|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
90-724 |
0e+00 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 568.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 90 FSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSLR-GSVTLNGEKVlQSRLLKVISAYVMQDDL 168
Cdd:TIGR00955 31 FCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGsGSVLLNGMPI-DAKEMRAISAYVQQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 169 LFPMLTVKETLMFASEFRLPRSLSKSKKMERVEALIDQLGLRNAANTVIGDEG-HRGVSGGERRRVSIGIDIIHDPIVLF 247
Cdd:TIGR00955 110 FIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGrVKGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 248 LDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSVFNGSPASLPGFFSDFGRPIPEKE 327
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENY 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 328 NISEFALDLVRELEGSNEGTKALvdFNEKWQQNKISLIqsapqtnkldqdrSLSLKEAINASVSR-GKLVSGSSRSNPTs 406
Cdd:TIGR00955 270 NPADFYVQVLAVIPGSENESRER--IEKICDSFAVSDI-------------GRDMLVNTNLWSGKaGGLVKDSENMEGI- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 407 metvsSYANPSLFETFILAKRYMKNWIRMPELVGTRIATVMVTGCLLATVYWKLDHTPRGAQERL-TLFAFVVPTMFYCC 485
Cdd:TIGR00955 334 -----GYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINgALFLFLTNMTFQNV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 486 LDNVPVFIQERYIFLRETTHNAYRTSSYVISHSLVSLPQLLAPSLVFSAITFWTVGLSGGLEGFVFYCLLIYASFWSGSS 565
Cdd:TIGR00955 409 FPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATS 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 566 VVTFISGVVPNIMLCYMVSITYLAYCLLLSGFYVNRDRIPFYWTWFHYISILKYPYEAVLINEFDDPSRCFvrgvqVFDS 645
Cdd:TIGR00955 489 FGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVDNIE-----CTSA 563
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15028219 646 TllggvsdsgkvklletlskslrtkiTESTCLRTGSDLLAQQGITQLSKWDCLWITFASGLFFRILFYFALLFGSRNKR 724
Cdd:TIGR00955 564 N-------------------------TTGPCPSSGEVILETLSFRNADLYLDLIGLVILIFFFRLLAYFALRIRIRRKR 617
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
91-716 |
9.10e-87 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 286.78 E-value: 9.10e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 91 SRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSLRGSVTLNGEKVLQSRLLKviSAYVMQDDLLF 170
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKR--TGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 171 PMLTVKETLMFASEFRLPRSLSKSKKMERVEALIDQLGLRNAANTVIGDEGHRGVSGGERRRVSIGIDIIHDPIVLFLDE 250
Cdd:PLN03211 153 PHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 251 PTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSVFNGSPASLPGFFSDFGRPIPEKENIS 330
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 331 EFALDL---VRELEGSNEGTKALVdfnekwqqnKISLIQS-----APQTNKLDQDRSLSLKEAINASVSRGKLVSGSSRS 402
Cdd:PLN03211 313 DFLLDLangVCQTDGVSEREKPNV---------KQSLVASyntllAPKVKAAIEMSHFPQANARFVGSASTKEHRSSDRI 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 403 nptsmeTVSSYANpslfETFILAKRYMKNwiRMPELVGT-RIATVMVTGCLLATVYWKLDHtpRGAQERLTLFAFVvpTM 481
Cdd:PLN03211 384 ------SISTWFN----QFSILLQRSLKE--RKHESFNTlRVFQVIAAALLAGLMWWHSDF--RDVQDRLGLLFFI--SI 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 482 FYCCL---DNVPVFIQERYIFLRETTHNAYRTSSYVISHSLVSLPQLLAPSLVFSAITFWTVGLSGGLEGFV--FYCLLI 556
Cdd:PLN03211 448 FWGVFpsfNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLltLLVLLG 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 557 YASFWSGSSvVTFISGVVPNIMLCYMVSITYLAYcLLLSGFYVNrdRIPFYWTWFHYISILKYPYEaVLINefddpsrcf 636
Cdd:PLN03211 528 YVLVSQGLG-LALGAAIMDAKKASTIVTVTMLAF-VLTGGFYVH--KLPSCMAWIKYISTTFYSYR-LLIN--------- 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 637 vrgVQVfdstllggvsDSGKvKLLETLSKSLRTKITESTClrtgsDLLAQQGITQLSKWDCLWITFASGLFFRILFYFAL 716
Cdd:PLN03211 594 ---VQY----------GEGK-RISSLLGCSLPHGSDRASC-----KFVEEDVAGQISPATSVSVLIFMFVGYRLLAYLAL 654
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
39-664 |
6.48e-76 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 266.97 E-value: 6.48e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 39 SFRKGDSGDGVKSD-DPAHHIIDVEALYVKPV-PYVLNFNNLQYDVTLRRRFG---FSRQN-----GVKT----LLDDVS 104
Cdd:TIGR00956 704 VFRRGSLKRAKKAGeTSASNKNDIEAGEVLGStDLTDESDDVNDEKDMEKESGediFHWRNltyevKIKKekrvILNNVD 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 105 GEASDGDILAVLGASGAGKSTLIDALAGRVAEGSLRGSVTLNGEKVLQSRLLKvISAYVMQDDLLFPMLTVKETLMFASE 184
Cdd:TIGR00956 784 GWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVITGGDRLVNGRPLDSSFQR-SIGYVQQQDLHLPTSTVRESLRFSAY 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 185 FRLPRSLSKSKKMERVEALIDQLGLRNAANTVIGDEGhRGVSGGERRRVSIGIDIIHDP-IVLFLDEPTSGLDSTNAFMV 263
Cdd:TIGR00956 863 LRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPG-EGLNVEQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWSI 941
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 264 VQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRG-KSVFNG----SPASLPGFFSDFG-RPIPEKENISEFALDLV 337
Cdd:TIGR00956 942 CKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGgQTVYFGdlgeNSHTIINYFEKHGaPKCPEDANPAEWMLEVI 1021
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 338 releGSNEGTKALVDFNEKW------QQNKisliqsapqtNKLDQ-DRSLSLKEAINASvsrgklvsgssrsnptsmETV 410
Cdd:TIGR00956 1022 ----GAAPGAHANQDYHEVWrnsseyQAVK----------NELDRlEAELSKAEDDNDP------------------DAL 1069
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 411 SSYANPSLFET-FILAKRYMKNWiRMPELVGTRIATVMVTGCLLATVYWKLDHTPRGAQER-LTLFAFVVPtmFYCCLDN 488
Cdd:TIGR00956 1070 SKYAASLWYQFkLVLWRTFQQYW-RTPDYLYSKFFLTIFAALFIGFTFFKVGTSLQGLQNQmFAVFMATVL--FNPLIQQ 1146
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 489 -VPVFI-QERYIFLRETTHNAYRTSSYVISHSLVSLPQLLAPSLVFSAITFWTVGL--------SGGLEGFVFYcLLIYA 558
Cdd:TIGR00956 1147 yLPPFVaQRDLYEVRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGFywnasktgQVHERGVLFW-LLSTM 1225
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 559 SFWSGSSVVTFISGVVPNIMLCYMVSITYLAYCLLLSGFYVNRDRIPFYWTWFHYISILKYPYEAVLinefddpsrcfvr 638
Cdd:TIGR00956 1226 FFLYFSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWIFMYRCSPFTYLVQALL------------- 1292
|
650 660
....*....|....*....|....*.
gi 15028219 639 gvqvfdSTLLGGVSDSGKVKLLETLS 664
Cdd:TIGR00956 1293 ------STGLADVPVTCKVKELLTFN 1312
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
89-307 |
1.22e-69 |
|
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: 227.15 E-value: 1.22e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 89 GFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGS-LRGSVTLNGEKvLQSRLLKVISAYVMQDD 167
Cdd:cd03234 12 KAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGtTSGQILFNGQP-RKPDQFQKCVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 168 LLFPMLTVKETLMFASEFRLPRSLSKSKKMERVEalidQLGLRNAANTVIGDEGHRGVSGGERRRVSIGIDIIHDPIVLF 247
Cdd:cd03234 91 ILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVE----DVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 248 LDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSVFNG 307
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
72-307 |
1.08e-67 |
|
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: 220.89 E-value: 1.08e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 72 VLNFNNLQYDVTLrrrfgfSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSLRGSVTLNGEKvL 151
Cdd:cd03213 3 TLSFRNLTVTVKS------SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRP-L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 152 QSRLLKVISAYVMQDDLLFPMLTVKETLMFASEFRlprslskskkmervealidqlglrnaantvigdeghrGVSGGERR 231
Cdd:cd03213 76 DKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR-------------------------------------GLSGGERK 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15028219 232 RVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSVFNG 307
Cdd:cd03213 119 RVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
86-632 |
3.82e-60 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 220.37 E-value: 3.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 86 RRFGFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVaEGSLR---GSVTLNG---EKVLqsRLLKVI 159
Cdd:TIGR00956 63 RKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNT-DGFHIgveGVITYDGitpEEIK--KHYRGD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 160 SAYVMQDDLLFPMLTVKETLMFASEFRLP--RSLSKSKKmERVEALID----QLGLRNAANTVIGDEGHRGVSGGERRRV 233
Cdd:TIGR00956 140 VVYNAETDVHFPHLTVGETLDFAARCKTPqnRPDGVSRE-EYAKHIADvymaTYGLSHTRNTKVGNDFVRGVSGGERKRV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 234 SIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQ-SGSIVIMSIHQPSARIVELLDRLIILSRGKSVFNGSPASL 312
Cdd:TIGR00956 219 SIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANiLDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 313 PGFFSDFGRPIPEKENISEFALDLV-RELEGSNEGTKALV-----DFNEKWQQNKISLIQSAPQTNKLDQDRSLSLKEAI 386
Cdd:TIGR00956 299 KQYFEKMGFKCPDRQTTADFLTSLTsPAERQIKPGYEKKVprtpqEFETYWRNSPEYAQLMKEIDEYLDRCSESDTKEAY 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 387 NASVSRGKlvsgSSRSNPTSMETVSsyanpslfetFILAKRYM--KNWIRM---PELVGTRIATVMVTGCLLATVYWKLD 461
Cdd:TIGR00956 379 RESHVAKQ----SKRTRPSSPYTVS----------FSMQVKYClaRNFLRMkgnPSFTLFMVFGNIIMALILSSVFYNLP 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 462 HTPRGAQERLTLFAFVVPTMFYCCLDNVPVFIQERYIFLRETTHNAYRTSSYVISHSLVSLPQLLAPSLVFSAITFWTVG 541
Cdd:TIGR00956 445 KNTSDFYSRGGALFFAILFNAFSSLLEIASMYEARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVN 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 542 LSGGLEGFVFYCLLIYASFWSGSSVVTFISGVVPNIMLCYMVSITYLAYCLLLSGFYVNRDRIPFYWTWFHYISILKYPY 621
Cdd:TIGR00956 525 FRRTAGRFFFYLLILFICTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAF 604
|
570
....*....|.
gi 15028219 622 EAVLINEFDDP 632
Cdd:TIGR00956 605 ESLMVNEFHGR 615
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
70-631 |
1.17e-56 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 210.09 E-value: 1.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 70 PYVLNFNNLQYDVTLRRRFgfsRQNGVK----TLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSLRGSVTL 145
Cdd:PLN03140 865 PLAMSFDDVNYFVDMPAEM---KEQGVTedrlQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRI 941
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 146 NGEKVLQSRLLKvISAYVMQDDLLFPMLTVKETLMFASEFRLPRSLSKSKKMERVEALIDQLGLRNAANTVIGDEGHRGV 225
Cdd:PLN03140 942 SGFPKKQETFAR-ISGYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTGL 1020
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 226 SGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSVF 305
Cdd:PLN03140 1021 STEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRGGQVI 1100
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 306 NGSP-----ASLPGFFSDF-GRP-IPEKENISEFALdlvrELEGSNEGTKALVDFNEKWQQNkisliqSAPQTNKldqdr 378
Cdd:PLN03140 1101 YSGPlgrnsHKIIEYFEAIpGVPkIKEKYNPATWML----EVSSLAAEVKLGIDFAEHYKSS------SLYQRNK----- 1165
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 379 slslkeainasvsrgKLVSGSSRSNP--TSMETVSSYANpSLFETF--ILAKRYMKNWiRMPELVGTRIATVMVTGCLLA 454
Cdd:PLN03140 1166 ---------------ALVKELSTPPPgaSDLYFATQYSQ-STWGQFksCLWKQWWTYW-RSPDYNLVRFFFTLAAALMVG 1228
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 455 TVYWKLDhTPRGAQERLT-----LFAFVVPTMFYCCLDNVPVFIQERYIFLRETTHNAYRTSSYVISHSLVSLPQLLAPS 529
Cdd:PLN03140 1229 TIFWKVG-TKRSNANDLTmvigaMYAAVLFVGINNCSTVQPMVAVERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQT 1307
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 530 LVFSAITFWTVGLSGGLEGFVFYCLLIYASF--WSGSSVVTFisGVVPNIMLCYMVSITYLAYCLLLSGFYVNRDRIPFY 607
Cdd:PLN03140 1308 TYYTLIVYAMVAFEWTAAKFFWFYFISFFSFlyFTYYGMMTV--SLTPNQQVAAIFAAAFYGLFNLFSGFFIPRPKIPKW 1385
|
570 580
....*....|....*....|....
gi 15028219 608 WTWFHYISILKYPYEAVLINEFDD 631
Cdd:PLN03140 1386 WVWYYWICPVAWTVYGLIVSQYGD 1409
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
70-307 |
8.38e-54 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 183.60 E-value: 8.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 70 PYVLNFNNLQYDVTLRRrfgfsrqnGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSLRGSVTLNGEK 149
Cdd:cd03232 1 GSVLTWKNLNYTVPVKG--------GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 150 VLQSrlLKVISAYVMQDDLLFPMLTVKETLMFAsefrlprslskskkmerveALIdqlglrnaantvigdeghRGVSGGE 229
Cdd:cd03232 73 LDKN--FQRSTGYVEQQDVHSPNLTVREALRFS-------------------ALL------------------RGLSVEQ 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15028219 230 RRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSR-GKSVFNG 307
Cdd:cd03232 114 RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
84-312 |
6.86e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 169.09 E-value: 6.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 84 LRRRFGfsrqngVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQ--SRLLKVIsA 161
Cdd:COG1131 6 LTKRYG------DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTS--GEVRVLGEDVARdpAEVRRRI-G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 162 YVMQDDLLFPMLTVKETLMFASEFRlprSLSKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIH 241
Cdd:COG1131 77 YVPQEPALYPDLTVRENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRKVGT-----LSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15028219 242 DPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSarIVELL-DRLIILSRGKSVFNGSPASL 312
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLE--EAERLcDRVAIIDKGRIVADGTPDEL 218
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
98-632 |
3.51e-43 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 168.87 E-value: 3.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 98 TLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVaEGSLR--GSVTLNGEKvLQSRLLKVISAYVMQDDLLFPMLTV 175
Cdd:PLN03140 179 TILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKL-DPSLKvsGEITYNGYR-LNEFVPRKTSAYISQNDVHVGVMTV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 176 KETLMFASE-------FRLPRSLSKSKK------------------MERVEA-LIDQ-----LGLRNAANTVIGDEGHRG 224
Cdd:PLN03140 257 KETLDFSARcqgvgtrYDLLSELARREKdagifpeaevdlfmkataMEGVKSsLITDytlkiLGLDICKDTIVGDEMIRG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 225 VSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQ-SGSIVIMSIHQPSARIVELLDRLIILSRGKS 303
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHlTEATVLMSLLQPAPETFDLFDDIILLSEGQI 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 304 VFNGSPASLPGFFSDFGRPIPEKENISEFaldlVRELEGSNEGTKALVDFNEKWQQnkISLIQSAPQTNKLDQDRSLSLK 383
Cdd:PLN03140 417 VYQGPRDHILEFFESCGFKCPERKGTADF----LQEVTSKKDQEQYWADRNKPYRY--ISVSEFAERFKSFHVGMQLENE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 384 EAINasvsrgklvSGSSRSNPTSMeTVSSYANPslfETFILAKRYMKNWIRMPE---LVGTRIATVMVTGCLLATVYWKL 460
Cdd:PLN03140 491 LSVP---------FDKSQSHKAAL-VFSKYSVP---KMELLKACWDKEWLLMKRnafVYVFKTVQIIIVAAIASTVFLRT 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 461 D-HTPRGAQERL----TLFAFVVpTMF------YCCLDNVPVFIQERYIFLrettHNAYrtsSYVISHSLVSLPQLLAPS 529
Cdd:PLN03140 558 EmHTRNEEDGALyigaLLFSMII-NMFngfaelALMIQRLPVFYKQRDLLF----HPPW---TFTLPTFLLGIPISIIES 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 530 LVFSAITFWTVGLSGGLEGFVFYCLLIYASFWSGSSVVTFISGVVPNIMLCYMVSITYLAYCLLLSGFYVNRDRIPFYWT 609
Cdd:PLN03140 630 VVWVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPNWWE 709
|
570 580
....*....|....*....|...
gi 15028219 610 WFHYISILKYPYEAVLINEFDDP 632
Cdd:PLN03140 710 WAYWVSPLSYGFNALAVNEMFAP 732
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
95-312 |
3.96e-41 |
|
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: 150.39 E-value: 3.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQ--SRLLKVISaYVMQDDLLFPM 172
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDS--GSILIDGEDVRKepREARRQIG-VLPDERGLYDR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 173 LTVKETLMFASEFRlprSLSKSKKMERVEALIDQLGLRNAANTVIGdeghrGVSGGERRRVSIGIDIIHDPIVLFLDEPT 252
Cdd:COG4555 89 LTVRENIRYFAELY---GLFDEELKKRIEELIELLGLEEFLDRRVG-----ELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 253 SGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSaRIVELLDRLIILSRGKSVFNGSPASL 312
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQ-EVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
424-627 |
4.12e-41 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 148.96 E-value: 4.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 424 LAKRYMKNWIRMPELVGTRIATVMVTGCLLATVYWKLDhTPRGAQERLTLFAFVVPTMFYCCLDNV-PVFIQERYIFLRE 502
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLG-NQQGGLNRPGLLFFSILFNAFSALSGIsPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 503 TTHNAYRTSSYVISHSLVSLPQLLAPSLVFSAITFWTVGLSGGLEGFVFYCLLIYASFWSGSSVVTFISGVVPNIMLCYM 582
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15028219 583 VSITYLAYCLLLSGFYVNRDRIPFYWTWFHYISILKYPYEAVLIN 627
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
86-302 |
8.91e-40 |
|
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: 145.69 E-value: 8.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 86 RRFGFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRvaEGSLRGSVTLNGEKVLQSRLLKV--ISAYV 163
Cdd:cd03225 3 KNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL--LGPTSGEVLVDGKDLTKLSLKELrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 164 MQD-DLLFPMLTVKETLMFASEFR-LPRSLSKskkmERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIH 241
Cdd:cd03225 81 FQNpDDQFFGPTVEEEVAFGLENLgLPEEEIE----ERVEEALELVGLEGLRDRSPFT-----LSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15028219 242 DPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSaRIVELLDRLIILSRGK 302
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDGK 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
84-312 |
3.30e-37 |
|
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: 138.79 E-value: 3.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 84 LRRRFGfsrqNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSR-LLKVISAY 162
Cdd:cd03263 6 LTKTYK----KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTS--GTAYINGYSIRTDRkAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 163 VMQDDLLFPMLTVKETLMFASEFRlprSLSKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHD 242
Cdd:cd03263 80 CPQFDALFDELTVREHLRFYARLK---GLPKSEIKEEVELLLRVLGLTDKANKRART-----LSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15028219 243 PIVLFLDEPTSGLDSTNAFMVVQVLKRIaQSGSIVIMSIHqpSARIVELL-DRLIILSRGKSVFNGSPASL 312
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTH--SMDEAEALcDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
97-307 |
7.90e-37 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 137.01 E-value: 7.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAE-GSLRGSVTLNGEKVLQ-SRLLKVISAYVMQDDLLFPMLT 174
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnVSVEGDIHYNGIPYKEfAEKYPGEIIYVSEEDVHFPTLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 175 VKETLMFASEFRlprslskskkmervealidqlglrnaantviGDEGHRGVSGGERRRVSIGIDIIHDPIVLFLDEPTSG 254
Cdd:cd03233 100 VRETLDFALRCK-------------------------------GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15028219 255 LDSTNAFMVVQVLKRIAQ-SGSIVIMSIHQPSARIVELLDRLIILSRGKSVFNG 307
Cdd:cd03233 149 LDSSTALEILKCIRTMADvLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
97-310 |
6.02e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 135.99 E-value: 6.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAegSLRGSVTLNGEKVLQSRllKVIsAYVMQD---DLLFPMl 173
Cdd:COG1121 19 RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP--PTSGTVRLFGKPPRRAR--RRI-GYVPQRaevDWDFPI- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 174 TVKETLM--FASEFRLPRSLSKSKKmERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFLDEP 251
Cdd:COG1121 93 TVRDVVLmgRYGRRGLFRRPSRADR-EAVDEALERVGLEDLADRPIGE-----LSGGQQQRVLLARALAQDPDLLLLDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15028219 252 TSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSArIVELLDRLIILSRGKsVFNGSPA 310
Cdd:COG1121 167 FAGVDAATEEALYELLRELRREGKTILVVTHDLGA-VREYFDRVLLLNRGL-VAHGPPE 223
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
90-318 |
2.71e-35 |
|
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: 133.61 E-value: 2.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 90 FSRQNGvKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSRLLKVIS--AYVMQ-- 165
Cdd:COG1122 8 FSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTS--GEVLVDGKDITKKNLRELRRkvGLVFQnp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 166 DDLLFpMLTVKETLMFAsefrlPRSL--SKSKKMERVEALIDQLGLRNAANTVIgdegHRgVSGGERRRVSI-GIdIIHD 242
Cdd:COG1122 85 DDQLF-APTVEEDVAFG-----PENLglPREEIRERVEEALELVGLEHLADRPP----HE-LSGGQKQRVAIaGV-LAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15028219 243 PIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSArIVELLDRLIILSRGKSVFNGSPASLpgfFSD 318
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDGRIVADGTPREV---FSD 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
97-310 |
5.04e-33 |
|
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: 127.85 E-value: 5.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAegSLRGSVTLNGEKVLQ------SRLLkvisAYVMQD-DLL 169
Cdd:COG1120 14 RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLK--PSSGEVLLDGRDLASlsrrelARRI----AYVPQEpPAP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 170 FPmLTVKETLMFAsefRLP-----RSLSKsKKMERVEALIDQLGLRNAAntvigdegHRGV---SGGERRRVSIGIDIIH 241
Cdd:COG1120 88 FG-LTVRELVALG---RYPhlglfGRPSA-EDREAVEEALERTGLEHLA--------DRPVdelSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15028219 242 DPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQS-GSIVIMSIHQPS--ARIVellDRLIILSRGKSVFNGSPA 310
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNlaARYA---DRLVLLKDGRIVAQGPPE 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
84-302 |
1.48e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 125.54 E-value: 1.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 84 LRRRFGfsRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvaegsL----RGSVTLNGEKVLQ------S 153
Cdd:COG1136 10 LTKSYG--TGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGG------LdrptSGEVLIDGQDISSlserelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 154 RL-LKVISaYVMQDDLLFPMLTVKETLMFASEFRlprSLSKSKKMERVEALIDQLGLRNAANtvigdegHRG--VSGGER 230
Cdd:COG1136 82 RLrRRHIG-FVFQFFNLLPELTALENVALPLLLA---GVSRKERRERARELLERVGLGDRLD-------HRPsqLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15028219 231 RRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIA-QSGSIVIMSIHqpSARIVELLDRLIILSRGK 302
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTH--DPELAARADRVIRLRDGR 221
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
84-308 |
1.58e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 127.53 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 84 LRRRFGfsrqngVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKvLQSRLLKVIsAYv 163
Cdd:COG4152 7 LTKRFG------DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDS--GEVLWDGEP-LDPEDRRRI-GY- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 164 mqddL-----LFPMLTVKETLM-FAsefRLpRSLSKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGI 237
Cdd:COG4152 76 ----LpeergLYPKMKVGEQLVyLA---RL-KGLSKAEAKRRADEWLERLGLGDRANKKVEE-----LSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15028219 238 DIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSarIVELL-DRLIILSRGKSVFNGS 308
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQME--LVEELcDRIVIINKGRKVLSGS 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
95-302 |
2.08e-32 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 123.28 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSRL-LKVISAYVMQDDLLFPML 173
Cdd:cd03230 11 GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDS--GEIKVLGKDIKKEPEeVKRRIGYLPEEPSLYENL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 174 TVKETLMFasefrlprslskskkmervealidqlglrnaantvigdeghrgvSGGERRRVSIGIDIIHDPIVLFLDEPTS 253
Cdd:cd03230 89 TVRENLKL--------------------------------------------SGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15028219 254 GLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSaRIVELLDRLIILSRGK 302
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGKTILLSSHILE-EAERLCDRVAILNNGR 172
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
84-302 |
2.30e-32 |
|
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: 124.91 E-value: 2.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 84 LRRRFGfsRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKVLQS--------RL 155
Cdd:cd03255 6 LSKTYG--GGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGG--LDRPTSGEVRVDGTDISKLsekelaafRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 156 LKVisAYVMQDDLLFPMLTVKETLMFASEFRlprSLSKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSI 235
Cdd:cd03255 82 RHI--GFVFQSFNLLPDLTALENVELPLLLA---GVPKKERRERAEELLERVGLGDRLNHYPSE-----LSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15028219 236 GIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIA-QSGSIVIMSIHQPsaRIVELLDRLIILSRGK 302
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDP--ELAEYADRIIELRDGK 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
87-300 |
4.18e-32 |
|
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: 124.12 E-value: 4.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 87 RFGFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVlqSRLLKVIsAYVMQD 166
Cdd:cd03293 7 SKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTS--GEVLVDGEPV--TGPGPDR-GYVFQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 167 DLLFPMLTVKETLMFASEFrlpRSLSKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVL 246
Cdd:cd03293 82 DALLPWLTVLDNVALGLEL---QGVPKAEARERAEELLELVGLSGFENAYPHQ-----LSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15028219 247 FLDEPTSGLDS-TNAFMVVQVLKRIAQSGSIVIMSIHQpsarIVE---LLDRLIILSR 300
Cdd:cd03293 154 LLDEPFSALDAlTREQLQEELLDIWRETGKTVLLVTHD----IDEavfLADRVVVLSA 207
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
100-253 |
4.22e-32 |
|
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: 121.60 E-value: 4.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQ--SRLLKVISAYVMQDDLLFPMLTVKE 177
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTE--GTILLDGQDLTDdeRKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15028219 178 TLMFAsefRLPRSLSKSKKMERVEALIDQLGLRNAANTVIGDEGHrGVSGGERRRVSIGIDIIHDPIVLFLDEPTS 253
Cdd:pfam00005 79 NLRLG---LLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPG-TLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
97-312 |
8.58e-32 |
|
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: 130.65 E-value: 8.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAegSLRGSVTLNGEKV-------LQSRLlkvisAYVMQDDLL 169
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP--PYSGSILINGVDLsdldpasWRRQI-----AWVPQNPYL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 170 FPMlTVKETLMF----ASEFRLPRSLSKSkkmeRVEALIDQL--GLrnaaNTVIGDEGhRGVSGGERRRVSIGIDIIHDP 243
Cdd:COG4988 423 FAG-TIRENLRLgrpdASDEELEAALEAA----GLDEFVAALpdGL----DTPLGEGG-RGLSGGQAQRLALARALLRDA 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15028219 244 IVLFLDEPTSGLDSTNAFMVVQVLKRIAQsGSIVIMSIHQPSAriVELLDRLIILSRGKSVFNGSPASL 312
Cdd:COG4988 493 PLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLAL--LAQADRILVLDDGRIVEQGTHEEL 558
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
94-312 |
1.76e-31 |
|
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: 123.06 E-value: 1.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 94 NGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKV--LQSRLLKVI---SAYVMQDDL 168
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTS--GSVLIDGTDInkLKGKALRQLrrqIGMIFQQFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 169 LFPMLTVKETLMFA-----SEFR-LPRSLSKSKKMERVEALiDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHD 242
Cdd:cd03256 89 LIERLSVLENVLSGrlgrrSTWRsLFGLFPKEEKQRALAAL-ERVGLLDKAYQRADQ-----LSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15028219 243 PIVLFLDEPTSGLDSTNAFMVVQVLKRIAQS-GSIVIMSIHQPS-ARivELLDRLIILSRGKSVFNGSPASL 312
Cdd:cd03256 163 PKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDlAR--EYADRIVGLKDGRIVFDGPPAEL 232
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
97-291 |
9.58e-31 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 119.89 E-value: 9.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEG-SLRGSVTLNGEKV--LQSRLLKVisAYVMQDDLLFPML 173
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfSASGEVLLNGRRLtaLPAEQRRI--GILFQDDLLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 174 TVKETLMFAsefrLPRSLSKSKKMERVEALIDQLGLrnaantviGDEGHRGV---SGGERRRVSIGIDIIHDPIVLFLDE 250
Cdd:COG4136 92 SVGENLAFA----LPPTIGRAQRRARVEQALEEAGL--------AGFADRDPatlSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15028219 251 PTSGLD-STNAFMVVQVLKRIAQSGSIVIMSIHQPS-----ARIVEL 291
Cdd:COG4136 160 PFSKLDaALRAQFREFVFEQIRQRGIPALLVTHDEEdapaaGRVLDL 206
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
100-302 |
3.21e-30 |
|
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: 118.66 E-value: 3.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGRvaEGSLRGSVTLNGEKVlqSRLLKVISAY-------VMQDDLLFPM 172
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKE--ELPTSGTIRVNGQDV--SDLRGRAIPYlrrkigvVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 173 LTVKETLMFASE--FRLPRSLSKskkmeRVEALIDQLGLRNAANTVigdegHRGVSGGERRRVSIGIDIIHDPIVLFLDE 250
Cdd:cd03292 93 RNVYENVAFALEvtGVPPREIRK-----RVPAALELVGLSHKHRAL-----PAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15028219 251 PTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHqpSARIVELLD-RLIILSRGK 302
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKINKAGTTVVVATH--AKELVDTTRhRVIALERGK 213
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
89-307 |
4.09e-30 |
|
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: 118.15 E-value: 4.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 89 GFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSRLLKVisAYVMQDDL 168
Cdd:cd03269 5 NVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDS--GEVLFDGKPLDIAARNRI--GYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 169 LFPMLTVKETLMFASEFRlprSLSKSKKMERVEALIDQLGLRNAANTVIgdeghRGVSGGERRRVSIGIDIIHDPIVLFL 248
Cdd:cd03269 81 LYPKMKVIDQLVYLAQLK---GLKKEEARRRIDEWLERLELSEYANKRV-----EELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15028219 249 DEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQpSARIVELLDRLIILSRGKSVFNG 307
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQ-MELVEELCDRVLLLNKGRAVLYG 210
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
68-312 |
4.53e-30 |
|
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: 125.65 E-value: 4.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 68 PVPYVLNFNNLqydvtlrrrfGFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNG 147
Cdd:COG4987 329 PGGPSLELEDV----------SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR--FLDPQSGSITLGG 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 148 ---EKVLQSRLLKVIsAYVMQDDLLFPMlTVKETLMF----ASEFRLPRSLskskkmERV--EALIDQL--GLrnaaNTV 216
Cdd:COG4987 397 vdlRDLDEDDLRRRI-AVVPQRPHLFDT-TLRENLRLarpdATDEELWAAL------ERVglGDWLAALpdGL----DTW 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 217 IGdEGHRGVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSiHQPSAriVELLDRLI 296
Cdd:COG4987 465 LG-EGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLIT-HRLAG--LERMDRIL 540
|
250
....*....|....*.
