|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
55-649 |
6.43e-146 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 437.17 E-value: 6.43e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 55 CRKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARkDPSGL--SGDVLINGAPRPAN-FKCNSGYVVQDDVV 130
Cdd:TIGR00955 32 CRERPRKHLLKNVSGVAKPGeLLAVMGSSGAGKTTLMNALAFR-SPKGVkgSGSVLLNGMPIDAKeMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 131 MGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQ-FIRGVSGGERKRTSIGMELITDPSILFL 209
Cdd:TIGR00955 111 IPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPgRVKGLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 210 DEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNN 289
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYN 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 290 PADFFLDIIngdstAVALNREEDFKATeiiepskqdkplIEKLAEIYVNSSFYKETKAELHQLSGGEKK--KKITVFKEI 367
Cdd:TIGR00955 271 PADFYVQVL-----AVIPGSENESRER------------IEKICDSFAVSDIGRDMLVNTNLWSGKAGGlvKDSENMEGI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 368 SYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSV-SAVE 446
Cdd:TIGR00955 334 GYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALFLFLTNMTFQNVfPVIN 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 447 LFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPsIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALA 526
Cdd:TIGR00955 414 VFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILP-ALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYL 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 527 IAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYa 606
Cdd:TIGR00955 493 ISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVDNIECTSANTTGPCPS- 571
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1149890125 607 tcTGEEYLVKQGIDLSPwgLWKNHVALACMIVIFLTIAYLKLL 649
Cdd:TIGR00955 572 --SGEVILETLSFRNAD--LYLDLIGLVILIFFFRLLAYFALR 610
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
37-652 |
1.74e-92 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 299.87 E-value: 1.74e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 37 LSFHNICYRVKL---KSGFLPCRKPV--------------EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKD 98
Cdd:PLN03211 40 LKFMDVCYRVKFenmKNKGSNIKRILghkpkisdetrqiqERTILNGVTGMASPGeILAVLGPSGSGKSTLLNALAGRIQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 99 PSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKV 178
Cdd:PLN03211 120 GNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTII 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 179 GTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTL 258
Cdd:PLN03211 200 GNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 259 LASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIING--DSTAVALNREEDFKATEIiepSKQDKPLIEKLAEIY 336
Cdd:PLN03211 280 LSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDLANGvcQTDGVSEREKPNVKQSLV---ASYNTLLAPKVKAAI 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 337 VNSSFYKETKAELHQLSGGEKKKKITvfkeISYTTSFcHQLRWVSKRSFK-------NLLgnpqaSIAQIIVTVVLGlvi 409
Cdd:PLN03211 357 EMSHFPQANARFVGSASTKEHRSSDR----ISISTWF-NQFSILLQRSLKerkhesfNTL-----RVFQVIAAALLA--- 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 410 GAIYFglKNDSTGIQNRAGVLFFLTTN-QCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDlLPMRMLPSII 488
Cdd:PLN03211 424 GLMWW--HSDFRDVQDRLGLLFFISIFwGVFPSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGD-LPMELILPTI 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 489 FTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNltTIASWLSWL 568
Cdd:PLN03211 501 FLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGFYVH--KLPSCMAWI 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 569 QYFSIPRYGFTAL---QHNEflGQNFCPGLNATGNNPCNYATCTgeeyLVKQGI--DLSPwglWKNHVALACMIVIFLTI 643
Cdd:PLN03211 579 KYISTTFYSYRLLinvQYGE--GKRISSLLGCSLPHGSDRASCK----FVEEDVagQISP---ATSVSVLIFMFVGYRLL 649
|
....*....
