|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
88-695 |
1.52e-170 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 501.88 E-value: 1.52e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 88 IPSQVKTNAKKLVFQNIQAVVLKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKNIETDGDIMING 167
Cdd:TIGR00955 10 VFGRVAQDGSWKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 168 RNMISNEMKKLSAYVQQDDVFIGTLTVRETLRFAAKLRSPSALGATELDSIVDELLVMMSLKKCENTKVGTMTE-KSLSR 246
Cdd:TIGR00955 90 MPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvKGLSG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 247 GERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSVYHMADQLILLSQGHVAYAG 326
Cdd:TIGR00955 170 GERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 327 PAKQVDAFFGRCGYPIPKFVSSPDHFMRVIShKSFETEDDYNKRIEKIVLE------HDIMKKEQSTHSTLSSSRREHPE 400
Cdd:TIGR00955 250 SPDQAVPFFSDLGHPCPENYNPADFYVQVLA-VIPGSENESRERIEKICDSfavsdiGRDMLVNTNLWSGKAGGLVKDSE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 401 TAPFT-FPRTWTAQFFFIFQRSSIQLWRERSVLLVKLIQTLIMSIMIGSTYYGLEIDKKSLPSFKGFAFVSVQMMHMLFM 479
Cdd:TIGR00955 329 NMEGIgYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALFLFLTNMTFQNV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 480 MPAMTVFWKDYPVVVREFQANMYSPSAYYLAKTTADSIQYLVFPVIFSGILLGMTSLPYSVVIITNYLIINILLSLNACS 559
Cdd:TIGR00955 409 FPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATS 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 560 VGQSFAAMCGHLATGMTVLPIVCVPLMVFGGFMITYEAIPWYFLPFAWVSWYKYGFEAITIvyfNHNSTISGCESNSSVA 639
Cdd:TIGR00955 489 FGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLI---NQWSDVDNIECTSANT 565
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 17539902 640 TLKMsidsnCTTGIEFIKAQAFEETHLWLDYTVILAVILFWKILGALLFTWRIRRA 695
Cdd:TIGR00955 566 TGPC-----PSSGEVILETLSFRNADLYLDLIGLVILIFFFRLLAYFALRIRIRRK 616
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
99-326 |
6.04e-79 |
|
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: 250.16 E-value: 6.04e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 99 LVFQNI-QAVVLKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnLKNIETDGDIMINGRNMISNEMKK 177
Cdd:cd03213 4 LSFRNLtVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGR-RTGLGVSGEVLINGRPLDKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 178 LSAYVQQDDVFIGTLTVRETLRFAAKLRSpsalgateldsivdellvmmslkkcentkvgtmteksLSRGERKRLAFACE 257
Cdd:cd03213 83 IIGYVPQDDILHPTLTVRETLMFAAKLRG-------------------------------------LSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17539902 258 ILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSVYHMADQLILLSQGHVAYAG 326
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
111-693 |
1.14e-67 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 241.94 E-value: 1.14e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 111 KKGVRQeILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKNIETDGDIMINGRNMISNeMKKLSAYVQQDDVFIG 190
Cdd:TIGR00956 772 KKEKRV-ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVITGGDRLVNGRPLDSS-FQRSIGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 191 TLTVRETLRFAAKLRSPSALGATELDSIVDELLVMMSLKKCENTKVGTMTEkSLSRGERKRLAFACEILTDPP-ILFCDE 269
Cdd:TIGR00956 850 TSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGE-GLNVEQRKRLTIGVELVAKPKlLLFLDE 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 270 PTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSVYHMADQLILLSQG-HVAYAGP----AKQVDAFFGRCGYP-IP 343
Cdd:TIGR00956 929 PTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGgQTVYFGDlgenSHTIINYFEKHGAPkCP 1008
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 344 KFVSSPDHFMRVIS-----------HKSFETEDDYNKRIEKIvlehDIMKKEQSTHSTLSSSRREHPETAPFTFprtwta 412
Cdd:TIGR00956 1009 EDANPAEWMLEVIGaapgahanqdyHEVWRNSSEYQAVKNEL----DRLEAELSKAEDDNDPDALSKYAASLWY------ 1078
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 413 QFFFIFQRSSIQLWRERSVLLVKLIQTLIMSIMIGSTYY-------GLEidKKSLPSFKGFAFVSVQMMHML--FMMPAM 483
Cdd:TIGR00956 1079 QFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFkvgtslqGLQ--NQMFAVFMATVLFNPLIQQYLppFVAQRD 1156
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 484 TVFwkdypvvVREFQANMYSPSAYYLAKTTADSIQYLVFPVIFSGILLGMTSL------PYSVVIITNY-LIINILLSLN 556
Cdd:TIGR00956 1157 LYE-------VRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGFywnaskTGQVHERGVLfWLLSTMFFLY 1229
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 557 ACSVGQSFAAMCGHLATGMTVLPIVCVPLMVFGGFMITYEAIP--WYFLpfAWVSWYKYGFEAI---------------T 619
Cdd:TIGR00956 1230 FSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPgfWIFM--YRCSPFTYLVQALlstgladvpvtckvkE 1307
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 620 IVYFNhNSTISGCE-------SNSSVATLKMSIDSNCT-----TGIEFIKAQAFEETHLWLDYTVILAVILFwKILGALL 687
Cdd:TIGR00956 1308 LLTFN-PPSGQTCGeymkpylENAGGYLLNPNATDSCSfcqysYTNDFLEPISSKYSGRWRNFGIFIAFIFF-NIIATVF 1385
|
....*.
gi 17539902 688 FTWRIR 693
Cdd:TIGR00956 1386 FYWLAR 1391
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
110-326 |
2.16e-66 |
|
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: 218.29 E-value: 2.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 110 KKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKNIETDGDIMINGRNMISNEMKKLSAYVQQDDVFI 189
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKPDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 190 GTLTVRETLRFAAKLRSPSALGatelDSIVDELLVMMSLKKCENTKVGTMTEKSLSRGERKRLAFACEILTDPPILFCDE 269
Cdd:cd03234 94 PGLTVRETLTYTAILRLPRKSS----DAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17539902 270 PTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSVYHMADQLILLSQGHVAYAG 326
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
110-687 |
6.33e-61 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 221.91 E-value: 6.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 110 KKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLK-NIETDGDIMINGrnMISNEMKK----LSAYVQQ 184
Cdd:TIGR00956 68 FRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGfHIGVEGVITYDG--ITPEEIKKhyrgDVVYNAE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 185 DDVFIGTLTVRETLRFAAKLRSPS--ALGATELD---SIVDELLVMMSLKKCENTKVGTMTEKSLSRGERKRLAFACEIL 259
Cdd:TIGR00956 146 TDVHFPHLTVGETLDFAARCKTPQnrPDGVSREEyakHIADVYMATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 260 TDPPILFCDEPTSGLDSFMSHQVIKALR-QLTIEGKTVICTIHQPSTSVYHMADQLILLSQGHVAYAGPAKQVDAFFGRC 338
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDSATALEFIRALKtSANILDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKM 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 339 GYPIPKFVSSPDHFMRVISHKSFETEDDYNKRIEKIVLE-----------HDIMK------KEQSTHSTLSSSRREHPE- 400
Cdd:TIGR00956 306 GFKCPDRQTTADFLTSLTSPAERQIKPGYEKKVPRTPQEfetywrnspeyAQLMKeideylDRCSESDTKEAYRESHVAk 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 401 -------TAPFTFPrtWTAQFFFIFQRSSIQLWRERSVLLVKLIQTLIMSIMIGSTYYGLEIDKKSlpsfkGFAFVSVQM 473
Cdd:TIGR00956 386 qskrtrpSSPYTVS--FSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSD-----FYSRGGALF 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 474 MHMLFMM----PAMTVFWKDYPVVVREFQANMYSPSAYYLAKTTADSIQYLVFPVIFSGILLGMTSLPYSVVIITNYLII 549
Cdd:TIGR00956 459 FAILFNAfsslLEIASMYEARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLI 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 550 NILLSLNACSVGQSFAAMCGHLATGMTVLPIVCVPLMVFGGFMITYEAIPWYFLPFAWVSWYKYGFEAITIVYFN----H 625
Cdd:TIGR00956 539 LFICTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVNEFHgrrfE 618
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17539902 626 NSTI--SGCESNS-----SVATLKMS-IDSNCTTGIEFIKAQ-AFEETHLWLDYTVILAVILFWKILGALL 687
Cdd:TIGR00956 619 CSQYvpSGGGYDNlgvtnKVCTVVGAePGQDYVDGDDYLKLSfQYYNSHKWRNFGIIIGFTVFFFFVYILL 689
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
118-593 |
8.67e-57 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 204.73 E-value: 8.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 118 ILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKNIETdGDIMINGRNMISNEMKKlSAYVQQDDVFIGTLTVRET 197
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFT-GTILANNRKPTKQILKR-TGFVTQDDILYPHLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 198 LRFAAKLRSPSALGATELDSIVDELLVMMSLKKCENTKVGTMTEKSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSF 277
Cdd:PLN03211 161 LVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 278 MSHQVIKALRQLTIEGKTVICTIHQPSTSVYHMADQLILLSQGHVAYAGPAKQVDAFFGRCGYPiPKFVSSPDHFMRVIS 357
Cdd:PLN03211 241 AAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFS-PSFPMNPADFLLDLA 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 358 HKSFETE---------------DDYNKRIE-KIVLEHDIMKKEQSTHSTLSSSRREHPETAPFTFPRTWTAQFFFIFQRs 421
Cdd:PLN03211 320 NGVCQTDgvserekpnvkqslvASYNTLLApKVKAAIEMSHFPQANARFVGSASTKEHRSSDRISISTWFNQFSILLQR- 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 422 SIQLWRERSVLLVKLIQTLIMSIMIGSTYYGLEidkkslpsfkgfaFVSVQ-MMHMLFMmpaMTVFWKDYP--------- 491
Cdd:PLN03211 399 SLKERKHESFNTLRVFQVIAAALLAGLMWWHSD-------------FRDVQdRLGLLFF---ISIFWGVFPsfnsvfvfp 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 492 ----VVVREFQANMYSPSAYYLAKTTADSIQYLVFPVIFSGILLGMTSLPYSVVIITNYLIINILLSLNACSVGQSFAAM 567
Cdd:PLN03211 463 qeraIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAA 542
|
490 500
....*....|....*....|....*.
gi 17539902 568 CGHLATGMTVLPIVCVPLMVFGGFMI 593
Cdd:PLN03211 543 IMDAKKASTIVTVTMLAFVLTGGFYV 568
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
99-326 |
3.85e-56 |
|
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: 189.38 E-value: 3.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 99 LVFQNIQAVVLKKKGVRQeILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnlKNIET-DGDIMINGRNmISNEMKK 177
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRQ-LLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGR--KTAGViTGEILINGRP-LDKNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 178 LSAYVQQDDVFIGTLTVRETLRFAAKLRspsalgateldsivdellvmmslkkcentkvgtmtekSLSRGERKRLAFACE 257
Cdd:cd03232 80 STGYVEQQDVHSPNLTVREALRFSALLR-------------------------------------GLSVEQRKRLTIGVE 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 258 ILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSVYHMADQLILLSQ-GHVAYAG 326
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
109-614 |
2.33e-49 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 187.36 E-value: 2.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 109 LKKKGV---RQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKNIeTDGDIMINGRNMISNEMKKLSAYVQQD 185
Cdd:PLN03140 883 MKEQGVtedRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGY-IEGDIRISGFPKKQETFARISGYCEQN 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 186 DVFIGTLTVRETLRFAAKLRSPSALGATELDSIVDELLVMMSLKKCENTKVGTMTEKSLSRGERKRLAFACEILTDPPIL 265
Cdd:PLN03140 962 DIHSPQVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSII 1041
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 266 FCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSVYHMADQLILLSQ-GHVAYAGP-----AKQVDAFFGRCG 339
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRgGQVIYSGPlgrnsHKIIEYFEAIPG 1121
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 340 YPIPKFVSSPDHFMRVISHKSFETeddynkRIEKIVLEHdimKKEQSTHSTLSSSRREHPETAP------FT--FPRTWT 411
Cdd:PLN03140 1122 VPKIKEKYNPATWMLEVSSLAAEV------KLGIDFAEH---YKSSSLYQRNKALVKELSTPPPgasdlyFAtqYSQSTW 1192
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 412 AQFFFIFQRSSIQLWRERSVLLVKLIQTLIMSIMIGSTYYGLEIDKKS---LPSFKGFAFVSVQMMHMLFMMPAMTVFWK 488
Cdd:PLN03140 1193 GQFKSCLWKQWWTYWRSPDYNLVRFFFTLAAALMVGTIFWKVGTKRSNandLTMVIGAMYAAVLFVGINNCSTVQPMVAV 1272
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 489 DYPVVVREFQANMYSPSAYYLAKTTADSIQYLVFPVIFSGILLGMTSLPYSVVIITNYLIINILLSLNACSVGQSFAAMC 568
Cdd:PLN03140 1273 ERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFISFFSFLYFTYYGMMTVSLT 1352
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 17539902 569 GHLATGMTVLPIVCVPLMVFGGFMITYEAIPWYFLPFAW---VSWYKYG 614
Cdd:PLN03140 1353 PNQQVAAIFAAAFYGLFNLFSGFFIPRPKIPKWWVWYYWicpVAWTVYG 1401
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
115-335 |
4.08e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 169.09 E-value: 4.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 115 RQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnLKNIeTDGDIMINGRNMISN--EMKKLSAYVQQDDVFIGTL 192
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLG--LLRP-TSGEVRVLGEDVARDpaEVRRRIGYVPQEPALYPDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 193 TVRETLRFAAKLRSpsaLGATELDSIVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILFCDEPTS 272
Cdd:COG1131 89 TVRENLRFFARLYG---LPRKEARERIDELLELFGLTDAADRKVGT-----LSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17539902 273 GLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTsVYHMADQLILLSQGHVAYAGPAKQV------DAFF 335
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEE-AERLCDRVAIIDKGRIVADGTPDELkarlleDVFL 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
104-337 |
5.24e-40 |
|
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: 146.93 E-value: 5.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 104 IQAVVLKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnLKNieTDGDIMINGRNMISNEMKKLS--AY 181
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGL-LKP--DSGSILIDGEDVRKEPREARRqiGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 182 VQQDDVFIGTLTVRETLRFAAKLRSpsaLGATELDSIVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTD 261
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYFAELYG---LFDEELKKRIEELIELLGLEEFLDRRVGE-----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17539902 262 PPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTsVYHMADQLILLSQGHVAYAGPAKQVDAFFGR 337
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQE-VEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
417-621 |
8.90e-40 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 145.11 E-value: 8.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 417 IFQRSSIQLWRERSVLLVKLIQTLIMSIMIGSTYYGLEiDKKSLPSFKGFAFVSVQMMHMLFMMPAMTVFWKDYPVVVRE 496
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLG-NQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 497 FQANMYSPSAYYLAKTTADSIQYLVFPVIFSGILLGMTSLPYSVVIITNYLIINILLSLNACSVGQSFAAMCGHLATGMT 576
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17539902 577 VLPIVCVPLMVFGGFMITYEAIPWYFLPFAWVSWYKYGFEAITIV 621
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
110-326 |
5.79e-39 |
|
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: 142.79 E-value: 5.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 110 KKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKNIETDGDIMINGRNM--ISNEMKKLSAYVQQDDV 187
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPYkeFAEKYPGEIIYVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 188 FIGTLTVRETLRFAAKLRSpsalgatelDSIVdellvmmslkkcentkvgtmteKSLSRGERKRLAFACEILTDPPILFC 267
Cdd:cd03233 94 HFPTLTVRETLDFALRCKG---------NEFV----------------------RGISGGERKRVSIAEALVSRASVLCW 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 268 DEPTSGLDSFMSHQVIKALRQLT-IEGKTVICTIHQPSTSVYHMADQLILLSQGHVAYAG 326
Cdd:cd03233 143 DNSTRGLDSSTALEILKCIRTMAdVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
118-620 |
1.30e-38 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 154.23 E-value: 1.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 118 ILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKNIETDGDIMINGRNMISNEMKKLSAYVQQDDVFIGTLTVRET 197
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKVSGEITYNGYRLNEFVPRKTSAYISQNDVHVGVMTVKET 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 198 LRFAAKLR-------------------------------SPSALGATELDSIVDELLVMMSLKKCENTKVGTMTEKSLSR 246
Cdd:PLN03140 260 LDFSARCQgvgtrydllselarrekdagifpeaevdlfmKATAMEGVKSSLITDYTLKILGLDICKDTIVGDEMIRGISG 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 247 GERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLT-IEGKTVICTIHQPSTSVYHMADQLILLSQGHVAYA 325
Cdd:PLN03140 340 GQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVhLTEATVLMSLLQPAPETFDLFDDIILLSEGQIVYQ 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 326 GPAKQVDAFFGRCGYPIPKFVSSPDHFMRVISHKSFETEDDYNKRIEKIVLEHDIMKKEQSTHstlSSSRREHPETAPFT 405
Cdd:PLN03140 420 GPRDHILEFFESCGFKCPERKGTADFLQEVTSKKDQEQYWADRNKPYRYISVSEFAERFKSFH---VGMQLENELSVPFD 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 406 FPRTWTAQFFF-------------IFQRSSIQLWRERSVLLVKLIQTLIMSImIGSTYYgLEIDKKSLPSFKGFAFVSVQ 472
Cdd:PLN03140 497 KSQSHKAALVFskysvpkmellkaCWDKEWLLMKRNAFVYVFKTVQIIIVAA-IASTVF-LRTEMHTRNEEDGALYIGAL 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 473 MMHMLFMM----PAMTVFWKDYPVVVREFQANMYSPSAYYLAKttadsiqylvfpvifsgILLGmtsLPYSV------VI 542
Cdd:PLN03140 575 LFSMIINMfngfAELALMIQRLPVFYKQRDLLFHPPWTFTLPT-----------------FLLG---IPISIiesvvwVV 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 543 ITNY--------------LIINILLSLNACSVGQSFAAMCGHLATGMTVLPIVCVPLMVFGGFMITYEAIPWYFLPFAWV 608
Cdd:PLN03140 635 ITYYsigfapeasrffkqLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPNWWEWAYWV 714
|
570
....*....|..
gi 17539902 609 SWYKYGFEAITI 620
Cdd:PLN03140 715 SPLSYGFNALAV 726
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
116-321 |
2.60e-38 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 141.07 E-value: 2.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNlknIETDGDIMINGRNMISNEMKKLS---AYVQQ--DDVFIG 190
Cdd:cd03225 14 RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL---GPTSGEVLVDGKDLTKLSLKELRrkvGLVFQnpDDQFFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 191 TlTVRETLRFAAKLRSpsaLGATELDSIVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILFCDEP 270
Cdd:cd03225 91 P-TVEEEVAFGLENLG---LPEEEIEERVEEALELVGLEGLRDRSPFT-----LSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17539902 271 TSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTsVYHMADQLILLSQGH 321
Cdd:cd03225 162 TAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDL-LLELADRVIVLEDGK 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
127-326 |
1.07e-36 |
|
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: 136.87 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 127 RPGELTFIMGSSGAGKTTLLNILTGRNLKnieTDGDIMINGRNmISNEMKKLSA---YVQQDDVFIGTLTVRETLRFAAK 203
Cdd:cd03263 26 YKGEIFGLLGHNGAGKTTTLKMLTGELRP---TSGTAYINGYS-IRTDRKAARQslgYCPQFDALFDELTVREHLRFYAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 204 LRSpsaLGATELDSIVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVI 283
Cdd:cd03263 102 LKG---LPKSEIKEEVELLLRVLGLTDKANKRART-----LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIW 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17539902 284 KALRQLtIEGKTVICTIHqpstsvyHM------ADQLILLSQGHVAYAG 326
Cdd:cd03263 174 DLILEV-RKGRSIILTTH-------SMdeaealCDRIAIMSDGKLRCIG 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
110-322 |
2.48e-33 |
|
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: 127.61 E-value: 2.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 110 KKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlknIE--TDGDIMINGRNMISNEMKKLSA------- 180
Cdd:cd03255 11 GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGG-----LDrpTSGEVRVDGTDISKLSEKELAAfrrrhig 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 181 YVQQDDVFIGTLTVRETLRFAAKLRSpsaLGATELDSIVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILT 260
Cdd:cd03255 86 FVFQSFNLLPDLTALENVELPLLLAG---VPKKERRERAEELLERVGLGDRLNHYPSE-----LSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539902 261 DPPILFCDEPTSGLDSFMSHQVIKALRQLT-IEGKTVICTIHQPstSVYHMADQLILLSQGHV 322
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDP--ELAEYADRIIELRDGKI 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
115-322 |
4.64e-33 |
|
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: 125.20 E-value: 4.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 115 RQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrNLKNieTDGDIMINGRNMISN--EMKKLSAYVQQDDVFIGTL 192
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILG-LLKP--DSGEIKVLGKDIKKEpeEVKRRIGYLPEEPSLYENL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 193 TVRETLRfaaklrspsalgateldsivdellvmmslkkcentkvgtmteksLSRGERKRLAFACEILTDPPILFCDEPTS 272
Cdd:cd03230 89 TVRENLK--------------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17539902 273 GLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTsVYHMADQLILLSQGHV 322
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGKTILLSSHILEE-AERLCDRVAILNNGRI 173
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
104-322 |
1.35e-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: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 104 IQAVVLKKK----GVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlknIE--TDGDIMINGRNMIS-NEmK 176
Cdd:COG1136 5 LELRNLTKSygtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGG-----LDrpTSGEVLIDGQDISSlSE-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 177 KLSA-------YVQQDdvF--IGTLTVRETLRFAAKLRSpsaLGATELDSIVDELLVMMSLKKCENTKVGTmteksLSRG 247
Cdd:COG1136 79 ELARlrrrhigFVFQF--FnlLPELTALENVALPLLLAG---VSRKERRERARELLERVGLGDRLDHRPSQ-----LSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17539902 248 ERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQPstSVYHMADQLILLSQGHV 322
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDP--ELAARADRVIRLRDGRI 222
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
119-272 |
2.02e-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: 122.37 E-value: 2.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 119 LKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrNLKNIEtdGDIMINGRNMISNEMKKLS---AYVQQDDVFIGTLTVR 195
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAG-LLSPTE--GTILLDGQDLTDDERKSLRkeiGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17539902 196 ETLRFAAKLRspsALGATELDSIVDELLVMMSLKKCENTKVGtMTEKSLSRGERKRLAFACEILTDPPILFCDEPTS 272
Cdd:pfam00005 78 ENLRLGLLLK---GLSKREKDARAEEALEKLGLGDLADRPVG-ERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
117-331 |
8.23e-32 |
|
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: 123.60 E-value: 8.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 117 EILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnLKNieTDGDIMINGRNMISNEMKKLS---AYVQQ--DDVFIGT 191
Cdd:COG1122 15 PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGL-LKP--TSGEVLVDGKDITKKNLRELRrkvGLVFQnpDDQLFAP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 192 lTVRETLRFaaklrSPSALG--ATELDSIVDELLVMMSLKKCENTKVgtmteKSLSRGERKRLAFACEILTDPPILFCDE 269
Cdd:COG1122 92 -TVEEDVAF-----GPENLGlpREEIRERVEEALELVGLEHLADRPP-----HELSGGQKQRVAIAGVLAMEPEVLVLDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17539902 270 PTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTsVYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:COG1122 161 PTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDGRIVADGTPREV 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
115-331 |
1.12e-31 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 124.00 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 115 RQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrNLKniETDGDIMINGRNMIS---NEMKKLSAYVQQDDVFIGT 191
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAG-LLK--PSSGEVLLDGRDLASlsrRELARRIAYVPQEPPAPFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 192 LTVRETL---RFA--AKLRSPSAlgatELDSIVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILF 266
Cdd:COG1120 90 LTVRELValgRYPhlGLFGRPSA----EDREAVEEALERTGLEHLADRPVDE-----LSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17539902 267 CDEPTSGLDsfMSHQ--VIKALRQLTIE-GKTVICTIHQPSTSVYHmADQLILLSQGHVAYAGPAKQV 331
Cdd:COG1120 161 LDEPTSHLD--LAHQleVLELLRRLARErGRTVVMVLHDLNLAARY-ADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
118-333 |
8.76e-31 |
|
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: 120.68 E-value: 8.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 118 ILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnlknIETD-GDIMINGRN---MISNEMKKL---SAYVQQDDVFIG 190
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGL----LRPDsGEVLIDGEDisgLSEAELYRLrrrMGMLFQSGALFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 191 TLTVRETLRFAakLRSPSALGATELDSIVDELLVMMSLKKCENTKVGtmtekSLSRGERKRLAFACEILTDPPILFCDEP 270
Cdd:cd03261 91 SLTVFENVAFP--LREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPA-----ELSGGMKKRVALARALALDPELLLYDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17539902 271 TSGLDSFMS---HQVIKALRQLTieGKTVICTIHQPSTsVYHMADQLILLSQGHVAYAGPAKQVDA 333
Cdd:cd03261 164 TAGLDPIASgviDDLIRSLKKEL--GLTSIMVTHDLDT-AFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
118-303 |
4.29e-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: 4.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 118 ILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKnieTDGDIMINGRNMISN--EMKKLSAYVQQDDVFIGTLTVR 195
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPP---SAGEVLWNGEPIRDAreDYRRRLAYLGHADGLKPELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 196 ETLRFAAKLRSPSALGATeldsiVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILFCDEPTSGLD 275
Cdd:COG4133 94 ENLRFWAALYGLRADREA-----IDEALEAVGLAGLADLPVRQ-----LSAGQKRRVALARLLLSPAPLWLLDEPFTALD 163
|
170 180
....*....|....*....|....*...
