|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-715 |
0e+00 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 1499.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 1 MTEVATSVVHEVLGPRFLEVDQPIIDYIINVLADEDFDFGDEGEGAFNAIGELLVGAECVSDFSECRLVCSKLSDKFGKH 80
Cdd:PLN03073 3 MTEVASSVVLEVLGRRIRDVDSPIIDYIINVLADEDFDFGPEGEGAFDALGELLVAAECVSDDAECRLVCSKLAEKFGKH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 81 GLVKPKPTVRSLTTPFRMDDGMD-EEVKKKKPEPIDGPVLTERDKMKIERRKRKDERQREAQYQIHLAEMEAVRAGMPVA 159
Cdd:PLN03073 83 GLVKPKPSVRSLAAPVRMSDGMDdSEVAKKKPEPDDGPLLSERDLAKIERRKRKEERQREVQYQAHVAEMEAAKAGMPGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 160 CVTHDGGGGGPNVKDIHLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMALHAIDGIPRNCQILHVEQ 239
Cdd:PLN03073 163 YVNHDGNGGGPAIKDIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIDGIPKNCQILHVEQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 240 EVVGDDTSALQCVLNSDIERTRLLEEEVRLHAQQRDLDFEDAAGNGKGDQIGAINKDAISQRLEEIYKRLELIDAYSAEA 319
Cdd:PLN03073 243 EVVGDDTTALQCVLNTDIERTQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELIDAYTAEA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 320 RAASILAGLSFSPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPKTFIVVSHARE 399
Cdd:PLN03073 323 RAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHARE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 400 FLNTVVTDILHLQGQKLTAYKGDYDTFERTREEQIKNQRKAIEANEKSRAHMQTFIDKFRYNAKRASLVQSRIKALDRLG 479
Cdd:PLN03073 403 FLNTVVTDILHLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRIKALDRLG 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 480 HMDEIVNDPDYKFEFPTPDDRPGAPIISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPT 559
Cdd:PLN03073 483 HVDAVVNDPDYKFEFPTPDDRPGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPS 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 560 SGTVFRSAKVRIAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKIT 639
Cdd:PLN03073 563 SGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKIT 642
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 640 FKKPHIILLDEPSNHLDLDAVEALIQGLVLFQGGILMVSHDEHLISGSVDELWVVSQGKVTPFHGTFLDYKKILQS 715
Cdd:PLN03073 643 FKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKKTLQS 718
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
177-709 |
0e+00 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 561.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 177 LENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMA--LHAIDG---IPRNCQILHVEQEVV-GDDTSALQ 250
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAgeLEPDSGevsIPKGLRIGYLPQEPPlDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 251 CVLNSDIERTRLLEEevrLHAQQRDLDFEDAAGNgkgdqigainkdaisqRLEEIYKRLELIDAYSAEARAASILAGLSF 330
Cdd:COG0488 81 TVLDGDAELRALEAE---LEELEAKLAEPDEDLE----------------RLAELQEEFEALGGWEAEARAEEILSGLGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 331 SPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPKTFIVVSHAREFLNTVVTDILH 410
Cdd:COG0488 142 PEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 411 LQGQKLTAYKGDYDTFERTREEQIKNQRKAIEANEKSRAHMQTFIDKFRYNAKRASLVQSRIKALDRLGHMDEIVNDPDY 490
Cdd:COG0488 222 LDRGKLTLYPGNYSAYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRDKTV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 491 KFEFPTPdDRPGAPIISFSDASFGYPGGPLmFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKVR 570
Cdd:COG0488 302 EIRFPPP-ERLGKKVLELEGLSKSYGDKTL-LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 571 IAVFSQHHvDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDE 650
Cdd:COG0488 380 IGYFDQHQ-EELDPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 743842931 651 PSNHLDLDAVEALIQGLVLFQGGILMVSHDEHLISGSVDELWVVSQGKVTPFHGTFLDY 709
Cdd:COG0488 459 PTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDY 517
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
175-713 |
9.28e-132 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 403.78 E-value: 9.28e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMA--LHAIDG---IPRNCQILHVEQEVVGDDTSAL 249
Cdd:PRK10636 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKneISADGGsytFPGNWQLAWVNQETPALPQPAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 250 QCVLNSDIErTRLLEEEVRLHAQQRDldfedaaGNgkgdqigainkdAISQrleeIYKRLELIDAYSAEARAASILAGLS 329
Cdd:PRK10636 82 EYVIDGDRE-YRQLEAQLHDANERND-------GH------------AIAT----IHGKLDAIDAWTIRSRAASLLHGLG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 330 FSPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPKTFIVVSHAREFLNTVVTDIL 409
Cdd:PRK10636 138 FSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKII 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 410 HLQGQKLTAYKGDYDTFERTREEQIKNQRKAIEANEKSRAHMQTFIDKFRYNAKRASLVQSRIKALDRlghMDEI----V 485
Cdd:PRK10636 218 HIEQQSLFEYTGNYSSFEVQRATRLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLER---MELIapahV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 486 NDPdYKFEFPTPDDRPGaPIISFSDASFGYpGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFR 565
Cdd:PRK10636 295 DNP-FHFSFRAPESLPN-PLLKMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 566 SAKVRIAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHI 645
Cdd:PRK10636 372 AKGIKLGYFAQHQLEFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNL 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 646 ILLDEPSNHLDLDAVEALIQGLVLFQGGILMVSHDEHLISGSVDELWVVSQGKVTPFHGTFLDYKKIL 713
Cdd:PRK10636 452 LLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWL 519
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
194-709 |
5.86e-84 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 275.23 E-value: 5.86e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 194 SVTLSFGRHYGLVGRNGTGKTTFlryMALHAIDGIPRNCQILHVEQEVVG---------DDTSALQCVLNSDIERTRLLE 264
Cdd:PRK15064 21 SVKFGGGNRYGLIGANGCGKSTF---MKILGGDLEPSAGNVSLDPNERLGklrqdqfafEEFTVLDTVIMGHTELWEVKQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 265 EEVRLHAQqrdLDFEDAAGNGKGDqigainkdaisqrLEEIYKRLeliDAYSAEARAASILAGLSFSPE-----MQKKAT 339
Cdd:PRK15064 98 ERDRIYAL---PEMSEEDGMKVAD-------------LEVKFAEM---DGYTAEARAGELLLGVGIPEEqhyglMSEVAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 340 ktfsgGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPKTFIVVSHAREFLNTVVTDILHLQGQKLTAY 419
Cdd:PRK15064 159 -----GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 420 KGDYDTFeRTREEQIKNQRKAIEANEKSR-AHMQTFIDKFRYNAKRASLVQSRIKALDRLgHMDEI-----VNdPDYKFE 493
Cdd:PRK15064 234 PGNYDEY-MTAATQARERLLADNAKKKAQiAELQSFVSRFSANASKAKQATSRAKQIDKI-KLEEVkpssrQN-PFIRFE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 494 FPTPDDRpgaPIISFSDASFGYPGGPLmFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKVRIAV 573
Cdd:PRK15064 311 QDKKLHR---NALEVENLTKGFDNGPL-FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 574 FSQHHVDGLDLSSNpLLYMMRCF--PGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEP 651
Cdd:PRK15064 387 YAQDHAYDFENDLT-LFDWMSQWrqEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 652 SNHLDLDAVEALIQGLVLFQGGILMVSHDEHLISGSVDELWVVSQGKVTPFHGTFLDY 709
Cdd:PRK15064 466 TNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEY 523
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
205-708 |
6.74e-65 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 226.76 E-value: 6.74e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 205 LVGRNGTGKTTFLRYMAlhaidgiprncqilhveQEVVGDDTsalQCVLNSDIERTRLLEEEVRlHAQQRDLDFEDAAGN 284
Cdd:PRK11147 34 LVGRNGAGKSTLMKILN-----------------GEVLLDDG---RIIYEQDLIVARLQQDPPR-NVEGTVYDFVAEGIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 285 GKGDQIGAINkdAISQ------------RLEEIYKRLELIDAYSAEARAASILAGLSFSPEMQKKAtktFSGGWRMRIAL 352
Cdd:PRK11147 93 EQAEYLKRYH--DISHlvetdpseknlnELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDAALSS---LSGGWLRKAAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 353 ARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPKTFIVVSHAREFLNTVVTDILHLQGQKLTAYKGDYDTFERTREE 432
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 433 qikNQRKAIEANE---KSRAHMQTFIdkfRYNAK----------RA--SLVQSRIKALDRLGHMDEIVNDPdykfefptp 497
Cdd:PRK11147 248 ---ALRVEELQNAefdRKLAQEEVWI---RQGIKarrtrnegrvRAlkALRRERSERREVMGTAKMQVEEA--------- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 498 dDRPGAPIISFSDASFGYPGGPLMfKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKVRIAVFSQH 577
Cdd:PRK11147 313 -SRSGKIVFEMENVNYQIDGKQLV-KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 578 HVDgLDlssnpllymmrcfpgvPEQKLRAHLG-----------SFGVTGNL---------ALQPMYTLSGGQKSRVAFAK 637
Cdd:PRK11147 391 RAE-LD----------------PEKTVMDNLAegkqevmvngrPRHVLGYLqdflfhpkrAMTPVKALSGGERNRLLLAR 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743842931 638 ITFKKPHIILLDEPSNHLDLDAVEALIQGLVLFQGGILMVSHDEHLISGSVDELWVVS-QGKVTPFHGTFLD 708
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEgNGKIGRYVGGYHD 525
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
195-709 |
3.39e-61 |
|
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: 214.80 E-value: 3.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 195 VTLSF--GRHYGLVGRNGTGKTTFLRYMAlhAID----GIPR---NCQILHVEQEVVGDDT-SALQCVLNSDIERTRLLE 264
Cdd:TIGR03719 24 ISLSFfpGAKIGVLGLNGAGKSTLLRIMA--GVDkdfnGEARpqpGIKVGYLPQEPQLDPTkTVRENVEEGVAEIKDALD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 265 E--EVRLHAQQRDLDFedaagngkgdqigainkDAISQRLEEIYKRLELIDAYSAEARAASILAGLSFSPEMQKKATktF 342
Cdd:TIGR03719 102 RfnEISAKYAEPDADF-----------------DKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWDADVTK--L 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPKTFIVVSHAREFLNTVVTDILHLQGQKLTAYKGD 422
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 423 YDTFERTREEQIKNQRKAIEANEKSRAHMQTFIdkfRYNAK-RASLVQSRIKALDRLGHMDEIVNDPDYKFEFPtPDDRP 501
Cdd:TIGR03719 243 YSSWLEQKQKRLEQEEKEESARQKTLKRELEWV---RQSPKgRQAKSKARLARYEELLSQEFQKRNETAEIYIP-PGPRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 502 GAPIISFSDASFGYpGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKVRIAVFSQHHvDG 581
Cdd:TIGR03719 319 GDKVIEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSR-DA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 582 LDLS-------SNPLLYMMRcfpGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNH 654
Cdd:TIGR03719 397 LDPNktvweeiSGGLDIIKL---GKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTND 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743842931 655 LDLDAVEALIQGLVLFQGGILMVSHDE--------HLISGSVDelwvvsqGKVTPFHGTFLDY 709
Cdd:TIGR03719 474 LDVETLRALEEALLNFAGCAVVISHDRwfldriatHILAFEGD-------SHVEWFEGNFSEY 529
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
184-711 |
2.20e-53 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 193.41 E-value: 2.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 184 VGGRDLIVDGsVTLSF--GRHYGLVGRNGTGKTTFLRYMA---------LHAIDGIprNCQILhvEQEVVGDDT-SALQC 251
Cdd:PRK11819 16 VPPKKQILKD-ISLSFfpGAKIGVLGLNGAGKSTLLRIMAgvdkefegeARPAPGI--KVGYL--PQEPQLDPEkTVREN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 252 VLNSDIERTRLLEE--EVRLHAQQRDLDFED-AAGNGK-GDQIGAINKDAISQRLEeiykrlelidaysaeaRAASILAg 327
Cdd:PRK11819 91 VEEGVAEVKAALDRfnEIYAAYAEPDADFDAlAAEQGElQEIIDAADAWDLDSQLE----------------IAMDALR- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 328 lsfSPEMQKKATKtFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPKTFIVVSHAREFLNTVVTD 407
Cdd:PRK11819 154 ---CPPWDAKVTK-LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGW 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 408 ILHLQGQKLTAYKGDYDTFERTREEQIKNQRKAIEANEKSRAHMQTFIdkfRYNAK-RaslvQSRIKAldRLGHMDEIVN 486
Cdd:PRK11819 230 ILELDRGRGIPWEGNYSSWLEQKAKRLAQEEKQEAARQKALKRELEWV---RQSPKaR----QAKSKA--RLARYEELLS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 487 DPDYKFE-----FPTPDDRPGAPIISFSDASFGYpGGPLMFKNLNF-----GIdldsrIAMVGPNGIGKSTILKLIAGEL 556
Cdd:PRK11819 301 EEYQKRNetneiFIPPGPRLGDKVIEAENLSKSF-GDRLLIDDLSFslppgGI-----VGIIGPNGAGKSTLFKMITGQE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 557 QPTSGTVFRSAKVRIAVFSQHHvDGLDLS-------SNPLLYMMRcfpGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQ 629
Cdd:PRK11819 375 QPDSGTIKIGETVKLAYVDQSR-DALDPNktvweeiSGGLDIIKV---GNREIPSRAYVGRFNFKGGDQQKKVGVLSGGE 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 630 KSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVLFQGGILMVSHDE--------HLISGSVDelwvvsqGKVTP 701
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRwfldriatHILAFEGD-------SQVEW 523
|
570
....*....|
gi 743842931 702 FHGTFLDYKK 711
Cdd:PRK11819 524 FEGNFQEYEE 533
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
506-698 |
1.86e-51 |
|
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: 175.33 E-value: 1.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGPLmFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKVRIAVFSQhhvdgldls 585
Cdd:cd03221 1 IELENLSKTYGGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 586 snpllymmrcfpgvpeqklrahlgsfgvtgnlalqpmytLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQ 665
Cdd:cd03221 71 ---------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE 111
|
170 180 190
....*....|....*....|....*....|...
gi 743842931 666 GLVLFQGGILMVSHDEHLISGSVDELWVVSQGK 698
Cdd:cd03221 112 ALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
175-415 |
4.01e-42 |
|
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: 149.52 E-value: 4.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMA--LHAIDGIPR---NCQILHVEQevvgddtsal 249
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAgeLEPDEGIVTwgsTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 250 qcvlnsdiertrlleeevrlhaqqrdldfedaagngkgdqigainkdaisqrleeiykrlelidaysaearaasilagls 329
Cdd:cd03221 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 330 fspemqkkatktFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPKTFIVVSHAREFLNTVVTDIL 409
Cdd:cd03221 71 ------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKII 138
|
....*.
gi 743842931 410 HLQGQK 415
Cdd:cd03221 139 ELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
123-428 |
1.68e-34 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 138.27 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 123 DKMKIERRKRKDErqreaqyQIHLAEMEAVRAGMPVacvthdgggggpnvkdIHLENFNISVGGRDLIVDGSVTLSFGRH 202
Cdd:COG0488 287 EKLEREEPPRRDK-------TVEIRFPPPERLGKKV----------------LELEGLSKSYGDKTLLDDLSLRIDRGDR 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 203 YGLVGRNGTGKTTFLRYMA--LHAIDG---IPRNCQILHVEQEvvgddtsalQCVLNSDierTRLLEEevrlhaqqrdld 277
Cdd:COG0488 344 IGLIGPNGAGKSTLLKLLAgeLEPDSGtvkLGETVKIGYFDQH---------QEELDPD---KTVLDE------------ 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 278 FEDAAGNGKgdqigainkdaisqrleeiykrlelidaysaEARAASILAGLSFSPEMQKKATKTFSGGWRMRIALARALF 357
Cdd:COG0488 400 LRDGAPGGT-------------------------------EQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLL 448
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743842931 358 IEPDILLLDEPTNHLDLHAVLWLESYLVKWPKTFIVVSHAREFLNTVVTDILHLQGQKLTAYKGDYDTFER 428
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
506-699 |
3.06e-31 |
|
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: 122.06 E-value: 3.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDLS 585
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVL--------------VDGKDIT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 586 SNPLLYMMR-------------CFP-------------GVPEQKLRAH----LGSFGVTGnLALQPMYTLSGGQKSRVAF 635
Cdd:COG1122 67 KKNLRELRRkvglvfqnpddqlFAPtveedvafgpenlGLPREEIRERveeaLELVGLEH-LADRPPHELSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743842931 636 AKITFKKPHIILLDEPSNHLDLDAVE---ALIQGLVLFQGGILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRellELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
505-699 |
8.59e-31 |
|
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: 121.30 E-value: 8.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 505 IISFSDASFGYPGGPLmFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF--------RSAKV---RIAV 573
Cdd:COG1120 1 MLEAENLSVGYGGRPV-LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgrdlasLSRRElarRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 574 FSQHHVDGLDLSSNPLLYMMRcfpgvpeqklRAHLGSFGV-----------------TGNLALQPMYTLSGGQKSRVAFA 636
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGR----------YPHLGLFGRpsaedreaveealertgLEHLADRPVDELSGGERQRVLIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743842931 637 KITFKKPHIILLDEPSNHLDLD---AVEALIQGLVLFQG-GILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAhqlEVLELLRRLARERGrTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
509-700 |
2.12e-30 |
|
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: 117.92 E-value: 2.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 509 SDASFGYPGGPLmFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVfrsakvriavfsqhHVDGLDLSSNP 588
Cdd:cd03214 3 ENLSVGYGGRTV-LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI--------------LLDGKDLASLS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 589 LLYMMRCFPGVPeQKLRAhlgsFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDL---DAVEALIQ 665
Cdd:cd03214 68 PKELARKIAYVP-QALEL----LGLA-HLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIahqIELLELLR 141
|
170 180 190
....*....|....*....|....*....|....*.
gi 743842931 666 GLVLFQG-GILMVSHDEHLISGSVDELWVVSQGKVT 700
Cdd:cd03214 142 RLARERGkTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
507-698 |
3.89e-30 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 116.19 E-value: 3.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 507 SFSDASFGYPGGPLmFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVfrsakvriavfsqhHVDGLDLSS 586
Cdd:cd00267 1 EIENLSFRYGGRTA-LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI--------------LIDGKDIAK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 587 NPLlymmrcfpgvpeQKLRAHLGsfgvtgnLALQpmytLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQG 666
Cdd:cd00267 66 LPL------------EELRRRIG-------YVPQ----LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEL 122
|
170 180 190
....*....|....*....|....*....|....*
gi 743842931 667 LV-LFQGG--ILMVSHDEHLISGSVDELWVVSQGK 698
Cdd:cd00267 123 LReLAEEGrtVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
507-704 |
9.91e-30 |
|
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: 117.25 E-value: 9.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 507 SFSDASFGYPGGPLMfKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAK------VRIAVFSQHH-- 578
Cdd:cd03235 1 EVEDLTVSYGGHPVL-EDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerKRIGYVPQRRsi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 579 -----VDGLDLSSNPLLYMMRCFPGVPE---QKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDE 650
Cdd:cd03235 80 drdfpISVRDVVLMGLYGHKGLFRRLSKadkAKVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743842931 651 PSNHLDLDAVEALIQGL-VLFQGG--ILMVSHDEHLISGSVDELWVVSQGKVtpFHG 704
Cdd:cd03235 159 PFAGVDPKTQEDIYELLrELRREGmtILVVTHDLGLVLEYFDRVLLLNRTVV--ASG 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
501-705 |
2.62e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 116.73 E-value: 2.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 501 PGAPIISFSDASFGYPGGPLmFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF------RSAKVRIAVF 574
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPV-LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 575 SQHH-------VDGLDLSSNPLLYMMRCFPGV-PEQKLRAH--LGSFGVTGnLALQPMYTLSGGQKSRVAFAKITFKKPH 644
Cdd:COG1121 81 PQRAevdwdfpITVRDVVLMGRYGRRGLFRRPsRADREAVDeaLERVGLED-LADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743842931 645 IILLDEPSNHLDLDAVEA---LIQGLVLFQGGILMVSHDEHLISGSVDELWVVSQGKVtpFHGT 705
Cdd:COG1121 160 LLLLDEPFAGVDAATEEAlyeLLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV--AHGP 221
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
409-494 |
2.11e-28 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 108.82 E-value: 2.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 409 LHLQGQKLTAYKGDYDTFERTREEQIKNQRKAIEANEKSRAHMQTFIDKFRYNAKRASLVQSRIKALDRLGHMdEIVNDP 488
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKMERI-EKPERD 79
|
....*.
gi 743842931 489 DYKFEF 494
Cdd:pfam12848 80 KPKLRF 85
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
496-700 |
3.67e-28 |
|
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: 119.86 E-value: 3.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 496 TPDDRPGAPIISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTV---------FRS 566
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdlsdLDP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 567 AKVR--IAVFSQH-HVDGLDLSSNPLLYMmrcfPGVPEQKLRAHLGSFGVTGNLALQPM----------YTLSGGQKSRV 633
Cdd:COG4988 407 ASWRrqIAWVPQNpYLFAGTIRENLRLGR----PDASDEELEAALEAAGLDEFVAALPDgldtplgeggRGLSGGQAQRL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743842931 634 AFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLV-LFQG-GILMVSHDEHLISgSVDELWVVSQGKVT 700
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRrLAKGrTVILITHRLALLA-QADRILVLDDGRIV 550
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
467-701 |
4.02e-28 |
|
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: 119.49 E-value: 4.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 467 LVQSRiKALDRLghmDEIVNDPDYKFEFPTPDDRPGAPIISFSDASFGYPGGPLM-FKNLNFGIDLDSRIAMVGPNGIGK 545
Cdd:COG4987 299 LGRVR-AAARRL---NELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPvLDGLSLTLPPGERVAIVGPSGSGK 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 546 STILKLIAGELQPTSGTV---------FRSAKVR--IAVFSQH-HV-DGlDLSSNplLYMMRcfPGVPEQKL-----RAH 607
Cdd:COG4987 375 STLLALLLRFLDPQSGSItlggvdlrdLDEDDLRrrIAVVPQRpHLfDT-TLREN--LRLAR--PDATDEELwaaleRVG 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 608 LGSF------------GVTGnlalqpmYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLV-LFQG-G 673
Cdd:COG4987 450 LGDWlaalpdgldtwlGEGG-------RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLeALAGrT 522
|
250 260
....*....|....*....|....*...
gi 743842931 674 ILMVSHDEHLIsGSVDELWVVSQGKVTP 701
Cdd:COG4987 523 VLLITHRLAGL-ERMDRILVLEDGRIVE 549
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
506-698 |
5.73e-28 |
|
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: 110.55 E-value: 5.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGPLM-FKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDL 584
Cdd:cd03228 1 IEFKNVSFSYPGRPKPvLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIL--------------IDGVDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 585 SSNPLLYMMRCFPGVPEQklrAHLGSFGVTGNLalqpmytLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALI 664
Cdd:cd03228 67 RDLDLESLRKNIAYVPQD---PFLFSGTIRENI-------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALIL 136
|
170 180 190
....*....|....*....|....*....|....*.
gi 743842931 665 QGLVLFQGG--ILMVSHDEHLISgSVDELWVVSQGK 698
Cdd:cd03228 137 EALRALAKGktVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
507-698 |
8.92e-28 |
|
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: 111.40 E-value: 8.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 507 SFSDASFGYPGGPLM-FKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDLS 585
Cdd:cd03225 1 ELKNLSFSYPDGARPaLDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVL--------------VDGKDLT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 586 SNPL-----------------LYMMRCFP---------GVPE----QKLRAHLGSFGVTGnLALQPMYTLSGGQKSRVAF 635
Cdd:cd03225 67 KLSLkelrrkvglvfqnpddqFFGPTVEEevafglenlGLPEeeieERVEEALELVGLEG-LRDRSPFTLSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 636 AKITFKKPHIILLDEPSNHLDLDAVEALIQGLV-LFQGG--ILMVSHDEHLISGSVDELWVVSQGK 698
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKkLKAEGktIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
514-685 |
1.27e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 110.40 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 514 GYPGGPLmFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKVRIAVFSQHH--VDGLDLSSNPLLY 591
Cdd:NF040873 1 GYGGRPV-LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSevPDSLPLTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 592 MMRCFPGVPEQKLRAH--------LGSFGVTGnLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEAL 663
Cdd:NF040873 80 MGRWARRGLWRRLTRDdraavddaLERVGLAD-LAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI 158
|
170 180
....*....|....*....|....*
gi 743842931 664 IQGLVLFQG---GILMVSHDEHLIS 685
Cdd:NF040873 159 IALLAEEHArgaTVVVVTHDLELVR 183
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
522-653 |
8.31e-27 |
|
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: 106.58 E-value: 8.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 522 FKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF-----------RSAKVRIAVFSQHHVDGLDLS--SNP 588
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdltdderKSLRKEIGYVFQDPQLFPRLTvrENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 589 LLYMMRCFPGVPE-----QKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSN 653
Cdd:pfam00005 81 RLGLLLKGLSKREkdaraEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
474-699 |
1.00e-26 |
|
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: 116.09 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 474 ALDRLGHMDEIVNDPDYKFEFPTPDDRPGApiISFSDASFGYPG-GPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLI 552
Cdd:COG2274 444 ALERLDDILDLPPEREEGRSKLSLPRLKGD--IELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 553 AGELQPTSGTVFrsakvriavfsqhhVDGLDLSS---------------NPLLY---------MMRcfPGVPEQKLRAHL 608
Cdd:COG2274 522 LGLYEPTSGRIL--------------IDGIDLRQidpaslrrqigvvlqDVFLFsgtirenitLGD--PDATDEEIIEAA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 609 GSFGVTGNLALQPM-Y---------TLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVLFQGG--ILM 676
Cdd:COG2274 586 RLAGLHDFIEALPMgYdtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGrtVII 665
|
250 260
....*....|....*....|...
gi 743842931 677 VSHDEHLISgSVDELWVVSQGKV 699
Cdd:COG2274 666 IAHRLSTIR-LADRIIVLDKGRI 687
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
506-699 |
1.24e-26 |
|
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: 106.92 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGG-PLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVfrsakvriavfsqhHVDGLDL 584
Cdd:cd03246 1 LEVENVSFRYPGAePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV--------------RLDGADI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 585 SSNPLLYMMRCFPGVPeQKLRAHLGSfgVTGNLalqpmytLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLD---AVE 661
Cdd:cd03246 67 SQWDPNELGDHVGYLP-QDDELFSGS--IAENI-------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEgerALN 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 743842931 662 ALIQGLVLFQGGILMVSHDEHLISgSVDELWVVSQGKV 699
Cdd:cd03246 137 QAIAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
504-686 |
2.25e-26 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 107.18 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 504 PIISFSDASFGYpGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF----RSAKVRIAVFSQH-- 577
Cdd:COG4133 1 MMLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLwngePIRDAREDYRRRLay 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 578 --HVDGLDLSSNPL--LYMMRCFPGV--PEQKLRAHLGSFGVTGnLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEP 651
Cdd:COG4133 80 lgHADGLKPELTVRenLRFWAALYGLraDREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 743842931 652 SNHLDLDAVEALIQGLVLF--QGG-ILMVSHDEHLISG 686
Cdd:COG4133 159 FTALDAAGVALLAELIAAHlaRGGaVLLTTHQPLELAA 196
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
175-699 |
6.36e-26 |
|
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: 112.30 E-value: 6.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNIS-VGGRDLIVDG-SVTLSFGRHYGLVGRNGTGKTTFLRymalhAIDG-IPRNCQIlhvEQEVVGDDTSALQc 251
Cdd:COG1123 5 LEVRDLSVRyPGGDVPAVDGvSLTIAPGETVALVGESGSGKSTLAL-----ALMGlLPHGGRI---SGEVLLDGRDLLE- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 252 vlnsdiertrlLEEEVRlhaqqrdldfedaagngkGDQIGAINKDAISQR-----LEEIYKRLELIDAYSAEARAASI-- 324
Cdd:COG1123 76 -----------LSEALR------------------GRRIGMVFQDPMTQLnpvtvGDQIAEALENLGLSRAEARARVLel 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 325 --LAGLsfsPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDL---HAVLWLESYLVKWP-KTFIVVSHAR 398
Cdd:COG1123 127 leAVGL---ERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVttqAEILDLLRELQRERgTTVLLITHDL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 399 EFLNTVVTDILHLQGQKLTaykgdydtfERTREEQIKNQRKAIEAneksrahmqtfidkfrynakraslvqsrikaldrl 478
Cdd:COG1123 204 GVVAEIADRVVVMDDGRIV---------EDGPPEEILAAPQALAA----------------------------------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 479 ghmdeiVNDPDYKFEFPTPDDRPGAPIISFSDASFGYP-GGPLMFKNLNfGIDLD----SRIAMVGPNGIGKSTILKLIA 553
Cdd:COG1123 240 ------VPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPvRGKGGVRAVD-DVSLTlrrgETLGLVGESGSGKSTLARLLL 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 554 GELQPTSGTVfrsakvriavfsqhHVDGLDLSS------------------------NP-------LLYMMRCFPGVPEQ 602
Cdd:COG1123 313 GLLRPTSGSI--------------LFDGKDLTKlsrrslrelrrrvqmvfqdpysslNPrmtvgdiIAEPLRLHGLLSRA 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 603 KLRAH----LGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLdAVEALIQGLVL-----FQGG 673
Cdd:COG1123 379 ERRERvaelLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDV-SVQAQILNLLRdlqreLGLT 457
|
570 580
....*....|....*....|....*.
gi 743842931 674 ILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:COG1123 458 YLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
506-699 |
8.92e-24 |
|
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: 8.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGPLmFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDLS 585
Cdd:cd03230 1 IEVRNLSKRYGKKTA-LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK--------------VLGKDIK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 586 SNPLlymmrcfpgvpeqKLRAHLGSfgVTGNLALQPMYT------LSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDA 659
Cdd:cd03230 66 KEPE-------------EVKRRIGY--LPEEPSLYENLTvrenlkLSGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 743842931 660 VEA---LIQGLVLFQGGILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:cd03230 131 RREfweLLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
493-681 |
3.69e-23 |
|
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: 103.98 E-value: 3.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 493 EFPTPDDR-PGAPIISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTV-------- 563
Cdd:TIGR02868 321 SAPAAGAVgLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvs 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 564 -FRSAKVR--IAVFSQH-HVDGLDLSSNPLLYMmrcfPGVPEQKLRAHLGSFGVTGNLALQP--MYT--------LSGGQ 629
Cdd:TIGR02868 401 sLDQDEVRrrVSVCAQDaHLFDTTVRENLRLAR----PDATDEELWAALERVGLADWLRALPdgLDTvlgeggarLSGGE 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 743842931 630 KSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGL--VLFQGGILMVSHDE 681
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLEDLlaALSGRTVVLITHHL 530
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
536-699 |
6.41e-23 |
|
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: 98.73 E-value: 6.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 536 AMVGPNGIGKSTILKLIAGELQPTSGTVF-----------RSAKVRIAVFSQHHVDGLDLSSNPLLYMMRcfpgVPEQKL 604
Cdd:TIGR03873 31 GLLGPNGSGKSTLLRLLAGALRPDAGTVDlagvdlhglsrRARARRVALVEQDSDTAVPLTVRDVVALGR----IPHRSL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 605 ------------RAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDA---VEALIQGLVL 669
Cdd:TIGR03873 107 wagdsphdaavvDRALARTELS-HLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAqleTLALVRELAA 185
|
170 180 190
....*....|....*....|....*....|
gi 743842931 670 FQGGILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:TIGR03873 186 TGVTVVAALHDLNLAASYCDHVVVLDGGRV 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
175-435 |
6.89e-23 |
|
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: 98.39 E-value: 6.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMA--LH------AIDGIPRNCQILHVEQEVvgddt 246
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAglLKpdsgsiLIDGEDVRKEPREARRQI----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 247 salqCVLNSDIERT-RL-LEEEVRLHAQQRDLdfedaagngkgdqigaiNKDAISQRLEEIYKRLELidaysaearaasi 324
Cdd:COG4555 77 ----GVLPDERGLYdRLtVRENIRYFAELYGL-----------------FDEELKKRIEELIELLGL------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 325 laglsfsPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKW---PKTFIVVSHAREFL 401
Cdd:COG4555 123 -------EEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEV 195
|
250 260 270
....*....|....*....|....*....|....
gi 743842931 402 NTVVTDILHLQGQKLTAYKGDYDTFERTREEQIK 435
Cdd:COG4555 196 EALCDRVVILHKGKVVAQGSLDELREEIGEENLE 229
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
506-699 |
7.54e-23 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 97.19 E-value: 7.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGPLmFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF--------------RSakvRI 571
Cdd:COG4619 1 LELEGLSFRVGGKPI-LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgkplsampppewRR---QV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 572 AVFSQHHV-------DGLDLssnPLLYMMRCFPgvpEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPH 644
Cdd:COG4619 77 AYVPQEPAlwggtvrDNLPF---PFQLRERKFD---RERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 743842931 645 IILLDEPSNHLDLD---AVEALIQGLVLFQG-GILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:COG4619 151 VLLLDEPTSALDPEntrRVEELLREYLAEEGrAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
506-685 |
7.66e-23 |
|
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: 97.18 E-value: 7.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGPLMF---KNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTV-----------------FR 565
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisklsekelaaFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 566 SAKVRIaVFSQHH-VDGLDLSSNPLLYMMrcFPGVP--EQKLRAH--LGSFGVTGNLALQPMyTLSGGQKSRVAFAKITF 640
Cdd:cd03255 81 RRHIGF-VFQSFNlLPDLTALENVELPLL--LAGVPkkERRERAEelLERVGLGDRLNHYPS-ELSGGQQQRVAIARALA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 743842931 641 KKPHIILLDEPSNHLDLD---AVEALIQGLVLFQG-GILMVSHDEHLIS 685
Cdd:cd03255 157 NDPKIILADEPTGNLDSEtgkEVMELLRELNKEAGtTIVVVTHDPELAE 205
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
495-694 |
2.26e-22 |
|
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: 101.59 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 495 PTPDDRP----GAPIISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTV------- 563
Cdd:TIGR02857 307 PLAGKAPvtaaPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIavngvpl 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 564 --FRSAKVR--IAVFSQH-HVDGLDLSSNPLLYMmrcfPGVPEQKLRAHLGSFGVTGNLALQPMYT----------LSGG 628
Cdd:TIGR02857 387 adADADSWRdqIAWVPQHpFLFAGTIAENIRLAR----PDASDAEIREALERAGLDEFVAALPQGLdtpigeggagLSGG 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743842931 629 QKSRVAFAKITFKKPHIILLDEPSNHLD-------LDAVEALIQGLVLfqggiLMVSHDEHLISGsVDELWVV 694
Cdd:TIGR02857 463 QAQRLALARAFLRDAPLLLLDEPTAHLDaeteaevLEALRALAQGRTV-----LLVTHRLALAAL-ADRIVVL 529
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
506-705 |
2.55e-22 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 96.42 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYpGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF--------------RSAKVRI 571
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLidgedisglseaelYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 572 AVFSQHHV--DGLDLSSN---PLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPmYTLSGGQKSRVAFAKITFKKPHII 646
Cdd:cd03261 80 GMLFQSGAlfDSLTVFENvafPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYP-AELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743842931 647 LLDEPSNHLD---LDAVEALIQGL-VLFQGGILMVSHDEHLISGSVDELWVVSQGKVtPFHGT 705
Cdd:cd03261 159 LYDEPTAGLDpiaSGVIDDLIRSLkKELGLTSIMVTHDLDTAFAIADRIAVLYDGKI-VAEGT 220
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
175-416 |
4.32e-22 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 94.88 E-value: 4.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMA----LHA----IDGIPRNC--------QILHVE 238
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALAdldpPTSgeiyLDGKPLSAmpppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 239 QEVVgddtsalqcvlnsdiertrLLEEEVRLHaqqrdLDFEDAAGNGKGDqigainkdaisqrleeiykrlelidaysaE 318
Cdd:COG4619 81 QEPA-------------------LWGGTVRDN-----LPFPFQLRERKFD-----------------------------R 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 319 ARAASILAGLSFSPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPK----TFIVV 394
Cdd:COG4619 108 ERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAeegrAVLWV 187
|
250 260
....*....|....*....|..
gi 743842931 395 SHAREFLNTVVTDILHLQGQKL 416
Cdd:COG4619 188 SHDPEQIERVADRVLTLEAGRL 209
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
505-684 |
4.84e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 95.12 E-value: 4.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 505 IISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDL 584
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVL--------------VNGQDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 585 SSNP---LLYMMRC---------------------FP----GVPEQKLRAH----LGSFGVTGNLALQPMyTLSGGQKSR 632
Cdd:COG2884 67 SRLKrreIPYLRRRigvvfqdfrllpdrtvyenvaLPlrvtGKSRKEIRRRvrevLDLVGLSDKAKALPH-ELSGGEQQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 633 VAFAKITFKKPHIILLDEPSNHLDLDAVEALIQglvLF----QGG--ILMVSHDEHLI 684
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIME---LLeeinRRGttVLIATHDLELV 200
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
506-700 |
8.70e-22 |
|
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: 93.15 E-value: 8.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPG-GPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDL 584
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT--------------LDGVPV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 585 SSnpLLYMMRCFPGVPEQklRAHLGSFGVTGNLALQpmytLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALI 664
Cdd:cd03247 67 SD--LEKALSSLISVLNQ--RPYLFDTTLRNNLGRR----FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL 138
|
170 180 190
....*....|....*....|....*....|....*....
gi 743842931 665 QGL--VLFQGGILMVSHdeHLISGS-VDELWVVSQGKVT 700
Cdd:cd03247 139 SLIfeVLKDKTLIWITH--HLTGIEhMDKILFLENGKII 175
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
503-685 |
1.09e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 94.34 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 503 APIISFSDASFGYPGGPLMFKNLNfGIDLD----SRIAMVGPNGIGKSTILKLIAGELQPTSGTVF------------RS 566
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALR-GVSLSieagEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidgqdisslserEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 567 AKVR---IA-VFSQHH-VDGLDLSSN---PLLYMmrcfpGVPEQKLRAH----LGSFGVTGNLALQPmYTLSGGQKSRVA 634
Cdd:COG1136 81 ARLRrrhIGfVFQFFNlLPELTALENvalPLLLA-----GVSRKERRERarelLERVGLGDRLDHRP-SQLSGGQQQRVA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 743842931 635 FAKITFKKPHIILLDEPSNHLDL---DAVEALIQGLVLFQG-GILMVSHDEHLIS 685
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSktgEEVLELLRELNRELGtTIVMVTHDPELAA 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
506-705 |
1.11e-21 |
|
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: 94.54 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYpGGPLMFKNLNFGIDlDSRI-AMVGPNGIGKSTILKLIAGELQPTSGTVfrsakvriavfsqhHVDGLDL 584
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAK-DGEItGLLGPNGAGKTTLLRMLAGLLKPDSGSI--------------LIDGEDV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 585 SSNPLLYMMRCF-----PGVPE-QKLRAHLGSFG----------------VTGNLALQPMY-----TLSGGQKSRVAFAK 637
Cdd:COG4555 66 RKEPREARRQIGvlpdeRGLYDrLTVRENIRYFAelyglfdeelkkrieeLIELLGLEEFLdrrvgELSTGMKKKVALAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743842931 638 ITFKKPHIILLDEPSNHLDLDAVEALIQGLVLF--QG-GILMVSHDEHLISGSVDELWVVSQGKVTpFHGT 705
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkEGkTVLFSSHIMQEVEALCDRVVILHKGKVV-AQGS 215
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
474-699 |
2.08e-21 |
|
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: 99.17 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 474 ALDRLghmDEIVNdpdykfefpTPDDRPGA------PIIS----FSDASFGYPG-GPLMFKNLNFGIDLDSRIAMVGPNG 542
Cdd:TIGR03375 434 ALQSL---DELMQ---------LPVERPEGtrflhrPRLQgeieFRNVSFAYPGqETPALDNVSLTIRPGEKVAIIGRIG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 543 IGKSTILKLIAGELQPTSGTVfrsakvRIAVFSQHHVDGLDLSSN--------PLLY-------MMRCfPGVPEQKLRAH 607
Cdd:TIGR03375 502 SGKSTLLKLLLGLYQPTEGSV------LLDGVDIRQIDPADLRRNigyvpqdpRLFYgtlrdniALGA-PYADDEEILRA 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 608 LGSFGVTGNLALQPM----------YTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVLFQGG--IL 675
Cdd:TIGR03375 575 AELAGVTEFVRRHPDgldmqigergRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGktLV 654
|
250 260
....*....|....*....|....
