQKQRIALARALLTDSKVLILDESTSNLDtITEKKIVNNLLNLQDK 660
|
....*..
gi 69354671 500 TLLIVSH 506
Cdd:TIGR01193 661 TIIFVAH 667
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
451-521 |
8.15e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.10 E-value: 8.15e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 69354671 451 KFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD----LNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVcTDIIHL 521
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrLNAARAIRRLSEEGKKTALVVEHDLAVLDYL-SDRIHV 144
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
640-802 |
8.21e-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: 46.28 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 640 LFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRLKIGFFNQQ-------YAEQLRMEETPTEYLQ 712
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRpymtlgtLRDQIIYPDSSEDMKR 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 713 RGFNlpYQDARKCLGRFGLEshaHTIQ-------ICK----LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDAL 781
Cdd:TIGR00954 547 RGLS--DKDLEQILDNVQLT---HILEreggwsaVQDwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYM 621
|
170 180
....*....|....*....|.
gi 69354671 782 GEAINEYKGAVIVVSHDARLI 802
Cdd:TIGR00954 622 YRLCREFGITLFSVSHRKSLW 642
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
726-803 |
8.85e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 45.56 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 726 LGRFGLESHAHTIQiCKLSGGQKARVVFAE-LACRePDVLILDEPTNNLDIE---SIDALGEAINEYKGAVIVvshdarL 801
Cdd:PRK11153 125 LELVGLSDKADRYP-AQLSGGQKQRVAIARaLASN-PKVLLCDEATSALDPAttrSILELLKDINRELGLTIV------L 196
|
..
gi 69354671 802 IT 803
Cdd:PRK11153 197 IT 198
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
627-774 |
8.99e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 45.12 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGYQGQKPLFKNLDFGIDMD----SRICIVGPNGVGKSTLLLLLTGKLTPTHGEMR---------------KNHR 687
Cdd:PRK13649 5 LQNVSYTYQAGTPFEGRALFDVNLTiedgSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRvddtlitstsknkdiKQIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 688 LKIGF-FnqQYAEQLRMEETPTEYLQRG---FNLPYQDA----RKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACR 759
Cdd:PRK13649 85 KKVGLvF--QFPESQLFEETVLKDVAFGpqnFGVSQEEAealaREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAM 162
|
170
....*....|....*
gi 69354671 760 EPDVLILDEPTNNLD 774
Cdd:PRK13649 163 EPKILVLDEPTAGLD 177
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
627-798 |
1.04e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 44.98 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 627 LHGVTFGY-QGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMR-----------KNHRLKIGFF- 693
Cdd:PRK13632 10 VENVSFSYpNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKidgitiskenlKEIRKKIGIIf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 694 ----NQ-----------------------------QYAEQLRMEetptEYLQRgfnlpyqdarkclgrfglESHahtiqi 740
Cdd:PRK13632 90 qnpdNQfigatveddiafglenkkvppkkmkdiidDLAKKVGME----DYLDK------------------EPQ------ 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 69354671 741 cKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEY----KGAVIVVSHD 798
Cdd:PRK13632 142 -NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrktrKKTLISITHD 202
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
624-802 |
1.11e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.56 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 624 VLGLHGVTFGyQGQKPLFKNLDFGIDMDSRICIVGPNGVGKStllllltGKLTPTHGEMRK-----NHRLKIGFFNQQYA 698
Cdd:COG2401 30 VLEAFGVELR-VVERYVLRDLNLEIEPGEIVLIVGASGSGKS-------TLLRLLAGALKGtpvagCVDVPDNQFGREAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 699 --EQLRMEETPTeylqrgfnlpyqDARKCLGRFGLeSHAHTIQIC--KLSGGQKARVVFAELACREPDVLILDEPTNNLD 774
Cdd:COG2401 102 liDAIGRKGDFK------------DAVELLNAVGL-SDAVLWLRRfkELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180 190
....*....|....*....|....*....|..
gi 69354671 775 IESID----ALGEAINEYKGAVIVVSHDARLI 802
Cdd:COG2401 169 RQTAKrvarNLQKLARRAGITLVVATHHYDVI 200
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
743-797 |
1.13e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 1.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKG----AVIVVSH 797
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTIITIAH 1417
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
309-506 |
1.19e-04 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 44.40 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 309 FSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIanRALSIPPNIDVLLCEQEV-VADET---PAVQAVLRAD 384
Cdd:cd03252 8 FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLI--QRFYVPENGRVLVDGHDLaLADPAwlrRQVGVVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 385 TkrlkLLEeeRRLQGQLEQGDDTAAerLEKVYEELRatgaaaaeakarriLAG---------LGFDPEMQNRPTqKFSGG 455
Cdd:cd03252 86 V----LFN--RSIRDNIALADPGMS--MERVIEAAK--------------LAGahdfiselpEGYDTIVGEQGA-GLSGG 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 69354671 456 WRMRVSLARALFMEPTLLMLDEPTNHLDLNA--VIWLNNYLQGWRKTLLIVSH 506
Cdd:cd03252 143 QRQRIAIARALIHNPRILIFDEATSALDYESehAIMRNMHDICAGRTVIIIAH 195
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
452-507 |
1.20e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 44.64 E-value: 1.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 452 FSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR----KTLLIVSHD 507
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHN 210
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
450-486 |
1.21e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 1.21e-04
10 20 30
....*....|....*....|....*....|....*..
gi 69354671 450 QKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNA 486
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
719-797 |
1.27e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.39 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 719 YQDARKCLGRFGLESHAHTIqICKLSGGQK-----ARVVFaelacREPDVLILDEPTNNLDIESIDALGEAINEYKG--- 790
Cdd:COG1129 118 RRRARELLARLGLDIDPDTP-VGDLSVAQQqlveiARALS-----RDARVLILDEPTASLTEREVERLFRIIRRLKAqgv 191
|
....*..
gi 69354671 791 AVIVVSH 797
Cdd:COG1129 192 AIIYISH 198
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
739-815 |
1.46e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 43.33 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 739 QICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAIN----EYKGAVIVVSHDARLITETNCQLWVVEE 814
Cdd:cd03222 68 QYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRrlseEGKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
.