gi 15028219 297 ILSRGKSVFNGSPASL 312
Cdd:COG4987 541 VLEDGRIVEQGTHEEL 556
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
89-302 |
5.83e-30 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 117.62 E-value: 5.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 89 GFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAG--RVAegslRGSVTLNGEKVLQSRLLKVISAYVMQD 166
Cdd:cd03259 5 GLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGleRPD----SGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 167 DLLFPMLTVKETLMFASEFRLprsLSKSKKMERVEALIDQLGLRNAANTVIgdeghRGVSGGERRRVSIGIDIIHDPIVL 246
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRG---VPKAEIRARVRELLELVGLEGLLNRYP-----HELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15028219 247 FLDEPTSGLDS-TNAFMVVQVLKRIAQSGSIVIMSIHQPsARIVELLDRLIILSRGK 302
Cdd:cd03259 153 LLDEPLSALDAkLREELREELKELQRELGITTIYVTHDQ-EEALALADRIAVMNEGR 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
84-310 |
8.84e-30 |
|
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: 117.92 E-value: 8.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 84 LRRRFGfsrqnGVKTLlDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSRLLKVISAYV 163
Cdd:cd03219 6 LTKRFG-----GLVAL-DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTS--GSVLFDGEDITGLPPHEIARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 164 ---MQDDLLFPMLTVKETLMFASEFRLPRSL-------SKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRV 233
Cdd:cd03219 78 grtFQIPRLFPELTVLENVMVAAQARTGSGLllararrEEREARERAEELLERVGLADLADRPAGE-----LSYGQQRRL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 234 SIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSG-SIVI----MSIhqpsarIVELLDRLIILSRGKSVFNGS 308
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGiTVLLvehdMDV------VMSLADRVTVLDQGRVIAEGT 226
|
..
gi 15028219 309 PA 310
Cdd:cd03219 227 PD 228
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
91-312 |
1.10e-29 |
|
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.
Pssm-ID: 132561 [Multi-domain] Cd Length: 301 Bit Score: 119.49 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 91 SRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSRL-LKVISAYVMQDDLL 169
Cdd:TIGR03522 9 TKLYGTQNALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDS--GSVQVCGEDVLQNPKeVQRNIGYLPEHNPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 170 FPMLTVKETLMF-ASEFRLPRSLSKskkmERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFL 248
Cdd:TIGR03522 87 YLDMYVREYLQFiAGIYGMKGQLLK----QRVEEMIELVGLRPEQHKKIGQ-----LSKGYRQRVGLAQALIHDPKVLIL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15028219 249 DEPTSGLDSTNAFMVVQVLKRIAQSGSIvIMSIHqpSARIVE-LLDRLIILSRGKSVFNGSPASL 312
Cdd:TIGR03522 158 DEPTTGLDPNQLVEIRNVIKNIGKDKTI-ILSTH--IMQEVEaICDRVIIINKGKIVADKKLDEL 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
97-294 |
4.46e-29 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 114.88 E-value: 4.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAegSLRGSVTLNGEKVLQSR--LLKVIsAYVMQDDLLFPMLT 174
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLP--PSAGEVLWNGEPIRDARedYRRRL-AYLGHADGLKPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 175 VKETLMFASEFRlPRSLSKskkmERVEALIDQLGLRNAANTVIgdeghRGVSGGERRRVSIGIDIIHDPIVLFLDEPTSG 254
Cdd:COG4133 92 VRENLRFWAALY-GLRADR----EAIDEALEAVGLAGLADLPV-----RQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15028219 255 LDSTNAFMVVQVLKRIAQSGSIVIMSIHQP----SARIVELLDR 294
Cdd:COG4133 162 LDAAGVALLAELIAAHLARGGAVLLTTHQPlelaAARVLDLGDF 205
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
95-301 |
7.03e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 114.55 E-value: 7.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAegSLRGSVTLNGEKVLQSRllKVIsAYVMQD---DLLFP 171
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLK--PTSGSIRVFGKPLEKER--KRI-GYVPQRrsiDRDFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 172 mLTVKETLM--FASEFRLPRSLSKSKKmERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFLD 249
Cdd:cd03235 85 -ISVRDVVLmgLYGHKGLFRRLSKADK-AKVDEALERVGLSELADRQIGE-----LSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15028219 250 EPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSArIVELLDRLIILSRG 301
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLLNRT 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
97-307 |
8.00e-29 |
|
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: 114.60 E-value: 8.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGdILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSR--LLKVISaYVMQDDLLFPMLT 174
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSS--GTIRIDGQDVLKQPqkLRRRIG-YLPQEFGVYPNFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 175 VKETLMFASefRLpRSLSKSKKMERVEALIDQLGLRNAANTVIGdeghrGVSGGERRRVSIGIDIIHDPIVLFLDEPTSG 254
Cdd:cd03264 89 VREFLDYIA--WL-KGIPSKEVKARVDEVLELVNLGDRAKKKIG-----SLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15028219 255 LDSTNAFMVVQVLKRIAqSGSIVIMSIHqpsarIVE----LLDRLIILSRGKSVFNG 307
Cdd:cd03264 161 LDPEERIRFRNLLSELG-EDRIVILSTH-----IVEdvesLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
95-309 |
9.32e-29 |
|
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: 114.91 E-value: 9.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAegSLRGSVTLNGEKV--LQSRLLKVI---SAYVMQDDLL 169
Cdd:cd03261 11 GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLR--PDSGEVLIDGEDIsgLSEAELYRLrrrMGMLFQSGAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 170 FPMLTVKETLMFA--SEFRLPRSLSKskkmERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLF 247
Cdd:cd03261 89 FDSLTVFENVAFPlrEHTRLSEEEIR----EIVLEKLEAVGLRGAEDLYPAE-----LSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15028219 248 LDEPTSGLDSTNAFMVVQVLKRIAQS-GSIVIMSIHQPSaRIVELLDRLIILSRGKSVFNGSP 309
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLD-TAFAIADRIAVLYDGKIVAEGTP 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
89-302 |
1.13e-28 |
|
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: 112.34 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 89 GFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAegSLRGSVTLNGEKVLQSRLLKVisayvmqddl 168
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK--PTSGEILIDGKDIAKLPLEEL---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 169 lfpmltvketlmfasefrlprslskskkMERVeALIDQLglrnaantvigdeghrgvSGGERRRVSIGIDIIHDPIVLFL 248
Cdd:cd00267 72 ----------------------------RRRI-GYVPQL------------------SGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15028219 249 DEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSArIVELLDRLIILSRGK 302
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPEL-AELAADRVIVLKDGK 157
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
100-312 |
1.22e-28 |
|
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: 114.07 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSRLLKVIS---AYVMQDDLLFPMLTVK 176
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRS--GSIRFDGRDITGLPPHERARagiGYVPEGRRIFPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 177 ETLMFASEFRLPRslSKSKKMERVEALIDQLG--LRNAANTvigdeghrgVSGGERRRVSIGIDIIHDPIVLFLDEPTSG 254
Cdd:cd03224 94 ENLLLGAYARRRA--KRKARLERVYELFPRLKerRKQLAGT---------LSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15028219 255 LdstnAFMVVQ----VLKRIAQSGSIVIMsIHQPSARIVELLDRLIILSRGKSVFNGSPASL 312
Cdd:cd03224 163 L----APKIVEeifeAIRELRDEGVTILL-VEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
84-312 |
1.70e-28 |
|
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: 120.39 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 84 LRRRFGFSRQNGVKtLLDDVSGEASDGDILAVLGASGAGKSTLidalaGRVAEGSLR---GSVTLNGEKV--LQSRLLKV 158
Cdd:COG1123 266 LSKRYPVRGKGGVR-AVDDVSLTLRRGETLGLVGESGSGKSTL-----ARLLLGLLRptsGSILFDGKDLtkLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 159 IS---AYVMQD--DLLFPMLTVKETLMFAseFRLPRSLSKSKKMERVEALIDQLGLrnaantvigDEGHRGV-----SGG 228
Cdd:COG1123 340 LRrrvQMVFQDpySSLNPRMTVGDIIAEP--LRLHGLLSRAERRERVAELLERVGL---------PPDLADRyphelSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 229 ERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQS-GSIVIMSIHqpSARIVELL-DRLIILSRGKSVFN 306
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISH--DLAVVRYIaDRVAVMYDGRIVED 486
|
....*.
gi 15028219 307 GSPASL 312
Cdd:COG1123 487 GPTEEV 492
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
86-312 |
1.74e-28 |
|
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: 120.01 E-value: 1.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 86 RRFGFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRV-AEGSLRGSVTLNGEKVLQS--RLLKVISAY 162
Cdd:COG1123 8 RDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLpHGGRISGEVLLDGRDLLELseALRGRRIGM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 163 VMQD-DLLFPMLTVKETLMFASEFRlprSLSKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIH 241
Cdd:COG1123 88 VFQDpMTQLNPVTVGDQIAEALENL---GLSRAEARARVLELLEAVGLERRLDRYPHQ-----LSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15028219 242 DPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSVFNGSPASL 312
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
100-312 |
1.80e-28 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 115.95 E-value: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVL-QSRLLKVISAYVMQDDLLFPMLTVKET 178
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTS--GTARVAGYDVVrEPRKVRRSIGIVPQYASVDEDLTGREN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 179 L-MFASEFRLPRSLSKskkmERVEALIDQLGLRNAANTVIGdeghrGVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDS 257
Cdd:TIGR01188 87 LeMMGRLYGLPKDEAE----ERAEELLELFELGEAADRPVG-----TYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15028219 258 TNAFMVVQVLKRIAQSGSIVIMSIHQPSAriVELL-DRLIILSRGKSVFNGSPASL 312
Cdd:TIGR01188 158 RTRRAIWDYIRALKEEGVTILLTTHYMEE--ADKLcDRIAIIDHGRIIAEGTPEEL 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
89-302 |
4.44e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 112.22 E-value: 4.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 89 GFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAG--RVAEGSlrgsVTLNGEKVLQSRLL----KVisAY 162
Cdd:COG4619 5 GLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADldPPTSGE----IYLDGKPLSAMPPPewrrQV--AY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 163 VMQDDLLFPMlTVKETLMFASEFRlprslSKSKKMERVEALIDQLGLrnaANTVIGDEGHRgVSGGERRRVSIGIDIIHD 242
Cdd:COG4619 79 VPQEPALWGG-TVRDNLPFPFQLR-----ERKFDRERALELLERLGL---PPDILDKPVER-LSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15028219 243 PIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSI-HQPsARIVELLDRLIILSRGK 302
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVsHDP-EQIERVADRVLTLEAGR 208
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
97-312 |
5.61e-28 |
|
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: 112.77 E-value: 5.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvaegsL----RGSVTLNGEKVLQ---SRLLKVIS--AYVMQDD 167
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIG------LlrpdSGEILVDGQDITGlseKELYELRRriGMLFQGG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 168 LLFPMLTVKETLMFasefrlP----RSLSKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDP 243
Cdd:COG1127 92 ALFDSLTVFENVAF------PlrehTDLSEAEIRELVLEKLELVGLPGAADKMPSE-----LSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15028219 244 IVLFLDEPTSGLDSTNAFMVVQVLKRIAQS-GSIVIMSIHQ-PSARivELLDRLIILSRGKSVFNGSPASL 312
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDlDSAF--AIADRVAVLADGKIIAEGTPEEL 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
92-302 |
3.03e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 110.14 E-value: 3.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 92 RQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKVlqSRL-LKVISAY------VM 164
Cdd:COG2884 10 RYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG--EERPTSGQVLVNGQDL--SRLkRREIPYLrrrigvVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 165 QDDLLFPMLTVKETLMFASEFRlprSLSKSKKMERVEALIDQLGLRNAANTVIgDEghrgVSGGERRRVSIGIDIIHDPI 244
Cdd:COG2884 86 QDFRLLPDRTVYENVALPLRVT---GKSRKEIRRRVREVLDLVGLSDKAKALP-HE----LSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15028219 245 VLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSarIVELLD-RLIILSRGK 302
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE--LVDRMPkRVLELEDGR 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
90-302 |
3.83e-27 |
|
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: 110.29 E-value: 3.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 90 FSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKV--LQSRLLKVIS---AYVM 164
Cdd:cd03257 11 FPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTS--GSIIFDGKDLlkLSRRLRKIRRkeiQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 165 QDDL--LFPMLTVKETLMFASEFRLPRSlSKSKKMERVEALIDQLGLrnaantvigDEGH-----RGVSGGERRRVSIGI 237
Cdd:cd03257 89 QDPMssLNPRMTIGEQIAEPLRIHGKLS-KKEARKEAVLLLLVGVGL---------PEEVlnrypHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15028219 238 DIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRI-AQSGSIVIMSIHQPSArIVELLDRLIILSRGK 302
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGV-VAKIADRVAVMYAGK 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
77-312 |
7.65e-27 |
|
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: 116.47 E-value: 7.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 77 NLQYDVTLRR-RFGFSRQNgvKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvaegsL----RGSVTLNGE--- 148
Cdd:COG2274 469 RLKGDIELENvSFRYPGDS--PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG------LyeptSGRILIDGIdlr 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 149 ----KVLQSRLlkvisAYVMQDDLLFPMlTVKETLMFASEfrlprSLSkskkMERVEALIDQLGLRNAA-------NTVI 217
Cdd:COG2274 541 qidpASLRRQI-----GVVLQDVFLFSG-TIRENITLGDP-----DAT----DEEIIEAARLAGLHDFIealpmgyDTVV 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 218 GDEGhRGVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQsGSIVIMSIHQPSarIVELLDRLII 297
Cdd:COG2274 606 GEGG-SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLS--TIRLADRIIV 681
|
250
....*....|....*
gi 15028219 298 LSRGKSVFNGSPASL 312
Cdd:COG2274 682 LDKGRIVEDGTHEEL 696
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
95-302 |
2.11e-26 |
|
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: 107.62 E-value: 2.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKVLQSR--LLKVIS--AYVMQDDLLF 170
Cdd:cd03262 11 GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINL--LEEPDSGTIIIDGLKLTDDKknINELRQkvGMVFQQFNLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 171 PMLTVKETLMFASefRLPRSLSKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFLDE 250
Cdd:cd03262 89 PHLTVLENITLAP--IKVKGMSKAEAEERALELLEKVGLADKADAYPAQ-----LSGGQQQRVAIARALAMNPKVMLFDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15028219 251 PTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPS-ARivELLDRLIILSRGK 302
Cdd:cd03262 162 PTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGfAR--EVADRVIFMDDGR 212
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
89-314 |
2.30e-26 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 108.15 E-value: 2.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 89 GFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAegSLRGSVTLNGEKVLQ--SRLLKVISAyVMQD 166
Cdd:TIGR03864 6 GLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYV--AQSGQISVAGHDLRRapRAALARLGV-VFQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 167 DLLFPMLTVKETLMF-ASEFRLPRSLSKskkmERVEALIDQLGLRNAAntvigDEGHRGVSGGERRRVSIGIDIIHDPIV 245
Cdd:TIGR03864 83 PTLDLDLSVRQNLRYhAALHGLSRAEAR----ARIAELLARLGLAERA-----DDKVRELNGGHRRRVEIARALLHRPAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15028219 246 LFLDEPTSGLDSTNAFMVVQVLKRIAQSGSI-VIMSIH-----QPSarivellDRLIILSRGKSVFNGSPASLPG 314
Cdd:TIGR03864 154 LLLDEPTVGLDPASRAAITAHVRALARDQGLsVLWATHlvdeiEAS-------DRLVVLHRGRVLADGAAAELRG 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
89-302 |
4.49e-26 |
|
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: 105.35 E-value: 4.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 89 GFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKV----LQSRLLKVISAYVM 164
Cdd:cd03229 5 NVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAG--LEEPDSGSILIDGEDLtdleDELPPLRRRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 165 QDDLLFPMLTVKETLMFasefrlprslskskkmervealidqlglrnaantvigdeghrGVSGGERRRVSIGIDIIHDPI 244
Cdd:cd03229 83 QDFALFPHLTVLENIAL------------------------------------------GLSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15028219 245 VLFLDEPTSGLDSTNAFMVVQVLKRI-AQSGSIVIMSIHQPsARIVELLDRLIILSRGK 302
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDL-DEAARLADRVVVLRDGK 178
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
92-304 |
5.21e-26 |
|
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: 106.19 E-value: 5.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 92 RQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSRLLKVISaYVMQD--DLL 169
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESS--GSILLNGKPIKAKERRKSIG-YVMQDvdYQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 170 FpMLTVKETLMFASEfrlprslSKSKKMERVEALIDQLGLRNAAntvigdEGH-RGVSGGERRRVSIGIDIIHDPIVLFL 248
Cdd:cd03226 85 F-TDSVREELLLGLK-------ELDAGNEQAETVLKDLDLYALK------ERHpLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 249 DEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPsarivELL----DRLIILSRGKSV 304
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDY-----EFLakvcDRVLLLANGAIV 205
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
89-304 |
6.37e-26 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 107.20 E-value: 6.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 89 GFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSR---LLKVISaYVMQ 165
Cdd:COG1124 10 SYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWS--GEVTFDGRPVTRRRrkaFRRRVQ-MVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 166 DDL--LFPMLTVKETLmfaSEfrlP-RSLSKSKKMERVEALIDQLGLrnaantvigDEGHRG-----VSGGERRRVSIGI 237
Cdd:COG1124 87 DPYasLHPRHTVDRIL---AE---PlRIHGLPDREERIAELLEQVGL---------PPSFLDryphqLSGGQRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15028219 238 DIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRI-AQSGSIVIMSIHqpSARIVELL-DRLIILSRGKSV 304
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSH--DLAVVAHLcDRVAVMQNGRIV 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
90-307 |
8.25e-26 |
|
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: 105.91 E-value: 8.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 90 FSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQS-----RLLKVISAyvm 164
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDA--GFATVDGFDVVKEpaearRRLGFVSD--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 165 qDDLLFPMLTVKETLMFASEFRlprSLSKSKKMERVEALIDQLGLRNAANTVIGdeghrGVSGGERRRVSIGIDIIHDPI 244
Cdd:cd03266 86 -STGLYDRLTARENLEYFAGLY---GLKGDELTARLEELADRLGMEELLDRRVG-----GFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15028219 245 VLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSaRIVELLDRLIILSRGKSVFNG 307
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQ-EVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
97-307 |
1.01e-25 |
|
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: 104.44 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQ-SR--LLKVIsAYVMQddllfpml 173
Cdd:cd03214 12 RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSS--GEILLDGKDLASlSPkeLARKI-AYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 174 tvketlmfasefrlprslskskkmerveaLIDQLGLRNAAntvigdegHRGV---SGGERRRVSIGIDIIHDPIVLFLDE 250
Cdd:cd03214 81 -----------------------------ALELLGLAHLA--------DRPFnelSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 251 PTSGLDSTNAFMVVQVLKRIAQS-GSIVIMSIHQPS--ARIVellDRLIILSRGKSVFNG 307
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNlaARYA---DRVILLKDGRIVAQG 180
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
84-310 |
1.57e-25 |
|
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: 106.28 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 84 LRRRFGfsrqnGVKTLlDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVlqSRLlkviSAYV 163
Cdd:COG0411 10 LTKRFG-----GLVAV-DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTS--GRILFDGRDI--TGL----PPHR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 164 M---------QDDLLFPMLTVKETLM-----------FASEFRLPRSLSKSKKM-ERVEALIDQLGLRNAANTVIGDegh 222
Cdd:COG0411 76 IarlgiartfQNPRLFPELTVLENVLvaaharlgrglLAALLRLPRARREEREArERAEELLERVGLADRADEPAGN--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 223 rgVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSG--SIVI----MSIhqpsarIVELLDRLI 296
Cdd:COG0411 153 --LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILLiehdMDL------VMGLADRIV 224
|
250
....*....|....
gi 15028219 297 ILSRGKSVFNGSPA 310
Cdd:COG0411 225 VLDFGRVIAEGTPA 238
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
100-312 |
4.61e-25 |
|
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: 104.29 E-value: 4.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAegSLRGSVTLNGEKVLQSRLLKVIS---AYVMQDDLLFPMLTVK 176
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP--PRSGSIRFDGEDITGLPPHRIARlgiGYVPEGRRIFPSLTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 177 ETLMFASEFRLPRSLSKsKKMERVEALIDQLG--LRNAANTvigdeghrgVSGGERRRVSIGIDIIHDPIVLFLDEPTSG 254
Cdd:COG0410 97 ENLLLGAYARRDRAEVR-ADLERVYELFPRLKerRRQRAGT---------LSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15028219 255 LdstnAFMVVQ----VLKRIAQSG-SIVImsIHQPSARIVELLDRLIILSRGKSVFNGSPASL 312
Cdd:COG0410 167 L----APLIVEeifeIIRRLNREGvTILL--VEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
100-332 |
6.47e-25 |
|
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: 103.95 E-value: 6.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVaeGSLRGSVTLNGEKVLQSRLLKVISAYVMQDDLLFPMLTVKETL 179
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFI--KPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 180 MFASEFRLprsLSKSKKMERVEALIDQLGLRNaantvIGDEGHRGVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTN 259
Cdd:cd03299 93 AYGLKKRK---VDKKEIERKVLEIAEMLGIDH-----LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15028219 260 AFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSVFNGSPASLpgffsdFGRPIPEKenISEF 332
Cdd:cd03299 165 KEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV------FKKPKNEF--VAEF 229
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
100-312 |
7.01e-25 |
|
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: 103.22 E-value: 7.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVL-QSRLLKVISAYVMQDDLLFPMLTVKET 178
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTS--GRATVAGHDVVrEPREVRRRIGIVFQDLSVDDELTGWEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 179 L-MFASEFRLPRSLSKskkmERVEALIDQLGLRNAANTVIgdeghRGVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDS 257
Cdd:cd03265 94 LyIHARLYGVPGAERR----ERIDELLDFVGLLEAADRLV-----KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15028219 258 TNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSVFNGSPASL 312
Cdd:cd03265 165 QTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
92-298 |
1.85e-24 |
|
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: 108.14 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 92 RQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAG--RVAEGSLR-GSVTLNG--EKVLQSRLlkvisAYVMQD 166
Cdd:TIGR02857 330 AYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGfvDPTEGSIAvNGVPLADadADSWRDQI-----AWVPQH 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 167 DLLFPMlTVKETLMF----ASEFRLPRSLSKSKKMERVEALIDQLglrnaaNTVIGDEGhRGVSGGERRRVSIGIDIIHD 242
Cdd:TIGR02857 405 PFLFAG-TIAENIRLarpdASDAEIREALERAGLDEFVAALPQGL------DTPIGEGG-AGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15028219 243 PIVLFLDEPTSGLDSTNAFMVVQVLKRIAQsGSIVIMSIHQPSarIVELLDRLIIL 298
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLA--LAALADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
100-307 |
2.49e-24 |
|
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: 101.90 E-value: 2.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAG-RVAEgslRGSVTLNGEKVLQ---SRLLKVISaYVMQDDLLFpMLTV 175
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGlYKPT---SGSVLLDGTDIRQldpADLRRNIG-YVPQDVTLF-YGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 176 KETLMFASEFRLPRSLSKSKKMERVEALIDQLGlrNAANTVIGdEGHRGVSGGERRRVSIGIDIIHDPIVLFLDEPTSGL 255
Cdd:cd03245 95 RDNITLGAPLADDERILRAAELAGVTDFVNKHP--NGLDLQIG-ERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15028219 256 DSTNAFMVVQVLKRIAqSGSIVIMSIHQPSarIVELLDRLIILSRGKSVFNG 307
Cdd:cd03245 172 DMNSEERLKERLRQLL-GDKTLIIITHRPS--LLDLVDRIIVMDSGRIVADG 220
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
97-311 |
1.26e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 100.96 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGekvlqsRLLKVISAY-------VM-QD-D 167
Cdd:COG4559 14 RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSS--GEVRLNG------RPLAAWSPWelarrraVLpQHsS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 168 LLFPmLTVKETLMFAsefRLPRSLSKSKKMERVEALIDQLGLRNAAntvigdegHR---GVSGGERRRVS-------IGI 237
Cdd:COG4559 86 LAFP-FTVEEVVALG---RAPHGSSAAQDRQIVREALALVGLAHLA--------GRsyqTLSGGEQQRVQlarvlaqLWE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 238 DIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHqpsarivEL-L-----DRLIILSRGKSVFNGSPAS 311
Cdd:COG4559 154 PVDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLH-------DLnLaaqyaDRILLLHQGRLVAQGTPEE 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
90-302 |
1.66e-23 |
|
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: 97.84 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 90 FSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNG---EKVLQSRLLKVIsAYVMQD 166
Cdd:cd03228 8 FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTS--GEILIDGvdlRDLDLESLRKNI-AYVPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 167 DLLFPMlTVKETLMfasefrlprslskskkmervealidqlglrnaantvigdeghrgvSGGERRRVSIGIDIIHDPIVL 246
Cdd:cd03228 85 PFLFSG-TIRENIL---------------------------------------------SGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15028219 247 FLDEPTSGLDSTNAFMVVQVLKRIAQsGSIVIMSIHQPSAriVELLDRLIILSRGK 302
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLST--IRDADRIIVLDDGR 171
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
89-312 |
2.57e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.83 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 89 GFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGslRGSVTLNGEKV-LQSRLLKVISAYVMQDD 167
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD--AGKITVLGVPVpARARLARARIGVVPQFD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 168 LLFPMLTVKETLM-FASEFRLprslsKSKKMERV-EALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIV 245
Cdd:PRK13536 124 NLDLEFTVRENLLvFGRYFGM-----STREIEAViPSLLEFARLESKADARVSD-----LSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15028219 246 LFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHqpsarIVE----LLDRLIILSRGKSVFNGSPASL 312
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTH-----FMEeaerLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
95-307 |
3.86e-23 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 98.06 E-value: 3.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQ-SRLLKVISAYVmQDDLLFPML 173
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDS--GEITFDGKSYQKnIEALRRIGALI-EAPGFYPNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 174 TVKETL-MFASEFRLPRslskskkmERVEALIDQLGLRNaantvIGDEGHRGVSGGERRRVSIGIDIIHDPIVLFLDEPT 252
Cdd:cd03268 88 TARENLrLLARLLGIRK--------KRIDEVLDVVGLKD-----SAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15028219 253 SGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSaRIVELLDRLIILSRGKSVFNG 307
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQGITVLISSHLLS-EIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
110-307 |
4.20e-23 |
|
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: 97.95 E-value: 4.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 110 GDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSRLLKVISAYVMQDDLLFPMLTVKETLMFAsefRLPR 189
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQS--GRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLG---LSPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 190 SLSKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLD-STNAFMVVQVLK 268
Cdd:cd03298 99 LKLTAEDRQAIEVALARVGLAGLEKRLPGE-----LSGGERQRVALARVLVRDKPVLLLDEPFAALDpALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 15028219 269 RIAQSGSIVIMSIHQPSaRIVELLDRLIILSRGKSVFNG 307
Cdd:cd03298 174 LHAETKMTVLMVTHQPE-DAKRLAQRVVFLDNGRIAAQG 211
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
100-336 |
6.11e-23 |
|
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: 99.45 E-value: 6.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNG-------EKVLQSRLLKVisAYVMQddllFP- 171
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTS--GTVTIDGrditakkKKKLKDLRKKV--GLVFQ----FPe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 172 ----MLTVKETLMFAsefrlPRSLSKSKK--MERVEALIDQLGLrnaantvigDEG--HR---GVSGGERRRVSI-GIdI 239
Cdd:TIGR04521 93 hqlfEETVYKDIAFG-----PKNLGLSEEeaEERVKEALELVGL---------DEEylERspfELSGGQMRRVAIaGV-L 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 240 IHDPIVLFLDEPTSGLD--STNAFMvvQVLKRIAQS-GSIVIMSIHQPSaRIVELLDRLIILSRGKSVFNGSPASL---P 313
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDpkGRKEIL--DLFKRLHKEkGLTVILVTHSME-DVAEYADRVIVMHKGKIVLDGTPREVfsdV 234
|
250 260
....*....|....*....|...