gi 743842931 676 MVSHDEHLISgSVDELWVVSQGKV 699
Cdd:TIGR03375 655 LVTHRTSLLD-LVDRIIVMDNGRI 677
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
504-699 |
2.50e-21 |
|
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: 94.00 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 504 PIISFSDASFGYPGGPLmFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSG---TVF---------RSAKVRI 571
Cdd:COG1119 2 PLLELRNVTVRRGGKTI-LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFgerrggedvWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 572 AVFS---QHHV---------------DGLDLSSNPLlymmrcfpgvPEQKLRAH--LGSFGVTGnLALQPMYTLSGGQKS 631
Cdd:COG1119 81 GLVSpalQLRFprdetvldvvlsgffDSIGLYREPT----------DEQRERARelLELLGLAH-LADRPFGTLSQGEQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743842931 632 RVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGL-VLFQGG---ILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLdKLAAEGaptLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
504-656 |
4.59e-21 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 93.20 E-value: 4.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 504 PIISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF--------------RSAKV 569
Cdd:COG3638 1 PMLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILvdgqdvtalrgralRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 570 RIA-VFSQHH-VDGLD---------LSSNPLL-YMMRCFPgvPEQKLRAH--LGSFGVtGNLALQPMYTLSGGQKSRVAF 635
Cdd:COG3638 81 RIGmIFQQFNlVPRLSvltnvlagrLGRTSTWrSLLGLFP--PEDRERALeaLERVGL-ADKAYQRADQLSGGQQQRVAI 157
|
170 180
....*....|....*....|.
gi 743842931 636 AKITFKKPHIILLDEPSNHLD 656
Cdd:COG3638 158 ARALVQEPKLILADEPVASLD 178
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
535-696 |
1.82e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 91.33 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 535 IAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKVRIAVFSQH-HVDgldlSSNPLLY--MMRCFPGVPEQKLRAHLGSF 611
Cdd:PRK09544 33 LTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKlYLD----TTLPLTVnrFLRLRPGTKKEDILPALKRV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 612 GvTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLD---AVEALIQGL-VLFQGGILMVSHDEHLISGS 687
Cdd:PRK09544 109 Q-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNgqvALYDLIDQLrRELDCAVLMVSHDLHLVMAK 187
|
....*....
gi 743842931 688 VDELWVVSQ 696
Cdd:PRK09544 188 TDEVLCLNH 196
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
506-680 |
1.10e-19 |
|
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: 88.30 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGPLMFKNLNfGIDLDSR----IAMVGPNGIGKSTILKLIAGELQPTSGTV-FRSAKV------RIAVF 574
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALE-DISLSVEegefVALVGPSGCGKSTLLRIIAGLERPTSGEVlVDGEPVtgpgpdRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 575 SQHHVdgldlssnpllymmrcFP---------------GVPEQKLRAH----LGSFGVTGNLALQPmYTLSGGQKSRVAF 635
Cdd:cd03293 80 QQDAL----------------LPwltvldnvalglelqGVPKAEARERaeelLELVGLSGFENAYP-HQLSGGMRQRVAL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 743842931 636 AKITFKKPHIILLDEPSNHLDldaveAL----IQGLVL-----FQGGILMVSHD 680
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALD-----ALtreqLQEELLdiwreTGKTVLLVTHD 191
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
506-699 |
1.46e-19 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 88.03 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGP-LMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLD- 583
Cdd:cd03245 3 IEFRNVSFSYPNQEiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVL--------------LDGTDi 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 584 --------------LSSNPLLY--------MMRCFPGVPEQKLRAHLGSfGVTGNLALQPM----------YTLSGGQKS 631
Cdd:cd03245 69 rqldpadlrrnigyVPQDVTLFygtlrdniTLGAPLADDERILRAAELA-GVTDFVNKHPNgldlqigergRGLSGGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 632 RVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVLFQGG--ILMVSHDEHLISgSVDELWVVSQGKV 699
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDktLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
510-700 |
1.49e-19 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 87.31 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 510 DASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF-----RSAKVRI--AVFSQHHVD-- 580
Cdd:cd03226 4 NISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILlngkpIKAKERRksIGYVMQDVDyq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 581 -GLDLSSNPLLYMMRCFPGVPEQKlRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLD--- 656
Cdd:cd03226 84 lFTDSVREELLLGLKELDAGNEQA-ETVLKDLDLYALKERHPL-SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDykn 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 743842931 657 LDAVEALIQGLVLFQGGILMVSHDEHLISGSVDELWVVSQGKVT 700
Cdd:cd03226 162 MERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
517-679 |
3.37e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.47 E-value: 3.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 517 GGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVfrSAKVRIAVFSQH--------HVDGLdlssNP 588
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI--KLDGGDIDDPDVaeachylgHRNAM----KP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 589 LLYMM------RCFPGVPEQKLRAHLGSFGVtGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVeA 662
Cdd:PRK13539 87 ALTVAenlefwAAFLGGEELDIAAALEAVGL-APLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV-A 164
|
170 180
....*....|....*....|.
gi 743842931 663 LIQGLV---LFQGGI-LMVSH 679
Cdd:PRK13539 165 LFAELIrahLAQGGIvIAATH 185
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
194-370 |
4.59e-19 |
|
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: 84.24 E-value: 4.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 194 SVTLSFGRHYGLVGRNGTGKTTFLRymalhAIDGI--PRNCQILHVEQEVVGDDTSALQcvlnsdiERTRLLEEEVRLha 271
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLK-----LIAGLlsPTEGTILLDGQDLTDDERKSLR-------KEIGYVFQDPQL-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 272 qqrdLDFEDAAGN-GKGDQIGAINKDAISQRLEEIYKRLELIDaysaearaasilaglsFSPEMQKKATKTFSGGWRMRI 350
Cdd:pfam00005 71 ----FPRLTVRENlRLGLLLKGLSKREKDARAEEALEKLGLGD----------------LADRPVGERPGTLSGGQRQRV 130
|
170 180
....*....|....*....|
gi 743842931 351 ALARALFIEPDILLLDEPTN 370
Cdd:pfam00005 131 AIARALLTKPKLLLLDEPTA 150
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
465-665 |
5.58e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 90.99 E-value: 5.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 465 ASLVQSRIKALDRLGH-MDEIVNDPDYKFEFPTPDDRPGapiISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGI 543
Cdd:COG1132 301 LNQLQRALASAERIFElLDEPPEIPDPPGAVPLPPVRGE---IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGS 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 544 GKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDLSSNPLLYMMRCF----------------------PGVPE 601
Cdd:COG1132 378 GKSTLVNLLLRFYDPTSGRIL--------------IDGVDIRDLTLESLRRQIgvvpqdtflfsgtirenirygrPDATD 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 602 QKLR-----AHLGSF---------------GVtgnlalqpmyTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLdAVE 661
Cdd:COG1132 444 EEVEeaakaAQAHEFiealpdgydtvvgerGV----------NLSGGQRQRIAIARALLKDPPILILDEATSALDT-ETE 512
|
....
gi 743842931 662 ALIQ 665
Cdd:COG1132 513 ALIQ 516
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
506-698 |
8.44e-19 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 84.55 E-value: 8.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYpGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDLS 585
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIL--------------IDGEDLT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 586 SnpllymMRCFPGVPEQKLRAHLGSFG------VTGNLAlqpmYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDL-- 657
Cdd:cd03229 66 D------LEDELPPLRRRIGMVFQDFAlfphltVLENIA----LGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPit 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 743842931 658 -DAVEALIQGLVLFQG-GILMVSHDEHLISGSVDELWVVSQGK 698
Cdd:cd03229 136 rREVRALLKSLQAQLGiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
523-699 |
1.03e-18 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 85.89 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 523 KNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF----------RSAKVRIAVFSQHHVDGLDLSSNPLLYM 592
Cdd:COG1131 17 DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvardpAEVRRRIGYVPQEPALYPDLTVRENLRF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 593 MRCFPGVPEQKLRAH----LGSFGVTGNLAlQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVE---ALIQ 665
Cdd:COG1131 97 FARLYGLPRKEARERidelLELFGLTDAAD-RKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRelwELLR 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 743842931 666 GLVLFQGGILMVSHD----EHLIsgsvDELWVVSQGKV 699
Cdd:COG1131 176 ELAAEGKTVLLSTHYleeaERLC----DRVAIIDKGRI 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
176-415 |
1.65e-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: 83.06 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 176 HLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMALhaidgiprncqilhveqevvgddtsalqcvlns 255
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAG--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 256 dieRTRLLEEEVRlhaqqrdldfedaagngkgdqigaINKDAISQRLEEIYKRlelidaysaearaasilaGLSFSPEMq 335
Cdd:cd00267 48 ---LLKPTSGEIL------------------------IDGKDIAKLPLEELRR------------------RIGYVPQL- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 336 kkatktfSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPK---TFIVVSHAREFLNTVVTDILHLQ 412
Cdd:cd00267 82 -------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLK 154
|
...
gi 743842931 413 GQK 415
Cdd:cd00267 155 DGK 157
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
124-490 |
2.19e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 89.62 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 124 KMKIERRKRKdERQREAQYQIHlaemEAVRAGMPVacvthdgggggpnvkdIHLENFNISVGGRDLIVDGSVTLSFGRHY 203
Cdd:PRK11147 290 ALRRERSERR-EVMGTAKMQVE----EASRSGKIV----------------FEMENVNYQIDGKQLVKDFSAQVQRGDKI 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 204 GLVGRNGTGKTTFLRYM--ALHAIDGIPRncqilhveqevVGddtsalqcvlnsdierTRLleeEVRLHAQQR-DLDFE- 279
Cdd:PRK11147 349 ALIGPNGCGKTTLLKLMlgQLQADSGRIH-----------CG----------------TKL---EVAYFDQHRaELDPEk 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 280 ---DAAGNGKgdQIGAINkdaisqrleeiykrlelidaysaeARAASILAGLS---FSPEMQKKATKTFSGGWRMRIALA 353
Cdd:PRK11147 399 tvmDNLAEGK--QEVMVN------------------------GRPRHVLGYLQdflFHPKRAMTPVKALSGGERNRLLLA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 354 RaLFIEP-DILLLDEPTNHLDLHAVLWLESYLVKWPKTFIVVSHAREFLNTVVTDILHLQGQ-KLTAYKGDYD------- 424
Cdd:PRK11147 453 R-LFLKPsNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNgKIGRYVGGYHdarqqqa 531
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743842931 425 ---TFERTREEQIKNQRKAIEANEKSRAHmqtfidKFRYNAKRaSLVQ--SRIKALD-RLGHMDEIVNDPDY 490
Cdd:PRK11147 532 qylALKQPAVKKKEEAAAPKAETVKRSSK------KLSYKLQR-ELEQlpQLLEDLEaEIEALQAQVADADF 596
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
505-715 |
2.27e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 89.62 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 505 IISFSDASFGYPGGPLMfKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKVRIA------------ 572
Cdd:PRK11147 3 LISIHGAWLSFSDAPLL-DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVArlqqdpprnveg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 573 -VFS--------------QHHVDGLDLSSNPLLYMMRCFPGVPEQ-----------KLRAHLGSFGVTGNlalQPMYTLS 626
Cdd:PRK11147 82 tVYDfvaegieeqaeylkRYHDISHLVETDPSEKNLNELAKLQEQldhhnlwqlenRINEVLAQLGLDPD---AALSSLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 627 GGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVLFQGGILMVSHDEHLISGSVDELWVVSQGKVTPFHGtf 706
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPG-- 236
|
....*....
gi 743842931 707 lDYKKILQS 715
Cdd:PRK11147 237 -NYDQYLLE 244
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
506-699 |
2.57e-18 |
|
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: 84.59 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDLS 585
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSIL--------------IDGQDIR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 586 SNPLLYMMRCFPGVP---------------------------EQKLRAHLG------SFG---VTGNLALQpmytLSGGQ 629
Cdd:cd03253 67 EVTLDSLRRAIGVVPqdtvlfndtigynirygrpdatdeeviEAAKAAQIHdkimrfPDGydtIVGERGLK----LSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743842931 630 KSRVAFAKITFKKPHIILLDEPSNHLD-------LDAVEALIQGLVLfqggiLMVSHDEHLISGSvDELWVVSQGKV 699
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDthtereiQAALRDVSKGRTT-----IVIAHRLSTIVNA-DKIIVLKDGRI 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
522-699 |
3.96e-18 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 83.50 E-value: 3.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 522 FKNLNFGIDLD---SRIAMVGPNGIGKSTILKLIAGELQPTSGTV-------FRSAKV--------RIA-VFSQH----H 578
Cdd:cd03297 10 LPDFTLKIDFDlneEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlFDSRKKinlppqqrKIGlVFQQYalfpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 579 vdgLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGnLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDlD 658
Cdd:cd03297 90 ---LNVRENLAFGLKRKRNREDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD-R 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 743842931 659 AVEALIQGLV-----LFQGGILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:cd03297 165 ALRLQLLPELkqikkNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
501-706 |
5.83e-18 |
|
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: 83.88 E-value: 5.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 501 PGAPIISFSDASFGYpGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVD 580
Cdd:COG1127 1 MSEPMIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIL--------------VD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 581 GLDLS--SNPLLYMMR----------------------CFP-----GVPEQKLRAH----LGSFGVTGNLALQPmYTLSG 627
Cdd:COG1127 66 GQDITglSEKELYELRrrigmlfqggalfdsltvfenvAFPlrehtDLSEAEIRELvlekLELVGLPGAADKMP-SELSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 628 GQKSRVAFAK--ITfkKPHIILLDEPSNHLD---LDAVEALIQGLV-LFQGGILMVSHDEHLISGSVDELWVVSQGKVTp 701
Cdd:COG1127 145 GMRKRVALARalAL--DPEILLYDEPTAGLDpitSAVIDELIRELRdELGLTSVVVTHDLDSAFAIADRVAVLADGKII- 221
|
....*
gi 743842931 702 FHGTF 706
Cdd:COG1127 222 AEGTP 226
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
506-699 |
1.31e-17 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 83.25 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGG-PLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDL 584
Cdd:TIGR04520 1 IEVENVSFSYPESeKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVT--------------VDGLDT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 585 SSNPLLYMMRCF-------P--------------------GVPEQKLRAH----LGSFGVTGnLALQPMYTLSGGQKSRV 633
Cdd:TIGR04520 67 LDEENLWEIRKKvgmvfqnPdnqfvgatveddvafglenlGVPREEMRKRvdeaLKLVGMED-FRDREPHLLSGGQKQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743842931 634 AFAKITFKKPHIILLDEPSNHLDLDA---VEALIQGLVLFQG-GILMVSHD-EHLISGsvDELWVVSQGKV 699
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGrkeVLETIRKLNKEEGiTVISITHDmEEAVLA--DRVIVMNKGKI 214
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
340-661 |
1.37e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 86.79 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 340 KTFSGGWRMRIALARALFIEPDILLLDEPTNHLD----LHAVLWLESYLVKwpKTFIVVSHAREFLNtVVTDILHLqgqk 415
Cdd:PRK13409 211 SELSGGELQRVAIAAALLRDADFYFFDEPTSYLDirqrLNVARLIRELAEG--KYVLVVEHDLAVLD-YLADNVHI---- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 416 ltAY--KGDYDTFErtreeQIKNQRKAIeaNEksrahmqtFIDKFrynakraslvqsrikaLDrlghmDEIVNDPDYKFE 493
Cdd:PRK13409 284 --AYgePGAYGVVS-----KPKGVRVGI--NE--------YLKGY----------------LP-----EENMRIRPEPIE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 494 F---PTPDDRPGAPIISFSDASFGYPGgplmFKnlnfgidLDSR---------IAMVGPNGIGKSTILKLIAGELQPTSG 561
Cdd:PRK13409 326 FeerPPRDESERETLVEYPDLTKKLGD----FS-------LEVEggeiyegevIGIVGPNGIGKTTFAKLLAGVLKPDEG 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 562 TVfrSAKVRIAVFSQhhvdgldlssnpllYMMRCFPGVPEQKLRAHLGSFG-------VTGNLALQPMY-----TLSGGQ 629
Cdd:PRK13409 395 EV--DPELKISYKPQ--------------YIKPDYDGTVEDLLRSITDDLGssyykseIIKPLQLERLLdknvkDLSGGE 458
|
330 340 350
....*....|....*....|....*....|..
gi 743842931 630 KSRVAFAKITFKKPHIILLDEPSNHLDldaVE 661
Cdd:PRK13409 459 LQRVAIAACLSRDADLYLLDEPSAHLD---VE 487
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
505-699 |
1.38e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 83.59 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 505 IISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSA-----------KVR--I 571
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkksllEVRktV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 572 AVFSQHHVDGL-------DLSSNPLLYmmrcfpGVP----EQKLRAHLGSFGVTGnLALQPMYTLSGGQKSRVAFAKITF 640
Cdd:PRK13639 81 GIVFQNPDDQLfaptveeDVAFGPLNL------GLSkeevEKRVKEALKAVGMEG-FENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743842931 641 KKPHIILLDEPSNHLDLDAVEALIQGLV-LFQGGILMV--SHDEHLISGSVDELWVVSQGKV 699
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYdLNKEGITIIisTHDVDLVPVYADKVYVMSDGKI 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
501-690 |
1.80e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 82.83 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 501 PGAPIISFSDAS--FGYPGGPLM-FKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKV------RI 571
Cdd:COG1116 3 AAAPALELRGVSkrFPTGGGGVTaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPvtgpgpDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 572 A-VFsQhhvdgldlssNPLLymmrcFP---------------GVP----EQKLRAHLGSFGVTGNLALQPmYTLSGGQKS 631
Cdd:COG1116 83 GvVF-Q----------EPAL-----LPwltvldnvalglelrGVPkaerRERARELLELVGLAGFEDAYP-HQLSGGMRQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 632 RVAFAKITFKKPHIILLDEPSNHLDldaveAL----IQGLVL-----FQGGILMVSHDehlisgsVDE 690
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALD-----ALtrerLQDELLrlwqeTGKTVLFVTHD-------VDE 201
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
506-705 |
3.70e-17 |
|
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: 82.11 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGY-PGGPLMFK---NLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDG 581
Cdd:TIGR04521 1 IKLKNVSYIYqPGTPFEKKaldDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVT--------------IDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 582 LDLSSNPLLYMMRC---------FP--------------------GVPEQ--KLRAH--LGSFGVTGNLALQPMYTLSGG 628
Cdd:TIGR04521 67 RDITAKKKKKLKDLrkkvglvfqFPehqlfeetvykdiafgpknlGLSEEeaEERVKeaLELVGLDEEYLERSPFELSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 629 QKSRVAFAKITFKKPHIILLDEPSNHLDLDAVE---ALIQGLVLFQG-GILMVSHDEHLISGSVDELWVVSQGKVTpFHG 704
Cdd:TIGR04521 147 QMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKeilDLFKRLHKEKGlTVILVTHSMEDVAEYADRVIVMHKGKIV-LDG 225
|
.
gi 743842931 705 T 705
Cdd:TIGR04521 226 T 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
175-415 |
4.51e-17 |
|
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: 80.22 E-value: 4.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMA--LHAIDGiprncQILHVEQEVVGDDTSALQCV 252
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAglLPPSAG-----EVLWNGEPIRDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 253 L----NSDIERTRLLEEEVRLHAQQRDLDFEDaagngkgdqigainkDAISQRLEEIYkrlelidaysaearaasiLAGL 328
Cdd:COG4133 78 AylghADGLKPELTVRENLRFWAALYGLRADR---------------EAIDEALEAVG------------------LAGL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 329 sfspemQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPK---TFIVVSHAREFLNTVv 405
Cdd:COG4133 125 ------ADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLArggAVLLTTHQPLELAAA- 197
|
250
....*....|
gi 743842931 406 tDILHLQGQK 415
Cdd:COG4133 198 -RVLDLGDFK 206
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
506-684 |
4.95e-17 |
|
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: 80.53 E-value: 4.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKV-------RIAVFSQHH 578
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlrgrAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 579 vdGLDLSSNPLLY----------MMRCFpGVPEQKLR----AHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPH 644
Cdd:cd03292 81 --GVVFQDFRLLPdrnvyenvafALEVT-GVPPREIRkrvpAALELVGLSHKHRALPA-ELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 743842931 645 IILLDEPSNHLDLD---AVEALIQGLVLFQGGILMVSHDEHLI 684
Cdd:cd03292 157 ILIADEPTGNLDPDttwEIMNLLKKINKAGTTVVVATHAKELV 199
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
505-656 |
5.35e-17 |
|
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: 81.19 E-value: 5.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 505 IISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF--------------RSAKVR 570
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILlegtditklrgkklRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 571 IAVFSQHH--VDGLDLSSNPLL----------YMMRCFPgvPEQKLRAH--LGSFGVTGnLALQPMYTLSGGQKSRVAFA 636
Cdd:TIGR02315 81 IGMIFQHYnlIERLTVLENVLHgrlgykptwrSLLGRFS--EEDKERALsaLERVGLAD-KAYQRADQLSGGQQQRVAIA 157
|
170 180
....*....|....*....|
gi 743842931 637 KITFKKPHIILLDEPSNHLD 656
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLD 177
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
517-679 |
5.81e-17 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 79.71 E-value: 5.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 517 GGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF----RSAKVRiAVFSQH-----HVDGL--DLS 585
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRwngtPLAEQR-DEPHENilylgHLPGLkpELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 586 SNPLLYMMRCFPGVPEQKLRAHLGSFGVTGnLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVeALIQ 665
Cdd:TIGR01189 90 ALENLHFWAAIHGGAQRTIEDALAAVGLTG-FEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV-ALLA 167
|
170
....*....|....*...
gi 743842931 666 GLV---LFQGGI-LMVSH 679
Cdd:TIGR01189 168 GLLrahLARGGIvLLTTH 185
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
515-682 |
6.48e-17 |
|
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: 84.60 E-value: 6.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 515 YPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKVRIAVFSQHHVdgLDLSSNPL----- 589
Cdd:TIGR03719 14 VPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQ--LDPTKTVRenvee 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 590 --------------LYMMRCFPGVPEQKLRA----------HLGSFGVTGNL-----AL------QPMYTLSGGQKSRVA 634
Cdd:TIGR03719 92 gvaeikdaldrfneISAKYAEPDADFDKLAAeqaelqeiidAADAWDLDSQLeiamdALrcppwdADVTKLSGGERRRVA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 743842931 635 FAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVLFQGGILMVSHDEH 682
Cdd:TIGR03719 172 LCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRY 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
523-699 |
7.82e-17 |
|
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: 79.86 E-value: 7.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 523 KNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF----------RSAKVRIAVFSQHhvDGLD--LSSNPLL 590
Cdd:cd03263 19 DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYingysirtdrKAARQSLGYCPQF--DALFdeLTVREHL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 591 YMMRCFPGVPEQKLRA----HLGSFGVTGnLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLD-------LDA 659
Cdd:cd03263 97 RFYARLKGLPKSEIKEevelLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDpasrraiWDL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 743842931 660 VEALIQGLvlfqgGILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:cd03263 176 ILEVRKGR-----SIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
523-700 |
8.17e-17 |
|
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: 80.45 E-value: 8.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 523 KNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTV----FRSAKVRI-------AVFSQHHVDGLDLSSNPLLY 591
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvagLVPWKRRKkflrrigVVFGQKTQLWWDLPVIDSFY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 592 MMRCFPGVPE---QKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLV 668
Cdd:cd03267 118 LLAAIYDLPParfKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLK 197
|
170 180 190
....*....|....*....|....*....|....*.
gi 743842931 669 LF----QGGILMVSHDEHLISGSVDELWVVSQGKVT 700
Cdd:cd03267 198 EYnrerGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
323-430 |
1.09e-16 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 83.79 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 323 SILAGLSFSPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPKTFIVVSHAREFLN 402
Cdd:PRK15064 420 GTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVS 499
|
90 100
....*....|....*....|....*...
gi 743842931 403 TVVTDILHLQGQKLTAYKGDYDTFERTR 430
Cdd:PRK15064 500 SLATRIIEITPDGVVDFSGTYEEYLRSQ 527
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
183-408 |
1.31e-16 |
|
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: 79.18 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 183 SVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMA-LHAIDGiprnCQILhVEQEVVGDDTSALQcVLNSDIER-- 259
Cdd:cd03268 9 TYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILgLIKPDS----GEIT-FDGKSYQKNIEALR-RIGALIEApg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 260 ---TRLLEEEVRLHAQQRDldfedaagngkgdqigaINKDAISQRLEEIykrlelidaysaearaasilaGLSFSPemqK 336
Cdd:cd03268 83 fypNLTARENLRLLARLLG-----------------IRKKRIDEVLDVV---------------------GLKDSA---K 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743842931 337 KATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPK---TFIVVSHAREFLNTVVTDI 408
Cdd:cd03268 122 KKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDqgiTVLISSHLLSEIQKVADRI 196
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
186-396 |
1.37e-16 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 79.72 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 186 GRDLIVDGsVTLSF--GRHYGLVGRNGTGKTTFLRYMA--LHA------IDGIPrncqilhveqeVVGDDTSALQCV--- 252
Cdd:COG1131 11 GDKTALDG-VSLTVepGEIFGLLGPNGAGKTTTIRMLLglLRPtsgevrVLGED-----------VARDPAEVRRRIgyv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 253 ---LNSDIERTrlLEEEVRLHAQQRDLDFEDAAgngkgdqigainkdaisQRLEEIYKRLELIDAysaearaasilagls 329
Cdd:COG1131 79 pqePALYPDLT--VRENLRFFARLYGLPRKEAR-----------------ERIDELLELFGLTDA--------------- 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 330 fspemQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKW---PKTFIVVSH 396
Cdd:COG1131 125 -----ADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaaeGKTVLLSTH 189
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
522-700 |
1.85e-16 |
|
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: 79.11 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 522 FKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKVR----IAVFSQHHVDGLDlssNplLYMMRCFP 597
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSsllgLGGGFNPELTGRE---N--IYLNGRLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 598 GVPEQKLRAHLG---SFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEpsnhldLDAV---------EALIQ 665
Cdd:cd03220 113 GLSRKEIDEKIDeiiEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE------VLAVgdaafqekcQRRLR 186
|
170 180 190
....*....|....*....|....*....|....*
gi 743842931 666 GLVLFQGGILMVSHDEHLISGSVDELWVVSQGKVT 700
Cdd:cd03220 187 ELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
528-699 |
1.89e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 79.77 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 528 GIDLDSR----IAMVGPNGIGKSTILKLIAGELQPTSGTVF------------RSAKVRiAVFSQHHVDGLDLSSNPL-- 589
Cdd:COG4559 19 DVSLTLRpgelTAIIGPNGAGKSTLLKLLTGELTPSSGEVRlngrplaawspwELARRR-AVLPQHSSLAFPFTVEEVva 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 590 --LYMMRCFPGVPEQKLRAHLGSFGVTGnLALQPMYTLSGGQKSRVAFAKI-------TFKKPHIILLDEPSNHLDL--- 657
Cdd:COG4559 98 lgRAPHGSSAAQDRQIVREALALVGLAH-LAGRSYQTLSGGEQQRVQLARVlaqlwepVDGGPRWLFLDEPTSALDLahq 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 743842931 658 DAVEALIQGLVLFQGGILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:COG4559 177 HAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRL 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
340-684 |
2.06e-16 |
|
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: 82.91 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 340 KTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLH---AVLWLESYLVKWPKTFIVVSHAREFLNTVvTDILHLqgqkl 416
Cdd:COG1245 211 SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYqrlNVARLIRELAEEGKYVLVVEHDLAILDYL-ADYVHI----- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 417 tAY--KGDYDTFErtreeQIKNQRKAIeaNEksrahmqtFIDkfrynakraslvqsrikaldrlGHM-DEIVNDPDYKFE 493
Cdd:COG1245 285 -LYgePGVYGVVS-----KPKSVRVGI--NQ--------YLD----------------------GYLpEENVRIRDEPIE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 494 F---PTPDDRPGAPIISFSDASFGYPGgplmfknlnFGIDLDS-------RIAMVGPNGIGKSTILKLIAGELQPTSGTV 563
Cdd:COG1245 327 FevhAPRREKEEETLVEYPDLTKSYGG---------FSLEVEGgeiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEV 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 564 frSAKVRIAVFSQhhvdgldlssnpllYMMRCFPGVPEQKLRAHLGS-FG-------VTGNLALQPMY-----TLSGGQK 630
Cdd:COG1245 398 --DEDLKISYKPQ--------------YISPDYDGTVEEFLRSANTDdFGssyykteIIKPLGLEKLLdknvkDLSGGEL 461
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 631 SRVAFAKITFKKPHIILLDEPSNHLDLD---AVEALIQGLVLFQG-GILMVSHDEHLI 684
Cdd:COG1245 462 QRVAIAACLSRDADLYLLDEPSAHLDVEqrlAVAKAIRRFAENRGkTAMVVDHDIYLI 519
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
517-680 |
2.08e-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: 78.72 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 517 GGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDLSSNPL----LYM 592
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIL--------------IDGRDVTGVPPerrnIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 593 M----RCFP---------------GVPEQKLRAH----LGSFGVTGNLALQPmYTLSGGQKSRVAFAKITFKKPHIILLD 649
Cdd:cd03259 77 VfqdyALFPhltvaeniafglklrGVPKAEIRARvrelLELVGLEGLLNRYP-HELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190
....*....|....*....|....*....|....*
gi 743842931 650 EPSNHLDLDAVEAL---IQGLVLFQG-GILMVSHD 680
Cdd:cd03259 156 EPLSALDAKLREELreeLKELQRELGiTTIYVTHD 190
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
466-702 |
2.36e-16 |
|
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: 82.87 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 466 SLVQSRiKALDRLGHMDEIVNDPDYKFEFPTPDDRpgapiISFSDASFGYPGG--PLmFKNLNFGIDLDSRIAMVGPNGI 543
Cdd:COG4618 297 QFVSAR-QAYRRLNELLAAVPAEPERMPLPRPKGR-----LSVENLTVVPPGSkrPI-LRGVSFSLEPGEVLGVIGPSGS 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 544 GKSTILKLIAGELQPTSGtvfrsaKVRIavfsqhhvDGLDLSS---------------NPLLymmrcFPG-VPE------ 601
Cdd:COG4618 370 GKSTLARLLVGVWPPTAG------SVRL--------DGADLSQwdreelgrhigylpqDVEL-----FDGtIAEniarfg 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 602 -----------QKLRAH-------------LGSFGVTgnlalqpmytLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDL 657
Cdd:COG4618 431 dadpekvvaaaKLAGVHemilrlpdgydtrIGEGGAR----------LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD 500
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 743842931 658 DAVEALIQGLVLF--QGG-ILMVSHDEHLISgSVDELWVVSQGKVTPF 702
Cdd:COG4618 501 EGEAALAAAIRALkaRGAtVVVITHRPSLLA-AVDKLLVLRDGRVQAF 547
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
506-706 |
2.47e-16 |
|
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: 79.12 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGP--LMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLD 583
Cdd:cd03249 1 IEFKNVSFRYPSRPdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIL--------------LDGVD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 584 LSSNPLlymmrcfpgvpeQKLRAHLG-----------------SFG-------------------------------VTG 615
Cdd:cd03249 67 IRDLNL------------RWLRSQIGlvsqepvlfdgtiaeniRYGkpdatdeeveeaakkanihdfimslpdgydtLVG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 616 NLALQpmytLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDaVEALIQ-GLVLFQGG--ILMVSHDEHLISGSvDELW 692
Cdd:cd03249 135 ERGSQ----LSGGQKQRIAIARALLRNPKILLLDEATSALDAE-SEKLVQeALDRAMKGrtTIVIAHRLSTIRNA-DLIA 208
|
250
....*....|....
gi 743842931 693 VVSQGKVTPfHGTF 706
Cdd:cd03249 209 VLQNGQVVE-QGTH 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
523-699 |
2.73e-16 |
|
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: 78.63 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 523 KNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTV-FRSAKV------RIA------------VFSQHHVD--- 580
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlFDGEDItglpphEIArlgigrtfqiprLFPELTVLenv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 581 --GLDLSSNPLLYMMRCFPGVPEQKLRAH--LGSFGVTGnLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPS---N 653
Cdd:cd03219 97 mvAAQARTGSGLLLARARREEREARERAEelLERVGLAD-LADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAaglN 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 743842931 654 HLDLDAVEALIQGLVLFQGGILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:cd03219 176 PEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
175-396 |
2.97e-16 |
|
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: 78.93 E-value: 2.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRymalhAIDGI--PRNCQILhveqeVVGDDTSALqcv 252
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLR-----ALAGLlkPSSGEVL-----LDGRDLASL--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 253 lnSDIERTRLLeeevrlhA---QQRDLDF----EDAAGNGKGDQIGAINKDaiSQRLEEIykrlelidaysaeARAASIL 325
Cdd:COG1120 69 --SRRELARRI-------AyvpQEPPAPFgltvRELVALGRYPHLGLFGRP--SAEDREA-------------VEEALER 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743842931 326 AGLSfspEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDL-HAVLWLEsyLVK-----WPKTFIVVSH 396
Cdd:COG1120 125 TGLE---HLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLaHQLEVLE--LLRrlareRGRTVVMVLH 196
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
515-656 |
3.07e-16 |
|
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: 78.76 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 515 YPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF--------------RSAKVRIAVFSQHH-- 578
Cdd:cd03256 10 YPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLidgtdinklkgkalRQLRRQIGMIFQQFnl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 579 VDGLD---------LSSNPLLY-MMRCFPgvPEQKLRAH--LGSFGVTGnLALQPMYTLSGGQKSRVAFAKITFKKPHII 646
Cdd:cd03256 90 IERLSvlenvlsgrLGRRSTWRsLFGLFP--KEEKQRALaaLERVGLLD-KAYQRADQLSGGQQQRVAIARALMQQPKLI 166
|
170
....*....|
gi 743842931 647 LLDEPSNHLD 656
Cdd:cd03256 167 LADEPVASLD 176
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
506-683 |
4.20e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 76.42 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGeLQP-TSGTVFRSAKVRIAVFSQHhvdgldl 584
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPwGSGRIGMPEGEDLLFLPQR------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 585 ssnPllYMmrcfpgvpeqklrahlgsfgVTGNLALQPMY----TLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAV 660
Cdd:cd03223 73 ---P--YL--------------------PLGTLREQLIYpwddVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180
....*....|....*....|...
gi 743842931 661 EALIQGLVLFQGGILMVSHDEHL 683
Cdd:cd03223 128 DRLYQLLKELGITVISVGHRPSL 150
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
506-701 |
4.98e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 77.87 E-value: 4.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGPLMFknlNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF---------RSAKVRIAVFSQ 576
Cdd:COG3840 2 LRLDDLTYRYGDFPLRF---DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILwngqdltalPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 577 -----HHVD-----GLDLSsnpllymmrcfPGV---PEQKLRAH--LGSFGVTGNLALQPmYTLSGGQKSRVAFAK-ITF 640
Cdd:COG3840 79 ennlfPHLTvaqniGLGLR-----------PGLkltAEQRAQVEqaLERVGLAGLLDRLP-GQLSGGQRQRVALARcLVR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 641 KKPhIILLDEPSNHLD-------LDAVEALIQGLvlfQGGILMVSHDEHLISGSVDELWVVSQGKVTP 701
Cdd:COG3840 147 KRP-ILLLDEPFSALDpalrqemLDLVDELCRER---GLTVLMVTHDPEDAARIADRVLLVADGRIAA 210
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
506-699 |
5.06e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 82.08 E-value: 5.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGP--LMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAkVRIAVFSQH--HVDG 581
Cdd:TIGR00958 479 IEFQDVSFSYPNRPdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDG-VPLVQYDHHylHRQV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 582 LDLSSNPLLY-----------MMRCfpgvPEQKLR-----AHLGSF------------GVTGNLalqpmytLSGGQKSRV 633
Cdd:TIGR00958 558 ALVGQEPVLFsgsvreniaygLTDT----PDEEIMaaakaANAHDFimefpngydtevGEKGSQ-------LSGGQKQRI 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743842931 634 AFAKITFKKPHIILLDEPSNHLDLdAVEALIQGLVLFQG-GILMVSHDEHLISGSvDELWVVSQGKV 699
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALDA-ECEQLLQESRSRASrTVLLIAHRLSTVERA-DQILVLKKGSV 691
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
506-699 |
7.02e-16 |
|
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: 77.21 E-value: 7.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGPLMFknlNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGT-------VFRSAKVRIAV---FS 575
Cdd:TIGR01277 1 LALDKVRYEYEHLPMEF---DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSikvndqsHTGLAPYQRPVsmlFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 576 QHHV-------DGLDLSSNPLLYMMrcfpGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHIILL 648
Cdd:TIGR01277 78 ENNLfahltvrQNIGLGLHPGLKLN----AEQQEKVVDAAQQVGIADYLDRLPE-QLSGGQRQRVALARCLVRPNPILLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 743842931 649 DEPSNHLD-LDAVE--ALIQGLVLFQG-GILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:TIGR01277 153 DEPFSALDpLLREEmlALVKQLCSERQrTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
174-396 |
7.95e-16 |
|
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: 77.93 E-value: 7.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 174 DIHLENFNISVGGRdLIVDG-SVTLSFGRHYGLVGRNGTGKTTFLRYMA----------------LHAIDGIPRNCQILH 236
Cdd:TIGR03873 1 GLRLSRVSWSAGGR-LIVDGvDVTAPPGSLTGLLGPNGSGKSTLLRLLAgalrpdagtvdlagvdLHGLSRRARARRVAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 237 VEQEV-VGDDTSALQCVLNSDIERTRLLeeevrlhaqqrdldfedaAGNGKGDQigainkdaisqrleeiykrlELIDAY 315
Cdd:TIGR03873 80 VEQDSdTAVPLTVRDVVALGRIPHRSLW------------------AGDSPHDA--------------------AVVDRA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 316 SAEARAASiLAGLSFSpemqkkatkTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHA---VLWLESYLVKWPKTFI 392
Cdd:TIGR03873 122 LARTELSH-LADRDMS---------TLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAqleTLALVRELAATGVTVV 191
|
....