gi 1149890125 644 AYLKLLFLK 652
Cdd:PLN03211 650 AYLALRRIK 658
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-568 |
9.94e-88 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 298.95 E-value: 9.94e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 27 DLKAFTEGAVLSFHNICYRVKLKSGflpcrkpvEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDpSGL--S 103
Cdd:TIGR00956 750 DMEKESGEDIFHWRNLTYEVKIKKE--------KRVILNNVDGWVKPGtLTALMGASGAGKTTLLNVLAERVT-TGVitG 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 104 GDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFI 183
Cdd:TIGR00956 821 GDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGE 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 184 rGVSGGERKRTSIGMELITDP-SILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASG 262
Cdd:TIGR00956 901 -GLNVEQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKG 979
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 263 -RLMFHGP----AQEALGYFESAGYH-CEAYNNPADFFLDIINGDSTAVAlnrEEDFkateiiepskqdkplieklAEIY 336
Cdd:TIGR00956 980 gQTVYFGDlgenSHTIINYFEKHGAPkCPEDANPAEWMLEVIGAAPGAHA---NQDY-------------------HEVW 1037
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 337 VNSSFYKETKAELHQ----LSGGEKKKKITVFKEisYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAI 412
Cdd:TIGR00956 1038 RNSSEYQAVKNELDRleaeLSKAEDDNDPDALSK--YAASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFT 1115
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 413 YFGLKNDSTGIQNRAG-----VLFFLTTNQcfssvSAVELFVVEKKLF-IHEYISGYYRVSSYFLGKLLSDlLPMRMLPS 486
Cdd:TIGR00956 1116 FFKVGTSLQGLQNQMFavfmaTVLFNPLIQ-----QYLPPFVAQRDLYeVRERPSRTFSWLAFIAAQITVE-IPYNLVAG 1189
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 487 IIFTCIVYFMLGLKPKA-------DAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLT 559
Cdd:TIGR00956 1190 TIFFFIWYYPVGFYWNAsktgqvhERGVLFWLLSTMFFLYFSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPS 1269
|
....*....
gi 1149890125 560 TIASWLSWL 568
Cdd:TIGR00956 1270 RMPGFWIFM 1278
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
34-268 |
5.28e-87 |
|
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: 269.81 E-value: 5.28e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 34 GAVLSFHNIcyRVKLKSGflpcRKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAP 112
Cdd:cd03213 1 GVTLSFRNL--TVTVKSS----PSKSGKQLLKNVSGKAKPGeLTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 113 RPA-NFKCNSGYVVQDDVVMGTLTVRENLQFSAALRlattmtnheknerinrviqelgldkvadskvgtqfirGVSGGER 191
Cdd:cd03213 75 LDKrSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR-------------------------------------GLSGGER 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149890125 192 KRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHG 268
Cdd:cd03213 118 KRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
51-652 |
4.22e-82 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 283.15 E-value: 4.22e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 51 GFLPCRKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPS--GLSGDVLINGAPrPANFK----CNSGY 123
Cdd:TIGR00956 64 KLKKFRDTKTFDILKPMDGLIKPGeLTVVLGRPGSGCSTLLKTIASNTDGFhiGVEGVITYDGIT-PEEIKkhyrGDVVY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 124 VVQDDVVMGTLTVRENLQFSAALRL-ATTMTNHEKNERINRV----IQELGLDKVADSKVGTQFIRGVSGGERKRTSIGM 198
Cdd:TIGR00956 143 NAETDVHFPHLTVGETLDFAARCKTpQNRPDGVSREEYAKHIadvyMATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 199 ELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIF-SIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYF 277
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLvAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYF 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 278 ESAGYHCEAYNNPADFFLDIINgdstavalnreedfKATEIIEPSKQDKPLI--EKLAEIYVNSSFYKETKAELHQ-LSG 354
Cdd:TIGR00956 303 EKMGFKCPDRQTTADFLTSLTS--------------PAERQIKPGYEKKVPRtpQEFETYWRNSPEYAQLMKEIDEyLDR 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 355 GEKKKKITVFKEI-------------SYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDST 421
Cdd:TIGR00956 369 CSESDTKEAYREShvakqskrtrpssPYTVSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTS 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 422 GIQNRAGVLFFLTTNQCFSSVSavELFVVEKKLFIHEYISGY--YRVSSYFLGKLLSDlLPMRMLPSIIFTCIVYFMLGL 499
Cdd:TIGR00956 449 DFYSRGGALFFAILFNAFSSLL--EIASMYEARPIVEKHRKYalYHPSADAIASIISE-IPFKIIESVVFNIILYFMVNF 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 500 KPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFT 579
Cdd:TIGR00956 526 RRTAGRFFFYLLILFICTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFE 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 580 ALQHNEFLGQNF-CPGLNATG----NNPCNYATCT------------GEEYLvKQGIDLSPWGLWKNHVALACMIVIFLT 642
Cdd:TIGR00956 606 SLMVNEFHGRRFeCSQYVPSGggydNLGVTNKVCTvvgaepgqdyvdGDDYL-KLSFQYYNSHKWRNFGIIIGFTVFFFF 684
|
650
....*....|
gi 1149890125 643 IAYLKLLFLK 652
Cdd:TIGR00956 685 VYILLTEFNK 694
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
55-268 |
1.79e-67 |
|
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: 220.22 E-value: 1.79e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 55 CRKPVEKE----ILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSG-LSGDVLINGAPR-PANFKCNSGYVVQD 127