gi 17539902 276 SFMSHQVIKALRQLTIEGKTVICTIHQP 303
Cdd:COG4133 164 AAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
116-331 |
1.53e-28 |
|
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: 121.86 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlknIE--TDGDIMINGRNMisnemKKLS--------AYVQQD 185
Cdd:COG2274 488 PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG-----LYepTSGRILIDGIDL-----RQIDpaslrrqiGVVLQD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 186 DV-FIGTltVRETLRFAAKLRSPS----ALGATELDSIVDELlvMMSLkkceNTKVGTMTeKSLSRGERKRLAFACEILT 260
Cdd:COG2274 558 VFlFSGT--IRENITLGDPDATDEeiieAARLAGLHDFIEAL--PMGY----DTVVGEGG-SNLSGGQRQRLAIARALLR 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17539902 261 DPPILFCDEPTSGLDSFMSHQVIKALRQLTiEGKTVICTIHQPSTSVyhMADQLILLSQGHVAYAGPAKQV 331
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIR--LADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
116-321 |
3.31e-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: 110.80 E-value: 3.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNlknIETDGDIMINGRN---MISNEMKKLSAYVQQddvfigtl 192
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLL---KPTSGEILIDGKDiakLPLEELRRRIGYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 193 tvretlrfaaklrspsalgateldsivdellvmmslkkcentkvgtmteksLSRGERKRLAFACEILTDPPILFCDEPTS 272
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17539902 273 GLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTsVYHMADQLILLSQGH 321
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPEL-AELAADRVIVLKDGK 157
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
116-333 |
3.60e-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: 113.54 E-value: 3.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnLknIE-TDGDIMINGRNMIS------NEMKKLSAYVQQDDVF 188
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIG--L--LRpDSGEILVDGQDITGlsekelYELRRRIGMLFQGGAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 189 IGTLTVRETLRFAakLRSPSALGATELDSIVDELLVMMSLKKCENtkvgtmteK---SLSRGERKRLAFACEILTDPPIL 265
Cdd:COG1127 94 FDSLTVFENVAFP--LREHTDLSEAEIRELVLEKLELVGLPGAAD--------KmpsELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17539902 266 FCDEPTSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQPStSVYHMADQLILLSQGHVAYAGPAKQVDA 333
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLD-SAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
115-330 |
4.56e-28 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 119.09 E-value: 4.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 115 RQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKnieTDGDIMING---RNMISNEMKKLSAYVQQDDV-FIG 190
Cdd:COG4988 349 GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP---YSGSILINGvdlSDLDPASWRRQIAWVPQNPYlFAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 191 tlTVRETLRFAAKLRSPS----ALGATELDSIVDEL---LvmmslkkceNTKVGtmtEKS--LSRGERKRLAFACEILTD 261
Cdd:COG4988 426 --TIRENLRLGRPDASDEeleaALEAAGLDEFVAALpdgL---------DTPLG---EGGrgLSGGQAQRLALARALLRD 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17539902 262 PPILFCDEPTSGLDSFMSHQVIKALRQLTiEGKTVICTIHQPSTSVYhmADQLILLSQGHVAYAGPAKQ 330
Cdd:COG4988 492 APLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ--ADRILVLDDGRIVEQGTHEE 557
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
116-320 |
9.42e-28 |
|
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: 111.19 E-value: 9.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnLKniETDGDIMINGRNMISNEMKKLSAYVQQD-DVFIGTLTV 194
Cdd:cd03226 13 TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGL-IK--ESSGSILLNGKPIKAKERRKSIGYVMQDvDYQLFTDSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 195 RETLRFAAKLRSPSAlgateldSIVDELLVMMSLKKcentkvgtMTEK---SLSRGERKRLAFACEILTDPPILFCDEPT 271
Cdd:cd03226 90 REELLLGLKELDAGN-------EQAETVLKDLDLYA--------LKERhplSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17539902 272 SGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTsVYHMADQLILLSQG 320
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQGKAVIVITHDYEF-LAKVCDRVLLLANG 202
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
113-337 |
9.91e-28 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 118.33 E-value: 9.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 113 GVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTgRNLKniETDGDIMINGRN---MISNEMKKLSAYVQQD-DVF 188
Cdd:COG4987 345 GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLL-RFLD--PQSGSITLGGVDlrdLDEDDLRRRIAVVPQRpHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 189 IGTLtvRETLRFA------AKLRSpsALGATELDSIVDEL---LvmmslkkceNTKVGtmtEK--SLSRGERKRLAFACE 257
Cdd:COG4987 422 DTTL--RENLRLArpdatdEELWA--ALERVGLGDWLAALpdgL---------DTWLG---EGgrRLSGGERRRLALARA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 258 ILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTiEGKTVICTIHQPstSVYHMADQLILLSQGHVAYAGPAKQVDAFFGR 337
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRL--AGLERMDRILVLEDGRIVEQGTHEELLAQNGR 562
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
117-333 |
1.15e-27 |
|
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: 111.37 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 117 EILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnLKNIeTDGDIMINGR---NMISNEMKKLS-AYVQQD-DVFiGT 191
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMG--LLPP-RSGSIRFDGRditGLPPHERARAGiGYVPEGrRIF-PE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 192 LTVRETLRFAAKLRSPSALGATeldsiVDELLVMMS-LKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILFCDEP 270
Cdd:cd03224 90 LTVEENLLLGAYARRRAKRKAR-----LERVYELFPrLKERRKQLAGT-----LSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539902 271 TSGLDSFMSHQVIKALRQLTIEGKTVIcTIHQPSTSVYHMADQLILLSQGHVAYAGPAKQVDA 333
Cdd:cd03224 160 SEGLAPKIVEEIFEAIRELRDEGVTIL-LVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
115-331 |
3.13e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 110.95 E-value: 3.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 115 RQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrNLKNieTDGDIMINGRNMisNEMKKLSAYV-QQDDVFIGT-L 192
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILG-LLPP--TSGTVRLFGKPP--RRARRRIGYVpQRAEVDWDFpI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 193 TVRETL---RFAAK--LRSPSAlgatELDSIVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILFC 267
Cdd:COG1121 93 TVRDVVlmgRYGRRglFRRPSR----ADREAVDEALERVGLEDLADRPIGE-----LSGGQQQRVLLARALAQDPDLLLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17539902 268 DEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTsVYHMADQLILLSQGHVAYaGPAKQV 331
Cdd:COG1121 164 DEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGA-VREYFDRVLLLNRGLVAH-GPPEEV 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
117-326 |
6.15e-26 |
|
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: 105.21 E-value: 6.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 117 EILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrNLKNIEtdGDIMINGRNmisnemkklsayvqqddvfIGTLTVRE 196
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAG-LLKPSS--GEILLDGKD-------------------LASLSPKE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 197 tlrfAAKLRS--PSALGATELDSIVDELLvmmslkkcentkvgtmteKSLSRGERKRLAFACEILTDPPILFCDEPTSGL 274
Cdd:cd03214 71 ----LARKIAyvPQALELLGLAHLADRPF------------------NELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17539902 275 DsfMSHQ--VIKALRQLTIE-GKTVICTIHQPSTsVYHMADQLILLSQGHVAYAG 326
Cdd:cd03214 129 D--IAHQieLLELLRRLARErGKTVVMVLHDLNL-AARYADRVILLKDGRIVAQG 180
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
116-330 |
7.56e-26 |
|
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: 106.55 E-value: 7.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNIL-------TGRnlknIETDG-DImingRNMISNEMKKLSAYVQQDDV 187
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfrfydvsSGS----ILIDGqDI----REVTLDSLRRAIGVVPQDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 188 FIGTlTVRETLRFAAklrspsaLGATELDSI-------VDEllVMMSLKKCENTKVGTMTEKsLSRGERKRLAFACEILT 260
Cdd:cd03253 86 LFND-TIGYNIRYGR-------PDATDEEVIeaakaaqIHD--KIMRFPDGYDTIVGERGLK-LSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 261 DPPILFCDEPTSGLDSFMSHQVIKALRQLTiEGKTVICTIHQPSTSVYhmADQLILLSQGHVAYAGPAKQ 330
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN--ADKIIVLKDGRIVERGTHEE 221
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
116-321 |
9.29e-26 |
|
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: 104.39 E-value: 9.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnLKNIeTDGDIMING---RNMISNEMKKLSAYVQQDdVFIGTL 192
Cdd:cd03228 15 KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLR--LYDP-TSGEILIDGvdlRDLDLESLRKNIAYVPQD-PFLFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 193 TVRETLrfaaklrspsalgateldsivdellvmmslkkcentkvgtmteksLSRGERKRLAFACEILTDPPILFCDEPTS 272
Cdd:cd03228 91 TIRENI---------------------------------------------LSGGQRQRIAIARALLRDPPILILDEATS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17539902 273 GLDSFMSHQVIKALRQLTiEGKTVICTIHQPSTsvYHMADQLILLSQGH 321
Cdd:cd03228 126 ALDPETEALILEALRALA-KGKTVIVIAHRLST--IRDADRIIVLDDGR 171
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
116-323 |
2.07e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 111.02 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnLKNIeTDGDIMINGRNMisNEMKKLS-----AYVQQdDVFIG 190
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLR--FYDP-TSGRILIDGVDI--RDLTLESlrrqiGVVPQ-DTFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 191 TLTVRETLRFAAKLRSP----SALGATELDSIVdellvmMSLKKCENTKVGtmtEK--SLSRGERKRLAFACEILTDPPI 264
Cdd:COG1132 427 SGTIRENIRYGRPDATDeeveEAAKAAQAHEFI------EALPDGYDTVVG---ERgvNLSGGQRQRIAIARALLKDPPI 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 265 LFCDEPTSGLDSFMSHQVIKALRQLTiEGKTVIcTI-HQPSTsVyHMADQLILLSQGHVA 323
Cdd:COG1132 498 LILDEATSALDTETEALIQEALERLM-KGRTTI-VIaHRLST-I-RNADRILVLDDGRIV 553
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
115-331 |
3.09e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 105.24 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 115 RQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlkNIETD-GDIMINGRNMIS---NEMKKLSAYVQQDdvfiG 190
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG----ELSPDsGEVRLNGRPLADwspAELARRRAVLPQH----S 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 191 TL----TVRETLRFAaklRSPSALGATELDSIVDELLvmmslkkcENTKVGTMTEKS---LSRGERKRLAFAcEILT--- 260
Cdd:PRK13548 86 SLsfpfTVEEVVAMG---RAPHGLSRAEDDALVAAAL--------AQVDLAHLAGRDypqLSGGEQQRVQLA-RVLAqlw 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17539902 261 ----DPPILFCDEPTSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQPS-TSVYhmADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK13548 154 epdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARY--ADRIVLLHQGRLVADGTPAEV 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
116-326 |
3.39e-25 |
|
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: 104.14 E-value: 3.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlknIE--TDGDIMINGRNmISNEM--KKLSAYVQQDDVFIGT 191
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAG-----LErpDSGEILIDGRD-VTGVPpeRRNIGMVFQDYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 192 LTVRETLRFAAKLRspsALGATELDSIVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILFCDEPT 271
Cdd:cd03259 87 LTVAENIAFGLKLR---GVPKAEIRARVRELLELVGLEGLLNRYPHE-----LSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17539902 272 SGLD----SFMSHQVIKALRQLtieGKTVICTIHQPStSVYHMADQLILLSQGHVAYAG 326
Cdd:cd03259 159 SALDaklrEELREELKELQREL---GITTIYVTHDQE-EALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
115-326 |
3.88e-25 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 103.77 E-value: 3.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 115 RQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrNLKNIEtdGDIMINGRNmiSNEMKKLSAYV-QQDDV---Fig 190
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILG-LLKPTS--GSIRVFGKP--LEKERKRIGYVpQRRSIdrdF-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 191 TLTVRETLRFAAKLRSPSALGATELD-SIVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILFCDE 269
Cdd:cd03235 84 PISVRDVVLMGLYGHKGLFRRLSKADkAKVDEALERVGLSELADRQIGE-----LSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17539902 270 PTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSVYHmADQLILLSqGHVAYAG 326
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEY-FDRVLLLN-RTVVASG 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
122-326 |
4.39e-25 |
|
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: 103.99 E-value: 4.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 122 IDGV---ARPGELTFIMGSSGAGKTTLLNILTGRnlknIETD-GDIMINGRNMISN--EMKKLSAYVQQDDVFIGTLTVR 195
Cdd:cd03266 21 VDGVsftVKPGEVTGLLGPNGAGKTTTLRMLAGL----LEPDaGFATVDGFDVVKEpaEARRRLGFVSDSTGLYDRLTAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 196 ETLRFAAKLRspsALGATELDSIVDELLVMMSLKKCENTKVGtmtekSLSRGERKRLAFACEILTDPPILFCDEPTSGLD 275
Cdd:cd03266 97 ENLEYFAGLY---GLKGDELTARLEELADRLGMEELLDRRVG-----GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17539902 276 SFMSHQVIKALRQLTIEGKTVICTIHQPStSVYHMADQLILLSQGHVAYAG 326
Cdd:cd03266 169 VMATRALREFIRQLRALGKCILFSTHIMQ-EVERLCDRVVVLHRGRVVYEG 218
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
118-322 |
7.78e-25 |
|
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: 103.46 E-value: 7.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 118 ILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnLKNIEtDGDIMINGRNMIS---NEMKKLSAYVQQDD-VFIGTlt 193
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMR--FYDPQ-KGQILIDGIDIRDisrKSLRSMIGVVLQDTfLFSGT-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 194 VRETLRFA---AK----LRSPSALGATELdsivdellvMMSLKKCENTKVGTmTEKSLSRGERKRLAFACEILTDPPILF 266
Cdd:cd03254 93 IMENIRLGrpnATdeevIEAAKEAGAHDF---------IMKLPNGYDTVLGE-NGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17539902 267 CDEPTSGLDSFMSHQVIKALRQLtIEGKTVICTIHQPSTSVYhmADQLILLSQGHV 322
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN--ADKILVLDDGKI 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
117-333 |
1.22e-24 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 103.03 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 117 EILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnLKNIeTDGDIMINGRNMISNEMKKL------SAYVQQDDVFIG 190
Cdd:cd03256 15 KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNG--LVEP-TSGSVLIDGTDINKLKGKALrqlrrqIGMIFQQFNLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 191 TLTVRETL---RFAAKLRSPSALGA-TELD-SIVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPIL 265
Cdd:cd03256 92 RLSVLENVlsgRLGRRSTWRSLFGLfPKEEkQRALAALERVGLLDKAYQRADQ-----LSGGQQQRVAIARALMQQPKLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17539902 266 FCDEPTSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQPSTSVYHmADQLILLSQGHVAYAGPAKQVDA 333
Cdd:cd03256 167 LADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREY-ADRIVGLKDGRIVFDGPPAELTD 234
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
115-326 |
2.08e-24 |
|
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: 101.50 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 115 RQEILKKIDGVARPGeLTFIMGSSGAGKTTLLNILTGRnlknIETD-GDIMINGRNMISN--EMKKLSAYVQQDDVFIGT 191
Cdd:cd03264 12 KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATL----TPPSsGTIRIDGQDVLKQpqKLRRRIGYLPQEFGVYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 192 LTVRETLRFAAKLRSPSAlgaTELDSIVDELLVMMSLKKCENTKVGtmtekSLSRGERKRLAFACEILTDPPILFCDEPT 271
Cdd:cd03264 87 FTVREFLDYIAWLKGIPS---KEVKARVDEVLELVNLGDRAKKKIG-----SLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17539902 272 SGLDSFMSHQVIKALRQLTiEGKTVICTIHQPStSVYHMADQLILLSQGHVAYAG 326
Cdd:cd03264 159 AGLDPEERIRFRNLLSELG-EDRIVILSTHIVE-DVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
109-326 |
2.09e-24 |
|
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: 101.52 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 109 LKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlknIE--TDGDIMINGRNMISNE--MKKLSAYVQQ 184
Cdd:cd03268 6 LTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILG-----LIkpDSGEITFDGKSYQKNIeaLRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 185 DdVFIGTLTVRETLRFAAKLRSPSalgatelDSIVDELLVMMSLKKCENTKVgtmteKSLSRGERKRLAFACEILTDPPI 264
Cdd:cd03268 81 P-GFYPNLTARENLRLLARLLGIR-------KKRIDEVLDVVGLKDSAKKKV-----KGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17539902 265 LFCDEPTSGLDSFMshqvIKALRQLTI----EGKTVICTIHQPStSVYHMADQLILLSQGHVAYAG 326
Cdd:cd03268 148 LILDEPTNGLDPDG----IKELRELILslrdQGITVLISSHLLS-EIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
128-326 |
2.38e-24 |
|
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: 101.60 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 128 PGELTFIMGSSGAGKTTLLNILTGrnLKNIeTDGDIMINGRNMISNEMK--------KLSAYVQQDDVFiGTLTVRETLR 199
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAG--LEKP-DGGTIVLNGTVLFDSRKKinlppqqrKIGLVFQQYALF-PHLNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 200 FAAKLRSPSalgatELDSIVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMS 279
Cdd:cd03297 98 FGLKRKRNR-----EDRISVDELLDLLGLDHLLNRYPAQ-----LSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17539902 280 HQVIKALRQL-TIEGKTVICTIHQPStSVYHMADQLILLSQGHVAYAG 326
Cdd:cd03297 168 LQLLPELKQIkKNLNIPVIFVTHDLS-EAEYLADRIVVMEDGRLQYIG 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
63-331 |
3.51e-24 |
|
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: 106.91 E-value: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 63 ELAHSSERFRKPKTLSVTNDTESARIPSQVKTNAKK--LVFQNIQAVVLKKKGVRQEILKKIDGVARPGELTFIMGSSGA 140
Cdd:COG1123 223 EDGPPEEILAAPQALAAVPRLGAARGRAAPAAAAAEplLEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGS 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 141 GKTTLLNILTGrnlknIE--TDGDIMINGRN---MISNEMKKLSAYVQ---QD--DVFIGTLTVRETLRFAAKLRSPsaL 210
Cdd:COG1123 303 GKSTLARLLLG-----LLrpTSGSILFDGKDltkLSRRSLRELRRRVQmvfQDpySSLNPRMTVGDIIAEPLRLHGL--L 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 211 GATELDSIVDELLVMMSLKKcentkvgTMTEK---SLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALR 287
Cdd:COG1123 376 SRAERRERVAELLERVGLPP-------DLADRyphELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLR 448
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 17539902 288 QLTIE-GKTVICTIHQPSTsVYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:COG1123 449 DLQRElGLTYLFISHDLAV-VRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
115-331 |
4.44e-24 |
|
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: 106.53 E-value: 4.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 115 RQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKNIETDGDIMINGRNMISNEMKKLS---AYVQQD-DVFIG 190
Cdd:COG1123 18 DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELSEALRGrriGMVFQDpMTQLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 191 TLTVRETLRFAAKLRSpsaLGATELDSIVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILFCDEP 270
Cdd:COG1123 98 PVTVGDQIAEALENLG---LSRAEARARVLELLEAVGLERRLDRYPHQ-----LSGGQRQRVAIAMALALDPDLLIADEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17539902 271 TSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQPSTsVYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:COG1123 170 TTALDVTTQAEILDLLRELQRErGTTVLLITHDLGV-VAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
101-322 |
5.52e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 100.90 E-value: 5.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 101 FQNiqavVLKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlknIE--TDGDIMINGRNMISNEMKKL 178
Cdd:COG2884 4 FEN----VSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG-----EErpTSGQVLVNGQDLSRLKRREI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 179 SAY------VQQDDVFIGTLTVRETLRFAakLRspsALGAT--ELDSIVDELLVMMSLKKCENTKVGTmteksLSRGERK 250
Cdd:COG2884 75 PYLrrrigvVFQDFRLLPDRTVYENVALP--LR---VTGKSrkEIRRRVREVLDLVGLSDKAKALPHE-----LSGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17539902 251 RLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTsVYHMADQLILLSQGHV 322
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLEL-VDRMPKRVLELEDGRL 215
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
119-331 |
1.33e-23 |
|
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: 100.20 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 119 LKKIDGVA---RPGELTFIMGSSGAGKTTLLNILTGRnLKniETDGDIMINGRNmISNemkkLSAYV----------QQD 185
Cdd:cd03219 13 LVALDDVSfsvRPGEIHGLIGPNGAGKTTLFNLISGF-LR--PTSGSVLFDGED-ITG----LPPHEiarlgigrtfQIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 186 DVFiGTLTVRETLRFAAKLRSPSALGAT-------ELDSIVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEI 258
Cdd:cd03219 85 RLF-PELTVLENVMVAAQARTGSGLLLArarreerEARERAEELLERVGLADLADRPAGE-----LSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539902 259 LTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPStSVYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMD-VVMSLADRVTVLDQGRVIAEGTPDEV 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
116-322 |
2.12e-23 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 98.73 E-value: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnLkNIETDGDIMINGRNMisNEMK-----KLSAYVQQDDVFIG 190
Cdd:COG4619 13 KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALAD--L-DPPTSGEIYLDGKPL--SAMPppewrRQVAYVPQEPALWG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 191 TlTVRETLRFAAKLRSPSALgatelDSIVDELLVMMSL------KKCENtkvgtmteksLSRGERKRLAFACEILTDPPI 264
Cdd:COG4619 88 G-TVRDNLPFPFQLRERKFD-----RERALELLERLGLppdildKPVER----------LSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17539902 265 LFCDEPTSGLDSFMSHQVIKALRQL-TIEGKTVICTIHQPsTSVYHMADQLILLSQGHV 322
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDP-EQIERVADRVLTLEAGRL 209
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
129-326 |
3.71e-22 |
|
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: 95.25 E-value: 3.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 129 GELTFIMGSSGAGKTTLLNILTGRNLKnieTDGDIMINGRNMISNEM--KKLSAYVQQDDVFiGTLTVRETLRFAaklRS 206
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETP---QSGRVLINGVDVTAAPPadRPVSMLFQENNLF-AHLTVEQNVGLG---LS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 207 PSaLGATELD-SIVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKA 285
Cdd:cd03298 97 PG-LKLTAEDrQAIEVALARVGLAGLEKRLPGE-----LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17539902 286 LRQLTIE-GKTVICTIHQPSTSVyHMADQLILLSQGHVAYAG 326
Cdd:cd03298 171 VLDLHAEtKMTVLMVTHQPEDAK-RLAQRVVFLDNGRIAAQG 211
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
115-317 |
3.73e-22 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 100.82 E-value: 3.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 115 RQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKnieTDGDIMINGRNMISNEMK---KLSAYV-QQDDVFIG 190
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDP---TEGSIAVNGVPLADADADswrDQIAWVpQHPFLFAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 191 TltVRETLRFAAKLRSPS----ALGATELDSIVDELLVMMslkkceNTKVGtmtEKS--LSRGERKRLAFACEILTDPPI 264
Cdd:TIGR02857 411 T--IAENIRLARPDASDAeireALERAGLDEFVAALPQGL------DTPIG---EGGagLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17539902 265 LFCDEPTSGLDSFMSHQVIKALRQLTiEGKTVICTIHQPSTSvyHMADQLILL 317
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALA--ALADRIVVL 529
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
129-321 |
4.16e-22 |
|
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: 93.79 E-value: 4.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 129 GELTFIMGSSGAGKTTLLNILTGRNLKnieTDGDIMINGRNM-----ISNEMKKLSAYVQQDDVFIGTLTVRETLRFAak 203
Cdd:cd03229 26 GEIVALLGPSGSGKSTLLRCIAGLEEP---DSGSILIDGEDLtdledELPPLRRRIGMVFQDFALFPHLTVLENIALG-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 204 lrspsalgateldsivdellvmmslkkcentkvgtmteksLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVI 283
Cdd:cd03229 101 ----------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVR 140
|
170 180 190
....*....|....*....|....*....|....*....
gi 17539902 284 KALRQLTIE-GKTVICTIHQPStSVYHMADQLILLSQGH 321
Cdd:cd03229 141 ALLKSLQAQlGITVVLVTHDLD-EAARLADRVVVLRDGK 178
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
104-322 |
4.50e-22 |
|
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: 94.90 E-value: 4.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 104 IQAVVLKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLniltgRNLKNIE--TDGDIMINGRNMI--SNEMKKLS 179
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLL-----RCINLLEepDSGTIIIDGLKLTddKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 180 AYV----QQDDVFiGTLTVRETLRFA---AKLRSPSALGATELdsivdELLvmmslkkcenTKVGtMTEK------SLSR 246
Cdd:cd03262 76 QKVgmvfQQFNLF-PHLTVLENITLApikVKGMSKAEAEERAL-----ELL----------EKVG-LADKadaypaQLSG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17539902 247 GERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTsVYHMADQLILLSQGHV 322
Cdd:cd03262 139 GQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGF-AREVADRVIFMDDGRI 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
99-326 |
7.03e-22 |
|
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: 94.99 E-value: 7.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 99 LVFQNiqaVVLKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILT-------GRnlknIETDG-DImingRNM 170
Cdd:cd03251 1 VEFKN---VTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPrfydvdsGR----ILIDGhDV----RDY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 171 ISNEMKKLSAYVQQDdVFIGTLTVRETLRFAAklrspsaLGATElDSIVDELL------VMMSLKKCENTKVGTMTEKsL 244
Cdd:cd03251 70 TLASLRRQIGLVSQD-VFLFNDTVAENIAYGR-------PGATR-EEVEEAARaanaheFIMELPEGYDTVIGERGVK-L 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 245 SRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTiEGKTVICTIHQPSTsVYHmADQLILLSQGHVAY 324
Cdd:cd03251 140 SGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLST-IEN-ADRIVVLEDGKIVE 216
|
..
gi 17539902 325 AG 326
Cdd:cd03251 217 RG 218
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
116-303 |
9.84e-22 |
|
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: 99.36 E-value: 9.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnlknIET-DGDIMINGRNMIS---NEMKKLSAYVQQDDVFIGT 191
Cdd:TIGR02868 348 PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL----LDPlQGEVTLDGVPVSSldqDEVRRRVSVCAQDAHLFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 192 lTVRETLRFAAKLRSPS----ALGATELDSIVDELLVMMslkkceNTKVGTMTeKSLSRGERKRLAFACEILTDPPILFC 267
Cdd:TIGR02868 424 -TVRENLRLARPDATDEelwaALERVGLADWLRALPDGL------DTVLGEGG-ARLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*.