gi 743842931 393 VVSH 396
Cdd:TIGR03873 192 AALH 195
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
506-699 |
1.75e-15 |
|
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: 75.99 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGPLMFknlNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF----------RSAKVRIAVFS 575
Cdd:cd03298 1 VRLDKIRFSYGEQPMHF---DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLingvdvtaapPADRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 576 QH----HVD---GLDLSSNPLLYMMrcfpGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHIILL 648
Cdd:cd03298 78 ENnlfaHLTveqNVGLGLSPGLKLT----AEDRQAIEVALARVGLAGLEKRLPG-ELSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 649 DEPSNHLDlDAVEALIQGLVL-----FQGGILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:cd03298 153 DEPFAALD-PALRAEMLDLVLdlhaeTKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
177-414 |
1.79e-15 |
|
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: 75.97 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 177 LENFNISVGGRDLIVDGSVTLSF--GRHYGLVGRNGTGKTTFLRYMA--LHA------IDGIPRNCQILHVEQEVVGddt 246
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIkkGEFVLIVGPNGSGKSTLLRLLNglLGPtsgevlVDGKDLTKLSLKELRRKVG--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 247 SALQcvlNSD---IERTrlLEEEVRLHAQQRDLDfedaagngkgdqigainKDAISQRLEEIYKRLELIDaysaearaas 323
Cdd:cd03225 79 LVFQ---NPDdqfFGPT--VEEEVAFGLENLGLP-----------------EEEIEERVEEALELVGLEG---------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 324 ilaglsfspeMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWP---KTFIVVSHAREF 400
Cdd:cd03225 127 ----------LRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKaegKTIIIVTHDLDL 196
|
250
....*....|....*
gi 743842931 401 LNTVVTDILHL-QGQ 414
Cdd:cd03225 197 LLELADRVIVLeDGK 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
522-684 |
2.06e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.27 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 522 FKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAkvRIAVFsqhhvdgLDLSS--NP----------- 588
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG--RVSAL-------LELGAgfHPeltgreniyln 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 589 -LLYmmrcfpGVPEQKLRAH---------LGSFgvtgnlALQPMYTLSGGQKSRVAFAKITFKKPHIILLDepsnhldld 658
Cdd:COG1134 113 gRLL------GLSRKEIDEKfdeivefaeLGDF------IDQPVKTYSSGMRARLAFAVATAVDPDILLVD--------- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 743842931 659 avEALIQGLVLFQ--------------GGILMVSHDEHLI 684
Cdd:COG1134 172 --EVLAVGDAAFQkkclarirelresgRTVIFVSHSMGAV 209
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
503-700 |
2.17e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 78.73 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 503 APIISFSDASFGYpGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVfrsakvriavfsqhHVDGL 582
Cdd:PRK09536 1 MPMIDVSDLSVEF-GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTV--------------LVAGD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 583 DLSSNPLLYMMRCFPGVPEQ-------KLRA--------HLGSFGVTGN-----------------LALQPMYTLSGGQK 630
Cdd:PRK09536 66 DVEALSARAASRRVASVPQDtslsfefDVRQvvemgrtpHRSRFDTWTEtdraaveramertgvaqFADRPVTSLSGGER 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743842931 631 SRVAFAKITFKKPHIILLDEPSNHLDLD-AVE--ALIQGLVLFQGGILMVSHDEHLISGSVDELWVVSQGKVT 700
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDINhQVRtlELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVR 218
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
496-667 |
2.34e-15 |
|
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: 75.97 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 496 TPDDRPGapIISFSDASFGYPGGP--LMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKV---- 569
Cdd:cd03248 4 APDHLKG--IVKFQNVTFAYPTRPdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPisqy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 570 -------RIAVFSQHHV-DGLDLSSNPLLYMMRC-FPGVPEQKLRAHLGSF------------GVTGNLalqpmytLSGG 628
Cdd:cd03248 82 ehkylhsKVSLVGQEPVlFARSLQDNIAYGLQSCsFECVKEAAQKAHAHSFiselasgydtevGEKGSQ-------LSGG 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 743842931 629 QKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGL 667
Cdd:cd03248 155 QKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQAL 193
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
506-700 |
2.55e-15 |
|
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: 76.38 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGPL---MFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTV--------------FRsAK 568
Cdd:COG1124 2 LEVRNLSVSYGQGGRrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVtfdgrpvtrrrrkaFR-RR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 569 VRIaVFsQHHvdglDLSSNPLLYM-------MRCFpGVPEQKLRAH--LGSFGVTGNLALQPMYTLSGGQKSRVAFAKIT 639
Cdd:COG1124 81 VQM-VF-QDP----YASLHPRHTVdrilaepLRIH-GLPDREERIAelLEQVGLPPSFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 640 FKKPHIILLDEPSNHLD-------LDAVEALIQ--GLvlfqgGILMVSHDEHLISGSVDELWVVSQGKVT 700
Cdd:COG1124 154 ILEPELLLLDEPTSALDvsvqaeiLNLLKDLREerGL-----TYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
175-418 |
4.21e-15 |
|
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: 75.06 E-value: 4.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDGsVTLSF--GRHYGLVGRNGTGKTTFLRymalhAIDGIprncqILHVEQEVVgddtsalqcV 252
Cdd:COG1122 1 IELENLSFSYPGGTPALDD-VSLSIekGEFVAIIGPNGSGKSTLLR-----LLNGL-----LKPTSGEVL---------V 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 253 LNSDIERTRLleEEVRLHAQqrdLDFEDAAgngkgDQIgainkdaISQR-LEEIykrlelidAYS----------AEARA 321
Cdd:COG1122 61 DGKDITKKNL--RELRRKVG---LVFQNPD-----DQL-------FAPTvEEDV--------AFGpenlglpreeIRERV 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 322 ASILA--GLSfspEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWP---KTFIVVSH 396
Cdd:COG1122 116 EEALElvGLE---HLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNkegKTVIIVTH 192
|
250 260
....*....|....*....|..
gi 743842931 397 AREFLNTVVTDILHLQGQKLTA 418
Cdd:COG1122 193 DLDLVAELADRVIVLDDGRIVA 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
505-705 |
5.17e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 76.04 E-value: 5.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 505 IISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAK-----------VRIAV 573
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkglmkLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 574 -----------FSQHHVDglDLSSNPLLYmmrcfpGVPEQKLRAH----LGSFGVTgNLALQPMYTLSGGQKSRVAFAKI 638
Cdd:PRK13636 85 gmvfqdpdnqlFSASVYQ--DVSFGAVNL------KLPEDEVRKRvdnaLKRTGIE-HLKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743842931 639 TFKKPHIILLDEPSNHLDLDAVEALIQGLVLFQGG----ILMVSHDEHLISGSVDELWVVSQGKVTpFHGT 705
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElgltIIIATHDIDIVPLYCDNVFVMKEGRVI-LQGN 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
528-699 |
6.78e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.19 E-value: 6.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 528 GIDLDSR----IAMVGPNGIGKSTILKLIAGELQPTSGTVF------------RSAKVRiAVFSQHH----------VDG 581
Cdd:PRK13548 20 DVSLTLRpgevVAILGPNGAGKSTLLRALSGELSPDSGEVRlngrpladwspaELARRR-AVLPQHSslsfpftveeVVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 582 LDLSSNPLLYmmRCFPGVPEQKLRAhlgsFGVTGnLALQPMYTLSGGQKSRVAFAKI------TFKKPHIILLDEPSNHL 655
Cdd:PRK13548 99 MGRAPHGLSR--AEDDALVAAALAQ----VDLAH-LAGRDYPQLSGGEQQRVQLARVlaqlwePDGPPRWLLLDEPTSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 743842931 656 DL---DAVEALIQGLVLFQG-GILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:PRK13548 172 DLahqHHVLRLARQLAHERGlAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
506-665 |
9.05e-15 |
|
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: 74.19 E-value: 9.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPG-GPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDL 584
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRIL--------------IDGHDV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 585 SsnpllymmrcfpGVPEQKLRAHLG-----SFGVTGNLALQPMY------------------------------------ 623
Cdd:cd03251 67 R------------DYTLASLRRQIGlvsqdVFLFNDTVAENIAYgrpgatreeveeaaraanahefimelpegydtvige 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 743842931 624 ---TLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAvEALIQ 665
Cdd:cd03251 135 rgvKLSGGQRQRIAIARALLKDPPILILDEATSALDTES-ERLVQ 178
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
137-373 |
9.07e-15 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 77.79 E-value: 9.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 137 QREAQYQIHLAEMEAV-RAGMPVACVTHDGGGGGPnVKDIHLENFNISVG--GRDLIVDG-SVTLSFGRHYGLVGRNGTG 212
Cdd:TIGR02868 295 QQLTRVRAAAERIVEVlDAAGPVAEGSAPAAGAVG-LGKPTLELRDLSAGypGAPPVLDGvSLDLPPGERVAILGPSGSG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 213 KTTFLRYMAlHAIDgiPRncqilhvEQEVVGDDTSALQCVLNSDIERTRLLEEEVRL-HAQQRD---LDFEDAAGngkgd 288
Cdd:TIGR02868 374 KSTLLATLA-GLLD--PL-------QGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLfDTTVREnlrLARPDATD----- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 289 qigainkdaisqrlEEIYKRLElidaysaEARAASILAGLS--FSPEMQKKAtKTFSGGWRMRIALARALFIEPDILLLD 366
Cdd:TIGR02868 439 --------------EELWAALE-------RVGLADWLRALPdgLDTVLGEGG-ARLSGGERQRLALARALLADAPILLLD 496
|
....*..
gi 743842931 367 EPTNHLD 373
Cdd:TIGR02868 497 EPTEHLD 503
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
177-396 |
1.08e-14 |
|
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: 72.85 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 177 LENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRymalhAIDGI--PRNCQILhveqeVVGDDTSALqcvln 254
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLK-----TLAGLlkPSSGEIL-----LDGKDLASL----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 255 SDIERTRLLeeevrlhaqqrdldfedaagngkgdqigAInkdaISQRLEeiykRLELIDaysaearaasiLAGLSFSpem 334
Cdd:cd03214 67 SPKELARKI----------------------------AY----VPQALE----LLGLAH-----------LADRPFN--- 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 335 qkkatkTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKW----PKTFIVVSH 396
Cdd:cd03214 97 ------ELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLarerGKTVVMVLH 156
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
169-427 |
1.18e-14 |
|
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: 77.28 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 169 GPNVKDIHLENFNIS--VGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMAlhaidgiprncqilhvEQEVvgDDT 246
Cdd:TIGR03719 315 GPRLGDKVIEAENLTkaFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMIT----------------GQEQ--PDS 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 247 SALQcvlnsdiertrlLEEEVRLHA--QQRD-LDfedaagngkgdqigaINKDAisqrLEEIYKRLELIDAYSAEARAAS 323
Cdd:TIGR03719 377 GTIE------------IGETVKLAYvdQSRDaLD---------------PNKTV----WEEISGGLDIIKLGKREIPSRA 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 324 ILAGLSFSPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPKTFIVVSHAREFLNT 403
Cdd:TIGR03719 426 YVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDR 505
|
250 260
....*....|....*....|....*
gi 743842931 404 VVTDILHLQGQ-KLTAYKGDYDTFE 427
Cdd:TIGR03719 506 IATHILAFEGDsHVEWFEGNFSEYE 530
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
517-692 |
1.49e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.91 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 517 GGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF----RSAKVRIAVFSQ----HHVDGL--DLSS 586
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwqgePIRRQRDEYHQDllylGHQPGIktELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 587 --NpLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALqPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALI 664
Cdd:PRK13538 92 leN-LRFYQRLHGPGDDEALWEALAQVGLAGFEDV-PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLE 169
|
170 180 190
....*....|....*....|....*....|....*
gi 743842931 665 QglvLF-----QGGI-LMVSH-DEHLISGSVDELW 692
Cdd:PRK13538 170 A---LLaqhaeQGGMvILTTHqDLPVASDKVRKLR 201
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
505-699 |
1.80e-14 |
|
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: 73.31 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 505 IISFSDASFGYPGGPLMFKNLNfGIDLD----SRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKV----------- 569
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALD-DVSFSikkgETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllklsrrlrki 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 570 ---RIAVFSQhhvdglD-LSS-NPL----------LYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMY--TLSGGQKSR 632
Cdd:cd03257 80 rrkEIQMVFQ------DpMSSlNPRmtigeqiaepLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYphELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743842931 633 VAFAKITFKKPHIILLDEPSNHLDLdAVEALIQGLVL-----FQGGILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDV-SVQAQILDLLKklqeeLGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
175-699 |
1.93e-14 |
|
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: 76.76 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRymALHAIDGI-PRNCQILH----------VE-QEVV 242
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMH--VLRGMDQYePTSGRIIYhvalcekcgyVErPSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 243 GDDTSALQCVLN---------SDIERTRL-------LEEEVRLHAQQRDLDFEDAAGNgkgdQIGAINKDAIsqrleeiY 306
Cdd:TIGR03269 79 GEPCPVCGGTLEpeevdfwnlSDKLRRRIrkriaimLQRTFALYGDDTVLDNVLEALE----EIGYEGKEAV-------G 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 307 KRLELIDAYSAEARAASIlaglsfspemqkkaTKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVK 386
Cdd:TIGR03269 148 RAVDLIEMVQLSHRITHI--------------ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 387 WPK----TFIVVSHAREFLNTVVTDILHLQGQKLTAyKGDYDTFERTREEQIKNQRKAIEANEKSRahmqtfIDKFRYNA 462
Cdd:TIGR03269 214 AVKasgiSMVLTSHWPEVIEDLSDKAIWLENGEIKE-EGTPDEVVAVFMEGVSEVEKECEVEVGEP------IIKVRNVS 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 463 KR-ASLVQSRIKALDRlghmdeivndpdykfefptpddrpgapiISFSdasfgypggplMFKNLNFGIdldsriamVGPN 541
Cdd:TIGR03269 287 KRyISVDRGVVKAVDN----------------------------VSLE-----------VKEGEIFGI--------VGTS 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 542 GIGKSTILKLIAGELQPTSGTV-FR-----------------SAKVRIAVFSQH-----HVD---------GLDLSSNpl 589
Cdd:TIGR03269 320 GAGKTTLSKIIAGVLEPTSGEVnVRvgdewvdmtkpgpdgrgRAKRYIGILHQEydlypHRTvldnlteaiGLELPDE-- 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 590 LYMMRCF-----PGVPEQKLRAHLGSFgvtgnlalqpMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLD----LDAV 660
Cdd:TIGR03269 398 LARMKAVitlkmVGFDEEKAEEILDKY----------PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVT 467
|
570 580 590
....*....|....*....|....*....|....*....
gi 743842931 661 EALIQGLVLFQGGILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:TIGR03269 468 HSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
475-684 |
2.04e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 76.77 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 475 LDRLGHMDEIVNDPDYKFEFPTPDDRPGAPIISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAG 554
Cdd:COG4178 332 VDRLAGFEEALEAADALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 555 eLQP-TSGTVFRSAKVRIAVFSQHhvdgldlssnPllYM----MR---CFPG----VPEQKLRAHLGSFGVtGNLALQP- 621
Cdd:COG4178 412 -LWPyGSGRIARPAGARVLFLPQR----------P--YLplgtLRealLYPAtaeaFSDAELREALEAVGL-GHLAERLd 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 622 -----MYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLV--LFQGGILMVSHDEHLI 684
Cdd:COG4178 478 eeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLReeLPGTTVISVGHRSTLA 547
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
182-478 |
2.47e-14 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 76.75 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 182 ISVGGRDLIVDGSVTLSF--GRHYGLVGRNGTGKTTFLRYMA-----LHAIDGIPRNCQILHVEQ---EVVGDDTSALQc 251
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLvpGSRIGLLGRNGAGKSTLIKLLAgelapVSGEIGLAKGIKLGYFAQhqlEFLRADESPLQ- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 252 vlnsdiERTRLLEEEvrLHAQQRDLdfedaagngkgdqigainkdaisqrleeiykrlelidaysaearaasiLAGLSFS 331
Cdd:PRK10636 397 ------HLARLAPQE--LEQKLRDY------------------------------------------------LGGFGFQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 332 PEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPKTFIVVSHAREFLNTVVTDILHL 411
Cdd:PRK10636 421 GDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLV 500
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 412 QGQKLTAYKGDYDTFERTREEQIKNQRKAIEANEKSRAH-MQTFIDKFRYNAKRASLVQSRIKALDRL 478
Cdd:PRK10636 501 HDGKVEPFDGDLEDYQQWLSDVQKQENQTDEAPKENNANsAQARKDQKRREAELRTQTQPLRKEIARL 568
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
504-699 |
2.78e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 73.49 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 504 PIISFSDASFGYPGG-PLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGL 582
Cdd:PRK13632 6 VMIKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIK--------------IDGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 583 DLSSNPLLYmMRCFPG---------------------------VPEQKLRAHLGSF----GVTGNLALQPMYtLSGGQKS 631
Cdd:PRK13632 72 TISKENLKE-IRKKIGiifqnpdnqfigatveddiafglenkkVPPKKMKDIIDDLakkvGMEDYLDKEPQN-LSGGQKQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743842931 632 RVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVLFQGG----ILMVSHD--EHLISgsvDELWVVSQGKV 699
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTrkktLISITHDmdEAILA---DKVIVFSEGKL 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
504-700 |
3.09e-14 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 73.36 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 504 PIISFSDASFGYPGG---PLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKV-------RIAV 573
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 574 FsQHH--------VD----GLDLSsnpllymmrcfpGVP--EQKLRAH--LGSFGVTGnLALQPMYTLSGGQKSRVAFAK 637
Cdd:COG4525 82 F-QKDallpwlnvLDnvafGLRLR------------GVPkaERRARAEelLALVGLAD-FARRRIWQLSGGMRQRVGIAR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743842931 638 ITFKKPHIILLDEPSNHLDLDAVEAlIQGLVL-----FQGGILMVSHD--EHLISGSvdELWVVS--QGKVT 700
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQ-MQELLLdvwqrTGKGVFLITHSveEALFLAT--RLVVMSpgPGRIV 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
503-699 |
3.93e-14 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 75.71 E-value: 3.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 503 APIISFSDASFGYPGGPLM-FKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGeLQPTSGTVFRSAKV------------ 569
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPaVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRISGEVLLdgrdllelseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 570 ---RIAVFSQHHVDGLDLSS--NPLLYMMRCFpGVPEQKLRAH----LGSFGVTGNLALQPmYTLSGGQKSRVAFAKITF 640
Cdd:COG1123 81 rgrRIGMVFQDPMTQLNPVTvgDQIAEALENL-GLSRAEARARvlelLEAVGLERRLDRYP-HQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743842931 641 KKPHIILLDEPSNHLDLDA---VEALIQGLVLFQG-GILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTqaeILDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
535-693 |
4.23e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 72.44 E-value: 4.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 535 IAMVGPNGIGKSTILKLIAGELQPTSGTVfrsakvriavfsqhHVDGLDLSSNPlLYMMRCFPGVPEQKLRAHLGSFG-- 612
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDI--------------EIELDTVSYKP-QYIKADYEGTVRDLLSSITKDFYth 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 613 ------VTGNLALQPMY-----TLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLD---AVEALIQGLVLF-QGGILMV 677
Cdd:cd03237 93 pyfkteIAKPLQIEQILdrevpELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlMASKVIRRFAENnEKTAFVV 172
|
170
....*....|....*.
gi 743842931 678 SHDEHLISGSVDELWV 693
Cdd:cd03237 173 EHDIIMIDYLADRLIV 188
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
517-688 |
4.55e-14 |
|
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: 71.37 E-value: 4.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 517 GGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTV--------FRSAKVRIAVFSQHHVDGLD--LSS 586
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVllnggpldFQRDSIARGLLYLGHAPGIKttLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 587 NPLLYMMRCFPGVpEQKLRAhLGSFGVTGnLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQG 666
Cdd:cd03231 91 LENLRFWHADHSD-EQVEEA-LARVGLNG-FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170 180
....*....|....*....|....*
gi 743842931 667 LV--LFQGG-ILMVSHDEHLISGSV 688
Cdd:cd03231 168 MAghCARGGmVVLTTHQDLGLSEAG 192
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
175-373 |
4.66e-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: 71.84 E-value: 4.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDGSVTLSFGRhYGLVGRNGTGKTTFLRYMAlhaidGI--PRNCQILHVEQEVVGDDTSAlqcv 252
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILA-----TLtpPSSGTIRIDGQDVLKQPQKL---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 253 lnsdieRTRL--LEEEVRLHAQQRDLDFEDAAGNGKGdqigaINKDAISQRLEEIYKRLELIDAYsaearaasilaglsf 330
Cdd:cd03264 71 ------RRRIgyLPQEFGVYPNFTVREFLDYIAWLKG-----IPSKEVKARVDEVLELVNLGDRA--------------- 124
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 743842931 331 spemqKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:cd03264 125 -----KKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
512-700 |
5.33e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 72.35 E-value: 5.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 512 SFGYpGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFR--------SAKV---RIAVFSQHHVD 580
Cdd:PRK11231 9 TVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLgdkpismlSSRQlarRLALLPQHHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 581 GLDLSSNPLLYMMRC----FPGVPEQKLRAHLG-SFGVTG--NLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSN 653
Cdd:PRK11231 88 PEGITVRELVAYGRSpwlsLWGRLSAEDNARVNqAMEQTRinHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 743842931 654 HLDLD-AVE--ALIQglVLFQGG--ILMVSHDEHLISGSVDELWVVSQGKVT 700
Cdd:PRK11231 168 YLDINhQVElmRLMR--ELNTQGktVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
506-685 |
7.99e-14 |
|
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: 70.96 E-value: 7.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGPLM----FKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAkvRIAVFSQhhvdg 581
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsftLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQ----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 582 ldlssNPllYMMR-------CFpGVP------EQKLRA----------------HLGSFGVtgnlalqpmyTLSGGQKSR 632
Cdd:cd03250 74 -----EP--WIQNgtireniLF-GKPfdeeryEKVIKAcalepdleilpdgdltEIGEKGI----------NLSGGQKQR 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743842931 633 VAFAKITFKKPHIILLDEP--------SNHLdldaVEALIQGLVLFQGGILMVSHDEHLIS 685
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPlsavdahvGRHI----FENCILGLLLNNKTRILVTHQLQLLP 192
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
504-699 |
8.06e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.09 E-value: 8.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 504 PIISFSDASFGYPG-GPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavFSQHHVDGL 582
Cdd:PRK13648 6 SIIVFKNVSFQYQSdASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIF---------YNNQAITDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 583 DLssnpllymmrcfpgvpeQKLRAHLG-------------------SFGVTGNL------------ALQP--MY------ 623
Cdd:PRK13648 77 NF-----------------EKLRKHIGivfqnpdnqfvgsivkydvAFGLENHAvpydemhrrvseALKQvdMLeradye 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 624 --TLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVLFQGG----ILMVSHDEHLISGSvDELWVVSQG 697
Cdd:PRK13648 140 pnALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhnitIISITHDLSEAMEA-DHVIVMNKG 218
|
..
gi 743842931 698 KV 699
Cdd:PRK13648 219 TV 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
175-396 |
8.65e-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: 69.73 E-value: 8.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRdLIVDGsVTLSFGRH--YGLVGRNGTGKTTFLRYMA-LHAIDgiprncqilhvEQEVVgddtsalqc 251
Cdd:cd03230 1 IEVRNLSKRYGKK-TALDD-ISLTVEKGeiYGLLGPNGAGKTTLIKIILgLLKPD-----------SGEIK--------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 252 VLNSDIERTRlleEEVRLHaqqrdldfedaagngkgdqIGAInkdaisqrLEEIykrlelidaysaearaasilaglSFS 331
Cdd:cd03230 59 VLGKDIKKEP---EEVKRR-------------------IGYL--------PEEP-----------------------SLY 85
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 332 PEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESY---LVKWPKTFIVVSH 396
Cdd:cd03230 86 ENLTVRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELlreLKKEGKTILLSSH 153
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
528-679 |
1.23e-13 |
|
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: 68.99 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 528 GIDLDSR----IAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDLSsnpllymmrcfPGVPEQK 603
Cdd:cd03216 18 GVSLSVRrgevHALLGENGAGKSTLMKILSGLYKPDSGEIL--------------VDGKEVS-----------FASPRDA 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743842931 604 LRAhlgsfGVtgnlalQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVLF--QG-GILMVSH 679
Cdd:cd03216 73 RRA-----GI------AMVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLraQGvAVIFISH 140
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
506-704 |
1.26e-13 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 70.30 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGpLMFKNLNFGIDlDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVfrsakvriavfsqhHVDGLDLS 585
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTI--------------RIDGQDVL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 586 SNPllymmrcfpgvpeQKLRAHLG----SFGVTGNL------------------------------------ALQPMYTL 625
Cdd:cd03264 65 KQP-------------QKLRRRIGylpqEFGVYPNFtvrefldyiawlkgipskevkarvdevlelvnlgdrAKKKIGSL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 626 SGGQKSRVAFAKITFKKPHIILLDEPSNHLDLD---AVEALIQGLVlfQGGILMVS-HDEHLISGSVDELWVVSQGKVTp 701
Cdd:cd03264 132 SGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEeriRFRNLLSELG--EDRIVILStHIVEDVESLCNQVAVLNKGKLV- 208
|
...
gi 743842931 702 FHG 704
Cdd:cd03264 209 FEG 211
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
512-657 |
1.42e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.56 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 512 SFGYpGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTV---------FRSAKV--RIAVFSQHHVD 580
Cdd:PRK10253 14 TLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhYASKEVarRIGLLAQNATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 581 GLDLSSNPLLYMMRcFPGVP---------EQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEP 651
Cdd:PRK10253 93 PGDITVQELVARGR-YPHQPlftrwrkedEEAVTKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
....*.
gi 743842931 652 SNHLDL 657
Cdd:PRK10253 171 TTWLDI 176
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
472-702 |
1.50e-13 |
|
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: 73.92 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 472 IKALDRLGHMDEIVNDPDYKFEFPTPDDRpgapiISFSDASFGYPGG--PLMfKNLNFGIDLDSRIAMVGPNGIGKSTIL 549
Cdd:TIGR01842 288 RQAYKRLNELLANYPSRDPAMPLPEPEGH-----LSVENVTIVPPGGkkPTL-RGISFSLQAGEALAIIGPSGSGKSTLA 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 550 KLIAGELQPTSGtvfrsaKVRI--AVFSQHHVDGLDLSSNPLLYMMRCFPG------------VPEQKLRAHLGSFGVTG 615
Cdd:TIGR01842 362 RLIVGIWPPTSG------SVRLdgADLKQWDRETFGKHIGYLPQDVELFPGtvaeniarfgenADPEKIIEAAKLAGVHE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 616 NLALQPM-Y---------TLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVLF--QGGI-LMVSHDEH 682
Cdd:TIGR01842 436 LILRLPDgYdtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkaRGITvVVITHRPS 515
|
250 260
....*....|....*....|
gi 743842931 683 LIsGSVDELWVVSQGKVTPF 702
Cdd:TIGR01842 516 LL-GCVDKILVLQDGRIARF 534
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
506-710 |
1.54e-13 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 74.01 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKvRIAVFSQHHVDGL--D 583
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF-SLKDIDRHTLRQFinY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 584 LSSNPLLY--------MMRCFPGVPEQKLRAHLGSFGVTGNLALQPM----------YTLSGGQKSRVAFAKITFKKPHI 645
Cdd:TIGR01193 553 LPQEPYIFsgsilenlLLGAKENVSQDEIWAACEIAEIKDDIENMPLgyqtelseegSSISGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 646 ILLDEPSNHLDLDAVEALIQGLV-LFQGGILMVSHDEHlISGSVDELWVVSQGKV--TPFHGTFLDYK 710
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNLLnLQDKTIIFVAHRLS-VAKQSDKIIVLDHGKIieQGSHDELLDRN 699
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
506-702 |
1.66e-13 |
|
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: 70.13 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGY-PGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVfrsakvriavfsqhHVDGLDL 584
Cdd:cd03369 7 IEVENLSVRYaPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI--------------EIDGIDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 585 SSNPLLYMMRCFPGVPEQKLrahLGSFGVTGNLALQPMYT----------------LSGGQKSRVAFAKITFKKPHIILL 648
Cdd:cd03369 73 STIPLEDLRSSLTIIPQDPT---LFSGTIRSNLDPFDEYSdeeiygalrvsegglnLSQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743842931 649 DEPSNHLDLDAvEALIQGLV--LFQGG-ILMVSHDEHLISgSVDELWVVSQGKVTPF 702
Cdd:cd03369 150 DEATASIDYAT-DALIQKTIreEFTNStILTIAHRLRTII-DYDKILVMDAGEVKEY 204
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
506-699 |
1.81e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 71.40 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGY-PGGPLMFK---NLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSA-------------K 568
Cdd:PRK13641 3 IKFENVDYIYsPGTPMEKKgldNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 569 VRIAVFSQHHVDGLDLSSNPLLYMMRCFP---GVPEQKLRAH----LGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFK 641
Cdd:PRK13641 83 LRKKVSLVFQFPEAQLFENTVLKDVEFGPknfGFSEDEAKEKalkwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743842931 642 KPHIILLDEPSNHLDLDAVEALIQGLVLFQGG---ILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
506-679 |
1.84e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.17 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYpGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTV----------FRSAKVRIAVFS 575
Cdd:PRK13536 42 IDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItvlgvpvparARLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 576 QhhVDGLDLS---SNPLLYMMRCFpGVPEQKLRAHLGS---FGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLD 649
Cdd:PRK13536 121 Q--FDNLDLEftvRENLLVFGRYF-GMSTREIEAVIPSlleFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190
....*....|....*....|....*....|...
gi 743842931 650 EPSNHLDLDAVEALIQGL--VLFQG-GILMVSH 679
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLrsLLARGkTILLTTH 230
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
523-683 |
2.03e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 70.23 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 523 KNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTV-FR-------SAKVRIAVFSQ--------HHV----DGL 582
Cdd:PRK11629 26 HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDViFNgqpmsklSSAAKAELRNQklgfiyqfHHLlpdfTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 583 DLSSNPLLyMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDL---DA 659
Cdd:PRK11629 106 ENVAMPLL-IGKKKPAEINSRALEMLAAVGLEHRANHRPS-ELSGGERQRVAIARALVNNPRLVLADEPTGNLDArnaDS 183
|
170 180
....*....|....*....|....*
gi 743842931 660 VEALIQGLVLFQG-GILMVSHDEHL 683
Cdd:PRK11629 184 IFQLLGELNRLQGtAFLVVTHDLQL 208
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
505-704 |
2.27e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.90 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 505 IISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF---------RSAKVRI---- 571
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWfsghditrlKNREVPFlrrq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 572 --AVFSQHHVDgLDLSSNPLLYMMRCFPGVPEQKLR----AHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHI 645
Cdd:PRK10908 81 igMIFQDHHLL-MDRTVYDNVAIPLIIAGASGDDIRrrvsAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 646 ILLDEPSNHLDldavEALIQGLV-LFQG------GILMVSHDEHLISGSVDELWVVSQGKVTPFHG 704
Cdd:PRK10908 159 LLADEPTGNLD----DALSEGILrLFEEfnrvgvTVLMATHDIGLISRRSYRMLTLSDGHLHGGVG 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
506-680 |
2.30e-13 |
|
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: 70.41 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDLS 585
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIF--------------IDGEDIR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 586 SNPLLYMMR----------CFP---------------GVPEQKLRA------HLGSFGVTGNLALQPmYTLSGGQKSRVA 634
Cdd:cd03295 67 EQDPVELRRkigyviqqigLFPhmtveenialvpkllKWPKEKIREradellALVGLDPAEFADRYP-HELSGGQQQRVG 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 743842931 635 FAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVLFQ----GGILMVSHD 680
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQqelgKTIVFVTHD 195
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
506-679 |
2.44e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.00 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGPLMFknlNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF-------RSAKVRIAV----- 573
Cdd:PRK10771 2 LKLTDITWLYHHLPMRF---DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTlngqdhtTTPPSRRPVsmlfq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 574 ----FSQHHVD---GLDLSsnpllymmrcfPGV---PEQK--LRAHLGSFGVTGNLALQPmYTLSGGQKSRVAFAKITFK 641
Cdd:PRK10771 79 ennlFSHLTVAqniGLGLN-----------PGLklnAAQRekLHAIARQMGIEDLLARLP-GQLSGGQRQRVALARCLVR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 743842931 642 KPHIILLDEPSNHLDldavEALIQG-LVLF-------QGGILMVSH 679
Cdd:PRK10771 147 EQPILLLDEPFSALD----PALRQEmLTLVsqvcqerQLTLLMVSH 188
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
175-396 |
2.89e-13 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 69.90 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDgsVTLSF--GRHYGLVGRNGTGKTTFLRYMAL--HAIDGIPRNCQILHVEQEVVGDDTSALQ 250
Cdd:cd03260 1 IELRDLNVYYGDKHALKD--ISLDIpkGEITALIGPSGCGKSTLLRLLNRlnDLIPGAPDEGEVLLDGKDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 251 CvlnsdieRTRL-------------LEEEVRLhaqqrdldfedaagngkGDQI-GAINKDAISQRLEEIYKRLELIDAYS 316
Cdd:cd03260 79 L-------RRRVgmvfqkpnpfpgsIYDNVAY-----------------GLRLhGIKLKEELDERVEEALRKAALWDEVK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 317 AEARAASilaglsfspemqkkatktFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPK--TFIVV 394
Cdd:cd03260 135 DRLHALG------------------LSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIV 196
|
..
gi 743842931 395 SH 396
Cdd:cd03260 197 TH 198
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
505-699 |
3.40e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.53 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 505 IISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKV-----------RIAV 573
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREvnaenekwvrsKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 574 FSQHHVDGL-------DLSSNPLlyMMRCFPGVPEQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHII 646
Cdd:PRK13647 84 VFQDPDDQVfsstvwdDVAFGPV--NMGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 647 LLDEPSNHLDLDAVEALIQGL-VLFQGG--ILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILdRLHNQGktVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
528-699 |
3.70e-13 |
|
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: 70.07 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 528 GIDLD----SRIAMVGPNGIGKSTILKLIAGELQPTSGTVF-------------RSAK--------------------VR 570
Cdd:COG0411 22 DVSLEvergEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfdgrditglpphrIARLgiartfqnprlfpeltvlenVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 571 IAVFSQHHVDGLDLSSNPLLYMMRcfpgvpEQKLRAH----LGSFGVTGnLALQPMYTLSGGQKSRVAFAKITFKKPHII 646
Cdd:COG0411 102 VAAHARLGRGLLAALLRLPRARRE------EREARERaeelLERVGLAD-RADEPAGNLSYGQQRRLEIARALATEPKLL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743842931 647 LLDEPS---NHLDLDAVEALIQGLVLFQG-GILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:COG0411 175 LLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
505-700 |
4.62e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 70.22 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 505 IISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF-----------RSAKVRIAV 573
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLirgepitkeniREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 574 FSQHHVDGL-------DLSSNPllymmrCFPGVPEQ----KLRAHLGSFGVTGNLALQPMYtLSGGQKSRVAFAKITFKK 642
Cdd:PRK13652 83 VFQNPDDQIfsptveqDIAFGP------INLGLDEEtvahRVSSALHMLGLEELRDRVPHH-LSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743842931 643 PHIILLDEPSNHLDLDAVEALIQGL----VLFQGGILMVSHDEHLISGSVDELWVVSQGKVT 700
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLndlpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
503-698 |
5.57e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 69.63 E-value: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 503 APIISFSDASFGYpGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVfrsakvriaVFSQHHVDGL 582
Cdd:PRK11300 3 QPLLSVSGLMMRF-GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI---------LLRGQHIEGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 583 DLSSNPLLYMMRCFPGVP--------EQKLRA---HLGSfGVTGNLALQPMY---------------------------- 623
Cdd:PRK11300 73 PGHQIARMGVVRTFQHVRlfremtviENLLVAqhqQLKT-GLFSGLLKTPAFrraesealdraatwlervgllehanrqa 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 624 -TLSGGQKSRVAFAKITFKKPHIILLDEPS---NHLDLDAVEALIQGLV-LFQGGILMVSHDEHLISGSVDELWVVSQGK 698
Cdd:PRK11300 152 gNLAYGQQRRLEIARCMVTQPEILMLDEPAaglNPKETKELDELIAELRnEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
505-656 |
6.40e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 69.83 E-value: 6.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 505 IISFSDASFGYPGGPL-MFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSgtvfrSAKVRIAvfsqhhVDGLD 583
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDD-----NPNSKIT------VDGIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 584 LSS---------------NPllymMRCFPG---------------VPEQKL----RAHLGSFGVTGNLALQPMYtLSGGQ 629
Cdd:PRK13640 74 LTAktvwdirekvgivfqNP----DNQFVGatvgddvafglenraVPRPEMikivRDVLADVGMLDYIDSEPAN-LSGGQ 148
|
170 180
....*....|....*....|....*..
gi 743842931 630 KSRVAFAKITFKKPHIILLDEPSNHLD 656
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLD 175
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
517-685 |
7.34e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.59 E-value: 7.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 517 GGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDLSS-NPLLYMMR- 594
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLL--------------FEGEDISTlKPEIYRQQv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 595 --C----------------FP------GVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDE 650
Cdd:PRK10247 84 syCaqtptlfgdtvydnliFPwqirnqQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 743842931 651 PSNHLDLD---AVEALIQGLVLFQG-GILMVSHDEHLIS 685
Cdd:PRK10247 164 ITSALDESnkhNVNEIIHRYVREQNiAVLWVTHDKDEIN 202
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
472-699 |
8.67e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 71.39 E-value: 8.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 472 IKALDRLghmDEIVN-DPDYKFEfPTPDDRPGAPIISFSDASFGYPGGPLM-FKNLNFGIDLDSRIAMVGPNGIGKSTIL 549
Cdd:PRK11160 308 IASARRI---NEITEqKPEVTFP-TTSTAAADQVSLTLNNVSFTYPDQPQPvLKGLSLQIKAGEKVALLGRTGCGKSTLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 550 KLIAGELQPTSGTV---------FRSAKVR--IAVFSQH-HVDGLDLSSNPLLYMmrcfPGVPEQKLRAHLGSFGVtGNL 617
Cdd:PRK11160 384 QLLTRAWDPQQGEIllngqpiadYSEAALRqaISVVSQRvHLFSATLRDNLLLAA----PNASDEALIEVLQQVGL-EKL 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 618 A--LQPMYT--------LSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDaVEALIQGLvLFQGG----ILMVSHDEHL 683
Cdd:PRK11160 459 LedDKGLNAwlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAE-TERQILEL-LAEHAqnktVLMITHRLTG 536
|
250
....*....|....*.
gi 743842931 684 ISgSVDELWVVSQGKV 699
Cdd:PRK11160 537 LE-QFDRICVMDNGQI 551
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
175-373 |
9.87e-13 |
|
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: 68.30 E-value: 9.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDL---IVDG-SVTLSFGRHYGLVGRNGTGKTTFLRY-MALHAIDG--IprncqilhveqEVVGDDts 247
Cdd:cd03257 2 LEVKNLSVSFPTGGGsvkALDDvSFSIKKGETLGLVGESGSGKSTLARAiLGLLKPTSgsI-----------IFDGKD-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 248 alqcVLNSDIERTRLLEEEVRLHAQqrdldfedaagngkgDQIGAIN---KdaISQRLEEIYKRLELIDAYSAEARAAS- 323
Cdd:cd03257 69 ----LLKLSRRLRKIRRKEIQMVFQ---------------DPMSSLNprmT--IGEQIAEPLRIHGKLSKKEARKEAVLl 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 743842931 324 ILAGLSFSPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:cd03257 128 LLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALD 177
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
504-679 |
1.38e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.57 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 504 PIISFSDASFGYPGGPLmFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAK-VRIAVFSQH----- 577
Cdd:PRK13543 10 PLLAAHALAFSRNEEPV-FGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtATRGDRSRFmaylg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 578 HVDGL--DLSSNPLLYMMRCFPGV-PEQKLRAHLGSFGVTGNlALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNH 654
Cdd:PRK13543 89 HLPGLkaDLSTLENLHFLCGLHGRrAKQMPGSALAIVGLAGY-EDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYAN 167
|
170 180
....*....|....*....|....*...