gi 69354671 815 Q 815
Cdd:cd03222 148 E 148
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
439-506 |
1.46e-04 |
|
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: 44.07 E-value: 1.46e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 69354671 439 GFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLN--AVIW--LNNYLQGwrKTLLIVSH 506
Cdd:cd03249 128 GYDTLVGERGSQ-LSGGQKQRIAIARALLRNPKILLLDEATSALDAEseKLVQeaLDRAMKG--RTTIVIAH 196
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
697-774 |
1.55e-04 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 44.18 E-value: 1.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 697 YAEQLRMEETpteylQRGFNLPYQDARKCLGRFGLESHAHTIqICKLSGGQKARVVFAELACREPDVLILDEPTNNLD 774
Cdd:cd03234 104 YTAILRLPRK-----SSDAIRKKRVEDVLLRDLALTRIGGNL-VKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
743-798 |
1.55e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.02 E-value: 1.55e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 69354671 743 LSGG--QKarVVFA-ELAcREPDVLILDEPTNNLDIESIDALGEAINEY--KG-AVIVVSHD 798
Cdd:COG3845 403 LSGGnqQK--VILArELS-RDPKLLIAAQPTRGLDVGAIEFIHQRLLELrdAGaAVLLISED 461
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
726-774 |
1.60e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 45.42 E-value: 1.60e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 69354671 726 LGRFGLESHAHTI-----QICKLSGGQKARVVFAELACREPDVLILDEPTNNLD 774
Cdd:TIGR00955 145 LQALGLRKCANTRigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
740-798 |
1.70e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 44.28 E-value: 1.70e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 69354671 740 ICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIE---SIDALGEAINEYKGAVIVVSHD 798
Cdd:cd03236 137 IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHD 198
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
639-821 |
1.72e-04 |
|
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: 43.56 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 639 PLFKNLDFGIDMDSRICIVGPNGVGKSTllllltgkltpthgemrknhrLKIGFFNQQYAEQLRME-------ETPTEYL 711
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKST---------------------LILALFRFLEAEEGKIEidgidisTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 712 QRGFNLPYQDA-------RKCLGRFGLESHAHTIQICK-------LSGGQKARVVFAELACREPDVLILDEPTNNLDIES 777
Cdd:cd03369 81 RSSLTIIPQDPtlfsgtiRSNLDPFDEYSDEEIYGALRvsegglnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 69354671 778 IDALGEAINE-YKGA-VIVVSHdaRLITETNC-QLWVVEEQSVSQID 821
Cdd:cd03369 161 DALIQKTIREeFTNStILTIAH--RLRTIIDYdKILVMDAGEVKEYD 205
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
687-798 |
1.76e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 44.39 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 687 RLKIGFFNQQYAEQLRME--ETPTEYLQRGFNLPYQ----DARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACRE 760
Cdd:PRK13646 84 RKRIGMVFQFPESQLFEDtvEREIIFGPKNFKMNLDevknYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMN 163
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 69354671 761 PDVLILDEPTNNLDIESIDALGEAINEYK----GAVIVVSHD 798
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHD 205
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
743-774 |
1.79e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 44.64 E-value: 1.79e-04
10 20 30
....*....|....*....|....*....|..
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLD 774
Cdd:PRK11000 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
321-508 |
1.89e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 44.64 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVvADETPA---VQAVLR----------ADTKR 387
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIA--GLEDITSGDLFIGEKRM-NDVPPAergVGMVFQsyalyphlsvAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 388 --LKLLEEERRlqgQLEQGDDTAAERLEkvyeelratgaaaaeakarriLAGLgfdpeMQNRPtQKFSGGWRMRVSLARA 465
Cdd:PRK11000 98 fgLKLAGAKKE---EINQRVNQVAEVLQ---------------------LAHL-----LDRKP-KALSGGQRQRVAIGRT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 69354671 466 LFMEPTLLMLDEPTNHLD----LNAVIWLNNYLQGWRKTLLIVSHDQ 508
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDaalrVQMRIEISRLHKRLGRTMIYVTHDQ 194
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
726-798 |
1.97e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 44.01 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 726 LGRFGLESHAHTIQ--------------ICKLSGGQKARVVFAELACREPDVLILDEPTNNLDI-ESID--ALGEAINEY 788
Cdd:PRK10575 117 LGRFGAADREKVEEaislvglkplahrlVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIaHQVDvlALVHRLSQE 196
|
90
....*....|.
gi 69354671 789 KG-AVIVVSHD 798
Cdd:PRK10575 197 RGlTVIAVLHD 207
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
321-506 |
1.97e-04 |
|
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: 42.80 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIAnralsippnidvllceqevvadetpavqAVLRADTKRLKLLEEERRLqgq 400
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKILS----------------------------GLYKPDSGEILVDGKEVSF--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 401 leqGDDTAAERlekvyeelratgaaaaeakarrilAGLGFDPEMqnrptqkfSGGWRMRVSLARALFMEPTLLMLDEPTN 480
Cdd:cd03216 67 ---ASPRDARR------------------------AGIAMVYQL--------SVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190
....*....|....*....|....*....|.
gi 69354671 481 HLDLNAVIWLNNYL-----QGwrKTLLIVSH 506
Cdd:cd03216 112 ALTPAEVERLFKVIrrlraQG--VAVIFISH 140
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
304-507 |
2.00e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 44.21 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSIS-AHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLlceqevvadetpavqaVLR 382
Cdd:PRK13644 2 IRLENVSYSyPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLN--GLLRPQKGKVL----------------VSG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 383 ADTKRLKLLEEERRLQGQLEQGDDT------AAERLEKVYEELRATGAAAAEAKARRiLAGLGFDpEMQNRPTQKFSGGW 456
Cdd:PRK13644 64 IDTGDFSKLQGIRKLVGIVFQNPETqfvgrtVEEDLAFGPENLCLPPIEIRKRVDRA-LAEIGLE-KYRHRSPKTLSGGQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 69354671 457 RMRVSLARALFMEPTLLMLDEPTNHLDLN---AVIWLNNYLQGWRKTLLIVSHD 507
Cdd:PRK13644 142 GQCVALAGILTMEPECLIFDEVTSMLDPDsgiAVLERIKKLHEKGKTIVYITHN 195
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
656-798 |
2.04e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 44.33 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 656 IVGPNGVGKSTLlllltgkltpthgeMR---------------------KNHRLKIGFF--------NQQYAEQLRmeet 706
Cdd:COG4152 32 LLGPNGAGKTTT--------------IRiilgilapdsgevlwdgepldPEDRRRIGYLpeerglypKMKVGEQLV---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 707 pteYLQRGFNLPYQDARK----CLGRFGLESHA-HTIQicKLSGGQKARVVF-AELACrEPDVLILDEPTNNLDIESIDA 780
Cdd:COG4152 94 ---YLARLKGLSKAEAKRradeWLERLGLGDRAnKKVE--ELSKGNQQKVQLiAALLH-DPELLILDEPFSGLDPVNVEL 167
|
170 180
....*....|....*....|.