gi 17539902 268 DEPTSGLDSFMSHQVIKALRQLTiEGKTVICTIHQP 303
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDLLAAL-SGRTVVLITHHL 530
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
117-333 |
3.37e-21 |
|
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: 93.12 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 117 EILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnLKNIeTDGDIMINGRNMI---SNEMKKLS-AYVQQD-DVFiGT 191
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISG--LLPP-RSGSIRFDGEDITglpPHRIARLGiGYVPEGrRIF-PS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 192 LTVRETLRFAAKLRSPSALGATELDSIVDELLVmmsLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILFCDEPT 271
Cdd:COG0410 93 LTVEENLLLGAYARRDRAEVRADLERVYELFPR---LKERRRQRAGT-----LSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17539902 272 SGLDSFMSHQVIKALRQLTIEGKTVICtIHQPSTSVYHMADQLILLSQGHVAYAGPAKQVDA 333
Cdd:COG0410 165 LGLAPLIVEEIFEIIRRLNREGVTILL-VEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
113-322 |
4.04e-21 |
|
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: 92.57 E-value: 4.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 113 GVRQEILKKIDGV---ARPGELTFIMGSSGAGKTTLLNILTGRNLKnieTDGDIMINGRNMI--SNEMKKL----SAYVQ 183
Cdd:cd03257 12 PTGGGSVKALDDVsfsIKKGETLGLVGESGSGKSTLARAILGLLKP---TSGSIIFDGKDLLklSRRLRKIrrkeIQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 184 QDDVF-------IGTLtVRETLRFAAKLRSPSALGAteldsIVDELLVMMSLKKcentKVGTMTEKSLSRGERKRLAFAC 256
Cdd:cd03257 89 QDPMSslnprmtIGEQ-IAEPLRIHGKLSKKEARKE-----AVLLLLVGVGLPE----EVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17539902 257 EILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQPSTsVYHMADQLILLSQGHV 322
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGV-VAKIADRVAVMYAGKI 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
107-323 |
7.89e-21 |
|
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: 92.17 E-value: 7.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 107 VVLKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLkniETDGDIMINGRNMISNEMKKLSAYVQ--- 183
Cdd:COG1124 9 VSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLER---PWSGEVTFDGRPVTRRRRKAFRRRVQmvf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 184 QDDvfIGTL----TVRETLRFAAKLrspsaLGATELDSIVDELLvmmslkkcenTKVGtMTEKSLSR-------GERKRL 252
Cdd:COG1124 86 QDP--YASLhprhTVDRILAEPLRI-----HGLPDREERIAELL----------EQVG-LPPSFLDRyphqlsgGQRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17539902 253 AFACEILTDPPILFCDEPTSGLDsfMSHQ-----VIKALRQltIEGKTVICTIHQPSTsVYHMADQLILLSQGHVA 323
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALD--VSVQaeilnLLKDLRE--ERGLTYLFVSHDLAV-VAHLCDRVAVMQNGRIV 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
112-323 |
8.27e-21 |
|
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: 91.38 E-value: 8.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 112 KGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlknIE--TDGDIMINGR--NMISNEMkklsAYVQQDDV 187
Cdd:cd03293 13 GGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAG-----LErpTSGEVLVDGEpvTGPGPDR----GYVFQQDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 188 FIGTLTVRETLRFAAKLRSpsaLGATELDSIVDELLVMMSLKKCENTkvgtmTEKSLSRGERKRLAFACEILTDPPILFC 267
Cdd:cd03293 84 LLPWLTVLDNVALGLELQG---VPKAEARERAEELLELVGLSGFENA-----YPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17539902 268 DEPTSGLDSF----MSHQVIKALRQltiEGKTVICTIHQPSTSVYhMADQLILLSQ--GHVA 323
Cdd:cd03293 156 DEPFSALDALtreqLQEELLDIWRE---TGKTVLLVTHDIDEAVF-LADRVVVLSArpGRIV 213
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
117-301 |
8.72e-21 |
|
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: 90.56 E-value: 8.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 117 EILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrNLKniETDGDIMINGRNMISN-----EMKKLSAYVQQD-DVFIG 190
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNG-LLR--PQSGAVLIDGEPLDYSrkgllERRQRVGLVFQDpDDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 191 TLTVRETLRFaaklrSPSALGAT--ELDSIVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILFCD 268
Cdd:TIGR01166 83 AADVDQDVAF-----GPLNLGLSeaEVERRVREALTAVGASGLRERPTHC-----LSGGEKKRVAIAGAVAMRPDVLLLD 152
|
170 180 190
....*....|....*....|....*....|...
gi 17539902 269 EPTSGLDSFMSHQVIKALRQLTIEGKTVICTIH 301
Cdd:TIGR01166 153 EPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
110-326 |
1.30e-20 |
|
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: 91.24 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 110 KKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlknI--ETDGDIMINGRNMISNE---MKKLSAYVQQ 184
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSG-----LlqPTSGEVRVAGLVPWKRRkkfLRRIGVVFGQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 185 DDVFIGTLTVRETLRFAAKLR--SPSALGATeldsiVDELLVMMSLKKCENTKVgtmteKSLSRGERKRLAFACEILTDP 262
Cdd:cd03267 103 KTQLWWDLPVIDSFYLLAAIYdlPPARFKKR-----LDELSELLDLEELLDTPV-----RQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539902 263 PILFCDEPTSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQpSTSVYHMADQLILLSQGHVAYAG 326
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHY-MKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
117-331 |
1.43e-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: 91.09 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 117 EILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRN--LKNIETDGDIMINGRNMISNEMKKLS-----AYV-QQDDVF 188
Cdd:cd03260 14 HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlIPGAPDEGEVLLDGKDIYDLDVDVLElrrrvGMVfQKPNPF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 189 igTLTVRETLRFAAKLRSpsALGATELDSIVDELLVMMSLKKCENTKVGTmteKSLSRGERKRLAFACEILTDPPILFCD 268
Cdd:cd03260 94 --PGSIYDNVAYGLRLHG--IKLKEELDERVEEALRKAALWDEVKDRLHA---LGLSGGQQQRLCLARALANEPEVLLLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539902 269 EPTSGLDSFMSHQVIKALRQLTIEGKTVICT--IHQpstsVYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:cd03260 167 EPTSALDPISTAKIEELIAELKKEYTIVIVThnMQQ----AARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
118-326 |
1.73e-20 |
|
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: 90.42 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 118 ILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLkniETDGDIMINGRNMiSNEMKKLSAYVQQDDVFIGTLTVRET 197
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIL---PDSGEVLFDGKPL-DIAARNRIGYLPEERGLYPKMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 198 LRFAAKLRspsALGATELDSIVDELLVMMSLKKCENTKVgtmteKSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSf 277
Cdd:cd03269 91 LVYLAQLK---GLKKEEARRRIDEWLERLELSEYANKRV-----EELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP- 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17539902 278 MSHQVIK-ALRQLTIEGKTVICTIHQPSTsVYHMADQLILLSQGHVAYAG 326
Cdd:cd03269 162 VNVELLKdVIRELARAGKTVILSTHQMEL-VEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
129-301 |
3.05e-20 |
|
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: 89.77 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 129 GELTFIMGSSGAGKTTLLNILTGRNLKnieTDGDIMINGRNmISNEMKKLSAY-------VQQDDVFIGTLTVRETLRFA 201
Cdd:cd03292 27 GEFVFLVGPSGAGKSTLLKLIYKEELP---TSGTIRVNGQD-VSDLRGRAIPYlrrkigvVFQDFRLLPDRNVYENVAFA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 202 AKLrspSALGATELDSIVDELLVMMSLKKcentKVGTMTEKsLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQ 281
Cdd:cd03292 103 LEV---TGVPPREIRKRVPAALELVGLSH----KHRALPAE-LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWE 174
|
170 180
....*....|....*....|
gi 17539902 282 VIKALRQLTIEGKTVICTIH 301
Cdd:cd03292 175 IMNLLKKINKAGTTVVVATH 194
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
120-329 |
6.07e-20 |
|
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: 90.91 E-value: 6.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 120 KKIDGV---ARPGELTFIMGSSGAGKTTLLNILTGRnLKniETDGDIMINGRNMISNEMK---KLSAYVQQDDVFIGtLT 193
Cdd:TIGR01188 7 KAVDGVnfkVREGEVFGFLGPNGAGKTTTIRMLTTL-LR--PTSGTARVAGYDVVREPRKvrrSIGIVPQYASVDED-LT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 194 VRETLRFAAKLRspsALGATELDSIVDELLVMMSLKKCENTKVGTMtekslSRGERKRLAFACEILTDPPILFCDEPTSG 273
Cdd:TIGR01188 83 GRENLEMMGRLY---GLPKDEAEERAEELLELFELGEAADRPVGTY-----SGGMRRRLDIAASLIHQPDVLFLDEPTTG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17539902 274 LDSFMSHQVIKALRQLTIEGKTVICTIHQpSTSVYHMADQLILLSQGHVAYAGPAK 329
Cdd:TIGR01188 155 LDPRTRRAIWDYIRALKEEGVTILLTTHY-MEEADKLCDRIAIIDHGRIIAEGTPE 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
119-331 |
6.99e-20 |
|
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: 89.71 E-value: 6.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 119 LKKIDGV---ARPGELTFIMGSSGAGKTTLLNILTGRnLKniETDGDIMINGRNmISNemkkLSAYV----------QQD 185
Cdd:COG0411 17 LVAVDDVsleVERGEIVGLIGPNGAGKTTLFNLITGF-YR--PTSGRILFDGRD-ITG----LPPHRiarlgiartfQNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 186 DVFiGTLTVRETLRFAAKLRSPSALGAT------------ELDSIVDELLVMMSLKKCENTKVGtmtekSLSRGERKRLA 253
Cdd:COG0411 89 RLF-PELTVLENVLVAAHARLGRGLLAAllrlprarreerEARERAEELLERVGLADRADEPAG-----NLSYGQQRRLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 254 FACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLT-IEGKTVICTIHqpstsvyHM------ADQLILLSQGHVAYAG 326
Cdd:COG0411 163 IARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEH-------DMdlvmglADRIVVLDFGRVIAEG 235
|
....*
gi 17539902 327 PAKQV 331
Cdd:COG0411 236 TPAEV 240
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
118-331 |
1.36e-19 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 88.60 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 118 ILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKnieTDG-DIMINGRNMIS---NEMKKLSAYVQQD--DVFIGT 191
Cdd:COG1119 18 ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPP---TYGnDVRLFGERRGGedvWELRKRIGLVSPAlqLRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 192 LTVRETLR--FAAKLRSPSALGATELDsIVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILFCDE 269
Cdd:COG1119 95 ETVLDVVLsgFFDSIGLYREPTDEQRE-RARELLELLGLAHLADRPFGT-----LSQGEQRRVLIARALVKDPELLILDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17539902 270 PTSGLDSFMSHQVIKALRQLTIEGKTVICTI-HQPS---TSVYHmadqLILLSQGHVAYAGPAKQV 331
Cdd:COG1119 169 PTAGLDLGARELLLALLDKLAAEGAPTLVLVtHHVEeipPGITH----VLLLKDGRVVAAGPKEEV 230
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
110-295 |
1.78e-19 |
|
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: 87.79 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 110 KKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnLKNiETDGDIMINGRN---MISNEMKKLS----AYV 182
Cdd:TIGR02211 12 QEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGG--LDN-PTSGEVLFNGQSlskLSSNERAKLRnkklGFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 183 QQDDVFIGTLTVRETLRFAAKLRSPSAlgaTELDSIVDELLVMMSLKKCENTKVGtmtekSLSRGERKRLAFACEILTDP 262
Cdd:TIGR02211 89 YQFHHLLPDFTALENVAMPLLIGKKSV---KEAKERAYEMLEKVGLEHRINHRPS-----ELSGGERQRVAIARALVNQP 160
|
170 180 190
....*....|....*....|....*....|...
gi 17539902 263 PILFCDEPTSGLDSFMSHQVIKALRQLTIEGKT 295
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNT 193
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
104-322 |
2.85e-19 |
|
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: 85.73 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 104 IQAVVLKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrNLKniETDGDIMINGRNMIS---NEMKKLSA 180
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILG-LLR--PTSGRVRLDGADISQwdpNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 181 YVQQDDvfigtltvretlrfaaklrspsalgateldsivdELLVmmslkkcentkvGTMTEKSLSRGERKRLAFACEILT 260
Cdd:cd03246 80 YLPQDD----------------------------------ELFS------------GSIAENILSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17539902 261 DPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTsvYHMADQLILLSQGHV 322
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPET--LASADRILVLEDGRV 173
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
101-331 |
3.11e-19 |
|
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: 87.25 E-value: 3.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 101 FQNIqAVVLKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILtgrNLKNIETDGDIMINGRNMISNEMKKLSA 180
Cdd:cd03258 4 LKNV-SKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI---NGLERPTSGSVLVDGTDLTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 181 YVQQddvfIG----------TLTVRETLRFAAKL-RSPSAlgatELDSIVDELLvmmslkkcenTKVGtMTEK------S 243
Cdd:cd03258 80 ARRR----IGmifqhfnllsSRTVFENVALPLEIaGVPKA----EIEERVLELL----------ELVG-LEDKadaypaQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 244 LSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQPSTsVYHMADQLILLSQGHV 322
Cdd:cd03258 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEV-VKRICDRVAVMEKGEV 219
|
....*....
gi 17539902 323 AYAGPAKQV 331
Cdd:cd03258 220 VEEGTVEEV 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
94-329 |
3.96e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 87.45 E-value: 3.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 94 TNAKKLVFQNIqAVVLKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlknIE--TDGDIMINGRnmi 171
Cdd:COG1116 3 AAAPALELRGV-SKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAG-----LEkpTSGEVLVDGK--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 172 snEMKKLS---AYVQQDDvfigTL----TVRETLRFAAKLRSpsaLGATELDSIVDELLVMMSLKKCENTKVGTmteksL 244
Cdd:COG1116 74 --PVTGPGpdrGVVFQEP----ALlpwlTVLDNVALGLELRG---VPKAERRERARELLELVGLAGFEDAYPHQ-----L 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 245 SRGERKRLAFACEILTDPPILFCDEPTSGLDSF----MSHQVIKALRQltiEGKTVICTIHQPSTSVYhMADQLILLSqg 320
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDALtrerLQDELLRLWQE---TGKTVLFVTHDVDEAVF-LADRVVVLS-- 213
|
....*....
gi 17539902 321 hvayAGPAK 329
Cdd:COG1116 214 ----ARPGR 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
109-333 |
6.21e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 86.73 E-value: 6.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 109 LKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLL---NIL----TGR-NLKNIETDGDIMINGRNMISNEMKKLSA 180
Cdd:PRK11264 9 LVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLrciNLLeqpeAGTiRVGDITIDTARSLSQQKGLIRQLRQHVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 181 YVQQ-----------DDVFIGTLTVRETLRFAAKLRSpsalgateldsivDELLVMMSLKKCENTkvgtmTEKSLSRGER 249
Cdd:PRK11264 89 FVFQnfnlfphrtvlENIIEGPVIVKGEPKEEATARA-------------RELLAKVGLAGKETS-----YPRRLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 250 KRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSvYHMADQLILLSQGHVAYAGPAK 329
Cdd:PRK11264 151 QRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFA-RDVADRAIFMDQGRIVEQGPAK 229
|
....
gi 17539902 330 QVDA 333
Cdd:PRK11264 230 ALFA 233
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
128-331 |
6.38e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.99 E-value: 6.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 128 PGELTFIMGSSGAGKTTLLNILTgRNLKniETDGDIMINGRNMISNEMKKLSAYV----QQDDVFIGtLTVRETLRFAak 203
Cdd:PRK11231 27 TGKITALIGPNGCGKSTLLKCFA-RLLT--PQSGTVFLGDKPISMLSSRQLARRLallpQHHLTPEG-ITVRELVAYG-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 204 lRSP--SALGATELDsivDELLVMMSLkkcENTKVGTMTEK---SLSRGERKRLAFACEILTDPPILFCDEPTSGLDsfM 278
Cdd:PRK11231 101 -RSPwlSLWGRLSAE---DNARVNQAM---EQTRINHLADRrltDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD--I 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17539902 279 SHQV--IKALRQLTIEGKTVICTIH---QPStsvyHMADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK11231 172 NHQVelMRLMRELNTQGKTVVTVLHdlnQAS----RYCDHLVVLANGHVMAQGTPEEV 225
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
122-337 |
1.09e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 87.09 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 122 IDGV---ARPGELTFIMGSSGAGKTTLLNILTGRnlknIETD-GDIMINGRNMisnemkklsayvQQDDV-FIGTL---- 192
Cdd:COG4152 17 VDDVsftVPKGEIFGLLGPNGAGKTTTIRIILGI----LAPDsGEVLWDGEPL------------DPEDRrRIGYLpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 193 ------TVRETLRFAAKLRSpsaLGATELDSIVDELLVMMSLKKCENTKVgtmteKSLSRGERKRLAFACEILTDPPILF 266
Cdd:COG4152 81 glypkmKVGEQLVYLARLKG---LSKAEAKRRADEWLERLGLGDRANKKV-----EELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17539902 267 CDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPStSVYHMADQLILLSQGHVAYAGPAKQVDAFFGR 337
Cdd:COG4152 153 LDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQME-LVEELCDRIVIINKGRKVLSGSVDEIRRQFGR 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
127-320 |
1.15e-18 |
|
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: 85.33 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 127 RPGELTFIMGSSGAGKTTLLNILTGRNlknIETDGDIMINGRNMISNEMKKLSA---YVQQDDV-FIGTLtvRETLRFAA 202
Cdd:cd03245 28 RAGEKVAIIGRVGSGKSTLLKLLAGLY---KPTSGSVLLDGTDIRQLDPADLRRnigYVPQDVTlFYGTL--RDNITLGA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 203 KLRSPSA-LGATELdSIVDELlvMMSLKKCENTKVGtmtEK--SLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMS 279
Cdd:cd03245 103 PLADDERiLRAAEL-AGVTDF--VNKHPNGLDLQIG---ERgrGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17539902 280 HQVIKALRQLtIEGKTVICTIHQPstSVYHMADQLILLSQG 320
Cdd:cd03245 177 ERLKERLRQL-LGDKTLIIITHRP--SLLDLVDRIIVMDSG 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
116-335 |
1.77e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 85.19 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnLKNIETdGDIMINGRNMISNE--MKKLSAYVQQDDVFiGTLT 193
Cdd:COG3840 12 GDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAG--FLPPDS-GRILWNGQDLTALPpaERPVSMLFQENNLF-PHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 194 VRET--LRFAAKLRspsaLGATELDSiVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILFCDEPT 271
Cdd:COG3840 88 VAQNigLGLRPGLK----LTAEQRAQ-VEQALERVGLAGLLDRLPGQ-----LSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539902 272 SGLDSFMSHQVIKALRQLTIE-GKTVICTIHQPStSVYHMADQLILLSQGHVAYAGPakqVDAFF 335
Cdd:COG3840 158 SALDPALRQEMLDLVDELCRErGLTVLMVTHDPE-DAARIADRVLLVADGRIAADGP---TAALL 218
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
122-331 |
2.62e-18 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 87.08 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 122 IDGVARPGELTFIMGSSGAGKTTLLNILTGrnlknIET--DGDIMINGRNMISNEmKKLS--------AYVQQDDVFIGT 191
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAG-----LERpdSGRIRLGGEVLQDSA-RGIFlpphrrriGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 192 LTVRETLRFAAKlRSPSALGATELDSIVD-----ELLvmmslkkceNTKVGTmteksLSRGERKRLAFACEILTDPPILF 266
Cdd:COG4148 92 LSVRGNLLYGRK-RAPRAERRISFDEVVEllgigHLL---------DRRPAT-----LSGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17539902 267 CDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTI-HQPsTSVYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:COG4148 157 MDEPLAALDLARKAEILPYLERLRDELDIPILYVsHSL-DEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
104-301 |
3.34e-18 |
|
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: 83.96 E-value: 3.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 104 IQAVVLKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnLKniETDGDIMINGRNMI--SNEMKKLSAY 181
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTL-LK--PTSGRATVAGHDVVrePREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 182 VQQDDVFIGTLTVRETLRFAAKLrspSALGATELDSIVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTD 261
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIHARL---YGVPGAERRERIDELLDFVGLLEAADRLVKT-----YSGGMRRRLEIARSLVHR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17539902 262 PPILFCDEPTSGLDSFMSHQVIKALRQLTIE-GKTVICTIH 301
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTH 190
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
129-303 |
4.12e-18 |
|
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: 83.31 E-value: 4.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 129 GELTFIMGSSGAGKTTLLNILTGRNLKnieTDGDIMINGRNM--ISNEMKKLSAYVQQDDVFIGTLTVRETLRFAAKLRS 206
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPP---LAGRVLLNGGPLdfQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHADHS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 207 psalgatelDSIVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKAL 286
Cdd:cd03231 103 ---------DEQVEEALARVGLNGFEDRPVAQ-----LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
170
....*....|....*..
gi 17539902 287 RQLTIEGKTVICTIHQP 303
Cdd:cd03231 169 AGHCARGGMVVLTTHQD 185
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
107-326 |
4.51e-18 |
|
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: 84.07 E-value: 4.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 107 VVLKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNlknIETDGDIMINGRNMI---SNEMKKLSAYVQ 183
Cdd:cd03252 6 VRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFY---VPENGRVLVDGHDLAladPAWLRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 184 QDDVFIGTlTVRETLRFAAKlrSPSALGATELDSIVDELLVMMSLKKCENTKVGtmtEK--SLSRGERKRLAFACEILTD 261
Cdd:cd03252 83 QENVLFNR-SIRDNIALADP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVG---EQgaGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539902 262 PPILFCDEPTSGLDSFMSHQVIKALRQLTiEGKTVICTIHQPSTsvYHMADQLILLSQGHVAYAG 326
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLST--VKNADRIIVMEKGRIVEQG 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
116-337 |
4.72e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.82 E-value: 4.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlkNIETD-GDIMINGRNMISNEMKKLS---AYVQQDDVFIGT 191
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAING----TLTPTaGTVLVAGDDVEALSARAASrrvASVPQDTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 192 LTVRETLRFAaklRSPSaLGATELDSIVDELLVMMSLKKCENTKVGTMTEKSLSRGERKRLAFACEILTDPPILFCDEPT 271
Cdd:PRK09536 92 FDVRQVVEMG---RTPH-RSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539902 272 SGLDsfMSHQV--IKALRQLTIEGKTVICTIHQPSTSVYHmADQLILLSQGHVAYAGPAKQV-------DAFFGR 337
Cdd:PRK09536 168 ASLD--INHQVrtLELVRRLVDDGKTAVAAIHDLDLAARY-CDELVLLADGRVRAAGPPADVltadtlrAAFDAR 239
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
116-326 |
5.47e-18 |
|
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: 83.74 E-value: 5.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNILtgrnlkniE-----TDGDIMINGRNMISNEMKKLS---AYVQQDDV 187
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL--------ErfydpTSGEILLDGVDIRDLNLRWLRsqiGLVSQEPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 188 FIGTlTVRETLRFAAKLRSPS----ALGATELDSIVdellvmMSLKKCENTKVGTMTeKSLSRGERKRLAFACEILTDPP 263
Cdd:cd03249 88 LFDG-TIAENIRYGKPDATDEeveeAAKKANIHDFI------MSLPDGYDTLVGERG-SQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539902 264 ILFCDEPTSGLDSFMSHQVIKALRQLtIEGKTVICTIHQPSTsVYHmADQLILLSQGHVAYAG 326
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRA-MKGRTTIVIAHRLST-IRN-ADLIAVLQNGQVVEQG 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
109-331 |
6.97e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 83.87 E-value: 6.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 109 LKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILtgrNLKNIETDGDIMINGRN--MISNEMKKLSAYvqqDD 186
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI---NFLEKPSEGSIVVNGQTinLVRDKDGQLKVA---DK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 187 VFIGTLTVRETLRFAA-KLRSpsalGATELDSIVDELLVMMSLKKCEN--------TKVGtMTEKS-------LSRGERK 250
Cdd:PRK10619 85 NQLRLLRTRLTMVFQHfNLWS----HMTVLENVMEAPIQVLGLSKQEAreravkylAKVG-IDERAqgkypvhLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 251 RLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSvYHMADQLILLSQGHVAYAGPAKQ 330
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFA-RHVSSHVIFLHQGKIEEEGAPEQ 238
|
.
gi 17539902 331 V 331
Cdd:PRK10619 239 L 239
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
127-331 |
8.10e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 85.53 E-value: 8.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 127 RPGELTFIMGSSGAGKTTLLNILTGrnlknIE--TDGDIMINGRNMISnemkkLSAY------VQQDDVFIGTLTVRETL 198
Cdd:COG3842 29 EPGEFVALLGPSGCGKTTLLRMIAG-----FEtpDSGRILLDGRDVTG-----LPPEkrnvgmVFQDYALFPHLTVAENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 199 RFAAKLRspsALGATELDSIVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILFCDEPTSGLDSF- 277
Cdd:COG3842 99 AFGLRMR---GVPKAEIRARVAELLELVGLEGLADRYPHQ-----LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKl 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17539902 278 ---MSHQVIKALRQLtieGKTVICtihqpstsVYH-------MADQLILLSQGHVAYAGPAKQV 331
Cdd:COG3842 171 reeMREELRRLQREL---GITFIY--------VTHdqeealaLADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
127-331 |
1.46e-17 |
|
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: 82.39 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 127 RPGELTFIMGSSGAGKTTLLNILTGrnlknIE--TDGDIMINGRNMISNEMKKLS-AYVQQDDVFIGTLTVRETLRFAAK 203
Cdd:cd03296 26 PSGELVALLGPSGSGKTTLLRLIAG-----LErpDSGTILFGGEDATDVPVQERNvGFVFQHYALFRHMTVFDNVAFGLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 204 LR-SPSALGATELDSIVDELLVMMSLKKCENTkvgtmTEKSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQV 282
Cdd:cd03296 101 VKpRSERPPEAEIRAKVHELLKLVQLDWLADR-----YPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKEL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17539902 283 IKALRQLTIEgktvictIHQPSTSVYH-------MADQLILLSQGHVAYAGPAKQV 331
Cdd:cd03296 176 RRWLRRLHDE-------LHVTTVFVTHdqeealeVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
99-326 |
2.02e-17 |
|
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: 80.43 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 99 LVFQNIQavvLKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrNLKniETDGDIMINGRNmISNEMKKL 178
Cdd:cd03247 1 LSINNVS---FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG-DLK--PQQGEITLDGVP-VSDLEKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 179 SAYvqqddvfIGTLTVRETLrFAAKLRspsalgateldsivdellvmmslkkcENtkVGtmteKSLSRGERKRLAFACEI 258
Cdd:cd03247 74 SSL-------ISVLNQRPYL-FDTTLR--------------------------NN--LG----RRFSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17539902 259 LTDPPILFCDEPTSGLDSFMSHQVIKALRQLTiEGKTVICTIHQpSTSVYHMaDQLILLSQGHVAYAG 326
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVL-KDKTLIWITHH-LTGIEHM-DKILFLENGKIIMQG 178
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
122-331 |
2.75e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.81 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 122 IDGVARPGELTFIMGSSGAGKTTLLNILTGRnlknIETDGDIMINGRNMISNEMKKLS---AYV--QQDDVFIgtLTVRE 196
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL----LPGQGEILLNGRPLSDWSAAELArhrAYLsqQQSPPFA--MPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 197 TLRfaakLRSPSALGATELDSIVDELLVMMSLKKcentKVGTMTEKsLSRGE--RKRLAFAC-----EILTDPPILFCDE 269
Cdd:COG4138 89 YLA----LHQPAGASSEAVEQLLAQLAEALGLED----KLSRPLTQ-LSGGEwqRVRLAAVLlqvwpTINPEGQLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17539902 270 PTSGLDsfMSHQVI--KALRQLTIEGKTVICTIHQPSTSVYHmADQLILLSQGHVAYAGPAKQV 331
Cdd:COG4138 160 PMNSLD--VAQQAAldRLLRELCQQGITVVMSSHDLNHTLRH-ADRVWLLKQGKLVASGETAEV 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
110-331 |
3.04e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 81.67 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 110 KKKGVRQEILKKIDGVARPGElTF-IMGSSGAGKTTLLNILTGrnlknIE--TDGDIMINGR--NMISnemkkLSAyvqq 184
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGE-SVgIIGRNGAGKSTLLKLIAG-----ILepTSGRVEVNGRvsALLE-----LGA---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 185 ddVFIGTLTVRETLRFAAklrspSALGAT--ELDSIVDELLVMMSLKKCENTKVgtmteKSLSRGERKRLAFACEILTDP 262
Cdd:COG1134 98 --GFHPELTGRENIYLNG-----RLLGLSrkEIDEKFDEIVEFAELGDFIDQPV-----KTYSSGMRARLAFAVATAVDP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17539902 263 PILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTsVYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:COG1134 166 DILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGA-VRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
117-303 |
3.78e-17 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 80.48 E-value: 3.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 117 EILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnlkNIETDGDIMINGR--NMISNEMKKLSAYVQQDDVFIGTLTV 194
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGL---LRPDSGEVRWNGTplAEQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 195 RETLRFAAKLrspsaLGATELDsiVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILFCDEPTSGL 274
Cdd:TIGR01189 91 LENLHFWAAI-----HGGAQRT--IEDALAAVGLTGFEDLPAAQ-----LSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180
....*....|....*....|....*....