gi 743842931 655 LDLDA---VEALIQGLVLFQGGILMVSH 679
Cdd:PRK13543 168 LDLEGitlVNRMISAHLRGGGAALVTTH 195
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
523-680 |
1.40e-12 |
|
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: 67.88 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 523 KNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKV-------RIAVFSQHHV-DGLDLSSNPLLYMMR 594
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQitepgpdRMVVFQNYSLlPWLTVRENIALAVDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 595 CFPGVPEQKLRA----HLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVLF 670
Cdd:TIGR01184 82 VLPDLSKSERRAiveeHIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170
....*....|....
gi 743842931 671 ----QGGILMVSHD 680
Cdd:TIGR01184 161 weehRVTVLMVTHD 174
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
527-705 |
1.41e-12 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 67.46 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 527 FGIDLDSR----IAMVGPNGIGKSTILKLIAGELQPTSGTV------------FRSAKVRIA-------VFSQHHVDGld 583
Cdd:cd03224 17 FGVSLTVPegeiVALLGRNGAGKTTLLKTIMGLLPPRSGSIrfdgrditglppHERARAGIGyvpegrrIFPELTVEE-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 584 lssNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSnhLDL-----D 658
Cdd:cd03224 95 ---NLLLGAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS--EGLapkivE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 743842931 659 AVEALIQGLVLFQGGILMVSHDEHLISGSVDELWVVSQGKVTpFHGT 705
Cdd:cd03224 170 EIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVV-LEGT 215
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
506-705 |
1.54e-12 |
|
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: 70.52 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPG-GPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTV-----------FRSAKVRIAV 573
Cdd:TIGR02203 331 VEFRNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQIlldghdladytLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 574 FSQHHVDGLDLSSNPLLYMMRcfPGVPEQKLR-----AHLGSF------------GVTGNLalqpmytLSGGQKSRVAFA 636
Cdd:TIGR02203 411 VSQDVVLFNDTIANNIAYGRT--EQADRAEIEralaaAYAQDFvdklplgldtpiGENGVL-------LSGGQRQRLAIA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 637 KITFKKPHIILLDEPSNHLD-------LDAVEALIQGLVlfqggILMVSHDEHLISGSvDELWVVSQGKVTPfHGT 705
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDneserlvQAALERLMQGRT-----TLVIAHRLSTIEKA-DRIVVMDDGRIVE-RGT 550
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
502-706 |
1.83e-12 |
|
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: 68.34 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 502 GAPIISFSDasFGYPGGPLMfKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAkvRIAVFSQHH--V 579
Cdd:cd03291 36 DDNNLFFSN--LCLVGAPVL-KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--RISFSSQFSwiM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 580 DGlDLSSNPLLYM----MRCFPGVPEQKLRAHLGSFGVTGNLAL-QPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNH 654
Cdd:cd03291 111 PG-TIKENIIFGVsydeYRYKSVVKACQLEEDITKFPEKDNTVLgEGGITLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 655 LDL----DAVEALIQGLVLFQGGILMVSHDEHLisGSVDELWVVSQGKvTPFHGTF 706
Cdd:cd03291 190 LDVftekEIFESCVCKLMANKTRILVTSKMEHL--KKADKILILHEGS-SYFYGTF 242
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
184-377 |
2.18e-12 |
|
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: 67.01 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 184 VGGRDLIVDG-SVTLSFGRHYGLVGRNGTGKTTFLRYMA--LHAIDGIPrncqilhveqEVVGDDTS----ALQCVLNSD 256
Cdd:cd03266 14 VKKTVQAVDGvSFTVKPGEVTGLLGPNGAGKTTTLRMLAglLEPDAGFA----------TVDGFDVVkepaEARRRLGFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 257 IERTRLLEeevRLHAQQRDLDFEDAAGngkgdqigaINKDAISQRLEEIYKRLELidaysaearaasilaglsfsPEMQK 336
Cdd:cd03266 84 SDSTGLYD---RLTARENLEYFAGLYG---------LKGDELTARLEELADRLGM--------------------EELLD 131
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 743842931 337 KATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAV 377
Cdd:cd03266 132 RRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
172-373 |
2.33e-12 |
|
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: 69.93 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 172 VKDIHLEnFNISVGGRDLIVDGsVTLSF--GRHYGLVGRNGTGKTTFLRYMA-LHAID-GiprncQILhveqevvgddts 247
Cdd:COG1123 263 VRNLSKR-YPVRGKGGVRAVDD-VSLTLrrGETLGLVGESGSGKSTLARLLLgLLRPTsG-----SIL------------ 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 248 alqcVLNSDIerTRLLEEEVRLHAQQRDLDFEDAAGngkgdqigAIN-KDAISQRLEEIYKRLELIDAYSAEARAASILA 326
Cdd:COG1123 324 ----FDGKDL--TKLSRRSLRELRRRVQMVFQDPYS--------SLNpRMTVGDIIAEPLRLHGLLSRAERRERVAELLE 389
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 743842931 327 --GLSfsPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:COG1123 390 rvGLP--PDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALD 436
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
176-411 |
2.55e-12 |
|
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: 66.79 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 176 HLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRymalhAIDGI--PRNCQIlhveqevvgddtsalqCVL 253
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLK-----AILGLlkPTSGSI----------------RVF 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 254 NSDIERTRLLeeeVRLHAQQRDLDF------EDAAGNGkgdqigainkdaisqrleeIYKRLELIDAYSAEARAAsILAG 327
Cdd:cd03235 60 GKPLEKERKR---IGYVPQRRSIDRdfpisvRDVVLMG-------------------LYGHKGLFRRLSKADKAK-VDEA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 328 LSFSpEMQKKATKTF---SGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWP---KTFIVVSHAREFL 401
Cdd:cd03235 117 LERV-GLSELADRQIgelSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRregMTILVVTHDLGLV 195
|
250
....*....|
gi 743842931 402 NTVVTDILHL 411
Cdd:cd03235 196 LEYFDRVLLL 205
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
534-699 |
3.00e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.17 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 534 RIAMVGPNGIGKSTILKLIAGeLQPTSGTVFRS------------AKVRiAVFSQHHvdgldlssnPLLYMMRCF----- 596
Cdd:COG4138 24 LIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNgrplsdwsaaelARHR-AYLSQQQ---------SPPFAMPVFqylal 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 597 ---PGVPEQKLRAHLGSfgVTGNLALQPMYT-----LSGGQKSRVAFAKITFK-----KPH--IILLDEPSNHLDLD--- 658
Cdd:COG4138 93 hqpAGASSEAVEQLLAQ--LAEALGLEDKLSrpltqLSGGEWQRVRLAAVLLQvwptiNPEgqLLLLDEPMNSLDVAqqa 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 743842931 659 AVEALIQGLVLFQGGILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:COG4138 171 ALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
503-680 |
3.49e-12 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 68.59 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 503 APIISFSDASFGYpGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGL 582
Cdd:COG3842 3 MPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIL--------------LDGR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 583 DLSS-------------NPLLymmrcFP---------------GVP--EQKLRAH--LGSFGVTGnLALQPMYTLSGGQK 630
Cdd:COG3842 68 DVTGlppekrnvgmvfqDYAL-----FPhltvaenvafglrmrGVPkaEIRARVAelLELVGLEG-LADRYPHQLSGGQQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 743842931 631 SRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVLFQG--GI--LMVSHD 680
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRelGItfIYVTHD 195
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
175-399 |
3.76e-12 |
|
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: 66.00 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMA--LHAIDGiprncqilhveqEVVGDDTsalqcv 252
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAglERPDSG------------EILIDGR------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 253 lnsDIertrlleeeVRLHAQQRD--LDFEDAA--------GN-GKGDQIGAINKDAISQRLEEIYKRLELidaysaeara 321
Cdd:cd03259 63 ---DV---------TGVPPERRNigMVFQDYAlfphltvaENiAFGLKLRGVPKAEIRARVRELLELVGL---------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 322 asilaglsfSPEMQKKATkTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPK----TFIVVSHA 397
Cdd:cd03259 121 ---------EGLLNRYPH-ELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelgiTTIYVTHD 190
|
..
gi 743842931 398 RE 399
Cdd:cd03259 191 QE 192
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
504-700 |
4.02e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 67.35 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 504 PIISFSDASFGYPGGP-LMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTV------------------- 563
Cdd:PRK13635 4 EIIRVEHISFRYPDAAtYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTItvggmvlseetvwdvrrqv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 564 ----------FRSAKVRIAVfsqhhVDGLDLSSNPLLYMMRcfpGVPEQKLRAHLGSFgvtgnlALQPMYTLSGGQKSRV 633
Cdd:PRK13635 84 gmvfqnpdnqFVGATVQDDV-----AFGLENIGVPREEMVE---RVDQALRQVGMEDF------LNREPHRLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 634 AFAKITFKKPHIILLDEPSNHLD-------LDAVEALIQglvlfQGGILMVS--HD--EhliSGSVDELWVVSQGKVT 700
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDprgrrevLETVRQLKE-----QKGITVLSitHDldE---AAQADRVIVMNKGEIL 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
505-699 |
4.58e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.95 E-value: 4.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 505 IISFSDASFGYPGGPLMfKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKV-------------RI 571
Cdd:PRK13638 1 MLATSDLWFRYQDEPVL-KGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldyskrgllalrqQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 572 AVFSQ---HHVDGLDLSSNpLLYMMRCFpGVPEQKLRAHlgsfgVTGNLAL--------QPMYTLSGGQKSRVAFAKITF 640
Cdd:PRK13638 80 ATVFQdpeQQIFYTDIDSD-IAFSLRNL-GVPEAEITRR-----VDEALTLvdaqhfrhQPIQCLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743842931 641 KKPHIILLDEPSNHLD---LDAVEALIQGLVLFQGGILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:PRK13638 153 LQARYLLLDEPTAGLDpagRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
536-681 |
4.63e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 68.32 E-value: 4.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 536 AMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDLSSNPL----LYMM----RCFP---------- 597
Cdd:PRK11607 49 ALLGASGCGKSTLLRMLAGFEQPTAGQIM--------------LDGVDLSHVPPyqrpINMMfqsyALFPhmtveqniaf 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 598 GVPEQKL-RAHLGSfGVTGNLALQPM--------YTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLD--------LDAV 660
Cdd:PRK11607 115 GLKQDKLpKAEIAS-RVNEMLGLVHMqefakrkpHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrmqLEVV 193
|
170 180
....*....|....*....|...
gi 743842931 661 EaliqglVLFQGGI--LMVSHDE 681
Cdd:PRK11607 194 D------ILERVGVtcVMVTHDQ 210
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
506-714 |
5.23e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.11 E-value: 5.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGY-PGGPLMFK---NLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTV---------------FRS 566
Cdd:PRK13646 3 IRFDNVSYTYqKGTPYEHQaihDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVtvdditithktkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 567 AKVRIAVFSQHHVDGL--DLSSNPLLYMMRCFP-GVPEQKLRAH--LGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFK 641
Cdd:PRK13646 83 VRKRIGMVFQFPESQLfeDTVEREIIFGPKNFKmNLDEVKNYAHrlLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 642 KPHIILLDEPSNHLD---LDAVEALIQGLVLFQG-GILMVSHDEHLISGSVDELWVVSQG----KVTPfHGTFLDYKKIL 713
Cdd:PRK13646 163 NPDIIVLDEPTAGLDpqsKRQVMRLLKSLQTDENkTIILVSHDMNEVARYADEVIVMKEGsivsQTSP-KELFKDKKKLA 241
|
.
gi 743842931 714 Q 714
Cdd:PRK13646 242 D 242
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
194-375 |
5.82e-12 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 66.75 E-value: 5.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 194 SVTLSFGRHYGLVGRNGTGKTTFLRYmalhaidgiprncqILHVEQEVVGDDTSALQCVLNSDIERTRLLEEEVRLHAQq 273
Cdd:TIGR02769 31 SLSIEEGETVGLLGRSGCGKSTLARL--------------LLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRDVQLVFQ- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 274 rdldfedaagngkgDQIGAIN-KDAISQRLEEIYKRLELIDAYSAEARAASILAGLSFSPEMQKKATKTFSGGWRMRIAL 352
Cdd:TIGR02769 96 --------------DSPSAVNpRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINI 161
|
170 180
....*....|....*....|...
gi 743842931 353 ARALFIEPDILLLDEPTNHLDLH 375
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMV 184
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
506-699 |
6.81e-12 |
|
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: 65.72 E-value: 6.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYpGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKvRIA-----------VF 574
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK-DITnlpphkrpvntVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 575 sQH-----HvdgLDLSSNPllymmrCFP----GVPEQKLRAhlgsfGVTGNLALQPM--------YTLSGGQKSRVAFAK 637
Cdd:cd03300 79 -QNyalfpH---LTVFENI------AFGlrlkKLPKAEIKE-----RVAEALDLVQLegyanrkpSQLSGGQQQRVAIAR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743842931 638 ITFKKPHIILLDEPSNHLDLDAVEALIQGLVLFQG--GI--LMVSHD-EHLISGSvDELWVVSQGKV 699
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGItfVFVTHDqEEALTMS-DRIAVMNKGKI 209
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
511-706 |
9.48e-12 |
|
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: 68.78 E-value: 9.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 511 ASFGYPGGPLMfKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAkvRIAVFSQHH--VDG------- 581
Cdd:TIGR01271 432 SNFSLYVTPVL-KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--RISFSPQTSwiMPGtikdnii 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 582 LDLSSNPLLYM-----------MRCFPgvpeQKLRAHLGSFGVTgnlalqpmytLSGGQKSRVAFAKITFKKPHIILLDE 650
Cdd:TIGR01271 509 FGLSYDEYRYTsvikacqleedIALFP----EKDKTVLGEGGIT----------LSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 651 PSNHLDL----DAVEALIQGLVLFQGGILMVSHDEHLisGSVDELWVVSQGkVTPFHGTF 706
Cdd:TIGR01271 575 PFTHLDVvtekEIFESCLCKLMSNKTRILVTSKLEHL--KKADKILLLHEG-VCYFYGTF 631
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
524-699 |
9.85e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 67.05 E-value: 9.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 524 NLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDLSSNPLLYMMRC-------- 595
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIF--------------IDGEDVTHRSIQQRDICmvfqsyal 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 596 FP---------------GVPEQKLRAHlgsfgVTGNLAL------QPMYT--LSGGQKSRVAFAKITFKKPHIILLDEPS 652
Cdd:PRK11432 90 FPhmslgenvgyglkmlGVPKEERKQR-----VKEALELvdlagfEDRYVdqISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 653 NHLDL-------DAVEALIQglvlfQGGI--LMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:PRK11432 165 SNLDAnlrrsmrEKIRELQQ-----QFNItsLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
176-417 |
9.89e-12 |
|
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: 64.59 E-value: 9.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 176 HLENFNISVGGRDLIVDG-SVTLSFGRHYGLVGRNGTGKTTFLRymalhAIDGIPRNCQ---ILHVEQEVVGDDTSALQC 251
Cdd:cd03226 1 RIENISFSYKKGTEILDDlSLDLYAGEIIALTGKNGAGKTTLAK-----ILAGLIKESSgsiLLNGKPIKAKERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 252 VLNsDIERtRLLEEEVRlhaqqRDLDfedaagngkgdqIGAINKDAISQRLEEIYKRLELIDaysaearaasilaglsfs 331
Cdd:cd03226 76 VMQ-DVDY-QLFTDSVR-----EELL------------LGLKELDAGNEQAETVLKDLDLYA------------------ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 332 peMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLH-----AVLWLEsyLVKWPKTFIVVSHAREFLNTVVT 406
Cdd:cd03226 119 --LKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKnmervGELIRE--LAAQGKAVIVITHDYEFLAKVCD 194
|
250
....*....|.
gi 743842931 407 DILHLQGQKLT 417
Cdd:cd03226 195 RVLLLANGAIV 205
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
501-685 |
1.01e-11 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 65.15 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 501 PGAPIISFSDA--SFGYPGGPL-MFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTV-------------- 563
Cdd:COG4181 4 SSAPIIELRGLtkTVGTGAGELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVrlagqdlfaldeda 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 564 ---FRSAKVRIaVF-SQHHVDGLDLSSNPLLymmrcfP----GVPE--QKLRAHLGSFGVTGNLALQPMyTLSGGQKSRV 633
Cdd:COG4181 84 rarLRARHVGF-VFqSFQLLPTLTALENVML------PlelaGRRDarARARALLERVGLGHRLDHYPA-QLSGGEQQRV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 634 AFAKITFKKPHIILLDEPSNHLDLDAVEALIQglVLF-----QGGIL-MVSHDEHLIS 685
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAATGEQIID--LLFelnreRGTTLvLVTHDPALAA 211
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
523-699 |
1.02e-11 |
|
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: 65.43 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 523 KNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSA---------KVRIAVFSQHHV--DGLDLSSNpLLY 591
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnlppeKRDISYVPQNYAlfPHMTVYKN-IAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 592 MMRcFPGVP----EQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGL 667
Cdd:cd03299 95 GLK-KRKVDkkeiERKVLEIAEMLGIDHLLNRKPE-TLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREEL 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 743842931 668 V----LFQGGILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:cd03299 173 KkirkEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
526-702 |
1.18e-11 |
|
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: 66.67 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 526 NFGIDLDSRI------AMVGPNGIGKSTILKLIAGELQPTSG-------TVFRSAKV--------RIA-VFSQ-----Hh 578
Cdd:TIGR02142 11 DFSLDADFTLpgqgvtAIFGRSGSGKTTLIRLIAGLTRPDEGeivlngrTLFDSRKGiflppekrRIGyVFQEarlfpH- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 579 vdgLDLSSNpLLY-MMRCFP---GVPEQKLRAHLGsfgvTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNH 654
Cdd:TIGR02142 90 ---LSVRGN-LRYgMKRARPserRISFERVIELLG----IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 743842931 655 LDLDAVEALIQGL----VLFQGGILMVSHDEHLISGSVDELWVVSQGKVTPF 702
Cdd:TIGR02142 162 LDDPRKYEILPYLerlhAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAA 213
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
205-416 |
1.26e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.38 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 205 LVGRNGTGKTTFLRymalhAIDGIPRNCQ-ILHVEQE---VVGDDTSALQCvlnSDIERTRLLEEEVRLHAQQRDLdfed 280
Cdd:PRK10619 36 IIGSSGSGKSTFLR-----CINFLEKPSEgSIVVNGQtinLVRDKDGQLKV---ADKNQLRLLRTRLTMVFQHFNL---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 281 aagngkgdqigAINKDAISQRLEEIYKRLELIDAySAEARAASILAGLSFSPEMQKKATKTFSGGWRMRIALARALFIEP 360
Cdd:PRK10619 104 -----------WSHMTVLENVMEAPIQVLGLSKQ-EARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 743842931 361 DILLLDEPTNHLD---LHAVLWLESYLVKWPKTFIVVSHAREFLNTVVTDILHLQGQKL 416
Cdd:PRK10619 172 EVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
191-374 |
1.27e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 66.53 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 191 VDG-SVTLSFGRHYGLVGRNGTGKTTFLRYMALhaidgiprncqilhVEQEVVGDDTSALQCVLNSDIERTRLLEEEVRL 269
Cdd:PRK11308 31 LDGvSFTLERGKTLAVVGESGCGKSTLARLLTM--------------IETPTGGELYYQGQDLLKADPEAQKLLRQKIQI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 270 HAQqrdldfedaagngkgDQIGAIN-KDAISQRLEEiykRLELIDAYSAEARAASILA-----GLSfsPEMQKKATKTFS 343
Cdd:PRK11308 97 VFQ---------------NPYGSLNpRKKVGQILEE---PLLINTSLSAAERREKALAmmakvGLR--PEHYDRYPHMFS 156
|
170 180 190
....*....|....*....|....*....|.
gi 743842931 344 GGWRMRIALARALFIEPDILLLDEPTNHLDL 374
Cdd:PRK11308 157 GGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
506-699 |
1.49e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 65.81 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGY-PGGP---LMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKVRIAVFSQHHVDG 581
Cdd:PRK13634 3 ITFQKVEHRYqYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 582 L----------------------DLSSNPLLYmmrcfpGVPE----QKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAF 635
Cdd:PRK13634 83 LrkkvgivfqfpehqlfeetvekDICFGPMNF------GVSEedakQKAREMIELVGLPEELLARSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743842931 636 AKITFKKPHIILLDEPSNHLD-------LDAVEALIQglvlfQGG--ILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDpkgrkemMEMFYKLHK-----EKGltTVLVTHSMEDAARYADQIVVMHKGTV 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
535-705 |
1.54e-11 |
|
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: 64.87 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 535 IAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDLSSNPL------------------------- 589
Cdd:cd03218 29 VGLLGPNGAGKTTTFYMIVGLVKPDSGKIL--------------LDGQDITKLPMhkrarlgigylpqeasifrkltvee 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 590 -----LYMMRCFPGVPEQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAV---E 661
Cdd:cd03218 95 nilavLEIRGLSKKEREEKLEELLEEFHIT-HLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVqdiQ 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 743842931 662 ALIQGLVLFQGGILMVSHDEHLISGSVDELWVVSQGKVTpFHGT 705
Cdd:cd03218 174 KIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVL-AEGT 216
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
523-699 |
1.63e-11 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 64.16 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 523 KNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF---------RSAKVRIAVFSQHHVDGLDLSSNPLLYMM 593
Cdd:cd03268 17 DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfdgksyqknIEALRRIGALIEAPGFYPNLTARENLRLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 594 RCFPGVPEQKLRAHLGSFGVtGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAV---EALIQGLVLF 670
Cdd:cd03268 97 ARLLGIRKKRIDEVLDVVGL-KDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIkelRELILSLRDQ 175
|
170 180
....*....|....*....|....*....
gi 743842931 671 QGGILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:cd03268 176 GITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
503-698 |
1.83e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 65.60 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 503 APIISFSDASFGYpGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF----------RSAKVRIA 572
Cdd:PRK13537 5 VAPIDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsraRHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 573 VFSQhhVDGLD----LSSNpLLYMMRCFpGVPEQKLRAH---LGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHI 645
Cdd:PRK13537 84 VVPQ--FDNLDpdftVREN-LLVFGRYF-GLSAAAARALvppLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 646 ILLDEPSNHLDLDAVEALIQGL--VLFQGG-ILMVSHDEHLISGSVDELWVVSQGK 698
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLrsLLARGKtILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
523-656 |
2.17e-11 |
|
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: 63.81 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 523 KNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF--------RSAKVR-IA-VFSQH----HVDGLDLSSNP 588
Cdd:cd03301 17 DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtdLPPKDRdIAmVFQNYalypHMTVYDNIAFG 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743842931 589 LlyMMRCFPGVP-EQKLR--AHLgsFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLD 656
Cdd:cd03301 97 L--KLRKVPKDEiDERVRevAEL--LQIEHLLDRKPK-QLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
516-699 |
2.22e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 64.70 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 516 PGGPLMFKNLN--FGI-----DLDSRI------AMVGPNGIGKSTILKLIAGELQPTSGTVFRSAkvriAVFSQHHVDG- 581
Cdd:PRK11247 9 QGTPLLLNAVSkrYGErtvlnQLDLHIpagqfvAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT----APLAEAREDTr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 582 LDLSSNPLLymmrcfpgvPEQKLRAHLGsFGVTGNL---ALQPMYT-------------LSGGQKSRVAFAKITFKKPHI 645
Cdd:PRK11247 85 LMFQDARLL---------PWKKVIDNVG-LGLKGQWrdaALQALAAvgladranewpaaLSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743842931 646 ILLDEPSNHLD-LDAVE--ALIQGLVLFQG-GILMVSHDehlISGSV---DELWVVSQGKV 699
Cdd:PRK11247 155 LLLDEPLGALDaLTRIEmqDLIESLWQQHGfTVLLVTHD---VSEAVamaDRVLLIEEGKI 212
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
517-656 |
2.82e-11 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 63.93 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 517 GGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGT--------VFRSAKVR--IA-VFSQHHVDGlDLS 585
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvVREPREVRrrIGiVFQDLSVDD-ELT 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743842931 586 SNPLLYMMRCFPGVPEQKLR---AHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLD 656
Cdd:cd03265 90 GWENLYIHARLYGVPGAERReriDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
513-681 |
2.87e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 513 FGYPGGPLMfKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF---RSAKVRIAVFSQH-----HVDGLdl 584
Cdd:PRK13540 9 FDYHDQPLL-QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILferQSIKKDLCTYQKQlcfvgHRSGI-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 585 ssNPLLYMMR-CFpgvpeQKLRAHLGSFGVT--------GNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHL 655
Cdd:PRK13540 86 --NPYLTLREnCL-----YDIHFSPGAVGITelcrlfslEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170 180
....*....|....*....|....*....
gi 743842931 656 DLDAVEALIQGLVLFQ---GGILMVSHDE 681
Cdd:PRK13540 159 DELSLLTIITKIQEHRakgGAVLLTSHQD 187
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
506-667 |
3.47e-11 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 63.66 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGY-PGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDL 584
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVL--------------VDGHDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 585 SSNPLLYMMRCFPGVPEQKLrahLGSFGVTGNLAL----QPMY-------------------------------TLSGGQ 629
Cdd:cd03252 67 ALADPAWLRRQVGVVLQENV---LFNRSIRDNIALadpgMSMErvieaaklagahdfiselpegydtivgeqgaGLSGGQ 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 743842931 630 KSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGL 667
Cdd:cd03252 144 RQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNM 181
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
506-704 |
3.54e-11 |
|
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: 62.95 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGPLMF-----KNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQP--TSGTVFrsakvriavfsqhh 578
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSgkqllKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVL-------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 579 VDGLDLSSNPLLYMMrCFpgVPEQKLraHLGSFGVTGNLalqpMYT-----LSGGQKSRVAFAKITFKKPHIILLDEPSN 653
Cdd:cd03213 70 INGRPLDKRSFRKII-GY--VPQDDI--LHPTLTVRETL----MFAaklrgLSGGERKRVSIALELVSNPSLLFLDEPTS 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 654 HLD----LDAVEALIQglvLFQGG--ILMVSHD-EHLISGSVDELWVVSQGKVTpFHG 704
Cdd:cd03213 141 GLDsssaLQVMSLLRR---LADTGrtIICSIHQpSSEIFELFDKLLLLSQGRVI-YFG 194
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
506-699 |
3.69e-11 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 63.40 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDLS 585
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIL--------------IDGIDIR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 586 SNPLLYMMRCFPGVPEQklrAHLGSFGVTGNLALQPMY-----------------------------------TLSGGQK 630
Cdd:cd03254 69 DISRKSLRSMIGVVLQD---TFLFSGTIMENIRLGRPNatdeevieaakeagahdfimklpngydtvlgenggNLSQGER 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743842931 631 SRVAFAKITFKKPHIILLDEPSNHLDLDAvEALIQG--LVLFQG-GILMVSHdeHL-ISGSVDELWVVSQGKV 699
Cdd:cd03254 146 QLLAIARAMLRDPKILILDEATSNIDTET-EKLIQEalEKLMKGrTSIIIAH--RLsTIKNADKILVLDDGKI 215
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
523-656 |
3.97e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 65.17 E-value: 3.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 523 KNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKVriaVFSQHHVD----GLdLSSNPLLymmrcFP- 597
Cdd:COG1118 19 DDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD---LFTNLPPRerrvGF-VFQHYAL-----FPh 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743842931 598 --------------GVPEQKLRA----HLGSFGVTGnlaLQPMY--TLSGGQKSRVAFAKITFKKPHIILLDEPSNHLD 656
Cdd:COG1118 90 mtvaeniafglrvrPPSKAEIRArveeLLELVQLEG---LADRYpsQLSGGQRQRVALARALAVEPEVLLLDEPFGALD 165
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
538-700 |
4.18e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.80 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 538 VGPNGIGKSTILKLIAGeLQPTSGTVfrsakvriavfsqhHVDGLDLSSNPL--LYMMRCF------------------- 596
Cdd:PRK03695 28 VGPNGAGKSTLLARMAG-LLPGSGSI--------------QFAGQPLEAWSAaeLARHRAYlsqqqtppfampvfqyltl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 597 ---PGVPEQKLRAHL----GSFGVTGNLAlQPMYTLSGGQKSRVAFAKITFK-----KPH--IILLDEPSNHLDLDAVEA 662
Cdd:PRK03695 93 hqpDKTRTEAVASALnevaEALGLDDKLG-RSVNQLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEPMNSLDVAQQAA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 743842931 663 LIQGLVLF--QGG-ILMVSHD-----EHlisgsVDELWVVSQGKVT 700
Cdd:PRK03695 172 LDRLLSELcqQGIaVVMSSHDlnhtlRH-----ADRVWLLKQGKLL 212
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
342-404 |
4.61e-11 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 61.85 E-value: 4.61e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 342 FSGGWRMRIALARALFIEPDILLLDEPTNHLDL---HAVLWLESYLVKWPKTFIVVSHAREFLNTV 404
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVegeRALNQAIAALKAAGATRIVIAHRPETLASA 162
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
535-697 |
4.66e-11 |
|
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: 63.22 E-value: 4.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 535 IAMVGPNGIGKSTILKLIAGELQPTSGTV-FRSA---------------KVR---IAVFSQH-----HVDGLDLSSNPLL 590
Cdd:COG4778 40 VALTGPSGAGKSTLLKCIYGNYLPDSGSIlVRHDggwvdlaqaspreilALRrrtIGYVSQFlrvipRVSALDVVAEPLL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 591 YMmrcfpGVPEQKLRAH----LGSFGVTGNL-ALQPMyTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDL---DAVEA 662
Cdd:COG4778 120 ER-----GVDREEARARarelLARLNLPERLwDLPPA-TFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAanrAVVVE 193
|
170 180 190
....*....|....*....|....*....|....*.
gi 743842931 663 LIQGLvLFQG-GILMVSHDEHLISGSVDELWVVSQG 697
Cdd:COG4778 194 LIEEA-KARGtAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
537-699 |
4.96e-11 |
|
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: 64.82 E-value: 4.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 537 MVGPNGIGKSTILKLIAGELQPTSGTVFRSAKVRIAVFSQHHVDGLDLSSNPLLYMMRCFP---------GVPEQ----K 603
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEEnvafglkmrKVPRAeikpR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 604 LRAHLGSFGVTGNLALQPmYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVLFQG--GI--LMVSH 679
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKP-HQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEqlGItfVFVTH 159
|
170 180
....*....|....*....|
gi 743842931 680 DEHLISGSVDELWVVSQGKV 699
Cdd:TIGR01187 160 DQEEAMTMSDRIAIMRKGKI 179
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
523-684 |
5.60e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 62.54 E-value: 5.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 523 KNLNFGIDLDSRIAMVGPNGIGKSTILKLIAG--ELQPTSGTVFrsakvriavfsqhhVDGLDLSSNPllymmrcfpgvP 600
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEIL--------------FKGEDITDLP-----------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 601 EQklRAHLGSF----------GVTGNLALQPM-YTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVL 669
Cdd:cd03217 72 EE--RARLGIFlafqyppeipGVKNADFLRYVnEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINK 149
|
170
....*....|....*...
gi 743842931 670 FQG---GILMVSHDEHLI 684
Cdd:cd03217 150 LREegkSVLIITHYQRLL 167
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
506-700 |
7.57e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 63.61 E-value: 7.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGG-PLMFKNLnFGIDLD----SRIAMVGPNGIGKSTILKLIAGELQPTSGTVfRSAKVRIAVFSQH--- 577
Cdd:PRK13649 3 INLQNVSYTYQAGtPFEGRAL-FDVNLTiedgSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSV-RVDDTLITSTSKNkdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 578 -----HVdGL----------------DLSSNPLLYmmrcfpGVP----EQKLRAHLGSFGVTGNLALQPMYTLSGGQKSR 632
Cdd:PRK13649 81 kqirkKV-GLvfqfpesqlfeetvlkDVAFGPQNF------GVSqeeaEALAREKLALVGISESLFEKNPFELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743842931 633 VAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLV-LFQGG--ILMVSHDEHLISGSVDELWVVSQGKVT 700
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKkLHQSGmtIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
342-396 |
8.55e-11 |
|
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: 61.24 E-value: 8.55e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 743842931 342 FSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWP--KTFIVVSH 396
Cdd:cd03228 97 LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAkgKTVIVIAH 153
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
528-659 |
8.96e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 63.94 E-value: 8.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 528 GIDLD----SRIAMVGPNGIGKSTILKLIAGELQPTSGTVF---------RSAKVRIA-VFsQhhvdgldlssNPLLY-- 591
Cdd:COG3839 21 DIDLDiedgEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILiggrdvtdlPPKDRNIAmVF-Q----------SYALYph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 592 M-----------MRcfpGVP----EQKLRAHLGSFGVTGNLALQPmYTLSGGQKSRVAFAKITFKKPHIILLDEP-SNhl 655
Cdd:COG3839 90 MtvyeniafplkLR---KVPkaeiDRRVREAAELLGLEDLLDRKP-KQLSGGQRQRVALGRALVREPKVFLLDEPlSN-- 163
|
....
gi 743842931 656 dLDA 659
Cdd:COG3839 164 -LDA 166
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
505-699 |
9.08e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.60 E-value: 9.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 505 IISFSDASFGY-PGGPLMFKNLnFGIDLD----SRIAMVGPNGIGKSTILKLIAGELQPTSGTV---------------F 564
Cdd:PRK13643 1 MIKFEKVNYTYqPNSPFASRAL-FDIDLEvkkgSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivvsstskqkeI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 565 RSAKVRIAVFSQHHVDGL-------DLSSNPLLYmmrcfpGVPE---QKLRAH-LGSFGVTGNLALQPMYTLSGGQKSRV 633
Cdd:PRK13643 80 KPVRKKVGVVFQFPESQLfeetvlkDVAFGPQNF------GIPKekaEKIAAEkLEMVGLADEFWEKSPFELSGGQMRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743842931 634 AFAKITFKKPHIILLDEPSNHLDldaVEALIQGLVLFQG------GILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLD---PKARIEMMQLFESihqsgqTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
194-373 |
1.24e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.34 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 194 SVTLSFGRHYGLVGRNGTGKTT----FLRYMALHA---IDGIP----RNCQILHVE---QEVVGDDTSALQCVLNSdier 259
Cdd:PRK15134 306 SFTLRPGETLGLVGESGSGKSTtglaLLRLINSQGeiwFDGQPlhnlNRRQLLPVRhriQVVFQDPNSSLNPRLNV---- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 260 TRLLEEEVRLHaqQRDLDfedaagngkgdqigainkdaisqrleeiykrlelidAYSAEARAASILAGLSFSPEMQKKAT 339
Cdd:PRK15134 382 LQIIEEGLRVH--QPTLS------------------------------------AAQREQQVIAVMEEVGLDPETRHRYP 423
|
170 180 190
....*....|....*....|....*....|....
gi 743842931 340 KTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
505-699 |
1.40e-10 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 61.83 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 505 IISFSDASFGYPGGPLMF---KNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF--------------RSA 567
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVtalKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgtdltllsgkelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 568 KVRIAVFSQHhvdgLDLSSNPLLYMMRCFP----GVPEQKLRAHlgsfgVTGNLALQPMY--------TLSGGQKSRVAF 635
Cdd:cd03258 81 RRRIGMIFQH----FNLLSSRTVFENVALPleiaGVPKAEIEER-----VLELLELVGLEdkadaypaQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743842931 636 AKITFKKPHIILLDEPSNHLD---LDAVEALIQ------GLVlfqggILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDpetTQSILALLRdinrelGLT-----IVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
523-699 |
1.43e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 62.76 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 523 KNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDLSSNPL-LYMMRCFPGV-- 599
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKII--------------IDGVDITDKKVkLSDIRKKVGLvf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 600 --PEQKLRAHLG----SFGVTgNLAL----------QPM---------------YTLSGGQKSRVAFAKITFKKPHIILL 648
Cdd:PRK13637 90 qyPEYQLFEETIekdiAFGPI-NLGLseeeienrvkRAMnivgldyedykdkspFELSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 743842931 649 DEPSNHLD---LDAVEALIQGL-VLFQGGILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:PRK13637 169 DEPTAGLDpkgRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
174-396 |
1.48e-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: 64.47 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 174 DIHLENFNISVGGRD-LIVDGsVTLSF--GRHYGLVGRNGTGKTTFLRYMA-LHA-------IDGIP---------RNcQ 233
Cdd:COG2274 473 DIELENVSFRYPGDSpPVLDN-ISLTIkpGERVAIVGRSGSGKSTLLKLLLgLYEptsgrilIDGIDlrqidpaslRR-Q 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 234 ILHVEQEVVgddtsalqcvLnsdIERTrlLEEEVRLHAQQRDLDfedaagngkgdqigainkdaisqrleeiykrlELID 313
Cdd:COG2274 551 IGVVLQDVF----------L---FSGT--IRENITLGDPDATDE--------------------------------EIIE 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 314 AysaeARAASILaglSFSPEMQKK-ATK------TFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVK 386
Cdd:COG2274 584 A----ARLAGLH---DFIEALPMGyDTVvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRR 656
|
250
....*....|..
gi 743842931 387 W--PKTFIVVSH 396
Cdd:COG2274 657 LlkGRTVIIIAH 668
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
181-396 |
1.68e-10 |
|
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: 62.13 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 181 NISV-----GGRDLIVDG-SVTLSFGRHYGLVGRNGTGKTTFLRYMA-LHA-------IDGIPrncqilhVEQEVVGDDT 246
Cdd:COG1124 6 NLSVsygqgGRRVPVLKDvSLEVAPGESFGLVGESGSGKSTLLRALAgLERpwsgevtFDGRP-------VTRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 247 SALQCVlnsdiertrlleeevrlhaqqrdldFEDAAGngkgdqigAIN-KDAISQRLEEIYKRLELIDAysaEARAASIL 325
Cdd:COG1124 79 RRVQMV-------------------------FQDPYA--------SLHpRHTVDRILAEPLRIHGLPDR---EERIAELL 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743842931 326 AGLSFSPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLH--AVLW--LESYLVKWPKTFIVVSH 396
Cdd:COG1124 123 EQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSvqAEILnlLKDLREERGLTYLFVSH 197
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
175-436 |
1.71e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 61.95 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMALHAIdgiPRNCQiLHVEQEVVgdDTSAlqcvlN 254
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEM---PRSGT-LNIAGNHF--DFSK-----T 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 255 SDIERTRLLEEEVRLHAQQRDL--------DFEDAAGNGKGdqigaINKDAISQRLEEIYKRLELIDaySAEAraasila 326
Cdd:PRK11124 72 PSDKAIRELRRNVGMVFQQYNLwphltvqqNLIEAPCRVLG-----LSKDQALARAEKLLERLRLKP--YADR------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 327 glsFSPEMqkkatktfSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPKTFI---VVSHAREFLNT 403
Cdd:PRK11124 138 ---FPLHL--------SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGItqvIVTHEVEVARK 206
|
250 260 270
....*....|....*....|....*....|...
gi 743842931 404 VVTDILHLQGQKLTAyKGDYDTFERTREEQIKN 436
Cdd:PRK11124 207 TASRVVYMENGHIVE-QGDASCFTQPQTEAFKN 238
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
317-396 |
1.74e-10 |
|
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: 61.33 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 317 AEARAASILA--GLSfspEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD------LHAvlWLESYLVKWP 388
Cdd:cd03293 108 ARERAEELLElvGLS---GFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDaltreqLQE--ELLDIWRETG 182
|
....*...