gi 69354671 781 LGEAINEYK--GA-VIVVSHD 798
Cdd:COG4152 168 LKDVIRELAakGTtVIFSSHQ 188
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
435-514 |
2.14e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 44.27 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 435 LAGLGFDpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------LNAVIWLNnylQGWRKTLLIVSHD 507
Cdd:PRK13637 129 IVGLDYE-DYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgrdeiLNKIKELH---KEYNMTIILVSHS 204
|
....*..
gi 69354671 508 qgfLDDV 514
Cdd:PRK13637 205 ---MEDV 208
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
453-526 |
2.22e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.48 E-value: 2.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 453 SGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTL----LIVSHDqgfLDdvctDIIHLdAQRL 526
Cdd:PRK11144 130 SGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREInipiLYVSHS---LD----EILRL-ADRV 199
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
730-798 |
2.22e-04 |
|
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: 43.61 E-value: 2.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 69354671 730 GLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAI----NEYKGAVIVVSHD 798
Cdd:TIGR01184 103 GLTEAADK-RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELmqiwEEHRVTVLMVTHD 174
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
321-483 |
2.24e-04 |
|
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: 44.71 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIanralsipPNIdVLLCEQEVVADETPAVQAVLRADTKRLKLLEEERRLqgq 400
Cdd:TIGR02203 350 SISLVIEPGETVALVGRSGSGKSTLVNLI--------PRF-YEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVL--- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 401 leqGDDTAAE-----RLEKVYEELRATGAAAAEAKARRILAGLGFDPEM-QNrpTQKFSGGWRMRVSLARALFMEPTLLM 474
Cdd:TIGR02203 418 ---FNDTIANniaygRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIgEN--GVLLSGGQRQRLAIARALLKDAPILI 492
|
....*....
gi 69354671 475 LDEPTNHLD 483
Cdd:TIGR02203 493 LDEATSALD 501
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
744-833 |
2.29e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 44.70 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 744 SGGQKARVVFAELACREPDVLILDEPTNNLD---IESIDALGEAINE-YKGAVIVVSHDARLITETNCQLWVVEEQSVSQ 819
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDktvQAQILALLKSLQQkHQLAYLFISHDLHVVRALCHQVIVLRQGEVVE 506
|
90 100
....*....|....*....|..
gi 69354671 820 iDGDFE--------DYKREVLE 833
Cdd:PRK15134 507 -QGDCErvfaapqqEYTRQLLA 527
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
435-508 |
2.37e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.62 E-value: 2.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 435 LAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-LNAVI---WLNNYLQGWRKTLLIVSHDQ 508
Cdd:PRK10938 385 LDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDpLNRQLvrrFVDVLISEGETQLLFVSHHA 462
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
453-490 |
2.42e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.87 E-value: 2.42e-04
10 20 30
....*....|....*....|....*....|....*...
gi 69354671 453 SGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWL 490
Cdd:PLN03211 208 SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
323-487 |
2.49e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.62 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 323 DLYIVAGRRYGLVGPNGKGKTTLlkhiaNRALSIppniDVLLCEQEVVADetpaVQAVLRADTKRL-KLLEEE--RRLQG 399
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSAL-----ARALAG----ELPLLSGERQSQ----FSHITRLSFEQLqKLVSDEwqRNNTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 400 QLEQG-DDTAAERLEKVYEELRATGAAAAEAKARRILAGLgfdpemqNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEP 478
Cdd:PRK10938 90 MLSPGeDDTGRTTAEIIQDEVKDPARCEQLAQQFGITALL-------DRRFKYLSTGETRKTLLCQALMSEPDLLILDEP 162
|
....*....
gi 69354671 479 TNHLDLNAV 487
Cdd:PRK10938 163 FDGLDVASR 171
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
744-802 |
2.62e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.63 E-value: 2.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 69354671 744 SGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEY---KGAVIVVSHDARLI 802
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLrdgKRSFIIVTHYQRIL 208
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
435-483 |
2.72e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 43.58 E-value: 2.72e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 69354671 435 LAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 483
Cdd:PRK13649 129 LALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
730-774 |
2.72e-04 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 43.38 E-value: 2.72e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 69354671 730 GLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPTNNLD 774
Cdd:cd03300 119 QLEGYANR-KPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
334-507 |
2.94e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.08 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 334 LVGPNGKGKTTLLKHIA----NRALSIPPNIDVLLceqeVVADETPAVQAVLRADTKRLKLleeeRRLQGQ-LEQGDDTA 408
Cdd:COG0419 28 IVGPNGAGKSTILEAIRyalyGKARSRSKLRSDLI----NVGSEEASVELEFEHGGKRYRI----ERRQGEfAEFLEAKP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 409 AERLE--------KVYEELRATGAAAAEAKARRI--------LAGLGFDPEMQNRPTQKFSGGWRMRVSLARALfmeptL 472
Cdd:COG0419 100 SERKEalkrllglEIYEELKERLKELEEALESALeelaelqkLKQEILAQLSGLDPIETLSGGERLRLALADLL-----S 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 69354671 473 LMLDepTNHLD---LNAVIwlnNYLqgwrKTLLIVSHD 507
Cdd:COG0419 175 LILD--FGSLDeerLERLL---DAL----EELAIITHV 203
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
453-506 |
2.98e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 44.43 E-value: 2.98e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 69354671 453 SGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------LNAviwLNNYLQGwrKTLLIVSH 506
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDaeterqiLEL---LAEHAQN--KTVLMITH 532
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
743-802 |
3.03e-04 |
|
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: 42.87 E-value: 3.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLD----IESIDALGEAINEYKGAVIVVSH---DARLI 802
Cdd:cd03298 129 LSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHqpeDAKRL 195
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
743-798 |
3.04e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 43.64 E-value: 3.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLDIES----IDALGEAINEYKGAVIVVSHD 798
Cdd:PRK13640 144 LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGkeqiLKLIRKLKKKNNLTVISITHD 203
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
329-513 |
3.28e-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: 41.98 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 329 GRRYGLVGPNGKGKTTLLKHIANraLSIPPNIDVLlceqeVVADETpavqavLRADTKRLKLLEEERRLQGQLEQGDdta 408
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAR--ELGPPGGGVI-----YIDGED------ILEEVLDQLLLIIVGGKKASGSGEL--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 409 aerlekvyeelratgaaaaeakarrilaglgfdpemqnrptqkfsggwRMRVSLARALFMEPTLLMLDEPTNHLD----- 483
Cdd:smart00382 66 ------------------------------------------------RLRLALALARKLKPDVLILDEITSLLDaeqea 97
|
170 180 190
....*....|....*....|....*....|....