Cdd:cd03234 10 GLKAKNWNkyarILNDVSLHVESGqVMAILGSSGSGKTTLLDAISGRVEGGGtTSGQILFNGQPRkPDQFQKCVAYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 128 DVVMGTLTVRENLQFSAALRLattmTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSIL 207
Cdd:cd03234 90 DILLPGLTVRETLTYTAILRL----PRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149890125 208 FLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHG 268
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
34-262 |
3.39e-64 |
|
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: 210.18 E-value: 3.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 34 GAVLSFHNICYRVKLKSGflpcrkpvEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAP 112
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGG--------KRQLLNNISGYVKPGtLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 113 RPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALrlattmtnheknerinrviqelgldkvadskvgtqfiRGVSGGERK 192
Cdd:cd03232 73 LDKNFQRSTGYVEQQDVHSPNLTVREALRFSALL-------------------------------------RGLSVEQRK 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 193 RTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASG 262
Cdd:cd03232 116 RLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRG 185
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
62-573 |
3.20e-59 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 215.87 E-value: 3.20e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 62 EILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAP-RPANFKCNSGYVVQDDVVMGTLTVREN 139
Cdd:PLN03140 894 QLLREVTGAFRPGvLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFPkKQETFARISGYCEQNDIHSPQVTVRES 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 140 LQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSS 219
Cdd:PLN03140 974 LIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 220 TANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLA-SGRLMFHGP----AQEALGYFES---AGYHCEAYnNPA 291
Cdd:PLN03140 1054 AAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKrGGQVIYSGPlgrnSHKIIEYFEAipgVPKIKEKY-NPA 1132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 292 DFFLDIingDSTAVALNREEDFkateiiepskqdkplieklAEIYVNSSFYKETKAELHQLSGGEKKKKITVFkEISYTT 371
Cdd:PLN03140 1133 TWMLEV---SSLAAEVKLGIDF-------------------AEHYKSSSLYQRNKALVKELSTPPPGASDLYF-ATQYSQ 1189
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 372 SFCHQLR-------WVSKRSfknllgnPQASIAQIIVTVVLGLVIGAIYF--GLKNDSTG-----IQNRAGVLFFLTTNQ 437
Cdd:PLN03140 1190 STWGQFKsclwkqwWTYWRS-------PDYNLVRFFFTLAAALMVGTIFWkvGTKRSNANdltmvIGAMYAAVLFVGINN 1262
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 438 CfSSVSAVelFVVEKKLFIHEYISGYYRVSSYFLGKLLSDlLPMRMLPSIIFTCIVYFMLGLKPKADAF----FVMMFTL 513
Cdd:PLN03140 1263 C-STVQPM--VAVERTVFYRERAAGMYSALPYAIAQVVCE-IPYVLIQTTYYTLIVYAMVAFEWTAAKFfwfyFISFFSF 1338
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 514 MMVAYSAsSMALAIAAGQsvvSVATLLMTICFVFMMIFSGLLVNLTTIASWlsWLQYFSI 573
Cdd:PLN03140 1339 LYFTYYG-MMTVSLTPNQ---QVAAIFAAAFYGLFNLFSGFFIPRPKIPKW--WVWYYWI 1392
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
63-651 |
1.10e-49 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 187.36 E-value: 1.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 63 ILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPS-GLSGDVLING------APRPAnfkcnSGYVVQDDVVMGTL 134
Cdd:PLN03140 180 ILKDASGIIKPSrMTLLLGPPSSGKTTLLLALAGKLDPSlKVSGEITYNGyrlnefVPRKT-----SAYISQNDVHVGVM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 135 TVRENLQFSA---------------ALR----------------LATTMTNHEKNERINRVIQELGLDKVADSKVGTQFI 183
Cdd:PLN03140 255 TVKETLDFSArcqgvgtrydllselARRekdagifpeaevdlfmKATAMEGVKSSLITDYTLKILGLDICKDTIVGDEMI 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 184 RGVSGGERKRTSIGmELITDPS-ILFLDEPTTGLDSSTANAVLLLLKRMSKQGR-TIIFSIHQPRYSIFKLFDSLTLLAS 261
Cdd:PLN03140 335 RGISGGQKKRVTTG-EMIVGPTkTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEaTVLMSLLQPAPETFDLFDDIILLSE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 262 GRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIIN-GDSTAVALNREEDFKATEIIEpskqdkpLIEKLAEIYVNSS 340
Cdd:PLN03140 414 GQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTSkKDQEQYWADRNKPYRYISVSE-------FAERFKSFHVGMQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 341 FYKETKAELHQLSGgekKKKITVFKEISYTTS----FCHQLRWV-SKRsfknllgNPQASIAQIIVTVVLGLVIGAIYF- 414
Cdd:PLN03140 487 LENELSVPFDKSQS---HKAALVFSKYSVPKMellkACWDKEWLlMKR-------NAFVYVFKTVQIIIVAAIASTVFLr 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 415 ---GLKNDSTGIQNRAGVLFFLTTNQcFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDlLPMRMLPSIIFTC 491
Cdd:PLN03140 557 temHTRNEEDGALYIGALLFSMIINM-FNGFAELALMIQRLPVFYKQRDLLFHPPWTFTLPTFLLG-IPISIIESVVWVV 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 492 IVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATL--LMTICFVFMMifSGLLVNLTTIASWLSWLQ 569
Cdd:PLN03140 635 ITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTggALVLLLVFLL--GGFILPKGEIPNWWEWAY 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 570 YFSIPRYGFTALQHNEFLGQNFCPGLNAtgnnpcNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLL 649
Cdd:PLN03140 713 WVSPLSYGFNALAVNEMFAPRWMNKMAS------DNSTRLGTAVLNIFDVFTDKNWYWIGVGALLGFTILFNVLFTLALT 786
|
..