gi 743842931 389 KTFIVVSH 396
Cdd:cd03293 183 KTVLLVTH 190
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
136-399 |
1.97e-10 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 63.84 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 136 RQREAQYqiHlAEMEAVRAGMPVACVTHDGGGGGPNVKD--------IHLENFNISVGGRDLIVDG-SVTLSFGRHYGLV 206
Cdd:TIGR02857 278 RQLGAQY--H-ARADGVAAAEALFAVLDAAPRPLAGKAPvtaapassLEFSGVSVAYPGRRPALRPvSFTVPPGERVALV 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 207 GRNGTGKTTflrymALHAIDGIprncqiLHVEQEVVgddtsalqcVLNSdiertrlleeevrlhaqqRDLDFEDAAGngK 286
Cdd:TIGR02857 355 GPSGAGKST-----LLNLLLGF------VDPTEGSI---------AVNG------------------VPLADADADS--W 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 287 GDQIGAInkdaiSQR--------LEEIykRLELIDAYSAEARAASILAGL-SFSPEM-QKKATKT------FSGGWRMRI 350
Cdd:TIGR02857 395 RDQIAWV-----PQHpflfagtiAENI--RLARPDASDAEIREALERAGLdEFVAALpQGLDTPIgeggagLSGGQAQRL 467
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 743842931 351 ALARALFIEPDILLLDEPTNHLDLH-AVLWLESYL-VKWPKTFIVVSHARE 399
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAEtEAEVLEALRaLAQGRTVLLVTHRLA 518
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
519-656 |
2.05e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 62.03 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 519 PLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDLSSNPLLYMMRCFPG 598
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVY--------------VDGLDTSDEENLWDIRNKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 599 V----PEQKLRAHLG----SFGvTGNLALQP---------------MYT--------LSGGQKSRVAFAKITFKKPHIIL 647
Cdd:PRK13633 89 MvfqnPDNQIVATIVeedvAFG-PENLGIPPeeirervdeslkkvgMYEyrrhaphlLSGGQKQRVAIAGILAMRPECII 167
|
....*....
gi 743842931 648 LDEPSNHLD 656
Cdd:PRK13633 168 FDEPTAMLD 176
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
528-680 |
2.36e-10 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 61.01 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 528 GIDLD----SRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDLSSnpllymmrcfPGVPEQK 603
Cdd:cd03262 18 GIDLTvkkgEVVVIIGPSGSGKSTLLRCINLLEEPDSGTII--------------IDGLKLTD----------DKKNINE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 604 LRAHLG----SFG------VTGNLALQPMY-------------------------------TLSGGQKSRVAFAKITFKK 642
Cdd:cd03262 74 LRQKVGmvfqQFNlfphltVLENITLAPIKvkgmskaeaeeralellekvgladkadaypaQLSGGQQQRVAIARALAMN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 743842931 643 PHIILLDEPSNHLDLDAVEALIQGLV-LFQGGILM--VSHD 680
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKdLAEEGMTMvvVTHE 194
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
175-416 |
2.37e-10 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 61.26 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMA--LHAIDGiprncqilHVEqevvgddtsalqcV 252
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILglLPPTSG--------TVR-------------L 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 253 LNSDIERTRLL------EEEVrlhaqqrDLDF----EDAAGNGkgdqigainkdaisqrleeIYKRLELIDAYSAE--AR 320
Cdd:COG1121 66 FGKPPRRARRRigyvpqRAEV-------DWDFpitvRDVVLMG-------------------RYGRRGLFRRPSRAdrEA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 321 AASILA--GLSfspEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKW---PKTFIVVS 395
Cdd:COG1121 120 VDEALErvGLE---DLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrreGKTILVVT 196
|
250 260
....*....|....*....|.
gi 743842931 396 HAREFLNTVVTDILHLQGQKL 416
Cdd:COG1121 197 HDLGAVREYFDRVLLLNRGLV 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
175-396 |
2.43e-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: 61.64 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRdLIVDG-SVTLSFGRHYGLVGRNGTGKTTFLRYMA--LHAIDGiprncqilhveQEVVgddtsalqc 251
Cdd:COG1119 4 LELRNVTVRRGGK-TILDDiSWTVKPGEHWAILGPNGAGKSTLLSLITgdLPPTYG-----------NDVR--------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 252 VLNSDIERTRLleEEVR---------LHAQ-QRDLDFEDAAGNGKGDQIGainkdaisqrleeIYKRLELIDaysaEARA 321
Cdd:COG1119 63 LFGERRGGEDV--WELRkriglvspaLQLRfPRDETVLDVVLSGFFDSIG-------------LYREPTDEQ----RERA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 322 ASILAGLsfspEMQKKATKTF---SGGWRMRIALARALFIEPDILLLDEPTNHLDLHA----VLWLESYLVKWPKTFIVV 394
Cdd:COG1119 124 RELLELL----GLAHLADRPFgtlSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLV 199
|
..
gi 743842931 395 SH 396
Cdd:COG1119 200 TH 201
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
175-436 |
2.50e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 61.18 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMALHAIdgiPRNCQILHVEQEVvgdDTSAlqcvlN 254
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLET---PDSGQLNIAGHQF---DFSQ-----K 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 255 SDIERTRLLEEEVRLHAQQRDLdfedaagngkgdqigaINKDAISQRLEEIYKRLELIDAYSAEARAASILAGLsfspEM 334
Cdd:COG4161 72 PSEKAIRLLRQKVGMVFQQYNL----------------WPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARL----RL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 335 QKKATK---TFSGGWRMRIALARALFIEPDILLLDEPTNHLD---LHAVLWLESYLVKWPKTFIVVSHAREFLNTVVTDI 408
Cdd:COG4161 132 TDKADRfplHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeiTAQVVEIIRELSQTGITQVIVTHEVEFARKVASQV 211
|
250 260
....*....|....*....|....*...
gi 743842931 409 LHLQGQKLTAYkGDYDTFERTREEQIKN 436
Cdd:COG4161 212 VYMEKGRIIEQ-GDASHFTQPQTEAFAH 238
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
515-656 |
2.54e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 61.64 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 515 YPGGPLMfKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVfRSAKVRI-------AVFSQHhvDGL----D 583
Cdd:PRK11248 11 YGGKPAL-EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI-TLDGKPVegpgaerGVVFQN--EGLlpwrN 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743842931 584 LSSNPLLYMMrcFPGVP----EQKLRAHLGSFGVTGNLAlQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLD 656
Cdd:PRK11248 87 VQDNVAFGLQ--LAGVEkmqrLEIAHQMLKKVGLEGAEK-RYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
191-391 |
2.57e-10 |
|
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: 60.85 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 191 VDG-SVTLSFGRHYGLVGRNGTGKTTFLRYMalhaidgiprnCQILHVeqevvgddTSALQCVLNSDIER-TRLLEEEVR 268
Cdd:cd03265 16 VRGvSFRVRRGEIFGLLGPNGAGKTTTIKML-----------TTLLKP--------TSGRATVAGHDVVRePREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 269 LHAQQRDLD-----FEDAAGNGKgdqIGAINKDAISQRLEEIYKRLELIDAysaearaasilaglsfspemQKKATKTFS 343
Cdd:cd03265 77 IVFQDLSVDdeltgWENLYIHAR---LYGVPGAERRERIDELLDFVGLLEA--------------------ADRLVKTYS 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 743842931 344 GGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPKTF 391
Cdd:cd03265 134 GGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEF 181
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
517-681 |
2.77e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 60.57 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 517 GGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQP---TSGTVFrsakvriavfsqhhVDGLDLSSNP----- 588
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVL--------------LNGRRLTALPaeqrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 589 ---LLYMMRCFP----------GVPE--------QKLRAHLGSFGVTGnLALQPMYTLSGGQKSRVAFAKITFKKPHIIL 647
Cdd:COG4136 78 igiLFQDDLLFPhlsvgenlafALPPtigraqrrARVEQALEEAGLAG-FADRDPATLSGGQRARVALLRALLAEPRALL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 743842931 648 LDEPSNHLDLD--------AVEALIQglvlFQGGILMVSHDE 681
Cdd:COG4136 157 LDEPFSKLDAAlraqfrefVFEQIRQ----RGIPALLVTHDE 194
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
536-699 |
2.98e-10 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 60.84 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 536 AMVGPNGIGKSTILKLIAGELQPTSGTVfrsakvriavfsqhHVDGLDLSSNPL--------------LY-------MMR 594
Cdd:cd03266 35 GLLGPNGAGKTTTLRMLAGLLEPDAGFA--------------TVDGFDVVKEPAearrrlgfvsdstgLYdrltareNLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 595 CFP---GVPEQKLRAHL----GSFGVtGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGL 667
Cdd:cd03266 101 YFAglyGLKGDELTARLeelaDRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFI 179
|
170 180 190
....*....|....*....|....*....|....*
gi 743842931 668 -VLFQGG--ILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:cd03266 180 rQLRALGkcILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
524-699 |
3.68e-10 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 60.82 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 524 NLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKVRIAVFSQHHVDGLDLSSNPLLYMMRCFPGV---- 599
Cdd:cd03296 20 DVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQHYALFRHMTVFDNVafgl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 600 ---------PEQKLRAH----LGSFGVTGnlaLQPMY--TLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALI 664
Cdd:cd03296 100 rvkprserpPEAEIRAKvhelLKLVQLDW---LADRYpaQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELR 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 743842931 665 QGLVLFQGGI----LMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:cd03296 177 RWLRRLHDELhvttVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
194-375 |
4.04e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 61.24 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 194 SVTLSFGRHYGLVGRNGTGKTTFLRYMalhaidgiprncqiLHVEQEVVGDdtsalQCVLNSDIerTRLLEEEVRlhAQQ 273
Cdd:PRK10419 32 SLSLKSGETVALLGRSGCGKSTLARLL--------------VGLESPSQGN-----VSWRGEPL--AKLNRAQRK--AFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 274 RD--LDFEDAagngkgdqIGAIN-KDAISQRLEEIYKRLELIDAYSAEARAASILAGLSFSPEMQKKATKTFSGGWRMRI 350
Cdd:PRK10419 89 RDiqMVFQDS--------ISAVNpRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180
....*....|....*....|....*
gi 743842931 351 ALARALFIEPDILLLDEPTNHLDLH 375
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLV 185
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
517-705 |
4.09e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 61.32 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 517 GGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF----------RS----AKVRIAVFSQHHVDGL 582
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILfdgenipamsRSrlytVRKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 583 DLSS-NPLLYMMRCFPGVPEQKLRA----HLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHIILLDEP---SNH 654
Cdd:PRK11831 98 DMNVfDNVAYPLREHTQLPAPLLHStvmmKLEAVGLRGAAKLMPS-ELSGGMARRAALARAIALEPDLIMFDEPfvgQDP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 743842931 655 LDLDAVEALIQGLVLFQG-GILMVSHDEHLISGSVDELWVVSQGKVTPfHGT 705
Cdd:PRK11831 177 ITMGVLVKLISELNSALGvTCVVVSHDVPEVLSIADHAYIVADKKIVA-HGS 227
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
535-667 |
4.44e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.80 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 535 IAMVGPNGIGKSTILK----LIAGELQPTS------GTVFRSAK----VRIA------VFSQHH-VDGLDLSSNPLLYMM 593
Cdd:PRK09984 33 VALLGPSGSGKSTLLRhlsgLITGDKSAGShiellgRTVQREGRlardIRKSrantgyIFQQFNlVNRLSVLENVLIGAL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 594 RCFP--------GVPEQKLRAH--LGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEAL 663
Cdd:PRK09984 113 GSTPfwrtcfswFTREQKQRALqaLTRVGMV-HFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIV 191
|
....
gi 743842931 664 IQGL 667
Cdd:PRK09984 192 MDTL 195
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
177-373 |
4.74e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 61.66 E-value: 4.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 177 LENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMAlhaidGI--PRNCQILhveqeVVGDDtsalqcVLN 254
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVA-----GLekPTEGQIF-----IDGED------VTH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 255 SDIertrlleeevrlhaQQRD--LDFEDAA---GNGKGDQIG------AINKDAISQRLEEIykrLELIDaysaearaas 323
Cdd:PRK11432 73 RSI--------------QQRDicMVFQSYAlfpHMSLGENVGyglkmlGVPKEERKQRVKEA---LELVD---------- 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 743842931 324 iLAGlsfspeMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:PRK11432 126 -LAG------FEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
516-699 |
4.94e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 62.55 E-value: 4.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 516 PGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELqPTSGtvfrSAKVRIAVFSQhhvdgLDLSS--------- 586
Cdd:PRK11174 360 PDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQG----SLKINGIELRE-----LDPESwrkhlswvg 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 587 -NPLLY---------MMRcfPGVPEQKLRAHLGSFGVTGNLALQP----------MYTLSGGQKSRVAFAKITFKKPHII 646
Cdd:PRK11174 430 qNPQLPhgtlrdnvlLGN--PDASDEQLQQALENAWVSEFLPLLPqgldtpigdqAAGLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 647 LLDEPSNHLDLDAVEALIQGL--VLFQGGILMVSHD-EHLIsgSVDELWVVSQGKV 699
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQALnaASRRQTTLMVTHQlEDLA--QWDQIWVMQDGQI 561
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
343-418 |
5.20e-10 |
|
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: 59.91 E-value: 5.20e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKW--PKTFIVVSHAREFLnTVVTDILHLQGQKLTA 418
Cdd:cd03245 142 SGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSLL-DLVDRIIVMDSGRIVA 218
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
504-656 |
5.20e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 61.89 E-value: 5.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 504 PIISFSDASFGYPGGPLMfKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLD 583
Cdd:PRK09452 13 PLVELRGISKSFDGKEVI-SNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM--------------LDGQD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 584 LSSNP--------------LLYMMRCFPGV---------PEQKLRA---------HLGSFgvtgnlALQPMYTLSGGQKS 631
Cdd:PRK09452 78 ITHVPaenrhvntvfqsyaLFPHMTVFENVafglrmqktPAAEITPrvmealrmvQLEEF------AQRKPHQLSGGQQQ 151
|
170 180
....*....|....*....|....*
gi 743842931 632 RVAFAKITFKKPHIILLDEPSNHLD 656
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALD 176
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
343-409 |
5.93e-10 |
|
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: 58.74 E-value: 5.93e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVK----WPKTFIVVSHAREFLNTVVTDIL 409
Cdd:cd03229 102 SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSlqaqLGITVVLVTHDLDEAARLADRVV 172
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
175-396 |
6.11e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 61.78 E-value: 6.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRymalhAIDGI--PRNCQILhveqeVVGDDTSALQcv 252
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLR-----AINGTltPTAGTVL-----VAGDDVEALS-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 253 lnsdierTRLLEEEVRLHAQQRDLDFEdaagnGKGDQIGAINKDAISQRLEEiykrleLIDAYSAEARAASILAGLSfsp 332
Cdd:PRK09536 72 -------ARAASRRVASVPQDTSLSFE-----FDVRQVVEMGRTPHRSRFDT------WTETDRAAVERAMERTGVA--- 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743842931 333 EMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDL-HAVLWLESY--LVKWPKTFIVVSH 396
Cdd:PRK09536 131 QFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDInHQVRTLELVrrLVDDGKTAVAAIH 197
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
506-699 |
6.87e-10 |
|
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: 59.89 E-value: 6.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYpGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAG-----ELQPTSGTVFRSAKvriavfsqhhvD 580
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGK-----------D 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 581 GLDLSSNPLLYMMRC---------FPG-------------------VPEQKLRAHLGSFGVTGNLALQPM-YTLSGGQKS 631
Cdd:cd03260 69 IYDLDVDVLELRRRVgmvfqkpnpFPGsiydnvayglrlhgiklkeELDERVEEALRKAALWDEVKDRLHaLGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743842931 632 RVAFAKITFKKPHIILLDEPSNHLDLDA---VEALIQGLVLfQGGILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPIStakIEELIAELKK-EYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
318-373 |
7.52e-10 |
|
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: 62.01 E-value: 7.52e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 318 EARAASILAGLSFSPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:COG4172 402 RARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
505-699 |
8.08e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 60.39 E-value: 8.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 505 IISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDL 584
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVL--------------VSGIDT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 585 SSNPLLYMMRCFPGV----PEQKLRAHLG----SFGvTGNLALQPM-----------------------YTLSGGQKSRV 633
Cdd:PRK13644 67 GDFSKLQGIRKLVGIvfqnPETQFVGRTVeedlAFG-PENLCLPPIeirkrvdralaeiglekyrhrspKTLSGGQGQCV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 634 AFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLV-LFQGG--ILMVSHD-EHLisGSVDELWVVSQGKV 699
Cdd:PRK13644 146 ALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKkLHEKGktIVYITHNlEEL--HDADRIIVMDRGKI 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
317-396 |
8.37e-10 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 60.10 E-value: 8.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 317 AEARAASILA--GLSfspEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD------LHAVL---WLESylv 385
Cdd:COG1116 115 RRERARELLElvGLA---GFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDaltrerLQDELlrlWQET--- 188
|
90
....*....|.
gi 743842931 386 kwPKTFIVVSH 396
Cdd:COG1116 189 --GKTVLFVTH 197
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
537-680 |
1.26e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 59.30 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 537 MVGPNGIGKSTILKLIAGELQPTSG------------TVFRSAKVRIaVFSQHHVDGLDLSSNPlLYMMRcFPGVPEQKL 604
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeilDEFRGSELQN-YFTKLLEGDVKVIVKP-QYVDL-IPKAVKGKV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 605 RAHLGSFGVTGN-------LALQPMY-----TLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLD---AVEALIQGLVL 669
Cdd:cd03236 108 GELLKKKDERGKldelvdqLELRHVLdrnidQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlNAARLIRELAE 187
|
170
....*....|.
gi 743842931 670 FQGGILMVSHD 680
Cdd:cd03236 188 DDNYVLVVEHD 198
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
175-399 |
1.30e-09 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 60.55 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDgsVTLSF--GRHYGLVGRNGTGKTTFLRymalhAIDGI--PRNCQILHVEQEVVgddtsalq 250
Cdd:COG1118 3 IEVRNISKRFGSFTLLDD--VSLEIasGELVALLGPSGSGKTTLLR-----IIAGLetPDSGRIVLNGRDLF-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 251 cvlnsdiertrlleeeVRLHAQQRD--LDFEDAA--------GN-GKGDQIGAINKDAISQRLEEIykrLELIDAYSAEA 319
Cdd:COG1118 68 ----------------TNLPPRERRvgFVFQHYAlfphmtvaENiAFGLRVRPPSKAEIRARVEEL---LELVQLEGLAD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 320 RAASILaglsfspemqkkatktfSGGWRMRIALARALFIEPDILLLDEPTNHLD--LHAVL--WLESYLVKWPKTFIVVS 395
Cdd:COG1118 129 RYPSQL-----------------SGGQRQRVALARALAVEPEVLLLDEPFGALDakVRKELrrWLRRLHDELGGTTVFVT 191
|
....
gi 743842931 396 HARE 399
Cdd:COG1118 192 HDQE 195
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
505-684 |
1.84e-09 |
|
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: 60.92 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 505 IISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIaGELQPT-SGTVFRSAKVRIAVFSQHHVDGLD 583
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVyGGRLTKPAKGKLFYVPQRPYMTLG 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 584 LSSNPLLYMMRCFP----GVPEQKLRAHLGSFGVTGNL-------ALQP-MYTLSGGQKSRVAFAKITFKKPHIILLDEP 651
Cdd:TIGR00954 530 TLRDQIIYPDSSEDmkrrGLSDKDLEQILDNVQLTHILereggwsAVQDwMDVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170 180 190
....*....|....*....|....*....|...
gi 743842931 652 SNHLDLDAVEALIQGLVLFQGGILMVSHDEHLI 684
Cdd:TIGR00954 610 TSAVSVDVEGYMYRLCREFGITLFSVSHRKSLW 642
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
539-705 |
1.86e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 58.50 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 539 GPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDLSSNPL----------------------------- 589
Cdd:COG1137 36 GPNGAGKTTTFYMIVGLVKPDSGRIF--------------LDGEDITHLPMhkrarlgigylpqeasifrkltvednila 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 590 -LYMMRCFPGVPEQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEAlIQGLV 668
Cdd:COG1137 102 vLELRKLSKKEREERLEELLEEFGIT-HLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVAD-IQKII 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 743842931 669 LF---QG-GILMVSHDEHLISGSVDELWVVSQGKVTpFHGT 705
Cdd:COG1137 180 RHlkeRGiGVLITDHNVRETLGICDRAYIISEGKVL-AEGT 219
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
341-418 |
1.96e-09 |
|
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: 60.55 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 341 TFSGGWRMRIALARALFIEPDILLLDEPTNHLDL---HAVLwleSYLVKW--PKTFIVVSHAREFLNTVvtD-ILHLQGQ 414
Cdd:COG4987 471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAateQALL---ADLLEAlaGRTVLLITHRLAGLERM--DrILVLEDG 545
|
....
gi 743842931 415 KLTA 418
Cdd:COG4987 546 RIVE 549
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
317-405 |
2.21e-09 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 57.92 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 317 AEARAASILA--GLSfspEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD---LHAVLWLESYLVKWPKTF 391
Cdd:cd03262 112 AEERALELLEkvGLA---DKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpelVGEVLDVMKDLAEEGMTM 188
|
90
....*....|....*...
gi 743842931 392 IVVSH----AREFLNTVV 405
Cdd:cd03262 189 VVVTHemgfAREVADRVI 206
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
526-700 |
2.64e-09 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 59.73 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 526 NFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTV-------FRSAKV--------RIA-VFSQH----HvdgLDLS 585
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIrlggevlQDSARGiflpphrrRIGyVFQEArlfpH---LSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 586 SNpLLYMMRcFPGVPEQKLR----------AHLgsfgvtgnLALQPMyTLSGGQKSRVAFAKITFKKPHIILLDEPSNHL 655
Cdd:COG4148 96 GN-LLYGRK-RAPRAERRISfdevvellgiGHL--------LDRRPA-TLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 743842931 656 D-------LDAVEALIQGLVLfqgGILMVSHdehlisgSVDE-------LWVVSQGKVT 700
Cdd:COG4148 165 DlarkaeiLPYLERLRDELDI---PILYVSH-------SLDEvarladhVVLLEQGRVV 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
176-396 |
2.81e-09 |
|
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: 57.69 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 176 HLENFNISVggrDLIVDGSVTlsfgrhyGLVGRNGTGKTTFLRYMA-LHAIDGiprncqilhveQEVVGDDTsalqcVLN 254
Cdd:cd03297 9 RLPDFTLKI---DFDLNEEVT-------GIFGASGAGKSTLLRCIAgLEKPDG-----------GTIVLNGT-----VLF 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 255 SDiertrllEEEVRLHAQQRdldfedaagngkgdQIGAINKDA-------ISQRLEEIYKRLElidaySAEAR--AASIL 325
Cdd:cd03297 63 DS-------RKKINLPPQQR--------------KIGLVFQQYalfphlnVRENLAFGLKRKR-----NREDRisVDELL 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743842931 326 AGLSFSPeMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPKTF----IVVSH 396
Cdd:cd03297 117 DLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLnipvIFVTH 190
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
186-399 |
2.94e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 59.05 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 186 GRDLIVDGsvtLSF----GRHYGLVGRNGTGKTTFLRyMALhaidGIprncqilhveqevVGDDTSALQCVLNSDIERTR 261
Cdd:PRK13537 18 GDKLVVDG---LSFhvqrGECFGLLGPNGAGKTTTLR-MLL----GL-------------THPDAGSISLCGEPVPSRAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 262 lleeevrlHAQQRdldfedaagNGKGDQIGAINKD-AISQRLEeIYKRLELIDAYSAEARAASILaglSFSPEMQKKATK 340
Cdd:PRK13537 77 --------HARQR---------VGVVPQFDNLDPDfTVRENLL-VFGRYFGLSAAAARALVPPLL---EFAKLENKADAK 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743842931 341 T--FSGGWRMRIALARALFIEPDILLLDEPTNHLDLHA--VLW--LESYLVKwPKTFIVVSHARE 399
Cdd:PRK13537 136 VgeLSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQArhLMWerLRSLLAR-GKTILLTTHFME 199
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
119-399 |
3.24e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 59.07 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 119 LTERDKMKIERRkRKDERQREAQYQIHLAEMEA-VRAGMPVAcvthdgggggpnvkdIHLENFNISVGGRDLIVDGSVTL 197
Cdd:PRK13536 1 LLTRAVAEEAPR-RLELSPIERKHQGISEAKASiPGSMSTVA---------------IDLAGVSKSYGDKAVVNGLSFTV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 198 SFGRHYGLVGRNGTGKTTFLRymalhaidgiprncQILHVEQEVVGDDTsalqcVLNSDI-ERTRLLEEEVRLHAQQRDL 276
Cdd:PRK13536 65 ASGECFGLLGPNGAGKSTIAR--------------MILGMTSPDAGKIT-----VLGVPVpARARLARARIGVVPQFDNL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 277 DFEDAAGN-----GKGDQIGAINKDAISQRLEEiYKRLElidaYSAEARAASIlaglsfspemqkkatktfSGGWRMRIA 351
Cdd:PRK13536 126 DLEFTVREnllvfGRYFGMSTREIEAVIPSLLE-FARLE----SKADARVSDL------------------SGGMKRRLT 182
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 743842931 352 LARALFIEPDILLLDEPTNHLDLHA--VLW--LESYLVKwPKTFIVVSHARE 399
Cdd:PRK13536 183 LARALINDPQLLILDEPTTGLDPHArhLIWerLRSLLAR-GKTILLTTHFME 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
175-417 |
4.26e-09 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 57.37 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDGsVTLSFGR---HYgLVGRNGTGKTTFLR--YMALHAIDGiprncQILhveqeVVGDDTSAL 249
Cdd:COG2884 2 IRFENVSKRYPGGREALSD-VSLEIEKgefVF-LTGPSGAGKSTLLKllYGEERPTSG-----QVL-----VNGQDLSRL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 250 QcvlNSDIERTRlleeevrlhaqqRdldfedaagngkgdQIGAINKDaisQRLeeIYKR---------LELIDAYSAEA- 319
Cdd:COG2884 70 K---RREIPYLR------------R--------------RIGVVFQD---FRL--LPDRtvyenvalpLRVTGKSRKEIr 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 320 -RAASILA--GLSfspemqKKATK---TFSGGWRMRIALARALFIEPDILLLDEPTNHLD-------------LHAVlwl 380
Cdd:COG2884 116 rRVREVLDlvGLS------DKAKAlphELSGGEQQRVAIARALVNRPELLLADEPTGNLDpetsweimelleeINRR--- 186
|
250 260 270
....*....|....*....|....*....|....*..
gi 743842931 381 esylvkwPKTFIVVSHAREFLNTVVTDILHLQGQKLT 417
Cdd:COG2884 187 -------GTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
495-711 |
4.56e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.99 E-value: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 495 PTPDDRPGAPIISFSDASFGYPG---GPLMfKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQP--TSGTVFR---- 565
Cdd:PLN03232 604 QNPPLQPGAPAISIKNGYFSWDSktsKPTL-SDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaeTSSVVIRgsva 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 566 ---------SAKVRIAVF------SQHHVDGLDLSSnpLLYMMRCFPGvpeqKLRAHLGSFGVTgnlalqpmytLSGGQK 630
Cdd:PLN03232 683 yvpqvswifNATVRENILfgsdfeSERYWRAIDVTA--LQHDLDLLPG----RDLTEIGERGVN----------ISGGQK 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 631 SRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVL--FQGGI-LMVSHDEHLISgSVDELWVVSQGKVTPfHGTFL 707
Cdd:PLN03232 747 QRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKdeLKGKTrVLVTNQLHFLP-LMDRIILVSEGMIKE-EGTFA 824
|
....
gi 743842931 708 DYKK 711
Cdd:PLN03232 825 ELSK 828
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
309-373 |
5.38e-09 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 57.06 E-value: 5.38e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743842931 309 LELIDAYSAEARAASILA--GLSfspEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:COG4181 115 LELAGRRDARARARALLErvGLG---HRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLD 178
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
495-665 |
5.99e-09 |
|
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: 59.06 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 495 PTPDDRPGAP-------IISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsa 567
Cdd:COG5265 340 PEVADAPDAPplvvgggEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIL--- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 568 kvriavfsqhhVDGLDLSSNPLLYMMRC----------F------------PGVPEQKLR-----AHLGSF------G-- 612
Cdd:COG5265 417 -----------IDGQDIRDVTQASLRAAigivpqdtvlFndtiayniaygrPDASEEEVEaaaraAQIHDFieslpdGyd 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 743842931 613 -VTGNLALQpmytLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDlDAVEALIQ 665
Cdd:COG5265 486 tRVGERGLK----LSGGEKQRVAIARTLLKNPPILIFDEATSALD-SRTERAIQ 534
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
185-373 |
6.50e-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: 57.06 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 185 GGRDLIVDGSVTLSF--GRHYGLVGRNGTGKTTFLRymalhaidgiprncqilhveqevvgddtsalqCvlnsdIERTRL 262
Cdd:COG4778 20 GGKRLPVLDGVSFSVaaGECVALTGPSGAGKSTLLK--------------------------------C-----IYGNYL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 263 LEE-EVRLHAQQRDLDFEDAAGngkgDQIGAINKDAI---SQRLEEIyKR---LEL---------IDAYSAEARAASILA 326
Cdd:COG4778 63 PDSgSILVRHDGGWVDLAQASP----REILALRRRTIgyvSQFLRVI-PRvsaLDVvaepllergVDREEARARARELLA 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 743842931 327 GLSFSPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:COG4778 138 RLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLD 184
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
174-396 |
6.78e-09 |
|
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: 59.00 E-value: 6.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 174 DIHLENFNISVGGRDLIVDGsVTLSF--GRHYGLVGRNGTGKTTFLRYMA--LHAIDGiprncQILhveqevvgddtsal 249
Cdd:COG4988 336 SIELEDVSFSYPGGRPALDG-LSLTIppGERVALVGPSGAGKSTLLNLLLgfLPPYSG-----SIL-------------- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 250 qcvLNsDIERTRLLEEEVRlhaqqrdldfedaagngkgDQIGAInkdaiSQR-------LEE-IykRLELIDAYSAEARA 321
Cdd:COG4988 396 ---IN-GVDLSDLDPASWR-------------------RQIAWV-----PQNpylfagtIREnL--RLGRPDASDEELEA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 322 ASILAGL-SFSPEMQKK-ATK------TFSGGWRMRIALARALFIEPDILLLDEPTNHLDLH--AVLW--LESYLVKwpK 389
Cdd:COG4988 446 ALEAAGLdEFVAALPDGlDTPlgeggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAEteAEILqaLRRLAKG--R 523
|
....*..
gi 743842931 390 TFIVVSH 396
Cdd:COG4988 524 TVILITH 530
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
340-396 |
7.13e-09 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 56.96 E-value: 7.13e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743842931 340 KTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPK----TFIVVSH 396
Cdd:cd03299 128 ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKefgvTVLHVTH 188
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
317-375 |
7.76e-09 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 58.19 E-value: 7.76e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743842931 317 AEARAASILA--GLSfspEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLH 375
Cdd:COG3842 112 IRARVAELLElvGLE---GLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAK 169
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
535-684 |
9.35e-09 |
|
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: 54.69 E-value: 9.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 535 IAMVGPNGIGKSTILKLIAGELQPTSGTVFRsakvriavfsqhhVDGLDLSSNPLLYMMrcfpgvpeqklrahlgsfgvt 614
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGVIY-------------IDGEDILEEVLDQLL--------------------- 50
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 615 GNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVLFQGGILMVSHDEHLI 684
Cdd:smart00382 51 LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVI 120
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
137-413 |
9.35e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 58.67 E-value: 9.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 137 QREAQYQIHLAEMEAVRAGMPVACVTHDGGgggpnvkdIHLENFNISV-GGRDLIVDGSVTLSFGRHYGLVGRNGTGKTT 215
Cdd:COG4178 333 DRLAGFEEALEAADALPEAASRIETSEDGA--------LALEDLTLRTpDGRPLLEDLSLSLKPGERLLITGPSGSGKST 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 216 FLRymalhAIDGI----------PRNCQILHVEQevvgddtsalqcvlnsdieRTRLLEeeVRLHAQ----QRDLDFEDA 281
Cdd:COG4178 405 LLR-----AIAGLwpygsgriarPAGARVLFLPQ-------------------RPYLPL--GTLREAllypATAEAFSDA 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 282 AgngkgdqigainkdaISQRLEEIykRLE-LIDAYSAEARAASILaglsfspemqkkatktfSGGWRMRIALARALFIEP 360
Cdd:COG4178 459 E---------------LREALEAV--GLGhLAERLDEEADWDQVL-----------------SLGEQQRLAFARLLLHKP 504
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 743842931 361 DILLLDEPTNHLDLHAVLWLESYLVK-WPK-TFIVVSHaREFLNTVVTDILHLQG 413
Cdd:COG4178 505 DWLFLDEATSALDEENEAALYQLLREeLPGtTVISVGH-RSTLAAFHDRVLELTG 558
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
536-680 |
9.62e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 56.63 E-value: 9.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 536 AMVGPNGIGKSTILKLIAGELQPTSGTVfrsakvriavfsqhHVDGLDLSSNP---------LL-----YMMRC------ 595
Cdd:COG4604 31 ALIGPNGAGKSTLLSMISRLLPPDSGEV--------------LVDGLDVATTPsrelakrlaILrqenhINSRLtvrelv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 596 ----FP---GVPEQKLRAH----LGSFGVTgnlALQPMY--TLSGGQKSR--VA--FAKITfkkpHIILLDEPSNHLDLD 658
Cdd:COG4604 97 afgrFPyskGRLTAEDREIideaIAYLDLE---DLADRYldELSGGQRQRafIAmvLAQDT----DYVLLDEPLNNLDMK 169
|
170 180
....*....|....*....|....*.
gi 743842931 659 -AVE--ALIQGLVLFQG-GILMVSHD 680
Cdd:COG4604 170 hSVQmmKLLRRLADELGkTVVIVLHD 195
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
523-699 |
9.89e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.11 E-value: 9.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 523 KNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTV-------------FRSAKVRIaVFS---------QHHVD 580
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliddhplhfgdysYRSQRIRM-IFQdpstslnprQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 581 GLDLssnPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAV 660
Cdd:PRK15112 109 ILDF---PLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 743842931 661 EALIQGLVLFQG--GILMVSHDEHL-----ISgsvDELWVVSQGKV 699
Cdd:PRK15112 186 SQLINLMLELQEkqGISYIYVTQHLgmmkhIS---DQVLVMHQGEV 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
205-417 |
1.11e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 56.25 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 205 LVGRNGTGKTTFLRYM-ALHAIDGiprncqilhveQEVVGDDTSAlqcvlNSDIERTRLLEEEVRLHAQQRDLdFEdaag 283
Cdd:PRK09493 32 IIGPSGSGKSTLLRCInKLEEITS-----------GDLIVDGLKV-----NDPKVDERLIRQEAGMVFQQFYL-FP---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 284 ngkgdQIGAINKDAISQRLEEIYKRLElidaysAEARAASILAGLSFSPEMQKKATKtFSGGWRMRIALARALFIEPDIL 363
Cdd:PRK09493 91 -----HLTALENVMFGPLRVRGASKEE------AEKQARELLAKVGLAERAHHYPSE-LSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743842931 364 LLDEPTNHLD---LHAVLWLESYLVKWPKTFIVVSHAREFLNTVVTDILHLQGQKLT 417
Cdd:PRK09493 159 LFDEPTSALDpelRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
175-416 |
1.27e-08 |
|
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: 55.96 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDL---IVDGsVTLSF--GRHYGLVGRNGTGKTTFLRYMALhaidgiprncqILHV---EQEVVGDDT 246
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKG-VSLSIekGEFVAIVGPSGSGKSTLLNILGG-----------LDRPtsgEVRVDGTDI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 247 SALqcvlnSDIERTRLLEEEVRLHAQQ----RDLDFEDaagNGK-GDQIGAINKDAISQRLEEIYKRLELIDAysAEARA 321
Cdd:cd03255 69 SKL-----SEKELAAFRRRHIGFVFQSfnllPDLTALE---NVElPLLLAGVPKKERRERAEELLERVGLGDR--LNHYP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 322 AsilaglsfspEMqkkatktfSGGWRMRIALARALFIEPDILLLDEPTNHLDLH---AVLWLESYLVKWP-KTFIVVSHA 397
Cdd:cd03255 139 S----------EL--------SGGQQQRVAIARALANDPKIILADEPTGNLDSEtgkEVMELLRELNKEAgTTIVVVTHD 200
|
250
....*....|....*....
gi 743842931 398 REFLNTvVTDILHLQGQKL 416
Cdd:cd03255 201 PELAEY-ADRIIELRDGKI 218
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
523-665 |
1.29e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 57.02 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 523 KNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTV----FRSAKVRIA-------VF---SQhhvdgL--DLss 586
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVrvlgYVPFKRRKEfarrigvVFgqrSQ-----LwwDL-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 587 nPL---LYMMRCFPGVPEQKLRAHLGSF----GVtGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDA 659
Cdd:COG4586 112 -PAidsFRLLKAIYRIPDAEYKKRLDELvellDL-GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
....*.