gi 15028219 314 GFFSDFGRPIPEkenISEFALDL 336
Cdd:TIGR04521 235 DELEKIGLDVPE---ITELARKL 254
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
93-282 |
6.86e-23 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 96.72 E-value: 6.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 93 QNGVKtLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvaegSLR---GSVTLNGEKVLQSR--LLKVIS--AYVMQ 165
Cdd:TIGR01166 2 PGGPE-VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNG-----LLRpqsGAVLIDGEPLDYSRkgLLERRQrvGLVFQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 166 --DDLLFPMlTVKETLMFAsefrlPRSL--SKSKKMERVE---ALIDQLGLRNAANTVIgdeghrgvSGGERRRVSIGID 238
Cdd:TIGR01166 76 dpDDQLFAA-DVDQDVAFG-----PLNLglSEAEVERRVRealTAVGASGLRERPTHCL--------SGGEKKRVAIAGA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15028219 239 IIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIH 282
Cdd:TIGR01166 142 VAMRPDVLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
109-307 |
9.10e-23 |
|
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: 96.98 E-value: 9.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 109 DGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKVLQSRLLKVIS------AYVMQDDLLFPMLTVKETLMFA 182
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAG--LEKPDGGTIVLNGTVLFDSRKKINLPpqqrkiGLVFQQYALFPHLNVRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 183 SefrlpRSLSKSKKMERVEALIDQLGLrnaanTVIGDEGHRGVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFM 262
Cdd:cd03297 100 L-----KRKRNREDRISVDELLDLLGL-----DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15028219 263 VVQVLKRIAQSGSI-VIMSIHQPSaRIVELLDRLIILSRGKSVFNG 307
Cdd:cd03297 170 LLPELKQIKKNLNIpVIFVTHDLS-EAEYLADRIVVMEDGRLQYIG 214
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
100-299 |
1.31e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 98.01 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQS---RllkvisAYVMQDDLLFPMLTVK 176
Cdd:COG4525 23 LQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSS--GEITLDGVPVTGPgadR------GVVFQKDALLPWLNVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 177 ETLMFAseFRLpRSLSKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLD 256
Cdd:COG4525 95 DNVAFG--LRL-RGVPKAERRARAEELLALVGLADFARRRIWQ-----LSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15028219 257 S-TNAFMVVQVLKRIAQSGSIVIMSIHQpsariVE----LLDRLIILS 299
Cdd:COG4525 167 AlTREQMQELLLDVWQRTGKGVFLITHS-----VEealfLATRLVVMS 209
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
70-312 |
1.99e-22 |
|
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: 97.08 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 70 PYVLNFNNlqydVTLRRrfgfsrqnGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlRGSVTLNGEK 149
Cdd:COG1119 1 DPLLELRN----VTVRR--------GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTY-GNDVRLFGER 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 150 V-------LQSRLlkvisAYV---MQDDLLfPMLTVKETLM---FASeFRLPRSLSKSKKmERVEALIDQLGLRNAANTV 216
Cdd:COG1119 68 RggedvweLRKRI-----GLVspaLQLRFP-RDETVLDVVLsgfFDS-IGLYREPTDEQR-ERARELLELLGLAHLADRP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 217 IGDeghrgVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSI-VIMSIHQPSArIVELLDRL 295
Cdd:COG1119 140 FGT-----LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPtLVLVTHHVEE-IPPGITHV 213
|
250
....*....|....*..
gi 15028219 296 IILSRGKSVFNGSPASL 312
Cdd:COG1119 214 LLLKDGRVVAAGPKEEV 230
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
99-312 |
3.04e-22 |
|
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: 96.40 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 99 LLDDVSGEASDGDILAVLGASGAGKSTLIDALAG-RVAEgslRGSVTLNGEKV--LQSRLLKVISAYVMQDDLLFPMlTV 175
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRfYVPE---NGRVLVDGHDLalADPAWLRRQVGVVLQENVLFNR-SI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 176 KETLMFASEFRLPRSLSKSKKMERVEALIDQLglRNAANTVIGDEGhRGVSGGERRRVSIGIDIIHDPIVLFLDEPTSGL 255
Cdd:cd03252 93 RDNIALADPGMSMERVIEAAKLAGAHDFISEL--PEGYDTIVGEQG-AGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15028219 256 DSTNAFMVVQVLKRIAqSGSIVIMSIHQPSAriVELLDRLIILSRGKSVFNGSPASL 312
Cdd:cd03252 170 DYESEHAIMRNMHDIC-AGRTVIIIAHRLST--VKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
92-312 |
4.31e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 97.57 E-value: 4.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 92 RQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQ-SRLLKVISAYVMQDDLLF 170
Cdd:PRK13537 15 KRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDA--GSISLCGEPVPSrARHARQRVGVVPQFDNLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 171 PMLTVKETLM-FASEFrlprSLSKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFLD 249
Cdd:PRK13537 93 PDFTVRENLLvFGRYF----GLSAAAARALVPPLLEFAKLENKADAKVGE-----LSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15028219 250 EPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIH--QPSARiveLLDRLIILSRGKSVFNGSPASL 312
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGKTILLTTHfmEEAER---LCDRLCVIEEGRKIAEGAPHAL 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
84-312 |
1.06e-21 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 97.09 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 84 LRRRFGfsrqngVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAG--RVAEGSlrgsVTLNGEKVlqSRLL----K 157
Cdd:COG3842 11 VSKRYG------DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfeTPDSGR----ILLDGRDV--TGLPpekrN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 158 VisAYVMQDDLLFPMLTVKETLMFASEFrlpRSLSKSKKMERVEALIDQLGLrnaantviGDEGHRGV---SGGERRRVS 234
Cdd:COG3842 79 V--GMVFQDYALFPHLTVAENVAFGLRM---RGVPKAEIRARVAELLELVGL--------EGLADRYPhqlSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 235 IGIDIIHDPIVLFLDEPTSGLDstnAFMVVQV---LKRI-AQSGSIVIMSIHQPSarivELL---DRLIILSRGKSVFNG 307
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALD---AKLREEMreeLRRLqRELGITFIYVTHDQE----EALalaDRIAVMNDGRIEQVG 218
|
....*
gi 15028219 308 SPASL 312
Cdd:COG3842 219 TPEEI 223
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
102-312 |
1.09e-21 |
|
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: 97.10 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 102 DVSGEASDGDILAVLGASGAGKSTLIDALAG--RVAEG--SLRGSVTLNGEKVLQSRLLKVISAYVMQDDLLFPMLTVKE 177
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGltRPDEGeiVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 178 TLMFASEFRLPrslskSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDS 257
Cdd:TIGR02142 95 NLRYGMKRARP-----SERRISFERVIELLGIGHLLGRLPGR-----LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15028219 258 TNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSVFNGSPASL 312
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
90-308 |
1.54e-21 |
|
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: 94.18 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 90 FSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKV--LQSRLLKVIS---AYVM 164
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING--LERPTSGSVLVDGTDLtlLSGKELRKARrriGMIF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 165 QDDLLFPMLTVKETLMFASEFrlpRSLSKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPI 244
Cdd:cd03258 89 QHFNLLSSRTVFENVALPLEI---AGVPKAEIEERVLELLELVGLEDKADAYPAQ-----LSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15028219 245 VLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSI-HQPSArIVELLDRLIILSRGKSVFNGS 308
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLItHEMEV-VKRICDRVAVMEKGEVVEEGT 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
81-284 |
1.78e-21 |
|
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: 98.59 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 81 DVTLRRRFGFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAegSLRGSVTLNGE---KVLQSRLLK 157
Cdd:TIGR02868 332 KPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD--PLQGEVTLDGVpvsSLDQDEVRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 158 VISaYVMQDDLLFPMlTVKETLMF----ASEFRLPRSLSKSKKMERVEALIDQLglrnaaNTVIGDEGHRgVSGGERRRV 233
Cdd:TIGR02868 410 RVS-VCAQDAHLFDT-TVRENLRLarpdATDEELWAALERVGLADWLRALPDGL------DTVLGEGGAR-LSGGERQRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15028219 234 SIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLkRIAQSGSIVIMSIHQP 284
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDL-LAALSGRTVVLITHHL 530
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
90-307 |
2.07e-21 |
|
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: 93.94 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 90 FSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVL--QSRLLKVISAYVMQDD 167
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTS--GEVRVAGLVPWkrRKKFLRRIGVVFGQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 168 LLFPMLTVKETL-MFASEFRLPRSLSKskkmERVEALIDQLGLrnaanTVIGDEGHRGVSGGERRRVSIGIDIIHDPIVL 246
Cdd:cd03267 105 QLWWDLPVIDSFyLLAAIYDLPPARFK----KRLDELSELLDL-----EELLDTPVRQLSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15028219 247 FLDEPTSGLDSTNAFMVVQVLKRI-AQSGSIVIMSIHQpSARIVELLDRLIILSRGKSVFNG 307
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHY-MKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
95-312 |
2.98e-21 |
|
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: 92.99 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKV----LQSRLLKVISaYVMQDDLLF 170
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDS--GKILLDGQDItklpMHKRARLGIG-YLPQEASIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 171 PMLTVKETLMFASEFRlprSLSKSKKMERVEALIDQLGLRNAANTVIGdeghrGVSGGERRRVSIGIDIIHDPIVLFLDE 250
Cdd:cd03218 88 RKLTVEENILAVLEIR---GLSKKEREEKLEELLEEFHITHLRKSKAS-----SLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15028219 251 PTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHqpSAR-IVELLDRLIILSRGKSVFNGSPASL 312
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITDH--NVReTLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
91-312 |
3.33e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 93.23 E-value: 3.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 91 SRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTL---IDALAgRVAEGSLR-GSVTLNGEKVlQSRLLKVISAYVMQD 166
Cdd:PRK09493 8 SKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLlrcINKLE-EITSGDLIvDGLKVNDPKV-DERLIRQEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 167 DLLFPMLTVKETLMFASefRLPRSLSKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVL 246
Cdd:PRK09493 86 FYLFPHLTALENVMFGP--LRVRGASKEEAEKQARELLAKVGLAERAHHYPSE-----LSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15028219 247 FLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPS-ARIVEllDRLIILSRGKSVFNGSPASL 312
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGfAEKVA--SRLIFIDKGRIAEDGDPQVL 223
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
90-312 |
4.02e-21 |
|
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: 92.67 E-value: 4.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 90 FSRQNGVKTLlDDVSGEASDGDILAVLGASGAGKSTLIDALAgRVAEGSlRGSVTLNG---EKVLQSRLLKVIsAYVMQD 166
Cdd:cd03254 10 FSYDEKKPVL-KDINFSIKPGETVAIVGPTGAGKTTLINLLM-RFYDPQ-KGQILIDGidiRDISRKSLRSMI-GVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 167 DLLFPMlTVKETLMFASEfrlprslskSKKMERVEALIDQLG-------LRNAANTVIGDEGHrGVSGGERRRVSIGIDI 239
Cdd:cd03254 86 TFLFSG-TIMENIRLGRP---------NATDEEVIEAAKEAGahdfimkLPNGYDTVLGENGG-NLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15028219 240 IHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIaQSGSIVIMSIHQPSarIVELLDRLIILSRGKSVFNGSPASL 312
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLS--TIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
95-310 |
4.18e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 93.37 E-value: 4.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrVAEGSlrGSVTLNGEKVLQSRL--LKVISAYVMQDDLLFPM 172
Cdd:COG4138 7 AVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQ--GEILLNGRPLSDWSAaeLARHRAYLSQQQSPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 173 LTVKETLMFAsefrLPRSLSKSKKMERVEALIDQLGLrnaantviGDEGHRGV---SGGERRRVSIGIDI--IHDPI--- 244
Cdd:COG4138 84 MPVFQYLALH----QPAGASSEAVEQLLAQLAEALGL--------EDKLSRPLtqlSGGEWQRVRLAAVLlqVWPTInpe 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 245 --VLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIH--QPSARIVellDRLIILSRGKSVFNGSPA 310
Cdd:COG4138 152 gqLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHdlNHTLRHA---DRVWLLKQGKLVASGETA 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
84-322 |
5.82e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 93.11 E-value: 5.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 84 LRRRFGfsrQNGVktlLDDVSGEASDGDILAVLGASGAGKSTLIDALagRVAEGSLRGSVTLNGEKVL------------ 151
Cdd:PRK10619 11 LHKRYG---EHEV---LKGVSLQANAGDVISIIGSSGSGKSTFLRCI--NFLEKPSEGSIVVNGQTINlvrdkdgqlkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 152 ---QSRLLKVISAYVMQDDLLFPMLTVKETLMFASEFRLprSLSKSKKMERVEALIDQLGLrnaantvigDEGHRG---- 224
Cdd:PRK10619 83 dknQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVL--GLSKQEARERAVKYLAKVGI---------DERAQGkypv 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 225 -VSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPS-ARIVEllDRLIILSRGK 302
Cdd:PRK10619 152 hLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGfARHVS--SHVIFLHQGK 229
|
250 260
....*....|....*....|
gi 15028219 303 SVFNGSPASLpgffsdFGRP 322
Cdd:PRK10619 230 IEEEGAPEQL------FGNP 243
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
100-322 |
6.46e-21 |
|
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: 92.14 E-value: 6.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSRLLKVIsayVMQDDLLFPMLTVKETL 179
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTS--GGVILEGKQITEPGPDRMV---VFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 180 MFASEfRLPRSLSKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTN 259
Cdd:TIGR01184 76 ALAVD-RVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ-----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15028219 260 AFMVVQVLKRIAQ-SGSIVIMSIHQPSARIVeLLDRLIILSRGKSVFNGSPASLPgffsdFGRP 322
Cdd:TIGR01184 150 RGNLQEELMQIWEeHRVTVLMVTHDVDEALL-LSDRVVMLTNGPAANIGQILEVP-----FPRP 207
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
97-312 |
7.40e-21 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 92.34 E-value: 7.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKV----LQSRLLKVISaYVMQDDLLFPM 172
Cdd:TIGR04406 14 RKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDA--GKILIDGQDIthlpMHERARLGIG-YLPQEASIFRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 173 LTVKETLMFASEFRlpRSLSKSKKMERVEALIDQLGLrnaanTVIGDEGHRGVSGGERRRVSIGIDIIHDPIVLFLDEPT 252
Cdd:TIGR04406 91 LTVEENIMAVLEIR--KDLDRAEREERLEALLEEFQI-----SHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15028219 253 SGLDSTNAFMVVQVLKRIAQSGSIVIMSIHqpSARivELL---DRLIILSRGKSVFNGSPASL 312
Cdd:TIGR04406 164 AGVDPIAVGDIKKIIKHLKERGIGVLITDH--NVR--ETLdicDRAYIISDGKVLAEGTPAEI 222
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
90-295 |
1.04e-20 |
|
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: 93.58 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 90 FSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAE-GSLRGSVTLNGEKVLQ---SRLLKV----IsA 161
Cdd:COG0444 11 FPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpGITSGEILFDGEDLLKlseKELRKIrgreI-Q 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 162 YVMQDDL--LFPMLTVKETLMFAseFRLPRSLSKSKKMERVEALIDQLGLRNAANtVIGDEGHRgVSGGERRRVSIGIDI 239
Cdd:COG0444 90 MIFQDPMtsLNPVMTVGDQIAEP--LRIHGGLSKAEARERAIELLERVGLPDPER-RLDRYPHE-LSGGMRQRVMIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15028219 240 IHDPIVLFLDEPTSGLDSTnafmvVQvlkriaqsgsivimsihqpsARIVELLDRL 295
Cdd:COG0444 166 ALEPKLLIADEPTTALDVT-----IQ--------------------AQILNLLKDL 196
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
95-291 |
1.79e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 90.32 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAegSLRGSVTLNGEKVLQSRLLKVIsAYVMQDDLLFPMLT 174
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP--PAAGTIKLDGGDIDDPDVAEAC-HYLGHRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 175 VKETLMFASEFRLPRSLSkskkmerVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIG-IDIIHDPIVLfLDEPTS 253
Cdd:PRK13539 90 VAENLEFWAAFLGGEELD-------IAAALEAVGLAPLAHLPFGY-----LSAGQKRRVALArLLVSNRPIWI-LDEPTA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15028219 254 GLDSTNAFMVVQVLKRIAQSGSIVIMSIHQP----SARIVEL 291
Cdd:PRK13539 157 ALDAAAVALFAELIRAHLAQGGIVIAATHIPlglpGARELDL 198
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
97-312 |
1.81e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 91.11 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKV----LQSRLLKVIsAYVMQDDLLFPM 172
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA--GNIIIDDEDIsllpLHARARRGI-GYLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 173 LTVKETLMFASEFRlpRSLSKSKKMERVEALIDQLGLRNAANTVigdegHRGVSGGERRRVSIGIDIIHDPIVLFLDEPT 252
Cdd:PRK10895 93 LSVYDNLMAVLQIR--DDLSAEQREDRANELMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15028219 253 SGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQpsarIVELLD---RLIILSRGKSVFNGSPASL 312
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRDSGLGVLITDHN----VRETLAvceRAYIVSQGHLIAHGTPTEI 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
66-312 |
1.81e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 96.00 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 66 VKPVPYVLNFNNLQYDVTLRR-RFGFsrqNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAG--RVAEgslrGS 142
Cdd:COG1132 324 IPDPPGAVPLPPVRGEIEFENvSFSY---PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRfyDPTS----GR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 143 VTLNG---EKVLQSRLLKVIsAYVMQDDLLFPMlTVKETLMF----ASEFRLPRSLSKSKKMERVEALIDQLglrnaaNT 215
Cdd:COG1132 397 ILIDGvdiRDLTLESLRRQI-GVVPQDTFLFSG-TIRENIRYgrpdATDEEVEEAAKAAQAHEFIEALPDGY------DT 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 216 VIGDEGHRgVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQsGSIVIMSIHQPSAriVELLDRL 295
Cdd:COG1132 469 VVGERGVN-LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLST--IRNADRI 544
|
250
....*....|....*..
gi 15028219 296 IILSRGKSVFNGSPASL 312
Cdd:COG1132 545 LVLDDGRIVEQGTHEEL 561
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
95-310 |
1.97e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 91.37 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKV--LQSRLLKVISAyVM--QDDLLF 170
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDS--GEVRLNGRPLadWSPAELARRRA-VLpqHSSLSF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 171 PmLTVKETLMFAsefRLPRSLSKSKKMERVEALIDQLGLrnaanTVIGDEGHRGVSGGERRRV----------SIGidii 240
Cdd:PRK13548 90 P-FTVEEVVAMG---RAPHGLSRAEDDALVAAALAQVDL-----AHLAGRDYPQLSGGEQQRVqlarvlaqlwEPD---- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15028219 241 HDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQsgsivimsiHQPSARIVEL--L-------DRLIILSRGKSVFNGSPA 310
Cdd:PRK13548 157 GPPRWLLLDEPTSALDLAHQHHVLRLARQLAH---------ERGLAVIVVLhdLnlaaryaDRIVLLHQGRLVADGTPA 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
86-302 |
2.65e-20 |
|
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: 88.81 E-value: 2.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 86 RRFGFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQ--SRLLKVISAYV 163
Cdd:cd03246 4 ENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTS--GRVRLDGADISQwdPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 164 MQDDLLFPMlTVKETLMfasefrlprslskskkmervealidqlglrnaantvigdeghrgvSGGERRRVSIGIDIIHDP 243
Cdd:cd03246 82 PQDDELFSG-SIAENIL---------------------------------------------SGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15028219 244 IVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSAriVELLDRLIILSRGK 302
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPET--LASADRILVLEDGR 172
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
110-312 |
3.66e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 89.81 E-value: 3.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 110 GDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQS----RLLKVISayvmQDDLLFPMLTVKETLMFAseF 185
Cdd:COG3840 25 GERVAILGPSGAGKSTLLNLIAGFLPPDS--GRILWNGQDLTALppaeRPVSMLF----QENNLFPHLTVAQNIGLG--L 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 186 RLPRSLSKSKKmERVEALIDQLGLRNaantvIGDEGHRGVSGGERRRVSIGIDIIHD-PIVLfLDEPTSGLD-STNAFMv 263
Cdd:COG3840 97 RPGLKLTAEQR-AQVEQALERVGLAG-----LLDRLPGQLSGGQRQRVALARCLVRKrPILL-LDEPFSALDpALRQEM- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15028219 264 VQVLKRIAQS-GSIVIMSIHQPS--ARIVellDRLIILSRGKSVFNGSPASL 312
Cdd:COG3840 169 LDLVDELCRErGLTVLMVTHDPEdaARIA---DRVLLVADGRIAADGPTAAL 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
89-304 |
5.47e-20 |
|
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: 89.55 E-value: 5.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 89 GFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSLR---GSVTLNGEKVLQSRLlKVIS----- 160
Cdd:cd03260 5 DLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGApdeGEVLLDGKDIYDLDV-DVLElrrrv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 161 AYVMQDDLLFPMlTVKETLMFAseFRLPRSLSKSKKMERVEALIDQLGLRNAANtvigDEGH-RGVSGGERRRVSIGIDI 239
Cdd:cd03260 84 GMVFQKPNPFPG-SIYDNVAYG--LRLHGIKLKEELDERVEEALRKAALWDEVK----DRLHaLGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15028219 240 IHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMS--IHQpSARIVellDRLIILSRGKSV 304
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVThnMQQ-AARVA---DRTAFLLNGRLV 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
84-310 |
5.53e-20 |
|
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: 89.71 E-value: 5.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 84 LRRRFG-FsrqngvkTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKVLQSRLLKVISAY 162
Cdd:cd03296 8 VSKRFGdF-------VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAG--LERPDSGTILFGGEDATDVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 163 VMQDDLLFPMLTVKETLMFASEFRlPRSL--SKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDII 240
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGLRVK-PRSErpPEAEIRAKVHELLKLVQLDWLADRYPAQ-----LSGGQRQRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 241 HDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSVFNGSPA 310
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPD 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
97-305 |
1.65e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 88.99 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQ------SRLLkvisAYVMQDDLL- 169
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDS--GSILIDGKDVTKlpeykrAKYI----GRVFQDPMMg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 170 -FPMLTVKETLMFASEFRLPRSLSKSKKMERVEALIDQL-----GLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDP 243
Cdd:COG1101 93 tAPSMTIEENLALAYRRGKRRGLRRGLTKKRRELFRELLatlglGLENRLDTKVGL-----LSGGQRQALSLLMATLTKP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15028219 244 IVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSI-VIM---SIHQpsAriVELLDRLIILSRGKSVF 305
Cdd:COG1101 168 KLLLLDEHTAALDPKTAALVLELTEKIVEENNLtTLMvthNMEQ--A--LDYGNRLIMMHEGRIIL 229
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
100-332 |
2.03e-19 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 88.13 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvaegsL----RGSVTLNGEKVLQSR--LLKVIS--AYVMQDDLLFP 171
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINL------LeepdSGTITVDGEDLTDSKkdINKLRRkvGMVFQQFNLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 172 MLTVKETLMFAsefrlPRS---LSKSKKMERVEALIDQLGLRNAANtvigdegH--RGVSGGERRRVSIGIDIIHDPIVL 246
Cdd:COG1126 91 HLTVLENVTLA-----PIKvkkMSKAEAEERAMELLERVGLADKAD-------AypAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 247 FLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPS-ARivELLDRLIILSRGKSVFNGSPASlpgFFSDfgrpiPE 325
Cdd:COG1126 159 LFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGfAR--EVADRVVFMDGGRIVEEGPPEE---FFEN-----PQ 228
|
....*..
gi 15028219 326 KENISEF 332
Cdd:COG1126 229 HERTRAF 235
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
91-309 |
2.20e-19 |
|
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: 87.68 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 91 SRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKVLQSRLLKVISAYVMQDDLLF 170
Cdd:cd03300 7 SKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAG--FETPTSGEILLDGKDITNLPPHKRPVNTVFQNYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 171 PMLTVKETLMFAseFRLpRSLSKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFLDE 250
Cdd:cd03300 85 PHLTVFENIAFG--LRL-KKLPKAEIKERVAEALDLVQLEGYANRKPSQ-----LSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15028219 251 PTSGLD-STNAFMVVQvLKRIAQS-GSIVIMSIHQPSARIVeLLDRLIILSRGKSVFNGSP 309
Cdd:cd03300 157 PLGALDlKLRKDMQLE-LKRLQKElGITFVFVTHDQEEALT-MSDRIAVMNKGKIQQIGTP 215
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
87-312 |
2.21e-19 |
|
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: 87.67 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 87 RFGFsrqNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALagrvaegsLR------GSVTLNGE---KVLQSRLLK 157
Cdd:cd03253 7 TFAY---DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL--------FRfydvssGSILIDGQdirEVTLDSLRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 158 VIsAYVMQDDLLFpmltvKETLMF--------ASEfrlpRSLSKSKKMERVEALIdqLGLRNAANTVIGDEGHRgVSGGE 229
Cdd:cd03253 76 AI-GVVPQDTVLF-----NDTIGYnirygrpdATD----EEVIEAAKAAQIHDKI--MRFPDGYDTIVGERGLK-LSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 230 RRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQsGSIVIMSIHQPSArIVElLDRLIILSRGKSVFNGSP 309
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLST-IVN-ADKIIVLKDGRIVERGTH 219
|
...