gi 1149890125 650 FL 651
Cdd:PLN03140 787 YL 788
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
380-584 |
1.31e-45 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 160.90 E-value: 1.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 380 VSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNdSTGIQNRAGVLFFLTTNQCFSSVSAVEL-FVVEKKLFIHE 458
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGN-QQGGLNRPGLLFFSILFNAFSALSGISPvFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 459 YISGYYRVSSYFLGKLLSDLlPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVAT 538
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSEL-PLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDAS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1149890125 539 LLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHN 584
Cdd:pfam01061 159 QLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
61-302 |
9.82e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 156.76 E-value: 9.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 61 KEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP---RPANFKCNSGYVVQDDVVMGTLTV 136
Cdd:COG1131 13 KTALDGVSLTVEPGeIFGLLGPNGAGKTTTIRMLLGLLRPT--SGEVRVLGEDvarDPAEVRRRIGYVPQEPALYPDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 137 RENLQFSAALRlatTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGL 216
Cdd:COG1131 91 RENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRKVGT-----LSGGMKQRLGLALALLHDPELLILDEPTSGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 217 DSSTANAVLLLLKRMSKQGRTIIFSIHQPRYsIFKLFDSLTLLASGRLMFHGPAQEAL-GYFEsagyhceaynnpaDFFL 295
Cdd:COG1131 163 DPEARRELWELLRELAAEGKTVLLSTHYLEE-AERLCDRVAIIDKGRIVADGTPDELKaRLLE-------------DVFL 228
|
....*..
gi 1149890125 296 DIINGDS 302
Cdd:COG1131 229 ELTGEEA 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
60-301 |
2.59e-41 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 150.39 E-value: 2.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP---RPANFKCNSGYVVQDDVVMGTLT 135
Cdd:COG4555 13 KVPALKDVSFTAKDGeITGLLGPNGAGKTTLLRMLAGLLKPD--SGSILIDGEDvrkEPREARRQIGVLPDERGLYDRLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 136 VRENLQFSAALRLattMTNHEKNERINRVIQELGLDKVADSKVGtqfirGVSGGERKRTSIGMELITDPSILFLDEPTTG 215
Cdd:COG4555 91 VRENIRYFAELYG---LFDEELKKRIEELIELLGLEEFLDRRVG-----ELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 216 LDSSTANAVLLLLKRMSKQGRTIIFSIHQPrYSIFKLFDSLTLLASGRLMFHGPAQEalgyfesagyHCEAYNNP--ADF 293
Cdd:COG4555 163 LDVMARRLLREILRALKKEGKTVLFSSHIM-QEVEALCDRVVILHKGKVVAQGSLDE----------LREEIGEEnlEDA 231
|
....*...