gi 743842931 660 VEALIQ 665
Cdd:COG4586 190 KEAIRE 195
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
168-404 |
1.39e-08 |
|
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: 57.89 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 168 GGPNVKDIHLENFNISVGgRDLI--VDG-SVTLSFGRHYGLVGRNGTGKTTFLRYMAlhaidGIprncqILHVEQEV--- 241
Cdd:TIGR03269 276 GEPIIKVRNVSKRYISVD-RGVVkaVDNvSLEVKEGEIFGIVGTSGAGKTTLSKIIA-----GV-----LEPTSGEVnvr 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 242 VGDDTsaLQCVLNSDIERTR------LLEEEVRLHAQQRDLDfedaagngkgdqigaiN-KDAISqrleeiykrLELIDA 314
Cdd:TIGR03269 345 VGDEW--VDMTKPGPDGRGRakryigILHQEYDLYPHRTVLD----------------NlTEAIG---------LELPDE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 315 YsAEARAASILAGLSFSPEMQK----KATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD-----------LHAVLW 379
Cdd:TIGR03269 398 L-ARMKAVITLKMVGFDEEKAEeildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkvdvthsiLKAREE 476
|
250 260
....*....|....*....|....*
gi 743842931 380 LEsylvkwpKTFIVVSHAREFLNTV 404
Cdd:TIGR03269 477 ME-------QTFIIVSHDMDFVLDV 494
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
530-708 |
1.46e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.37 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 530 DLDSRI------AMVGPNGIGKSTILKLIAGELqpTSGTVFRSAKVR---------------------IAVFSQHHVDGL 582
Cdd:PRK13547 19 DLSLRIepgrvtALLGRNGAGKSTLLKALAGDL--TGGGAPRGARVTgdvtlngeplaaidaprlarlRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 583 DLSSNPLLyMMRCFPGVPEQKLRAH---------LGSFGVTGnLALQPMYTLSGGQKSRVAFAKI---------TFKKPH 644
Cdd:PRK13547 97 AFSAREIV-LLGRYPHARRAGALTHrdgeiawqaLALAGATA-LVGRDVTTLSGGELARVQFARVlaqlwpphdAAQPPR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743842931 645 IILLDEPSNHLD-------LDAVEALIQGlvlFQGGILMVSHDEHLISGSVDELWVVSQGKVTPfHGTFLD 708
Cdd:PRK13547 175 YLLLDEPTAALDlahqhrlLDTVRRLARD---WNLGVLAIVHDPNLAARHADRIAMLADGAIVA-HGAPAD 241
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
528-680 |
1.47e-08 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 56.16 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 528 GIDLD----SRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDLSSnpllymmrcfPGVPEQK 603
Cdd:COG1126 19 GISLDvekgEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIT--------------VDGEDLTD----------SKKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 604 LRAHLG----SFG------VTGNLALQPMY-------------------------------TLSGGQKSRVAFAKITFKK 642
Cdd:COG1126 75 LRRKVGmvfqQFNlfphltVLENVTLAPIKvkkmskaeaeeramellervgladkadaypaQLSGGQQQRVAIARALAME 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 743842931 643 PHIILLDEPSNHLD---LDAVEALIQGLVlfQGGI--LMVSHD 680
Cdd:COG1126 155 PKVMLFDEPTSALDpelVGEVLDVMRDLA--KEGMtmVVVTHE 195
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
194-396 |
1.51e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 56.63 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 194 SVTLSFGRHYGLVGRNGTGKTTFLRYM-ALHaidgIPRNCQILHV-EQEVVGDDTSALQCVLNSD-IERTRlleeeVRLH 270
Cdd:PRK13651 27 SVEINQGEFIAIIGQTGSGKTTFIEHLnALL----LPDTGTIEWIfKDEKNKKKTKEKEKVLEKLvIQKTR-----FKKI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 271 AQQRDLDfedaagngkgDQIGAINKDAISQRLEE-IYKRLEL------IDAYSAEARAASILAGLSFSPEMQKKATKTFS 343
Cdd:PRK13651 98 KKIKEIR----------RRVGVVFQFAEYQLFEQtIEKDIIFgpvsmgVSKEEAKKRAAKYIELVGLDESYLQRSPFELS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 344 GGWRMRIALARALFIEPDILLLDEPTNHLDLHAV---LWLESYLVKWPKTFIVVSH 396
Cdd:PRK13651 168 GGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVkeiLEIFDNLNKQGKTIILVTH 223
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
506-699 |
1.58e-08 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 55.58 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGY-PGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVfrsakvriavfsqhHVDGLDL 584
Cdd:cd03244 3 IEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSI--------------LIDGVDI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 585 SSNPLLYMMRCFPGVP---------------------EQKL-----RAHLGSFGVTGNLALQPMYT-----LSGGQKSRV 633
Cdd:cd03244 69 SKIGLHDLRSRISIIPqdpvlfsgtirsnldpfgeysDEELwqaleRVGLKEFVESLPGGLDTVVEeggenLSVGQRQLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743842931 634 AFAKITFKKPHIILLDEPSNHLDlDAVEALIQGLV---LFQGGILMVSHDEHLISGSvDELWVVSQGKV 699
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVD-PETDALIQKTIreaFKDCTVLTIAHRLDTIIDS-DRILVLDKGRV 215
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
528-680 |
1.65e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 55.91 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 528 GIDLDSR----IAMVGPNGIGKSTILKLIAGELQPTSGTV------------FRSAKVRIAVFSQH------------HV 579
Cdd:PRK11264 21 GIDLEVKpgevVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidtarsLSQQKGLIRQLRQHvgfvfqnfnlfpHR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 580 DGLD-LSSNPLLymmrcFPGVP----EQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHIILLDEPSNH 654
Cdd:PRK11264 101 TVLEnIIEGPVI-----VKGEPkeeaTARARELLAKVGLAGKETSYPR-RLSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180
....*....|....*....|....*....
gi 743842931 655 LDLDAV-EAL--IQGLVLFQGGILMVSHD 680
Cdd:PRK11264 175 LDPELVgEVLntIRQLAQEKRTMVIVTHE 203
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
317-373 |
1.91e-08 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 55.47 E-value: 1.91e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 743842931 317 AEARAASILAGLSFSPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:TIGR02324 125 ARARARELLARLNIPERLWHLPPATFSGGEQQRVNIARGFIADYPILLLDEPTASLD 181
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
524-656 |
2.05e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.63 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 524 NLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSG-------TVFR-SAKVRIA--VFsQHHVdgldlssnpLLYMM 593
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGhirfhgtDVSRlHARDRKVgfVF-QHYA---------LFRHM 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743842931 594 RCFPGVP--------EQKLRAHLGSFGVT--------GNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLD 656
Cdd:PRK10851 90 TVFDNIAfgltvlprRERPNAAAIKAKVTqllemvqlAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
329-416 |
2.15e-08 |
|
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: 55.17 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 329 SFSPEMQK-------KATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWP--KTFIVVSHAre 399
Cdd:cd03248 131 SFISELASgydtevgEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPerRTVLVIAHR-- 208
|
90
....*....|....*....
gi 743842931 400 fLNTV--VTDILHLQGQKL 416
Cdd:cd03248 209 -LSTVerADQILVLDGGRI 226
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
175-367 |
2.69e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 54.63 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDGSVTLsfgrhygLVGRNGTGKTTFLRYMALhAIDGIPRNCQILHVEQEVVGDDTSALQCVLN 254
Cdd:COG0419 5 LRLENFRSYRDTETIDFDDGLNL-------IVGPNGAGKSTILEAIRY-ALYGKARSRSKLRSDLINVGSEEASVELEFE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 255 SDIERTRLleeeVRlhAQQRDLDFEDAAGNGKGDQIGAINKDAISQRLEEIYKRL-ELIDAYSAEARAASILAGLSFSPE 333
Cdd:COG0419 77 HGGKRYRI----ER--RQGEFAEFLEAKPSERKEALKRLLGLEIYEELKERLKELeEALESALEELAELQKLKQEILAQL 150
|
170 180 190
....*....|....*....|....*....|....
gi 743842931 334 MQKKATKTFSGGWRMRIALARALFIEPDILLLDE 367
Cdd:COG0419 151 SGLDPIETLSGGERLRLALADLLSLILDFGSLDE 184
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
495-691 |
2.92e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 56.89 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 495 PTPDDRPGAP-------IISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTvfrsa 567
Cdd:PRK13657 317 PDVRDPPGAIdlgrvkgAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGR----- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 568 kVRIavfsqhhvDGLDLSS---------------NPLLyMMRCF--------PGVPEQKLRAHLGSFGVTGNLALQPM-- 622
Cdd:PRK13657 392 -ILI--------DGTDIRTvtraslrrniavvfqDAGL-FNRSIednirvgrPDATDEEMRAAAERAQAHDFIERKPDgy 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 623 --------YTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDL-------DAVEALIQGLVLF----------QGGILMV 677
Cdd:PRK13657 462 dtvvgergRQLSGGERQRLAIARALLKDPPILILDEATSALDVeteakvkAALDELMKGRTTFiiahrlstvrNADRILV 541
|
250
....*....|....*
gi 743842931 678 SHDEHLI-SGSVDEL 691
Cdd:PRK13657 542 FDNGRVVeSGSFDEL 556
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
517-656 |
2.99e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 56.19 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 517 GGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF----RSAKVRIA------VFSQH----HVD-- 580
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFigekRMNDVPPAergvgmVFQSYalypHLSva 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 581 -----GLDLSSNPLLYMMRCFPGVPEQKLRAHLgsfgvtgnLALQPMyTLSGGQKSRVAFAKITFKKPHIILLDEPSNHL 655
Cdd:PRK11000 94 enmsfGLKLAGAKKEEINQRVNQVAEVLQLAHL--------LDRKPK-ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
.
gi 743842931 656 D 656
Cdd:PRK11000 165 D 165
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
522-656 |
3.54e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.58 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 522 FKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGEL--QPTSGTVfrsaKVRIAVFSQHH--VDGLDLSSNPLlymmrcfp 597
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCV----DVPDNQFGREAslIDAIGRKGDFK-------- 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 598 gvpeQKLRAhLGSFGVTGN-LALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLD 656
Cdd:COG2401 114 ----DAVEL-LNAVGLSDAvLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
200-373 |
4.60e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 54.68 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 200 GRHYGLVGRNGTGKTTFLRYMAlhaidGI--PRNCQILhveqevvgddtsALQCVLNSDIERTRLLEEEVRLHAQQRDLD 277
Cdd:PRK11247 38 GQFVAVVGRSGCGKSTLLRLLA-----GLetPSAGELL------------AGTAPLAEAREDTRLMFQDARLLPWKKVID 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 278 fedAAGNG-KGDQigainKDAISQRLEeiykrlelidAYSAEARAASILAGLSfspemqkkatktfsGGWRMRIALARAL 356
Cdd:PRK11247 101 ---NVGLGlKGQW-----RDAALQALA----------AVGLADRANEWPAALS--------------GGQKQRVALARAL 148
|
170
....*....|....*..
gi 743842931 357 FIEPDILLLDEPTNHLD 373
Cdd:PRK11247 149 IHRPGLLLLDEPLGALD 165
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
536-699 |
4.71e-08 |
|
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: 54.21 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 536 AMVGPNGIGKSTILKLIAGELQPTSGTV-FRSAKVRIAVfsQHHVD------GL--DLS-SNPLLYMMRcFPGVPEQKLR 605
Cdd:cd03269 30 GLLGPNGAGKTTTIRMILGIILPDSGEVlFDGKPLDIAA--RNRIGylpeerGLypKMKvIDQLVYLAQ-LKGLKKEEAR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 606 AH----LGSFGVtGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLD---LDAVEALIQGLVLFQGGILMVS 678
Cdd:cd03269 107 RRidewLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDpvnVELLKDVIRELARAGKTVILST 185
|
170 180
....*....|....*....|.
gi 743842931 679 HDEHLISGSVDELWVVSQGKV 699
Cdd:cd03269 186 HQMELVEELCDRVLLLNKGRA 206
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
175-373 |
5.24e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 55.48 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMAlhaidGIprncqilhvEQEVVGddtsalqcvln 254
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIA-----GL---------EHQTSG----------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 255 sdieRTRLLEEEV-RLHAQQRDLDFEDaagngkgdQIGAINK-----DAISQRLEeIYKRLELIDAYSAEARAASILAGL 328
Cdd:PRK10851 58 ----HIRFHGTDVsRLHARDRKVGFVF--------QHYALFRhmtvfDNIAFGLT-VLPRRERPNAAAIKAKVTQLLEMV 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 743842931 329 SFSpEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:PRK10851 125 QLA-HLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
504-656 |
5.74e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 54.40 E-value: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 504 PIISFSDASFGYpGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLI--AGELQP---TSGTVF---------RSAKV 569
Cdd:PRK14239 4 PILQVSDLSVYY-NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVynghniyspRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 570 RI-----AVFSQHHVDGLDLSSNpLLYMMRcFPGVP--------------------EQKLRAHLGSFGvtgnlalqpmyt 624
Cdd:PRK14239 83 DLrkeigMVFQQPNPFPMSIYEN-VVYGLR-LKGIKdkqvldeavekslkgasiwdEVKDRLHDSALG------------ 148
|
170 180 190
....*....|....*....|....*....|..
gi 743842931 625 LSGGQKSRVAFAKITFKKPHIILLDEPSNHLD 656
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
176-373 |
5.96e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 53.64 E-value: 5.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 176 HLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMALHAIDGIprncqilHVEQEVVGDDTS--ALQcvl 253
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAF-------SASGEVLLNGRRltALP--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 254 nsdIERTR--LLeeevrlhaQQRDLDFE--DAAGN---GKGDQIGAIN-KDAISQRLEEiykrlelidaysaearaasil 325
Cdd:COG4136 73 ---AEQRRigIL--------FQDDLLFPhlSVGENlafALPPTIGRAQrRARVEQALEE--------------------- 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 743842931 326 AGLSfspEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:COG4136 121 AGLA---GFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
175-419 |
7.25e-08 |
|
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: 53.44 E-value: 7.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRymalhAIDGIprncqILHVEQEVVGDDTSalqcVLN 254
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIR-----MILGI-----ILPDSGEVLFDGKP----LDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 255 SDIERTRLLEEEVRLHAQQRDLDFEDAAGNGKGdqigaINKDAISQRLEEIYKRLELidaysaearaasilaglsfsPEM 334
Cdd:cd03269 67 AARNRIGYLPEERGLYPKMKVIDQLVYLAQLKG-----LKKEEARRRIDEWLERLEL--------------------SEY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 335 QKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESY---LVKWPKTFIVVSHAREFLNTVVTDILHL 411
Cdd:cd03269 122 ANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVireLARAGKTVILSTHQMELVEELCDRVLLL 201
|
....*...
gi 743842931 412 QGQKLTAY 419
Cdd:cd03269 202 NKGRAVLY 209
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
503-699 |
7.58e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.16 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 503 APIISFSDASFG-YPGGPLmfknlnfgidldsriAMVGPNGIGKSTILKLIAGELQPTSGTV-FRSAkvriavfSQHHVD 580
Cdd:PRK11701 17 GPRKGCRDVSFDlYPGEVL---------------GIVGESGSGKTTLLNALSARLAPDAGEVhYRMR-------DGQLRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 581 GLDLSSNPLLYMMRCFPGV----PEQKLRAHLgSFGvtGNLALQPM------Y--------------------------T 624
Cdd:PRK11701 75 LYALSEAERRRLLRTEWGFvhqhPRDGLRMQV-SAG--GNIGERLMavgarhYgdiratagdwlerveidaariddlptT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 625 LSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLdAVEA----LIQGLVLFQG-GILMVSHD---EHLISgsvDELWVVSQ 696
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV-SVQArlldLLRGLVRELGlAVVIVTHDlavARLLA---HRLLVMKQ 227
|
...
gi 743842931 697 GKV 699
Cdd:PRK11701 228 GRV 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
185-396 |
8.02e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 53.01 E-value: 8.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 185 GGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLrymalHAIDGI----------PRNCQILHVEQEVVGDDT---SALQC 251
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLL-----KVLAGVlrptsgtvrrAGGARVAYVPQRSEVPDSlplTVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 252 VLNSDIERTRLLeeevrlhaqqRDLDFEDAAgngkgdqigainkdAISQRLEeiykRLELIDaysaearaasiLAGLSFS 331
Cdd:NF040873 78 VAMGRWARRGLW----------RRLTRDDRA--------------AVDDALE----RVGLAD-----------LAGRQLG 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 332 pemqkkatkTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKW---PKTFIVVSH 396
Cdd:NF040873 119 ---------ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEharGATVVVVTH 177
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
528-681 |
8.13e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 55.41 E-value: 8.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 528 GIDLDSR----IAMVGPNGIGKSTILKLIAGELQPTSGTV--------FRSAK----VRIAVFSQH--HVDGLDLSSNpl 589
Cdd:COG1129 22 GVSLELRpgevHALLGENGAGKSTLMKILSGVYQPDSGEIlldgepvrFRSPRdaqaAGIAIIHQElnLVPNLSVAEN-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 590 LYM---MRCFPGVPEQKLR----AHLGSFGVTGNLAlQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEA 662
Cdd:COG1129 100 IFLgrePRRGGLIDWRAMRrrarELLARLGLDIDPD-TPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVER 178
|
170 180
....*....|....*....|....*
gi 743842931 663 L---IQGLVLfQG-GILMVSH--DE 681
Cdd:COG1129 179 LfriIRRLKA-QGvAIIYISHrlDE 202
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
535-694 |
8.82e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 52.57 E-value: 8.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 535 IAMVGPNGIGKSTILKLIAGELQPTSGTvfrsakvriavfsqhhvDGLDLSSnpllymmrcfpgvpeqklrahlgsfgvt 614
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQLIPNGDN-----------------DEWDGIT---------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 615 gnLALQPMY-TLSGGQKSRVAFAKITFKKPHIILLDEPSNHLD----LDAVEALIQGLVLFQGGILMVSHDEHLISGSVD 689
Cdd:cd03222 63 --PVYKPQYiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSD 140
|
....*
gi 743842931 690 ELWVV 694
Cdd:cd03222 141 RIHVF 145
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
316-405 |
9.15e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 53.99 E-value: 9.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 316 SAEARAASILAGLSFSPEmQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD---LHAVLWLESYLVKWPKTFI 392
Cdd:PRK11264 120 EATARARELLAKVGLAGK-ETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDpelVGEVLNTIRQLAQEKRTMV 198
|
90
....*....|....*..
gi 743842931 393 VVSH----AREFLNTVV 405
Cdd:PRK11264 199 IVTHemsfARDVADRAI 215
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
340-396 |
9.71e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 9.71e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743842931 340 KTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLV----KWPKTFIVVSH 396
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdikdKADKTIITIAH 1417
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
175-436 |
1.16e-07 |
|
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: 53.44 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRdLIVDGsVTLSF--GRHYGLVGRNGTGKTTFLRYMA-LHAID-GiprncQILHVEQEVVGDDTSALQ 250
Cdd:COG1127 6 IEVRNLTKSFGDR-VVLDG-VSLDVprGEILAIIGGSGSGKSVLLKLIIgLLRPDsG-----EILVDGQDITGLSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 251 CV------------LNSD-----------IERTRLLEEEVRlhaqqrdldfedaagngkgdqigainkDAISQRLEeiyk 307
Cdd:COG1127 79 ELrrrigmlfqggaLFDSltvfenvafplREHTDLSEAEIR---------------------------ELVLEKLE---- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 308 RLELIDA---YSAEaraasilaglsfspemqkkatktFSGGWRMRIALARALFIEPDILLLDEPT-----------NHL- 372
Cdd:COG1127 128 LVGLPGAadkMPSE-----------------------LSGGMRKRVALARALALDPEILLYDEPTagldpitsaviDELi 184
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743842931 373 -DLHAVLWLesylvkwpkTFIVVSHAREFLNTVVTDILHLQGQKLTAYkGDYDTFERTREEQIKN 436
Cdd:COG1127 185 rELRDELGL---------TSVVVTHDLDSAFAIADRVAVLADGKIIAE-GTPEELLASDDPWVRQ 239
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
175-373 |
1.25e-07 |
|
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: 53.27 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRdLIVDGsVTLSF--GRHYGLVGRNGTGKTTFLRYMAlhaidGI--PRNCQILHVEQEVVGDDTSAL- 249
Cdd:cd03261 1 IELRGLTKSFGGR-TVLKG-VDLDVrrGEILAIIGPSGSGKSTLLRLIV-----GLlrPDSGEVLIDGEDISGLSEAELy 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 250 -----------QCVLNSDI-----------ERTRLLEEEVRlhaqqrdldfedaagngkgdqigainkDAISQRLEeiyk 307
Cdd:cd03261 74 rlrrrmgmlfqSGALFDSLtvfenvafplrEHTRLSEEEIR---------------------------EIVLEKLE---- 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 308 rlelidaysaearaasiLAGLsfsPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:cd03261 123 -----------------AVGL---RGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLD 168
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
175-378 |
1.51e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 53.24 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMA--LHAIDGiprNCQILHveQEVvgDDTSALQcv 252
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSgeLSPDSG---EVRLNG--RPL--ADWSPAE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 253 lnsdIERTR-------------LLEEEVRLhaqqrdldfedaagngkgdqiGAINKDAISQRLEEiykrleLIDAYSAEA 319
Cdd:PRK13548 74 ----LARRRavlpqhsslsfpfTVEEVVAM---------------------GRAPHGLSRAEDDA------LVAAALAQV 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 320 RAASiLAGLSFSpemqkkatkTFSGGWRMRIALARAL------FIEPDILLLDEPTNHLDL---HAVL 378
Cdd:PRK13548 123 DLAH-LAGRDYP---------QLSGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDLahqHHVL 180
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
343-373 |
1.64e-07 |
|
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: 52.73 E-value: 1.64e-07
10 20 30
....*....|....*....|....*....|.
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:cd03296 138 SGGQRQRVALARALAVEPKVLLLDEPFGALD 168
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
191-373 |
1.66e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 53.58 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 191 VDG-SVTLSFGRHYGLVGRNGTGKTTFLRymalhaidgiprncQILHVEQ----EVV--GDDTSALqcvlnSDIERTRLl 263
Cdd:COG4608 34 VDGvSFDIRRGETLGLVGESGCGKSTLGR--------------LLLRLEEptsgEILfdGQDITGL-----SGRELRPL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 264 eeevRLHAQqrdLDFED--AAGNGKgDQIGAInkdaisqrLEEIYKRLELIDAYSAEARAASILA--GLSfsPEMQKKAT 339
Cdd:COG4608 94 ----RRRMQ---MVFQDpyASLNPR-MTVGDI--------IAEPLRIHGLASKAERRERVAELLElvGLR--PEHADRYP 155
|
170 180 190
....*....|....*....|....*....|....
gi 743842931 340 KTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:COG4608 156 HEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
473-699 |
1.90e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 55.02 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 473 KALDRLGHMDEIVNDPDYK-------FEFPTPDDRPGAPIISFsdASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGK 545
Cdd:TIGR01257 892 RALEKTEPLTEEMEDPEHPegindsfFERELPGLVPGVCVKNL--VKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGK 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 546 STILKLIAGELQPTSGTVFRSAK--------VR--IAVFSQHHV--DGLDLSSNPLLYMMRCFPGVPEQKL--RAHLGSF 611
Cdd:TIGR01257 970 TTTLSILTGLLPPTSGTVLVGGKdietnldaVRqsLGMCPQHNIlfHHLTVAEHILFYAQLKGRSWEEAQLemEAMLEDT 1049
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 612 GVTGNLAlQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVLFQGG--ILMVSH--DEHLISGs 687
Cdd:TIGR01257 1050 GLHHKRN-EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGrtIIMSTHhmDEADLLG- 1127
|
250
....*....|..
gi 743842931 688 vDELWVVSQGKV 699
Cdd:TIGR01257 1128 -DRIAIISQGRL 1138
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
523-699 |
1.97e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 52.76 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 523 KNLNF---------GIDLDSR----IAMVGPNGIGKSTILKLIAG--ELQPTSGTVfrsakvriavfsqhHVDGLDLSSN 587
Cdd:COG0396 4 KNLHVsvegkeilkGVNLTIKpgevHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSI--------------LLDGEDILEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 588 PllymmrcfpgvPEQklRAHLGSF----------GVT---------GNLALQPMYT------------------------ 624
Cdd:COG0396 70 S-----------PDE--RARAGIFlafqypveipGVSvsnflrtalNARRGEELSAreflkllkekmkelgldedfldry 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 625 ----LSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVLFQG---GILMVSHDEHLIS-GSVDELWVVSQ 696
Cdd:COG0396 137 vnegFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpdrGILIITHYQRILDyIKPDFVHVLVD 216
|
...
gi 743842931 697 GKV 699
Cdd:COG0396 217 GRI 219
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
535-680 |
2.18e-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: 54.02 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 535 IAMVGPNGIGKSTILKLIAGELQPT-----------------SGTVF-------RSAKVRIAVFSQhHVDgldlssnpll 590
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNlgdydeepswdevlkrfRGTELqdyfkklANGEIKVAHKPQ-YVD---------- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 591 YMMRCFPGVPEQKLRA--HLGSF-GVTGNLALQPMY-----TLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLD---A 659
Cdd:COG1245 171 LIPKVFKGTVRELLEKvdERGKLdELAEKLGLENILdrdisELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYqrlN 250
|
170 180
....*....|....*....|.
gi 743842931 660 VEALIQGLVLFQGGILMVSHD 680
Cdd:COG1245 251 VARLIRELAEEGKYVLVVEHD 271
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
527-652 |
2.25e-07 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 52.29 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 527 FGIDLD----SRIAMVGPNGIGKSTILKLIAGELQPTSGTVfrsakvriavfsqhHVDGLDLSSNP--------LLYMM- 593
Cdd:COG0410 20 HGVSLEveegEIVALLGRNGAGKTTLLKAISGLLPPRSGSI--------------RFDGEDITGLPphriarlgIGYVPe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 594 --RCFPG--VpEQKLR--AHLGSFGVTGNLALQPMY---------------TLSGGQKSRVAFAKITFKKPHIILLDEPS 652
Cdd:COG0410 86 grRIFPSltV-EENLLlgAYARRDRAEVRADLERVYelfprlkerrrqragTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
174-373 |
2.54e-07 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 53.15 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 174 DIHLENFNISVGGRDlIVDGsVTLSF--GRHYGLVGRNGTGKTTFLRYMA-LHAIDG--IprncqilHVEQEVVGDdtsa 248
Cdd:COG3839 3 SLELENVSKSYGGVE-ALKD-IDLDIedGEFLVLLGPSGCGKSTLLRMIAgLEDPTSgeI-------LIGGRDVTD---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 249 lqcvlnsdiertrlleeevrLHAQQRDLD--FEDAA--------GN-GKGDQIGAINKDAISQRLEEIYKRLElIDAYsa 317
Cdd:COG3839 70 --------------------LPPKDRNIAmvFQSYAlyphmtvyENiAFPLKLRKVPKAEIDRRVREAAELLG-LEDL-- 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 318 earaasilaglsfspeMQKKAtKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:COG3839 127 ----------------LDRKP-KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
204-374 |
2.67e-07 |
|
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: 53.19 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 204 GLVGRNGTGKTTFLRYMAlhaidGIPRNcqilhVEQEVVGDDTsalqcVLNSDiertrllEEEVRLHAQQRdldfedaag 283
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIA-----GLTRP-----DEGEIVLNGR-----TLFDS-------RKGIFLPPEKR--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 284 ngkgdQIGAINKDA-------ISQRLEEIYKRlelIDAYSAEARAASILAGLSFSPEMQKKaTKTFSGGWRMRIALARAL 356
Cdd:TIGR02142 76 -----RIGYVFQEArlfphlsVRGNLRYGMKR---ARPSERRISFERVIELLGIGHLLGRL-PGRLSGGEKQRVAIGRAL 146
|
170
....*....|....*...
gi 743842931 357 FIEPDILLLDEPTNHLDL 374
Cdd:TIGR02142 147 LSSPRLLLMDEPLAALDD 164
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
204-369 |
2.70e-07 |
|
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: 52.05 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 204 GLVGRNGTGKTTFLRymalhAIDGI--PRNCQILhveqeVVGDDTSALQCvlnsdIERTRL----------------LEE 265
Cdd:cd03224 30 ALLGRNGAGKTTLLK-----TIMGLlpPRSGSIR-----FDGRDITGLPP-----HERARAgigyvpegrrifpeltVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 266 EVRLHAQQRdldfedaagngkgdqigaiNKDAISQRLEEIYK---RLElidaysaearaasilaglsfspEMQKKATKTF 342
Cdd:cd03224 95 NLLLGAYAR-------------------RRAKRKARLERVYElfpRLK----------------------ERRKQLAGTL 133
|
170 180
....*....|....*....|....*..
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPT 369
Cdd:cd03224 134 SGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
343-419 |
2.77e-07 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 53.98 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLD------LHAVLwleSYLVKWPKTFIVVSHAREFLNtVVTDILHLQGQKL 416
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaaLAAAI---RALKARGATVVVITHRPSLLA-AVDKLLVLRDGRV 544
|
...
gi 743842931 417 TAY 419
Cdd:COG4618 545 QAF 547
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
317-396 |
3.03e-07 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 51.97 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 317 AEARAASILAGLSFSPEMQKKATKTfSGGWRMRIALARALFIEPDILLLDEPTNHLDLHA---VLWLESYLVK-WPKTFI 392
Cdd:COG1136 121 RRERARELLERVGLGDRLDHRPSQL-SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeeVLELLRELNReLGTTIV 199
|
....
gi 743842931 393 VVSH 396
Cdd:COG1136 200 MVTH 203
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
524-702 |
3.04e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 52.95 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 524 NLNFGIDLD---SRI-AMVGPNGIGKSTILKLIAGELQPTSG-------TVFRSA--------KVRIA-VFSQH------ 577
Cdd:PRK11144 12 DLCLTVNLTlpaQGItAIFGRSGAGKTSLINAISGLTRPQKGrivlngrVLFDAEkgiclppeKRRIGyVFQDArlfphy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 578 HVDGldlssNpLLYMMRCfpgvpeqKLRAHLGSfgVTGNLALQPM-----YTLSGGQKSRVAFAKITFKKPHIILLDEPS 652
Cdd:PRK11144 92 KVRG-----N-LRYGMAK-------SMVAQFDK--IVALLGIEPLldrypGSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743842931 653 NHLDL-------DAVEALIQGLVLfqgGILMVSH--DE--HLisgsVDELWVVSQGKVTPF 702
Cdd:PRK11144 157 ASLDLprkrellPYLERLAREINI---PILYVSHslDEilRL----ADRVVVLEQGKVKAF 210
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
489-704 |
3.71e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.44 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 489 DYKFEFPTPDDRPGAPIISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF---- 564
Cdd:PRK10522 306 PYKAEFPRPQAFPDWQTLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILldgk 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 565 ------RSA--KVRIAVFSQHH-----VDGLDLSSNPLLYmmrcfpgvpeQKLRAHLG---SFGVTGNLALQPmyTLSGG 628
Cdd:PRK10522 386 pvtaeqPEDyrKLFSAVFTDFHlfdqlLGPEGKPANPALV----------EKWLERLKmahKLELEDGRISNL--KLSKG 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 629 QKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLV--LFQGG--ILMVSHDEHLISGSvDELWVVSQGKVTPFHG 704
Cdd:PRK10522 454 QKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLplLQEMGktIFAISHDDHYFIHA-DRLLEMRNGQLSELTG 532
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
503-680 |
3.93e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 53.57 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 503 APIISFSDASFGYPGGP---LMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTvFRSAKVRIA------- 572
Cdd:PRK10535 2 TALLELKDIRRSYPSGEeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGT-YRVAGQDVAtldadal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 573 ----------VFSQHHV-DGLDLSSN---PLLYmmrcfPGVP--EQKLRAH--LGSFGVTGNLALQPMyTLSGGQKSRVA 634
Cdd:PRK10535 81 aqlrrehfgfIFQRYHLlSHLTAAQNvevPAVY-----AGLErkQRLLRAQelLQRLGLEDRVEYQPS-QLSGGQQQRVS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 743842931 635 FAKITFKKPHIILLDEPSNHLDLDAVEALIQGL-VLFQGG--ILMVSHD 680
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILhQLRDRGhtVIIVTHD 203
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
175-411 |
4.17e-07 |
|
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: 51.88 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLrymalHAIDGIPrNCQILHVEQEVVGDDTSALqcvln 254
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLS-----KTIAGHP-SYEVTSGTILFKGQDLLEL----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 255 SDIERTRL-------LEEEVrlhAQQRDLDFEDAAGNGkgdQIGAINKDAISqrleeiykrlelIDAYSAEARAAsiLAG 327
Cdd:TIGR01978 70 EPDERARAglflafqYPEEI---PGVSNLEFLRSALNA---RRSARGEEPLD------------LLDFEKLLKEK--LAL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 328 LSFSPEMQKKATKT-FSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKW--PKT-FIVVSHAREFLNT 403
Cdd:TIGR01978 130 LDMDEEFLNRSVNEgFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLrePDRsFLIITHYQRLLNY 209
|
....*...
gi 743842931 404 VVTDILHL 411
Cdd:TIGR01978 210 IKPDYVHV 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
295-396 |
4.24e-07 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 51.10 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 295 KDAISQRLEEIYKRLElIDAYsaearaasilaglsfspeMQKKaTKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDL 374
Cdd:cd03301 104 KDEIDERVREVAELLQ-IEHL------------------LDRK-PKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA 163
|
90 100
....*....|....*....|....*.
gi 743842931 375 HAVLWLESYLVKWPK----TFIVVSH 396
Cdd:cd03301 164 KLRVQMRAELKRLQQrlgtTTIYVTH 189
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
343-699 |
4.49e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.17 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLDLHA---VLWLESYLvkwpktfivvshaREFLNTVVTDILHlqgqKLTAY 419
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVqaqILQLLREL-------------QQELNMGLLFITH----NLSIV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 420 KGDYDTFERTREEQiknqrkAIEANEKSRAhmqtfidkfrYNAKRASLVQSRIKAldrlghmdEIVNDPDykfefPTPDD 499
Cdd:PRK15134 221 RKLADRVAVMQNGR------CVEQNRAATL----------FSAPTHPYTQKLLNS--------EPSGDPV-----PLPEP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 500 RPgaPIISFSDASFGYP----------GGPLMFKNLNFGIDLDSRIAMVGPNGIGKST----ILKLIA--GEL----QPT 559
Cdd:PRK15134 272 AS--PLLDVEQLQVAFPirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINsqGEIwfdgQPL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 560 SGTVFRS---AKVRIAVFSQHHVDGLdlssNPLLYMMRcfpgVPEQKLRAHLGSFG----------VTGNLALQP----M 622
Cdd:PRK15134 350 HNLNRRQllpVRHRIQVVFQDPNSSL----NPRLNVLQ----IIEEGLRVHQPTLSaaqreqqviaVMEEVGLDPetrhR 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 623 Y--TLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDlDAVEALIqgLVLFQG-------GILMVSHDEHLISGSVDELWV 693
Cdd:PRK15134 422 YpaEFSGGQRQRIAIARALILKPSLIILDEPTSSLD-KTVQAQI--LALLKSlqqkhqlAYLFISHDLHVVRALCHQVIV 498
|
....*.
gi 743842931 694 VSQGKV 699
Cdd:PRK15134 499 LRQGEV 504
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
178-407 |
4.71e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 51.43 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 178 ENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLrYMAlhaIDGIPRNCQILHVEQEvvgdDTSALQcvlnsdi 257
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTF-YMV---VGIVPRDAGNIIIDDE----DISLLP------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 258 ertrlleeevrLHAQQRdldfedaagngKGdqIGAINKDA-ISQRL---EEIYKRLELIDAYSAEA---RAASILAGLSF 330
Cdd:PRK10895 72 -----------LHARAR-----------RG--IGYLPQEAsIFRRLsvyDNLMAVLQIRDDLSAEQredRANELMEEFHI 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 331 SpEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESylvkwpktfiVVSHAREF-LNTVVTD 407
Cdd:PRK10895 128 E-HLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKR----------IIEHLRDSgLGVLITD 194
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
340-413 |
4.86e-07 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 50.23 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 340 KTFSGGWRMRIALARALFIEPDILLLDEPTNHLD------LHAVlwLESYLVkwpkTFIVVSHaREFLNTVVTDILHLQG 413
Cdd:cd03223 90 DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDeesedrLYQL--LKELGI----TVISVGH-RPSLWKFHDRVLDLDG 162
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
535-699 |
5.28e-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: 51.73 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 535 IAMVGPNGIGKSTILKLIAGELQPTSGTVF--------------RSAKVRIAVFSQHHVDGLDLSSN-------PLLYMM 593
Cdd:TIGR02769 40 VGLLGRSGCGKSTLARLLLGLEKPAQGTVSfrgqdlyqldrkqrRAFRRDVQLVFQDSPSAVNPRMTvrqiigePLRHLT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 594 RCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVLFQ-- 671
Cdd:TIGR02769 120 SLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQqa 199
|
170 180 190
....*....|....*....|....*....|
gi 743842931 672 GGI--LMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:TIGR02769 200 FGTayLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
522-680 |
5.30e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 51.63 E-value: 5.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 522 FKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF-------------RSAkvRIA-VFsQHHVDG----LD 583
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILidgkdvtklpeykRAK--YIGrVF-QDPMMGtapsMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 584 LSSNPLLYMMRCF-----PGVPEQK---LRAHLGSFGvtgnLAL-----QPMYTLSGGQKSRVAFAKITFKKPHIILLDE 650
Cdd:COG1101 99 IEENLALAYRRGKrrglrRGLTKKRrelFRELLATLG----LGLenrldTKVGLLSGGQRQALSLLMATLTKPKLLLLDE 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 743842931 651 PSNHLD-------LDAVEALIQglvlfQGGI--LMVSHD 680
Cdd:COG1101 175 HTAALDpktaalvLELTEKIVE-----ENNLttLMVTHN 208
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
515-659 |
5.41e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.15 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 515 YPGGPLMFKnlnfGIDLDSR----IAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKV--------R-IA-VFsQhhvd 580
Cdd:PRK11650 13 YDGKTQVIK----GIDLDVAdgefIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVvnelepadRdIAmVF-Q---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 581 gldlssNPLLY-MMRCFP---------GVPEQKLRAHLGSfgVTGNLALQPMYT-----LSGGQKSRVAFAKITFKKPHI 645
Cdd:PRK11650 84 ------NYALYpHMSVREnmayglkirGMPKAEIEERVAE--AARILELEPLLDrkpreLSGGQRQRVAMGRAIVREPAV 155
|
170
....*....|....*
gi 743842931 646 ILLDEP-SNhldLDA 659
Cdd:PRK11650 156 FLFDEPlSN---LDA 167
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
341-401 |
5.61e-07 |
|
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: 50.55 E-value: 5.61e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743842931 341 TFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWP----KTFIVVSHAREFL 401
Cdd:cd03250 127 NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLllnnKTRILVTHQLQLL 191
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
185-396 |
5.97e-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: 51.25 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 185 GGRDLIVDGSvTLSFGRHYGLVGRNGTGKTTFLRYMA--LHAIDGiprncqilhvEQEVVGDDTSALQCVLNSDIERTrl 262
Cdd:cd03237 11 GEFTLEVEGG-SISESEVIGILGPNGIGKTTFIKMLAgvLKPDEG----------DIEIELDTVSYKPQYIKADYEGT-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 263 leeeVRlhaqqrdlDFEDAAGNGKGDQigainkdaiSQRLEEIYKRLELIDAYSAEARaasilaglsfspemqkkatkTF 342
Cdd:cd03237 78 ----VR--------DLLSSITKDFYTH---------PYFKTEIAKPLQIEQILDREVP--------------------EL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLD----LHAVLWLESYLVKWPKTFIVVSH 396
Cdd:cd03237 117 SGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrLMASKVIRRFAENNEKTAFVVEH 174
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
341-373 |
7.54e-07 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 52.47 E-value: 7.54e-07
10 20 30
....*....|....*....|....*....|...
gi 743842931 341 TFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:COG1132 476 NLSGGQRQRIAIARALLKDPPILILDEATSALD 508
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
174-373 |
8.16e-07 |
|
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: 52.41 E-value: 8.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 174 DIHLENFNISVGGRDLIVDGSVTLSF--GRHYGLVGRNGTGKTTFlrymalhaIDGIPRNcqILHVEQEVVGDDTsalqc 251
Cdd:TIGR02203 330 DVEFRNVTFRYPGRDRPALDSISLVIepGETVALVGRSGSGKSTL--------VNLIPRF--YEPDSGQILLDGH----- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 252 vlnsDIERTRL--LEEEVRLHAQQRDLdFEDAAGN----GKGDQIGainkdaiSQRLEEIykrleLIDAYSAEARAASIL 325
Cdd:TIGR02203 395 ----DLADYTLasLRRQVALVSQDVVL-FNDTIANniayGRTEQAD-------RAEIERA-----LAAAYAQDFVDKLPL 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 743842931 326 aGLSFspEMQKKATKtFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:TIGR02203 458 -GLDT--PIGENGVL-LSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
342-373 |
9.57e-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: 49.62 E-value: 9.57e-07
10 20 30
....*....|....*....|....*....|..