gi 17539902 275 DSFMSHQVIKALRQLTIEGKTVICTIHQP 303
Cdd:TIGR01189 159 DKAGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
101-331 |
4.80e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 80.91 E-value: 4.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 101 FQNiqavVLKKKGVRQeILKKIDGVARPGELTFIMGSSGAGKTTLLniltgRNLKNIE--TDGDIM-----INGRNMISN 173
Cdd:PRK09493 4 FKN----VSKHFGPTQ-VLHNIDLNIDQGEVVVIIGPSGSGKSTLL-----RCINKLEeiTSGDLIvdglkVNDPKVDER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 174 EMKKLSAYV-QQDDVFiGTLTVRETLRFAA-KLRSPSALGATELDSivdELLvmmslkkcenTKVGtMTEKS------LS 245
Cdd:PRK09493 74 LIRQEAGMVfQQFYLF-PHLTALENVMFGPlRVRGASKEEAEKQAR---ELL----------AKVG-LAERAhhypseLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 246 RGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSvYHMADQLILLSQGHVAYA 325
Cdd:PRK09493 139 GGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFA-EKVASRLIFIDKGRIAED 217
|
....*.
gi 17539902 326 GPAKQV 331
Cdd:PRK09493 218 GDPQVL 223
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
108-331 |
1.44e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 79.74 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 108 VLKKKGvRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILtGRNLKniETDGDIMINGRNMI---SNEMKKLSAYVQQ 184
Cdd:COG4604 7 VSKRYG-GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMI-SRLLP--PDSGEVLVDGLDVAttpSRELAKRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 185 DDVFIGTLTVRETLRFAaklRSPSALGA-TELD-SIVDELLVMMSLkkcentkvGTMTEK---SLSRGERKRlAF-ACEI 258
Cdd:COG4604 83 ENHINSRLTVRELVAFG---RFPYSKGRlTAEDrEIIDEAIAYLDL--------EDLADRyldELSGGQRQR-AFiAMVL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17539902 259 LTDPPILFCDEPTSGLDsfMSH--QVIKALRQLTIE-GKTVICTIHQPS-TSVYhmADQLILLSQGHVAYAGPAKQV 331
Cdd:COG4604 151 AQDTDYVLLDEPLNNLD--MKHsvQMMKLLRRLADElGKTVVIVLHDINfASCY--ADHIVAMKDGRVVAQGTPEEI 223
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
115-326 |
1.46e-16 |
|
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: 83.33 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 115 RQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILtgrnLKNIE-TDGDIMINGRNMISNEMKKLSAY---VQQDDVfig 190
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLL----FRFYDvTSGRILIDGQDIRDVTQASLRAAigiVPQDTV--- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 191 tL---TVRETLRFAAklrspsaLGATE-----------LDSIVdellvmMSLKKCENTKVGtmtEK--SLSRGERKRLAF 254
Cdd:COG5265 443 -LfndTIAYNIAYGR-------PDASEeeveaaaraaqIHDFI------ESLPDGYDTRVG---ERglKLSGGEKQRVAI 505
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17539902 255 ACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTiEGKTVICTIHQPSTSVYhmADQLILLSQGHVAYAG 326
Cdd:COG5265 506 ARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAHRLSTIVD--ADEILVLEAGRIVERG 574
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
110-326 |
1.99e-16 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 78.73 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 110 KKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlknIE--TDGDIMINGRnmisnemkkLSAYVQQDDV 187
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAG-----IYppDSGTVTVRGR---------VSSLLGLGGG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 188 FIGTLTVRETLRFAAKLrspsaLGAT--ELDSIVDELLVMMSLKKCENTKVgtmteKSLSRGERKRLAFACEILTDPPIL 265
Cdd:cd03220 95 FNPELTGRENIYLNGRL-----LGLSrkEIDEKIDEIIEFSELGDFIDLPV-----KTYSSGMKARLAFAIATALEPDIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17539902 266 FCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPStSVYHMADQLILLSQGHVAYAG 326
Cdd:cd03220 165 LIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPS-SIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
109-331 |
2.16e-16 |
|
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: 79.12 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 109 LKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlknIE--TDGDIMINGRNMISNEMKKLS----AYV 182
Cdd:cd03218 6 LSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVG-----LVkpDSGKILLDGQDITKLPMHKRArlgiGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 183 QQD-DVFIGtLTVRETLRFAAKLRSPSAlgaTELDSIVDELLVMMSLKKCENTKVGtmtekSLSRGERKRLAFACEILTD 261
Cdd:cd03218 81 PQEaSIFRK-LTVEENILAVLEIRGLSK---KEREEKLEELLEEFHITHLRKSKAS-----SLSGGERRRVEIARALATN 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17539902 262 PPILFCDEPTSGLDSfMSHQVIKAL-RQLTIEGKTVICTIHQPSTSVyHMADQLILLSQGHVAYAGPAKQV 331
Cdd:cd03218 152 PKFLLLDEPFAGVDP-IAVQDIQKIiKILKDRGIGVLITDHNVRETL-SITDRAYIIYEGKVLAEGTPEEI 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
116-322 |
2.23e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.95 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTgRNLKniETDGDIMINGRNmisnemkkLSAYVQQD---------- 185
Cdd:PRK11160 353 QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT-RAWD--PQQGEILLNGQP--------IADYSEAAlrqaisvvsq 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 186 --DVFIGTLtvRETLRFAAKLRSPSALGA----TELDSIVDEllvmmslKKCENTKVGtmtE--KSLSRGERKRLAFACE 257
Cdd:PRK11160 422 rvHLFSATL--RDNLLLAAPNASDEALIEvlqqVGLEKLLED-------DKGLNAWLG---EggRQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539902 258 ILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTiEGKTVICTIHQpSTSVYHMaDQLILLSQGHV 322
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHR-LTGLEQF-DRICVMDNGQI 551
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
59-336 |
4.09e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 80.26 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 59 QVEKELAHSSERFRKPKTLSVTNDTESARIPSQVKtnakklvfqNIQAVVLKKKGVRQEILKK--IDGVA---RPGELTF 133
Cdd:PRK13536 1 LLTRAVAEEAPRRLELSPIERKHQGISEAKASIPG---------SMSTVAIDLAGVSKSYGDKavVNGLSftvASGECFG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 134 IMGSSGAGKTTLLNILTGRNLKNIetdGDIMINGRNMISNE--MKKLSAYVQQDDVFIGTLTVRETLR-FAAKLRspsaL 210
Cdd:PRK13536 72 LLGPNGAGKSTIARMILGMTSPDA---GKITVLGVPVPARArlARARIGVVPQFDNLDLEFTVRENLLvFGRYFG----M 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 211 GATELDSIVDELLVMMSLKKCENTKVGtmtekSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLT 290
Cdd:PRK13536 145 STREIEAVIPSLLEFARLESKADARVS-----DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLL 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 17539902 291 IEGKTVICTIHQPSTSvYHMADQLILLSQGH-VAYAGPAKQVDAFFG 336
Cdd:PRK13536 220 ARGKTILLTTHFMEEA-ERLCDRLCVLEAGRkIAEGRPHALIDEHIG 265
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
128-327 |
7.27e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 79.36 E-value: 7.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 128 PGELTFIMGSSGAGKTTLLNILTGrnlknI--ETDGDIMINGRNMISNEMKklsaYVQQddvfIGT-----------LTV 194
Cdd:COG4586 47 PGEIVGFIGPNGAGKSTTIKMLTG-----IlvPTSGEVRVLGYVPFKRRKE----FARR----IGVvfgqrsqlwwdLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 195 RETLRFAAKLRSpsaLGATELDSIVDELLVMMSLKKCENTKVgtmteKSLSRGERKRlafaCEI----LTDPPILFCDEP 270
Cdd:COG4586 114 IDSFRLLKAIYR---IPDAEYKKRLDELVELLDLGELLDTPV-----RQLSLGQRMR----CELaaalLHRPKILFLDEP 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17539902 271 TSGLDSFMSHQVIKALRQLTIE-GKTVICTIHqpstsvyHMAD------QLILLSQGHVAYAGP 327
Cdd:COG4586 182 TIGLDVVSKEAIREFLKEYNRErGTTILLTSH-------DMDDiealcdRVIVIDHGRIIYDGS 238
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
117-331 |
9.65e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 79.35 E-value: 9.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 117 EILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnLKNIeTDGDIMINGRNMisNEM--KKLS-AYVQQDDVFIGTLT 193
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG--LEDP-TSGEILIGGRDV--TDLppKDRNiAMVFQSYALYPHMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 194 VRETLRFAAKLRSPSalgATELDSIVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILFCDEPTSG 273
Cdd:COG3839 92 VYENIAFPLKLRKVP---KAEIDRRVREAAELLGLEDLLDRKPKQ-----LSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17539902 274 LDSFMSHQVIKALRQLTIEGKTvictihqpsTSVY--H-------MADQLILLSQGHVAYAGPAKQV 331
Cdd:COG3839 164 LDAKLRVEMRAEIKRLHRRLGT---------TTIYvtHdqveamtLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
129-322 |
9.87e-16 |
|
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: 76.52 E-value: 9.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 129 GELTFIMGSSGAGKTTLLNILTGrnLKNIeTDGDIMINGRNMISNEMKKLS-AYVQQDDVFIGTLTVRETLRFAAKLRSp 207
Cdd:cd03301 26 GEFVVLLGPSGCGKTTTLRMIAG--LEEP-TSGRIYIGGRDVTDLPPKDRDiAMVFQNYALYPHMTVYDNIAFGLKLRK- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 208 saLGATELDSIVDELLVMMSLKKCENTKVgtmteKSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALR 287
Cdd:cd03301 102 --VPKDEIDERVREVAELLQIEHLLDRKP-----KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELK 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 17539902 288 QLTIE-GKTVICTIHQpSTSVYHMADQLILLSQGHV 322
Cdd:cd03301 175 RLQQRlGTTTIYVTHD-QVEAMTMADRIAVMNDGQI 209
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
127-349 |
1.53e-15 |
|
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: 81.21 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 127 RPGELTFIMGSSGAGKTTLLNILTGrnlKNIETDGDIMINGRNMISN--EMKKLSAYVQQDDVFIGTLTVRETLRFAAKL 204
Cdd:TIGR01257 1963 RPGECFGLLGVNGAGKTTTFKMLTG---DTTVTSGDATVAGKSILTNisDVHQNMGYCPQFDAIDDLLTGREHLYLYARL 2039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 205 RspsALGATELDSIVDELLVMMSLKKCENTKVGTMtekslSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIK 284
Cdd:TIGR01257 2040 R---GVPAEEIEKVANWSIQSLGLSLYADRLAGTY-----SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWN 2111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539902 285 ALRQLTIEGKTVICTIHQpSTSVYHMADQLILLSQGHVAYAGPAKQVDAFFGRcGYPIPKFVSSP 349
Cdd:TIGR01257 2112 TIVSIIREGRAVVLTSHS-MEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGD-GYIVTMKIKSP 2174
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
117-304 |
1.55e-15 |
|
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: 76.32 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 117 EILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlknIE--TDGDIMINGRNmisnemkkLSA-------------- 180
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAG-----LDrpTSGTVRLAGQD--------LFAldedararlrarhv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 181 -YVQQDDVFIGTLTVRETLRFAAKLRspsalGATELDSIVDELLvmmslkkcenTKVG-----TMTEKSLSRGERKRLAF 254
Cdd:COG4181 93 gFVFQSFQLLPTLTALENVMLPLELA-----GRRDARARARALL----------ERVGlghrlDHYPAQLSGGEQQRVAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17539902 255 ACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQPS 304
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPA 208
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
118-322 |
2.03e-15 |
|
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: 76.12 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 118 ILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlknIET--DGDIMINGRNMIsnemkKLSAY------VQQDDVFI 189
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAG-----FETptSGEILLDGKDIT-----NLPPHkrpvntVFQNYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 190 GTLTVRETLRFAAKLRSpsaLGATELDSIVDELLVMMSLKKCENTKVgtmteKSLSRGERKRLAFACEILTDPPILFCDE 269
Cdd:cd03300 85 PHLTVFENIAFGLRLKK---LPKAEIKERVAEALDLVQLEGYANRKP-----SQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17539902 270 PTSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQPSTSVyHMADQLILLSQGHV 322
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEAL-TMSDRIAVMNKGKI 209
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
115-288 |
2.33e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 75.60 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 115 RQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKNIETDGDIMINGR--NMISNEMKKLsAYVQQDDVFIGTL 192
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSASGEVLLNGRrlTALPAEQRRI-GILFQDDLLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 193 TVRETLRFAAklrsPSALGATELDSIVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILFCDEPTS 272
Cdd:COG4136 92 SVGENLAFAL----PPTIGRAQRRARVEQALEEAGLAGFADRDPAT-----LSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170
....*....|....*.
gi 17539902 273 GLDsfmshqviKALRQ 288
Cdd:COG4136 163 KLD--------AALRA 170
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
126-337 |
2.98e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 79.23 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 126 ARPGELTFIMGSSGAGKTTLLNIL-------TGRnlknIETDGdimINGRNMISNEMKKLSAYVQQDDVFIGTlTVRETL 198
Cdd:PRK13657 358 AKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGR----ILIDG---TDIRTVTRASLRRNIAVVFQDAGLFNR-SIEDNI 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 199 RfaakLRSPSA-----LGATELDSIVDellVMMSLKKCENTKVGtmtEK--SLSRGERKRLAFACEILTDPPILFCDEPT 271
Cdd:PRK13657 430 R----VGRPDAtdeemRAAAERAQAHD---FIERKPDGYDTVVG---ERgrQLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17539902 272 SGLDSFMSHQVIKALRQLTiEGKTVICTIHQPSTsVYHmADQLILLSQGHVAYAGPAKQVDAFFGR 337
Cdd:PRK13657 500 SALDVETEAKVKAALDELM-KGRTTFIIAHRLST-VRN-ADRILVFDNGRVVESGSFDELVARGGR 562
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
117-276 |
3.30e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.91 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 117 EILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnLKNIETdGDIMINGRNMISNEMKKLSAYVQQDDVFIGTLTVRE 196
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAG--LLPPAA-GTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 197 TLRFAAKLrspsaLGATELDsiVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILFCDEPTSGLDS 276
Cdd:PRK13539 93 NLEFWAAF-----LGGEELD--IAAALEAVGLAPLAHLPFGY-----LSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
118-322 |
4.01e-15 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 75.20 E-value: 4.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 118 ILKKIDGVARPGELTFIMGSSGAGKTTLLNILtgRNLKNIeTDGDIMINGRNMISNEMK----KLSAYVQQDDVFIGTlt 193
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALL--ENFYQP-QGGQVLLDGKPISQYEHKylhsKVSLVGQEPVLFARS-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 194 VRETLRFAakLRSPSALGATELDSIVDELLVMMSLKKCENTKVGtmtEKS--LSRGERKRLAFACEILTDPPILFCDEPT 271
Cdd:cd03248 104 LQDNIAYG--LQSCSFECVKEAAQKAHAHSFISELASGYDTEVG---EKGsqLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17539902 272 SGLDSFMSHQVIKALRQlTIEGKTVICTIHQPSTsVYHmADQLILLSQGHV 322
Cdd:cd03248 179 SALDAESEQQVQQALYD-WPERRTVLVIAHRLST-VER-ADQILVLDGGRI 226
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
118-350 |
4.10e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 76.02 E-value: 4.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 118 ILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKNIETD-----GDIMINGRNMI---SNEMKKLSAYVQQDDVFI 189
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRgarvtGDVTLNGEPLAaidAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 190 GTLTVRETLRFAaklRSPSALGATELdSIVDELLVMMSLKKCENTKVGTMTEKSLSRGERKRLAFA---------CEILT 260
Cdd:PRK13547 96 FAFSAREIVLLG---RYPHARRAGAL-THRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFArvlaqlwppHDAAQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 261 DPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKT-VICTIHQPSTSVYHmADQLILLSQGHVAYAGPAKQV--DAFFGR 337
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARH-ADRIAMLADGAIVAHGAPADVltPAHIAR 250
|
250
....*....|....
gi 17539902 338 C-GYPIpKFVSSPD 350
Cdd:PRK13547 251 CyGFAV-RLVDAGD 263
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
127-301 |
1.10e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 75.23 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 127 RPGELTFIMGSSGAGKTTLLNILTGRNLKNIetdGDIMINGRNMISN--EMKKLSAYVQQDDVFIGTLTVRETLRFAAKL 204
Cdd:PRK13537 31 QRGECFGLLGPNGAGKTTTLRMLLGLTHPDA---GSISLCGEPVPSRarHARQRVGVVPQFDNLDPDFTVRENLLVFGRY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 205 RSPSALGATELdsiVDELLVMMSLKKCENTKVGtmtekSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIK 284
Cdd:PRK13537 108 FGLSAAAARAL---VPPLLEFAKLENKADAKVG-----ELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWE 179
|
170
....*....|....*..
gi 17539902 285 ALRQLTIEGKTVICTIH 301
Cdd:PRK13537 180 RLRSLLARGKTILLTTH 196
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
99-328 |
2.34e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 73.18 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 99 LVFQNIQAVVLKKkgvrqEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKNIeTDGDIMINGRNMisNEM--- 175
Cdd:COG0396 1 LEIKNLHVSVEGK-----EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEV-TSGSILLDGEDI--LELspd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 176 ---KKLSAYVQQDDVFIGTLTVRETLRFAAKLRSPSALGATELDSIVDELLVMMSLKKcentkvgTMTEKSL----SRGE 248
Cdd:COG0396 73 eraRAGIFLAFQYPVEIPGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDE-------DFLDRYVnegfSGGE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 249 RKRLafacEILT----DPPILFCDEPTSGLDsfmshqvIKALRQLtIEGktvICTIHQPSTSV-----------YHMADQ 313
Cdd:COG0396 146 KKRN----EILQmlllEPKLAILDETDSGLD-------IDALRIV-AEG---VNKLRSPDRGIliithyqrildYIKPDF 210
|
250
....*....|....*
gi 17539902 314 LILLSQGHVAYAGPA 328
Cdd:COG0396 211 VHVLVDGRIVKSGGK 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
128-331 |
2.39e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 73.67 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 128 PGELTFIMGSSGAGKTTLLNILtGRNLKniETDGDIMINGRNMISNEMKKLS---AYVQQDDVFIGTLTVREtlrFAAKL 204
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLKML-GRHQP--PSEGEILLDAQPLESWSSKAFArkvAYLPQQLPAAEGMTVRE---LVAIG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 205 RSP--SALG--ATELDSIVDELLVMMSLKKCENTKVgtmteKSLSRGERKRLAFACEILTDPPILFCDEPTSGLDsfMSH 280
Cdd:PRK10575 110 RYPwhGALGrfGAADREKVEEAISLVGLKPLAHRLV-----DSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD--IAH 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17539902 281 QV-----IKALRQLtiEGKTVICTIHQPSTSVYHmADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK10575 183 QVdvlalVHRLSQE--RGLTVIAVLHDINMAARY-CDYLVALRGGEMIAQGTPAEL 235
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
117-331 |
4.83e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 72.80 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 117 EILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnLKniETDGDIMINGRNM------ISNEMKKLSAYVQQDDVFIG 190
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGI-LK--PTSGEVLIKGEPIkydkksLLEVRKTVGIVFQNPDDQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 191 TLTVRETLRFAaklrsPSALGAT--ELDSIVDELLVMMSLKKCENTkvgtmTEKSLSRGERKRLAFACEILTDPPILFCD 268
Cdd:PRK13639 93 APTVEEDVAFG-----PLNLGLSkeEVEKRVKEALKAVGMEGFENK-----PPHHLSGGQKKRVAIAGILAMKPEIIVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17539902 269 EPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPS-TSVYhmADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK13639 163 EPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDlVPVY--ADKVYVMSDGKIIKEGTPKEV 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
116-331 |
5.01e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 74.21 E-value: 5.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlknIE--TDGDIMINGRNM--ISNEMKKLSAYVQQDDVFiGT 191
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAG-----FEtpDSGRIMLDGQDIthVPAENRHVNTVFQSYALF-PH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 192 LTVRETLRFAAKL-RSPSAlgatELDSIVDELLVMMSLKKCENTKVgtmteKSLSRGERKRLAFACEILTDPPILFCDEP 270
Cdd:PRK09452 101 MTVFENVAFGLRMqKTPAA----EITPRVMEALRMVQLEEFAQRKP-----HQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539902 271 TSGLDSFMSHQV---IKAL-RQLTIegkTVICTIHQPSTSVyHMADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK09452 172 LSALDYKLRKQMqneLKALqRKLGI---TFVFVTHDQEEAL-TMSDRIVVMRDGRIEQDGTPREI 232
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
118-330 |
7.37e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 72.04 E-value: 7.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 118 ILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlkNIETD-GDIMINGRNmISnemkKLSAY--------VQQDDVf 188
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAG----SLPPDsGSILIDGKD-VT----KLPEYkrakyigrVFQDPM- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 189 IGT---LTVRETLRFAAK------LRspSALGATELDSIVDELLVM-MSLKKCENTKVGtmtekSLSRGERKRLAFACEI 258
Cdd:COG1101 91 MGTapsMTIEENLALAYRrgkrrgLR--RGLTKKRRELFRELLATLgLGLENRLDTKVG-----LLSGGQRQALSLLMAT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 259 LTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGK-TVICTIHqpstsvyHMAD------QLILLSQGHVAY--AGPAK 329
Cdd:COG1101 164 LTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTH-------NMEQaldygnRLIMMHEGRIILdvSGEEK 236
|
.
gi 17539902 330 Q 330
Cdd:COG1101 237 K 237
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
102-303 |
9.09e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.35 E-value: 9.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 102 QNIQAVVLKKKGVRQ-----EILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKnieTDGDIMINGRN---MISN 173
Cdd:PRK10584 4 ENIVEVHHLKKSVGQgehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDG---SSGEVSLVGQPlhqMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 174 EMKKLSA----YVQQDDVFIGTLTVRETLRFAAKLRspsalGATELDSIVD--ELLVMMSLKKcentKVGTMTEKsLSRG 247
Cdd:PRK10584 81 ARAKLRAkhvgFVFQSFMLIPTLNALENVELPALLR-----GESSRQSRNGakALLEQLGLGK----RLDHLPAQ-LSGG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17539902 248 ERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQP 303
Cdd:PRK10584 151 EQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDL 207
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
109-332 |
1.01e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.97 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 109 LKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKNIETDGDIMINGRNM-----ISNEMKKLSA--- 180
Cdd:PRK09984 10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVqregrLARDIRKSRAntg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 181 YVQQDDVFIGTLTVRETLRFAAKLRSPSALGATELDSIVDELLVMMSLKKCENTKVGTMTEKSLSRGERKRLAFACEILT 260
Cdd:PRK09984 90 YIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539902 261 DPPILFCDEPTSGLDSFMSHQVIKALRQLT-IEGKTVICTIHQPSTSVYHmADQLILLSQGHVAYAGPAKQVD 332
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRDINqNDGITVVVTLHQVDYALRY-CERIVALRQGHVFYDGSSQQFD 241
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
127-303 |
1.26e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.22 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 127 RPGELTFIMGSSGAGKTTLLNILTGRNLKnieTDGDIMINGRnmisnEMKKLSAYVQQDDVFIG-------TLTVRETLR 199
Cdd:PRK13538 25 NAGELVQIEGPNGAGKTSLLRILAGLARP---DAGEVLWQGE-----PIRRQRDEYHQDLLYLGhqpgiktELTALENLR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 200 FAAKLRspsalGATELDSIVDeLLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMS 279
Cdd:PRK13538 97 FYQRLH-----GPGDDEALWE-ALAQVGLAGFEDVPVRQ-----LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGV 165
|
170 180
....*....|....*....|....
gi 17539902 280 HQVIKALRQLTIEGKTVICTIHQP 303
Cdd:PRK13538 166 ARLEALLAQHAEQGGMVILTTHQD 189
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
118-355 |
2.74e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 71.98 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 118 ILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnLKNIeTDGDIMINGRNMisNE---MKKLSAYVQQDDVFIGTLTV 194
Cdd:PRK11000 18 ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAG--LEDI-TSGDLFIGEKRM--NDvppAERGVGMVFQSYALYPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 195 RETLRFAAKLrspSALGATELDSIVDELLVMMSLKKCENTKvgtmtEKSLSRGERKRLAFACEILTDPPILFCDEPTSGL 274
Cdd:PRK11000 93 AENMSFGLKL---AGAKKEEINQRVNQVAEVLQLAHLLDRK-----PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 275 DSfmshqvikALR-QLTIEgktvICTIHQP--STSVY--H-------MADQLILLSQGHVAYAGpaKQVDAFFgrcgYPI 342
Cdd:PRK11000 165 DA--------ALRvQMRIE----ISRLHKRlgRTMIYvtHdqveamtLADKIVVLDAGRVAQVG--KPLELYH----YPA 226
|
250
....*....|....*...