gi 15028219 310 ASL 312
Cdd:cd03253 220 EEL 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
84-304 |
3.21e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.62 E-value: 3.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 84 LRRRFGfsrqnGVKtLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKV-----LQSRLLKV 158
Cdd:COG1129 10 ISKSFG-----GVK-ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDS--GEILLDGEPVrfrspRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 159 isAYVMQDDLLFPMLTVKETLMFASEFRLPRSLSKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGID 238
Cdd:COG1129 82 --AIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGD-----LSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 239 IIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSG-SIVIMSiHqpsaRIVELL---DRLIILSRGKSV 304
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGvAIIYIS-H----RLDEVFeiaDRVTVLRDGRLV 219
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
90-356 |
4.61e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 88.99 E-value: 4.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 90 FSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNG----EKvlQSRLLKVISAyVM- 164
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTS--GEVRVLGyvpfKR--RKEFARRIGV-VFg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 165 QDDLLFPMLTVKETL-MFASEFRLPRSLSKskkmERVEALIDQLGLRNAANTVIgdeghRGVSGGERRRVSIGIDIIHDP 243
Cdd:COG4586 103 QRSQLWWDLPAIDSFrLLKAIYRIPDAEYK----KRLDELVELLDLGELLDTPV-----RQLSLGQRMRCELAAALLHRP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 244 IVLFLDEPTSGLDstnafMVVQV-----LKRI-AQSGSIVIMSIHQpSARIVELLDRLIILSRGKSVFNGspaSLPGFFS 317
Cdd:COG4586 174 KILFLDEPTIGLD-----VVSKEairefLKEYnRERGTTILLTSHD-MDDIEALCDRVIVIDHGRIIYDG---SLEELKE 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 15028219 318 DFGrpiPEK-------ENISEFALDLVRELEgSNEGTKALVDFNEK 356
Cdd:COG4586 245 RFG---PYKtivlelaEPVPPLELPRGGEVI-EREGNRVRLEVDPR 286
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
100-318 |
5.08e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 87.83 E-value: 5.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSR--LLKV--ISAYVMQ--DDLLF-Pm 172
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTS--GEVLIKGEPIKYDKksLLEVrkTVGIVFQnpDDQLFaP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 173 lTVKETLMFASefrLPRSLSKSKKMERVEALIDQLGLRNAANTVigdeGHRgVSGGERRRVSIGIDIIHDPIVLFLDEPT 252
Cdd:PRK13639 95 -TVEEDVAFGP---LNLGLSKEEVEKRVKEALKAVGMEGFENKP----PHH-LSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 253 SGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQpsariVELL----DRLIILSRGKSVFNGSPASLpgfFSD 318
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLNKEGITIIISTHD-----VDLVpvyaDKVYVMSDGKIIKEGTPKEV---FSD 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
98-302 |
5.33e-19 |
|
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: 86.72 E-value: 5.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 98 TLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvaegsL----RGSVTLNGEKV----------LQSRLLkvisAYV 163
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAG------LdrptSGTVRLAGQDLfaldedararLRARHV----GFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 164 MQDDLLFPMLTVKETLMFASEFRlprslSKSKKMERVEALIDQLGLrnaantvigdeGHR------GVSGGERRRVSIGI 237
Cdd:COG4181 96 FQSFQLLPTLTALENVMLPLELA-----GRRDARARARALLERVGL-----------GHRldhypaQLSGGEQQRVALAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15028219 238 DIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRI-AQSGSIVIMSIHQPS--ARIvellDRLIILSRGK 302
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPAlaARC----DRVLRLRAGR 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
100-312 |
5.43e-19 |
|
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: 86.52 E-value: 5.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAgRVAEGSlRGSVTLNGEKV----LQSrlLKVISAYVMQDDLLFPMlTV 175
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIP-RFYDVD-SGRILIDGHDVrdytLAS--LRRQIGLVSQDVFLFND-TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 176 KETLMF----ASEFRLPRSLSKSKKMERVEALIDQLGlrnaanTVIGDeghRGV--SGGERRRVSIGIDIIHDPIVLFLD 249
Cdd:cd03251 93 AENIAYgrpgATREEVEEAARAANAHEFIMELPEGYD------TVIGE---RGVklSGGQRQRIAIARALLKDPPILILD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15028219 250 EPTSGLDSTNAFMVVQVLKRIAQS-GSIVIMsiHQPSAriVELLDRLIILSRGKSVFNGSPASL 312
Cdd:cd03251 164 EATSALDTESERLVQAALERLMKNrTTFVIA--HRLST--IENADRIVVLEDGKIVERGTHEEL 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
98-298 |
2.37e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.44 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 98 TLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLqsrllkvisAYVMQ---DDLLFPmLT 174
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTS--GTVRRAGGARV---------AYVPQrseVPDSLP-LT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 175 VKETLMFA--SEFRLPRSLSKSKKMERVEALiDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFLDEPT 252
Cdd:NF040873 74 VRDLVAMGrwARRGLWRRLTRDDRAAVDDAL-ERVGLADLAGRQLGE-----LSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15028219 253 SGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSAriVELLDRLIIL 298
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTHDLEL--VRRADPCVLL 191
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
76-309 |
2.38e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.83 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 76 NNLQYDVTLRRR----FGFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRV--AEGSLRGSVTLNGEK 149
Cdd:PRK13631 14 NPLSDDIILRVKnlycVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIksKYGTIQVGDIYIGDK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 150 VLQS---------------RLLKVISaYVMQddllFPML-----TVKETLMFAsefrlPRSL--SKSKKMERVEALIDQL 207
Cdd:PRK13631 94 KNNHelitnpyskkiknfkELRRRVS-MVFQ----FPEYqlfkdTIEKDIMFG-----PVALgvKKSEAKKLAKFYLNKM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 208 GLRNAantvIGDEGHRGVSGGERRRVSI-GIDIIHDPIVLFlDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQpSA 286
Cdd:PRK13631 164 GLDDS----YLERSPFGLSGGQKRRVAIaGILAIQPEILIF-DEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT-ME 237
|
250 260
....*....|....*....|...
gi 15028219 287 RIVELLDRLIILSRGKSVFNGSP 309
Cdd:PRK13631 238 HVLEVADEVIVMDKGKILKTGTP 260
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
100-310 |
2.66e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 85.84 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAG--RVAEGSLR-GSVTLNGEKVLQSRlLKVisAYVMQD-DLLFPMLTV 175
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGllLPEAGTITvGGMVLSEETVWDVR-RQV--GMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 176 KETLMFASEFR-LPRslskSKKMERVEALIDQLGLRNAANtvigDEGHRgVSGGERRRVSI-GIdIIHDPIVLFLDEPTS 253
Cdd:PRK13635 100 QDDVAFGLENIgVPR----EEMVERVDQALRQVGMEDFLN----REPHR-LSGGQKQRVAIaGV-LALQPDIIILDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 254 GLDSTNAFMVVQVLKRIAQSGSIVIMSI-HQpsarIVELL--DRLIILSRGKSVFNGSPA 310
Cdd:PRK13635 170 MLDPRGRREVLETVRQLKEQKGITVLSItHD----LDEAAqaDRVIVMNKGEILEEGTPE 225
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
86-321 |
4.27e-18 |
|
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: 84.86 E-value: 4.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 86 RRFGFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKVLQsrlLKVISAYVMQ 165
Cdd:TIGR02769 13 RTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLG--LEKPAQGTVSFRGQDLYQ---LDRKQRRAFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 166 DD--LLF--------PMLTVKETLmfASEFRLPRSLSKSKKMERVEALIDQLGLRNAantvIGDEGHRGVSGGERRRVSI 235
Cdd:TIGR02769 88 RDvqLVFqdspsavnPRMTVRQII--GEPLRHLTSLDESEQKARIAELLDMVGLRSE----DADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 236 GIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSVFNGSPASLPGF 315
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSF 241
|
....*.
gi 15028219 316 FSDFGR 321
Cdd:TIGR02769 242 KHPAGR 247
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
90-309 |
4.76e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 86.81 E-value: 4.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 90 FSRQNGVktllDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKVLQSRLLKVISAYVMQDDLL 169
Cdd:PRK11607 29 FDGQHAV----DDVSLTIYKGEIFALLGASGCGKSTLLRMLAG--FEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 170 FPMLTVKETLMFA-SEFRLPRSLSKSkkmeRVEALIDQLGLRNAANTvigdEGHRgVSGGERRRVSIGIDIIHDPIVLFL 248
Cdd:PRK11607 103 FPHMTVEQNIAFGlKQDKLPKAEIAS----RVNEMLGLVHMQEFAKR----KPHQ-LSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15028219 249 DEPTSGLDST----NAFMVVQVLKRIaqsGSIVIMSIH-QPSAriVELLDRLIILSRGKSVFNGSP 309
Cdd:PRK11607 174 DEPMGALDKKlrdrMQLEVVDILERV---GVTCVMVTHdQEEA--MTMAGRIAIMNRGKFVQIGEP 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
81-256 |
5.00e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.81 E-value: 5.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 81 DVTLRRrfgfsrqnGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTL-NGEKVlqsrllkvi 159
Cdd:COG0488 3 NLSKSF--------GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDS--GEVSIpKGLRI--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 160 sAYVMQDDLLFPMLTVKETLM-------------FASEFRLPRSLSKSKKMERVEALIDQLGLRNA---ANTVI------ 217
Cdd:COG0488 64 -GYLPQEPPLDDDLTVLDTVLdgdaelraleaelEELEAKLAEPDEDLERLAELQEEFEALGGWEAearAEEILsglgfp 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15028219 218 GDEGHRGV---SGGERRRVSIGIDIIHDPIVLFLDEPTSGLD 256
Cdd:COG0488 143 EEDLDRPVselSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
109-347 |
5.60e-18 |
|
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: 89.30 E-value: 5.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 109 DGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGeKVLQSRLLKVISAYVM--QDDLLFPMLTVKETLMFASEFR 186
Cdd:TIGR01257 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTS--GTVLVGG-KDIETNLDAVRQSLGMcpQHNILFHHLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 187 lprSLSKSKKMERVEALIDQLGLRNAANtvigdEGHRGVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQV 266
Cdd:TIGR01257 1032 ---GRSWEEAQLEMEAMLEDTGLHHKRN-----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 267 LKRIaQSGSIVIMSIHQPSARIVeLLDRLIILSRGKSVFNGSPASLPGFFSdfgrpipekeniSEFALDLVRELE----- 341
Cdd:TIGR01257 1104 LLKY-RSGRTIIMSTHHMDEADL-LGDRIAIISQGRLYCSGTPLFLKNCFG------------TGFYLTLVRKMKniqsq 1169
|
....*..
gi 15028219 342 -GSNEGT 347
Cdd:TIGR01257 1170 rGGCEGT 1176
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
97-256 |
6.54e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.54 E-value: 6.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKV----LQSRLLKVISaYVMQDDLLFPM 172
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDS--GRIFLDGEDIthlpMHKRARLGIG-YLPQEASIFRK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 173 LTVKETLMFASEFrlpRSLSKSKKMERVEALIDQLGLRNAANTvigdeghRG--VSGGERRRVSIGIDIIHDPIVLFLDE 250
Cdd:COG1137 93 LTVEDNILAVLEL---RKLSKKEREERLEELLEEFGITHLRKS-------KAysLSGGERRRVEIARALATNPKFILLDE 162
|
....*.
gi 15028219 251 PTSGLD 256
Cdd:COG1137 163 PFAGVD 168
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
84-302 |
6.63e-18 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 83.17 E-value: 6.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 84 LRRRFgfsRQNGVKT-LLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKVL------QSRLL 156
Cdd:TIGR02211 7 LGKRY---QEGKLDTrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGG--LDNPTSGEVLFNGQSLSklssneRAKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 157 KVISAYVMQDDLLFPMLTVKETLMFASefrLPRSLSKSKKMERVEALIDQLGLRNAANtvigdegHRG--VSGGERRRVS 234
Cdd:TIGR02211 82 NKKLGFIYQFHHLLPDFTALENVAMPL---LIGKKSVKEAKERAYEMLEKVGLEHRIN-------HRPseLSGGERQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 235 IGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRI--AQSGSIVIMSiHQPsaRIVELLDRLIILSRGK 302
Cdd:TIGR02211 152 IARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELnrELNTSFLVVT-HDL--ELAKKLDRVLEMKDGQ 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
95-312 |
1.30e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.66 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKV--LQSRLLKVISAYVMQDDLLFPM 172
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTA--GTVLVAGDDVeaLSARAASRRVASVPQDTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 173 LTVKETLMFAsefRLPRSLSKSKKMERVEALIDQlGLRNAANTVIGDEGHRGVSGGERRRVSIGIDIIHDPIVLFLDEPT 252
Cdd:PRK09536 92 FDVRQVVEMG---RTPHRSRFDTWTETDRAAVER-AMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15028219 253 SGLDSTNAFMVVQVLKRIAQSGSIVIMSIH--QPSARIVellDRLIILSRGKSVFNGSPASL 312
Cdd:PRK09536 168 ASLDINHQVRTLELVRRLVDDGKTAVAAIHdlDLAARYC---DELVLLADGRVRAAGPPADV 226
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
95-283 |
1.82e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 82.37 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALagRVAEGSLRGSVTLNGEK--------VLQSRLLKVISAYVMQD 166
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVL--NLLEMPRSGTLNIAGNHfdfsktpsDKAIRELRRNVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 167 DLLFPMLTVKETLMFAsefrlP---RSLSKSKKMERVEALIDQLGLRNAAntvigDEGHRGVSGGERRRVSIGIDIIHDP 243
Cdd:PRK11124 91 YNLWPHLTVQQNLIEA-----PcrvLGLSKDQALARAEKLLERLRLKPYA-----DRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15028219 244 IVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQ 283
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
92-311 |
2.11e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 82.29 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 92 RQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrVAEGSlrGSVTLNGEKVLQSRL--LKVISAYVMQDDLL 169
Cdd:PRK03695 4 NDVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGS--GSIQFAGQPLEAWSAaeLARHRAYLSQQQTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 170 FPMLTVKETLMFAsefrLPRSLSKSKKMERVEALIDQLGLrnaantviGDEGHRGV---SGGERRRVSIGIDI--IHDPI 244
Cdd:PRK03695 81 PFAMPVFQYLTLH----QPDKTRTEAVASALNEVAEALGL--------DDKLGRSVnqlSGGEWQRVRLAAVVlqVWPDI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15028219 245 -----VLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSaRIVELLDRLIILSRGKSVFNGSPAS 311
Cdd:PRK03695 149 npagqLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLN-HTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
97-319 |
2.28e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 86.05 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVaegSLRGSVTLNG----EKVLQSRLLKVisAYVMQDDLLFPM 172
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL---PYQGSLKINGielrELDPESWRKHL--SWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 173 lTVKETLMF----ASEFRLPRSLSKSKKMERVEALidQLGLrnaaNTVIGDEGhRGVSGGERRRVSIGIDIIHDPIVLFL 248
Cdd:PRK11174 438 -TLRDNVLLgnpdASDEQLQQALENAWVSEFLPLL--PQGL----DTPIGDQA-AGLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15028219 249 DEPTSGLDSTNAFMVVQVLKRIAQsGSIVIMSIHqpsaRIVEL--LDRLIILSRGKSVFNGSPASL---PGFFSDF 319
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNAASR-RQTTLMVTH----QLEDLaqWDQIWVMQDGQIVQQGDYAELsqaGGLFATL 580
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
95-302 |
2.81e-17 |
|
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: 81.15 E-value: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKVLQSRLLKVISAYVMQDDLLFPMLT 174
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAG--LEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQNYALYPHMT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 175 VKETLMFAseFRLpRSLSKSKKMERVEALIDQLGLRNaantvIGDEGHRGVSGGERRRVSIGIDIIHDPIVLFLDEPTSG 254
Cdd:cd03301 89 VYDNIAFG--LKL-RKVPKDEIDERVREVAELLQIEH-----LLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15028219 255 LDSTNAFMVVQVLKRIAQS-GSIVIMSIH-QPSAriVELLDRLIILSRGK 302
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRlGTTTIYVTHdQVEA--MTMADRIAVMNDGQ 208
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
97-311 |
5.10e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.02 E-value: 5.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSRL-LKVIS---AYVMQ--DDLLF 170
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTS--GKIIIDGVDITDKKVkLSDIRkkvGLVFQypEYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 171 PMlTVKETLMFAsefrlPRSL--SKSKKMERVEALIDQLGLrnaANTVIGDEGHRGVSGGERRRVSIGIDIIHDPIVLFL 248
Cdd:PRK13637 98 EE-TIEKDIAFG-----PINLglSEEEIENRVKRAMNIVGL---DYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15028219 249 DEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSVFNGSPAS 311
Cdd:PRK13637 169 DEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
95-274 |
1.06e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 80.06 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDAL-------AG--RVAEGSLRGSVTLNGEkvlQSRLLKVISAYVMQ 165
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGqlNIAGHQFDFSQKPSEK---AIRLLRQKVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 166 DDLLFPMLTVKETLMFASEFRLprSLSKSKKMERVEALIDQLGLRNAAntvigDEGHRGVSGGERRRVSIGIDIIHDPIV 245
Cdd:COG4161 90 QYNLWPHLTVMENLIEAPCKVL--GLSKEQAREKAMKLLARLRLTDKA-----DRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180
....*....|....*....|....*....
gi 15028219 246 LFLDEPTSGLDSTNAFMVVQVLKRIAQSG 274
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTG 191
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
92-345 |
1.07e-16 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 80.04 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 92 RQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIdALAGRVAEGSlRGSVTLNGEKVLQ---SRLLKVIsAYVMQDDL 168
Cdd:cd03295 9 RYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTM-KMINRLIEPT-SGEIFIDGEDIREqdpVELRRKI-GYVIQQIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 169 LFPMLTVKETLMFasefrLPRSL--SKSKKMERVEALIDQLGLRNAAntvIGDEGHRGVSGGERRRVSIGIDIIHDPIVL 246
Cdd:cd03295 86 LFPHMTVEENIAL-----VPKLLkwPKEKIRERADELLALVGLDPAE---FADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 247 FLDEPTSGLDSTNAFMVVQVLKRIAQ-SGSIVIMSIHQPSARIVeLLDRLIILSRGKSVFNGSPASLpgffsdFGRPipe 325
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQeLGKTIVFVTHDIDEAFR-LADRIAIMKNGEIVQVGTPDEI------LRSP--- 227
|
250 260
....*....|....*....|
gi 15028219 326 kenisefALDLVRELEGSNE 345
Cdd:cd03295 228 -------ANDFVAEFVGADR 240
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
90-353 |
1.97e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 81.28 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 90 FSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvaegsL----RGSVTLNGEKVLQ---SRLLKV---I 159
Cdd:COG1135 11 FPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL------LerptSGSVLVDGVDLTAlseRELRAArrkI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 160 SaYVMQDDLLFPMLTVKETLMFASEFrlpRSLSKSKKMERVEALIDQLGLrnaantvigdEGHRGV-----SGGERRRVS 234
Cdd:COG1135 85 G-MIFQHFNLLSSRTVAENVALPLEI---AGVPKAEIRKRVAELLELVGL----------SDKADAypsqlSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 235 IGIDIIHDPIVLFLDEPTSGLD--STNAfmVVQVLKRIAQS-G-SIVI----MSIhqpsarIVELLDRLIILSRGKSVFN 306
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDpeTTRS--ILDLLKDINRElGlTIVLitheMDV------VRRICDRVAVLENGRIVEQ 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 15028219 307 GSPASLpgffsdFGRP--------IPEKENISEFALDLVRELEGSNEGTKALVDF 353
Cdd:COG1135 223 GPVLDV------FANPqseltrrfLPTVLNDELPEELLARLREAAGGGRLVRLTF 271
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
73-307 |
2.59e-16 |
|
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: 77.35 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 73 LNFNNLQydvtlrrrFGFSRQNgvKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKV-- 150
Cdd:cd03247 1 LSINNVS--------FSYPEQE--QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DLKPQQGEITLDGVPVsd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 151 LQSRLLKVISaYVMQDDLLFpmltvKETLMfasefrlprslskskkmervealiDQLGLRnaantvigdeghrgVSGGER 230
Cdd:cd03247 69 LEKALSSLIS-VLNQRPYLF-----DTTLR------------------------NNLGRR--------------FSGGER 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15028219 231 RRVSIGIDIIHD-PIVLfLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSariVELLDRLIILSRGKSVFNG 307
Cdd:cd03247 105 QRLALARILLQDaPIVL-LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTG---IEHMDKILFLENGKIIMQG 178
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
84-304 |
3.64e-16 |
|
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: 76.31 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 84 LRRRFGfsrqnGVKTLlDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVlqsrllkvisayv 163
Cdd:cd03216 6 ITKRFG-----GVKAL-DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDS--GEILVDGKEV------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 164 mqddllfpmltvketlmfasEFRLPRslsksKKMERVEALIDQLglrnaantvigdeghrgvSGGERRRVSIGIDIIHDP 243
Cdd:cd03216 65 --------------------SFASPR-----DARRAGIAMVYQL------------------SVGERQMVEIARALARNA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15028219 244 IVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSaRIVELLDRLIILSRGKSV 304
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLD-EVFEIADRVTVLRDGRVV 161
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
100-312 |
7.08e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 77.61 E-value: 7.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAG--RVAEgslrGSVTLNGEKVLQ---SRLLKVISAYVMQDDLLFPMLT 174
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGdpRATS----GRIVFDGKDITDwqtAKIMREAVAIVPEGRRVFSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 175 VKETLMFASEFrlPRSLSKSKKMERVEALIDQLGLRNA--ANTvigdeghrgVSGGERRRVSIGIDIIHDPIVLFLDEPT 252
Cdd:PRK11614 97 VEENLAMGGFF--AERDQFQERIKWVYELFPRLHERRIqrAGT---------MSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 253 SGLDSTNAFMVVQVLKRIAQSGsIVIMSIHQPSARIVELLDRLIILSRGKSVFNGSPASL 312
Cdd:PRK11614 166 LGLAPIIIQQIFDTIEQLREQG-MTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDAL 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
100-310 |
8.07e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.84 E-value: 8.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKV-----LQSRLLKVisAYVMQDDLLFPMLT 174
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDS--GEILIDGKPVrirspRDAIALGI--GMVHQHFMLVPNLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 175 VKETLMFASEFRLPRSLSKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSI------GIDIihdpivLFL 248
Cdd:COG3845 97 VAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVED-----LSVGEQQRVEIlkalyrGARI------LIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15028219 249 DEPTSGL--DSTNAFMvvQVLKRIAQSG-SIVIMS--IHQpsarIVELLDRLIILSRGKSVFNGSPA 310
Cdd:COG3845 166 DEPTAVLtpQEADELF--EILRRLAAEGkSIIFIThkLRE----VMAIADRVTVLRRGKVVGTVDTA 226
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
97-310 |
8.77e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 78.33 E-value: 8.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEG------SLRGSVTLNGEKVLQ---SRLLKVISAYVMQDD 167
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgaRVTGDVTLNGEPLAAidaPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 168 LLFPmLTVKETLMFAsefRLPRSLSKSKKMERVEALIDQLGLRNAANTVIGdeghRGV---SGGERRRVSIGI------- 237
Cdd:PRK13547 94 PAFA-FSAREIVLLG---RYPHARRAGALTHRDGEIAWQALALAGATALVG----RDVttlSGGELARVQFARvlaqlwp 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15028219 238 --DIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSI-HQP--SARIVellDRLIILSRGKSVFNGSPA 310
Cdd:PRK13547 166 phDAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIvHDPnlAARHA---DRIAMLADGAIVAHGAPA 240
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
89-282 |
1.13e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.43 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 89 GFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSRLLKvisAYVMQDDL 168
Cdd:PRK11248 6 HLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQH--GSITLDGKPVEGPGAER---GVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 169 LFPMLTVKETLMFASEFrlpRSLSKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFL 248
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQL---AGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQ-----LSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190
....*....|....*....|....*....|....*
gi 15028219 249 DEPTSGLDS-TNAFMVVQVLKRIAQSGSIVIMSIH 282
Cdd:PRK11248 153 DEPFGALDAfTREQMQTLLLKLWQETGKQVLLITH 187
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
93-291 |
1.74e-15 |
|
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: 75.47 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 93 QNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAegSLRGSVTLNGEKVLQSR-LLKVISAYVMQDDLLFP 171
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLR--PDSGEVRWNGTPLAEQRdEPHENILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 172 MLTVKETLMFASEFRLPRSLSkskkmerVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFLDEP 251
Cdd:TIGR01189 87 ELSALENLHFWAAIHGGAQRT-------IEDALAAVGLTGFEDLPAAQ-----LSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15028219 252 TSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQP----SARIVEL 291
Cdd:TIGR01189 155 TTALDKAGVALLAGLLRAHLARGGIVLLTTHQDlglvEARELRL 198
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
81-308 |
1.86e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.01 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 81 DVTLRrrFGFSRQNgvktlLDDVSGEASDGDILAVLGASGAGKSTLIdALAGRVAEGSLrGSVTLNGE---KVLQSRLLK 157
Cdd:PRK13657 339 DVSFS--YDNSRQG-----VEDVSFEAKPGQTVAIVGPTGAGKSTLI-NLLQRVFDPQS-GRILIDGTdirTVTRASLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 158 VIsAYVMQDDLLFPMlTVKETLMF----ASEFRLPRSLSKSKKMERVEALIDQLglrnaaNTVIGDEGhRGVSGGERRRV 233
Cdd:PRK13657 410 NI-AVVFQDAGLFNR-SIEDNIRVgrpdATDEEMRAAAERAQAHDFIERKPDGY------DTVVGERG-RQLSGGERQRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15028219 234 SIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSiHQPSAriVELLDRLIILSRGKSVFNGS 308
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIA-HRLST--VRNADRILVFDNGRVVESGS 552
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
108-308 |
2.06e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.98 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 108 SDGDILAVLGASGAGKSTLIDALAGRVAEGSLRGS-VTLNGEKVLQS-RLLKVI------SAYVMQDDLLFPMLTVKETL 179
Cdd:PRK09984 28 HHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGShIELLGRTVQREgRLARDIrksranTGYIFQQFNLVNRLSVLENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 180 MFASEFRLP------RSLSKSKKMERVEALIdQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFLDEPTS 253
Cdd:PRK09984 108 LIGALGSTPfwrtcfSWFTREQKQRALQALT-RVGMVHFAHQRVST-----LSGGQQQRVAIARALMQQAKVILADEPIA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15028219 254 GLDSTNAFMVVQVLKRIAQSGSI-VIMSIHQPSARIvELLDRLIILSRGKSVFNGS 308
Cdd:PRK09984 182 SLDPESARIVMDTLRDINQNDGItVVVTLHQVDYAL-RYCERIVALRQGHVFYDGS 236
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
100-308 |
2.83e-15 |
|
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: 79.38 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIdALAGRVAEGSlRGSVTLNGEKVLQSRL--LKVISAYVMQDDLLFPMlTVKE 177
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLV-NLIPRFYEPD-SGQILLDGHDLADYTLasLRRQVALVSQDVVLFND-TIAN 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 178 TLMF-----ASEFRLPRSLSKSKKMERVEALidQLGLrnaaNTVIGDEGHRgVSGGERRRVSIGIDIIHDPIVLFLDEPT 252
Cdd:TIGR02203 425 NIAYgrteqADRAEIERALAAAYAQDFVDKL--PLGL----DTPIGENGVL-LSGGQRQRLAIARALLKDAPILILDEAT 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15028219 253 SGLDSTNAFMVVQVLKRIAQS-GSIVIMsiHQPSAriVELLDRLIILSRGKSVFNGS 308
Cdd:TIGR02203 498 SALDNESERLVQAALERLMQGrTTLVIA--HRLST--IEKADRIVVMDDGRIVERGT 550
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
97-309 |
2.89e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.87 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSLRGSVTLNGEKVLQ----SRLLKVISaYVMQDDLLFPM 172
Cdd:COG0396 13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEVTSGSILLDGEDILElspdERARAGIF-LAFQYPVEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 173 LTVKETLMFASEFRLPRSLSKSKKMERVEALIDQLGLRNAAntvigdeGHRGV----SGGERRRVSIGIDIIHDPIVLFL 248
Cdd:COG0396 92 VSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEDF-------LDRYVnegfSGGEKKRNEILQMLLLEPKLAIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15028219 249 DEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPsaRIVELL--DRLIILSRGKSVFNGSP 309
Cdd:COG0396 165 DETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQ--RILDYIkpDFVHVLVDGRIVKSGGK 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
102-309 |
3.32e-15 |
|
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: 76.53 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 102 DVSGEASDGDILAVLGASGAGKSTLIDALaGRVAEGSlRGSVTLNGEKVLQ---SRLLKVIS---AYVMQDDLLFPMLTV 175
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCI-NRLIEPT-SGKVLIDGQDIAAmsrKELRELRRkkiSMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 176 KETLMFASEFRlprSLSKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFLDEPTSGL 255
Cdd:cd03294 120 LENVAFGLEVQ---GVPRAEREERAAEALELVGLEGWEHKYPDE-----LSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15028219 256 DST-NAFMVVQVLKRIAQSGSIVIMSIHQPsARIVELLDRLIILSRGKSVFNGSP 309
Cdd:cd03294 192 DPLiRREMQDELLRLQAELQKTIVFITHDL-DEALRLGDRIAIMKDGRLVQVGTP 245
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
100-344 |
3.71e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 76.41 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGE--------KVLQSRLLKVISAYVMQDDLLFP 171
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSS--GTITIAGYhitpetgnKNLKKLRKKVSLVFQFPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 172 MlTVKETLMFAsefrlPRSLSKSKKMERVEAL--IDQLGLrnaaNTVIGDEGHRGVSGGERRRVSIGIDIIHDPIVLFLD 249
Cdd:PRK13641 101 N-TVLKDVEFG-----PKNFGFSEDEAKEKALkwLKKVGL----SEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 250 EPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSaRIVELLDRLIILSRGKSVFNGSPASLpgfFSDfgRPIPEKENI 329
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMD-DVAEYADDVLVLEHGKLIKHASPKEI---FSD--KEWLKKHYL 244
|
250
....*....|....*.