gi 69354671 484 ----LNAVIWLNNYLQGWRKTLLIVSHDQGFLDD 513
Cdd:smart00382 98 llllLEELRLLLLLKSEKNLTVILTTNDEKDLGP 131
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
743-826 |
3.32e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 44.07 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKGA--VIVVSHdaRLITETNC-QLWVVEE-QSVS 818
Cdd:PRK11174 486 LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRqtTLMVTH--QLEDLAQWdQIWVMQDgQIVQ 563
|
....*...
gi 69354671 819 QidGDFED 826
Cdd:PRK11174 564 Q--GDYAE 569
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
739-798 |
3.35e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.22 E-value: 3.35e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 69354671 739 QICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKG---AVIVVSHD 798
Cdd:PRK10762 392 AIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeglSIILVSSE 454
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
726-798 |
3.55e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 43.18 E-value: 3.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 69354671 726 LGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKG--AVIVVSHD 798
Cdd:COG4674 136 LETIGLTDKADR-LAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGkhSVVVVEHD 209
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
743-799 |
3.57e-04 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 42.85 E-value: 3.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 743 LSGGQKARV--VFAELAcrEPDVLILDEPTNNLD-----------IESIDALGeaineykGAVIVVSHDA 799
Cdd:COG4136 134 LSGGQRARValLRALLA--EPRALLLDEPFSKLDaalraqfrefvFEQIRQRG-------IPALLVTHDE 194
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
451-506 |
3.57e-04 |
|
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: 42.99 E-value: 3.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 69354671 451 KFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------LNAviwLNNYLQGwrKTLLIVSH 506
Cdd:cd03253 137 KLSGGEKQRVAIARAILKNPPILLLDEATSALDthtereiQAA---LRDVSKG--RTTIVIAH 194
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
313-483 |
3.98e-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: 42.63 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 313 AHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRalsIPPNIDVllcEQEVVADETPAvqavlradtkrlklLE 392
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSV---EGDIHYNGIPY--------------KE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 393 EERRLQGQL---EQGDD-----TAAERLEkvyeelratgaaaaeakarrilaglgFDPEMQ-NRPTQKFSGGWRMRVSLA 463
Cdd:cd03233 77 FAEKYPGEIiyvSEEDVhfptlTVRETLD--------------------------FALRCKgNEFVRGISGGERKRVSIA 130
|
170 180
....*....|....*....|
gi 69354671 464 RALFMEPTLLMLDEPTNHLD 483
Cdd:cd03233 131 EALVSRASVLCWDNSTRGLD 150
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
742-820 |
4.11e-04 |
|
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: 42.54 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 742 KLSGGQKARVVFAELACREPDVLILDEPTNNLD----IESIDALGEAINEYKGAVIVVSH---DARLITEtncQLWVVEE 814
Cdd:TIGR01277 128 QLSGGQRQRVALARCLVRPNPILLLDEPFSALDpllrEEMLALVKQLCSERQRTLLMVTHhlsDARAIAS---QIAVVSQ 204
|
....*.
gi 69354671 815 QSVSQI 820
Cdd:TIGR01277 205 GKIKVV 210
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
743-797 |
4.17e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 43.15 E-value: 4.17e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLD----IESIDALGEAINEYKGAVIVVSH 797
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH 203
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
743-798 |
4.26e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 43.00 E-value: 4.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 69354671 743 LSGGQKARVVFAElACRE--PDV------LILDEPTNNLDIESIDALGEAINEY---KGAVIVVSHD 798
Cdd:PRK03695 127 LSGGEWQRVRLAA-VVLQvwPDInpagqlLLLDEPMNSLDVAQQAALDRLLSELcqqGIAVVMSSHD 192
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
320-506 |
4.67e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 42.84 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 320 VNADLY---IVAgrrygLVGPNGKGKTTLLKHIaNRALSIPPNI----DVLLCEQEVVADETPAVQavLRadtKRLKLLE 392
Cdd:PRK14239 24 VSLDFYpneITA-----LIGPSGSGKSTLLRSI-NRMNDLNPEVtitgSIVYNGHNIYSPRTDTVD--LR---KEIGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 393 EER---------------RLQGQLEQgddtaaERLEKVYEElratgaaaaeakarrILAGLGFDPEMQNR---PTQKFSG 454
Cdd:PRK14239 93 QQPnpfpmsiyenvvyglRLKGIKDK------QVLDEAVEK---------------SLKGASIWDEVKDRlhdSALGLSG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 69354671 455 GWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK--TLLIVSH 506
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTR 205
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
730-798 |
4.81e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 43.14 E-value: 4.81e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 69354671 730 GLESHAHTI--QickLSGGQKARVVFAE-LACRePDVLILDEPTNNLDIE---SIDALGEAIN-EYKGAVIVVSHD 798
Cdd:COG1135 129 GLSDKADAYpsQ---LSGGQKQRVGIARaLANN-PKVLLCDEATSALDPEttrSILDLLKDINrELGLTIVLITHE 200
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
610-802 |
4.86e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 43.66 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 610 VRFTFPDPPPLSPPVLGLHGVTFGYQGQK-PLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRl 688
Cdd:PRK11160 324 VTFPTTSTAAADQVSLTLNNVSFTYPDQPqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQ- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 689 KIGFFNQQyaeQLRmeETPTEYLQRGF--------NL-----PYQDARKC--LGRFGLESHAHTIQICK---------LS 744
Cdd:PRK11160 403 PIADYSEA---ALR--QAISVVSQRVHlfsatlrdNLllaapNASDEALIevLQQVGLEKLLEDDKGLNawlgeggrqLS 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 69354671 745 GGQKARVVFAELACREPDVLILDEPTNNLDIES---IDALGEAINEYKgAVIVVSHdaRLI 802
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerqILELLAEHAQNK-TVLMITH--RLT 535
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
624-798 |
4.94e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 42.77 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 624 VLGLHGVTFGYQGQKPL--FKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHG-----------EMRKNHRLKI 690
Cdd:PRK13642 4 ILEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGkvkidgelltaENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 691 GFFNQQYAEQL--RMEETPTEYLQRGFNLPYQDARKCLGRFGLESHA---HTIQICKLSGGQKARVVFAELACREPDVLI 765
Cdd:PRK13642 84 GMVFQNPDNQFvgATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMldfKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 69354671 766 LDEPTNNLD----IESIDALGEAINEYKGAVIVVSHD 798
Cdd:PRK13642 164 LDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
636-798 |
5.07e-04 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 42.80 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 636 GQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRLKIGFFNQQYAEQL-------------- 701
Cdd:COG4559 12 GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRavlpqhsslafpft 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 702 -----RMEETPteyLQRGFNLPYQDARKCLGRFGLESHAHTiQICKLSGGQKARVVFA-------ELACREPDVLILDEP 769
Cdd:COG4559 92 veevvALGRAP---HGSSAAQDRQIVREALALVGLAHLAGR-SYQTLSGGEQQRVQLArvlaqlwEPVDGGPRWLFLDEP 167
|
170 180 190
....*....|....*....|....*....|..