gi 17539902 343 PKFVS----SPD-HFMRV 355
Cdd:PRK11000 227 NRFVAgfigSPKmNFLPV 244
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
118-320 |
7.06e-13 |
|
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: 67.88 E-value: 7.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 118 ILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlkNIE-TDGDIMINGRnmisnemkklSAYVQQDDvFIGTLTVRE 196
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG----ELEkLSGSVSVPGS----------IAYVSQEP-WIQNGTIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 197 TLRFAAKLRSP---SALGATELDSIVDellvmmSLKKCENTKVGtmtEK--SLSRGERKRLAFACEILTDPPILFCDEPT 271
Cdd:cd03250 85 NILFGKPFDEEryeKVIKACALEPDLE------ILPDGDLTEIG---EKgiNLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17539902 272 SGLDSFMSHQVI-KALRQLTIEGKTVICTIHQpsTSVYHMADQLILLSQG 320
Cdd:cd03250 156 SAVDAHVGRHIFeNCILGLLLNNKTRILVTHQ--LQLLPHADQIVVLDNG 203
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
117-331 |
8.03e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 69.45 E-value: 8.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 117 EILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnLKniETDGDIMINGRNMISNEMKKLSAYV----QQDDVFIGTL 192
Cdd:PRK13652 18 EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGI-LK--PTSGSVLIRGEPITKENIREVRKFVglvfQNPDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 193 TVRETLRFAaklrsPSALGATE--LDSIVDELLVMMSLKKCEntkvgTMTEKSLSRGERKRLAFACEILTDPPILFCDEP 270
Cdd:PRK13652 95 TVEQDIAFG-----PINLGLDEetVAHRVSSALHMLGLEELR-----DRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17539902 271 TSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQPSTsVYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDL-VPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
109-331 |
1.26e-12 |
|
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: 68.07 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 109 LKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnlknIETD-GDIMINGRNMISNEMKKLS----AYVQ 183
Cdd:TIGR04406 7 LIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGL----VRPDaGKILIDGQDITHLPMHERArlgiGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 184 QDDVFIGTLTVRETLRFAAKLRSpsALGATELDSIVDELLVMMSLKKCENTKVGtmtekSLSRGERKRLAFACEILTDPP 263
Cdd:TIGR04406 83 QEASIFRKLTVEENIMAVLEIRK--DLDRAEREERLEALLEEFQISHLRDNKAM-----SLSGGERRRVEIARALATNPK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17539902 264 ILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSVyHMADQLILLSQGHVAYAGPAKQV 331
Cdd:TIGR04406 156 FILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETL-DICDRAYIISDGKVLAEGTPAEI 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
99-332 |
1.27e-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: 67.17 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 99 LVFQNIQAVVLKKkgvrqEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrNLKNIETDGDIMINGRNMIS---NEM 175
Cdd:cd03217 1 LEIKDLHVSVGGK-----EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPKYEVTEGEILFKGEDITDlppEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 176 KKLSAYV-QQDDVFIGTLTVRETLRFaaklrspsalgateldsiVDEllvmmslkkcentkvgtmtekSLSRGERKRlaf 254
Cdd:cd03217 75 ARLGIFLaFQYPPEIPGVKNADFLRY------------------VNE---------------------GFSGGEKKR--- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 255 aCEILT----DPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSVYHMADQLILLSQGHVAYAGPAKQ 330
Cdd:cd03217 113 -NEILQllllEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHVLYDGRIVKSGDKEL 191
|
..
gi 17539902 331 VD 332
Cdd:cd03217 192 AL 193
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
111-331 |
1.41e-12 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 70.48 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 111 KKGV---RQEILKKIDGVA---RPGELTFIMGSSGAGKTTL-LNILtgrNLknIETDGDIMINGRNMIS---NEMKKLSA 180
Cdd:COG4172 288 KRGLfrrTVGHVKAVDGVSltlRRGETLGLVGESGSGKSTLgLALL---RL--IPSEGEIRFDGQDLDGlsrRALRPLRR 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 181 YVQ---QDDvFiGTL----TVRETLRFAAKLRSPsALGATELDSIVDELLvmmslkkcenTKVGtMTEKSLSR------- 246
Cdd:COG4172 363 RMQvvfQDP-F-GSLsprmTVGQIIAEGLRVHGP-GLSAAERRARVAEAL----------EEVG-LDPAARHRyphefsg 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 247 GERKRLAFACEILTDPPILFCDEPTSGLDsfMS--HQVIKALRQLTIEgktvictiHQPS--------TSVYHMADQLIL 316
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPTSALD--VSvqAQILDLLRDLQRE--------HGLAylfishdlAVVRALAHRVMV 498
|
250
....*....|....*
gi 17539902 317 LSQGHVAYAGPAKQV 331
Cdd:COG4172 499 MKDGKVVEQGPTEQV 513
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
119-331 |
1.57e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.58 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 119 LKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKnieTDGDIMINGRNMiSNEMKKLSA-----YVQQDDVFIGTLT 193
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP---TKGTITINNINY-NKLDHKLAAqlgigIIYQELSVIDELT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 194 VRETLrFAAKLRSPSALGA-----TELDSIVDELLVMMSLKKCENTKVGtmtekSLSRGERKRLAFACEILTDPPILFCD 268
Cdd:PRK09700 97 VLENL-YIGRHLTKKVCGVniidwREMRVRAAMMLLRVGLKVDLDEKVA-----NLSISHKQMLEIAKTLMLDAKVIIMD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539902 269 EPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPStSVYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK09700 171 EPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLA-EIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
115-331 |
2.22e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 68.96 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 115 RQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnLKNiETDGDIMINGRnmisnEMKKLSA------YVQQDDVF 188
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAG--LEH-QTSGHIRFHGT-----DVSRLHArdrkvgFVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 189 IGTLTVRETLRFAAKL----RSPSAlgaTELDSIVDELLVMMSLkkcenTKVGTMTEKSLSRGERKRLAFACEILTDPPI 264
Cdd:PRK10851 86 FRHMTVFDNIAFGLTVlprrERPNA---AAIKAKVTQLLEMVQL-----AHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17539902 265 LFCDEPTSGLDSFMSHQVIKALRQLTIEGK--TVICTIHQpsTSVYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKftSVFVTHDQ--EEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
117-333 |
2.66e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 67.95 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 117 EILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnLKniETDGDIMING------RNMISNEMKKLSAYVQQDDVFIG 190
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGI-LK--PSSGRILFDGkpidysRKGLMKLRESVGMVFQDPDNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 191 TLTVRETLRFAA-KLRSPSalgaTELDSIVDELLvmmslkkcENTKVGTMTEK---SLSRGERKRLAFACEILTDPPILF 266
Cdd:PRK13636 97 SASVYQDVSFGAvNLKLPE----DEVRKRVDNAL--------KRTGIEHLKDKpthCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17539902 267 CDEPTSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQPSTsVYHMADQLILLSQGHVAYAGPAKQVDA 333
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDI-VPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
117-331 |
2.97e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 67.25 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 117 EILKKIDGVARPGELTFIMGSSGAGKTTLLNILTgrnlKNIE------TDGDIMINGRNMISNEMKKLSAYVQQddVF-- 188
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFN----RLIElypearVSGEVYLDGQDIFKMDVIELRRRVQM--VFqi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 189 ---IGTLTVRETLRFAAKLRSpSALGATELDSIVDELLVMMSLKKCENTKVGTMTEKsLSRGERKRLAFACEILTDPPIL 265
Cdd:PRK14247 91 pnpIPNLSIFENVALGLKLNR-LVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGK-LSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17539902 266 FCDEPTSGLDSFMSHQVIKALRQLTIEgKTVICTIHQPSTSVyHMADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAA-RISDYVAFLYKGQIVEWGPTREV 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
119-331 |
3.11e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 67.70 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 119 LKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnLKNIETdGDIMINGRNMIS----NEMKKLSAYVQQ--DDVFIGTl 192
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNG--LLRPQK-GKVLVSGIDTGDfsklQGIRKLVGIVFQnpETQFVGR- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 193 TVRETLRFAAKlrsPSALGATELDSIVDELLVMMSLKKCENTkvgtmTEKSLSRGERKRLAFACEILTDPPILFCDEPTS 272
Cdd:PRK13644 94 TVEEDLAFGPE---NLCLPPIEIRKRVDRALAEIGLEKYRHR-----SPKTLSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17539902 273 GLDSFMSHQVIKALRQLTIEGKTVICTIHqpSTSVYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLHEKGKTIVYITH--NLEELHDADRIIVMDRGKIVLEGEPENV 222
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
104-331 |
3.15e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 68.07 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 104 IQAVVLKK-----KGV--RQEILKKIDGVA---RPGELTFIMGSSGAGKTTLlniltGRNLKNIE--TDGDIMINGRNMI 171
Cdd:PRK11308 6 LQAIDLKKhypvkRGLfkPERLVKALDGVSftlERGKTLAVVGESGCGKSTL-----ARLLTMIEtpTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 172 SN---EMKKLSAYVQQddVF---IGTLTVRETLRfaAKLRSPSALGaTELDSI--VDELLVMMSlkkcentKVGTMTEKS 243
Cdd:PRK11308 81 KAdpeAQKLLRQKIQI--VFqnpYGSLNPRKKVG--QILEEPLLIN-TSLSAAerREKALAMMA-------KVGLRPEHY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 244 ------LSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSVYHMADQLILL 317
Cdd:PRK11308 149 dryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVM 228
|
250
....*....|....
gi 17539902 318 SQGHVAYAGPAKQV 331
Cdd:PRK11308 229 YLGRCVEKGTKEQI 242
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
132-331 |
3.33e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 68.36 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 132 TFIMGSSGAGKTTLLNILTGrnLKNIETdGDIMINGRNMISNEM-------KKLSAYVQQDDVFIGTLTVRETLRFAAKL 204
Cdd:PRK11144 27 TAIFGRSGAGKTSLINAISG--LTRPQK-GRIVLNGRVLFDAEKgiclppeKRRIGYVFQDARLFPHYKVRGNLRYGMAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 205 RSPSalgatELDSIVdELLVMMSLKKcentkvgtMTEKSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIK 284
Cdd:PRK11144 104 SMVA-----QFDKIV-ALLGIEPLLD--------RYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17539902 285 ALRQLTIEGKTVICTIHQPSTSVYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK11144 170 YLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
119-331 |
3.67e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.45 E-value: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 119 LKKIDGVARPGELTFIMGSSGAGKTTLLNILTG--RNLKNIETDGDIMING---RNMISNEMKKLSAYVQQDDVFIGTLT 193
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllQPTEGKVTVGDIVVSStskQKEIKPVRKKVGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 194 VRETLRFAaklrsPSALGAT--ELDSIVDELLVMMSLKKcentkvgTMTEKS---LSRGERKRLAFACEILTDPPILFCD 268
Cdd:PRK13643 102 VLKDVAFG-----PQNFGIPkeKAEKIAAEKLEMVGLAD-------EFWEKSpfeLSGGQMRRVAIAGILAMEPEVLVLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539902 269 EPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQpSTSVYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK13643 170 EPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHL-MDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
104-335 |
4.23e-12 |
|
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: 69.06 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 104 IQAVVLKKKGVrqEILKKIDGVARPGELTFIMGSSGAGKTTLLNILtgRNLKNIE-TDGDIM-----------INGRNMI 171
Cdd:TIGR03269 3 VKNLTKKFDGK--EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVL--RGMDQYEpTSGRIIyhvalcekcgyVERPSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 172 SNEMKKLSAYVQQDDV-FIG---TLTVRETLRFAAKLRSPSAL--GATELDSIVDEL---------LVMMSLKKCENTKV 236
Cdd:TIGR03269 79 GEPCPVCGGTLEPEEVdFWNlsdKLRRRIRKRIAIMLQRTFALygDDTVLDNVLEALeeigyegkeAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 237 G---TMTEKSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQPSTsVYHMAD 312
Cdd:TIGR03269 159 ShriTHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEV-IEDLSD 237
|
250 260
....*....|....*....|...
gi 17539902 313 QLILLSQGHVAYAGPAKQVDAFF 335
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVVAVF 260
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
104-331 |
4.53e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 66.94 E-value: 4.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 104 IQAVVLKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnLKniETDGDIMINGrNMISNE-----MKKL 178
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGL-LK--PQSGEIKIDG-ITISKEnlkeiRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 179 SAYVQQ-DDVFIGtLTVRETLRFAA--KLRSPSalgatELDSIVDELlvmmslkkceNTKVGtMTE------KSLSRGER 249
Cdd:PRK13632 86 GIIFQNpDNQFIG-ATVEDDIAFGLenKKVPPK-----KMKDIIDDL----------AKKVG-MEDyldkepQNLSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 250 KRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEG-KTVICTIHQPSTSVyhMADQLILLSQGHVAYAGPA 328
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAI--LADKVIVFSEGKLIAQGKP 226
|
...
gi 17539902 329 KQV 331
Cdd:PRK13632 227 KEI 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
128-320 |
4.98e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 66.65 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 128 PGELTFIMGSSGAGKTTLLNILTGRnlknIETD-GDIMINGRNMISNEMKKlsAYVQQDDVFIGTLTVRETLRFAAKLRs 206
Cdd:PRK11248 26 SGELLVVLGPSGCGKTTLLNLIAGF----VPYQhGSITLDGKPVEGPGAER--GVVFQNEGLLPWRNVQDNVAFGLQLA- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 207 psALGATELDSIVDELLVMMSLKKCENTKVGtmtekSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKAL 286
Cdd:PRK11248 99 --GVEKMQRLEIAHQMLKKVGLEGAEKRYIW-----QLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLL 171
|
170 180 190
....*....|....*....|....*....|....*
gi 17539902 287 RQLTIE-GKTVICTIHQPSTSVYhMADQLILLSQG 320
Cdd:PRK11248 172 LKLWQEtGKQVLLITHDIEEAVF-MATELVLLSPG 205
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
130-326 |
6.22e-12 |
|
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: 69.27 E-value: 6.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 130 ELTFIMGSSGAGKTTLLNILTGRNLKnieTDGDIMINGRNMISN--EMKKLSAYVQQDDVFIGTLTVRETLRFAAKLRSP 207
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPP---TSGTVLVGGKDIETNldAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGR 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 208 SALGAT-ELDSIVDEllVMMSLKKCENTKvgtmtekSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKAL 286
Cdd:TIGR01257 1034 SWEEAQlEMEAMLED--TGLHHKRNEEAQ-------DLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17539902 287 RQLTiEGKTVICTIHQPSTSVYhMADQLILLSQGHVAYAG 326
Cdd:TIGR01257 1105 LKYR-SGRTIIMSTHHMDEADL-LGDRIAIISQGRLYCSG 1142
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
126-327 |
7.02e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 65.76 E-value: 7.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 126 ARPGELTFIMGSSGAGKTTLLNILTGRNLKnieTDGDIMINGRNMISNEMKK--LSAYVQQDDVFiGTLTVRET--LRFA 201
Cdd:PRK10771 22 VERGERVAILGPSGAGKSTLLNLIAGFLTP---ASGSLTLNGQDHTTTPPSRrpVSMLFQENNLF-SHLTVAQNigLGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 202 AKLRSPSALGATeLDSIVDEllvmMSLKKCENTKVGtmtekSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQ 281
Cdd:PRK10771 98 PGLKLNAAQREK-LHAIARQ----MGIEDLLARLPG-----QLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17539902 282 VIKALRQLTIEGK-TVICTIHQPSTSVyHMADQLILLSQGHVAYAGP 327
Cdd:PRK10771 168 MLTLVSQVCQERQlTLLMVSHSLEDAA-RIAPRSLVVADGRIAWDGP 213
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
113-330 |
8.39e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.20 E-value: 8.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 113 GVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILtgrnLKNIE-TDGDIMINGRNMIS---NEMKKLSAYVQQDDvF 188
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLI----QRHFDvSEGDIRFHDIPLTKlqlDSWRSRLAVVSQTP-F 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 189 IGTLTVRETLrfaaKLRSPSALG-----ATELDSIVDELLvmmSLKKCENTKVGtmtEKS--LSRGERKRLAFACEILTD 261
Cdd:PRK10789 400 LFSDTVANNI----ALGRPDATQqeiehVARLASVHDDIL---RLPQGYDTEVG---ERGvmLSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17539902 262 PPILFCDEPTSGLDSFMSHQVIKALRQLTiEGKTVICTIHQPSTSVyhMADQLILLSQGHVAYAGPAKQ 330
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLSALT--EASEILVMQHGHIAQRGNHDQ 535
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
119-323 |
9.75e-12 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 63.60 E-value: 9.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 119 LKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnlknIE-TDGDIMINGRnmisnemkklsayvqqddvfigtltvret 197
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGL----YKpDSGEILVDGK----------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 198 lrfAAKLRSPSAlgATELdsivdellvmmslkkcentKVGTMTEksLSRGERKRLAFACEILTDPPILFCDEPTSGLDSF 277
Cdd:cd03216 63 ---EVSFASPRD--ARRA-------------------GIAMVYQ--LSVGERQMVEIARALARNARLLILDEPTAALTPA 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17539902 278 MSHQVIKALRQLTIEGKTVICTIHQPSTsVYHMADQLILLSQGHVA 323
Cdd:cd03216 117 EVERLFKVIRRLRAQGVAVIFISHRLDE-VFEIADRVTVLRDGRVV 161
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
129-322 |
9.77e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.29 E-value: 9.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 129 GELTFIMGSSGAGKTTLLNILTGRNLKnieTDGDIMINGRNMI----SNEMKKLSAYVQQDDVFIGTLTVRETLR----F 200
Cdd:PRK11614 31 GEIVTLIGANGAGKTTLLGTLCGDPRA---TSGRIVFDGKDITdwqtAKIMREAVAIVPEGRRVFSRMTVEENLAmggfF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 201 AAKLRSPSALGAteldsiVDELLVMMSLKKCEntKVGTMtekslSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSH 280
Cdd:PRK11614 108 AERDQFQERIKW------VYELFPRLHERRIQ--RAGTM-----SGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17539902 281 QVIKALRQLTIEGKTvICTIHQPSTSVYHMADQLILLSQGHV 322
Cdd:PRK11614 175 QIFDTIEQLREQGMT-IFLVEQNANQALKLADRGYVLENGHV 215
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
114-326 |
9.81e-12 |
|
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: 66.62 E-value: 9.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 114 VRQEILKKIDGVA---RPGELTFIMGSSGAGKTTLLNILTGRNLKNIETDGDIMINGRNMIS---NEMKKLS----AYVQ 183
Cdd:COG0444 13 TRRGVVKAVDGVSfdvRRGETLGLVGESGSGKSTLARAILGLLPPPGITSGEILFDGEDLLKlseKELRKIRgreiQMIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 184 QD--DVFIGTLTVRETLRFAAKLRSPsaLGATELDSIVDELLvmmslkkcenTKVG-TMTEKSLSR-------GERKRLA 253
Cdd:COG0444 93 QDpmTSLNPVMTVGDQIAEPLRIHGG--LSKAEARERAIELL----------ERVGlPDPERRLDRyphelsgGMRQRVM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17539902 254 FACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQPSTsVYHMADQLIllsqghVAYAG 326
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGV-VAEIADRVA------VMYAG 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
116-275 |
1.00e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.78 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnlknIETD-GDIMINGRNMIsnemkklsAYVQQDDVFIGTLTV 194
Cdd:COG0488 11 RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGE----LEPDsGEVSIPKGLRI--------GYLPQEPPLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 195 RETL------------RFAAKLRSPS-----------------ALGATELDSIVDELLVMMSLKKCE-NTKVGTmteksL 244
Cdd:COG0488 79 LDTVldgdaelraleaELEELEAKLAepdedlerlaelqeefeALGGWEAEARAEEILSGLGFPEEDlDRPVSE-----L 153
|
170 180 190
....*....|....*....|....*....|.
gi 17539902 245 SRGERKRLAFACEILTDPPILFCDEPTSGLD 275
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
118-323 |
1.17e-11 |
|
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: 64.82 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 118 ILKKIDGVARPGELTFIMGSSGAGKTTLLNILtgrnLKNIE-TDGDIMINGRNmIS----NEMKKLSAYVQQDDV-FIGT 191
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLAL----FRLVElSSGSILIDGVD-ISkiglHDLRSRISIIPQDPVlFSGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 192 ltVRETL----RFA-AKLRSpsALGATELDSIVDELLVMMSLKKCENtkvgtmtEKSLSRGERKRLAFACEILTDPPILF 266
Cdd:cd03244 94 --IRSNLdpfgEYSdEELWQ--ALERVGLKEFVESLPGGLDTVVEEG-------GENLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17539902 267 CDEPTSGLDSFMSHQVIKALRQlTIEGKTVICTIHQPSTsVYHMaDQLILLSQGHVA 323
Cdd:cd03244 163 LDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDT-IIDS-DRILVLDKGRVV 216
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
127-322 |
1.43e-11 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 67.52 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 127 RPGELTFIMGSSGAGKTTLLNILTGrnLkNIETDGDIMINGRnMISNEmkKLSAYVQQddvfigtltvretlrFAA---- 202
Cdd:COG4615 356 RRGELVFIVGGNGSGKSTLAKLLTG--L-YRPESGEILLDGQ-PVTAD--NREAYRQL---------------FSAvfsd 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 203 -----KLrspsaLG--ATELDSIVDELLVMMSLKkcenTKV----GTMTEKSLSRGERKRLAFACEILTDPPILFCDE-- 269
Cdd:COG4615 415 fhlfdRL-----LGldGEADPARARELLERLELD----HKVsvedGRFSTTDLSQGQRKRLALLVALLEDRPILVFDEwa 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539902 270 ----PTsgldsF---MSHQVIKALRQltiEGKTVICTIH--QpstsvY-HMADQLILLSQGHV 322
Cdd:COG4615 486 adqdPE-----FrrvFYTELLPELKA---RGKTVIAISHddR-----YfDLADRVLKMDYGKL 535
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
133-331 |
1.49e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 66.03 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 133 FIMGSSGAGKTTLLNILTGRnLKNIETD---GDIMIN-----GRNMISNEMKKL----------SAYVQQDDVFIGTLTV 194
Cdd:PRK13631 56 FIIGNSGSGKSTLVTHFNGL-IKSKYGTiqvGDIYIGdkknnHELITNPYSKKIknfkelrrrvSMVFQFPEYQLFKDTI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 195 RETLRFAaklrsPSALGATELDS--IVDELLVMMSLKKcentkvgTMTEKS---LSRGERKRLAFACEILTDPPILFCDE 269
Cdd:PRK13631 135 EKDIMFG-----PVALGVKKSEAkkLAKFYLNKMGLDD-------SYLERSpfgLSGGQKRRVAIAGILAIQPEILIFDE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17539902 270 PTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQpSTSVYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK13631 203 PTAGLDPKGEHEMMQLILDAKANNKTVFVITHT-MEHVLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
117-332 |
1.69e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.00 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 117 EILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlknIET--DGDIMINGR---NMISNEMKKLSAY-VQQDDVFIG 190
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAG-----IVPpdSGTLEIGGNpcaRLTPAKAHQLGIYlVPQEPLLFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 191 TLTVRETLRFaaklRSPSALGATE-LDSIVDELLVMMSLKkcentkvgtMTEKSLSRGERKRLAFACEILTDPPILFCDE 269
Cdd:PRK15439 100 NLSVKENILF----GLPKRQASMQkMKQLLAALGCQLDLD---------SSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539902 270 PTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPStSVYHMADQLILLSQGHVAYAGPAKQVD 332
Cdd:PRK15439 167 PTASLTPAETERLFSRIRELLAQGVGIVFISHKLP-EIRQLADRISVMRDGTIALSGKTADLS 228
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
117-327 |
1.72e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.14 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 117 EILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKNietDGDIMINGRNMISNEMKKLSAYV------QQDDVFIG 190
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQ---RGRVKVMGREVNAENEKWVRSKVglvfqdPDDQVFSS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 191 TltVRETLRFAAKlrsPSALGATELDSIVDELLVMMSLKKcentkvgtMTEKS---LSRGERKRLAFACEILTDPPILFC 267
Cdd:PRK13647 96 T--VWDDVAFGPV---NMGLDKDEVERRVEEALKAVRMWD--------FRDKPpyhLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17539902 268 DEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSVyHMADQLILLSQGHV-AYAGP 327
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAA-EWADQVIVLKEGRVlAEGDK 222
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
116-330 |
1.91e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.14 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNIL-------TGRnlknIE--TDGDIMIngrnmisnemkkLS--AYVQQ 184
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpygSGR----IArpAGARVLF------------LPqrPYLPL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 185 ddvfiGTLtvRETLRFAAKLRSPS------ALGATELDSIVDELlvmmslkkcentKVGTMTEKSLSRGERKRLAFACEI 258
Cdd:COG4178 440 -----GTL--REALLYPATAEAFSdaelreALEAVGLGHLAERL------------DEEADWDQVLSLGEQQRLAFARLL 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17539902 259 LTDPPILFCDEPTSGLDSFMSHQVIKALRQlTIEGKTVICTIHQPSTSVYHmaDQLILLSQGHVAYAGPAKQ 330
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHRSTLAAFH--DRVLELTGDGSWQLLPAEA 569
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
99-348 |
2.14e-11 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 64.63 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 99 LVFQNiqavVLKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTgrnlKNIE-TDGDIMINGRNMISNEMKK 177
Cdd:cd03295 1 IEFEN----VTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMIN----RLIEpTSGEIFIDGEDIREQDPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 178 LS---AYVQQDdvfIGTL---TVRETLRFAAKLrspSALGATELDSIVDELLVMMSLkkcENTKVGTMTEKSLSRGERKR 251
Cdd:cd03295 73 LRrkiGYVIQQ---IGLFphmTVEENIALVPKL---LKWPKEKIRERADELLALVGL---DPAEFADRYPHELSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 252 LAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQPSTSVyHMADQLILLSQGHVA-YAGPak 329
Cdd:cd03295 144 VGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAF-RLADRIAIMKNGEIVqVGTP-- 220
|
250
....*....|....*....