gi 743842931 342 FSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:cd03247 99 FSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
343-399 |
9.59e-07 |
|
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: 50.31 E-value: 9.59e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPK----TFIVVSHARE 399
Cdd:cd03300 132 SGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQE 192
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
175-378 |
1.03e-06 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 50.50 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMA--LHAIDGiprncqilhveqevvgddtsalQCV 252
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTgeLTPSSG----------------------EVR 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 253 LNsDIERTRLLEEEV-RLHA---QQRDLDF-----EDAAgngkgdqIGAINKDAISQRLEEIYKR-LELIDAysaearaa 322
Cdd:COG4559 60 LN-GRPLAAWSPWELaRRRAvlpQHSSLAFpftveEVVA-------LGRAPHGSSAAQDRQIVREaLALVGL-------- 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 323 SILAGLSFSpemqkkatkTFSGGWRMRIALARAL-------FIEPDILLLDEPTNHLDL---HAVL 378
Cdd:COG4559 124 AHLAGRSYQ---------TLSGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSALDLahqHAVL 180
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
342-411 |
1.04e-06 |
|
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: 49.83 E-value: 1.04e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743842931 342 FSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLE---SYLVKWPKTFIVVSHAREFLNTVVTDILHL 411
Cdd:cd03217 105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAeviNKLREEGKSVLIITHYQRLLDYIKPDRVHV 177
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
163-373 |
1.09e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.34 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 163 HDGGGGGPNVKDIHLENFNISVGGR---DLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMAL--------------HAI 225
Cdd:PTZ00265 371 NDDGKKLKDIKKIQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERlydptegdiiindsHNL 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 226 DGIprNCQILHVEQEVVGDDTSALQCVLNSDIERT-------RLLEEEVR--LHAQQRDLDFEDAAGNGKGDQIGAINKD 296
Cdd:PTZ00265 451 KDI--NLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlEALSNYYNedGNDSQENKNKRNSCRAKCAGDLNDMSNT 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 297 AISQRLEEIYKRLELIDAYSAEARAASILAG--LSFSPE-----MQKKATKtFSGGWRMRIALARALFIEPDILLLDEPT 369
Cdd:PTZ00265 529 TDSNELIEMRKNYQTIKDSEVVDVSKKVLIHdfVSALPDkyetlVGSNASK-LSGGQKQRISIARAIIRNPKILILDEAT 607
|
....
gi 743842931 370 NHLD 373
Cdd:PTZ00265 608 SSLD 611
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
317-373 |
1.10e-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: 50.38 E-value: 1.10e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743842931 317 AEARAASILA--GLSfspemqKKATK---TFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:COG1126 113 AEERAMELLErvGLA------DKADAypaQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
302-396 |
1.13e-06 |
|
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: 50.41 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 302 LEEIYKrlelIDAYSAEARAASILAGLSFSPEMqKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLE 381
Cdd:cd03267 119 LAAIYD----LPPARFKKRLDELSELLDLEELL-DTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIR 193
|
90
....*....|....*....
gi 743842931 382 SYLVKWPK----TFIVVSH 396
Cdd:cd03267 194 NFLKEYNRergtTVLLTSH 212
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
497-669 |
1.21e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 51.64 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 497 PDDRP-GAPIISFSDASFGYPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF----------- 564
Cdd:PRK10790 331 NDDRPlQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRldgrplsslsh 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 565 RSAKVRIAVFSQHHV---D--------GLDLSSN---------PLLYMMRCFPGvpeqKLRAHLGSfgvTGNlalqpmyT 624
Cdd:PRK10790 411 SVLRQGVAMVQQDPVvlaDtflanvtlGRDISEEqvwqaletvQLAELARSLPD----GLYTPLGE---QGN-------N 476
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 743842931 625 LSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVL 669
Cdd:PRK10790 477 LSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAA 521
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
521-699 |
1.23e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 50.43 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 521 MFKNLNFGIDLDSRIAMVGPNGIGKSTILKL-------------IAGELQPTSGTVFRSAKVRI-----AVFSQH----H 578
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVlnrlieiydskikVDGKVLYFGKDIFQIDAIKLrkevgMVFQQPnpfpH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 579 VDGLDLSSNPL----LYMMRCFPGVPEQKLRaHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNH 654
Cdd:PRK14246 105 LSIYDNIAYPLkshgIKEKREIKKIVEECLR-KVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 743842931 655 LDL---DAVEALIQGLVLfQGGILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:PRK14246 184 IDIvnsQAIEKLITELKN-EIAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
506-699 |
1.26e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 51.56 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGP-LMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF-----------RSAKVRIAV 573
Cdd:PRK11176 342 IEFRNVTFTYPGKEvPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILldghdlrdytlASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 574 FSQH-HVDGLDLSSN------------------PLLYMMRcFPGVPEQKLRAHLGSFGVtgnlalqpmyTLSGGQKSRVA 634
Cdd:PRK11176 422 VSQNvHLFNDTIANNiayarteqysreqieeaaRMAYAMD-FINKMDNGLDTVIGENGV----------LLSGGQRQRIA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743842931 635 FAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVLFQGG--ILMVSHDEHLISGSvDELWVVSQGKV 699
Cdd:PRK11176 491 IARALLRDSPILILDEATSALDTESERAIQAALDELQKNrtSLVIAHRLSTIEKA-DEILVVEDGEI 556
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
311-700 |
1.43e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.56 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 311 LIDAYSAEARAASILA--GLSFSPEMQkkaTKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD------LHAVLwleS 382
Cdd:COG1129 111 LIDWRAMRRRARELLArlGLDIDPDTP---VGDLSVAQQQLVEIARALSRDARVLILDEPTASLTereverLFRII---R 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 383 YLVKWPKTFIVVSHareFLN---------TVVTDilhlqGQkltaYKGDYDTFERTREEQIKnqrkaieaneksraHMqt 453
Cdd:COG1129 185 RLKAQGVAIIYISH---RLDevfeiadrvTVLRD-----GR----LVGTGPVAELTEDELVR--------------LM-- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 454 fidkfrynakraslvqsrikaldrLGHmdeivndpDYKFEFPTPDDRPGAPIISFSDASfgypgGPLMFKNlnfgIDLDS 533
Cdd:COG1129 237 ------------------------VGR--------ELEDLFPKRAAAPGEVVLEVEGLS-----VGGVVRD----VSFSV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 534 R----IAMVGPNGIGKSTILKLIAGELQPTSGTVF-RSAKVRI-----AVfsQHHV---------DGL--DLS--SN--- 587
Cdd:COG1129 276 RageiLGIAGLVGAGRTELARALFGADPADSGEIRlDGKPVRIrsprdAI--RAGIayvpedrkgEGLvlDLSirENitl 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 588 PLLYMMRCFPGVPEQKLRAH----LGSFGV-TGNLAlQPMYTLSGG--QKsrVAFAKITFKKPHIILLDEPSNHLDLDA- 659
Cdd:COG1129 354 ASLDRLSRGGLLDRRRERALaeeyIKRLRIkTPSPE-QPVGNLSGGnqQK--VVLAKWLATDPKVLILDEPTRGIDVGAk 430
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 743842931 660 --VEALIQGLVLfQG-GILMVSHD-EHLISGSvDELWVVSQGKVT 700
Cdd:COG1129 431 aeIYRLIRELAA-EGkAVIVISSElPELLGLS-DRILVMREGRIV 473
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
495-706 |
1.47e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.05 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 495 PTPDDRPGAPIISFSDASFGY--PGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGT--VFR----- 565
Cdd:PLN03130 604 PNPPLEPGLPAISIKNGYFSWdsKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDAsvVIRgtvay 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 566 --------SAKVR-----------------IAVFSQHHvdglDLSSnpllymmrcFPGVPEQKlrahLGSFGVtgnlalq 620
Cdd:PLN03130 684 vpqvswifNATVRdnilfgspfdperyeraIDVTALQH----DLDL---------LPGGDLTE----IGERGV------- 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 621 pmyTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDL----DAVEALIQGlVLFQGGILMVSHDEHLISgSVDELWVVSQ 696
Cdd:PLN03130 740 ---NISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhvgrQVFDKCIKD-ELRGKTRVLVTNQLHFLS-QVDRIILVHE 814
|
250
....*....|
gi 743842931 697 GKVTPfHGTF 706
Cdd:PLN03130 815 GMIKE-EGTY 823
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
523-699 |
1.50e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 50.50 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 523 KNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrsakvriavfsqhhVDGLDLSSNPL------LYMMRCF 596
Cdd:PRK13650 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQII--------------IDGDLLTEENVwdirhkIGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 597 P--------------------GVPEQKLRAHlgsfgVTGNLALQPMYT--------LSGGQKSRVAFAKITFKKPHIILL 648
Cdd:PRK13650 90 PdnqfvgatveddvafglenkGIPHEEMKER-----VNEALELVGMQDfkereparLSGGQKQRVAIAGAVAMRPKIIIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 743842931 649 DEPSNHLDLDAVEALIQGLVL----FQGGILMVSHDEHLISGSvDELWVVSQGKV 699
Cdd:PRK13650 165 DEATSMLDPEGRLELIKTIKGirddYQMTVISITHDLDEVALS-DRVLVMKNGQV 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
503-679 |
1.60e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.45 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 503 APIISFSDASFGYPGgplmFKNLNfGIDLDSRI----AMVGPNGIGKSTILKLIAGELQPTSGTV--------FRSAK-- 568
Cdd:PRK11288 2 SPYLSFDGIGKTFPG----VKALD-DISFDCRAgqvhALMGENGAGKSTLLKILSGNYQPDAGSIlidgqemrFASTTaa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 569 --VRIAVFSQ--HHVDGLDLSSNplLYMMRcFP---GVPEQKL-----RAHLGSFGVTGNlALQPMYTLSGGQKSRVAFA 636
Cdd:PRK11288 77 laAGVAIIYQelHLVPEMTVAEN--LYLGQ-LPhkgGIVNRRLlnyeaREQLEHLGVDID-PDTPLKYLSIGQRQMVEIA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 743842931 637 KITFKKPHIILLDEPSNHLDLDAVEALI--------QGLVlfqggILMVSH 679
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSAREIEQLFrvirelraEGRV-----ILYVSH 198
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
175-373 |
1.64e-06 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 50.99 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMAlhaidgiprncqilHVEQEVVGddtsalQCVLN 254
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLA--------------GFEQPTAG------QIMLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 255 S-DIERTRLLEEEVRLHAQQRDLdF------EDAAGNGKGDQIGainKDAISQRLEEiykrlelidaysaearaasiLAG 327
Cdd:PRK11607 80 GvDLSHVPPYQRPINMMFQSYAL-FphmtveQNIAFGLKQDKLP---KAEIASRVNE--------------------MLG 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 743842931 328 LSFSPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:PRK11607 136 LVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
523-656 |
1.79e-06 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 49.58 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 523 KNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQP---TSGTV-FRSAKVRIAVFSQH--HVDGLD-----------LS 585
Cdd:cd03234 24 NDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQIlFNGQPRKPDQFQKCvaYVRQDDillpgltvretLT 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 586 SNPLLYMMRCFPGVPEQKLRAHLGSfgvtGNLALQP-----MYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLD 656
Cdd:cd03234 104 YTAILRLPRKSSDAIRKKRVEDVLL----RDLALTRiggnlVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
524-650 |
1.86e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.04 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 524 NLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTV-FRSAKVRIAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQ 602
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVdIKGSAALIAISSGLNGQLTGIENIELKGLMMGLTKEKIK 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 743842931 603 KLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDE 650
Cdd:PRK13545 122 EIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
529-695 |
2.21e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.14 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 529 IDLDSRI-AMVGPNGIGKSTILKLIA----GELQPTS------GTVFRSAKVRIAV---FSqhHVDGLDL----SSNPLL 590
Cdd:cd03240 18 IEFFSPLtLIVGQNGAGKTTIIEALKyaltGELPPNSkggahdPKLIREGEVRAQVklaFE--NANGKKYtitrSLAILE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 591 YMMRCfpgvpeqklraHLGSFGVtgnLALQPMYTLSGGQKS------RVAFAKITFKKPHIILLDEPSNHLD-------- 656
Cdd:cd03240 96 NVIFC-----------HQGESNW---PLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeenieesl 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 743842931 657 LDAVEALiQGLVLFQggILMVSHDEHLIsGSVDELWVVS 695
Cdd:cd03240 162 AEIIEER-KSQKNFQ--LIVITHDEELV-DAADHIYRVE 196
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
536-679 |
2.60e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.17 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 536 AMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKVRIAVFSQHH--------VDGLD--LSSNPLLYMMRCFPGVPEQKLR 605
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHqnmgycpqFDAIDdlLTGREHLYLYARLRGVPAEEIE 2048
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 606 A----HLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEAL---IQGLVLFQGGILMVS 678
Cdd:TIGR01257 2049 KvanwSIQSLGLS-LYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwntIVSIIREGRAVVLTS 2127
|
.
gi 743842931 679 H 679
Cdd:TIGR01257 2128 H 2128
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
343-399 |
2.62e-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: 50.10 E-value: 2.62e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLDLHA---VLwleSYLVKWPKTF---IV-VSHARE 399
Cdd:COG4148 135 SGGERQRVAIGRALLSSPRLLLMDEPLAALDLARkaeIL---PYLERLRDELdipILyVSHSLD 195
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
175-396 |
2.65e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 49.53 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDlIVDGsVTLSFGRH--YGLVGRNGTGKTTFLRYMalhaidgiprNCQI-LHVEQEVVGDDTSALQC 251
Cdd:PRK14247 4 IEIRDLKVSFGQVE-VLDG-VNLEIPDNtiTALMGPSGSGKSTLLRVF----------NRLIeLYPEARVSGEVYLDGQD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 252 VLNSD-IERTRLLEEEVRLHAQQRDLD-FEDAAGNGKGDQIgAINKDAISQRLEEIYKRLELIDAYSAEARAAsilAGls 329
Cdd:PRK14247 72 IFKMDvIELRRRVQMVFQIPNPIPNLSiFENVALGLKLNRL-VKSKKELQERVRWALEKAQLWDEVKDRLDAP---AG-- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743842931 330 fspemqkkatkTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPK--TFIVVSH 396
Cdd:PRK14247 146 -----------KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
174-396 |
2.65e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 50.79 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 174 DIHLENFNISVGGRDL--IVDGSVTLSFGRHYGLVGRNGTGKTT----FLRYmalHAIDgiprncqilhvEQEVVGDdts 247
Cdd:PRK11176 341 DIEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTianlLTRF---YDID-----------EGEILLD--- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 248 alqcvlNSDIERTRL--LEEEVRLHAQQRDLdFEDAAGNGkgdqigainkdaISQRLEEIYKRLELIDAysaeARAASil 325
Cdd:PRK11176 404 ------GHDLRDYTLasLRNQVALVSQNVHL-FNDTIANN------------IAYARTEQYSREQIEEA----ARMAY-- 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 326 aGLSFSPEMqKKATKT--------FSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYL--VKWPKTFIVVS 395
Cdd:PRK11176 459 -AMDFINKM-DNGLDTvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALdeLQKNRTSLVIA 536
|
.
gi 743842931 396 H 396
Cdd:PRK11176 537 H 537
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
536-679 |
2.81e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.41 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 536 AMVGPNGIGKSTILKLIAGELQPTSGTVF-RSAKVRIA------------VFsQHH--VDGLDLSSNPLLYMMRCFPGVP 600
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLYQPDSGEILiDGKPVRIRsprdaialgigmVH-QHFmlVPNLTVAENIVLGLEPTKGGRL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 601 -----EQKLRAHLGSFGvtgnLALQP---MYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVLF-- 670
Cdd:COG3845 114 drkaaRARIRELSERYG----LDVDPdakVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLaa 189
|
170
....*....|
gi 743842931 671 QG-GILMVSH 679
Cdd:COG3845 190 EGkSIIFITH 199
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
343-396 |
3.43e-06 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 48.69 E-value: 3.43e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPK--TFIVVSH 396
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKgrTTIVIAH 196
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
341-411 |
3.63e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.87 E-value: 3.63e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 341 TFSGGWRMRIALARALFIEPDILLLDEPTNHLDL---HAVL-WLESyLVKWPKTFIV-VSHAREflntvvtDILHL 411
Cdd:PRK11144 128 SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkRELLpYLER-LAREINIPILyVSHSLD-------EILRL 195
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
620-687 |
4.22e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 47.70 E-value: 4.22e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743842931 620 QPMYTLSGGQKSRVAFAKITFKKPH--IILLDEPSNHLDLDAVEAL---IQGLVLFQGGILMVSHDEHLISGS 687
Cdd:cd03238 83 QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLlevIKGLIDLGNTVILIEHNLDVLSSA 155
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
298-373 |
4.23e-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: 49.28 E-value: 4.23e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 298 ISQRLEEIYKRLELIDAYSAEARAASILA--GLSFSPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:COG0444 105 VGDQIAEPLRIHGGLSKAEARERAIELLErvGLPDPERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTALD 182
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
505-656 |
4.25e-06 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 48.55 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 505 IISFSDASFGYpGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF--------RSAKVRI----- 571
Cdd:PRK09493 1 MIEFKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIvdglkvndPKVDERLirqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 572 -AVFSQHHvdgldlssnpLLYMMRCFPGV--------------PEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFA 636
Cdd:PRK09493 80 gMVFQQFY----------LFPHLTALENVmfgplrvrgaskeeAEKQARELLAKVGLAERAHHYPS-ELSGGQQQRVAIA 148
|
170 180
....*....|....*....|
gi 743842931 637 KITFKKPHIILLDEPSNHLD 656
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSALD 168
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
194-403 |
4.36e-06 |
|
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: 48.17 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 194 SVTLSFGRHYGLVGRNGTGKTTFLRYMALHAIdgiPRNCQIlhveqEVVGDDTSALQCvlnsdiERTRLLEEEVRLHAQq 273
Cdd:cd03292 21 NISISAGEFVFLVGPSGAGKSTLLKLIYKEEL---PTSGTI-----RVNGQDVSDLRG------RAIPYLRRKIGVVFQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 274 rdlDFEDAAGNGKGDQIgAINKDAISQRLEEIYKRL-ELIDAYSAEARAASILAGLSfspemqkkatktfsGGWRMRIAL 352
Cdd:cd03292 86 ---DFRLLPDRNVYENV-AFALEVTGVPPREIRKRVpAALELVGLSHKHRALPAELS--------------GGEQQRVAI 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 743842931 353 ARALFIEPDILLLDEPTNHLD---LHAVLWLESYLVKWPKTFIVVSHAREFLNT 403
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDpdtTWEIMNLLKKINKAGTTVVVATHAKELVDT 201
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
191-373 |
4.96e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 49.32 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 191 VDG-SVTLSFGRHYGLVGRNGTGKTTFLRymalhAIDGIprncqILHVEQEVVGddtsalqcvLNSDIerTRLLEEEVRL 269
Cdd:PRK15079 37 VDGvTLRLYEGETLGVVGESGCGKSTFAR-----AIIGL-----VKATDGEVAW---------LGKDL--LGMKDDEWRA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 270 HAQQRDLDFED--AAGNGKGdQIGAInkdaISQRLEEIYKRLeliDAYSAEARAASILAGLSFSPEMQKKATKTFSGGWR 347
Cdd:PRK15079 96 VRSDIQMIFQDplASLNPRM-TIGEI----IAEPLRTYHPKL---SRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQC 167
|
170 180
....*....|....*....|....*.
gi 743842931 348 MRIALARALFIEPDILLLDEPTNHLD 373
Cdd:PRK15079 168 QRIGIARALILEPKLIICDEPVSALD 193
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
317-396 |
4.96e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 48.27 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 317 AEARAASILAGLSFSPEMQKKATKtFSGGWRMRIALARALFIEPDILLLDEPTNHLDLH---AVLWLESYL-VKWPKTFI 392
Cdd:PRK11629 122 INSRALEMLAAVGLEHRANHRPSE-LSGGERQRVAIARALVNNPRLVLADEPTGNLDARnadSIFQLLGELnRLQGTAFL 200
|
....
gi 743842931 393 VVSH 396
Cdd:PRK11629 201 VVTH 204
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
536-691 |
5.03e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 48.95 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 536 AMVGPNGIGKSTILKLIAGELQPTSGTVfrsakvriavfsqhHVDGLDLSSNP----------------------LLYMM 593
Cdd:COG4152 31 GLLGPNGAGKTTTIRIILGILAPDSGEV--------------LWDGEPLDPEDrrrigylpeerglypkmkvgeqLVYLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 594 RcFPGVP----EQKLRAHLGSFGVTGNLAlQPMYTLSGGQKSRVAFAkITF-KKPHIILLDEPSNHLDLDAVEALIQGLV 668
Cdd:COG4152 97 R-LKGLSkaeaKRRADEWLERLGLGDRAN-KKVEELSKGNQQKVQLI-AALlHDPELLILDEPFSGLDPVNVELLKDVIR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 743842931 669 -LFQGG--ILMVSHD--------EHLI---------SGSVDEL 691
Cdd:COG4152 174 eLAAKGttVIFSSHQmelveelcDRIViinkgrkvlSGSVDEI 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
342-397 |
5.29e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 48.68 E-value: 5.29e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 342 FSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPK--TFIVVSHA 397
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTHS 207
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
506-680 |
5.30e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 48.93 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGY-PGGPLMFK---NLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTV---FRSAKVRIAVFSQHH 578
Cdd:PRK13651 3 IKVKNIVKIFnKKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 579 VDGLDLSSNPllyMMRCFPGVPEqkLRAHLG------------------------SFGVTGNLALQ-------------- 620
Cdd:PRK13651 83 VLEKLVIQKT---RFKKIKKIKE--IRRRVGvvfqfaeyqlfeqtiekdiifgpvSMGVSKEEAKKraakyielvgldes 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 621 -----PmYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLV-LFQGG--ILMVSHD 680
Cdd:PRK13651 158 ylqrsP-FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDnLNKQGktIILVTHD 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
517-656 |
5.36e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 48.70 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 517 GGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAgELQPTSGTVfrsakvriavfsqhHVDGLDLSSNPLLYMMRCF 596
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDI--------------QIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 597 pGVPEQK-------LRAHLGSFG---------VTGNLALQPM----------------YTLSGGQKSRVAFAKITFKKPH 644
Cdd:cd03289 80 -GVIPQKvfifsgtFRKNLDPYGkwsdeeiwkVAEEVGLKSVieqfpgqldfvlvdggCVLSHGHKQLMCLARSVLSKAK 158
|
170
....*....|..
gi 743842931 645 IILLDEPSNHLD 656
Cdd:cd03289 159 ILLLDEPSAHLD 170
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
520-684 |
5.38e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.56 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 520 LMFKNLNFGID-----------LDSRIAMV-GPNGIGKSTILKLIAGELQPTSGTVF-------RSAKVRIAVFSQHHVD 580
Cdd:PRK13541 2 LSLHQLQFNIEqknlfdlsitfLPSAITYIkGANGCGKSSLLRMIAGIMQPSSGNIYykncninNIAKPYCTYIGHNLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 581 GLDLSSNPLLYMMRCFPGVPEQkLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAv 660
Cdd:PRK13541 82 KLEMTVFENLKFWSEIYNSAET-LYAAIHYFKLH-DLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN- 158
|
170 180
....*....|....*....|....*...
gi 743842931 661 EALIQGLVLFQ---GGI-LMVSHDEHLI 684
Cdd:PRK13541 159 RDLLNNLIVMKansGGIvLLSSHLESSI 186
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
535-650 |
5.64e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 48.66 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 535 IAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKVRIAVFSQHHVDGLDLSSNpLLYMMRCFPGVPEQ--KLRAHLGSFG 612
Cdd:PRK13546 53 IGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGIEN-IEFKMLCMGFKRKEikAMTPKIIEFS 131
|
90 100 110
....*....|....*....|....*....|....*...
gi 743842931 613 VTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDE 650
Cdd:PRK13546 132 ELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
535-656 |
5.69e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.81 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 535 IAMVGPNGIGKSTILKLIAGELQPT-----------------SGTVF-------RSAKVRIAVFSQhHVDgldlssnpll 590
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNlgdyeeepswdevlkrfRGTELqnyfkklYNGEIKVVHKPQ-YVD---------- 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743842931 591 YMMRCFPG--------VPEQ-KLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLD 656
Cdd:PRK13409 171 LIPKVFKGkvrellkkVDERgKLDEVVERLGLE-NILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
504-685 |
5.78e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 48.49 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 504 PIISFSDASFGYPGGPLMfKNLNFGIDLDSRIAMVGPNGIGKSTILKLIaGELQPTSGTVFRSAKVRIavFSQH------ 577
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKIL-EGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEF--FNQNiyerrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 578 HVDGLD-----LSSNPLLYMMRCFPGV----------PEQKLRAHLGS-------FGVTGNLALQPMYTLSGGQKSRVAF 635
Cdd:PRK14258 82 NLNRLRrqvsmVHPKPNLFPMSVYDNVaygvkivgwrPKLEIDDIVESalkdadlWDEIKHKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 743842931 636 AKITFKKPHIILLDEPSNHLDLDA---VEALIQGLVL-FQGGILMVSHDEHLIS 685
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIAsmkVESLIQSLRLrSELTMVIVSHNLHQVS 215
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
318-373 |
6.31e-06 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 48.32 E-value: 6.31e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 318 EARAASILA--GLSfspEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:COG4525 112 RARAEELLAlvGLA---DFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
195-373 |
6.39e-06 |
|
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: 47.96 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 195 VTLSFGRH--YGLVGRNGTGKTTFLRymalhAIDGIPRncqilhveqevvgdDTSALQCVLNSDIerTRLLEEEVRlhAQ 272
Cdd:cd03258 24 VSLSVPKGeiFGIIGRSGAGKSTLIR-----CINGLER--------------PTSGSVLVDGTDL--TLLSGKELR--KA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 273 QRD----------LDFEDAAGN-GKGDQIGAINKDAISQRLEEIykrLELI------DAYSAEaraasilaglsfspemq 335
Cdd:cd03258 81 RRRigmifqhfnlLSSRTVFENvALPLEIAGVPKAEIEERVLEL---LELVgledkaDAYPAQ----------------- 140
|
170 180 190
....*....|....*....|....*....|....*...
gi 743842931 336 kkatktFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:cd03258 141 ------LSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
303-399 |
6.47e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 48.51 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 303 EEIYKRLelidaysaeaRAASILAGLSFSpEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHA---VLW 379
Cdd:PRK13637 117 EEIENRV----------KRAMNIVGLDYE-DYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGrdeILN 185
|
90 100
....*....|....*....|.
gi 743842931 380 LESYLVKWPK-TFIVVSHARE 399
Cdd:PRK13637 186 KIKELHKEYNmTIILVSHSME 206
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
190-373 |
6.77e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.59 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 190 IVDGSVTlsfgrhyGLVGRNGTGKTTFLRYMalhaidgiprNCQILHVEQEVVGDDTSALQCVLNSDIERTRlleeevrl 269
Cdd:PRK13649 30 IEDGSYT-------AFIGHTGSGKSTIMQLL----------NGLHVPTQGSVRVDDTLITSTSKNKDIKQIR-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 270 haqqrdldfedaagngkgDQIGAINKDAISQRLEE-IYKRLEL------IDAYSAEARAASILAGLSFSPEMQKKATKTF 342
Cdd:PRK13649 85 ------------------KKVGLVFQFPESQLFEEtVLKDVAFgpqnfgVSQEEAEALAREKLALVGISESLFEKNPFEL 146
|
170 180 190
....*....|....*....|....*....|.
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:PRK13649 147 SGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
537-716 |
6.80e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 48.69 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 537 MVGPNGIGKSTILKLIAGELQPTSGTVfrsaKVRiAVFSQHHVDGLDLSSNPL-------------LYMMRCFP------ 597
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTI----QVG-DIYIGDKKNNHELITNPYskkiknfkelrrrVSMVFQFPeyqlfk 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 598 --------------GVPE----QKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDA 659
Cdd:PRK13631 132 dtiekdimfgpvalGVKKseakKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKG 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743842931 660 VEALIQgLVL----FQGGILMVSHDEHLISGSVDELWVVSQGKV----TPFHgTFLDyKKILQSS 716
Cdd:PRK13631 212 EHEMMQ-LILdakaNNKTVFVITHTMEHVLEVADEVIVMDKGKIlktgTPYE-IFTD-QHIINST 273
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
187-373 |
7.32e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.57 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 187 RDLIV-----DGSVT--------LSFGRHYGLVGRNGTGKT-TFLRYMALHAIDGIprncqilhveqeVVGDDTSALQCV 252
Cdd:PRK09473 16 KDLRVtfstpDGDVTavndlnfsLRAGETLGIVGESGSGKSqTAFALMGLLAANGR------------IGGSATFNGREI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 253 LNsdiertrLLEEEV-RLHAQQRDLDFEDAagngkgdqIGAINKDA-ISQRLEEI---YKRLELIDAYSAEAR---AASI 324
Cdd:PRK09473 84 LN-------LPEKELnKLRAEQISMIFQDP--------MTSLNPYMrVGEQLMEVlmlHKGMSKAEAFEESVRmldAVKM 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 743842931 325 laglsfsPEMQKKAT---KTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:PRK09473 149 -------PEARKRMKmypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
343-373 |
7.84e-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: 47.61 E-value: 7.84e-06
10 20 30
....*....|....*....|....*....|.
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:cd03251 140 SGGQRQRIAIARALLKDPPILILDEATSALD 170
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
623-702 |
9.81e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 48.08 E-value: 9.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 623 YTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQglvLF------QGG-ILMVSHDEHLISGSVDELWVVS 695
Cdd:PRK13645 149 FELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFIN---LFerlnkeYKKrIIMVTHNMDQVLRIADEVIVMH 225
|
90
....*....|.
gi 743842931 696 QGKV----TPF 702
Cdd:PRK13645 226 EGKVisigSPF 236
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
308-396 |
9.95e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 47.72 E-value: 9.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 308 RLELIDAYSAEARAASILaglsfsPEMQKKATKT---FSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYL 384
Cdd:PRK14258 120 KLEIDDIVESALKDADLW------DEIKHKIHKSaldLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLI 193
|
90
....*....|....*.
gi 743842931 385 ----VKWPKTFIVVSH 396
Cdd:PRK14258 194 qslrLRSELTMVIVSH 209
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
200-396 |
1.14e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 47.81 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 200 GRHYGLVGRNGTGKTTFLRYM--ALHAIDGIPRNCQILHV---EQEVVGDDTSALQCVLNsdIERTRLLEEEVrlhaqQR 274
Cdd:PRK13643 32 GSYTALIGHTGSGKSTLLQHLngLLQPTEGKVTVGDIVVSstsKQKEIKPVRKKVGVVFQ--FPESQLFEETV-----LK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 275 DLDFedaagngkGDQIGAINKDaisqrleeiykrlelidaySAEARAASILAGLSFSPEMQKKATKTFSGGWRMRIALAR 354
Cdd:PRK13643 105 DVAF--------GPQNFGIPKE-------------------KAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 743842931 355 ALFIEPDILLLDEPTNHLDLHA---VLWLESYLVKWPKTFIVVSH 396
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKArieMMQLFESIHQSGQTVVLVTH 202
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
315-429 |
1.14e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.17 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 315 YSAEARAASILAGLSFSP-----EMQKKATkTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHA-------VLWLES 382
Cdd:TIGR00957 730 YQQVLEACALLPDLEILPsgdrtEIGEKGV-NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVgkhifehVIGPEG 808
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 743842931 383 YLVKwpKTFIVVSHAREFLNTVVTDILHLQG--------QKLTAYKGDYDTFERT 429
Cdd:TIGR00957 809 VLKN--KTRILVTHGISYLPQVDVIIVMSGGkisemgsyQELLQRDGAFAEFLRT 861
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
336-427 |
1.18e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 47.47 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 336 KKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYL--VKWPKTFIVVSH-----AR-----EFLNT 403
Cdd:PRK14243 146 KQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMheLKEQYTIIIVTHnmqqaARvsdmtAFFNV 225
|
90 100
....*....|....*....|....
gi 743842931 404 VVTDilhlqGQKLTAYKGDYDTFE 427
Cdd:PRK14243 226 ELTE-----GGGRYGYLVEFDRTE 244
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
205-402 |
1.27e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.83 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 205 LVGRNGTGKTTF---LRYmalhAIDGI-PRNCQILHVEQEVVGddtsalqcvlnsdiertrllEEEVRLhaqQRDLDFED 280
Cdd:cd03240 27 IVGQNGAGKTTIieaLKY----ALTGElPPNSKGGAHDPKLIR--------------------EGEVRA---QVKLAFEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 281 AagngKGDQIGAINK-----DAISQRLEEIYKRLEL-IDAYSAEARaasILAGLSFspemqkkatktfsggwrmRIALAR 354
Cdd:cd03240 80 A----NGKKYTITRSlaileNVIFCHQGESNWPLLDmRGRCSGGEK---VLASLII------------------RLALAE 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 743842931 355 ALFIEPDILLLDEPTNHLD-------LHAVlwLESYLVKWPKTFIVVSHAREFLN 402
Cdd:cd03240 135 TFGSNCGILALDEPTTNLDeenieesLAEI--IEERKSQKNFQLIVITHDEELVD 187
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
165-419 |
1.29e-05 |
|
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: 47.14 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 165 GGGGGPNVKDIHLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMAlhaidGI--PRNCQIlhveqEVV 242
Cdd:cd03220 13 YKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLA-----GIypPDSGTV-----TVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 243 GDDTSALQcvLNSDIERTRLLEEEVRLhaqqrdldfedaagngkgdqIGAI---NKDAISQRLEEIYKRLELIDAYSaea 319
Cdd:cd03220 83 GRVSSLLG--LGGGFNPELTGRENIYL--------------------NGRLlglSRKEIDEKIDEIIEFSELGDFID--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 320 raasilaglsfspemqkKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLH----AVLWLESyLVKWPKTFIVVS 395
Cdd:cd03220 138 -----------------LPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqekCQRRLRE-LLKQGKTVILVS 199
|
250 260
....*....|....*....|....
gi 743842931 396 HAREFLNTVVTDILHLQGQKLTAY 419
Cdd:cd03220 200 HDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
343-425 |
1.29e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 48.30 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLDLH---AVLW-LESYLVKwpKTFIVVSHAREFLNTVVTdILHLQGQKLTA 418
Cdd:PRK11174 487 SVGQAQRLALARALLQPCQLLLLDEPTASLDAHseqLVMQaLNAASRR--QTTLMVTHQLEDLAQWDQ-IWVMQDGQIVQ 563
|
....*..
gi 743842931 419 yKGDYDT 425
Cdd:PRK11174 564 -QGDYAE 569
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
340-405 |
1.48e-05 |
|
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: 46.83 E-value: 1.48e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 340 KTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKW--PKTFIVVSHArefLNTVV 405
Cdd:cd03254 138 GNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLmkGRTSIIIAHR---LSTIK 202
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
194-396 |
1.55e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 47.47 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 194 SVTLSFGRHYGLVGRNGTGKTTFLRYmalhaIDGI--PRNCQILHveqevvgddtsalqcvlnSDIERTRLLEEEVRLHA 271
Cdd:PRK13646 27 NTEFEQGKYYAIVGQTGSGKSTLIQN-----INALlkPTTGTVTV------------------DDITITHKTKDKYIRPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 272 QQRdldfedaagngkgdqIGAINKDAISQRLEEIYKRlELI--------DAYSAEARAASILAGLSFSPEMQKKATKTFS 343
Cdd:PRK13646 84 RKR---------------IGMVFQFPESQLFEDTVER-EIIfgpknfkmNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMS 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743842931 344 GGWRMRIALARALFIEPDILLLDEPTNHLD---LHAVLWL-ESYLVKWPKTFIVVSH 396
Cdd:PRK13646 148 GGQMRKIAIVSILAMNPDIIVLDEPTAGLDpqsKRQVMRLlKSLQTDENKTIILVSH 204
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
173-471 |
1.79e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 47.69 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 173 KDIHLENF-NIsvggrdlivdGSVTLSFGRHY-GLVGRNGTGKTTFLRymALHAIDGIPRNCQI----LHVEQEVVGDDT 246
Cdd:COG3593 4 EKIKIKNFrSI----------KDLSIELSDDLtVLVGENNSGKSSILE--ALRLLLGPSSSRKFdeedFYLGDDPDLPEI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 247 SaLQCVLNSDIErtRLLEEEVRLHAQQrdlDFEDAagngkgdqIGAINKDaISQRLEEIYKRLELIDAYSAEARAASILA 326
Cdd:COG3593 72 E-IELTFGSLLS--RLLRLLLKEEDKE---ELEEA--------LEELNEE-LKEALKALNELLSEYLKELLDGLDLELEL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 327 GLSFSPEMQKKATKTFSGG-------------WRMRIALARALFI-----EPDILLLDEPTNHLDLHAVLWLESYL---V 385
Cdd:COG3593 137 SLDELEDLLKSLSLRIEDGkelpldrlgsgfqRLILLALLSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLkelS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 386 KWPKTFIVVSHAREFLNTV-VTDILHLqgqkltaykgdydtferTREEQIKNQRKAIEANEKSRAHMQTFIDkfrynAKR 464
Cdd:COG3593 217 EKPNQVIITTHSPHLLSEVpLENIRRL-----------------RRDSGGTTSTKLIDLDDEDLRKLLRYLG-----VTR 274
|
....*..
gi 743842931 465 ASLVQSR 471
Cdd:COG3593 275 SELLFAR 281
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
343-373 |
1.87e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 46.95 E-value: 1.87e-05
10 20 30
....*....|....*....|....*....|.
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
185-373 |
2.10e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 46.84 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 185 GGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMALHAIdgiPRNCQILHVEQEVVGDDTSALqcvlnSDIERTRLLE 264
Cdd:PRK11701 17 GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLA---PDAGEVHYRMRDGQLRDLYAL-----SEAERRRLLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 265 EE---VRLHAqqRD-LDFEDAAGNGKGDQIGAINkdaisqrlEEIYKRLElidaysaeARAASILAGLSFSPEMQKKATK 340
Cdd:PRK11701 89 TEwgfVHQHP--RDgLRMQVSAGGNIGERLMAVG--------ARHYGDIR--------ATAGDWLERVEIDAARIDDLPT 150
|
170 180 190
....*....|....*....|....*....|...
gi 743842931 341 TFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
303-373 |
2.32e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 47.33 E-value: 2.32e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743842931 303 EEIYKRLElidaysaeaRAASILAgLSFSPEMQKKAtktFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:PRK11000 108 EEINQRVN---------QVAEVLQ-LAHLLDRKPKA---LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
325-373 |
2.47e-05 |
|
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: 46.30 E-value: 2.47e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 743842931 325 LAGLSfspEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:TIGR01184 101 LVGLT---EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
320-373 |
2.53e-05 |
|
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: 46.41 E-value: 2.53e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 320 RAASILA--GLSfspEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:cd03256 124 RALAALErvGLL---DKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLD 176
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
175-380 |
2.71e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 46.26 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRY-MALHAIDG--IPRNCQ--ILHVEQEVVGDDTSAL 249
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVvLGLVAPDEgvIKRNGKlrIGYVPQKLYLDTTLPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 250 QcvlnsdIERTRLLEEEVRlhaqqrdldfedaagngKGDQIGAInkdaisqrleeiyKRLE---LIDAysaearaasila 326
Cdd:PRK09544 85 T------VNRFLRLRPGTK-----------------KEDILPAL-------------KRVQaghLIDA------------ 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 743842931 327 glsfspEMQKkatktFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWL 380
Cdd:PRK09544 117 ------PMQK-----LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVAL 159
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
343-375 |
2.72e-05 |
|
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: 46.07 E-value: 2.72e-05
10 20 30
....*....|....*....|....*....|...