gi 69354671 770 TNNLDIESIDALGEAINEY---KGAVIVVSHD 798
Cdd:COG4559 168 TSALDLAHQHAVLRLARQLarrGGGVVAVLHD 199
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
742-796 |
5.11e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.62 E-value: 5.11e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 69354671 742 KLSGGQKARVVFAELACREPDVLILDEPTNNLD------IESIdalgeaINEY--KG-AVIVVS 796
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgakyeIYTI------INELaaEGkGVIVIS 461
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
636-797 |
5.18e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.10 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 636 GQKPLFKNLDFGI---DMdsrICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRlKIGFFNQQYAEQL---------RM 703
Cdd:PRK13538 12 DERILFSGLSFTLnagEL---VQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGE-PIRRQRDEYHQDLlylghqpgiKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 704 EETPTEYLQrgFNLP---YQDARKC---LGRFGL----ESHAHTiqickLSGGQKARVVFAELACREPDVLILDEPTNNL 773
Cdd:PRK13538 88 ELTALENLR--FYQRlhgPGDDEALweaLAQVGLagfeDVPVRQ-----LSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180
....*....|....*....|....*..
gi 69354671 774 DIESIDALGEAINEY---KGAVIVVSH 797
Cdd:PRK13538 161 DKQGVARLEALLAQHaeqGGMVILTTH 187
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
743-774 |
5.30e-04 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 42.15 E-value: 5.30e-04
10 20 30
....*....|....*....|....*....|...
gi 69354671 743 LSGGQKARVVFA-ELACRePDVLILDEPTNNLD 774
Cdd:cd03213 112 LSGGERKRVSIAlELVSN-PSLLFLDEPTSGLD 143
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
452-511 |
5.64e-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: 42.32 E-value: 5.64e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 69354671 452 FSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNN-----YLQGWRKTLLIVSHDQGFL 511
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegilkFLQDDKRTLVLVTHKLQYL 205
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
630-775 |
5.73e-04 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 43.29 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 630 VTFGYQgqkPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKN----HRLKIGFFNQQYA------- 698
Cdd:PRK09536 11 VEFGDT---TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvEALSARAASRRVAsvpqdts 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 699 -------EQ-LRMEETPteylQRGFNLPYQDA-----RKCLGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLI 765
Cdd:PRK09536 88 lsfefdvRQvVEMGRTP----HRSRFDTWTETdraavERAMERTGVAQFADR-PVTSLSGGERQRVLLARALAQATPVLL 162
|
170
....*....|
gi 69354671 766 LDEPTNNLDI 775
Cdd:PRK09536 163 LDEPTASLDI 172
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
742-829 |
6.19e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 42.78 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 742 KLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEY--KGAVIVVSH----------------DARLIT 803
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLadRLTVIIVTHnlaqaarisdraalffDGRLVE 242
|
90 100 110
....*....|....*....|....*....|..
gi 69354671 804 ETNC-QLWVVEEQS-----VSQIDGDFEDYKR 829
Cdd:PRK14271 243 EGPTeQLFSSPKHAetaryVAGLSGDVKDAKR 274
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
726-814 |
6.58e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 42.28 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 726 LGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAI----NEYKGAVIVVSHDARL 801
Cdd:PRK11300 138 LERVGLLEHANR-QAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIaelrNEHNVTVLLIEHDMKL 216
|
90
....*....|...
gi 69354671 802 ITETNCQLWVVEE 814
Cdd:PRK11300 217 VMGISDRIYVVNQ 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
719-842 |
6.72e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.07 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 719 YQDARKCLGRFGLESHAHTIqICKLSGGQKARVVFAELACREPDVLILDEPTNNL-DIESiDALGEAINEYK--GAVIV- 794
Cdd:PRK10762 119 YAEADKLLARLNLRFSSDKL-VGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTET-ESLFRVIRELKsqGRGIVy 196
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 69354671 795 VSHDARLITETNCQLWV------VEEQSVSQIDGDfedykrevleALGEVMVSR 842
Cdd:PRK10762 197 ISHRLKEIFEICDDVTVfrdgqfIAEREVADLTED----------SLIEMMVGR 240
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
434-507 |
6.97e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.31 E-value: 6.97e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 434 ILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTL----LIVSHD 507
Cdd:PRK10261 446 LLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFgiayLFISHD 523
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
443-483 |
7.09e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.14 E-value: 7.09e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 69354671 443 EMQNR----PTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 483
Cdd:PRK14267 138 EVKDRlndyPSN-LSGGQRQRLVIARALAMKPKILLMDEPTANID 181
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
742-815 |
7.43e-04 |
|
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: 43.17 E-value: 7.43e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 69354671 742 KLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINE-YKG-AVIVVSHdaRLITETNCQLWVVEEQ 815
Cdd:TIGR02203 469 LLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERlMQGrTTLVIAH--RLSTIEKADRIVVMDD 542
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
443-515 |
7.62e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 42.18 E-value: 7.62e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 69354671 443 EMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNA---VIWLNNYLQGWRKTLLIVSHDQGFLDDVC 515
Cdd:PRK15056 134 EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTearIISLLRELRDEGKTMLVSTHNLGSVTEFC 209
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
742-820 |
7.65e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.92 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 742 KLSGGQKARVVFA-ELACRePDVLILDEPTNNLDIESIDALGEAIN----EYKGAVIVVSHDARLITETNCQLWV----- 811
Cdd:PRK10261 168 QLSGGMRQRVMIAmALSCR-PAVLIADEPTTALDVTIQAQILQLIKvlqkEMSMGVIFITHDMGVVAEIADRVLVmyqge 246
|
90
....*....|
gi 69354671 812 -VEEQSVSQI 820
Cdd:PRK10261 247 aVETGSVEQI 256
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
720-830 |
8.02e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.85 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 720 QDARKCLGrfgLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIES---IDALGEAINEYKGAVIVVS 796
Cdd:PRK09700 390 ENQRELLA---LKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAkaeIYKVMRQLADDGKVILMVS 466
|
90 100 110
....*....|....*....|....*....|....