gi 17539902 330 qvDAFFGRcgyPIPKFVSS 348
Cdd:cd03295 221 --DEILRS---PANDFVAE 234
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
119-327 |
2.26e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 65.59 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 119 LKKIDGVARPGELTFIMGSSGAGKTTLLNILtgrNLKNIETDGDIMINGRNMISNEMKKLSAYVQQddvfIGTL------ 192
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCI---NLLERPTSGRVLVDGQDLTALSEKELRKARRQ----IGMIfqhfnl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 193 ----TVRETLRFAAKLrspSALGATELDSIVDELLVMMSLkkcentkvgtmTEK------SLSRGERKRLAFACEILTDP 262
Cdd:PRK11153 94 lssrTVFDNVALPLEL---AGTPKAEIKARVTELLELVGL-----------SDKadrypaQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17539902 263 PILFCDEPTSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQPSTsVYHMADQLILLSQGHVAYAGP 327
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDV-VKRICDRVAVIDAGRLVEQGT 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
118-329 |
3.31e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 64.44 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 118 ILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKNIETDGDIMINGRNMISNEM----KKLSAYVQQ-DDVFIGTl 192
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVwdirEKVGIVFQNpDNQFVGA- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 193 TVRETLRFAAKLRspsALGATELDSIVDELLV---MMSLKKCEntkvgtmtEKSLSRGERKRLAFACEILTDPPILFCDE 269
Cdd:PRK13640 101 TVGDDVAFGLENR---AVPRPEMIKIVRDVLAdvgMLDYIDSE--------PANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17539902 270 PTSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQPSTSVyhMADQLILLSQGHV-AYAGPAK 329
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEAN--MADQVLVLDDGKLlAQGSPVE 229
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
113-322 |
3.56e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 63.36 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 113 GVRQEiLKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlknIE--TDGDIMINGRN---MISNE---MKKLSAYVQQ 184
Cdd:PRK10908 13 GGRQA-LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG-----IErpSAGKIWFSGHDitrLKNREvpfLRRQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 185 DDVFIGTLTVRETLRFaaklrsPSALGATELDSIVDELLVMMS----LKKCENTKVgtmtekSLSRGERKRLAFACEILT 260
Cdd:PRK10908 87 DHHLLMDRTVYDNVAI------PLIIAGASGDDIRRRVSAALDkvglLDKAKNFPI------QLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17539902 261 DPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQpSTSVYHMADQLILLSQGHV 322
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHD-IGLISRRSYRMLTLSDGHL 215
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
125-328 |
4.35e-11 |
|
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: 65.96 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 125 VARPGELTFIMGSSGAGKTTLLNILTGR---NLKNIETDGD-----------IMINGRNMISNEMKKLSAYVQQDD---- 186
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGElkpNLGDYDEEPSwdevlkrfrgtELQDYFKKLANGEIKVAHKPQYVDlipk 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 187 VFIGtlTVRETLRfaaklrspsalGATE---LDSIVDELlvmmSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPP 263
Cdd:COG1245 175 VFKG--TVRELLE-----------KVDErgkLDELAEKL----GLENILDRDISE-----LSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539902 264 ILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSVYhMADQLillsqgHVAYAGPA 328
Cdd:COG1245 233 FYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDY-LADYV------HILYGEPG 290
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
115-331 |
5.08e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 63.71 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 115 RQEILKKIDgVARPGELTF-IMGSSGAGKTTLL---NILTGRNlKNIETDGDIMINGRNMISNEMKKLSAYVQQDDVF-- 188
Cdd:PRK14267 16 SNHVIKGVD-LKIPQNGVFaLMGPSGCGKSTLLrtfNRLLELN-EEARVEGEVRLFGRNIYSPDVDPIEVRREVGMVFqy 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 189 ---IGTLTVRETLRFAAKLRSpSALGATELDSIVDELLVMMSL----KKCENTKVGtmtekSLSRGERKRLAFACEILTD 261
Cdd:PRK14267 94 pnpFPHLTIYDNVAIGVKLNG-LVKSKKELDERVEWALKKAALwdevKDRLNDYPS-----NLSGGQRQRLVIARALAMK 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 262 PPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTiHQPSTSVyHMADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK14267 168 PKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVT-HSPAQAA-RVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
116-331 |
5.53e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.53 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDgVARPGELTF-IMGSSGAGKTTLLNILTgRNLK----NIETDGDIMINGRNMISNEMKKLSAYV----QQDD 186
Cdd:PRK14246 23 KAILKDIT-IKIPNNSIFgIMGPSGSGKSTLLKVLN-RLIEiydsKIKVDGKVLYFGKDIFQIDAIKLRKEVgmvfQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 187 VFiGTLTVRETLrfAAKLRSPSALGATELDSIVDELLVMMSLKKCENTKVGTMTEKsLSRGERKRLAFACEILTDPPILF 266
Cdd:PRK14246 101 PF-PHLSIYDNI--AYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQ-LSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539902 267 CDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTiHQPStSVYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAIVIVS-HNPQ-QVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
127-302 |
7.48e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 65.25 E-value: 7.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 127 RPGELTFIMGSSGAGKTTLLNILTGrnlkNIETDGDIMINGRnmisnEMKKLS--------AYVQQD-DVFIGTLtvRET 197
Cdd:PRK11174 374 PAGQRIALVGPSGAGKTSLLNALLG----FLPYQGSLKINGI-----ELRELDpeswrkhlSWVGQNpQLPHGTL--RDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 198 LRFAAKLRSPSALGATELDSIVDELLVMMSLKKceNTKVGtmtEKS--LSRGERKRLAFACEILTDPPILFCDEPTSGLD 275
Cdd:PRK11174 443 VLLGNPDASDEQLQQALENAWVSEFLPLLPQGL--DTPIG---DQAagLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180
....*....|....*....|....*..
gi 17539902 276 SFMSHQVIKALRQLTiEGKTVICTIHQ 302
Cdd:PRK11174 518 AHSEQLVMQALNAAS-RRQTTLMVTHQ 543
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
93-289 |
8.05e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.12 E-value: 8.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 93 KTNAKKLVFQNIQAVVLKKkgvrqEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKNIeTDGDIMINGRNMIS 172
Cdd:CHL00131 2 NKNKPILEIKNLHASVNEN-----EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKI-LEGDILFKGESILD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 173 NEMKKLS------AYvqQDDVFIGTLTVRETLRFAAKLRSpSALGATELDSIvdELLVMMSlkkcENTKVGTMTEKSLSR 246
Cdd:CHL00131 76 LEPEERAhlgiflAF--QYPIEIPGVSNADFLRLAYNSKR-KFQGLPELDPL--EFLEIIN----EKLKLVGMDPSFLSR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17539902 247 --------GERKRLAFACEILTDPPILFCDEPTSGLDsfmshqvIKALRQL 289
Cdd:CHL00131 147 nvnegfsgGEKKRNEILQMALLDSELAILDETDSGLD-------IDALKII 190
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
119-352 |
1.66e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 63.17 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 119 LKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlknIE--TDGDIMINGRNMISNEMKKLSAYVQQddvfIGTL---- 192
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL-----LErpTSGSVLVDGVDLTALSERELRAARRK----IGMIfqhf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 193 ------TVRETLRFAAKLrspSALGATELDSIVDELLvmmSLkkcentkVGtMTEKS------LSRGERKRLAFACEILT 260
Cdd:COG1135 92 nllssrTVAENVALPLEI---AGVPKAEIRKRVAELL---EL-------VG-LSDKAdaypsqLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 261 DPPILFCDEPTSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQpstsvyhM------ADQLILLSQGHVAYAGPAKQVda 333
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHE-------MdvvrriCDRVAVLENGRIVEQGPVLDV-- 228
|
250 260
....*....|....*....|
gi 17539902 334 fFGRCGYPIPK-FVSSPDHF 352
Cdd:COG1135 229 -FANPQSELTRrFLPTVLND 247
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
113-301 |
1.66e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.78 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 113 GVRQeiLKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlKNIETDGDIMINGRNM-ISNEMKKLSAYV---QQDDVF 188
Cdd:PRK11288 16 GVKA--LDDISFDCRAGQVHALMGENGAGKSTLLKILSG---NYQPDAGSILIDGQEMrFASTTAALAAGVaiiYQELHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 189 IGTLTVRETLRFAaklRSPSALG---ATELDSIVDELLVMMSLKKCENTKVgtmteKSLSRGERKRLAFACEILTDPPIL 265
Cdd:PRK11288 91 VPEMTVAENLYLG---QLPHKGGivnRRLLNYEAREQLEHLGVDIDPDTPL-----KYLSIGQRQMVEIAKALARNARVI 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 17539902 266 FCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIH 301
Cdd:PRK11288 163 AFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
129-331 |
1.81e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 62.37 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 129 GELTFIMGSSGAGKTTLLNILTGRnLKniETDGDIMINGRNMISNEM------KKLSAYVQQDDVFIGTLTVRETLRFAa 202
Cdd:PRK13637 33 GEFVGLIGHTGSGKSTLIQHLNGL-LK--PTSGKIIIDGVDITDKKVklsdirKKVGLVFQYPEYQLFEETIEKDIAFG- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 203 klrsPSALGATElDSIVDELLVMMSLKKCENTKVGTMTEKSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQV 282
Cdd:PRK13637 109 ----PINLGLSE-EEIENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEI 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17539902 283 IKALRQLTIEGKTVICTIHQPSTSVYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK13637 184 LNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
116-330 |
2.16e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 63.97 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNILtgRNLKNiETDGDIMINGRNMISNEMKKLS---AYVQQDDVFIGTl 192
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALL--QNLYQ-PTGGQVLLDGVPLVQYDHHYLHrqvALVGQEPVLFSG- 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 193 TVRET----LRFAAKLRSPSALGATELDSIVdellvmMSLKKCENTKVGtmtEKS--LSRGERKRLAFACEILTDPPILF 266
Cdd:TIGR00958 570 SVRENiaygLTDTPDEEIMAAAKAANAHDFI------MEFPNGYDTEVG---EKGsqLSGGQKQRIAIARALVRKPRVLI 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539902 267 CDEPTSGLDSfmshQVIKALRQL-TIEGKTVICTIHQPSTSvyHMADQLILLSQGHVAYAGPAKQ 330
Cdd:TIGR00958 641 LDEATSALDA----ECEQLLQESrSRASRTVLLIAHRLSTV--ERADQILVLKKGSVVEMGTHKQ 699
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
117-329 |
2.40e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.59 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 117 EILKKIDGVARPGELTFIMGSSGAGKTTLLNILtgrNLKNIETDGDIMINGRNMISNEMKKLSAYVQQDDVFI------- 189
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL---GCLDKPTSGTYRVAGQDVATLDADALAQLRREHFGFIfqryhll 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 190 GTLTVRETLRFAAKLrspSALGATELDSIVDELLVMMSLKKCENTKVGtmtekSLSRGERKRLAFACEILTDPPILFCDE 269
Cdd:PRK10535 99 SHLTAAQNVEVPAVY---AGLERKQRLLRAQELLQRLGLEDRVEYQPS-----QLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 270 PTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPstSVYHMADQLILLSQGHVAYAGPAK 329
Cdd:PRK10535 171 PTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP--QVAAQAERVIEIRDGEIVRNPPAQ 228
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
116-333 |
2.42e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.95 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTG--RNLKnietdGDIMINGRNMISNE-----MKKLSAYVQQD-DV 187
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGllRPQK-----GAVLWQGKPLDYSKrgllaLRQQVATVFQDpEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 188 FIGTLTVRETLRFAakLRSpsaLGATElDSI---VDELLVMMSLKKCENTKVgtmteKSLSRGERKRLAFACEILTDPPI 264
Cdd:PRK13638 89 QIFYTDIDSDIAFS--LRN---LGVPE-AEItrrVDEALTLVDAQHFRHQPI-----QCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17539902 265 LFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTsVYHMADQLILLSQGHVAYAGPAKQVDA 333
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
129-331 |
2.76e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.54 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 129 GELTFIMGSSGAGKTTLLniltgRNLKNIET--DGDIMINGRNM---ISNEMKKLSAYVQQDDVFIGTLTVREtlrFAAK 203
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLL-----RTLSRLMTpaHGHVWLDGEHIqhyASKEVARRIGLLAQNATTPGDITVQE---LVAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 204 LRSPSALGATELDSiVDELLVMMSLKKCENTKVGTMTEKSLSRGERKRLAFACEILTDPPILFCDEPTSGLDsfMSHQV- 282
Cdd:PRK10253 105 GRYPHQPLFTRWRK-EDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD--ISHQId 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17539902 283 -IKALRQLTIE-GKTVICTIHQPSTSVYHmADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK10253 182 lLELLSELNREkGYTLAAVLHDLNQACRY-ASHLIALREGKIVAQGAPKEI 231
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
129-333 |
3.21e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 61.32 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 129 GELTFIMGSSGAGKTTLLNILTGRnlknIETD-GDIMINGRNM-------ISNEMKKLSAYVQQDDVFIgTLTVRETLRF 200
Cdd:PRK11831 33 GKITAIMGPSGIGKTTLLRLIGGQ----IAPDhGEILFDGENIpamsrsrLYTVRKRMSMLFQSGALFT-DMNVFDNVAY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 201 AakLRSPSALGATELDSIvdellVMMSLKKCENTKVGTMTEKSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSH 280
Cdd:PRK11831 108 P--LREHTQLPAPLLHST-----VMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17539902 281 QVIKALRQLTIE-GKTVICTIHQpSTSVYHMADQLILLSQGHVAYAGPAKQVDA 333
Cdd:PRK11831 181 VLVKLISELNSAlGVTCVVVSHD-VPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
127-331 |
4.95e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.33 E-value: 4.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 127 RPGELTFIMGSSGAGKTTLLNILTGRnlknIETDGDIMINGRNMIS---NEMKKLSAYV--QQDDVFIgtLTVRE--TLR 199
Cdd:PRK03695 20 RAGEILHLVGPNGAGKSTLLARMAGL----LPGSGSIQFAGQPLEAwsaAELARHRAYLsqQQTPPFA--MPVFQylTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 200 FAAKlrSPSALGATELDSIVDELLVMMSLKKCENTkvgtmteksLSRGE--RKRLAFAC-----EILTDPPILFCDEPTS 272
Cdd:PRK03695 94 QPDK--TRTEAVASALNEVAEALGLDDKLGRSVNQ---------LSGGEwqRVRLAAVVlqvwpDINPAGQLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17539902 273 GLDsfMSHQVI--KALRQLTIEGKTVICTIHQPSTSvYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK03695 163 SLD--VAQQAAldRLLSELCQQGIAVVMSSHDLNHT-LRHADRVWLLKQGKLLASGRRDEV 220
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
119-331 |
5.62e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.80 E-value: 5.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 119 LKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnLKniETDGDIMInGRNMISNEM--KKLSAYVQQddvfIGTL---- 192
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGL-LQ--PTSGTVTI-GERVITAGKknKKLKPLRKK----VGIVfqfp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 193 -------TVRETLRFAaklrsPSALGATELDSI--VDELLVMMSLkkceNTKVGTMTEKSLSRGERKRLAFACEILTDPP 263
Cdd:PRK13634 95 ehqlfeeTVEKDICFG-----PMNFGVSEEDAKqkAREMIELVGL----PEELLARSPFELSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17539902 264 ILFCDEPTSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQpSTSVYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK13634 166 VLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHS-MEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
119-301 |
8.03e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.49 E-value: 8.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 119 LKKIDGVA---RPGELTFIMGSSGAGKTTLLNILtgrNLKNIETDGDIMINGRNMISNEMKKLSAYVQQDDVFigTLTVR 195
Cdd:PRK13651 20 LKALDNVSveiNQGEFIAIIGQTGSGKTTFIEHL---NALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKLVI--QKTRF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 196 ETLRFAAKLRSPSAL-----------GATELDSIVDEllVMMSLKKCENTK--------VG---TMTEKS---LSRGERK 250
Cdd:PRK13651 95 KKIKKIKEIRRRVGVvfqfaeyqlfeQTIEKDIIFGP--VSMGVSKEEAKKraakyielVGldeSYLQRSpfeLSGGQKR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17539902 251 RLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIH 301
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
125-328 |
8.22e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 8.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 125 VARPGELTFIMGSSGAGKTTLLNILTGR---NLKNIETDGDI--MIN--GRNMISNEMKKLSA----------YVQQ-DD 186
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGElipNLGDYEEEPSWdeVLKrfRGTELQNYFKKLYNgeikvvhkpqYVDLiPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 187 VFIGTltVRETLRFAAKlrspsalgATELDSIVDELlvmmSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILF 266
Cdd:PRK13409 175 VFKGK--VRELLKKVDE--------RGKLDEVVERL----GLENILDRDISE-----LSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17539902 267 CDEPTSGLDSFMSHQVIKALRQLTiEGKTVICTIHQPSTSVYhMADQLillsqgHVAYAGPA 328
Cdd:PRK13409 236 FDEPTSYLDIRQRLNVARLIRELA-EGKYVLVVEHDLAVLDY-LADNV------HIAYGEPG 289
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
128-275 |
9.62e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.09 E-value: 9.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 128 PGELTFIMGSSGAGKTTLLNILTGrnLKNIETdGDIMINGRNMISNEMKKLSAYVQQDDVFIGTLTVRETLRFAAKL--- 204
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAG--LLHVES-GQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLhgr 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17539902 205 ---RSPSAlgateldsivdeLLVMMSLKKCENTKVgtmteKSLSRGERKRLAFACEILTDPPILFCDEPTSGLD 275
Cdd:PRK13543 113 rakQMPGS------------ALAIVGLAGYEDTLV-----RQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
119-322 |
1.28e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 61.19 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 119 LKKIDGVARPGELTFIMGSSGAGKTTLLNILTgrNLKNIEtDGDIMINGRNM----ISNEMKKLSAYVQQDDVFIGTLT- 193
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLT--RFYDID-EGEILLDGHDLrdytLASLRNQVALVSQNVHLFNDTIAn 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 194 ----------VRETLRFAAKLrspsalgATELDSIvdellvmmslKKCEN---TKVGtmtEK--SLSRGERKRLAFACEI 258
Cdd:PRK11176 436 niayarteqySREQIEEAARM-------AYAMDFI----------NKMDNgldTVIG---ENgvLLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17539902 259 LTDPPILFCDEPTSGLDSFMSHQVIKALRQLTiEGKTVICTIHQPSTsvYHMADQLILLSQGHV 322
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDELQ-KNRTSLVIAHRLST--IEKADEILVVEDGEI 556
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
129-326 |
1.36e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.92 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 129 GELTFIMGSSGAGKTTLLNILTGRnLKNIETdGDIMINGRnmisnemkklSAYVQQDDvFIGTLTVRETLRFAAKLRSPS 208
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLISAMLGE-LSHAET-SSVVIRGS----------VAYVPQVS-WIFNATVRENILFGSDFESER 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 209 ALGATELDSIVDELLVMMSLKKCENTKVGTmtekSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQ 288
Cdd:PLN03232 710 YWRAIDVTALQHDLDLLPGRDLTEIGERGV----NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK 785
|
170 180 190
....*....|....*....|....*....|....*...
gi 17539902 289 LTIEGKTVICTIHQpsTSVYHMADQLILLSQGHVAYAG 326
Cdd:PLN03232 786 DELKGKTRVLVTNQ--LHFLPLMDRIILVSEGMIKEEG 821
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
114-303 |
1.58e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.43 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 114 VRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnLKNIETDGDIMINgRNMISNEMKKLSAYVQQDDVfigtLT 193
Cdd:COG2401 41 VERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA-LKGTPVAGCVDVP-DNQFGREASLIDAIGRKGDF----KD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 194 VRETLRfAAKLRSPSALGATeldsiVDEllvmmslkkcentkvgtmteksLSRGERKRLAFACEILTDPPILFCDEPTSG 273
Cdd:COG2401 115 AVELLN-AVGLSDAVLWLRR-----FKE----------------------LSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190
....*....|....*....|....*....|.
gi 17539902 274 LDSFMSHQVIKALRQLTIE-GKTVICTIHQP 303
Cdd:COG2401 167 LDRQTAKRVARNLQKLARRaGITLVVATHHY 197
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
127-275 |
1.71e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 58.89 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 127 RPGELTFIMGSSGAGKTTLLNILTGRnlknIETD-GDIMINGRNmISNemkkLSAYV----------QQDDVFIGtLTVR 195
Cdd:COG1137 27 NQGEIVGLLGPNGAGKTTTFYMIVGL----VKPDsGRIFLDGED-ITH----LPMHKrarlgigylpQEASIFRK-LTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 196 ETLRFAAKLRSPSAlgaTELDSIVDELLVMMSLKKCENTKVGtmtekSLSRGERKRLAFACEILTDPPILFCDEPTSGLD 275
Cdd:COG1137 97 DNILAVLELRKLSK---KEREERLEELLEEFGITHLRKSKAY-----SLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
119-297 |
2.10e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.43 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 119 LKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlknIE--TDGDIMINGRNM-ISNEMKKLSA---YVQQDDVFIGTL 192
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYG-----LYqpDSGEILIDGKPVrIRSPRDAIALgigMVHQHFMLVPNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 193 TVRETLRFAAKLRSPSALGATELDSIVDELlvmmslkkCE--------NTKVGTmteksLSRGERKRLafacEIL----T 260
Cdd:COG3845 96 TVAENIVLGLEPTKGGRLDRKAARARIREL--------SErygldvdpDAKVED-----LSVGEQQRV----EILkalyR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17539902 261 DPPILFCDEPTSGL-----DSFMshqviKALRQLTIEGKTVI 297
Cdd:COG3845 159 GARILILDEPTAVLtpqeaDELF-----EILRRLAAEGKSII 195
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
134-337 |
2.23e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.50 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 134 IMGSSGAGKTTLLNILTGRNlknIETDGDIMINGRNMIS---NEMKKLSAYVQQDDVFI-GTLTVRETL-RFAAKLRSPS 208
Cdd:PRK10790 372 LVGHTGSGKSTLASLLMGYY---PLTEGEIRLDGRPLSSlshSVLRQGVAMVQQDPVVLaDTFLANVTLgRDISEEQVWQ 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 209 ALGATELDSIVdellvmMSLKKCENTKVGTMTeKSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQ 288
Cdd:PRK10790 449 ALETVQLAELA------RSLPDGLYTPLGEQG-NNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAA 521
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17539902 289 LTiEGKTVICTIHQPSTSVyhMADQLILLSQGHVAYAGPAKQVDAFFGR 337
Cdd:PRK10790 522 VR-EHTTLVVIAHRLSTIV--EADTILVLHRGQAVEQGTHQQLLAAQGR 567
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
118-358 |
2.42e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 58.71 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 118 ILKKIDGVARPGELTFIMGSSGAGKTTLLNILtgrnLKNIETDGDIMINGRN---MISNEMKKLSAYVQQDdVFIGTLTV 194
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAF----LRLLNTEGDIQIDGVSwnsVPLQKWRKAFGVIPQK-VFIFSGTF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 195 RETLRFAAKLRSPSALGATE---LDSIVDELLVMMSLKKCENTKVgtmteksLSRGERKRLAFACEILTDPPILFCDEPT 271
Cdd:cd03289 94 RKNLDPYGKWSDEEIWKVAEevgLKSVIEQFPGQLDFVLVDGGCV-------LSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 272 SGLDSfMSHQVIKALRQLTIEGKTVICTIHQpstsVYHMAD--QLILLSQGHVayagpaKQVDAffgrcgypIPKFVSSP 349
Cdd:cd03289 167 AHLDP-ITYQVIRKTLKQAFADCTVILSEHR----IEAMLEcqRFLVIEENKV------RQYDS--------IQKLLNEK 227
|
....*....
gi 17539902 350 DHFMRVISH 358
Cdd:cd03289 228 SHFKQAISP 236
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
129-331 |
2.68e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 59.46 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 129 GELTFIMGSSGAGKTTLLNILTGRNlknIETDGDIMINGRNM--ISNEMKKLSAYVQQDDVFiGTLTVRETLRFAAKlrs 206
Cdd:PRK11607 45 GEIFALLGASGCGKSTLLRMLAGFE---QPTAGQIMLDGVDLshVPPYQRPINMMFQSYALF-PHMTVEQNIAFGLK--- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 207 PSALGATELDSIVDELLVMMSLKKCENTKvgtmtEKSLSRGERKRLAFACEILTDPPILFCDEPTSGLDS----FMSHQV 282
Cdd:PRK11607 118 QDKLPKAEIASRVNEMLGLVHMQEFAKRK-----PHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKklrdRMQLEV 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17539902 283 IKALRQLtieGKTVICTIHQPSTSVYhMADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK11607 193 VDILERV---GVTCVMVTHDQEEAMT-MAGRIAIMNRGKFVQIGEPEEI 237
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
114-295 |
4.37e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.52 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 114 VRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnlkNIETDGDIMINGRNmisneMKKLSA------------Y 181
Cdd:PRK11629 20 VQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL---DTPTSGDVIFNGQP-----MSKLSSaakaelrnqklgF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 182 VQQDDVFIGTLTVRETLRFaaklrsPSALGATELDSIVDELLVMMSLKKCEntKVGTMTEKSLSRGERKRLAFACEILTD 261
Cdd:PRK11629 92 IYQFHHLLPDFTALENVAM------PLLIGKKKPAEINSRALEMLAAVGLE--HRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190
....*....|....*....|....*....|....
gi 17539902 262 PPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKT 295
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGT 197
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
96-326 |
4.43e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.10 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 96 AKKLVFQNIQAVVLKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnLKNIETD----GDIMINGRNMI 171
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNG--LIISETGqtivGDYAIPANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 172 SNEMKKLSAYV----QQDDVFIGTLTVRETLRFAaklrsPSALGAT--ELDSIVDELLVMMSLKKcENTKVGTMtekSLS 245
Cdd:PRK13645 82 IKEVKRLRKEIglvfQFPEYQLFQETIEKDIAFG-----PVNLGENkqEAYKKVPELLKLVQLPE-DYVKRSPF---ELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 246 RGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSVYHMADQLILLSQGHVAYA 325
Cdd:PRK13645 153 GGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISI 232
|
.