gi 15028219 330 SEFALDL-VRELEGSN 344
Cdd:PRK13641 245 DEPATSRfASKLEKGG 260
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
97-332 |
4.00e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.56 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDAL-------AG--RVAEGSLRGSVTLNGEKVLqSRLLKVISAYVMQDD 167
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGtiRVGDITIDTARSLSQQKGL-IRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 168 LLFPMLTVKETLMFASEfrLPRSLSKSKKMERVEALIDQLGLRNAANTVigdegHRGVSGGERRRVSIGIDIIHDPIVLF 247
Cdd:PRK11264 95 NLFPHRTVLENIIEGPV--IVKGEPKEEATARARELLAKVGLAGKETSY-----PRRLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 248 LDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPS-ARivELLDRLIILSRGKSVFNGSPASLpgfFSDfgrpiPEK 326
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSfAR--DVADRAIFMDQGRIVEQGPAKAL---FAD-----PQQ 237
|
....*.
gi 15028219 327 ENISEF 332
Cdd:PRK11264 238 PRTRQF 243
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
110-308 |
6.13e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.36 E-value: 6.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 110 GDILAVLGASGAGKST-------LIDALAGRVAEGSL------RGSVTLNGEKVLQSRLLKVIS-AYVMQDDL--LFPML 173
Cdd:PRK10261 42 GETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDKMllrrrsRQVIELSEQSAAQMRHVRGADmAMIFQEPMtsLNPVF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 174 TVKETLmfASEFRLPRSLSKSKKMERVEALIDQLGLRNAaNTVIGDEGHRgVSGGERRRVSIGIDIIHDPIVLFLDEPTS 253
Cdd:PRK10261 122 TVGEQI--AESIRLHQGASREEAMVEAKRMLDQVRIPEA-QTILSRYPHQ-LSGGMRQRVMIAMALSCRPAVLIADEPTT 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15028219 254 GLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSVFNGS 308
Cdd:PRK10261 198 ALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGS 252
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
84-301 |
6.59e-15 |
|
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: 74.78 E-value: 6.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 84 LRRRFGFSRQNGVK-TLLDDVSGEASDGDILAVLGASGAGKSTLIDALAG--RVAEGSLRgsVTLNGEKVlqsrllkvis 160
Cdd:COG4778 10 LSKTFTLHLQGGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnyLPDSGSIL--VRHDGGWV---------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 161 ayvmqdDLL----FPMLTV-KETLMFASEF-R-LPR--------------SLSKSKKMERVEALIDQLGL-----RNAAN 214
Cdd:COG4778 78 ------DLAqaspREILALrRRTIGYVSQFlRvIPRvsaldvvaepllerGVDREEARARARELLARLNLperlwDLPPA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 215 TVigdeghrgvSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARiVELLDR 294
Cdd:COG4778 152 TF---------SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVR-EAVADR 221
|
....*..
gi 15028219 295 LIILSRG 301
Cdd:COG4778 222 VVDVTPF 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
100-312 |
7.00e-15 |
|
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: 74.88 E-value: 7.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALagrvaegsLR------GSVTLNGEKV--LQSRLLKVISAYVMQDDLLFP 171
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLL--------ERfydptsGEILLDGVDIrdLNLRWLRSQIGLVSQEPVLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 172 MlTVKETLMFAsefRLPRSLSKSKKMERvEALIDQL--GLRNAANTVIGDEGHRgVSGGERRRVSIGIDIIHDPIVLFLD 249
Cdd:cd03249 91 G-TIAENIRYG---KPDATDEEVEEAAK-KANIHDFimSLPDGYDTLVGERGSQ-LSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15028219 250 EPTSGLDSTNAFMVVQVLKRIAQsGSIVIMSIHQPSAriVELLDRLIILSRGKSVFNGSPASL 312
Cdd:cd03249 165 EATSALDAESEKLVQEALDRAMK-GRTTIVIAHRLST--IRNADLIAVLQNGQVVEQGTHDEL 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
110-313 |
8.22e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.78 E-value: 8.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 110 GDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGekVLQSRLLKV----ISAY-VMQDDLLFPMLTVKETLMfase 184
Cdd:PRK15439 37 GEVHALLGGNGAGKSTLMKIIAGIVPPDS--GTLEIGG--NPCARLTPAkahqLGIYlVPQEPLLFPNLSVKENIL---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 185 FRLPRSlskSKKMERVEALIDQLG----LRNAANTV-IGDeghrgvsggeRRRVSIGIDIIHDPIVLFLDEPTSGL---D 256
Cdd:PRK15439 109 FGLPKR---QASMQKMKQLLAALGcqldLDSSAGSLeVAD----------RQIVEILRGLMRDSRILILDEPTASLtpaE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15028219 257 STNAFMVVQVLKriAQSGSIVIMSIHQPSARivELLDRLIILSRGKSVFNGSPASLP 313
Cdd:PRK15439 176 TERLFSRIRELL--AQGVGIVFISHKLPEIR--QLADRISVMRDGTIALSGKTADLS 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
95-312 |
9.74e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.22 E-value: 9.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSRLLKV--ISAYVMQ--DDLLF 170
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTS--GSVLIRGEPITKENIREVrkFVGLVFQnpDDQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 171 PMlTVKETLMFASefrLPRSLSKSKKMERVEALIDQLGLRNAANTVigdeGHRgVSGGERRRVSIGIDIIHDPIVLFLDE 250
Cdd:PRK13652 93 SP-TVEQDIAFGP---INLGLDEETVAHRVSSALHMLGLEELRDRV----PHH-LSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15028219 251 PTSGLDSTNAFMVVQVLKRIAQS-GSIVIMSIHQPSArIVELLDRLIILSRGKSVFNGSPASL 312
Cdd:PRK13652 164 PTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDL-VPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
97-338 |
1.25e-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: 77.15 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSLRGSVTLN----------------GEK--VLQSRLLKV 158
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHvalcekcgyverpskvGEPcpVCGGTLEPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 159 ISAYVMQDDLLFPMLTVKETLMFASEFRL----------PRSL-----SKSKKMERVEALIDQLGLRNAANTVIgdeghR 223
Cdd:TIGR03269 93 EVDFWNLSDKLRRRIRKRIAIMLQRTFALygddtvldnvLEALeeigyEGKEAVGRAVDLIEMVQLSHRITHIA-----R 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 224 GVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSI-VIMSIHQPSArIVELLDRLIILSRGK 302
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIsMVLTSHWPEV-IEDLSDKAIWLENGE 246
|
250 260 270
....*....|....*....|....*....|....*.
gi 15028219 303 SVFNGSPASLPGFFSDfGRPIPEKENISEFALDLVR 338
Cdd:TIGR03269 247 IKEEGTPDEVVAVFME-GVSEVEKECEVEVGEPIIK 281
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
96-302 |
1.38e-14 |
|
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: 72.46 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 96 VKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKVLQSRLLKVIS---AYVMQD---DLL 169
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFG--LRPPASGEITLDGKPVTRRSPRDAIRagiAYVPEDrkrEGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 170 FPMLTVKEtlmfasefrlprslskskkmervealidqlglrnaaNTVIGdeghRGVSGGERRRVSIGIDIIHDPIVLFLD 249
Cdd:cd03215 90 VLDLSVAE------------------------------------NIALS----SLLSGGNQQKVVLARWLARDPRVLILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15028219 250 EPTSGLD-STNAFmVVQVLKRIAQSGSIVIMSihqpSARIVELL---DRLIILSRGK 302
Cdd:cd03215 130 EPTRGVDvGAKAE-IYRLIRELADAGKAVLLI----SSELDELLglcDRILVMYEGR 181
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
97-310 |
1.40e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 77.90 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGR--VAEGSlrgsvtlngekVLQSRLLkvisAYVMQDDLLFPMlT 174
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQfeISEGR-----------VWAERSI----AYVPQQAWIMNA-T 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 175 VKETLMFASEFRLPRsLSKSKKMERVEALIDQLGlrNAANTVIGDEGhRGVSGGERRRVSIGIDIIHDPIVLFLDEPTSG 254
Cdd:PTZ00243 737 VRGNILFFDEEDAAR-LADAVRVSQLEADLAQLG--GGLETEIGEKG-VNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15028219 255 LDSTNAFMVVQVLKRIAQSGSIVIMSIHQpsARIVELLDRLIILSRGKSVFNGSPA 310
Cdd:PTZ00243 813 LDAHVGERVVEECFLGALAGKTRVLATHQ--VHVVPRADYVVALGDGRVEFSGSSA 866
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
97-312 |
1.42e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.44 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALaGRVAEGSlRGSVTLNGEKV--LQSRLLKVISAYVMQDDLLFPMLT 174
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPS-EGEILLDAQPLesWSSKAFARKVAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 175 VKETLMFAsefRLP--RSLSK--SKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFLDE 250
Cdd:PRK10575 102 VRELVAIG---RYPwhGALGRfgAADREKVEEAISLVGLKPLAHRLVDS-----LSGGERQRAWIAMLVAQDSRCLLLDE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15028219 251 PTSGLDSTNAFMVVQVLKRIAQS-GSIVIMSIH--QPSARIVellDRLIILSRGKSVFNGSPASL 312
Cdd:PRK10575 174 PTSALDIAHQVDVLALVHRLSQErGLTVIAVLHdiNMAARYC---DYLVALRGGEMIAQGTPAEL 235
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
91-310 |
1.48e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 73.96 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 91 SRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIdALAGRVAEGSlRGSVTLNGEKVLQSR---LLKVISayVMQDD 167
Cdd:COG4604 8 SKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLL-SMISRLLPPD-SGEVLVDGLDVATTPsreLAKRLA--ILRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 168 LLFPM-LTVKETLMFAsefRLPRS---LSKSKKmERVEALIDQLGLRNAANTVIgDEghrgVSGGERRRVSIGIDIIHDP 243
Cdd:COG4604 84 NHINSrLTVRELVAFG---RFPYSkgrLTAEDR-EIIDEAIAYLDLEDLADRYL-DE----LSGGQRQRAFIAMVLAQDT 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15028219 244 IVLFLDEPTSGLDSTNAFMVVQVLKRIA-QSGSIVIMSIH---QPSAriveLLDRLIILSRGKSVFNGSPA 310
Cdd:COG4604 155 DYVLLDEPLNNLDMKHSVQMMKLLRRLAdELGKTVVIVLHdinFASC----YADHIVAMKDGRVVAQGTPE 221
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
91-313 |
2.25e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 76.69 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 91 SRQNGVKTL--LDDVSGEASDGDILAVLGASGAGKSTLIDAL-------AG--RVAEgslRGSVTLNGEKVlqSRLLKVI 159
Cdd:PRK10535 13 SYPSGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptSGtyRVAG---QDVATLDADAL--AQLRREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 160 SAYVMQDDLLFPMLTVKETLMFASEFRlprSLSKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDI 239
Cdd:PRK10535 88 FGFIFQRYHLLSHLTAAQNVEVPAVYA---GLERKQRLLRAQELLQRLGLEDRVEYQPSQ-----LSGGQQQRVSIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 240 IHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQP-----SARIVELLDRLIIL---SRGKSVFNGSPAS 311
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPqvaaqAERVIEIRDGEIVRnppAQEKVNVAGGTEP 239
|
..
gi 15028219 312 LP 313
Cdd:PRK10535 240 VV 241
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
100-309 |
3.44e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 73.73 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSR--LLKVISAYVM----QDDLLFPML 173
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSS--GRILFDGKPIDYSRkgLMKLRESVGMvfqdPDNQLFSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 174 TVKETLMFASEFRLPrslsKSKKMERVEALIDQLGLRNaantvIGDEGHRGVSGGERRRVSIGIDIIHDPIVLFLDEPTS 253
Cdd:PRK13636 100 VYQDVSFGAVNLKLP----EDEVRKRVDNALKRTGIEH-----LKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15028219 254 GLDSTNAFMVVQVLKRIAQSGSIVIMsIHQPSARIVELL-DRLIILSRGKSVFNGSP 309
Cdd:PRK13636 171 GLDPMGVSEIMKLLVEMQKELGLTII-IATHDIDIVPLYcDNVFVMKEGRVILQGNP 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
82-256 |
3.53e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 74.98 E-value: 3.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 82 VTLRrrfGFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKVLQsrllkvISA 161
Cdd:PRK09452 15 VELR---GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAG--FETPDSGRIMLDGQDITH------VPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 162 ------YVMQDDLLFPMLTVKETLMFAseFRLpRSLSKSKKMERV-EAL----IDQLGLRNAANtvigdeghrgVSGGER 230
Cdd:PRK09452 84 enrhvnTVFQSYALFPHMTVFENVAFG--LRM-QKTPAAEITPRVmEALrmvqLEEFAQRKPHQ----------LSGGQQ 150
|
170 180
....*....|....*....|....*.
gi 15028219 231 RRVSIGIDIIHDPIVLFLDEPTSGLD 256
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
86-312 |
3.89e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 73.26 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 86 RRFGFSRqnGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGslRGSVTLNGEKV---LQSRLLKVISAY 162
Cdd:PRK11831 11 RGVSFTR--GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD--HGEILFDGENIpamSRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 163 VM--QDDLLFPMLTVKETLMFA--SEFRLPRSLSKSKKMERVEAlidqLGLRNAANTVIGDeghrgVSGGERRRVSIGID 238
Cdd:PRK11831 87 SMlfQSGALFTDMNVFDNVAYPlrEHTQLPAPLLHSTVMMKLEA----VGLRGAAKLMPSE-----LSGGMARRAALARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15028219 239 IIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSVFNGSPASL 312
Cdd:PRK11831 158 IALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
93-282 |
4.50e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.99 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 93 QNGvKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSrLLKVISAYVMQD---DLL 169
Cdd:PRK15056 17 RNG-HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLAS--GKISILGQPTRQA-LQKNLVAYVPQSeevDWS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 170 FPMLtVKETLMFASE-----FRLPrslsKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPI 244
Cdd:PRK15056 93 FPVL-VEDVVMMGRYghmgwLRRA----KKRDRQIVTAALARVDMVEFRHRQIGE-----LSGGQKKRVFLARAIAQQGQ 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 15028219 245 VLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIH 282
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTH 200
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
90-342 |
4.64e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 73.10 E-value: 4.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 90 FSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSRLLKVIS--AYVMQD- 166
Cdd:PRK13632 15 FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQS--GEIKIDGITISKENLKEIRKkiGIIFQNp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 167 DLLFPMLTVKETLMFASEFR-LPRslsksKKMER-VEALIDQLGLRNAantvIGDEGHRgVSGGERRRVSIGIDIIHDPI 244
Cdd:PRK13632 93 DNQFIGATVEDDIAFGLENKkVPP-----KKMKDiIDDLAKKVGMEDY----LDKEPQN-LSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 245 VLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVeLLDRLIILSRGKSVFNGSPASLpgfFSDfgRPIP 324
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI---LNN--KEIL 236
|
250
....*....|....*....
gi 15028219 325 EKENI-SEFALDLVRELEG 342
Cdd:PRK13632 237 EKAKIdSPFIYKLSKKLKG 255
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
91-302 |
5.18e-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: 71.35 E-value: 5.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 91 SRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAegSLRGSVTLNGeKVlqsrllkvisAYVMQDDLLF 170
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELE--KLSGSVSVPG-SI----------AYVSQEPWIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 171 PMlTVKETLMFASEFRlprslskskkMERVEALIDQLGLR-------NAANTVIGDeghRGV--SGGERRRVSIGIDIIH 241
Cdd:cd03250 79 NG-TIRENILFGKPFD----------EERYEKVIKACALEpdleilpDGDLTEIGE---KGInlSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15028219 242 DPIVLFLDEPTSGLDS-TNAFMVVQVLKRIAQSGSIVIMSIHQPSarIVELLDRLIILSRGK 302
Cdd:cd03250 145 DADIYLLDDPLSAVDAhVGRHIFENCILGLLLNNKTRILVTHQLQ--LLPHADQIVVLDNGR 204
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
95-309 |
6.01e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 72.35 E-value: 6.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKV--LQSRLLKVISAYVMQDDLLFPM 172
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQS--GTVFLGDKPIsmLSSRQLARRLALLPQHHLTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 173 LTVKETLMFAsefrlpRS--------LSKSKKMeRVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPI 244
Cdd:PRK11231 91 ITVRELVAYG------RSpwlslwgrLSAEDNA-RVNQAMEQTRINHLADRRLTD-----LSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15028219 245 VLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIH---QPSarivELLDRLIILSRGKSVFNGSP 309
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHdlnQAS----RYCDHLVVLANGHVMAQGTP 222
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
86-321 |
6.94e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.41 E-value: 6.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 86 RRFGFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKV-----LQSRLLKVIS 160
Cdd:PRK10419 14 AHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVG--LESPSQGNVSWRGEPLaklnrAQRKAFRRDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 161 AYVMQDDL--LFPMLTVKETLmfASEFRLPRSLSKSKKMERVEALIDQLGLRNAantvIGDEGHRGVSGGERRRVSIGID 238
Cdd:PRK10419 92 QMVFQDSIsaVNPRKTVREII--REPLRHLLSLDKAERLARASEMLRAVDLDDS----VLDKRPPQLSGGQLQRVCLARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 239 IIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSI-HqpSARIVE-LLDRLIILSRGKSVFNGSPASLPGFF 316
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFItH--DLRLVErFCQRVMVMDNGQIVETQPVGDKLTFS 243
|
....*
gi 15028219 317 SDFGR 321
Cdd:PRK10419 244 SPAGR 248
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
100-302 |
1.04e-13 |
|
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: 74.09 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGrVAEGSLRGSVTLNGEKVLQSRLLKVIS---AYVMQD---DLLFPML 173
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKFEGNVFINGKPVDIRNPAQAIRagiAMVPEDrkrHGIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 174 TVKETLMFAS--EFRLPRSLSKSKKMERVEALIDQLGLRNAANTV-IGdeghrGVSGGERRRVSIGIDIIHDPIVLFLDE 250
Cdd:TIGR02633 355 GVGKNITLSVlkSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLpIG-----RLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15028219 251 PTSGLDSTNAFMVVQVLKRIAQSGSIVIMsIHQPSARIVELLDRLIILSRGK 302
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQEGVAIIV-VSSELAEVLGLSDRVLVIGEGK 480
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
100-312 |
1.18e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 72.07 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAG--RVAEGSLR-GSVTLNG---EKVLQSRLLKVISAYVMQDDLLFPML 173
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllQPTEGKVTvGDIVVSStskQKEIKPVRKKVGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 174 TVKETLMFASEFRLPRSLSKSKKMERVEalidQLGLRNAantvIGDEGHRGVSGGERRRVSIGIDIIHDPIVLFLDEPTS 253
Cdd:PRK13643 102 VLKDVAFGPQNFGIPKEKAEKIAAEKLE----MVGLADE----FWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15028219 254 GLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSaRIVELLDRLIILSRGKSVFNGSPASL 312
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSGQTVVLVTHLMD-DVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
89-304 |
2.02e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.59 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 89 GFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKStlIDALAgrvaegSLR-----------GSVTLNGEKVLQS--RL 155
Cdd:PRK15134 14 AFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKS--VTALS------ILRllpsppvvypsGDIRFHGESLLHAseQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 156 LKVIS----AYVMQDDL--LFPMLTVKETLmfASEFRLPRSLSKskKMERVEAL--IDQLGLRNAANTvIGDEGHRgVSG 227
Cdd:PRK15134 86 LRGVRgnkiAMIFQEPMvsLNPLHTLEKQL--YEVLSLHRGMRR--EAARGEILncLDRVGIRQAAKR-LTDYPHQ-LSG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15028219 228 GERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSI-HQPSarIV-ELLDRLIILSRGKSV 304
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFItHNLS--IVrKLADRVAVMQNGRCV 236
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
100-312 |
2.43e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.92 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAG-RVAEgslRGSVTLNGEKVLQS--RLLKVISAYVMQD--DLLFPMlT 174
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGiYLPQ---RGRVKVMGREVNAEneKWVRSKVGLVFQDpdDQVFSS-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 175 VKETLMFAsefrlPRS--LSKSKKMERVEALIDQLGLRNAAntvigDEGHRGVSGGERRRVSIGIDIIHDPIVLFLDEPT 252
Cdd:PRK13647 97 VWDDVAFG-----PVNmgLDKDEVERRVEEALKAVRMWDFR-----DKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 253 SGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSArIVELLDRLIILSRGKSVFNGSPASL 312
Cdd:PRK13647 167 AYLDPRGQETLMEILDRLHNQGKTVIVATHDVDL-AAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
95-302 |
2.84e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.74 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKVlqsRLLKVISA------YVMQDDL 168
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFG--ADPADSGEIRLDGKPV---RIRSPRDAiragiaYVPEDRK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 169 ---LFPMLTVKETLMFASEFRLPRS--LSKSKKMERVEALIDQLGLR-NAANTVIGDeghrgVSGGERRRVSIGIDIIHD 242
Cdd:COG1129 338 gegLVLDLSIRENITLASLDRLSRGglLDRRRERALAEEYIKRLRIKtPSPEQPVGN-----LSGGNQQKVVLAKWLATD 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 243 PIVLFLDEPTSGLDstnafmvV-------QVLKRIAQSGSIVIMSihqpSARIVELL---DRLIILSRGK 302
Cdd:COG1129 413 PKVLILDEPTRGID-------VgakaeiyRLIRELAAEGKAVIVI----SSELPELLglsDRILVMREGR 471
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
106-312 |
3.14e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 69.61 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 106 EASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSRLLKVISAYVMQDDLLFPMLTVKETLMFASEF 185
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNLIAGFLTPAS--GSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 186 RLprSLSKSKKmERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQ 265
Cdd:PRK10771 99 GL--KLNAAQR-EKLHAIARQMGIEDLLARLPGQ-----LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15028219 266 VLKRIAQSGSI-VIMSIHQ--PSARIVellDRLIILSRGKSVFNGSPASL 312
Cdd:PRK10771 171 LVSQVCQERQLtLLMVSHSleDAARIA---PRSLVVADGRIAWDGPTDEL 217
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
70-267 |
4.48e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 70.76 E-value: 4.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 70 PYVLNFNNLQ--YDVtlrRRFGFSRQNGVKTLlDDVSGEASDGDILAVLGASGAGKSTLIDALAgrVAEGSLRGSVTLNG 147
Cdd:PRK11308 3 QPLLQAIDLKkhYPV---KRGLFKPERLVKAL-DGVSFTLERGKTLAVVGESGCGKSTLARLLT--MIETPTGGELYYQG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 148 EKVLQS-----RLLKVISAYVMQDDL--LFPMLTVKETLmfASEFRLPRSLSKSKKMERVEALIDQLGLRNAantvigde 220
Cdd:PRK11308 77 QDLLKAdpeaqKLLRQKIQIVFQNPYgsLNPRKKVGQIL--EEPLLINTSLSAAERREKALAMMAKVGLRPE-------- 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15028219 221 gHRG-----VSGGERRRVSIGIDIIHDPIVLFLDEPTSGLD-STNAfmvvQVL 267
Cdd:PRK11308 147 -HYDryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDvSVQA----QVL 194
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
67-312 |
4.70e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 72.16 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 67 KPVPYVLNFNNLQydvtlrrrfgFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAgrvaegslR------ 140
Cdd:PRK11160 333 AADQVSLTLNNVS----------FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT--------Rawdpqq 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 141 GSVTLNGEKVL---QSRLLKVISaYVMQDDLLFPMlTVKETLMFASEfrlprslskSKKMERVEALIDQLGLRNAA---- 213
Cdd:PRK11160 395 GEILLNGQPIAdysEAALRQAIS-VVSQRVHLFSA-TLRDNLLLAAP---------NASDEALIEVLQQVGLEKLLeddk 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 214 --NTVIGdEGHRGVSGGERRRVSIGIDIIHD-PIVLfLDEPTSGLDSTNAFMVVQVLKRIAQsGSIVIMSIHQPSAriVE 290
Cdd:PRK11160 464 glNAWLG-EGGRQLSGGEQRRLGIARALLHDaPLLL-LDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRLTG--LE 538
|
250 260
....*....|....*....|..
gi 15028219 291 LLDRLIILSRGKSVFNGSPASL 312
Cdd:PRK11160 539 QFDRICVMDNGQIIEQGTHQEL 560
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
95-256 |
5.18e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.02 E-value: 5.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAegSLRGSVTLnGEKVlqsrllKVisAYVMQD-DLLFPML 173
Cdd:COG0488 326 GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELE--PDSGTVKL-GETV------KI--GYFDQHqEELDPDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 174 TVKETLmfasefrlpRSLSKSKKMERVEALIDQLGLRNA-ANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFLDEPT 252
Cdd:COG0488 395 TVLDEL---------RDGAPGGTEQEVRGYLGRFLFSGDdAFKPVGV-----LSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
....
gi 15028219 253 SGLD 256
Cdd:COG0488 461 NHLD 464
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
112-302 |
6.50e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 70.67 E-value: 6.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 112 ILAVLGASGAGKSTLIDALAGRVAEGslRGSVTLNGeKVLQSRLLKVISA-------YVMQDDLLFPMLTVKETLMFASe 184
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQ--KGRIVLNG-RVLFDAEKGICLPpekrrigYVFQDARLFPHYKVRGNLRYGM- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 185 frlprslskSKKM-ERVEALIDQLGLrnaantvigdeGH------RGVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDS 257
Cdd:PRK11144 102 ---------AKSMvAQFDKIVALLGI-----------EPlldrypGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15028219 258 TNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGK 302
Cdd:PRK11144 162 PRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
110-318 |
7.70e-13 |
|
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: 72.35 E-value: 7.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 110 GDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSrllkvIS------AYVMQDDLLFPMLTVKETLMFAS 183
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTS--GDATVAGKSILTN-----ISdvhqnmGYCPQFDAIDDLLTGREHLYLYA 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 184 EFR-LPrslskSKKMERVEAL-IDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAF 261
Cdd:TIGR01257 2038 RLRgVP-----AEEIEKVANWsIQSLGLSLYADRLAGT-----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15028219 262 MVVQVLKRIAQSGSIVIMSIHQpSARIVELLDRLIILSRGKSVFNGSPASLPGFFSD 318
Cdd:TIGR01257 2108 MLWNTIVSIIREGRAVVLTSHS-MEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGD 2163
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
90-295 |
9.06e-13 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 71.25 E-value: 9.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 90 FSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKStlIDALA--GRVAEGSLR--GSVTLNGEKVLQ---SRLLKV---- 158
Cdd:COG4172 16 FGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKS--VTALSilRLLPDPAAHpsGSILFDGQDLLGlseRELRRIrgnr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 159 IsAYVMQDDL--LFPMLTV----KETLmfasefRLPRSLSKSKKMERVEALIDQLGLRNAAnTVIGDEGHRgVSGGERRR 232
Cdd:COG4172 94 I-AMIFQEPMtsLNPLHTIgkqiAEVL------RLHRGLSGAAARARALELLERVGIPDPE-RRLDAYPHQ-LSGGQRQR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15028219 233 VSIGIDIIHDPIVLFLDEPTSGLDSTnafmvVQvlkriaqsgsivimsihqpsARIVELLDRL 295
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALDVT-----VQ--------------------AQILDLLKDL 202
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
70-295 |
1.23e-12 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 70.87 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 70 PYVLNFNNLQYDVTLRRRFgFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGslrGSVTLNGEK 149
Cdd:COG4172 273 PPLLEARDLKVWFPIKRGL-FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE---GEIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 150 V--LQSRLLKvisAY------VMQDDL--LFPMLTVKETLmfaSE-FRL-PRSLSKSKKMERVEALIDQLGLrnaantvi 217
Cdd:COG4172 349 LdgLSRRALR---PLrrrmqvVFQDPFgsLSPRMTVGQII---AEgLRVhGPGLSAAERRARVAEALEEVGL-------- 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 218 gDEGHRG-----VSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDstnafMVVQvlkriaqsgsivimsihqpsARIVELL 292
Cdd:COG4172 415 -DPAARHrypheFSGGQRQRIAIARALILEPKLLVLDEPTSALD-----VSVQ--------------------AQILDLL 468
|
...
gi 15028219 293 DRL 295
Cdd:COG4172 469 RDL 471
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
68-308 |
1.54e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.50 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 68 PVPY------VLNFNNLQYDVTLRRRFgFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEgslRG 141
Cdd:PRK15134 265 PVPLpepaspLLDVEQLQVAFPIRKGI-LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS---QG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 142 SVTLNGEKVLQ---SRLLKVIS--AYVMQD--DLLFPMLTVKETLMFASEFRLPrSLSKSKKMERVEALIDQLGLRNAAN 214
Cdd:PRK15134 341 EIWFDGQPLHNlnrRQLLPVRHriQVVFQDpnSSLNPRLNVLQIIEEGLRVHQP-TLSAAQREQQVIAVMEEVGLDPETR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 215 tvigdegHR---GVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVEL 291
Cdd:PRK15134 420 -------HRypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRAL 492
|
250
....*....|....*..