gi 69354671 797 HDARLITETNCQLWVVEEQSVSQIDGDFEDYKRE 830
Cdd:PRK09700 467 SELPEIITVCDRIAVFCEGRLTQILTNRDDMSEE 500
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
720-774 |
8.21e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 41.99 E-value: 8.21e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 69354671 720 QDARKCLGRFGLEShAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLD 774
Cdd:PRK11248 107 EIAHQMLKKVGLEG-AEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
744-802 |
8.62e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 41.94 E-value: 8.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 69354671 744 SGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKG---AVIVVSHDARLI 802
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTsenSIILITHYQRLL 214
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
443-514 |
8.75e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 42.03 E-value: 8.75e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 69354671 443 EMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK----TLLIVSHDqgfLDDV 514
Cdd:PRK13650 132 DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyqmTVISITHD---LDEV 204
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
443-507 |
9.50e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 41.90 E-value: 9.50e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 69354671 443 EMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK----TLLIVSHD 507
Cdd:PRK11300 145 EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehnvTVLLIEHD 213
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
450-522 |
9.54e-04 |
|
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: 40.60 E-value: 9.54e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 69354671 450 QKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGfLDDVCTDIIHLD 522
Cdd:cd03223 90 DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGHRPS-LWKFHDRVLDLD 161
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
743-774 |
9.75e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 41.68 E-value: 9.75e-04
10 20 30
....*....|....*....|....*....|..
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLD 774
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
453-483 |
1.05e-03 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 41.99 E-value: 1.05e-03
10 20 30
....*....|....*....|....*....|.
gi 69354671 453 SGGWRMRVSLARALFMEPTLLMLDEPTNHLD 483
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
628-787 |
1.06e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 42.64 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 628 HGVTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEM-----------RKNHRLKIG----- 691
Cdd:PRK13657 338 DDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIlidgtdirtvtRASLRRNIAvvfqd 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 692 --FFNQQYAEQLRM------EETPTEYLQRGFNLPYQDARKclgrFGLESHAHTiQICKLSGGQKARVVFAELACREPDV 763
Cdd:PRK13657 418 agLFNRSIEDNIRVgrpdatDEEMRAAAERAQAHDFIERKP----DGYDTVVGE-RGRQLSGGERQRLAIARALLKDPPI 492
|
170 180
....*....|....*....|....
gi 69354671 764 LILDEPTNNLDIESIDALGEAINE 787
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDE 516
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
743-802 |
1.10e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 40.77 E-value: 1.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 69354671 743 LSGGQKARVVFA-ELACR-EPDVLILDEPTNNLDIESIDALGEAINEY---KGAVIVVSHDARLI 802
Cdd:cd03238 88 LSGGELQRVKLAsELFSEpPGTLFILDEPSTGLHQQDINQLLEVIKGLidlGNTVILIEHNLDVL 152
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
451-483 |
1.13e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 1.13e-03
10 20 30
....*....|....*....|....*....|...
gi 69354671 451 KFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 483
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
743-798 |
1.15e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 41.69 E-value: 1.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKG--AVIVVSHD 798
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEqyTIIIVTHN 209
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
654-806 |
1.19e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.05 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 654 ICIVGPNGVGKStllllltgkltpthgemrknHRLKigffnqQYAEQLRMEETPTEYLQRGFNLPYQDARKCLGRFGLES 733
Cdd:smart00382 5 ILIVGPPGSGKT--------------------TLAR------ALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKK 58
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 69354671 734 HAhtiqickLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKGAVIVVSHDARLITETN 806
Cdd:smart00382 59 AS-------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTN 124
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
744-810 |
1.23e-03 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 41.22 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 744 SGGQKARVVFAELACREPDVLILDEptnnldiesidALG-----------EAINEYK---GAVIVVSHDARLItETNCQ- 808
Cdd:COG1134 148 SSGMRARLAFAVATAVDPDILLVDE-----------VLAvgdaafqkkclARIRELResgRTVIFVSHSMGAV-RRLCDr 215
|
...
gi 69354671 809 -LW 810
Cdd:COG1134 216 aIW 218
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
321-479 |
1.28e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.42 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIAN-RALsippnidvllceQ----EV----VADetpavqAVLRADT------ 385
Cdd:NF033858 19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGaRKI------------QqgrvEVlggdMAD------ARHRRAVcpriay 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 386 ------KRL--KLLEEER-----RLQGQleqgddTAAERLEKVyEELratgaaaaeakarriLAGLGFDPeMQNRPTQKF 452
Cdd:NF033858 81 mpqglgKNLypTLSVFENldffgRLFGQ------DAAERRRRI-DEL---------------LRATGLAP-FADRPAGKL 137
|
170 180
....*....|....*....|....*..
gi 69354671 453 SGGWRMRVSLARALFMEPTLLMLDEPT 479
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
632-797 |
1.35e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 40.70 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 632 FGYQGQkPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEmrknhrlkIGFFNQQYAEQLRMEETPTEYL 711
Cdd:PRK13540 9 FDYHDQ-PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGE--------ILFERQSIKKDLCTYQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 712 --QRGFNlPYQDARK-CLGRFGLESHAHTI-QICK--------------LSGGQKARVVFAELACREPDVLILDEPTNNL 773
Cdd:PRK13540 80 ghRSGIN-PYLTLREnCLYDIHFSPGAVGItELCRlfslehlidypcglLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170 180
....*....|....*....|....*..
gi 69354671 774 DIESIDALGEAINEYK---GAVIVVSH 797
Cdd:PRK13540 159 DELSLLTIITKIQEHRakgGAVLLTSH 185
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
452-484 |
1.35e-03 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 42.59 E-value: 1.35e-03
10 20 30
....*....|....*....|....*....|...
gi 69354671 452 FSGGWRMRVSLARALFMEPTLLMLDEPTNHLDL 484
Cdd:TIGR01271 549 LSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
743-774 |
1.45e-03 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 41.60 E-value: 1.45e-03
10 20 30
....*....|....*....|....*....|....*...
gi 69354671 743 LSGGQKARV------VfaelacREPDVLILDEPTNNLD 774
Cdd:COG3839 134 LSGGQRQRValgralV------REPKVFLLDEPLSNLD 165
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
443-483 |
1.46e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.64 E-value: 1.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 69354671 443 EMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 483
Cdd:NF000106 136 EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
321-482 |
1.50e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 42.12 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKHIAnralSIPPNIDVllcEQEVVADETPAVQAVLRaDTKR--LKLLEEERRLQ 398
Cdd:TIGR02633 19 GIDLEVRPGECVGLCGENGAGKSTLMKILS----GVYPHGTW---DGEIYWSGSPLKASNIR-DTERagIVIIHQELTLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 399 GQLeqgddTAAERL---EKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLML 475
Cdd:TIGR02633 91 PEL-----SVAENIflgNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLIL 165
|
....*..