gi 17539902 326 G 326
Cdd:PRK13645 233 G 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
119-297 |
5.02e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 59.26 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 119 LKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlknIE--TDGDIMINGRnmisnEMKKLS---------AYVQQDDV 187
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSG-----VYqpDSGEILLDGE-----PVRFRSprdaqaagiAIIHQELN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 188 FIGTLTVRETLRFAAKLRSPSALGATELDSIVDELLVMMSLKKCENTKVGtmtekSLSRGERKRLAFACEILTDPPILFC 267
Cdd:COG1129 90 LVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVG-----DLSVAQQQLVEIARALSRDARVLIL 164
|
170 180 190
....*....|....*....|....*....|
gi 17539902 268 DEPTSGLDSFMSHQVIKALRQLTIEGKTVI 297
Cdd:COG1129 165 DEPTASLTEREVERLFRIIRRLKAQGVAII 194
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
129-329 |
5.66e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.59 E-value: 5.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 129 GELTFIMGSSGAGKTTLLNILTG--RnlkniETDGDIMINGRNMISNEMKKLSAYVQQDD-------VFIGTLTVRETLR 199
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGfvR-----LASGKISILGQPTRQALQKNLVAYVPQSEevdwsfpVLVEDVVMMGRYG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 200 FAAKLRSPSAlgatELDSIVDELLVMMSLKKCENTKVGtmtekSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMS 279
Cdd:PRK15056 108 HMGWLRRAKK----RDRQIVTAALARVDMVEFRHRQIG-----ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17539902 280 HQVIKALRQLTIEGKTVICTIHQPStSVYHMADQLILLsQGHVAYAGPAK 329
Cdd:PRK15056 179 ARIISLLRELRDEGKTMLVSTHNLG-SVTEFCDYTVMV-KGTVLASGPTE 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
115-333 |
6.48e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.49 E-value: 6.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 115 RQ--EILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnlknIE-TDGDIMINGRNMISNEMKKLSAYVQ---QDDVf 188
Cdd:PRK15112 23 RQtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGM----IEpTSGELLIDDHPLHFGDYSYRSQRIRmifQDPS- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 189 iGTLTVREtlRFAAKLRSPSALGaTELDSIVDELLVMMSLKKcentkVGTMTEKS------LSRGERKRLAFACEILTDP 262
Cdd:PRK15112 98 -TSLNPRQ--RISQILDFPLRLN-TDLEPEQREKQIIETLRQ-----VGLLPDHAsyyphmLAPGQKQRLGLARALILRP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539902 263 PILFCDEPTSGLDSFMSHQVIKALrqLTIEGKTVICTIH--QPSTSVYHMADQLILLSQGHVAYAGPAKQVDA 333
Cdd:PRK15112 169 KVIIADEALASLDMSMRSQLINLM--LELQEKQGISYIYvtQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
301-353 |
6.64e-09 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 58.38 E-value: 6.64e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 17539902 301 HQPSTSVYHMADQLILLSQGH-VAYAGPAKQVDAFFGRCGYPIPKFVSSPDHFM 353
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGlTVYHGPVKKVEEYFAGLGINVPERVNPPDHFI 54
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
116-302 |
7.11e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.11 E-value: 7.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnLKNIETdGDIMINGRNMisneMKKLSAYvQQDDVFIG----- 190
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAG--LLNPEK-GEILFERQSI----KKDLCTY-QKQLCFVGhrsgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 191 --TLTVRETLRFAAKLRSpSALGateldsiVDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACEILTDPPILFCD 268
Cdd:PRK13540 86 npYLTLRENCLYDIHFSP-GAVG-------ITELCRLFSLEHLIDYPCGL-----LSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190
....*....|....*....|....*....|....
gi 17539902 269 EPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQ 302
Cdd:PRK13540 153 EPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
98-322 |
7.61e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.93 E-value: 7.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 98 KLVFQNIQavvlKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnLKNIeTDGDIMINGRNMisNEMKK 177
Cdd:PRK11650 3 GLKLQAVR----KSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG--LERI-TSGEIWIGGRVV--NELEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 178 LS---AYVQQDDVFIGTLTVRETLRFAAKLRspsALGATELDSIVDELLVMMSLkkcentkvGTMTE---KSLSRGERKR 251
Cdd:PRK11650 74 ADrdiAMVFQNYALYPHMSVRENMAYGLKIR---GMPKAEIEERVAEAARILEL--------EPLLDrkpRELSGGQRQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 252 LAFACEILTDPPILFCDEPTSGLDSfmshqvikALR-QLTIEgktvICTIHQ--PSTSVY--H-------MADQLILLSQ 319
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLDA--------KLRvQMRLE----IQRLHRrlKTTSLYvtHdqveamtLADRVVVMNG 210
|
...
gi 17539902 320 GHV 322
Cdd:PRK11650 211 GVA 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
117-275 |
8.58e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 58.54 E-value: 8.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 117 EILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnlknIETDGDIMINGRNMisnemkKLsAYVQQD-DVFIGTLTVR 195
Cdd:COG0488 329 TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGE----LEPDSGTVKLGETV------KI-GYFDQHqEELDPDKTVL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 196 ETLR-FAAKLRSPSA---LGAteldsivdellvM-----MSLKKCentkvgtmteKSLSRGERKRLAFACEILTDPPILF 266
Cdd:COG0488 398 DELRdGAPGGTEQEVrgyLGR------------FlfsgdDAFKPV----------GVLSGGEKARLALAKLLLSPPNVLL 455
|
....*....
gi 17539902 267 CDEPTSGLD 275
Cdd:COG0488 456 LDEPTNHLD 464
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
128-331 |
1.36e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 56.47 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 128 PGELTFIMGSSGAGKTTLLNILTGRnlknIETD-GDIMINGRNMISNEMKKLS------------AYVQQD-------DV 187
Cdd:PRK11701 31 PGEVLGIVGESGSGKTTLLNALSAR----LAPDaGEVHYRMRDGQLRDLYALSeaerrrllrtewGFVHQHprdglrmQV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 188 FIGTlTVRETL-----RFAAKLRSPSA--LGATELD-SIVDELlvmmslkkcentkvgtmtEKSLSRGERKRLAFACEIL 259
Cdd:PRK11701 107 SAGG-NIGERLmavgaRHYGDIRATAGdwLERVEIDaARIDDL------------------PTTFSGGMQQRLQIARNLV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17539902 260 TDPPILFCDEPTSGLDSFMSHQVIKALRQLTIE-GKTVICTIHqpSTSVYHM-ADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK11701 168 THPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTH--DLAVARLlAHRLLVMKQGRVVESGLTDQV 239
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
120-322 |
1.37e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.91 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 120 KKIDGVA---RPGELTFIMGSSGAGKTTLLNILTGRNLKNIEtdGDIMINGRNM-ISNEMKKLS---AYVQQD---DVFI 189
Cdd:TIGR02633 274 KRVDDVSfslRRGEILGVAGLVGAGRTELVQALFGAYPGKFE--GNVFINGKPVdIRNPAQAIRagiAMVPEDrkrHGIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 190 GTLTVRETLRFAAkLRSPSALG----ATELDSIvDELLVMMSLKkcenTKVGTMTEKSLSRGERKRLAFACEILTDPPIL 265
Cdd:TIGR02633 352 PILGVGKNITLSV-LKSFCFKMridaAAELQII-GSAIQRLKVK----TASPFLPIGRLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17539902 266 FCDEPTSGLDSFMSHQVIKALRQLTIEGKTVIcTIHQPSTSVYHMADQLILLSQGHV 322
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLAQEGVAII-VVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
71-320 |
1.60e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 57.67 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 71 FRKPKTLSVTNDTESARIPsQVKTNAKKLVFQNIQAvvlkKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILT 150
Cdd:PRK10522 296 FNKLNKLALAPYKAEFPRP-QAFPDWQTLELRNVTF----AYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLT 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 151 GRnlkNIETDGDIMINGRnMISneMKKLSAYVQQddvfigtltvretlrFAA---------KLRSPSalGATELDSIVDE 221
Cdd:PRK10522 371 GL---YQPQSGEILLDGK-PVT--AEQPEDYRKL---------------FSAvftdfhlfdQLLGPE--GKPANPALVEK 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 222 LLVMMSLKKCENTKVGTMTEKSLSRGERKRLAFACEILTDPPILFCDEPTSGLD----SFMSHQVIKALRQLtieGKTVI 297
Cdd:PRK10522 428 WLERLKMAHKLELEDGRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDphfrREFYQVLLPLLQEM---GKTIF 504
|
250 260
....*....|....*....|...
gi 17539902 298 CTIHqpSTSVYHMADQLILLSQG 320
Cdd:PRK10522 505 AISH--DDHYFIHADRLLEMRNG 525
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
104-331 |
2.50e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 57.12 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 104 IQAVVLKKK--GVRQEILKKIDGVA---RPGELTFIMGSSGAGKTTLLNILTGRnlknIE-TDGDI----------MING 167
Cdd:TIGR03269 280 IKVRNVSKRyiSVDRGVVKAVDNVSlevKEGEIFGIVGTSGAGKTTLSKIIAGV----LEpTSGEVnvrvgdewvdMTKP 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 168 RNMISNEMKKLSAYVQQDDVFIGTLTVRETLRFAAKLRSPSALGatELDSIVDELLVMMSLKKCENTkVGTMTEKsLSRG 247
Cdd:TIGR03269 356 GPDGRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLELPDELA--RMKAVITLKMVGFDEEKAEEI-LDKYPDE-LSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 248 ERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQPSTsVYHMADQLILLSQGHVAYAG 326
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDF-VLDVCDRAALMRDGKIVKIG 510
|
....*
gi 17539902 327 PAKQV 331
Cdd:TIGR03269 511 DPEEI 515
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
115-330 |
2.96e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 55.17 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 115 RQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRN--LKNIETDGDIMINGRNMISN-----EMKKLSAYV-QQDD 186
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlNPEVTITGSIVYNGHNIYSPrtdtvDLRKEIGMVfQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 187 VFigTLTVRETLRFAakLRSPSALGATELDSIVDELLVMMSL-----KKCENTKVGtmteksLSRGERKRLAFACEILTD 261
Cdd:PRK14239 97 PF--PMSIYENVVYG--LRLKGIKDKQVLDEAVEKSLKGASIwdevkDRLHDSALG------LSGGQQQRVCIARVLATS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539902 262 PPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICT--IHQPS----TSVYHMADQLILLSQGHVAYAGPAKQ 330
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTrsMQQASrisdRTGFFLDGDLIEYNDTKQMFMNPKHK 241
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
119-331 |
3.41e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 55.87 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 119 LKKIDGVA---RPGELTFIMGSSGAGKTTLLNILTGrnLKNIeTDGDIMINGRN---MISNEMKKLSAYVQ---QDDvfI 189
Cdd:PRK15079 34 LKAVDGVTlrlYEGETLGVVGESGCGKSTFARAIIG--LVKA-TDGEVAWLGKDllgMKDDEWRAVRSDIQmifQDP--L 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 190 GTLTVRETLR--FAAKLRS--PSaLGATEldsIVDELLVMMslkkcenTKVGTMTE------KSLSRGERKRLAFACEIL 259
Cdd:PRK15079 109 ASLNPRMTIGeiIAEPLRTyhPK-LSRQE---VKDRVKAMM-------LKVGLLPNlinrypHEFSGGQCQRIGIARALI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539902 260 TDPPILFCDEPTSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQPSTsVYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK15079 178 LEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAV-VKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
101-329 |
3.90e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.22 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 101 FQNIQAVV-----LKKKGvrqeiLKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnLKniETDGDIMINGRNMISNE- 174
Cdd:PRK13641 5 FENVDYIYspgtpMEKKG-----LDNISFELEEGSFVALVGHTGSGKSTLMQHFNAL-LK--PSSGTITIAGYHITPETg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 175 -------MKKLSAYVQQDDVFIGTLTVRETLRFAaklrsPSALGATELDSIVDELLVMmslkkcenTKVG---TMTEKS- 243
Cdd:PRK13641 77 nknlkklRKKVSLVFQFPEAQLFENTVLKDVEFG-----PKNFGFSEDEAKEKALKWL--------KKVGlseDLISKSp 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 244 --LSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQpSTSVYHMADQLILLSQGH 321
Cdd:PRK13641 144 feLSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHN-MDDVAEYADDVLVLEHGK 222
|
....*....
gi 17539902 322 -VAYAGPAK 329
Cdd:PRK13641 223 lIKHASPKE 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
91-297 |
4.69e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.33 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 91 QVKTNAKKLVFQNI-QAVVLKKKGVRQEILKKIDGVA---RPGELTFIMGSSGAGKTTLLNILTGRNLKnieTDGDIMIN 166
Cdd:PRK09700 247 QNRFNAMKENVSNLaHETVFEVRNVTSRDRKKVRDISfsvCRGEILGFAGLVGSGRTELMNCLFGVDKR---AGGEIRLN 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 167 GRNM-ISNE---MKKLSAYV---QQDDVFIGTLTVRETLRFAAKLRSPSALGATELDSIVDELLVMMSLKKCENTKVGTM 239
Cdd:PRK09700 324 GKDIsPRSPldaVKKGMAYItesRRDNGFFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHSV 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 240 TEK--SLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVI 297
Cdd:PRK09700 404 NQNitELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVIL 463
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-358 |
4.70e-08 |
|
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: 56.84 E-value: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 22 LITSLDVDPTQKSRSPTPKPTPIPvlindtpvaseieQVEKELAHSSERFRKPKTLSVTNDTESARIPSQVKTNAKKLVF 101
Cdd:TIGR01271 1159 VNSSIDVDGLMRSVSRVFKFIDLP-------------QEEPRPSGGGGKYQLSTVLVIENPHAQKCWPSGGQMDVQGLTA 1225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 102 QNIQAvvlkkkgvRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILtgrnLKNIETDGDIMINGR--NMISNEMKKLS 179
Cdd:TIGR01271 1226 KYTEA--------GRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL----LRLLSTEGEIQIDGVswNSVTLQTWRKA 1293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 180 AYVQQDDVFIGTLTVRETLRFAAKLRSPSALGATE---LDSIVDELLVMMSLKKCENTKVgtmteksLSRGERKRLAFAC 256
Cdd:TIGR01271 1294 FGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEevgLKSVIEQFPDKLDFVLVDGGYV-------LSNGHKQLMCLAR 1366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 257 EILTDPPILFCDEPTSGLDSfMSHQVIKALRQLTIEGKTVICTIHQpstsvyhmADQLILLSQGHVAYAGPAKQVDAffg 336
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDP-VTLQIIRKTLKQSFSNCTVILSEHR--------VEALLECQQFLVIEGSSVKQYDS--- 1434
|
330 340
....*....|....*....|..
gi 17539902 337 rcgypIPKFVSSPDHFMRVISH 358
Cdd:TIGR01271 1435 -----IQKLLNETSLFKQAMSA 1451
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
129-331 |
4.88e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 54.76 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 129 GELTFIMGSSGAGKTTLLNILTGrnlknIE--TDGDIMINGRNMISNEMKKLSAYV-----QQDDVFIGTlTVRETLRFA 201
Cdd:PRK13648 35 GQWTSIVGHNGSGKSTIAKLMIG-----IEkvKSGEIFYNNQAITDDNFEKLRKHIgivfqNPDNQFVGS-IVKYDVAFG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 202 AKlrsPSALGATELDSIVDEllvmmSLKKCENTKVGTMTEKSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQ 281
Cdd:PRK13648 109 LE---NHAVPYDEMHRRVSE-----ALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17539902 282 VIKALRQLTIEGKTVICTIHQPSTSVYHmADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK13648 181 LLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
129-329 |
5.32e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.50 E-value: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 129 GELTFIMGSSGAGKTTLLNILTGrnLKNiETDGDIMINGRNMISNEmkklsayVQQDDVFI--------GTLTVRETLRF 200
Cdd:PRK11432 32 GTMVTLLGPSGCGKTTVLRLVAG--LEK-PTEGQIFIDGEDVTHRS-------IQQRDICMvfqsyalfPHMSLGENVGY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 201 AAKLRspsALGATELDSIVDELLVMMSLKKCENTKVgtmteKSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSH 280
Cdd:PRK11432 102 GLKML---GVPKEERKQRVKEALELVDLAGFEDRYV-----DQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRR 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17539902 281 QVIKALRQLTIE-GKTVICTIHQpSTSVYHMADQLILLSQGHVAYAGPAK 329
Cdd:PRK11432 174 SMREKIRELQQQfNITSLYVTHD-QSEAFAVSDTVIVMNKGKIMQIGSPQ 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
109-318 |
5.37e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.95 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 109 LKKKGVR---QEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnlknIE-TDGDIMINGRNM--ISNEM-KKLSAY 181
Cdd:PRK10247 10 LQNVGYLagdAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASL----ISpTSGTLLFEGEDIstLKPEIyRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 182 VQQDDVFIGTlTVRETLRFAAKLRSPsalgATELDSIVDELlvmMSLKKCENTKVGTMTEksLSRGERKRLAFACEILTD 261
Cdd:PRK10247 86 CAQTPTLFGD-TVYDNLIFPWQIRNQ----QPDPAIFLDDL---ERFALPDTILTKNIAE--LSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17539902 262 PPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSVYHmADQLILLS 318
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITLQ 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
29-326 |
7.55e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.94 E-value: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 29 DPTQKSRSPTpkptpipVLINDTPVASEIEQvekeLAHSSERFRKPKTLSVTNDTESARIPsQVKTNAKklvFQNIQAVV 108
Cdd:PTZ00243 611 RPTKRHPSPS-------VVVEDTDYGSPSSA----SRHIVEGGTGGGHEATPTSERSAKTP-KMKTDDF---FELEPKVL 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 109 LKKkgVRQEILKkidgvarpGELTFIMGSSGAGKTTLLNILtgrnLKNIETDGDIMINGRNMisnemkklsAYVQQdDVF 188
Cdd:PTZ00243 676 LRD--VSVSVPR--------GKLTVVLGATGSGKSTLLQSL----LSQFEISEGRVWAERSI---------AYVPQ-QAW 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 189 IGTLTVRETLRF-----AAKLRspSALGATELDSIVDELLVMMSlkkcenTKVGtmtEK--SLSRGERKRLAFACEILTD 261
Cdd:PTZ00243 732 IMNATVRGNILFfdeedAARLA--DAVRVSQLEADLAQLGGGLE------TEIG---EKgvNLSGGQKARVSLARAVYAN 800
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539902 262 PPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQpsTSVYHMADQLILLSQGHVAYAG 326
Cdd:PTZ00243 801 RDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQ--VHVVPRADYVVALGDGRVEFSG 863
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
109-326 |
7.63e-08 |
|
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: 52.71 E-value: 7.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 109 LKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNiltgrnlKNIETDGDIMINgrnmisnemKKLSAYVQQDDVF 188
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN-------EGLYASGKARLI---------SFLPKFSRNKLIF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 189 IGtltvretlrfaaklrspsalgatELDSIVDELLVMMSLkkceNTKVGTmteksLSRGERKRLAFACEI-LTDPPILFC 267
Cdd:cd03238 65 ID-----------------------QLQFLIDVGLGYLTL----GQKLST-----LSGGELQRVKLASELfSEPPGTLFI 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 268 -DEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSVYhmADQLILLSQGHVAYAG 326
Cdd:cd03238 113 lDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS--ADWIIDFGPGSGKSGG 170
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
129-394 |
9.34e-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: 9.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 129 GELTFIMGSSGAGKTTLLNILTGRNLKnieTDGDIMINGRnmisnemkklSAYVQQDdVFIGTLTVRETLRFAAKLRSPS 208
Cdd:TIGR00957 664 GALVAVVGQVGCGKSSLLSALLAEMDK---VEGHVHMKGS----------VAYVPQQ-AWIQNDSLRENILFGKALNEKY 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 209 ALGATELDSIVDELLVMMSlkkCENTKVGtmtEK--SLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKAL 286
Cdd:TIGR00957 730 YQQVLEACALLPDLEILPS---GDRTEIG---EKgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHV 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 287 --RQLTIEGKTVICTIHqpSTSVYHMADQLILLSQGHVAYAGPAKQV---DAFFGR--CGY-PIPKFVSSPDHFMRVISh 358
Cdd:TIGR00957 804 igPEGVLKNKTRILVTH--GISYLPQVDVIIVMSGGKISEMGSYQELlqrDGAFAEflRTYaPDEQQGHLEDSWTALVS- 880
|
250 260 270
....*....|....*....|....*....|....*.
gi 17539902 359 ksfeTEDDYNKRIEKIVLEHDIMKKEQSTHSTLSSS 394
Cdd:TIGR00957 881 ----GEGKEAKLIENGMLVTDVVGKQLQRQLSASSS 912
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
129-331 |
1.28e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 54.27 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 129 GELTFIMGSSGAGKTTLLNILTgrnlKNIE-TDGDIMINGRNM--ISNE-----MKKLSAYVQQDDVFIGTLTVRETLRF 200
Cdd:PRK10070 54 GEIFVIMGLSGSGKSTMVRLLN----RLIEpTRGQVLIDGVDIakISDAelrevRRKKIAMVFQSFALMPHMTVLDNTAF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 201 AAKLrspSALGATELDSIVDELLVMMSLkkcENTKVGTMTEksLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSH 280
Cdd:PRK10070 130 GMEL---AGINAEERREKALDALRQVGL---ENYAHSYPDE--LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17539902 281 QVIKALRQLTIEGKTVICTIHQPSTSVYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK10070 202 EMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
244-318 |
1.32e-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: 51.77 E-value: 1.32e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539902 244 LSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIegkTVICTIHQPSTSVYHmaDQLILLS 318
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGI---TVISVGHRPSLWKFH--DRVLDLD 161
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
116-301 |
1.52e-07 |
|
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: 50.91 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlKNIETDGDIMINGRNMIsnemkklsAYVQQddvfigtltvr 195
Cdd:cd03221 13 KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG---ELEPDEGIVTWGSTVKI--------GYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 196 etlrfaaklrspsalgateldsivdellvmmslkkcentkvgtmteksLSRGERKRLAFACEILTDPPILFCDEPTSGLD 275
Cdd:cd03221 71 ------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180
....*....|....*....|....*.
gi 17539902 276 SFMSHQVIKALRQLTiegKTVICTIH 301
Cdd:cd03221 103 LESIEALEEALKEYP---GTVILVSH 125
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
108-331 |
1.80e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 54.33 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 108 VLKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTllnilTGRNL-KNIETDGDIMINGRNMISNEMKKLsayvqqdd 186
Cdd:PRK15134 291 ILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKST-----TGLALlRLINSQGEIWFDGQPLHNLNRRQL-------- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 187 vfigtLTVREtlRFAAKLRSP-SALGAT-ELDSIVDELLVM----MSLKKCENTKVGTMTEKSL------------SRGE 248
Cdd:PRK15134 358 -----LPVRH--RIQVVFQDPnSSLNPRlNVLQIIEEGLRVhqptLSAAQREQQVIAVMEEVGLdpetrhrypaefSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 249 RKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSVYHMADQLILLSQGHVAYAGPA 328
Cdd:PRK15134 431 RQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDC 510
|
...
gi 17539902 329 KQV 331
Cdd:PRK15134 511 ERV 513
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
124-297 |
2.28e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.02 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 124 GVARPGELTFIMGSSGAGKTTLLNILTGRnlknIETD-GDImingrnmisNEMKKLS---AYVQQDdvfiGTLTVRETLR 199
Cdd:COG1245 361 GEIREGEVLGIVGPNGIGKTTFAKILAGV----LKPDeGEV---------DEDLKISykpQYISPD----YDGTVEEFLR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 200 FAAKLRSPSALGATEldsIVDELlvmmSLKKCENTKVgtmteKSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMS 279
Cdd:COG1245 424 SANTDDFGSSYYKTE---IIKPL----GLEKLLDKNV-----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 491
|
170
....*....|....*....
gi 17539902 280 HQVIKALRQLTIE-GKTVI 297
Cdd:COG1245 492 LAVAKAIRRFAENrGKTAM 510
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
116-312 |
2.29e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 52.73 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNlkniETDGDIMINGRNMISNE------------MKKLSAYVQ 183
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMN----ELESEVRVEGRVEFFNQniyerrvnlnrlRRQVSMVHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 184 QDDVFigTLTVRETLRFAAKLrspsaLG---ATELDSIVDELLVMMSLKKCENTKVGTmTEKSLSRGERKRLAFACEILT 260
Cdd:PRK14258 96 KPNLF--PMSVYDNVAYGVKI-----VGwrpKLEIDDIVESALKDADLWDEIKHKIHK-SALDLSGGQQQRLCIARALAV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17539902 261 DPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSVYHMAD 312
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
220-336 |
2.45e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.20 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 220 DELLVMMSLkkcenTKVGTMTEKSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICT 299
Cdd:NF000106 126 DELLERFSL-----TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLT 200
|
90 100 110
....*....|....*....|....*....|....*..
gi 17539902 300 IhQPSTSVYHMADQLILLSQGHVAYAGPAKQVDAFFG 336
Cdd:NF000106 201 T-QYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
129-328 |
4.14e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 51.82 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 129 GELTFIMGSSGAGKTTLLNILTGRNLKNietDGDIMINGRNM----ISNEMKKLSAYVQQDDVFIGTLTVRETLRFAAKL 204
Cdd:PRK10895 29 GEIVGLLGPNGAGKTTTFYMVVGIVPRD---AGNIIIDDEDIsllpLHARARRGIGYLPQEASIFRRLSVYDNLMAVLQI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 205 RSPsaLGATELDSIVDELLVMMSLKKCENTkVGtmteKSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIK 284
Cdd:PRK10895 106 RDD--LSAEQREDRANELMEEFHIEHLRDS-MG----QSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17539902 285 ALRQLTIEGKTVICTIHQPSTSVyHMADQLILLSQGH-VAYAGPA 328
Cdd:PRK10895 179 IIEHLRDSGLGVLITDHNVRETL-AVCERAYIVSQGHlIAHGTPT 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
106-322 |
4.43e-07 |
|
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: 50.51 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 106 AVVLKKKGVRQEI-LKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnLKNIETdGDIMINGRnmisnemkklsayvqq 184
Cdd:cd03215 2 EPVLEVRGLSVKGaVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFG--LRPPAS-GEITLDGK---------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 185 ddvfigtltvretlrfAAKLRSPS---ALGA---TElDSIVDELLVMMSLKkcENTKVGTMteksLSRGERKRLAFACEI 258
Cdd:cd03215 63 ----------------PVTRRSPRdaiRAGIayvPE-DRKREGLVLDLSVA--ENIALSSL----LSGGNQQKVVLARWL 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17539902 259 LTDPPILFCDEPTSGLD----SFMsHQVIKALRQltiEGKTVICTihqpST---SVYHMADQLILLSQGHV 322
Cdd:cd03215 120 ARDPRVLILDEPTRGVDvgakAEI-YRLIRELAD---AGKAVLLI----SSeldELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
98-388 |
5.08e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 51.70 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 98 KLVFQNIQAVVLKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRnLKniETDGDIMINGRNMISNEMKK 177
Cdd:PRK13646 2 TIRFDNVSYTYQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAL-LK--PTTGTVTVDDITITHKTKDK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 178 LSAYVQQDdvfIG-TLTVRETLRFAAKLRSPSALGATELDSIVDELL-----VMMSLKKCENtkVGTMTEKSLSRGERKR 251
Cdd:PRK13646 79 YIRPVRKR---IGmVFQFPESQLFEDTVEREIIFGPKNFKMNLDEVKnyahrLLMDLGFSRD--VMSQSPFQMSGGQMRK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 252 LAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQpSTSVYHMADQLILLSQGHVAYAGPAKq 330
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDeNKTIILVSHD-MNEVARYADEVIVMKEGSIVSQTSPK- 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17539902 331 vdAFFGRCGYPIPKFVSSPDhfmrvISHKSFETEDDYNKRIEKIVLEHD---IMKKEQSTH 388
Cdd:PRK13646 232 --ELFKDKKKLADWHIGLPE-----IVQLQYDFEQKYQTKLKDIALTEEefvSLYKEWQHE 285
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
129-331 |
5.18e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 51.67 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 129 GELTFIMGSSGAGKTTLLNILTGRNL--KNIETDGDIMINGRNM---ISNEMKKLSAYVQQDDVFIGTLTVRETLRFAak 203
Cdd:PRK13649 33 GSYTAFIGHTGSGKSTIMQLLNGLHVptQGSVRVDDTLITSTSKnkdIKQIRKKVGLVFQFPESQLFEETVLKDVAFG-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 204 lrsPSALGAT--ELDSIVDELLVMMSLKKcentkvgTMTEKS---LSRGERKRLAFACEILTDPPILFCDEPTSGLDSFM 278
Cdd:PRK13649 111 ---PQNFGVSqeEAEALAREKLALVGISE-------SLFEKNpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17539902 279 SHQVIKALRQLTIEGKTVICTIHQpSTSVYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK13649 181 RKELMTLFKKLHQSGMTIVLVTHL-MDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
117-275 |
7.09e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 51.19 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 117 EILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRN--LKNIETDGDIMINGRNMISNEMK--KLSAYV----QQDDVF 188
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPGARVEGEILLDGEDIYDPDVDvvELRRRVgmvfQKPNPF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 189 igTLTVRETLRFAAKL---RSPSalgatELDSIVDEllvmmSLKKC---ENTK-----VGTmtekSLSRGERKRLAFACE 257
Cdd:COG1117 105 --PKSIYDNVAYGLRLhgiKSKS-----ELDEIVEE-----SLRKAalwDEVKdrlkkSAL----GLSGGQQQRLCIARA 168
|
170
....*....|....*...