gi 15028219 292 LDRLIILSRGKSVFNGS 308
Cdd:PRK15134 493 CHQVIVLRQGEVVEQGD 509
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
95-304 |
1.57e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.33 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLlDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSRLLKVISAYVM---QDDLLFP 171
Cdd:PRK11288 16 GVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDA--GSILIDGQEMRFASTTAALAAGVAiiyQELHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 172 MLTVKETLMFAsefRLPRS---LSKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFL 248
Cdd:PRK11288 93 EMTVAENLYLG---QLPHKggiVNRRLLNYEAREQLEHLGVDIDPDTPLKY-----LSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15028219 249 DEPTSGL---DSTNAFMVVQVLKriaQSGSIVIMSIHQpSARIVELLDRLIILSRGKSV 304
Cdd:PRK11288 165 DEPTSSLsarEIEQLFRVIRELR---AEGRVILYVSHR-MEEIFALCDAITVFKDGRYV 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
89-302 |
1.59e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.17 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 89 GFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAG--RVAEGSLRGSVTLNGEKVLQSRLLkvisayvMQD 166
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGleTPSAGELLAGTAPLAEAREDTRLM-------FQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 167 DLLFPMLTVKETLMFAsefrlprsLSKSKKMERVEALiDQLGLRNAANtvigdEGHRGVSGGERRRVSIGIDIIHDPIVL 246
Cdd:PRK11247 90 ARLLPWKKVIDNVGLG--------LKGQWRDAALQAL-AAVGLADRAN-----EWPAALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15028219 247 FLDEPTSGLDSTNAFMVVQVLKRI-AQSGSIVIMSIHQPSaRIVELLDRLIILSRGK 302
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVS-EAVAMADRVLLIEEGK 211
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
81-309 |
1.63e-12 |
|
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: 67.52 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 81 DVTLRRRfgfsrqNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAgRVAEGSlRGSVTLNGEKVLQSRLLKVIS 160
Cdd:cd03244 7 NVSLRYR------PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALF-RLVELS-SGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 161 AYVM--QDDLLFPMlTVKETLMF---ASEFRLPRSLSKSKKMERVEALIDQLglrnaaNTVIgDEGHRGVSGGERRRVSI 235
Cdd:cd03244 79 RISIipQDPVLFSG-TIRSNLDPfgeYSDEELWQALERVGLKEFVESLPGGL------DTVV-EEGGENLSVGQRQLLCL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15028219 236 GIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRiAQSGSIVIMSIHqpsaRIVELL--DRLIILSRGKSVFNGSP 309
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAH----RLDTIIdsDRILVLDKGRVVEFDSP 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
89-307 |
1.81e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.20 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 89 GFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKVlqSRLLKVISA-----YV 163
Cdd:PRK09700 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSG--IHEPTKGTITINNINY--NKLDHKLAAqlgigII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 164 MQDDLLFPMLTVKETLMFAsefRLPR------SLSKSKKM-ERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIG 236
Cdd:PRK09700 86 YQELSVIDELTVLENLYIG---RHLTkkvcgvNIIDWREMrVRAAMMLLRVGLKVDLDEKVAN-----LSISHKQMLEIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15028219 237 IDIIHDPIVLFLDEPTSGLdsTNA-----FMVVQVLKRIAQSgsivIMSIHQPSARIVELLDRLIILSRGKSVFNG 307
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSL--TNKevdylFLIMNQLRKEGTA----IVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
97-309 |
2.68e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 66.40 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSLRGSVTLNGEKVLQ------SRLLKVISayvMQDDLLF 170
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKGEDITDlppeerARLGIFLA---FQYPPEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 171 PMLTVKETLmfasefrlpRSLSKskkmervealidqlglrnaantvigdeghrGVSGGERRRVSIGIDIIHDPIVLFLDE 250
Cdd:cd03217 90 PGVKNADFL---------RYVNE------------------------------GFSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15028219 251 PTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQpsARIVELL--DRLIILSRGKSVFNGSP 309
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREEGKSVLIITHY--QRLLDYIkpDRVHVLYDGRIVKSGDK 189
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
100-309 |
2.89e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.19 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDAL-------AGRVA---EGSLRGSVTLNGEKVLQS--------RLLKVISA 161
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLnalllpdTGTIEwifKDEKNKKKTKEKEKVLEKlviqktrfKKIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 162 YVMQDDLLFPML-------TVKETLMFAsefrlPRSLSKSKK--MERVEALIDQLGLrnaantvigDEGHR-----GVSG 227
Cdd:PRK13651 103 IRRRVGVVFQFAeyqlfeqTIEKDIIFG-----PVSMGVSKEeaKKRAAKYIELVGL---------DESYLqrspfELSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 228 GERRRVSI-GIdIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSaRIVELLDRLIILSRGKSVFN 306
Cdd:PRK13651 169 GQKRRVALaGI-LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD-NVLEWTKRTIFFKDGKIIKD 246
|
...
gi 15028219 307 GSP 309
Cdd:PRK13651 247 GDT 249
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
99-267 |
3.28e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 66.76 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 99 LLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKV----------LQSRLLkvisAYVMQDDL 168
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTS--GDVIFNGQPMsklssaakaeLRNQKL----GFIYQFHH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 169 LFPMLTVKETLMfasefrLPRSLSKSKKMERVEALIDQL---GLRNAANtvigdegHRG--VSGGERRRVSIGIDIIHDP 243
Cdd:PRK11629 98 LLPDFTALENVA------MPLLIGKKKPAEINSRALEMLaavGLEHRAN-------HRPseLSGGERQRVAIARALVNNP 164
|
170 180
....*....|....*....|....
gi 15028219 244 IVLFLDEPTSGLDSTNAFMVVQVL 267
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLL 188
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
100-336 |
3.58e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.50 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSRLLKVIS------AYVMQ--DDLLFP 171
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTT--GTVTVDDITITHKTKDKYIRpvrkriGMVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 172 MLTVKETLMFASEFRLPrsLSKSKkmERVEALIDQLGL-RNaantvIGDEGHRGVSGGERRRVSIGIDIIHDPIVLFLDE 250
Cdd:PRK13646 101 DTVEREIIFGPKNFKMN--LDEVK--NYAHRLLMDLGFsRD-----VMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 251 PTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSVFNGSPASLpgfFSDfgrpipeKENIS 330
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL---FKD-------KKKLA 241
|
....*.
gi 15028219 331 EFALDL 336
Cdd:PRK13646 242 DWHIGL 247
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
87-282 |
3.73e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.21 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 87 RFGFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAE-GSLRGSVTLNGEKVL---QSRLLKVIS-- 160
Cdd:PRK09473 19 RVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAnGRIGGSATFNGREILnlpEKELNKLRAeq 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 161 -AYVMQDDL--LFPMLTVKETLMfaSEFRLPRSLSKSKKMERVEALIDQLGLRNAANTvIGDEGHRgVSGGERRRVSIGI 237
Cdd:PRK09473 99 iSMIFQDPMtsLNPYMRVGEQLM--EVLMLHKGMSKAEAFEESVRMLDAVKMPEARKR-MKMYPHE-FSGGMRQRVMIAM 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15028219 238 DIIHDPIVLFLDEPTSGLDSTnafmvVQV--------LKRiaQSGSIVIMSIH 282
Cdd:PRK09473 175 ALLCRPKLLIADEPTTALDVT-----VQAqimtllneLKR--EFNTAIIMITH 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
81-312 |
4.36e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.13 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 81 DVTLRrrfGFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKVLQSRLLKVIS 160
Cdd:PRK11000 3 SVTLR---NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAG--LEDITSGDLFIGEKRMNDVPPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 161 AYVMQDDLLFPMLTVKETLMFASEfrlprsLSKSKKME---RVEALIDQLGLrnaantvigdeGH------RGVSGGERR 231
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMSFGLK------LAGAKKEEinqRVNQVAEVLQL-----------AHlldrkpKALSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 232 RVSIGIDIIHDPIVLFLDEPTSGLDstnAFMVVQVLKRIA----QSGSIVIMSIH-QPSAriVELLDRLIILSRGKSVFN 306
Cdd:PRK11000 141 RVAIGRTLVAEPSVFLLDEPLSNLD---AALRVQMRIEISrlhkRLGRTMIYVTHdQVEA--MTLADKIVVLDAGRVAQV 215
|
....*.
gi 15028219 307 GSPASL 312
Cdd:PRK11000 216 GKPLEL 221
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
95-284 |
4.84e-12 |
|
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: 65.59 E-value: 4.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSRLLKVIS-AYVMQDDLLFPML 173
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLA--GRVLLNGGPLDFQRDSIARGlLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 174 TVKETLMFASEFRlprslskskKMERVEALIDQLGLRNaantvIGDEGHRGVSGGERRRVSIGIDIIHDPIVLFLDEPTS 253
Cdd:cd03231 89 SVLENLRFWHADH---------SDEQVEEALARVGLNG-----FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190
....*....|....*....|....*....|.
gi 15028219 254 GLDSTNAFMVVQVLKRIAQSGSIVIMSIHQP 284
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
95-307 |
5.06e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 66.47 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRV---AEGSLRGSVTLNGEKVLQSRL--LKVISAYVMQDDLL 169
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelyPEARVSGEVYLDGQDIFKMDVieLRRRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 170 FPMLTVKETLmfASEFRLPRsLSKSKK--MERVEALIDQLGLRNAANTVIGDEGHRgVSGGERRRVSIGIDIIHDPIVLF 247
Cdd:PRK14247 94 IPNLSIFENV--ALGLKLNR-LVKSKKelQERVRWALEKAQLWDEVKDRLDAPAGK-LSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15028219 248 LDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSiHQP--SARIVellDRLIILSRGKSVFNG 307
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKDMTIVLVT-HFPqqAARIS---DYVAFLYKGQIVEWG 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
93-312 |
5.21e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 67.06 E-value: 5.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 93 QNGVKTLLDDVSGEASDGDILAVLGASGAGKST---LIDALAgrVAEGslrGSVTLNGEKVLQSRLLKV---ISAYVMQD 166
Cdd:PRK13650 16 EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLL--EAES---GQIIIDGDLLTEENVWDIrhkIGMVFQNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 167 DLLFPMLTVKETLMFASEfrlPRSLSKSKKMERVEALIDQLGLRNAANTvigdEGHRgVSGGERRRVSIGIDIIHDPIVL 246
Cdd:PRK13650 91 DNQFVGATVEDDVAFGLE---NKGIPHEEMKERVNEALELVGMQDFKER----EPAR-LSGGQKQRVAIAGAVAMRPKII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15028219 247 FLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSI-HQPSAriVELLDRLIILSRGKSVFNGSPASL 312
Cdd:PRK13650 163 ILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISItHDLDE--VALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
96-310 |
8.90e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 65.89 E-value: 8.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 96 VKTL----LDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVlqSRLLKVISAYvmqddllFP 171
Cdd:cd03237 7 KKTLgeftLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDE--GDIEIELDTV--SYKPQYIKAD-------YE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 172 MlTVKETLMFASEFRLPRSLSKSKKME--RVEALIDQLgLRNaantvigdeghrgVSGGERRRVSIGIDIIHDPIVLFLD 249
Cdd:cd03237 76 G-TVRDLLSSITKDFYTHPYFKTEIAKplQIEQILDRE-VPE-------------LSGGELQRVAIAACLSKDADIYLLD 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15028219 250 EPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIilsrgksVFNGSPA 310
Cdd:cd03237 141 EPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLI-------VFEGEPS 194
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
100-312 |
9.34e-12 |
|
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: 68.31 E-value: 9.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLI-------DALAGRVaegslrgsvTLNGE---KVLQSRLLKVIsAYVMQDDLL 169
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLArllfrfyDVTSGRI---------LIDGQdirDVTQASLRAAI-GIVPQDTVL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 170 FpmltvKETLMF--------ASEfrlprslskskkmERVEALID--QL-----GLRNAANTVIGDeghRGV--SGGERRR 232
Cdd:COG5265 444 F-----NDTIAYniaygrpdASE-------------EEVEAAARaaQIhdfieSLPDGYDTRVGE---RGLklSGGEKQR 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 233 VSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQS-GSIVIMsiHQPSArIVElLDRLIILSRGKSVFNGSPAS 311
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGrTTLVIA--HRLST-IVD-ADEILVLEAGRIVERGTHAE 578
|
.
gi 15028219 312 L 312
Cdd:COG5265 579 L 579
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
101-302 |
9.98e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.03 E-value: 9.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 101 DDVSGEASDGDILAVLGASGAGKSTLIDALAGrVAEGSLRGSVTLNGEKVLQSRLLKVIS---AYVMQD---DLLFPMLT 174
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPGRWEGEIFIDGKPVKIRNPQQAIAqgiAMVPEDrkrDGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 175 VKE--TLMFASEFRLPRSLSKSKKMERVEALIDQLGLRNAANTV-IGdeghrGVSGGERRRVSIGIDIIHDPIVLFLDEP 251
Cdd:PRK13549 358 VGKniTLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASPELaIA-----RLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15028219 252 TSGLDSTNAFMVVQVLKRIAQSGSIVIMSihqpSARIVELL---DRLIILSRGK 302
Cdd:PRK13549 433 TRGIDVGAKYEIYKLINQLVQQGVAIIVI----SSELPEVLglsDRVLVMHEGK 482
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
88-312 |
1.00e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.18 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 88 FGFSRQNGVKTLLDDVSGEASDGdilaVLGASGAGKSTLIDALAGRVAEGslRGSVTLNGEKVLQSR----LLKVISAYV 163
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTG----LVGANGCGKSTLFMNLSGLLRPQ--KGAVLWQGKPLDYSKrgllALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 164 MQD------------DLLFPM--LTVKETLMfasefrlprslskSKKMERVEALIDQLGLRNaantvigdEGHRGVSGGE 229
Cdd:PRK13638 83 FQDpeqqifytdidsDIAFSLrnLGVPEAEI-------------TRRVDEALTLVDAQHFRH--------QPIQCLSHGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 230 RRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSArIVELLDRLIILSRGKSVFNGSP 309
Cdd:PRK13638 142 KKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLRQGQILTHGAP 220
|
...
gi 15028219 310 ASL 312
Cdd:PRK13638 221 GEV 223
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
99-302 |
1.00e-11 |
|
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: 65.18 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 99 LLDDVSGEASDGDILAVLGASGAGKSTLIdALAGRVAEGSlRGSVTLNGEKV--LQSRLLKVISAYVMQDDLLFPMlTVK 176
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVV-ALLENFYQPQ-GGQVLLDGKPIsqYEHKYLHSKVSLVGQEPVLFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 177 ETLMFAsefrLPrslskSKKMERVEALIDQ-------LGLRNAANTVIGDEGHRgVSGGERRRVSIGIDIIHDPIVLFLD 249
Cdd:cd03248 106 DNIAYG----LQ-----SCSFECVKEAAQKahahsfiSELASGYDTEVGEKGSQ-LSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15028219 250 EPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSiHQPSarIVELLDRLIILSRGK 302
Cdd:cd03248 176 EATSALDAESEQQVQQALYDWPERRTVLVIA-HRLS--TVERADQILVLDGGR 225
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
95-288 |
1.03e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 65.57 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTL---IDALAGRVAEGSLRGSVTLNGEKVLQSR-----LLKVIsAYVMQD 166
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLlrsINRMNDLNPEVTITGSIVYNGHNIYSPRtdtvdLRKEI-GMVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 167 DLLFPMlTVKETLMFAseFRLPRSLSKSKKMERVEALIDQLGLRNAANTVIGDEGhRGVSGGERRRVSIGIDIIHDPIVL 246
Cdd:PRK14239 95 PNPFPM-SIYENVVYG--LRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSA-LGLSGGQQQRVCIARVLATSPKII 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15028219 247 FLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIM--SIHQPSaRI 288
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLLGLKDDYTMLLVtrSMQQAS-RI 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
102-302 |
1.05e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.89 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 102 DVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKVLQSRLLKVIS---AYVMQ---DDLLFPMLTV 175
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFG--VDKRAGGEIRLNGKDISPRSPLDAVKkgmAYITEsrrDNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 176 KETLMFASEFRLPRS------LSKSKKMERVEALIDQLGLRNAA-NTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFL 248
Cdd:PRK09700 359 AQNMAISRSLKDGGYkgamglFHEVDEQRTAENQRELLALKCHSvNQNITE-----LSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15028219 249 DEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSihqpSARIVELL---DRLIILSRGK 302
Cdd:PRK09700 434 DEPTRGIDVGAKAEIYKVMRQLADDGKVILMV----SSELPEIItvcDRIAVFCEGR 486
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
59-307 |
1.21e-11 |
|
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: 64.86 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 59 IDVEALYVKpvpYVLnFNNLQYDVTLRRRFGFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGS 138
Cdd:cd03220 1 IELENVSKS---YPT-YKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 139 lrGSVTLNGekvlqsrllKVISayvmqddLLF------PMLTVKETLMF-ASEFRLPRSLSKsKKMERVEALIDqlglrn 211
Cdd:cd03220 77 --GTVTVRG---------RVSS-------LLGlgggfnPELTGRENIYLnGRLLGLSRKEID-EKIDEIIEFSE------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 212 aantvIGDEGHRGV---SGGERRRVSIGIDIIHDPIVLFLDEPTSGLDstNAFM--VVQVLKRIAQSGSIVIMSIHQPSA 286
Cdd:cd03220 132 -----LGDFIDLPVktySSGMKARLAFAIATALEPDILLIDEVLAVGD--AAFQekCQRRLRELLKQGKTVILVSHDPSS 204
|
250 260
....*....|....*....|.
gi 15028219 287 rIVELLDRLIILSRGKSVFNG 307
Cdd:cd03220 205 -IKRLCDRALVLEKGKIRFDG 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
97-304 |
1.54e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 66.27 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTL--LDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVL-----QSRLLKVISAYVMQDDL- 168
Cdd:PRK15079 32 KTLkaVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATD--GEVAWLGKDLLgmkddEWRAVRSDIQMIFQDPLa 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 169 -LFPMLTVKETLMFASEFRLPRsLSKSKKMERVEALIDQLGLRnaaNTVIGDEGHRgVSGGERRRVSIGIDIIHDPIVLF 247
Cdd:PRK15079 110 sLNPRMTIGEIIAEPLRTYHPK-LSRQEVKDRVKAMMLKVGLL---PNLINRYPHE-FSGGQCQRIGIARALILEPKLII 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15028219 248 LDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSV 304
Cdd:PRK15079 185 CDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 241
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
110-256 |
1.55e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.80 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 110 GDILAVLGASGAGKSTLIDALAGrVAEGSlRGSVTLNGEKVLQ------SRLLKVISAYVMQDDLLFPMLTVKETLMFAS 183
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAG-LDDGS-SGEVSLVGQPLHQmdeearAKLRAKHVGFVFQSFMLIPTLNALENVELPA 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15028219 184 efrLPRSLSKSKKMERVEALIDQLGLrnaantvigdeGHR------GVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLD 256
Cdd:PRK10584 114 ---LLRGESSRQSRNGAKALLEQLGL-----------GKRldhlpaQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
95-302 |
1.59e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.34 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLlDDVSGEASDGDILAVLGASGAGKSTLIDALAG--RVAEGSLR---GSVTLNGEKVLQSRLLKVISayvmQDDLL 169
Cdd:PRK10762 16 GVKAL-SGAALNVYPGRVMALVGENGAGKSTMMKVLTGiyTRDAGSILylgKEVTFNGPKSSQEAGIGIIH----QELNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 170 FPMLTVKETLMFASEFRLPRSLSKSKKM-ERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFL 248
Cdd:PRK10762 91 IPQLTIAENIFLGREFVNRFGRIDWKKMyAEADKLLARLNLRFSSDKLVGE-----LSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15028219 249 DEPTSGLDSTNA---FMVVQVLKriAQSGSIVIMSiHQpSARIVELLDRLIILSRGK 302
Cdd:PRK10762 166 DEPTDALTDTETeslFRVIRELK--SQGRGIVYIS-HR-LKEIFEICDDVTVFRDGQ 218
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
84-307 |
1.63e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 65.33 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 84 LRRRFGfsRQNGvktlLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVA-----------EGSLRGSVTLNGEKvlQ 152
Cdd:PRK11701 12 LTKLYG--PRKG----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLApdagevhyrmrDGQLRDLYALSEAE--R 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 153 SRLLKVISAYVMQD--DLLFPMLT----VKETLMFASEFRLPRSLSKSKK-MERVEalIDQLGLrnaantvigDEGHRGV 225
Cdd:PRK11701 84 RRLLRTEWGFVHQHprDGLRMQVSaggnIGERLMAVGARHYGDIRATAGDwLERVE--IDAARI---------DDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 226 SGGERRRVSIGIDIIHDPIVLFLDEPTSGLDstnafmvVQVLKRI--------AQSGSIVIMSIHQPS-ARIveLLDRLI 296
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLD-------VSVQARLldllrglvRELGLAVVIVTHDLAvARL--LAHRLL 223
|
250
....*....|.
gi 15028219 297 ILSRGKSVFNG 307
Cdd:PRK11701 224 VMKQGRVVESG 234
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
97-284 |
2.18e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.67 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAG--RVAEGSLRgsvtLNGEKVLQSRllkviSAYvmQDDLLF---- 170
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGlaRPDAGEVL----WQGEPIRRQR-----DEY--HQDLLYlghq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 171 ----PMLTVKETLMFASefRLPRSLSKskkmERVEALIDQLGLRNAANTVIgdeghRGVSGGERRRVSIGIDIIHDPIVL 246
Cdd:PRK13538 83 pgikTELTALENLRFYQ--RLHGPGDD----EALWEALAQVGLAGFEDVPV-----RQLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 15028219 247 FLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQP 284
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQD 189
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
84-312 |
2.42e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 66.75 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 84 LRRRFgFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSLRGSVTLNGEKV--------LQSRL 155
Cdd:TIGR03269 285 VSKRY-ISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVdmtkpgpdGRGRA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 156 LKVIsAYVMQDDLLFPMLTVKETLMFASEFRLPRSLSKSKKMERVEAlidqLGLRNAANTVIGDEGHRGVSGGERRRVSI 235
Cdd:TIGR03269 364 KRYI-GILHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAVITLKM----VGFDEEKAEEILDKYPDELSEGERHRVAL 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15028219 236 GIDIIHDPIVLFLDEPTSGLDSTNAFMVVQ-VLK-RIAQSGSIVIMSiHQPSArIVELLDRLIILSRGKSVFNGSPASL 312
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKaREEMEQTFIIVS-HDMDF-VLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
100-302 |
2.44e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.57 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKVL----QSRLLKVIsAYVMQD---DLLFPM 172
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYG--ALPRTSGYVTLDGHEVVtrspQDGLANGI-VYISEDrkrDGLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 173 LTVKETLMFASEFRLPRSLSKSKKMERVEALIDQLGLRN----AANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFL 248
Cdd:PRK10762 345 MSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRLFNiktpSMEQAIGL-----LSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15028219 249 DEPTSGLDSTNAFMVVQVLKRIAQSG-SIVIMSIHQPsarivELL---DRLIILSRGK 302
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLINQFKAEGlSIILVSSEMP-----EVLgmsDRILVMHEGR 472
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
84-310 |
2.74e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 64.63 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 84 LRRRFGfsrqngvkTLL--DDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKV--LQSRLLK-- 157
Cdd:PRK11300 11 LMMRFG--------GLLavNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTG--GTILLRGQHIegLPGHQIArm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 158 -VISAYvmQDDLLFPMLTVKETLMFASEFRLPRSL------------SKSKKMERVEALIDQLGLRNAANTVIGDeghrg 224
Cdd:PRK11300 81 gVVRTF--QHVRLFREMTVIENLLVAQHQQLKTGLfsgllktpafrrAESEALDRAATWLERVGLLEHANRQAGN----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 225 VSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSV 304
Cdd:PRK11300 154 LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPL 233
|
....*.
gi 15028219 305 FNGSPA 310
Cdd:PRK11300 234 ANGTPE 239
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
81-294 |
3.01e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 66.75 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 81 DVTLRRRFGfsrqngvKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvaegsL----RGSVTL-NGEKVL---Q 152
Cdd:COG4178 367 DLTLRTPDG-------RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG------LwpygSGRIARpAGARVLflpQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 153 srllkviSAYvmqddllFPMLTVKETLMFASEfrlPRSLSKskkmERVEALIDQLGLRNAANTVigDEG---HRGVSGGE 229
Cdd:COG4178 434 -------RPY-------LPLGTLREALLYPAT---AEAFSD----AELREALEAVGLGHLAERL--DEEadwDQVLSLGE 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15028219 230 RRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRiAQSGSIVImSI-HQPS-----ARIVELLDR 294
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVI-SVgHRSTlaafhDRVLELTGD 559
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
93-309 |
3.20e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 65.83 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 93 QNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIdALAGRVAEGSlRGSVTLNG---EKVLQSRLLKVIS---AYVMQD 166
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMV-RLLNRLIEPT-RGQVLIDGvdiAKISDAELREVRRkkiAMVFQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 167 DLLFPMLTVKETLMFASEFrlpRSLSKSKKMERVEALIDQLGLRNAANTViGDEghrgVSGGERRRVSIGIDIIHDPIVL 246
Cdd:PRK10070 115 FALMPHMTVLDNTAFGMEL---AGINAEERREKALDALRQVGLENYAHSY-PDE----LSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15028219 247 FLDEPTSGLDS-TNAFMVVQVLKRIAQSGSIVIMSIHQPSaRIVELLDRLIILSRGKSVFNGSP 309
Cdd:PRK10070 187 LMDEAFSALDPlIRTEMQDELVKLQAKHQRTIVFISHDLD-EAMRIGDRIAIMQNGEVVQVGTP 249
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
86-279 |
4.87e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.19 E-value: 4.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 86 RRFGFsrQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAgrvaegSL----RGSVTLNGEKVLQ---SRLLKV 158
Cdd:PRK10247 11 QNVGY--LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVA------SLisptSGTLLFEGEDISTlkpEIYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 159 ISaYVMQDDLLFPMlTVKETLMFASEFRlprslSKSKKMERVEALIDQLGLRNAantvIGDEGHRGVSGGERRRVSIGID 238
Cdd:PRK10247 83 VS-YCAQTPTLFGD-TVYDNLIFPWQIR-----NQQPDPAIFLDDLERFALPDT----ILTKNIAELSGGEKQRISLIRN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15028219 239 IIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIM 279
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVL 192
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
110-318 |
6.26e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 63.85 E-value: 6.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 110 GDILAVLGASGAGKSTLIDALAG--RVAEGS--LRGSVTLNGEKVLQSRllKVISAYVMQDDLLFPMLTVKETLMFASE- 184
Cdd:PRK13644 28 GEYIGIIGKNGSGKSTLALHLNGllRPQKGKvlVSGIDTGDFSKLQGIR--KLVGIVFQNPETQFVGRTVEEDLAFGPEn 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 185 FRLPRSlskskkmeRVEALIDqlglRNAANTVIGDEGHRG---VSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAF 261
Cdd:PRK13644 106 LCLPPI--------EIRKRVD----RALAEIGLEKYRHRSpktLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15028219 262 MVVQVLKRIAQSGSIVIMSIHQPSAriVELLDRLIILSRGKSVFNGSPASLpgfFSD 318
Cdd:PRK13644 174 AVLERIKKLHEKGKTIVYITHNLEE--LHDADRIIVMDRGKIVLEGEPENV---LSD 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
100-336 |
6.33e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 63.89 E-value: 6.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLnGEKVLQS----RLLKVIS---AYVMQddllFP- 171
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTS--GTVTI-GERVITAgkknKKLKPLRkkvGIVFQ----FPe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 172 -ML---TVKETLMFA-SEFrlprSLSKSKKMERVEALIDQLGLRNAantvIGDEGHRGVSGGERRRVSIGIDIIHDPIVL 246
Cdd:PRK13634 96 hQLfeeTVEKDICFGpMNF----GVSEEDAKQKAREMIELVGLPEE----LLARSPFELSGGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 247 FLDEPTSGLDSTNAFMVVQVLKRIAQSGSI-VIMSIHQ--PSARIVellDRLIILSRGKSVFNGSPASLpgfFSDfgrpi 323
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEMFYKLHKEKGLtTVLVTHSmeDAARYA---DQIVVMHKGTVFLQGTPREI---FAD----- 236
|
250
....*....|...