gi 69354671 476 DEPTNHL 482
Cdd:TIGR02633 166 DEPSSSL 172
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
743-815 |
1.58e-03 |
|
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: 40.93 E-value: 1.58e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEY-KG-AVIVVSHdaRLITETNCQLWVVEEQ 815
Cdd:cd03252 139 LSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIcAGrTVIIIAH--RLSTVKNADRIIVMEK 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
719-798 |
1.60e-03 |
|
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: 41.09 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 719 YQDARKCLGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPTNNLD----IESIDALGEAINEYKGAVIV 794
Cdd:cd03294 138 EERAAEALELVGLEGWEHK-YPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQDELLRLQAELQKTIVF 216
|
....
gi 69354671 795 VSHD 798
Cdd:cd03294 217 ITHD 220
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
744-798 |
1.64e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 41.49 E-value: 1.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 69354671 744 SGGQKARVVFAELACREPDVLILDEPTNNLDIeSIDAlgEAIN-------EYKGAVIVVSHD 798
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDV-SVQA--QVLNlmmdlqqELGLSYVFISHD 214
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
625-797 |
1.71e-03 |
|
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: 40.53 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 625 LGLHGVTFGY----QGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTgkltpthGEMRKNHrlkiGFFNQQ---- 696
Cdd:cd03250 1 ISVEDASFTWdsgeQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALL-------GELEKLS----GSVSVPgsia 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 697 YAEQlrmeeTPteYLQRG-------FNLPYQDARK-------CLGRfGLESHAHTIQIC------KLSGGQKARVVFAEL 756
Cdd:cd03250 70 YVSQ-----EP--WIQNGtirenilFGKPFDEERYekvikacALEP-DLEILPDGDLTEigekgiNLSGGQKQRISLARA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 69354671 757 ACREPDVLILDEPTNNLDIE---SI--DALGEAINEYKgAVIVVSH 797
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHvgrHIfeNCILGLLLNNK-TRILVTH 186
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
321-507 |
1.74e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 41.56 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 321 NADLYIVAGRRYGLVGPNGKGKTTLLKhIANRALSiPPNIDVLLCEQEVVADETPAVQAVLRadtKRLKLLEEERRLQGQ 400
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVR-LLNRLIE-PTRGQVLIDGVDIAKISDAELREVRR---KKIAMVFQSFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 401 LEQGDDTA----------AERLEKVYEELRAtgaaaaeakarrilagLGFDPEMQNRPTQkFSGGWRMRVSLARALFMEP 470
Cdd:PRK10070 121 MTVLDNTAfgmelaginaEERREKALDALRQ----------------VGLENYAHSYPDE-LSGGMRQRVGLARALAINP 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 69354671 471 TLLMLDEPTNHLDLNAVIWLNNYL----QGWRKTLLIVSHD 507
Cdd:PRK10070 184 DILLMDEAFSALDPLIRTEMQDELvklqAKHQRTIVFISHD 224
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
451-507 |
1.84e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 41.23 E-value: 1.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 69354671 451 KFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGW--RKTLLIVSHD 507
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLadRLTVIIVTHN 221
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
453-506 |
1.95e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 41.87 E-value: 1.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 69354671 453 SGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK--TLLIVSH 506
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKgrTTFIIAH 528
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
742-798 |
2.42e-03 |
|
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: 41.25 E-value: 2.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 69354671 742 KLSGGQKARVVFAELACREPDVLILDEPTNNLDI----ESIDALGEAINEYKGAVIVVSHD 798
Cdd:TIGR02142 131 RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHS 191
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
740-796 |
2.49e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.45 E-value: 2.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 740 ICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEY--KG-AVIVVS 796
Cdd:PRK13549 403 IARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLvqQGvAIIVIS 462
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
437-512 |
2.65e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 39.61 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 437 GLGFDPemQNRPTQKFSGGWRMRVSLARALFMEP--TLLMLDEPTNHLDLNAVIWLNNYLQGWRK---TLLIVSHDQGFL 511
Cdd:cd03238 75 GLGYLT--LGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLIDlgnTVILIEHNLDVL 152
|
.
gi 69354671 512 D 512
Cdd:cd03238 153 S 153
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
742-774 |
2.78e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 40.98 E-value: 2.78e-03
10 20 30
....*....|....*....|....*....|...
gi 69354671 742 KLSGGQKARVVFAELACREPDVLILDEPTNNLD 774
Cdd:PRK11650 134 ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
332-483 |
2.80e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 40.60 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 332 YGLVGPNGKGKTTLLKHIANRalsIPPNIDVLLCEQEVVADETPAVQAVLRADTKRLKLLEEERRLQGQLEQG------D 405
Cdd:PRK13631 55 YFIIGNSGSGKSTLVTHFNGL---IKSKYGTIQVGDIYIGDKKNNHELITNPYSKKIKNFKELRRRVSMVFQFpeyqlfK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 406 DTA-----------------AERLEKVYeelratgaaaaeakarriLAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFM 468
Cdd:PRK13631 132 DTIekdimfgpvalgvkkseAKKLAKFY------------------LNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAI 193
|
170
....*....|....*
gi 69354671 469 EPTLLMLDEPTNHLD 483
Cdd:PRK13631 194 QPEILIFDEPTAGLD 208
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
710-796 |
2.90e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.25 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 710 YLQRGFNLPYQDARKCLGRFGLESHA-------------------HTIQICKLSGGQKARVVFAELACREPDVLILDEPT 770
Cdd:PRK10982 340 YLDIGFNSLISNIRNYKNKVGLLDNSrmksdtqwvidsmrvktpgHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
90 100 110
....*....|....*....|....*....|
gi 69354671 771 NNLDI----ESIDALGEAINEYKGAVIVVS 796
Cdd:PRK10982 420 RGIDVgakfEIYQLIAELAKKDKGIIIISS 449
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
743-803 |
3.01e-03 |
|
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: 40.17 E-value: 3.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 69354671 743 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAI-NEYKGA-VIVVSHdaRLIT 803
Cdd:cd03244 140 LSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIrEAFKDCtVLTIAH--RLDT 200
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
624-804 |
3.22e-03 |
|
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: 40.02 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 624 VLGLHGVT--FGyqGQKPLfKNLDFGIDMDSRICIVGPNGVGKSTllllltgkltpthgemrknhrlkigFFNQ---QYA 698
Cdd:COG0411 4 LLEVRGLTkrFG--GLVAV-DDVSLEVERGEIVGLIGPNGAGKTT-------------------------LFNLitgFYR 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 699 ------------------------------------------EQLRM---EETPTEYLQRGFNLP---------YQDARK 724
Cdd:COG0411 56 ptsgrilfdgrditglpphriarlgiartfqnprlfpeltvlENVLVaahARLGRGLLAALLRLPrarreereaRERAEE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 725 CLGRFGLESHAHTiQICKLSGGQKARVvfaELA---CREPDVLILDEPTNNLDIESIDALGE---AINEYKG-AVIVVSH 797
Cdd:COG0411 136 LLERVGLADRADE-PAGNLSYGQQRRL---EIAralATEPKLLLLDEPAAGLNPEETEELAElirRLRDERGiTILLIEH 211
|
....*..