gi 17539902 258 ILTDPPILFCDEPTSGLD 275
Cdd:COG1117 169 LAVEPEVLLMDEPTSALD 186
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
122-275 |
1.04e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 50.76 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 122 IDGVA---RPGELTFIMGSSGAGKTTLLNILTG--RnlkniETDGDIMINGRN-------MISNemKKLSAYVQQDDVFi 189
Cdd:PRK11300 21 VNNVNlevREQEIVSLIGPNGAGKTTVFNCLTGfyK-----PTGGTILLRGQHieglpghQIAR--MGVVRTFQHVRLF- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 190 GTLTVRETLRFAAKLRSPSALGA----------TELDSI--VDELLVMMSLKKCENTKVGTmteksLSRGERKRLAFACE 257
Cdd:PRK11300 93 REMTVIENLLVAQHQQLKTGLFSgllktpafrrAESEALdrAATWLERVGLLEHANRQAGN-----LAYGQQRRLEIARC 167
|
170
....*....|....*...
gi 17539902 258 ILTDPPILFCDEPTSGLD 275
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLN 185
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
95-331 |
1.08e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.86 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 95 NAKKLVFQNIQAvvlkKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTL---LNILTgrnlknIETDGDIMINGRNM- 170
Cdd:PRK13633 6 KCKNVSYKYESN----EESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALL------IPSEGKVYVDGLDTs 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 171 -ISN--EMKKLSAYVQQ--DDVFIGTLtVRETLRFAaklrsPSALG--ATELDSIVDEllvmmSLKKCENTKVGTMTEKS 243
Cdd:PRK13633 76 dEENlwDIRNKAGMVFQnpDNQIVATI-VEEDVAFG-----PENLGipPEEIRERVDE-----SLKKVGMYEYRRHAPHL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 244 LSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLT-IEGKTVICTIHQPSTSVyhMADQLILLSQGHV 322
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNkKYGITIILITHYMEEAV--EADRIIVMDSGKV 222
|
....*....
gi 17539902 323 AYAGPAKQV 331
Cdd:PRK13633 223 VMEGTPKEI 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
127-332 |
1.27e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 127 RPGELTFIMGSSGAGKTTLLNILTGRNLKnieTDGDIMINGRNMISNE----MKKLSAYVQQD---DVFIGTLTVRETLR 199
Cdd:PRK10762 276 RKGEILGVSGLMGAGRTELMKVLYGALPR---TSGYVTLDGHEVVTRSpqdgLANGIVYISEDrkrDGLVLGMSVKENMS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 200 FAAkLRSPSALGAtELDSiVDELLVMMSLKKCENTKVGTMTE--KSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSF 277
Cdd:PRK10762 353 LTA-LRYFSRAGG-SLKH-ADEQQAVSDFIRLFNIKTPSMEQaiGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVG 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17539902 278 MSHQVIKALRQLTIEGKTVIcTIHQPSTSVYHMADQLILLSQGHVAYAGPAKQVD 332
Cdd:PRK10762 430 AKKEIYQLINQFKAEGLSII-LVSSEMPEVLGMSDRILVMHEGRISGEFTREQAT 483
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
109-288 |
1.62e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 50.07 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 109 LKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlknIE--TDGDIMINGRNMIS---NEMKKLSAYVQ 183
Cdd:PRK10419 18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVG-----LEspSQGNVSWRGEPLAKlnrAQRKAFRRDIQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 184 ---QDDvfIGTLTVRETLR--FAAKLRSPSALGATELDSIVDELLVMMSLKKCENTKVgtmtEKSLSRGERKRLAFACEI 258
Cdd:PRK10419 93 mvfQDS--ISAVNPRKTVReiIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKR----PPQLSGGQLQRVCLARAL 166
|
170 180 190
....*....|....*....|....*....|...
gi 17539902 259 LTDPPILFCDEPTSGLDSFMSHQVI---KALRQ 288
Cdd:PRK10419 167 AVEPKLLILDEAVSNLDLVLQAGVIrllKKLQQ 199
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
129-320 |
2.00e-06 |
|
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: 49.25 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 129 GELTFIMGSSGAGKTTLLNILTGR----------NLKNIETDGDIMINGRNMISnemkklSAYVQQDDVFIGTlTVRETL 198
Cdd:cd03290 27 GQLTMIVGQVGCGKSSLLLAILGEmqtlegkvhwSNKNESEPSFEATRSRNRYS------VAYAAQKPWLLNA-TVEENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 199 RFAA---KLRSPSALGATELDSIVDellvmmSLKKCENTKVGtmtEK--SLSRGERKRLAFACEILTDPPILFCDEPTSG 273
Cdd:cd03290 100 TFGSpfnKQRYKAVTDACSLQPDID------LLPFGDQTEIG---ERgiNLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17539902 274 LDSFMSHQVIKA--LRQLTIEGKTVICTIHQPSTSVYhmADQLILLSQG 320
Cdd:cd03290 171 LDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLPH--ADWIIAMKDG 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
136-275 |
2.64e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.89 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 136 GSSGAGKTTLLNILTGrnLKNIeTDGDIMINGRNMISNEM--KKLSAYVQQDDVFIGTLTVRETLRFAAKLRSpsaLGAT 213
Cdd:NF033858 299 GSNGCGKSTTMKMLTG--LLPA-SEGEAWLFGQPVDAGDIatRRRVGYMSQAFSLYGELTVRQNLELHARLFH---LPAA 372
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17539902 214 ELDSIVDELLVMMSLKKCENTKVGtmtekSLSRGERKRLAFACEILTDPPILFCDEPTSGLD 275
Cdd:NF033858 373 EIAARVAEMLERFDLADVADALPD-----SLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
127-331 |
3.53e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 49.72 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 127 RPGELTFIMGSSGAGKTTLLNILTGRNLKNIETDGDIMINGR---NMISNEMKKLSAYvQQDDVFIGTLT-------VRE 196
Cdd:PRK09473 40 RAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGReilNLPEKELNKLRAE-QISMIFQDPMTslnpymrVGE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 197 TLRFAAKLRSpsALGATEldsIVDELLVMM-SLKKCENTKVGTMTEKSLSRGERKRLAFACEILTDPPILFCDEPTSGLD 275
Cdd:PRK09473 119 QLMEVLMLHK--GMSKAE---AFEESVRMLdAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17539902 276 SFMSHQVIKALRQLTIEGKTVICTIHQPSTSVYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK09473 194 VTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
110-336 |
3.94e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.89 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 110 KKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKNietDGDIMINGrnmiSNEMKKLSAYVQqddvfi 189
Cdd:PRK13545 31 SKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPN---KGTVDIKG----SAALIAISSGLN------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 190 GTLTVRETLRFAAKLRspsALGATELDSIVDELLVMMSLKKCENTKVgtmteKSLSRGERKRLAFACEILTDPPILFCDE 269
Cdd:PRK13545 98 GQLTGIENIELKGLMM---GLTKEKIKEIIPEIIEFADIGKFIYQPV-----KTYSSGMKSRLGFAISVHINPDILVIDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17539902 270 PTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPStSVYHMADQLILLSQGHVAYAGPAKQVDAFFG 336
Cdd:PRK13545 170 ALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLS-QVKSFCTKALWLHYGQVKEYGDIKEVVDHYD 235
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
243-317 |
5.85e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.83 E-value: 5.85e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17539902 243 SLSRGERKRLAFACEILT---DPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHqpSTSVYHMADQLILL 317
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH--NMHVVKVADYVLEL 884
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
151-307 |
6.44e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 6.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 151 GRNLKNIETDGDIMINGRNMIS---NEMKKLSAYVQQDDVFIgTLTVRETLRFAAKLRSPSALGATELDSIVDELLvmMS 227
Cdd:PTZ00265 1267 GEDSTVFKNSGKILLDGVDICDynlKDLRNLFSIVSQEPMLF-NMSIYENIKFGKEDATREDVKRACKFAAIDEFI--ES 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 228 LKKCENTKVGTMTeKSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSV 307
Cdd:PTZ00265 1344 LPNKYDTNVGPYG-KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI 1422
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
433-609 |
7.44e-06 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 48.54 E-value: 7.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 433 LVKLIQTLIMSIMIGSTYYGLEIDKKSLPSFK-----GFAFVSVQMMHMLFMMPAMTVFWkdypvVVREFQANMY----- 502
Cdd:pfam12698 123 LLQQLNASALVLLLEALSTSAPIPVESTPLFNpqsgyAYYLVGLILMIIILIGAAIIAVS-----IVEEKESRIKerllv 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 503 ---SPSAYYLAKTTADSIQYLVFPVIFSGILLGMTSLPYSVViitnYLIINILLSLNAC-SVGQSFAAMCGHLATGMTVL 578
Cdd:pfam12698 198 sgvSPLQYWLGKILGDFLVGLLQLLIILLLLFGIGIPFGNLG----LLLLLFLLYGLAYiALGYLLGSLFKNSEDAQSII 273
|
170 180 190
....*....|....*....|....*....|....*..
gi 17539902 579 PIVCVPLMVFGGFMITYEAIPW------YFLPFAWVS 609
Cdd:pfam12698 274 GIVILLLSGFFGGLFPLEDPPSflqwifSIIPFFSPI 310
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
116-326 |
8.07e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.86 E-value: 8.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 116 QEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKNIeTDGDIMINGRNMISNEMKKLSA----YVQQDDVFIGT 191
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEV-TGGTVEFKGKDLLELSPEDRAGegifMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 192 LTVRETLRFAA----KLRSPSALGATELDSIVDE---LLVMMSLKKCENTKVGtmteksLSRGERKRLAFACEILTDPPI 264
Cdd:PRK09580 93 VSNQFFLQTALnavrSYRGQEPLDRFDFQDLMEEkiaLLKMPEDLLTRSVNVG------FSGGEKKRNDILQMAVLEPEL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17539902 265 LFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSVYHMADQLILLSQGHVAYAG 326
Cdd:PRK09580 167 CILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSG 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
129-367 |
1.03e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 47.80 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 129 GELTFIMGSSGAGKTTLLNILTGrnLKNIETdGDIMINGRNMISN---EMKKLSAYVQQ--DDVFIGTlTVRETLRFAAK 203
Cdd:PRK13650 33 GEWLSIIGHNGSGKSTTVRLIDG--LLEAES-GQIIIDGDLLTEEnvwDIRHKIGMVFQnpDNQFVGA-TVEDDVAFGLE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 204 LRspsALGATELDSIVDE---LLVMMSLKKCENTKvgtmteksLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSH 280
Cdd:PRK13650 109 NK---GIPHEEMKERVNEaleLVGMQDFKEREPAR--------LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 281 QVIKALRQLTIE-GKTVICTIHQPSTSVyhMADQLILLSQGHVAYAGPAKQVdafFGRC------GYPIPkFVSSpdhFM 353
Cdd:PRK13650 178 ELIKTIKGIRDDyQMTVISITHDLDEVA--LSDRVLVMKNGQVESTSTPREL---FSRGndllqlGLDIP-FTTS---LV 248
|
250
....*....|....
gi 17539902 354 RVISHKSFETEDDY 367
Cdd:PRK13650 249 QSLRQNGYDLPEGY 262
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
120-320 |
1.72e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.00 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 120 KKIDGVA---RPGELTFIMGSSGAGKTTLLNIL----TGRNlknietDGDIMINGRNM-ISNEMKKLS---AYVQQD--- 185
Cdd:PRK13549 276 KRVDDVSfslRRGEILGIAGLVGAGRTELVQCLfgayPGRW------EGEIFIDGKPVkIRNPQQAIAqgiAMVPEDrkr 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 186 DVFIGTLTVRETLRFAAkLRSPSALG----ATELDSIVDELLVMmslkkcentKVGTMTE----KSLSRGERKRLAFACE 257
Cdd:PRK13549 350 DGIVPVMGVGKNITLAA-LDRFTGGSriddAAELKTILESIQRL---------KVKTASPelaiARLSGGNQQKAVLAKC 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539902 258 ILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVIcTIHQPSTSVYHMADQLILLSQG 320
Cdd:PRK13549 420 LLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAII-VISSELPEVLGLSDRVLVMHEG 481
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
107-335 |
2.15e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 107 VVLKKKGVRQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILtgrnLKNIETD-GDIMINGRNM----ISNEMKKLSAY 181
Cdd:PLN03232 1240 VHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNAL----FRIVELEkGRIMIDDCDVakfgLTDLRRVLSII 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 182 VQQDDVFIGTLtvretlRFAAKLRSP-------SALGATELDSIVDELLVMMSLKKCENTKvgtmtekSLSRGERKRLAF 254
Cdd:PLN03232 1316 PQSPVLFSGTV------RFNIDPFSEhndadlwEALERAHIKDVIDRNPFGLDAEVSEGGE-------NFSVGQRQLLSL 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 255 ACEILTDPPILFCDEPTSGLDSfmshqVIKALRQLTIEGKTVICTI----HQPSTSVyhMADQLILLSQGHV-AYAGP-- 327
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVDV-----RTDSLIQRTIREEFKSCTMlviaHRLNTII--DCDKILVLSSGQVlEYDSPqe 1455
|
250
....*....|
gi 17539902 328 --AKQVDAFF 335
Cdd:PLN03232 1456 llSRDTSAFF 1465
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
244-292 |
2.46e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.39 E-value: 2.46e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 17539902 244 LSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIE 292
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQE 205
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
128-331 |
3.35e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.16 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 128 PGELTFIMGSSGAGKTTllnilTGRNL-KNIET-DGDIMINGRNMISNEMKKLSAyVQQDDVFI-----GTLTVRETLRF 200
Cdd:PRK10261 349 PGETLSLVGESGSGKST-----TGRALlRLVESqGGEIIFNGQRIDTLSPGKLQA-LRRDIQFIfqdpyASLDPRQTVGD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 201 A--AKLRSPSALGATELDSIVDELLvmmslkkcenTKVGTMTEKS------LSRGERKRLAFACEILTDPPILFCDEPTS 272
Cdd:PRK10261 423 SimEPLRVHGLLPGKAAAARVAWLL----------ERVGLLPEHAwrypheFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17539902 273 GLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSVYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAV 551
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
128-326 |
3.88e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.04 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 128 PGELTFIMGSSGAGKTTLLNILTGRnLKNIeTDGDIMINGRnmisnemkklSAYVQQDDvFIGTLTVRETLRFAAKLRSP 207
Cdd:PLN03130 642 VGSLVAIVGSTGEGKTSLISAMLGE-LPPR-SDASVVIRGT----------VAYVPQVS-WIFNATVRDNILFGSPFDPE 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 208 ---SALGATELDSIVDellvmmSLKKCENTKVGtmtEK--SLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQV 282
Cdd:PLN03130 709 ryeRAIDVTALQHDLD------LLPGGDLTEIG---ERgvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQV 779
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17539902 283 IKALRQLTIEGKTVICTIHQpstsvYHM---ADQLILLSQGHVAYAG 326
Cdd:PLN03130 780 FDKCIKDELRGKTRVLVTNQ-----LHFlsqVDRIILVHEGMIKEEG 821
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
108-322 |
4.86e-05 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 45.44 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 108 VLKKKGVRqEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNlkniETDGDIMINGRNMISNEMKKLSAYVQQ--- 184
Cdd:PRK11247 18 VSKRYGER-TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLE----TPSAGELLAGTAPLAEAREDTRLMFQDarl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 185 -------DDVFIGtltvretLRFAAKLRSPSALGATELDSIVDELlvmmslkkcentkvgtmtEKSLSRGERKRLAFACE 257
Cdd:PRK11247 93 lpwkkviDNVGLG-------LKGQWRDAALQALAAVGLADRANEW------------------PAALSGGQKQRVALARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17539902 258 ILTDPPILFCDEPTSGLDSF----MsHQVIKALRQLtiEGKTVICTIHQPSTSVyHMADQLILLSQGHV 322
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALtrieM-QDLIESLWQQ--HGFTVLLVTHDVSEAV-AMADRVLLIEEGKI 212
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
128-306 |
5.12e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.90 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 128 PGELTFIMGSSGAGKTTLLNILtGRNLkNIETDGDIMINGRNMISNEMKKLSAyvqqddvfigtltvretlrfaaklrsp 207
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL-AREL-GPPGGGVIYIDGEDILEEVLDQLLL--------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 208 salgateldsivdellvmmslkkcentKVGTMTEKSLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALR 287
Cdd:smart00382 52 ---------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEE 104
|
170 180
....*....|....*....|....*
gi 17539902 288 QLTI------EGKTVICTIHQPSTS 306
Cdd:smart00382 105 LRLLlllkseKNLTVILTTNDEKDL 129
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
118-326 |
5.58e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.83 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 118 ILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlKNIETDGDIMINGRNMISNEMKKLSAYVQQDDVFIGtLTVREt 197
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMG---ELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFG-LSYDE- 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 198 lrfaakLRSPSALGATELdsivDELLVMMSLKKCENTKVGTMTeksLSRGERKRLAFACEILTDPPILFCDEPTSGLDSF 277
Cdd:TIGR01271 516 ------YRYTSVIKACQL----EEDIALFPEKDKTVLGEGGIT---LSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17539902 278 MSHQVIKALRQLTIEGKTVICTihqpSTSVYHM--ADQLILLSQGHVAYAG 326
Cdd:TIGR01271 583 TEKEIFESCLCKLMSNKTRILV----TSKLEHLkkADKILLLHEGVCYFYG 629
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
104-323 |
9.30e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.39 E-value: 9.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 104 IQAVVLKKKGV-RQEILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGRNLKnieTDGDIMINGRnmisnEMKKLS--- 179
Cdd:COG1129 252 PGEVVLEVEGLsVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPA---DSGEIRLDGK-----PVRIRSprd 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 180 ------AYVQQD---DVFIGTLTVRE--TLRFAAKLRSPSALGATELDSIVDELLVMMSLK-KCENTKVGTmteksLSRG 247
Cdd:COG1129 324 airagiAYVPEDrkgEGLVLDLSIREniTLASLDRLSRGGLLDRRRERALAEEYIKRLRIKtPSPEQPVGN-----LSGG 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 248 ERKRLAFACEILTDPPILFCDEPTSGLDsfmshqvIKA-------LRQLTIEGKTVICTihqpsTS----VYHMADQLIL 316
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPTRGID-------VGAkaeiyrlIRELAAEGKAVIVI-----SSelpeLLGLSDRILV 466
|
....*..
gi 17539902 317 LSQGHVA 323
Cdd:COG1129 467 MREGRIV 473
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
118-326 |
1.21e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 44.46 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 118 ILKKIDGVARPGELTFIMGSSGAGKTTLLNILTGrnlKNIETDGDIMINGRNMISNEMKklsayvqqddvFIGTLTVRET 197
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILG---ELEPSEGKIKHSGRISFSSQFS-----------WIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 198 LRFAA---KLRSPSALGATELDSIVdellvmMSLKKCENTKVGTmTEKSLSRGERKRLAFACEILTDPPILFCDEPTSGL 274
Cdd:cd03291 118 IIFGVsydEYRYKSVVKACQLEEDI------TKFPEKDNTVLGE-GGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17539902 275 DSFMSHQVIKALRQLTIEGKTVICTihqpSTSVYHM--ADQLILLSQGHVAYAG 326
Cdd:cd03291 191 DVFTEKEIFESCVCKLMANKTRILV----TSKMEHLkkADKILILHEGSSYFYG 240
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
243-329 |
1.41e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 43.33 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 243 SLSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSVYHMADQLillsqgHV 322
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRI------HV 144
|
....*..
gi 17539902 323 AYAGPAK 329
Cdd:cd03222 145 FEGEPGV 151
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
120-297 |
3.08e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 120 KKIDGV---ARPGELTFIMGSSGAGKTTLLNILTGRNL-KNIEtdGDIMINGR----NMISNEMKKLSAYVQQDDVFIGt 191
Cdd:NF040905 274 KVVDDVslnVRRGEIVGIAGLMGAGRTELAMSVFGRSYgRNIS--GTVFKDGKevdvSTVSDAIDAGLAYVTEDRKGYG- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 192 LTVRETLRF---AAKLRSPSALGateldsIVD---ELLVMMSLKKCENTKVGTMTEK--SLSRGERKRLAFACEILTDPP 263
Cdd:NF040905 351 LNLIDDIKRnitLANLGKVSRRG------VIDeneEIKVAEEYRKKMNIKTPSVFQKvgNLSGGNQQKVVLSKWLFTDPD 424
|
170 180 190
....*....|....*....|....*....|....
gi 17539902 264 ILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVI 297
Cdd:NF040905 425 VLILDEPTRGIDVGAKYEIYTIINELAAEGKGVI 458
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
244-331 |
4.63e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.31 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 244 LSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSVYHMADQLILLSQGHVA 323
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
....*...
gi 17539902 324 YAGPAKQV 331
Cdd:PRK10261 249 ETGSVEQI 256
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
244-331 |
8.90e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.04 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 244 LSRGERKRLAFACEILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPSTSVYHMADQLILLSQGHVA 323
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
....*...
gi 17539902 324 YAGPAKQV 331
Cdd:PRK11022 234 ETGKAHDI 241
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
219-304 |
1.85e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.84 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 219 VDELLVMMSLKKCENTKVGTMTEKSLSRGERK--RLAFAC-EILTDPPILFCDEPTSGLDSFMSHQVIKALRQLTIEGKT 295
Cdd:pfam13304 212 VDDRLRERGLILLENGGGGELPAFELSDGTKRllALLAALlSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQ 291
|
....*....
gi 17539902 296 VICTIHQPS 304
Cdd:pfam13304 292 LILTTHSPL 300
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
122-331 |
2.11e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 40.45 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 122 IDGVA---RPGELTFIMGSSGAGKT----TLLNIL-TGRNlkniETDGDIMINGRNMISNEMK-KLSAYVQQD--DVFIG 190
Cdd:PRK10418 19 VHGVSltlQRGRVLALVGGSGSGKSltcaAALGILpAGVR----QTAGRVLLDGKPVAPCALRgRKIATIMQNprSAFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 191 TLT----VRETLRFAAKLRS----PSALGATELDSiVDELLVMMSLKkcentkvgtmteksLSRGERKRLAFACEILTDP 262
Cdd:PRK10418 95 LHTmhthARETCLALGKPADdatlTAALEAVGLEN-AARVLKLYPFE--------------MSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 263 PILFCDEPTSGLDSFMSHQVIKALRQLTIE-GKTVICTIHQPSTsVYHMADQLILLSQGHVAYAGPAKQV 331
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGV-VARLADDVAVMSHGRIVEQGDVETL 228
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
129-163 |
2.52e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 39.69 E-value: 2.52e-03
10 20 30
....*....|....*....|....*....|....*
gi 17539902 129 GELTFIMGSSGAGKTTLLNILTGRNlkNIETdGDI 163
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLLNALLPEL--VLAT-GEI 116
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
119-323 |
2.55e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 40.96 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 119 LKKIDGVA---RPGELTFIMGSSGAGKTTLLNILTGRNLKNiETDGDIMINGRNM----ISNEMKKLSAYVQQDDVFIGT 191
Cdd:TIGR02633 14 VKALDGIDlevRPGECVGLCGENGAGKSTLMKILSGVYPHG-TWDGEIYWSGSPLkasnIRDTERAGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539902 192 LTVRETLRFAAKLRSPSalGATELDSIV---DELLVMMSLKKCENTK-VGtmtekSLSRGERKRLAFACEILTDPPILFC 267
Cdd:TIGR02633 93 LSVAENIFLGNEITLPG--GRMAYNAMYlraKNLLRELQLDADNVTRpVG-----DYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17539902 268 DEPTSGLDSFMSHQVIKALRQLTIEGKTVICTIHQPStSVYHMADQLILLSQG-HVA 323
Cdd:TIGR02633 166 DEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLN-EVKAVCDTICVIRDGqHVA 221
|
|
| EutP |
COG4917 |
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ... |
133-155 |
5.61e-03 |
|
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];
Pssm-ID: 443945 [Multi-domain] Cd Length: 145 Bit Score: 37.86 E-value: 5.61e-03
10 20
....*....|....*....|...
gi 17539902 133 FIMGSSGAGKTTLLNILTGRNLK 155
Cdd:COG4917 5 MLIGRSGAGKTTLTQALNGEELE 27
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
129-152 |
8.84e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.91 E-value: 8.84e-03
10 20
....*....|....*....|....
gi 17539902 129 GELTFIMGSSGAGKTTLLNILTGR 152
Cdd:pfam03193 106 GKTTVLAGQSGVGKSTLLNALLPE 129
|
|
| |