gi 15028219 324 peKENISEFALDL 336
Cdd:PRK13634 237 --PDELEAIGLDL 247
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
97-308 |
6.53e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.53 E-value: 6.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRV----AEGSLRGSVTLNGEKVLQSRLLKVIS--AYVMQDDLLF 170
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydSKIKVDGKVLYFGKDIFQIDAIKLRKevGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 171 PMLTVKETLMFASEFRLPRSLSKSKKMerVEALIDQLGLRNAANTVIGDEGHRgVSGGERRRVSIGIDIIHDPIVLFLDE 250
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKI--VEECLRKVGLWKEVYDRLNSPASQ-LSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15028219 251 PTSGLDSTNAFMVVQVLKRIAQSGSIVIMSiHQPSaRIVELLDRLIILSRGKSVFNGS 308
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNEIAIVIVS-HNPQ-QVARVADYVAFLYNGELVEWGS 235
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
97-301 |
7.16e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.15 E-value: 7.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRV--AEGS---LRGSVtlngekvlqsrllkvisAYVMQDDLLFP 171
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELshAETSsvvIRGSV-----------------AYVPQVSWIFN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 172 MlTVKETLMFASEFrlprslskskKMERVEALIDQLGLRNAANTVIGDE----GHRGV--SGGERRRVSIGIDIIHDPIV 245
Cdd:PLN03232 693 A-TVRENILFGSDF----------ESERYWRAIDVTALQHDLDLLPGRDlteiGERGVniSGGQKQRVSMARAVYSNSDI 761
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15028219 246 LFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQpsARIVELLDRLIILSRG 301
Cdd:PLN03232 762 YIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQ--LHFLPLMDRIILVSEG 815
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
84-256 |
7.33e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.53 E-value: 7.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 84 LRRRFG-FsrqngvkTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKV----LQSRLlKV 158
Cdd:NF033858 272 LTMRFGdF-------TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASE--GEAWLFGQPVdagdIATRR-RV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 159 isAYVMQDDLLFPMLTVKETLMF-ASEFRLPRSLSKskkmERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGI 237
Cdd:NF033858 342 --GYMSQAFSLYGELTVRQNLELhARLFHLPAAEIA----ARVAEMLERFDLADVADALPDS-----LPLGIRQRLSLAV 410
|
170
....*....|....*....
gi 15028219 238 DIIHDPIVLFLDEPTSGLD 256
Cdd:NF033858 411 AVIHKPELLILDEPTSGVD 429
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
75-309 |
1.27e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 63.10 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 75 FNNLQYDVTLRRRFGFSRqngvktlLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrgSVTLNGEKVLQSR 154
Cdd:PRK13645 9 LDNVSYTYAKKTPFEFKA-------LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISET---GQTIVGDYAIPAN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 155 LLKVISAYVMQDDL----LFPML-----TVKETLMFAsefrlPRSLSKSKK--MERVEALIDQLGLRNaantvigDEGHR 223
Cdd:PRK13645 79 LKKIKEVKRLRKEIglvfQFPEYqlfqeTIEKDIAFG-----PVNLGENKQeaYKKVPELLKLVQLPE-------DYVKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 224 G---VSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQS-GSIVIMSIHQPSaRIVELLDRLIILS 299
Cdd:PRK13645 147 SpfeLSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMD-QVLRIADEVIVMH 225
|
250
....*....|
gi 15028219 300 RGKSVFNGSP 309
Cdd:PRK13645 226 EGKVISIGSP 235
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
100-302 |
1.56e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.98 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGrVAEGSlRGSVTLNGEKVLQSRLLKVIS---AYVMQDDL---LFPML 173
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFG-IREKS-AGTITLHGKKINNHNANEAINhgfALVTEERRstgIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 174 TVKETLMFAS--EFRLPRSLSKSKKMER-VEALIDQLGLRNAAN-TVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFLD 249
Cdd:PRK10982 342 DIGFNSLISNirNYKNKVGLLDNSRMKSdTQWVIDSMRVKTPGHrTQIGS-----LSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15028219 250 EPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSihqpSARIVELL---DRLIILSRGK 302
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAELAKKDKGIIII----SSEMPELLgitDRILVMSNGL 468
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
104-310 |
1.57e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.42 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 104 SGEASDGDILAVLGASGAGKSTLIDALAGRVA--EGSLRGSVTlngekvlqsrllkvIS---AYVMQDdllFPMlTVKET 178
Cdd:COG1245 360 GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKpdEGEVDEDLK--------------ISykpQYISPD---YDG-TVEEF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 179 LMFASEFRLPRSLSKSKkmerveaLIDQLGLRNaantvIGDEGHRGVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDST 258
Cdd:COG1245 422 LRSANTDDFGSSYYKTE-------IIKPLGLEK-----LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 259 NAFMVVQVLKRIAQSGSIVIMsihqpsarIVE--------LLDRLIilsrgksVFNGSPA 310
Cdd:COG1245 490 QRLAVAKAIRRFAENRGKTAM--------VVDhdiylidyISDRLM-------VFEGEPG 534
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
90-356 |
1.73e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 62.51 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 90 FSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSLRGS------VTLNGEKVLQSRLlKVisAYV 163
Cdd:PRK13640 13 FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSkitvdgITLTAKTVWDIRE-KV--GIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 164 MQD-DLLFPMLTVKETLMFASEFR-LPRSlskskKMER-VEALIDQLGLRNAAntvigDEGHRGVSGGERRRVSI-GIDI 239
Cdd:PRK13640 90 FQNpDNQFVGATVGDDVAFGLENRaVPRP-----EMIKiVRDVLADVGMLDYI-----DSEPANLSGGQKQRVAIaGILA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 240 IhDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSI-HQPSAriVELLDRLIILSRGKSVFNGSPASL---PGF 315
Cdd:PRK13640 160 V-EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISItHDIDE--ANMADQVLVLDDGKLLAQGSPVEIfskVEM 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15028219 316 FSDFGRPIP----EKENISEFALDLVRELEGSNEGTKALVDFNEK 356
Cdd:PRK13640 237 LKEIGLDIPfvykLKNKLKEKGISVPQEINTEEKLVQYLCQLNSK 281
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
109-332 |
2.29e-10 |
|
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: 61.61 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 109 DGDILAVLGASGAGKSTLIDALAGRV--------AEGS-------LRGSVTLNG-EKVLQSRLLKVISA-YVmqdDLLfP 171
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLkpnlgkfdDPPDwdeildeFRGSELQNYfTKLLEGDVKVIVKPqYV---DLI-P 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 172 MlTVKETlmfASEFrlprsLSKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFLDEP 251
Cdd:cd03236 101 K-AVKGK---VGEL-----LKKKDERGKLDELVDQLELRHVLDRNIDQ-----LSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 252 TSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSarIVELLDRLIILSRGKsvfngspaslPGFFSDFGRPIPEKENISE 331
Cdd:cd03236 167 SSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLA--VLDYLSDYIHCLYGE----------PGAYGVVTLPKSVREGINE 234
|
.
gi 15028219 332 F 332
Cdd:cd03236 235 F 235
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
95-283 |
2.48e-10 |
|
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: 63.31 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLlDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSLRGSVTLNGEKVLQSRLLKVISA---YVMQDDLLFP 171
Cdd:TIGR02633 13 GVKAL-DGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNIRDTERAgivIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 172 MLTVKETLMFASEFRLPRSLSKSKKM-ERVEALIDQLGLRNAANT-VIGDEGhrgvsGGERRRVSIGIDIIHDPIVLFLD 249
Cdd:TIGR02633 92 ELSVAENIFLGNEITLPGGRMAYNAMyLRAKNLLRELQLDADNVTrPVGDYG-----GGQQQLVEIAKALNKQARLLILD 166
|
170 180 190
....*....|....*....|....*....|....
gi 15028219 250 EPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQ 283
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKAHGVACVYISHK 200
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
99-309 |
3.08e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 62.41 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 99 LLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKV--LQSRLLKVisAYVMQDDLLFPMLTVK 176
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTS--GHIRFHGTDVsrLHARDRKV--GFVFQHYALFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 177 ETLMFASEFrLPRSLSKSKKM--ERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFLDEPTSG 254
Cdd:PRK10851 93 DNIAFGLTV-LPRRERPNAAAikAKVTQLLEMVQLAHLADRYPAQ-----LSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15028219 255 LDStnafmvvQVLKRIAQ---------SGSIVIMSIHQPSAriVELLDRLIILSRGKSVFNGSP 309
Cdd:PRK10851 167 LDA-------QVRKELRRwlrqlheelKFTSVFVTHDQEEA--MEVADRVVVMSQGNIEQAGTP 221
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
73-308 |
4.33e-10 |
|
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: 63.22 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 73 LNFNNLQYdvtlrrRFGFSRQngvktLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKV-- 150
Cdd:TIGR01193 474 IVINDVSY------SYGYGSN-----ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARS--GEILLNGFSLkd 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 151 LQSRLLKVISAYVMQDDLLFPMLTVKETLMFASEFRLPRSLSKSKKMERVEALIDQLGLrnAANTVIGDEGHrGVSGGER 230
Cdd:TIGR01193 541 IDRHTLRQFINYLPQEPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPL--GYQTELSEEGS-SISGGQK 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15028219 231 RRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMsiHQPSarIVELLDRLIILSRGKSVFNGS 308
Cdd:TIGR01193 618 QRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDKTIIFVA--HRLS--VAKQSDKIIVLDHGKIIEQGS 691
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
88-329 |
4.71e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 61.26 E-value: 4.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 88 FGFSRQNGVKTLlDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEgsLRGSVTLNGEKVLQSR---LLKVISAYVM 164
Cdd:PRK13642 12 FKYEKESDVNQL-NGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE--FEGKVKIDGELLTAENvwnLRRKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 165 QDDLLFPMLTVKETLMFASEFR-LPRSlSKSKKMERVEALIDQLGLRNAantvigdEGHRgVSGGERRRVSIGIDIIHDP 243
Cdd:PRK13642 89 NPDNQFVGATVEDDVAFGMENQgIPRE-EMIKRVDEALLAVNMLDFKTR-------EPAR-LSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 244 IVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVElLDRLIILSRGKSVFNGSPASLPGFFSDF---G 320
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMveiG 238
|
....*....
gi 15028219 321 RPIPEKENI 329
Cdd:PRK13642 239 LDVPFSSNL 247
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
99-322 |
6.26e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.48 E-value: 6.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 99 LLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEG--SLRGSVTLNGEKVLQSRLLKVISAYVMQD--DLLFPMLT 174
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrQTAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 175 ----VKETLmfasefrlpRSLSKSKKMERVEALIDQLGLRNAAnTVIGDEGHRgVSGGERRRVSIGIDIIHDPIVLFLDE 250
Cdd:PRK10418 98 mhthARETC---------LALGKPADDATLTAALEAVGLENAA-RVLKLYPFE-MSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15028219 251 PTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSVFNGSPASLpgffsdFGRP 322
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL------FNAP 232
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
96-397 |
6.41e-10 |
|
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: 63.01 E-value: 6.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 96 VKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRV--AEGSLRGSvtlngekvlqSRLlkvisAYVMQDDLLFPMl 173
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELepSEGKIKHS----------GRI-----SFSPQTSWIMPG- 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 174 TVKETLMFA---SEFRLpRSLSKSKKMERvealiDQLGLRNAANTVIGdEGHRGVSGGERRRVSIGIDIIHDPIVLFLDE 250
Cdd:TIGR01271 502 TIKDNIIFGlsyDEYRY-TSVIKACQLEE-----DIALFPEKDKTVLG-EGGITLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 251 PTSGLDSTNAFMVVQ--VLKRIAQSGSIVIMSIHQPSARIvellDRLIILSRGKSVFNGSPASLPGFFSDFGRPIPEKEN 328
Cdd:TIGR01271 575 PFTHLDVVTEKEIFEscLCKLMSNKTRILVTSKLEHLKKA----DKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEA 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 329 ISEFA--------LDLVRELEGSNEGT-------------KALVDFNEKWQQN----------KISLIQSAP---QTNKL 374
Cdd:TIGR01271 651 FDNFSaerrnsilTETLRRVSIDGDSTvfsgpetikqsfkQPPPEFAEKRKQSiilnpiasarKFSFVQMGPqkaQATTI 730
|
330 340 350
....*....|....*....|....*....|..
gi 15028219 375 DQ------DRSLSL---KEAINASVSRGKLVS 397
Cdd:TIGR01271 731 EDavrepsERKFSLvpeDEQGEESLPRGNQYH 762
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
100-312 |
6.88e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 62.34 E-value: 6.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTlIDALAGRVAEGSlRGSVTLNGEKVLQSRL--LKVISAYVMQDDLLFPMlTVKE 177
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKST-IANLLTRFYDID-EGEILLDGHDLRDYTLasLRNQVALVSQNVHLFND-TIAN 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 178 TLMFASEFRLPR-SLSKSKKMERVEALIDQLglRNAANTVIGDEGhRGVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLD 256
Cdd:PRK11176 436 NIAYARTEQYSReQIEEAARMAYAMDFINKM--DNGLDTVIGENG-VLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15028219 257 STNafmvvqvlKRIAQSG---------SIVIMsiHQPSAriVELLDRLIILSRGKSVFNGSPASL 312
Cdd:PRK11176 513 TES--------ERAIQAAldelqknrtSLVIA--HRLST--IEKADEILVVEDGEIVERGTHAEL 565
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
95-309 |
8.58e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.00 E-value: 8.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQ--SRLLKVISAYVMQDDLLFPM 172
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAH--GHVWLDGEHIQHyaSKEVARRIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 173 LTVKEtlmFASEFRLPRSLSKSKKMERVEALIDQlGLRNAANTVIGDEGHRGVSGGERRRVSIGIDIIHDPIVLFLDEPT 252
Cdd:PRK10253 96 ITVQE---LVARGRYPHQPLFTRWRKEDEEAVTK-AMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15028219 253 SGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSVFNGSP 309
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAP 228
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
100-307 |
1.04e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.53 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKST-------LIDaLAGRVAEGSLrgsvTLNGEKVLQ------SRLLKVISAYVMQD 166
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVsslaimgLID-YPGRVMAEKL----EFNGQDLQRisekerRNLVGAEVAMIFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 167 DL--LFPMLTVKETLMFAseFRLPRSLSKSKKMERVEALIDQLGLRNAANTVigDEGHRGVSGGERRRVSIGIDIIHDPI 244
Cdd:PRK11022 98 PMtsLNPCYTVGFQIMEA--IKVHQGGNKKTRRQRAIDLLNQVGIPDPASRL--DVYPHQLSGGMSQRVMIAMAIACRPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15028219 245 VLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSVFNG 307
Cdd:PRK11022 174 LLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
100-338 |
1.04e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 60.14 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSRLLKVISAYVMQDDLLFPML------ 173
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQ--GSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPesqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 174 -TVKETLMFAsefrlPRSLSKSKkmERVEALI-DQLGLRNAANTVIgDEGHRGVSGGERRRVSIGIDIIHDPIVLFLDEP 251
Cdd:PRK13649 101 eTVLKDVAFG-----PQNFGVSQ--EEAEALArEKLALVGISESLF-EKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 252 TSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSaRIVELLDRLIILSRGKSVFNGSPASLpgfFSD--------FGRPi 323
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMD-DVANYADFVYVLEKGKLVLSGKPKDI---FQDvdfleekqLGVP- 247
|
250
....*....|....*
gi 15028219 324 pekeNISEFALDLVR 338
Cdd:PRK13649 248 ----KITKFAQRLAD 258
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
110-312 |
1.06e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 61.66 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 110 GDILAVLGASGAGKSTLIdALAGRVAEGSlRGSVTLNGEKVLQ--SRLLKVISAYVMQDDLLFPMlTVKETLMFASEFRL 187
Cdd:TIGR00958 507 GEVVALVGPSGSGKSTVA-ALLQNLYQPT-GGQVLLDGVPLVQydHHYLHRQVALVGQEPVLFSG-SVRENIAYGLTDTP 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 188 PRSLSKSKKMERVEALIdqLGLRNAANTVIGDEGHRgVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTnafmVVQVL 267
Cdd:TIGR00958 584 DEEIMAAAKAANAHDFI--MEFPNGYDTEVGEKGSQ-LSGGQKQRIAIARALVRKPRVLILDEATSALDAE----CEQLL 656
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15028219 268 KRIAQSGSIVIMSI-HQPSarIVELLDRLIILSRGKSVFNGSPASL 312
Cdd:TIGR00958 657 QESRSRASRTVLLIaHRLS--TVERADQILVLKKGSVVEMGTHKQL 700
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
97-312 |
1.11e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.11 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALA---GRVAEGSLRGSVTLNGEKVLQSR---LLKVISAYVMQDDLLF 170
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNrmnDKVSGYRYSGDVLLGGRSIFNYRdvlEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 171 PMLTVKETLMFASEFRL-PRslsksKKMERV-EALIDQLGLRNAANTVIGDEGHRgVSGGERRRVSIGIDIIHDPIVLFL 248
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKLvPR-----KEFRGVaQARLTEVGLWDAVKDRLSDSPFR-LSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15028219 249 DEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSihQPSARIVELLDRLIILSRGKSVFNGSPASL 312
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLADRLTVIIVT--HNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
104-310 |
1.18e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.36 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 104 SGEASDGDILAVLGASGAGKSTLIDALAGRV--AEGSLRGSVTlngekvlqsrllkvIS---AYVMQDdllFPMlTVKET 178
Cdd:PRK13409 359 GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLkpDEGEVDPELK--------------ISykpQYIKPD---YDG-TVEDL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 179 LMFASEfrlprSLSKSkkMERVEaLIDQLGLRNaantvIGDEGHRGVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDST 258
Cdd:PRK13409 421 LRSITD-----DLGSS--YYKSE-IIKPLQLER-----LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15028219 259 NAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIilsrgksVFNGSPA 310
Cdd:PRK13409 488 QRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLM-------VFEGEPG 532
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
90-336 |
2.59e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 58.61 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 90 FSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKVLQSRLLKV---ISAYVMQD 166
Cdd:PRK13648 15 FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIG--IEKVKSGEIFYNNQAITDDNFEKLrkhIGIVFQNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 167 DLLFPMLTVKETLMFASEfrlPRSLSKSKKMERVEALIDQLGLRNAANtvigDEGHrGVSGGERRRVSIGIDIIHDPIVL 246
Cdd:PRK13648 93 DNQFVGSIVKYDVAFGLE---NHAVPYDEMHRRVSEALKQVDMLERAD----YEPN-ALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 247 FLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVElLDRLIILSRGKSVFNGSPASLpgfFSDfgrpipeK 326
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI---FDH-------A 233
|
250
....*....|
gi 15028219 327 ENISEFALDL 336
Cdd:PRK13648 234 EELTRIGLDL 243
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
95-302 |
2.73e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 57.96 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKV--LQSR---LLKVISAYVMQDDLL 169
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG--IERPSAGKIWFSGHDItrLKNRevpFLRRQIGMIFQDHHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 170 FPMLTVKETLMfasefrLPRSLSKSKKME---RVEALIDQLGLRNAA-NTVIGdeghrgVSGGERRRVSIGIDIIHDPIV 245
Cdd:PRK10908 91 LMDRTVYDNVA------IPLIIAGASGDDirrRVSAALDKVGLLDKAkNFPIQ------LSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15028219 246 LFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQpSARIVELLDRLIILSRGK 302
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHD-IGLISRRSYRMLTLSDGH 214
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
86-312 |
3.00e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 59.35 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 86 RRFGFSrqngvkTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGrvAEGSLRGSVTLNGEKVLQSRLLKVISAYVMQ 165
Cdd:PRK11432 14 KRFGSN------TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAG--LEKPTEGQIFIDGEDVTHRSIQQRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 166 DDLLFPMLTVKETLMFASEFRlprSLSKSKKMERVE---ALIDQLGLrnaantviGDEGHRGVSGGERRRVSIGIDIIHD 242
Cdd:PRK11432 86 SYALFPHMSLGENVGYGLKML---GVPKEERKQRVKealELVDLAGF--------EDRYVDQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 243 PIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSVFNGSPASL 312
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
90-283 |
3.85e-09 |
|
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: 57.34 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 90 FSRQNGVKTLlDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAegSLRGSVTLNGEKVLQSRLLKVIS------AYV 163
Cdd:cd03290 8 FSWGSGLATL-SNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ--TLEGKVHWSNKNESEPSFEATRSrnrysvAYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 164 MQDDLLFPMlTVKETLMFASEFrlprslskskKMERVEALIDQLGLRNAANTV-IGDE---GHRGV--SGGERRRVSIGI 237
Cdd:cd03290 85 AQKPWLLNA-TVEENITFGSPF----------NKQRYKAVTDACSLQPDIDLLpFGDQteiGERGInlSGGQRQRICVAR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15028219 238 DIIHDPIVLFLDEPTSGLDS--TNAFMVVQVLKRIAQSGSIVIMSIHQ 283
Cdd:cd03290 154 ALYQNTNIVFLDDPFSALDIhlSDHLMQEGILKFLQDDKRTLVLVTHK 201
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
97-256 |
3.94e-09 |
|
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: 59.56 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEgslrgsvtLNGEKVLQSRLlKVisAYVMQDDLLFPMLTVK 176
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD--------FNGEARPQPGI-KV--GYLPQEPQLDPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 177 ETLM-------------------FASEFRLPRSLSKskKMERVEALIDQLGLRNAANTV----------IGDEGHRGVSG 227
Cdd:TIGR03719 87 ENVEegvaeikdaldrfneisakYAEPDADFDKLAA--EQAELQEIIDAADAWDLDSQLeiamdalrcpPWDADVTKLSG 164
|
170 180
....*....|....*....|....*....
gi 15028219 228 GERRRVSIGIDIIHDPIVLFLDEPTSGLD 256
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
97-312 |
4.20e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 59.73 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGR--VAEGSLRgsvtLNGEKV--LQSRLLKVISAYVMQDdllfPM 172
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYypLTEGEIR----LDGRPLssLSHSVLRQGVAMVQQD----PV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 173 LTVKEtlMFASeFRLPRSLSKSKKMERVEALidQL-----GLRNAANTVIGDEGHRgVSGGERRRVSIGIDIIHDPIVLF 247
Cdd:PRK10790 426 VLADT--FLAN-VTLGRDISEEQVWQALETV--QLaelarSLPDGLYTPLGEQGNN-LSVGQKQLLALARVLVQTPQILI 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15028219 248 LDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSiHQPSArIVElLDRLIILSRGKSVFNGSPASL 312
Cdd:PRK10790 500 LDEATANIDSGTEQAIQQALAAVREHTTLVVIA-HRLST-IVE-ADTILVLHRGQAVEQGTHQQL 561
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
89-256 |
5.34e-09 |
|
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: 55.15 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 89 GFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGekvlqsrllKVISAYVmqddl 168
Cdd:cd03221 5 NLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDE--GIVTWGS---------TVKIGYF----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 169 lfpmltvketlmfasefrlprslskskkmervealiDQLglrnaantvigdeghrgvSGGERRRVSIGIDIIHDPIVLFL 248
Cdd:cd03221 69 ------------------------------------EQL------------------SGGEKMRLALAKLLLENPNLLLL 94
|
....*...
gi 15028219 249 DEPTSGLD 256
Cdd:cd03221 95 DEPTNHLD 102
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
83-310 |
6.79e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 57.01 E-value: 6.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 83 TLRRRFGFSRQNGVKTL--LDDVSGEASDGDILAVLGASGAGKSTLIDALAGrVAEGSlRGSVTLNGEkvlqsrllkvIS 160
Cdd:COG1134 23 SLKELLLRRRRTRREEFwaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAG-ILEPT-SGRVEVNGR----------VS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 161 AyvmqddLL-----F-PMLTVKETLMFASefRLpRSLSKS---KKMERVEALIDqlglrnaantvIGDEGHRGV---SGG 228
Cdd:COG1134 91 A------LLelgagFhPELTGRENIYLNG--RL-LGLSRKeidEKFDEIVEFAE-----------LGDFIDQPVktySSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 229 ERRRVSIGIdIIH-DPIVLFLDEPTSGLDStnAFM--VVQVLKRIAQSGSIVIMSIHQPSArIVELLDRLIILSRGKSVF 305
Cdd:COG1134 151 MRARLAFAV-ATAvDPDILLVDEVLAVGDA--AFQkkCLARIRELRESGRTVIFVSHSMGA-VRRLCDRAIWLEKGRLVM 226
|
....*
gi 15028219 306 NGSPA 310
Cdd:COG1134 227 DGDPE 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
100-257 |
7.18e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.37 E-value: 7.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGS-----LRGSVtlngekvlqsrllkvisAYVMQDDLLFPMlT 174
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdasvvIRGTV-----------------AYVPQVSWIFNA-T 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 175 VKETLMFASEFRLPRSlsksKKMERVEALIDQLGLRNAAN-TVIGDeghRGV--SGGERRRVSIGIDIIHDPIVLFLDEP 251
Cdd:PLN03130 695 VRDNILFGSPFDPERY----ERAIDVTALQHDLDLLPGGDlTEIGE---RGVniSGGQKQRVSMARAVYSNSDVYIFDDP 767
|
....*.
gi 15028219 252 TSGLDS 257
Cdd:PLN03130 768 LSALDA 773
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
100-308 |
7.18e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 58.27 E-value: 7.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIdalagRVAEGSLR---GSVTLNGEKVL-----QSRLLKVISAYVMQDdllFP 171
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLI-----RCINLLERptsGRVLVDGQDLTalsekELRKARRQIGMIFQH---FN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 172 ML---TVKETLMFASEFrlpRSLSKSKKMERVEALIDQLGL---RNA--ANtvigdeghrgVSGGERRRVSIGIDIIHDP 243
Cdd:PRK11153 93 LLssrTVFDNVALPLEL---AGTPKAEIKARVTELLELVGLsdkADRypAQ----------LSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15028219 244 IVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSI-HQPSArIVELLDRLIILSRGKSVFNGS 308
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLItHEMDV-VKRICDRVAVIDAGRLVEQGT 224
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
97-321 |
8.62e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 58.57 E-value: 8.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIdALAGR---VAEGSLR-GSVTLNGEKV--LQSRLlkvisAYVMQDDLLF 170
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLL-SLIQRhfdVSEGDIRfHDIPLTKLQLdsWRSRL-----AVVSQTPFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 171 PMlTVketlmfASEFRLPRSLSKSKKMERVEALI----DQLGLRNAANTVIGDeghRGV--SGGERRRVSIGIDIIHDPI 244
Cdd:PRK10789 402 SD-TV------ANNIALGRPDATQQEIEHVARLAsvhdDILRLPQGYDTEVGE---RGVmlSGGQKQRISIARALLLNAE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 245 VLFLDEPTSGLDSTNAFMVVQVLKRIAQsGSIVIMSIHQPSArIVElLDRLIILSRGKSVFNGSPASL---PGFFSDFGR 321
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLSA-LTE-ASEILVMQHGHIAQRGNHDQLaqqSGWYRDMYR 548
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
94-255 |
9.08e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.40 E-value: 9.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 94 NGVKTLlDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSLRGSVTLNGEKvLQSRLLK-------VIsayVMQD 166
Cdd:PRK13549 16 GGVKAL-DNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGEE-LQASNIRdteragiAI---IHQE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 167 DLLFPMLTVKETLMFASEFRLPRSLSKSKKMERVEALIDQLGLRNAANTVIGDEGhrgvsGGERRRVSIGIDIIHDPIVL 246
Cdd:PRK13549 91 LALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLG-----LGQQQLVEIAKALNKQARLL 165
|
....*....
gi 15028219 247 FLDEPTSGL 255
Cdd:PRK13549 166 ILDEPTASL 174
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
96-319 |
1.46e-08 |
|
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: 56.79 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 96 VKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRV--AEGSLRGSvtlngekvlqSRLlkvisAYVMQDDLLFPMl 173
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELepSEGKIKHS----------GRI-----SFSSQFSWIMPG- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 174 TVKETLMFA---SEFRLpRSLSKSKKMERvealiDQLGLRNAANTVIGdEGHRGVSGGERRRVSIGIDIIHDPIVLFLDE 250
Cdd:cd03291 113 TIKENIIFGvsyDEYRY-KSVVKACQLEE-----DITKFPEKDNTVLG-EGGITLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15028219 251 PTSGLDSTNAFMVVQ--VLKRIAQSGSIVIMSihqpSARIVELLDRLIILSRGKSVFNGSPASLPGFFSDF 319
Cdd:cd03291 186 PFGYLDVFTEKEIFEscVCKLMANKTRILVTS----KMEHLKKADKILILHEGSSYFYGTFSELQSLRPDF 252
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
95-256 |
1.72e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.89 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrgsvtlngEKVLQSRLLKVisAYVMQD---DLLFP 171
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDE---------GVIKRNGKLRI--GYVPQKlylDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 172 mLTVKETLMFASEFR----LPrslskskKMERVEA--LIDQlglrnaantvigdeGHRGVSGGERRRVSIGIDIIHDPIV 245
Cdd:PRK09544 84 -LTVNRFLRLRPGTKkediLP-------ALKRVQAghLIDA--------------PMQKLSGGETQRVLLARALLNRPQL 141
|
170
....*....|.