gi 69354671 798 DARLITE 804
Cdd:COG0411 212 DMDLVMG 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
723-796 |
3.60e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 40.96 E-value: 3.60e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 69354671 723 RKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIES---IDALGEAINEYKGAVIVVS 796
Cdd:TIGR02633 384 GSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVS 460
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
453-484 |
3.66e-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: 40.23 E-value: 3.66e-03
10 20 30
....*....|....*....|....*....|..
gi 69354671 453 SGGWRMRVSLARALFMEPTLLMLDEPTNHLDL 484
Cdd:cd03291 161 SGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
742-774 |
3.84e-03 |
|
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: 40.02 E-value: 3.84e-03
10 20 30
....*....|....*....|....*....|...
gi 69354671 742 KLSGGQKARVVFAELACREPDVLILDEPTNNLD 774
Cdd:cd03296 136 QLSGGQRQRVALARALAVEPKVLLLDEPFGALD 168
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
443-514 |
3.92e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.61 E-value: 3.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 69354671 443 EMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLN---AVIWLNNYLQGWRKTLLI-VSHDQGFLDDV 514
Cdd:PRK10261 160 TILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTiqaQILQLIKVLQKEMSMGVIfITHDMGVVAEI 235
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
448-483 |
4.29e-03 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 40.44 E-value: 4.29e-03
10 20 30
....*....|....*....|....*....|....*.
gi 69354671 448 PTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 483
Cdd:COG4172 154 PHQ-LSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
742-798 |
4.31e-03 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 40.20 E-value: 4.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 69354671 742 KLSGGQKARVVFAELACREPDVLILDEPTNNLD--------IESIDALgeainEYKGAVIV-VSHD 798
Cdd:PRK11607 149 QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrmqLEVVDIL-----ERVGVTCVmVTHD 209
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
727-798 |
4.49e-03 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 39.82 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 727 GRFGLESHAHTiQICKLSGGQKARV----VFAELacrEPDV------LILDEPTNNLDIESIDALGEAINEYK---GAVI 793
Cdd:COG4138 112 EALGLEDKLSR-PLTQLSGGEWQRVrlaaVLLQV---WPTInpegqlLLLDEPMNSLDVAQQAALDRLLRELCqqgITVV 187
|
....*
gi 69354671 794 VVSHD 798
Cdd:COG4138 188 MSSHD 192
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
304-514 |
4.80e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 39.68 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 304 IKLEKFSISAHGkELFVNADLYIVAGRRYGLVGPNGKGKTtlLKHIAnrALSI-PPNIDVLlcEQEVVADETPAVQAVLR 382
Cdd:PRK10418 5 IELRNIALQAAQ-PLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAA--ALGIlPAGVRQT--AGRVLLDGKPVAPCALR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 383 ADTKRLkLLEEERRLQGQLEQGDDTAAERLEKVyeelratGAAAAEAKARRILAGLGF-DPE--MQNRPTQkFSGGWRMR 459
Cdd:PRK10418 78 GRKIAT-IMQNPRSAFNPLHTMHTHARETCLAL-------GKPADDATLTAALEAVGLeNAArvLKLYPFE-MSGGMLQR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 69354671 460 VSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKT----LLIVSHDQGFL----DDV 514
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKralgMLLVTHDMGVVarlaDDV 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
452-524 |
5.31e-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: 40.70 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 452 FSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------LNAVIWLNNYLQGwrKTLLIVSHDQGFLDDVCTDIIHLDAQ 524
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahvgkhiFEHVIGPEGVLKN--KTRILVTHGISYLPQVDVIIVMSGGK 838
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
446-479 |
5.59e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 40.00 E-value: 5.59e-03
10 20 30
....*....|....*....|....*....|....
gi 69354671 446 NRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPT 479
Cdd:COG1129 389 EQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
742-787 |
6.41e-03 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 39.70 E-value: 6.41e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 69354671 742 KLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINE 787
Cdd:PRK11432 136 QISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRE 181
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
680-798 |
6.66e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 39.63 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 680 GEMRKNHRLKIGFFNQQYAEQLRMeeTPTEYLQRGFNLP-------YQDARKCLGRFGLESHAHTIQIcKLSGGQKARVV 752
Cdd:PRK10070 98 AELREVRRKKIAMVFQSFALMPHM--TVLDNTAFGMELAginaeerREKALDALRQVGLENYAHSYPD-ELSGGMRQRVG 174
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 69354671 753 FAELACREPDVLILDEPTNNLD----IESIDALGEAINEYKGAVIVVSHD 798
Cdd:PRK10070 175 LARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHD 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
453-483 |
7.04e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 39.25 E-value: 7.04e-03
10 20 30
....*....|....*....|....*....|.
gi 69354671 453 SGGWRMRVSLARALFMEPTLLMLDEPTNHLD 483
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
438-483 |
8.32e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 39.44 E-value: 8.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 69354671 438 LGFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 483
Cdd:PRK11650 122 LELEPLLDRKPRE-LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
686-800 |
8.85e-03 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 39.01 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 686 HRLKIGFFNQQYA-------EQ-----LRMEETPTEYLQrgfnlpyQDARKCLGRFGLESHAHTiQICKLSGGQKARVVF 753
Cdd:TIGR01187 40 HLRHINMVFQSYAlfphmtvEEnvafgLKMRKVPRAEIK-------PRVLEALRLVQLEEFADR-KPHQLSGGQQQRVAL 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 69354671 754 AELACREPDVLILDEPTNNLDIESIDALG---EAINEYKG-AVIVVSHDAR 800
Cdd:TIGR01187 112 ARALVFKPKILLLDEPLSALDKKLRDQMQlelKTIQEQLGiTFVFVTHDQE 162
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
438-526 |
9.28e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 39.04 E-value: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 69354671 438 LGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK---TLLIVSHDQGFLDDV 514
Cdd:PRK13641 132 VGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEY 211
|
90
....*....|..
gi 69354671 515 CTDIIHLDAQRL 526
Cdd:PRK13641 212 ADDVLVLEHGKL 223
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
630-665 |
9.71e-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: 39.42 E-value: 9.71e-03
10 20 30
....*....|....*....|....*....|....*.
gi 69354671 630 VTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKS 665
Cdd:COG5265 363 VSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKS 398
|
|
| |