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLDLH 375
Cdd:cd03253 139 SGGEKQRVAIARAILKNPPILLLDEATSALDTH 171
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
343-396 |
2.72e-05 |
|
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: 45.11 E-value: 2.72e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESY---LVKWPKTFIVVSH 396
Cdd:cd03216 84 SVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVirrLRAQGVAVIFISH 140
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
341-401 |
2.82e-05 |
|
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: 47.60 E-value: 2.82e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743842931 341 TFSGGWRMRIALARALFIEPDILLLDEPTNHLD-LHAVLWLESYLVKW--PKTFIVVSHAREFL 401
Cdd:TIGR01271 548 TLSGGQRARISLARAVYKDADLYLLDSPFTHLDvVTEKEIFESCLCKLmsNKTRILVTSKLEHL 611
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
317-416 |
2.96e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 46.36 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 317 AEARAASILAGLSFSPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPK---TFIV 393
Cdd:PRK13641 121 AKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVIL 200
|
90 100
....*....|....*....|...
gi 743842931 394 VSHAREFLNTVVTDILHLQGQKL 416
Cdd:PRK13641 201 VTHNMDDVAEYADDVLVLEHGKL 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
317-373 |
3.01e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 46.55 E-value: 3.01e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 743842931 317 AEARAASILAGLSFSPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:PRK13634 121 AKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
328-396 |
3.15e-05 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 45.23 E-value: 3.15e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743842931 328 LSFSPEMQKkatktFSGGWRMRIALARALFIEPDILLLDEPTNHLD---LHAVLWLESYLVKWPKTFIVVSH 396
Cdd:cd03213 103 LMFAAKLRG-----LSGGERKRVSIALELVSNPSLLFLDEPTSGLDsssALQVMSLLRRLADTGRTIICSIH 169
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
333-418 |
3.67e-05 |
|
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: 45.56 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 333 EMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD---LHAVLWLESYLVKWPK-TFIVVSHAREFLNTVVTDI 408
Cdd:cd03298 120 GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalRAEMLDLVLDLHAETKmTVLMVTHQPEDAKRLAQRV 199
|
90
....*....|
gi 743842931 409 LHLQGQKLTA 418
Cdd:cd03298 200 VFLDNGRIAA 209
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
504-699 |
3.71e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.97 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 504 PIISFSDASFGYPGGPLMfKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFRSAKVRI-AVFSQHHVDGL 582
Cdd:PRK15439 10 PLLCARSISKQYSGVEVL-KGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCArLTPAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 583 DL-SSNPLLymmrcFP----------GVP-----EQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHII 646
Cdd:PRK15439 89 YLvPQEPLL-----FPnlsvkenilfGLPkrqasMQKMKQLLAALGCQLDLDSSAG-SLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 647 LLDEPSNHLDLDAVEALIQGL--VLFQG-GILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIreLLAQGvGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
161-373 |
3.85e-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: 45.75 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 161 VTHDGGGGGPNVKDIhleNFNISVGgrDLIVdgsvtlsfgrhygLVGRNGTGKTTFLRYMalhaidgiprNCQILHVEQE 240
Cdd:cd03295 6 VTKRYGGGKKAVNNL---NLEIAKG--EFLV-------------LIGPSGSGKTTTMKMI----------NRLIEPTSGE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 241 VV--GDDTSALqcvlnsdiertrlleEEVRL-----HAQQrdldfedaagngkgdQIGAINKDAISQRLEEIYKrLELID 313
Cdd:cd03295 58 IFidGEDIREQ---------------DPVELrrkigYVIQ---------------QIGLFPHMTVEENIALVPK-LLKWP 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743842931 314 AYSAEARAASILAGLSFSP-EMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:cd03295 107 KEKIRERADELLALVGLDPaEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
315-426 |
3.85e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 46.38 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 315 YSAEARAASILAGLSFSPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD---LHAVLWLESYLVKWPKTF 391
Cdd:PRK13631 150 SEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDpkgEHEMMQLILDAKANNKTV 229
|
90 100 110
....*....|....*....|....*....|....*
gi 743842931 392 IVVSHAREFLNTVVTDILHLQGQKLTAYKGDYDTF 426
Cdd:PRK13631 230 FVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
195-419 |
4.07e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 45.84 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 195 VTLSF--GRHYGLVGRNGTGKTTFLRYMA--LHAIDG-IPRNCQIlhveqevvgddtSALqcvlnsdiertrlLE----- 264
Cdd:COG1134 45 VSFEVerGESVGIIGRNGAGKSTLLKLIAgiLEPTSGrVEVNGRV------------SAL-------------LElgagf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 265 -------EEVRLhaqqrdldfedaagngkgdqIGAI---NKDAISQRLEEIykrlelidaysaearaasilagLSFSpEM 334
Cdd:COG1134 100 hpeltgrENIYL--------------------NGRLlglSRKEIDEKFDEI----------------------VEFA-EL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 335 QKKAT---KTFSGGWRMRIALARALFIEPDILLLDEptnhldlhaVL-------------WLESyLVKWPKTFIVVSHAR 398
Cdd:COG1134 137 GDFIDqpvKTYSSGMRARLAFAVATAVDPDILLVDE---------VLavgdaafqkkclaRIRE-LRESGRTVIFVSHSM 206
|
250 260
....*....|....*....|.
gi 743842931 399 EFLNTVVTDILHLQGQKLTAY 419
Cdd:COG1134 207 GAVRRLCDRAIWLEKGRLVMD 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
343-373 |
5.27e-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: 45.71 E-value: 5.27e-05
10 20 30
....*....|....*....|....*....|.
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:cd03294 162 SGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
311-374 |
5.44e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.39 E-value: 5.44e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743842931 311 LIDAYSAEARAASILAGLSFSPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDL 374
Cdd:PRK10261 433 LLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
343-373 |
6.22e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 46.36 E-value: 6.22e-05
10 20 30
....*....|....*....|....*....|.
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
343-397 |
6.30e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 45.15 E-value: 6.30e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLES--YLVKWPKTFIVVSHA 397
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEEtlLGLKDDYTMLLVTRS 206
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
535-683 |
7.12e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 44.77 E-value: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 535 IAMVGPNGIGKSTILKLIAGELQPTSGTVF------------RSAKVRIA----VF-SQHHVDGLDLSSN-PLLYMMRcf 596
Cdd:PRK10584 39 IALIGESGSGKSTLLAILAGLDDGSSGEVSlvgqplhqmdeeARAKLRAKhvgfVFqSFMLIPTLNALENvELPALLR-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 597 pGVPEQKLRAH----LGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDL---DAVEALIQGLVL 669
Cdd:PRK10584 117 -GESSRQSRNGakalLEQLGLGKRLDHLPA-QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRqtgDKIADLLFSLNR 194
|
170
....*....|....*
gi 743842931 670 FQGGIL-MVSHDEHL 683
Cdd:PRK10584 195 EHGTTLiLVTHDLQL 209
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
343-386 |
7.47e-05 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 44.57 E-value: 7.47e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVK 386
Cdd:cd03234 145 SGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQ 188
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
535-698 |
8.25e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.03 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 535 IAMVGPNGIGKSTILKLIAGELQPTS--GTVFRSAKV-------RIAVFSQHHVDGLDLSSNPLLY---MMRCFPGVPEQ 602
Cdd:PLN03211 97 LAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKptkqilkRTGFVTQDDILYPHLTVRETLVfcsLLRLPKSLTKQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 603 -KLRAH---LGSFGVT--GNLALQPMYT--LSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLV-LFQGG 673
Cdd:PLN03211 177 eKILVAesvISELGLTkcENTIIGNSFIrgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGsLAQKG 256
|
170 180
....*....|....*....|....*....
gi 743842931 674 ILMVShDEHLISGSV----DELWVVSQGK 698
Cdd:PLN03211 257 KTIVT-SMHQPSSRVyqmfDSVLVLSEGR 284
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
535-699 |
8.39e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 44.96 E-value: 8.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 535 IAMVGPNGIGKSTILKLIAGELQPTSGTV------------------------FRSAKVRIAVFSQH-----HVDGLDLS 585
Cdd:PRK10619 34 ISIIGSSGSGKSTFLRCINFLEKPSEGSIvvngqtinlvrdkdgqlkvadknqLRLLRTRLTMVFQHfnlwsHMTVLENV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 586 SNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAV-EAL- 663
Cdd:PRK10619 114 MEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVgEVLr 193
|
170 180 190
....*....|....*....|....*....|....*..
gi 743842931 664 -IQGLVLFQGGILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:PRK10619 194 iMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
342-432 |
8.47e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 45.04 E-value: 8.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 342 FSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPK--TFIVVSHAREFLNTVVTDILHLQGQKLTAY 419
Cdd:PRK14246 154 LSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELVEW 233
|
90
....*....|...
gi 743842931 420 KGDYDTFERTREE 432
Cdd:PRK14246 234 GSSNEIFTSPKNE 246
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
343-396 |
8.52e-05 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 45.87 E-value: 8.52e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLDLHAvlwlESYLVKWPK----TFIVVSH 396
Cdd:TIGR00958 619 SGGQKQRIAIARALVRKPRVLILDEATSALDAEC----EQLLQESRSrasrTVLLIAH 672
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
343-373 |
8.97e-05 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 45.07 E-value: 8.97e-05
10 20 30
....*....|....*....|....*....|.
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
204-369 |
1.01e-04 |
|
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: 44.20 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 204 GLVGRNGTGKTTFLRymalhAIDGI--PRNCQILHVEQEVVGDDTSalqcvlnsdiERTRL----------------LEE 265
Cdd:COG0410 33 ALLGRNGAGKTTLLK-----AISGLlpPRSGSIRFDGEDITGLPPH----------RIARLgigyvpegrrifpsltVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 266 EVRLHAQQRDldfedaagngkgdqigaiNKDAISQRLEEIYK---RLElidaysaearaasilaglsfspEMQKKATKTF 342
Cdd:COG0410 98 NLLLGAYARR------------------DRAEVRADLERVYElfpRLK----------------------ERRRQRAGTL 137
|
170 180
....*....|....*....|....*..
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPT 369
Cdd:COG0410 138 SGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
610-700 |
1.14e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.43 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 610 SFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDA---VEALIQGLVLFQGGILMVSHDEHLISG 686
Cdd:PRK15439 389 ALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSArndIYQLIRSIAAQNVAVLFISSDLEEIEQ 468
|
90
....*....|....
gi 743842931 687 SVDELWVVSQGKVT 700
Cdd:PRK15439 469 MADRVLVMHQGEIS 482
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
174-396 |
1.17e-04 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 44.23 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 174 DIHLENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMA--LhaidgIPRNCQILHVEQevvgdDTSALqc 251
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFArlL-----TPQSGTVFLGDK-----PISML-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 252 vlnSDiertRLLEEEVRLHAQQRdldfedaagngkgdqigaINKDAISQRLEEIYKR---LELIDAYSAEARAASILAgl 328
Cdd:PRK11231 70 ---SS----RQLARRLALLPQHH------------------LTPEGITVRELVAYGRspwLSLWGRLSAEDNARVNQA-- 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743842931 329 sfspeMQKKATKTF--------SGGWRMRIALARALFIEPDILLLDEPTNHLDL-HAV--LWLESYLVKWPKTFIVVSH 396
Cdd:PRK11231 123 -----MEQTRINHLadrrltdlSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDInHQVelMRLMRELNTQGKTVVTVLH 196
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
343-373 |
1.18e-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: 1.18e-04
10 20 30
....*....|....*....|....*....|.
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:cd03252 140 SGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
506-665 |
1.20e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGY---PGGPLmFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAG--ELQPTSGTVFRSAKV----------- 569
Cdd:PTZ00265 1166 IEIMDVNFRYisrPNVPI-YKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfyDLKNDHHIVFKNEHTndmtneqdyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 570 ------------------------RIAVFSQHH---VDGLDL---------------SSNPLLYMMRCFPGVPEQKLRAH 607
Cdd:PTZ00265 1245 deeqnvgmknvnefsltkeggsgeDSTVFKNSGkilLDGVDIcdynlkdlrnlfsivSQEPMLFNMSIYENIKFGKEDAT 1324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743842931 608 LGSFGVTGNLA--------LQPMY---------TLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAvEALIQ 665
Cdd:PTZ00265 1325 REDVKRACKFAaidefiesLPNKYdtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS-EKLIE 1398
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
177-377 |
1.29e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 44.39 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 177 LENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTFLRYMALHAidgIPRNCQILHVEQEVVGDDTSALQcvlnsd 256
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQ---PPSEGEILLDAQPLESWSSKAFA------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 257 iertrlleEEVRLHAQQ----RDLDFEDAAGNGKGDQIGAINKDAIS--QRLEEiykrlelidaysaearaASILAGLSf 330
Cdd:PRK10575 85 --------RKVAYLPQQlpaaEGMTVRELVAIGRYPWHGALGRFGAAdrEKVEE-----------------AISLVGLK- 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 743842931 331 spEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDL-HAV 377
Cdd:PRK10575 139 --PLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIaHQV 184
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
191-416 |
1.36e-04 |
|
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: 43.96 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 191 VDGsVTLSFGRH--YGLVGRNGTGKTTFLrymalHAIDGI--PRNCQILHVEQEVVG---DDTSALqcvlnsDIERT--- 260
Cdd:cd03219 16 LDD-VSFSVRPGeiHGLIGPNGAGKTTLF-----NLISGFlrPTSGSVLFDGEDITGlppHEIARL------GIGRTfqi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 261 -RLLE-----EEVRLHAQQRDLDFEDAAGNGKGdqigainKDAISQRLEEIYKRLELidaysaeARAASILAGlsfspem 334
Cdd:cd03219 84 pRLFPeltvlENVMVAAQARTGSGLLLARARRE-------EREARERAEELLERVGL-------ADLADRPAG------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 335 qkkatkTFSGGWRMRIALARALFIEPDILLLDEPT---NHLDLHAVLWLESYLVKWPKTFIVVSHAREFLNTVVTDILHL 411
Cdd:cd03219 143 ------ELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVL 216
|
....*.
gi 743842931 412 -QGQKL 416
Cdd:cd03219 217 dQGRVI 222
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
343-373 |
1.41e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 43.80 E-value: 1.41e-04
10 20 30
....*....|....*....|....*....|.
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:PRK10771 131 SGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
517-679 |
1.44e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.16 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 517 GGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVF------------RSAKVRIAVFSQHH--VDGL 582
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITinninynkldhkLAAQLGIGIIYQELsvIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 583 DLSSNplLYMMRC----FPGVP-----EQKLRAHLGSFGVTGNLAL-QPMYTLSGGQKSRVAFAKITFKKPHIILLDEPS 652
Cdd:PRK09700 96 TVLEN--LYIGRHltkkVCGVNiidwrEMRVRAAMMLLRVGLKVDLdEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190
....*....|....*....|....*....|
gi 743842931 653 NHL---DLDAVEALIQGLVLFQGGILMVSH 679
Cdd:PRK09700 174 SSLtnkEVDYLFLIMNQLRKEGTAIVYISH 203
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
341-374 |
1.45e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 44.46 E-value: 1.45e-04
10 20 30
....*....|....*....|....*....|....
gi 743842931 341 TFSGGWRMRIALARALFIEPDILLLDEPTNHLDL 374
Cdd:cd03291 159 TLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
294-396 |
1.49e-04 |
|
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: 45.12 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 294 NKDAISQrlEEIYKRLELidaysAEARAASILAGLSFSPEMQKKATkTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:TIGR01193 572 AKENVSQ--DEIWAACEI-----AEIKDDIENMPLGYQTELSEEGS-SISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
90 100
....*....|....*....|....
gi 743842931 374 LHAVLWLESYLVKWP-KTFIVVSH 396
Cdd:TIGR01193 644 TITEKKIVNNLLNLQdKTIIFVAH 667
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
523-698 |
1.52e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 45.23 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 523 KNLNFGIDLDSRIAMVGPNGIGKS----TILKLI---AGELQPTSGTVFRSAKVRIAVFSQ-----HHVDGLDLS---SN 587
Cdd:PRK10261 33 RNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqaGGLVQCDKMLLRRRSRQVIELSEQsaaqmRHVRGADMAmifQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 588 PLLYMMRCFPgVPEQ---KLRAHLGSFGVTGNLALQPM-----------------YTLSGGQKSRVAFAKITFKKPHIIL 647
Cdd:PRK10261 113 PMTSLNPVFT-VGEQiaeSIRLHQGASREEAMVEAKRMldqvripeaqtilsrypHQLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 743842931 648 LDEPSNHLDLDAVEALIQGLVLFQG----GILMVSHDEHLISGSVDELWVVSQGK 698
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKemsmGVIFITHDMGVVAEIADRVLVMYQGE 246
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
625-705 |
1.53e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 45.04 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 625 LSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLV-LFQGG--ILMVSHD-EHLISGSVDELWVVSQGKVT 700
Cdd:TIGR00955 167 LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKgLAQKGktIICTIHQpSSELFELFDKIILMAEGRVA 246
|
....*
gi 743842931 701 pFHGT 705
Cdd:TIGR00955 247 -YLGS 250
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
498-680 |
1.63e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 44.32 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 498 DDRPGAPIISFSDASFGYPGGPLMfKNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTVFrSAKVRI---AVF 574
Cdd:PRK14271 14 DVDAAAPAMAAVNLTLGFAGKTVL-DQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRY-SGDVLLggrSIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 575 S-------QHHVDGLDLSSNP--------LLYMMRCFPGVPEQKLR----AHLGSFG----VTGNLALQPmYTLSGGQKS 631
Cdd:PRK14271 92 NyrdvlefRRRVGMLFQRPNPfpmsimdnVLAGVRAHKLVPRKEFRgvaqARLTEVGlwdaVKDRLSDSP-FRLSGGQQQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 743842931 632 RVAFAKITFKKPHIILLDEPSNHLD---LDAVEALIQGLVlFQGGILMVSHD 680
Cdd:PRK14271 171 LLCLARTLAVNPEVLLLDEPTSALDpttTEKIEEFIRSLA-DRLTVIIVTHN 221
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
343-373 |
1.67e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 44.95 E-value: 1.67e-04
10 20 30
....*....|....*....|....*....|.
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALD 503
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
506-656 |
1.76e-04 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 43.85 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 506 ISFSDASFGYPGGPLMFkNLNFGIDLDSRIAMVGPNGIGKSTILKLI-------AGEL----------QPTSGTVFRSAK 568
Cdd:COG4161 3 IQLKNINCFYGSHQALF-DINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLniaghqfdfsQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 569 VRIA-VFSQHHV-DGLDLSSNPLLYMMRCFpGVPEQKLRA----HLGSFGVTGNLALQPMYtLSGGQKSRVAFAKITFKK 642
Cdd:COG4161 82 QKVGmVFQQYNLwPHLTVMENLIEAPCKVL-GLSKEQAREkamkLLARLRLTDKADRFPLH-LSGGQQQRVAIARALMME 159
|
170
....*....|....
gi 743842931 643 PHIILLDEPSNHLD 656
Cdd:COG4161 160 PQVLLFDEPTAALD 173
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
317-373 |
1.93e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.34 E-value: 1.93e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 743842931 317 AEARAASILAGLSFSpEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:NF000106 121 ARARADELLERFSLT-EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
622-698 |
2.00e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 43.94 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 622 MY--TLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLdAVEALIQGLV-----LFQGGILMVSHDEHLISGSVDELWVV 694
Cdd:PRK09473 157 MYphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAQIMTLLnelkrEFNTAIIMITHDLGVVAGICDKVLVM 235
|
....
gi 743842931 695 SQGK 698
Cdd:PRK09473 236 YAGR 239
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
312-391 |
2.01e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 44.02 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 312 IDAYSAEARAASILAGLSFSpEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPKTF 391
Cdd:PRK13652 109 LDEETVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETY 187
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
343-377 |
2.32e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 42.94 E-value: 2.32e-04
10 20 30
....*....|....*....|....*....|....*
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLDLHAV 377
Cdd:PRK13539 129 SAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
523-699 |
2.61e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.48 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 523 KNLNFGIDLDSRIAMVGPNGIGKSTILKLIAGE--LQPTSGTVFrsakvriavFSQHHVDGLDlssnpllymmrcfpgvP 600
Cdd:CHL00131 24 KGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDIL---------FKGESILDLE----------------P 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 601 EQklRAHLGSF----------GVT----------------GNLALQPMYTL-------------------------SGGQ 629
Cdd:CHL00131 79 EE--RAHLGIFlafqypieipGVSnadflrlaynskrkfqGLPELDPLEFLeiineklklvgmdpsflsrnvnegfSGGE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743842931 630 KSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVLF---QGGILMVSHDEHLISGSV-DELWVVSQGKV 699
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLmtsENSIILITHYQRLLDYIKpDYVHVMQNGKI 230
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
624-700 |
2.62e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.34 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 624 TLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDA---VEALIQGLVLFQGGILMVSHDEHLISGSVDELWVVSQGKVT 700
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAkfeIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA 470
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
342-401 |
2.63e-04 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 43.09 E-value: 2.63e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743842931 342 FSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLES-----YLVKWPKTFIVVSHAREFL 401
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegilkFLQDDKRTLVLVTHKLQYL 205
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
472-665 |
2.85e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.63 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 472 IKALDRLGHMDEIVNDPDYKFEFPTPDDRPGAPIISFSDASFGYPGGP--LMFKNLNFGIDLDSRIAMVGPNGIGKSTIL 549
Cdd:PTZ00265 349 MKSLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKdvEIYKDLNFTLTEGKTYAFVGESGCGKSTIL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 550 KLIAGELQPTSGTV------------FRSAKVRIAVFSQhhvDGLdLSSNPL-------LYMMRCFPGVPEQ-------- 602
Cdd:PTZ00265 429 KLIERLYDPTEGDIiindshnlkdinLKWWRSKIGVVSQ---DPL-LFSNSIknnikysLYSLKDLEALSNYynedgnds 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 603 ----------------KLRAHLGSFGVTGNLALQPMYT-------------------------------------LSGGQ 629
Cdd:PTZ00265 505 qenknkrnscrakcagDLNDMSNTTDSNELIEMRKNYQtikdsevvdvskkvlihdfvsalpdkyetlvgsnaskLSGGQ 584
|
250 260 270
....*....|....*....|....*....|....*.
gi 743842931 630 KSRVAFAKITFKKPHIILLDEPSNHLDlDAVEALIQ 665
Cdd:PTZ00265 585 KQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQ 619
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
177-368 |
3.13e-04 |
|
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: 42.92 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 177 LENFNISVGGRDLIVDGSVTLSFGRHYGLVGRNGTGKTTfLRYMalhaIDGIPRncqilhVEQ-EVVGDDTsalqcvlns 255
Cdd:cd03218 3 AENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTT-TFYM----IVGLVK------PDSgKILLDGQ--------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 256 DI------ERTRL----LEEEVRLHaqqRDLDFEDaagngkgdqigaiNKDAISQRLEEIYKRLElidaysaeARAASIL 325
Cdd:cd03218 63 DItklpmhKRARLgigyLPQEASIF---RKLTVEE-------------NILAVLEIRGLSKKERE--------EKLEELL 118
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 743842931 326 AGLSFSPEMQKKATkTFSGGWRMRIALARALFIEPDILLLDEP 368
Cdd:cd03218 119 EEFHITHLRKSKAS-SLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
621-656 |
3.26e-04 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 43.08 E-value: 3.26e-04
10 20 30
....*....|....*....|....*....|....*.
gi 743842931 621 PMYtLSGGQKSRVAFAKITFKKPHIILLDEPSNHLD 656
Cdd:PRK11124 139 PLH-LSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
515-680 |
3.38e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 43.23 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 515 YPGGPLMFKNLNFGIDLDSRIAMVGPNGIGKSTILK------------------------LIAGELQPTS-----GTVF- 564
Cdd:PRK14243 19 YYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndlipgfrvegkvtfhgknLYAPDVDPVEvrrriGMVFq 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 565 ------RSAKVRIAVFSQhhVDGLDLSSNPLLymmrcfpgvpEQKLRAHLGSFGVTGNLAlQPMYTLSGGQKSRVAFAKI 638
Cdd:PRK14243 99 kpnpfpKSIYDNIAYGAR--INGYKGDMDELV----------ERSLRQAALWDEVKDKLK-QSGLSLSGGQQQRLCIARA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 743842931 639 TFKKPHIILLDEPSNHLD---LDAVEALIQGLVLfQGGILMVSHD 680
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDpisTLRIEELMHELKE-QYTIIIVTHN 209
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
318-373 |
3.46e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 42.76 E-value: 3.46e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 318 EARAASILA--GLSfspEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:PRK11248 106 LEIAHQMLKkvGLE---GAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
342-396 |
3.57e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 43.48 E-value: 3.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 743842931 342 FSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKW----PKTFIVVSH 396
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqakhQRTIVFISH 223
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
175-373 |
4.04e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 43.17 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 175 IHLENFNISVGGRdLIVDGsvtLSF----GRHYGLVGRNGTGKTTFLRyMALHAID---GiprncQILhVEQEVVGDDts 247
Cdd:COG4152 2 LELKGLTKRFGDK-TAVDD---VSFtvpkGEIFGLLGPNGAGKTTTIR-IILGILApdsG-----EVL-WDGEPLDPE-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 248 alqcvlnsDIERTRLLEEEVRLHAQQRdldfedaagngKGDQI-------GaINKDAISQRLEEIYKRLELidaysaear 320
Cdd:COG4152 69 --------DRRRIGYLPEERGLYPKMK-----------VGEQLvylarlkG-LSKAEAKRRADEWLERLGL--------- 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 743842931 321 aasilaglsfsPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:COG4152 120 -----------GDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
343-373 |
4.06e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 42.46 E-value: 4.06e-04
10 20 30
....*....|....*....|....*....|.
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:PRK10584 148 SGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
317-369 |
5.08e-04 |
|
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: 42.33 E-value: 5.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 743842931 317 AEARAASILAGLSFSPEMQKKAtKTFSGGWRMRIALARALFIEPDILLLDEPT 369
Cdd:COG0411 129 ARERAEELLERVGLADRADEPA-GNLSYGQQRRLEIARALATEPKLLLLDEPA 180
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
335-373 |
5.43e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 42.37 E-value: 5.43e-04
10 20 30
....*....|....*....|....*....|....*....
gi 743842931 335 QKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:PRK13639 131 ENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
525-656 |
5.47e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 42.39 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 525 LNFGIDLDSRIAMVGPNGIGKSTILKLIAGELQPTSGTV-----------FRSAKVRIAVFSQH---HVDGLDLSSNPLL 590
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVkidgelltaenVWNLRRKIGMVFQNpdnQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 591 YMMRcfPGVPEQKLRAHLGSFGVTGNL----ALQPMyTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLD 656
Cdd:PRK13642 106 GMEN--QGIPREEMIKRVDEALLAVNMldfkTREPA-RLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
308-381 |
5.87e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 42.28 E-value: 5.87e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743842931 308 RLELIDAYSAEARAASIlaglsfsPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDL-HAVLWLE 381
Cdd:PRK10253 117 RKEDEEAVTKAMQATGI-------THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIsHQIDLLE 184
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
343-399 |
6.04e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 42.63 E-value: 6.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPK----TFIVVSHARE 399
Cdd:PRK09452 146 SGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRklgiTFVFVTHDQE 206
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
343-368 |
6.15e-04 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 42.05 E-value: 6.15e-04
10 20
....*....|....*....|....*.
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEP 368
Cdd:COG3840 131 SGGQRQRVALARCLVRKRPILLLDEP 156
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
343-385 |
6.34e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 42.94 E-value: 6.34e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLV 385
Cdd:PLN03211 208 SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLG 250
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
343-411 |
6.95e-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: 41.02 E-value: 6.95e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLD----LHAVLWLESYLVKWPKTFIVVSHAREFLnTVVTDILHL 411
Cdd:cd03222 73 SGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrLNAARAIRRLSEEGKKTALVVEHDLAVL-DYLSDRIHV 144
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
624-705 |
7.09e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 41.80 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 624 TLSGGQKSRVAFAKITFKKPHIILLDEPSNHLD----LDaVEALIQGLVLFQGGILMVSHDEHLISGSVDELWVVSQGKV 699
Cdd:PRK10895 137 SLSGGERRRVEIARALAANPKFILLDEPFAGVDpisvID-IKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
....*.
gi 743842931 700 TPfHGT 705
Cdd:PRK10895 216 IA-HGT 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
318-375 |
7.57e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 41.62 E-value: 7.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 318 EARAASILAGLSFSPEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLH 375
Cdd:PRK10247 114 PAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
291-369 |
7.79e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 42.70 E-value: 7.79e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743842931 291 GAINKDAISQRLEEIYKRLELidaysaeaRAASIlaglsfspemqKKATKTFSGGWRMRIALARALFIEPDILLLDEPT 369
Cdd:COG1129 363 GLLDRRRERALAEEYIKRLRI--------KTPSP-----------EQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
621-699 |
7.99e-04 |
|
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: 42.50 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 621 PMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDA---VEALIQGLVLFQGGILMVSHDEHLISGSVDELWVVSQG 697
Cdd:TIGR02633 400 PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
..
gi 743842931 698 KV 699
Cdd:TIGR02633 480 KL 481
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
324-373 |
8.08e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.49 E-value: 8.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 743842931 324 ILAGLSFSPEMQKKAtKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:PRK13409 437 IIKPLQLERLLDKNV-KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
343-368 |
9.29e-04 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 41.55 E-value: 9.29e-04
10 20
....*....|....*....|....*.
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEP 368
Cdd:COG1137 138 SGGERRRVEIARALATNPKFILLDEP 163
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
340-384 |
9.43e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 40.94 E-value: 9.43e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 743842931 340 KTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYL 384
Cdd:PRK13538 128 RQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
342-396 |
1.07e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 41.62 E-value: 1.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 743842931 342 FSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKWPK--TFIVVSH 396
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTH 220
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
204-373 |
1.10e-03 |
|
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: 42.08 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 204 GLVGRNGTGKTTFLRYMAlhaidGiprncqilhVEQEVVGDDTSAL------QcVLNSDIERTrlleeeVRlhaqqrdld 277
Cdd:COG1245 370 GIVGPNGIGKTTFAKILA-----G---------VLKPDEGEVDEDLkisykpQ-YISPDYDGT------VE--------- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 278 fedaagngkgdqigAINKDAISQRLEEIYKRLELIDaysaearaasilaGLSFSPEMQKKAtKTFSGGWRMRIALARALF 357
Cdd:COG1245 420 --------------EFLRSANTDDFGSSYYKTEIIK-------------PLGLEKLLDKNV-KDLSGGELQRVAIAACLS 471
|
170
....*....|....*.
gi 743842931 358 IEPDILLLDEPTNHLD 373
Cdd:COG1245 472 RDADLYLLDEPSAHLD 487
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
620-684 |
1.17e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 1.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743842931 620 QPMYTLSGGQKSRVafaKITF------KKPHIILLDEPSNHLDLDAVEALIQGL--VLFQG-GILMVSHDEHLI 684
Cdd:PRK00635 805 RPLSSLSGGEIQRL---KLAYellapsKKPTLYVLDEPTTGLHTHDIKALIYVLqsLTHQGhTVVIIEHNMHVV 875
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
304-373 |
1.25e-03 |
|
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: 40.95 E-value: 1.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 304 EIYKRLELIDAYSAEARAASILAGLSFSPEMQKKAtKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:cd03263 97 RFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRA-RTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
620-684 |
1.37e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 1.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743842931 620 QPMYTLSGGQKSRVAFAKITFKK---PHIILLDEPSNHLDLDAVEAL---IQGLVLFQGGILMVSHDEHLI 684
Cdd:TIGR00630 825 QPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLlevLQRLVDKGNTVVVIEHNLDVI 895
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
624-685 |
1.50e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 1.50e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743842931 624 TLSGGQKSRVAFAK--------ITFkkphiiLLDEPSNHL---DLDAVEALIQGLVLFQGGILMVSHDEHLIS 685
Cdd:PRK00635 476 TLSGGEQERTALAKhlgaeligITY------ILDEPSIGLhpqDTHKLINVIKKLRDQGNTVLLVEHDEQMIS 542
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
195-396 |
1.51e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 41.26 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 195 VTLSF--GRHYGLVGRNGTGKTTFLrymaLHaIDGIprncqilHVEQE----VVGDDTSAlqcvlnsdiERTRLLEEEVR 268
Cdd:PRK13647 24 LSLSIpeGSKTALLGPNGAGKSTLL----LH-LNGI-------YLPQRgrvkVMGREVNA---------ENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 269 LHAQQRDLD------FEDAAgngkgdqIGAIN----KDAISQRLEEIykrLELIDAYsaearaasilaglsfspEMQKKA 338
Cdd:PRK13647 83 LVFQDPDDQvfsstvWDDVA-------FGPVNmgldKDEVERRVEEA---LKAVRMW-----------------DFRDKP 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743842931 339 TKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD------LHAVLWLesyLVKWPKTFIVVSH 396
Cdd:PRK13647 136 PYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDprgqetLMEILDR---LHNQGKTVIVATH 196
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
343-375 |
1.59e-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: 41.73 E-value: 1.59e-03
10 20 30
....*....|....*....|....*....|...
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLDLH 375
Cdd:COG5265 496 SGGEKQRVAIARTLLKNPPILIFDEATSALDSR 528
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
620-700 |
1.69e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.53 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 620 QPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDAVEALIQGLVLF-QGG--ILMVSHDEHLISGSVDELWVVSQ 696
Cdd:PRK10762 391 QAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFkAEGlsIILVSSEMPEVLGMSDRILVMHE 470
|
....
gi 743842931 697 GKVT 700
Cdd:PRK10762 471 GRIS 474
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
172-396 |
1.94e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.75 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 172 VKDIHLENF----NISVggrDLIVDGSVTLsfgrhygLVGRNGTGKTTFLRYMALH------AIDGIP-RNCQILHVEQE 240
Cdd:COG3950 3 IKSLTIENFrgfeDLEI---DFDNPPRLTV-------LVGENGSGKTTLLEAIALAlsgllsRLDDVKfRKLLIRNGEFG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 241 --------------VVGDDTSALQCVLNSDIERT----RLLEEEVRLHA-----QQRDLDFEDAAGNGKGDQIGAInKDA 297
Cdd:COG3950 73 dsaklilyygtsrlLLDGPLKKLERLKEEYFSRLdgydSLLDEDSNLREflewlREYLEDLENKLSDELDEKLEAV-REA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 298 ISQRLEEIyKRLElidaYSAEARAASIL--AGLSFSPEMqkkatktFSGGWR----------MRIALARALFIEPD---- 361
Cdd:COG3950 152 LNKLLPDF-KDIR----IDRDPGRLVILdkNGEELPLNQ-------LSDGERsllalvgdlaRRLAELNPALENPLegeg 219
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 743842931 362 ILLLDEPTNHldLHaVLW----LESyLVKW-PKT-FIVVSH 396
Cdd:COG3950 220 IVLIDEIDLH--LH-PKWqrriLPD-LRKIfPNIqFIVTTH 256
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
333-373 |
1.95e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 40.94 E-value: 1.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 743842931 333 EMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:PRK13640 135 DYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
343-425 |
1.96e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 41.24 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLESYLVKW--PKTFIVVSHAREFLnTVVTDILHLQgQKLTAYK 420
Cdd:PRK10789 453 SGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWgeGRTVIISAHRLSAL-TEASEILVMQ-HGHIAQR 530
|
....*
gi 743842931 421 GDYDT 425
Cdd:PRK10789 531 GNHDQ 535
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
287-396 |
2.00e-03 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 41.63 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 287 GDQIGAINKDAISQRLEE----IYKRLELIDAYSAE------------------ARAASILAGLSFSPEMQKKATKtFSG 344
Cdd:PRK10535 69 GQDVATLDADALAQLRREhfgfIFQRYHLLSHLTAAqnvevpavyaglerkqrlLRAQELLQRLGLEDRVEYQPSQ-LSG 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 743842931 345 GWRMRIALARALFIEPDILLLDEPTNHLDLHA---VLWLESYLVKWPKTFIVVSH 396
Cdd:PRK10535 148 GQQQRVSIARALMNGGQVILADEPTGALDSHSgeeVMAILHQLRDRGHTVIIVTH 202
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
522-553 |
2.01e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.75 E-value: 2.01e-03
10 20 30
....*....|....*....|....*....|...
gi 743842931 522 FKNLNFGIDLDSRIAM-VGPNGIGKSTILKLIA 553
Cdd:COG3950 14 FEDLEIDFDNPPRLTVlVGENGSGKTTLLEAIA 46
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
318-375 |
2.39e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 2.39e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 743842931 318 EARAASILAGLSfsPEMQKKATkTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLH 375
Cdd:PTZ00243 762 EADLAQLGGGLE--TEIGEKGV-NLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
343-376 |
2.90e-03 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 39.34 E-value: 2.90e-03
10 20 30
....*....|....*....|....*....|....
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLDLHA 376
Cdd:cd03215 106 SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
320-373 |
3.06e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 40.22 E-value: 3.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 743842931 320 RAASILAGLSFSPeMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:PRK13636 121 RVDNALKRTGIEH-LKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
343-373 |
3.07e-03 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 40.00 E-value: 3.07e-03
10 20 30
....*....|....*....|....*....|.
gi 743842931 343 SGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:PRK13635 142 SGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
195-373 |
3.86e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 39.69 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 195 VTLSF--GRHYGLVGRNGTGKTTFLRYMalhaidgiprNCQILHVEQEVVGDDTSAlqcvlnSDIERTRLLEEEVRLHAQ 272
Cdd:PRK13633 29 VNLEVkkGEFLVILGRNGSGKSTIAKHM----------NALLIPSEGKVYVDGLDT------SDEENLWDIRNKAGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 273 QRDLDF------EDAAgngKGDQIGAINKDAISQRLEEIYKRLELIdaysaearaasilaglsfspEMQKKATKTFSGGW 346
Cdd:PRK13633 93 NPDNQIvativeEDVA---FGPENLGIPPEEIRERVDESLKKVGMY--------------------EYRRHAPHLLSGGQ 149
|
170 180
....*....|....*....|....*..
gi 743842931 347 RMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLD 176
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
342-373 |
3.91e-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: 3.91e-03
10 20 30
....*....|....*....|....*....|..
gi 743842931 342 FSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
303-373 |
4.15e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 40.17 E-value: 4.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743842931 303 EEIYKR-LELIDaysaearaasiLAGLSfspEMQKKATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:PRK11153 115 AEIKARvTELLE-----------LVGLS---DKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
625-656 |
4.33e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 39.44 E-value: 4.33e-03
10 20 30
....*....|....*....|....*....|..
gi 743842931 625 LSGGQKSRVAFAKITFKKPHIILLDEPSNHLD 656
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANID 181
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
528-573 |
4.37e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.49 E-value: 4.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 528 GIDLD----SRIAMVGPNGIGKSTILKLIAGELQPTSGTV------FRSAKVRIAV 573
Cdd:NF033858 19 DVSLDipagCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVevlggdMADARHRRAV 74
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
342-433 |
4.83e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.39 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 342 FSGGWRMRIALARALFIEPDILLLDEPTNHLDLHAVLWLE---SYLVKWPKTFIVVSHAREFLNTVVTDILHLQGQKLTA 418
Cdd:PRK09580 146 FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAdgvNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIV 225
|
90
....*....|....*
gi 743842931 419 YKGDYdTFERTREEQ 433
Cdd:PRK09580 226 KSGDF-TLVKQLEEQ 239
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
620-700 |
6.49e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 39.53 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743842931 620 QPMYTLSGGQKSRVAFAKITFKKPHIILLDEPSNHLDLDA---VEALIQGLVLFQGGILMVSHDEHLISGSVDELWVVSQ 696
Cdd:PRK13549 401 LAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAkyeIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHE 480
|
....
gi 743842931 697 GKVT 700
Cdd:PRK13549 481 GKLK 484
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
340-373 |
8.36e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 39.26 E-value: 8.36e-03
10 20 30
....*....|....*....|....*....|....
gi 743842931 340 KTFSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:TIGR00955 165 KGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
317-376 |
8.76e-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: 39.42 E-value: 8.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743842931 317 AEARAASILAGLS------FSPEMqkkATKTFSGGWRMRIALARALFIEPDILLLDEPTNHLDLHA 376
Cdd:TIGR02633 376 AAAELQIIGSAIQrlkvktASPFL---PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGA 438
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
342-373 |
8.82e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 38.32 E-value: 8.82e-03
10 20 30
....*....|....*....|....*....|..
gi 743842931 342 FSGGWRMRIALARALFIEPDILLLDEPTNHLD 373
Cdd:PRK10908 138 LSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
|
| |