gi 15028219 246 LFLDEPTSGLD 256
Cdd:PRK09544 142 LVLDEPTQGVD 152
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
110-312 |
1.74e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.19 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 110 GDILAVLGASGAGKSTLIDALAGRVAEGSLRGSVTLNGEKVLQ------SRLlKVISAYvmQDDLLFPMLTVKETLMFAS 183
Cdd:CHL00131 33 GEIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKGESILDlepeerAHL-GIFLAF--QYPIEIPGVSNADFLRLAY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 184 EFRLP-RSLSKSKKMERVEALIDQLGLRNAANTVIGDEGHRGVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDstnafm 262
Cdd:CHL00131 110 NSKRKfQGLPELDPLEFLEIINEKLKLVGMDPSFLSRNVNEGFSGGEKKRNEILQMALLDSELAILDETDSGLD------ 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15028219 263 vVQVLKRIA--------QSGSIVIMSIHQpsarivELLDRLI-----ILSRGKSVFNGSpASL 312
Cdd:CHL00131 184 -IDALKIIAeginklmtSENSIILITHYQ------RLLDYIKpdyvhVMQNGKIIKTGD-AEL 238
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
112-305 |
1.96e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.00 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 112 ILAVLGASGAGKSTLIDALaGRVAE----GSLRGSVTLNGEKVLQSRL----LKVISAYVMQDDLLFPMLTVKETLMFAS 183
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRTF-NRLLElneeARVEGEVRLFGRNIYSPDVdpieVRREVGMVFQYPNPFPHLTIYDNVAIGV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 184 EFRlprSLSKSKKM--ERVEALIDQLGLRNAANTVIGDEGHRgVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAF 261
Cdd:PRK14267 111 KLN---GLVKSKKEldERVEWALKKAALWDEVKDRLNDYPSN-LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTA 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15028219 262 MVVQVLKRIAQSGSIVIMSiHQP--SARIVE-----LLDRLIILSRGKSVF 305
Cdd:PRK14267 187 KIEELLFELKKEYTIVLVT-HSPaqAARVSDyvaflYLGKLIEVGPTRKVF 236
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
141-288 |
2.19e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.73 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 141 GSVTLNGEKVLQSRL--LKVISAYVMQDDLLFPMlTVKETLMFASEFRLPRSLSKSKKMERVEALIDQLglRNAANTVIG 218
Cdd:PTZ00265 1277 GKILLDGVDICDYNLkdLRNLFSIVSQEPMLFNM-SIYENIKFGKEDATREDVKRACKFAAIDEFIESL--PNKYDTNVG 1353
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 219 DEGhRGVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARI 288
Cdd:PTZ00265 1354 PYG-KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI 1422
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
100-256 |
2.92e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 56.39 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAG--RVAEGSLRgsvtLNGEKV--LQSRLLKVisAYVMQDDLLFPMLTV 175
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGleRITSGEIW----IGGRVVneLEPADRDI--AMVFQNYALYPHMSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 176 KETLMFAsefrLP-RSLSKSKKMERVEAlidqlglrnAANTV-IG---DEGHRGVSGGERRRVSIGIDIIHDPIVLFLDE 250
Cdd:PRK11650 94 RENMAYG----LKiRGMPKAEIEERVAE---------AARILeLEpllDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
....*.
gi 15028219 251 PTSGLD 256
Cdd:PRK11650 161 PLSNLD 166
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
191-307 |
3.36e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.28 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 191 LSKSKKMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRI 270
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAK-----YSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM 190
|
90 100 110
....*....|....*....|....*....|....*..
gi 15028219 271 AQSGSIVIMSIhQPSARIVELLDRLIILSRGKSVFNG 307
Cdd:NF000106 191 VRDGATVLLTT-QYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
81-302 |
5.39e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.19 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 81 DVTLRRRFGfsrqngvKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAG-RVAEgslRGSVTLNGE-----KVLQSR 154
Cdd:COG3845 262 NLSVRDDRG-------VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGlRPPA---SGSIRLDGEditglSPRERR 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 155 LLKVisAYVMQDDL---LFPMLTVKETLMFASEFRLPRS----LSKSKKMERVEALIDQLGLRNA-ANTVIgdeghRGVS 226
Cdd:COG3845 332 RLGV--AYIPEDRLgrgLVPDMSVAENLILGRYRRPPFSrggfLDRKAIRAFAEELIEEFDVRTPgPDTPA-----RSLS 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15028219 227 GGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSihqpSARIVELL---DRLIILSRGK 302
Cdd:COG3845 405 GGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLI----SEDLDEILalsDRIAVMYEGR 479
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
110-282 |
5.60e-08 |
|
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: 55.95 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 110 GDILAVLGASGAGKSTLIDALAGRV--------AEGS-------LRGSVTLNGEKVLQSRLLKVI--SAYVmqdDLLfPM 172
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELkpnlgdydEEPSwdevlkrFRGTELQDYFKKLANGEIKVAhkPQYV---DLI-PK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 173 L---TVKETLMFASEFrlprslskskkmERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFLD 249
Cdd:COG1245 175 VfkgTVRELLEKVDER------------GKLDELAEKLGLENILDRDISE-----LSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|...
gi 15028219 250 EPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIH 282
Cdd:COG1245 238 EPSSYLDIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
97-309 |
7.48e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 54.32 E-value: 7.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTL---IDAL----AGRVAegsLRGSVTLNGEKV--LQSRLLKV-------IS 160
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALlipsEGKVY---VDGLDTSDEENLwdIRNKAGMVfqnpdnqIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 161 AYVMQDDLLF-PmltvkETL-MFASEFRlprslskskkmERVEALIDQLGL----RNAANTVigdeghrgvSGGERRRVS 234
Cdd:PRK13633 100 ATIVEEDVAFgP-----ENLgIPPEEIR-----------ERVDESLKKVGMyeyrRHAPHLL---------SGGQKQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15028219 235 I-GIDIIHdPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVElLDRLIILSRGKSVFNGSP 309
Cdd:PRK13633 155 IaGILAMR-PECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTP 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
102-310 |
8.41e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.44 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 102 DVSGEASDGDILAVLGASGAGKSTLIDALAG-RVAEGslrGSVTLNGEKV----LQSRLLKVIsAYVMQDDL---LF--- 170
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGlRPARG---GRIMLNGKEInalsTAQRLARGL-VYLPEDRQssgLYlda 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 171 PMLTVKETLMFAsefRLPRSLSKSKKMERVEALIDQLGLRNAAntviGDEGHRGVSGGERRRVSIGIDIIHDPIVLFLDE 250
Cdd:PRK15439 357 PLAWNVCALTHN---RRGFWIKPARENAVLERYRRALNIKFNH----AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 251 PTSGLDSTNAFMVVQVLKRIAQSGSIVIMsIHQPSARIVELLDRLIILSRGKsvFNGSPA 310
Cdd:PRK15439 430 PTRGVDVSARNDIYQLIRSIAAQNVAVLF-ISSDLEEIEQMADRVLVMHQGE--ISGALT 486
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
100-304 |
9.36e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.63 E-value: 9.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAgRVAEgSLRGSVTLNGEKV--LQSRLLKVIS---AYVMQDDL--LFPM 172
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALL-RLVE-SQGGEIIFNGQRIdtLSPGKLQALRrdiQFIFQDPYasLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 173 LTVKETLMfaSEFRLPRSLSKSKKMERVEALIDQLGLRNAANTVIGDEghrgVSGGERRRVSIGIDIIHDPIVLFLDEPT 252
Cdd:PRK10261 418 QTVGDSIM--EPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15028219 253 SGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSV 304
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
90-257 |
9.76e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.72 E-value: 9.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 90 FSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEgsLRGSVTLNGEkvlqsrllkviSAYV-----M 164
Cdd:TIGR00957 644 FTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK--VEGHVHMKGS-----------VAYVpqqawI 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 165 QDDllfpmlTVKETLMFASEFRLPRSLSKskkMERVEALIDQLGLRNAANTVIGDEGhRGVSGGERRRVSIGIDIIHDPI 244
Cdd:TIGR00957 711 QND------SLRENILFGKALNEKYYQQV---LEACALLPDLEILPSGDRTEIGEKG-VNLSGGQKQRVSLARAVYSNAD 780
|
170
....*....|...
gi 15028219 245 VLFLDEPTSGLDS 257
Cdd:TIGR00957 781 IYLFDDPLSAVDA 793
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
97-256 |
1.01e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEgslrgsvtLNGEKVLQSRLlKVisAYVMQDDLLFPMLTVK 176
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKE--------FEGEARPAPGI-KV--GYLPQEPQLDPEKTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 177 ETLM---------------FASEFRLPRSLSKS--KKMERVEALIDQLGLRNAANTV----------IGDEGHRGVSGGE 229
Cdd:PRK11819 89 ENVEegvaevkaaldrfneIYAAYAEPDADFDAlaAEQGELQEIIDAADAWDLDSQLeiamdalrcpPWDAKVTKLSGGE 168
|
170 180
....*....|....*....|....*..
gi 15028219 230 RRRVSIGIDIIHDPIVLFLDEPTSGLD 256
Cdd:PRK11819 169 RRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
109-278 |
1.08e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.20 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 109 DGDILAVLGASGAGKSTLIDALAGRV--------AEGS-------LRGSVTLNGEKVLQSRLLKVI--SAYVmqdDLLfP 171
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELipnlgdyeEEPSwdevlkrFRGTELQNYFKKLYNGEIKVVhkPQYV---DLI-P 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 172 ML---TVKETLMFASEfrlprslskskkMERVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFL 248
Cdd:PRK13409 174 KVfkgKVRELLKKVDE------------RGKLDEVVERLGLENILDRDISE-----LSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|
gi 15028219 249 DEPTSGLDSTNAFMVVQVLKRIAQSGSIVI 278
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLIRELAEGKYVLV 266
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
88-301 |
1.21e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.04 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 88 FGFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSLRGSVtlngekvlqsrllkvisayVMQDD 167
Cdd:COG2401 34 FGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV-------------------DVPDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 168 LLFPMLTVKEtlmfasefRLPRSLSKSKKMErveaLIDQLGLRNAANTVigdEGHRGVSGGERRRVSIGIDIIHDPIVLF 247
Cdd:COG2401 95 QFGREASLID--------AIGRKGDFKDAVE----LLNAVGLSDAVLWL---RRFKELSTGQKFRFRLALLLAERPKLLV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15028219 248 LDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSI-HQPSarIVELL--DRLIILSRG 301
Cdd:COG2401 160 IDEFCSHLDRQTAKRVARNLQKLARRAGITLVVAtHHYD--VIDDLqpDLLIFVGYG 214
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
95-259 |
2.00e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.03 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLlDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSLRGSVTLNGEkVLQSRLLK-------VIsayVMQDD 167
Cdd:NF040905 13 GVKAL-DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSYEGEILFDGE-VCRFKDIRdsealgiVI---IHQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 168 LLFPMLTVKETLMFASEfRLPRSL-SKSKKMERVEALIDQLGLRNAANTVIGDeghRGVsgGERRRVSIGIDIIHDPIVL 246
Cdd:NF040905 88 ALIPYLSIAENIFLGNE-RAKRGViDWNETNRRARELLAKVGLDESPDTLVTD---IGV--GKQQLVEIAKALSKDVKLL 161
|
170
....*....|....*.
gi 15028219 247 FLDEPTSGL---DSTN 259
Cdd:NF040905 162 ILDEPTAALneeDSAA 177
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
100-258 |
3.06e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 52.35 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALaGR----VAEGSLRGSVTLNGEKVLQSRL------LKVisAYVMQDDLL 169
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRCL-NRmndlIPGARVEGEILLDGEDIYDPDVdvvelrRRV--GMVFQKPNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 170 FPMlTVKETLMFAseFRLPRSLSKSKKMERVEALidqlgLRNAAntvIGDE-GHR------GVSGGERRRVSIGIDIIHD 242
Cdd:COG1117 104 FPK-SIYDNVAYG--LRLHGIKSKSELDEIVEES-----LRKAA---LWDEvKDRlkksalGLSGGQQQRLCIARALAVE 172
|
170
....*....|....*...
gi 15028219 243 PIVLFLDEPTSGLD--ST 258
Cdd:COG1117 173 PEVLLMDEPTSALDpiST 190
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
81-285 |
7.35e-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: 49.84 E-value: 7.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 81 DVTLRRRFGfsrqngvKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAG--RVAEGSLrgsvtlngEKVLQSRLLkv 158
Cdd:cd03223 5 NLSLATPDG-------RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGlwPWGSGRI--------GMPEGEDLL-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 159 isaYVMQDDLlFPMLTVKETLMFASEFRLprslskskkmervealidqlglrnaantvigdeghrgvSGGERRRVSIGID 238
Cdd:cd03223 68 ---FLPQRPY-LPLGTLREQLIYPWDDVL--------------------------------------SGGEQQRLAFARL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15028219 239 IIHDPIVLFLDEPTSGLDSTNAFMVVQVLKriaQSGSIVIMSIHQPS 285
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEESEDRLYQLLK---ELGITVISVGHRPS 149
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
83-310 |
8.21e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 51.33 E-value: 8.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 83 TLRRRFGFSRQNGVKTLlDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKV------LQSRLL 156
Cdd:PRK15112 13 TFRYRTGWFRRQTVEAV-KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTS--GELLIDDHPLhfgdysYRSQRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 157 KVIsayvMQD--DLLFPMLTVKETLMFAseFRLPRSLSKSKKMERVEALIDQLGLRNaantvigDEGH---RGVSGGERR 231
Cdd:PRK15112 90 RMI----FQDpsTSLNPRQRISQILDFP--LRLNTDLEPEQREKQIIETLRQVGLLP-------DHASyypHMLAPGQKQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15028219 232 RVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSVFNGSPA 310
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTA 235
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
95-300 |
1.17e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 48.90 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 95 GVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDAL---AGRVAEGSLRGSVTLNGEkvlqsrllkvISAYVmqddllfp 171
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIglaLGGAQSATRRRSGVKAGC----------IVAAV-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 172 mltvKETLMFasefrlprslskskkmerveaLIDQLglrnaantvigdeghrgvSGGERRRVSIGIDIIH-----DPIVL 246
Cdd:cd03227 68 ----SAELIF---------------------TRLQL------------------SGGEKELSALALILALaslkpRPLYI 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15028219 247 fLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPsaRIVELLDRLIILSR 300
Cdd:cd03227 105 -LDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLP--ELAELADKLIHIKK 155
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
99-314 |
1.41e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.49 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 99 LLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVA--EGSL-------------------RGSV-TLNGEKVL-QSRL 155
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLldDGRIiyeqdlivarlqqdpprnvEGTVyDFVAEGIEeQAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 156 LK---VISAYVMQD---DLLFPMLTVKETLMFASEFRLPrslskskkmERVEALIDQLGLrnAANTVIGDeghrgVSGGE 229
Cdd:PRK11147 98 LKryhDISHLVETDpseKNLNELAKLQEQLDHHNLWQLE---------NRINEVLAQLGL--DPDAALSS-----LSGGW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 230 RRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIaqSGSIVIMS-----IHQPSARIVElldrliiLSRGKSV 304
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF--QGSIIFIShdrsfIRNMATRIVD-------LDRGKLV 232
|
250
....*....|
gi 15028219 305 fngspaSLPG 314
Cdd:PRK11147 233 ------SYPG 236
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
97-256 |
2.11e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.28 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTL-LDDVSGEASDGDILAVLGASGAGKSTLIDALAG--RVAEGSLRgsvTLNG---EKVLQSRLLKVIsAYvMQDDL-- 168
Cdd:NF033858 13 KTVaLDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGarKIQQGRVE---VLGGdmaDARHRRAVCPRI-AY-MPQGLgk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 169 -LFPMLTVKETLMFaseF-RLpRSLSKSKKMERVEALIDQLGL-----RNAANtvigdeghrgVSGGERRRVSIGIDIIH 241
Cdd:NF033858 88 nLYPTLSVFENLDF---FgRL-FGQDAAERRRRIDELLRATGLapfadRPAGK----------LSGGMKQKLGLCCALIH 153
|
170
....*....|....*
gi 15028219 242 DPIVLFLDEPTSGLD 256
Cdd:NF033858 154 DPDLLILDEPTTGVD 168
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
100-326 |
2.48e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 50.19 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGrVAEGSLRgsVTLNGEKVLQSRLL--------KVIS---AYVMQD-- 166
Cdd:PRK15093 23 VDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWR--VTADRMRFDDIDLLrlsprerrKLVGhnvSMIFQEpq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 167 DLLFPMLTVKETLMFAsefrLPRSLSKSKKMERVE-------ALIDQLGLRNaantvigdegHRGVSG--------GERR 231
Cdd:PRK15093 100 SCLDPSERVGRQLMQN----IPGWTYKGRWWQRFGwrkrraiELLHRVGIKD----------HKDAMRsfpyelteGECQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 232 RVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIILSRGKSVFNGSPAS 311
Cdd:PRK15093 166 KVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKE 245
|
250 260
....*....|....*....|....*..
gi 15028219 312 LPGF------------FSDFGRPIPEK 326
Cdd:PRK15093 246 LVTTphhpytqaliraIPDFGSAMPHK 272
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
225-332 |
3.46e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.95 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 225 VSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPSARIVELLDRLIilsrgksV 304
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIH-------V 144
|
90 100
....*....|....*....|....*...
gi 15028219 305 FNGSpaslPGFFSDFGRPIPEKENISEF 332
Cdd:cd03222 145 FEGE----PGVYGIASQPKGTREGINRF 168
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
89-256 |
6.81e-06 |
|
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: 49.16 E-value: 6.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 89 GFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLnGEKVlqsrllKVisAYVMQD-D 167
Cdd:TIGR03719 327 NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDS--GTIEI-GETV------KL--AYVDQSrD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 168 LLFPMLTVKETLMFASEFRLprsLSKSKKMERveALIDQLGLRNaantviGDEGHR-GV-SGGERRRVSIGIDIIHDPIV 245
Cdd:TIGR03719 396 ALDPNKTVWEEISGGLDIIK---LGKREIPSR--AYVGRFNFKG------SDQQKKvGQlSGGERNRVHLAKTLKSGGNV 464
|
170
....*....|.
gi 15028219 246 LFLDEPTSGLD 256
Cdd:TIGR03719 465 LLLDEPTNDLD 475
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
100-310 |
1.56e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 47.08 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLI-------DALAGRVAEGSL--RGSvTLNGEKVLQSRLLKVIsAYVMQDDLLF 170
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFRVEGKVtfHGK-NLYAPDVDPVEVRRRI-GMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 171 PMlTVKETLMFAsefrlPRSLSKSKKM-ERVEALIDQLGLRNAANTVIGDEGhRGVSGGERRRVSIGIDIIHDPIVLFLD 249
Cdd:PRK14243 104 PK-SIYDNIAYG-----ARINGYKGDMdELVERSLRQAALWDEVKDKLKQSG-LSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15028219 250 EPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSiH--QPSARI--------VELLD------RLIILSRGKSVFNgSPA 310
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVT-HnmQQAARVsdmtaffnVELTEgggrygYLVEFDRTEKIFN-SPQ 251
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
191-328 |
2.68e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 191 LSKSKKM---ERVEALIDQLglrnaaNTVIGDEGHRgVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVL 267
Cdd:PTZ00265 550 VDVSKKVlihDFVSALPDKY------ETLVGSNASK-LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15028219 268 KRI-AQSGSIVIMSIHQPSAriVELLDRLIILSRGKsvfNGSPASLPGFFSDFGRPIPEKEN 328
Cdd:PTZ00265 623 NNLkGNENRITIIIAHRLST--IRYANTIFVLSNRE---RGSTVDVDIIGEDPTKDNKENNN 679
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
81-312 |
5.19e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.89 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 81 DVTLRRRfgfsrqNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAgRVAEGSlRGSVTLNGEKVLQSRL--LKV 158
Cdd:PLN03232 1239 DVHLRYR------PGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALF-RIVELE-KGRIMIDDCDVAKFGLtdLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 159 ISAYVMQDDLLFPMlTVKETLMFASEFRlPRSLSKSKKMERVEALIDQ--LGLRNAANtvigdEGHRGVSGGERRRVSIG 236
Cdd:PLN03232 1311 VLSIIPQSPVLFSG-TVRFNIDPFSEHN-DADLWEALERAHIKDVIDRnpFGLDAEVS-----EGGENFSVGQRQLLSLA 1383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15028219 237 IDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSiHQPSArIVElLDRLIILSRGKSVFNGSPASL 312
Cdd:PLN03232 1384 RALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIA-HRLNT-IID-CDKILVLSSGQVLEYDSPQEL 1456
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
99-283 |
9.30e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.17 E-value: 9.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 99 LLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSRllkviSAYvmQDDLLF-------- 170
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEK--GEILFERQSIKKDL-----CTY--QKQLCFvghrsgin 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 171 PMLTVKETLMFASEFrlprslsKSKKMErVEALIDQLGLRNAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIVLFLDE 250
Cdd:PRK13540 87 PYLTLRENCLYDIHF-------SPGAVG-ITELCRLFSLEHLIDYPCGL-----LSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190
....*....|....*....|....*....|...
gi 15028219 251 PTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQ 283
Cdd:PRK13540 154 PLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
170-310 |
9.95e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 9.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 170 FPMLTVKETLMFASEFRlPRSLSKSKKME----RVEALIDqLGL-----RNAANTVigdeghrgvSGGERRRVSI----G 236
Cdd:PRK00635 424 FQQMSLQELFIFLSQLP-SKSLSIEEVLQglksRLSILID-LGLpyltpERALATL---------SGGEQERTALakhlG 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 237 IDIIHdpIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQpsARIVELLDRLIILSR------GKSVFNGSPA 310
Cdd:PRK00635 493 AELIG--ITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD--EQMISLADRIIDIGPgagifgGEVLFNGSPR 568
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
175-307 |
1.00e-04 |
|
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: 43.47 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 175 VKETLMFASEFRLPRSLSKSKKMERVeaLIDQLglRNAANTVIG----DEGHRGVSGGERRRVSIG--IDIIHDPIVLFL 248
Cdd:cd03238 38 VNEGLYASGKARLISFLPKFSRNKLI--FIDQL--QFLIDVGLGyltlGQKLSTLSGGELQRVKLAseLFSEPPGTLFIL 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15028219 249 DEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQPsaRIVELLDRLIIL------SRGKSVFNG 307
Cdd:cd03238 114 DEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNL--DVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
97-293 |
2.97e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 44.52 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAgRVAegSLRGSVTLNGEKVLQSRLLKVISAYVMQDDLLFpmltvk 176
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLL--STEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVF------ 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 177 etlMFASEFRLPRSLSKSKKMERVEALIDQLGLRNAA-------NTVIGDEGHRgVSGGERRRVSIGIDIIHDPIVLFLD 249
Cdd:TIGR01271 1303 ---IFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIeqfpdklDFVLVDGGYV-LSNGHKQLMCLARSILSKAKILLLD 1378
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15028219 250 EPTSGLDSTNAFMVVQVLKRiAQSGSIVIMSIHqpsaRIVELLD 293
Cdd:TIGR01271 1379 EPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEH----RVEALLE 1417
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
110-282 |
5.10e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 42.14 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 110 GDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVLQSRLLKVIsAYVMQDDLLFPMLTVKETLMF--ASEFRL 187
Cdd:PRK13543 37 GEALLVQGDNGAGKTTLLRVLAGLLHVES--GQIQIDGKTATRGDRSRFM-AYLGHLPGLKADLSTLENLHFlcGLHGRR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 188 PRSLSKSKkmervealIDQLGLRNAANTVIgdeghRGVSGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVL 267
Cdd:PRK13543 114 AKQMPGSA--------LAIVGLAGYEDTLV-----RQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI 180
|
170
....*....|....*
gi 15028219 268 KRIAQSGSIVIMSIH 282
Cdd:PRK13543 181 SAHLRGGGAALVTTH 195
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
100-302 |
5.18e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.24 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSLRGSVTLNGEKVLQSRLLKVIS---AYVMQDDL---LFPML 173
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRNISGTVFKDGKEVDVSTVSDAIDaglAYVTEDRKgygLNLID 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 174 TVKETLMFASEFRLPRS--LSKSKKMERVEALIDQLGLRnaANTVigDEGHRGVSGGERRRVSIGIDIIHDPIVLFLDEP 251
Cdd:NF040905 356 DIKRNITLANLGKVSRRgvIDENEEIKVAEEYRKKMNIK--TPSV--FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEP 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15028219 252 TSGLDSTNAFMVVQVLKRIAQSGSIVIMsIhqpSARIVELL---DRLIILSRGK 302
Cdd:NF040905 432 TRGIDVGAKYEIYTIINELAAEGKGVIV-I---SSELPELLgmcDRIYVMNEGR 481
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
97-307 |
7.37e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.09 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 97 KTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSLRGSVTLNGEKVLQsrllkvisayvmqddlLFPMLTVK 176
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLE----------------LSPEDRAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 177 ETLMFA-----------SEFRLPRSLSKSKKMERVEALI---------DQLGLRNAANTVIGDEGHRGVSGGERRRVSIG 236
Cdd:PRK09580 78 EGIFMAfqypveipgvsNQFFLQTALNAVRSYRGQEPLDrfdfqdlmeEKIALLKMPEDLLTRSVNVGFSGGEKKRNDIL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 237 IDIIHDPIVLFLDEPTSGLDstnafmvVQVLKRIAQ--------SGSIVIMSIHQpsaRIVELL--DRLIILSRGKSVFN 306
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLD-------IDALKIVADgvnslrdgKRSFIIVTHYQ---RILDYIkpDYVHVLYQGRIVKS 227
|
.
gi 15028219 307 G 307
Cdd:PRK09580 228 G 228
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
86-312 |
1.35e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 42.24 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 86 RRFGFSRQNGVKTLLDDVSGEASDGDILAVLGASGAGKSTLIDALAgRVAEgSLRGSVTLNGEKVLQSRL--LKVISAYV 163
Cdd:TIGR00957 1288 RNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLF-RINE-SAEGEIIIDGLNIAKIGLhdLRFKITII 1365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 164 MQDDLLFPMLTVKETLMFA--SEFRLPRSLSKSKKMERVEALIDQLGLRNAantvigdEGHRGVSGGERRRVSIGIDIIH 241
Cdd:TIGR00957 1366 PQDPVLFSGSLRMNLDPFSqySDEEVWWALELAHLKTFVSALPDKLDHECA-------EGGENLSVGQRQLVCLARALLR 1438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15028219 242 DPIVLFLDEPTSGLDSTNAFMVVQVLKriAQSGSIVIMSIhqpSARIVELLD--RLIILSRGKSVFNGSPASL 312
Cdd:TIGR00957 1439 KTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTI---AHRLNTIMDytRVIVLDKGEVAEFGAPSNL 1506
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
100-148 |
3.27e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.18 E-value: 3.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 15028219 100 LDDVSGEASDGDILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGE 148
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTV--GKVDRNGE 86
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
72-291 |
3.53e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 72 VLNFNNLQYDVTLRRRFGFSrqngvKTLLDDVsgeasdgdILAVLGASGAGKSTLIDALAGRVAEGSlrGSVTLNGEKVl 151
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFDLS-----ITFLPSA--------ITYIKGANGCGKSSLLRMIAGIMQPSS--GNIYYKNCNI- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15028219 152 qSRLLKVISAYVMQDDLLFPMLTVKETLMFASEFRlprslsksKKMERVEALIDQLGLRNaantvIGDEGHRGVSGGERR 231
Cdd:PRK13541 65 -NNIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIY--------NSAETLYAAIHYFKLHD-----LLDEKCYSLSSGMQK 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15028219 232 RVSIGIDIIHDPIVLFLDEPTSGLDSTNAFMVVQVLKRIAQSGSIVIMSIHQ----PSARIVEL 291
Cdd:PRK13541 131 IVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSHLessiKSAQILQL 194
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
110-147 |
4.37e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.91 E-value: 4.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 15028219 110 GDILAVLGASGAGKSTLIDALA--GRVAEGSLRGSVTLNG 147
Cdd:COG4637 21 GPLTVLIGANGSGKSNLLDALRflSDAARGGLQDALARRG 60
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
108-133 |
5.90e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 39.53 E-value: 5.90e-03
10 20
....*....|....*....|....*.
gi 15028219 108 SDGDILAVLGASGAGKSTLIDALAGR 133
Cdd:PRK01889 193 SGGKTVALLGSSGVGKSTLVNALLGE 218
|
|
| PRK06547 |
PRK06547 |
hypothetical protein; Provisional |
98-133 |
6.38e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235825 Cd Length: 172 Bit Score: 38.18 E-value: 6.38e-03
10 20 30
....*....|....*....|....*....|....*...
gi 15028219 98 TLLDDVSGEASDGDILAVL--GASGAGKSTLIDALAGR 133
Cdd:PRK06547 1 MLVALIAARLCGGGMITVLidGRSGSGKTTLAGALAAR 38
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
114-131 |
9.85e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.27 E-value: 9.85e-03
|
| |