gi 1149890125 294 FLDIINGD 301
Cdd:COG4555 232 FVALIGSE 239
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
52-268 |
2.17e-40 |
|
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: 146.25 E-value: 2.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 52 FLPCRKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSG-LSGDVLINGAP-RPANFKCNSG--YVVQ 126
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGeMVLVLGRPGSGCSTLLKALANRTEGNVsVEGDIHYNGIPyKEFAEKYPGEiiYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 127 DDVVMGTLTVRENLQFSAALRlattmtnheknerinrviqelgldkvadskvGTQFIRGVSGGERKRTSIGMELITDPSI 206
Cdd:cd03233 91 EDVHFPTLTVRETLDFALRCK-------------------------------GNEFVRGISGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149890125 207 LFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHG 268
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
77-272 |
1.66e-32 |
|
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: 124.92 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLING---APRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRlatTMT 153
Cdd:cd03263 32 GLLGHNGAGKTTTLKMLTGELRPT--SGTAYINGysiRTDRKAARQSLGYCPQFDALFDELTVREHLRFYARLK---GLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 154 NHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMsK 233
Cdd:cd03263 107 KSEIKEEVELLLRVLGLTDKANKRART-----LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV-R 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 1149890125 234 QGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:cd03263 181 KGRSIILTTHSMD-EAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
61-268 |
2.97e-32 |
|
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: 123.84 E-value: 2.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 61 KEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP---RPANFKCNSGYVVQDDVVMGTLTVR 137
Cdd:cd03264 13 KRALDGVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPPS--SGTIRIDGQDvlkQPQKLRRRIGYLPQEFGVYPNFTVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 138 ENLQFSAALRlatTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:cd03264 91 EFLDYIAWLK---GIPSKEVKARVDEVLELVNLGDRAKKKIGS-----LSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1149890125 218 SSTANAVLLLLKRMSKqGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHG 268
Cdd:cd03264 163 PEERIRFRNLLSELGE-DRIVILSTHIVE-DVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
60-263 |
5.15e-31 |
|
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: 120.26 E-value: 5.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP----RPANFKCNSGYVVQD-DVVMGT 133
Cdd:cd03225 13 ARPALDDISLTIKKGeFVLIVGPNGSGKSTLLRLLNGLLGPT--SGEVLVDGKDltklSLKELRRKVGLVFQNpDDQFFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 134 LTVRENLQFSAALRlatTMTNHEKNERINRVIQELGLDKVADskvgtQFIRGVSGGERKRTSIGMELITDPSILFLDEPT 213
Cdd:cd03225 91 PTVEEEVAFGLENL---GLPEEEIEERVEEALELVGLEGLRD-----RSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1149890125 214 TGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYsIFKLFDSLTLLASGR 263
Cdd:cd03225 163 AGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDL-LLELADRVIVLEDGK 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
60-274 |
9.01e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 120.96 E-value: 9.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpsGL----SGDVLINGAPrPANFKCNSGYVVQD------- 127
Cdd:COG1121 18 GRPVLEDVSLTIPPGeFVAIVGPNGAGKSTLLKAIL------GLlpptSGTVRLFGKP-PRRARRRIGYVPQRaevdwdf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 128 -----DVVMGTLTVRENL--QFSAALRlattmtnheknERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMEL 200
Cdd:COG1121 91 pitvrDVVLMGRYGRRGLfrRPSRADR-----------EAVDEALERVGLEDLADRPIGE-----LSGGQQQRVLLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149890125 201 ITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLAsGRLMFHGPAQEAL 274
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLG-AVREYFDRVLLLN-RGLVAHGPPEEVL 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
36-274 |
1.86e-30 |
|
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: 120.15 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 36 VLSFHNICYRVKlksgflpcrkpvEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP-- 112
Cdd:COG1120 1 MLEAENLSVGYG------------GRPVLDDVSLSLPPGeVTALLGPNGSGKSTLLRALAGLLKPS--SGEVLLDGRDla 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 113 --RPANFKCNSGYVVQDDVVMGTLTVREnlqfSAAL-RLATT----MTNHEKNERINRVIQELGLDKVADSKVGTqfirg 185
Cdd:COG1120 67 slSRRELARRIAYVPQEPPAPFGLTVRE----LVALgRYPHLglfgRPSAEDREAVEEALERTGLEHLADRPVDE----- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 186 VSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK-QGRTIIFSIHQP----RYSifklfDSLTLLA 260
Cdd:COG1120 138 LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLnlaaRYA-----DRLVLLK 212
|
250
....*....|....
gi 1149890125 261 SGRLMFHGPAQEAL 274
Cdd:COG1120 213 DGRIVAQGPPEEVL 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
35-264 |
4.79e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 118.22 E-value: 4.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 35 AVLSFHNICYRVKLKSGflpcrkpvEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP- 112
Cdd:COG1136 3 PLLELRNLTKSYGTGEG--------EVTALRGVSLSIEAGeFVAIVGPSGSGKSTLLNILGGLDRPT--SGEVLIDGQDi 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 113 -----------RPANFkcnsGYVVQDDVVMGTLTVRENLQFsaALRLATtMTNHEKNERINRVIQELGLDKVADSKVGTq 181
Cdd:COG1136 73 sslserelarlRRRHI----GFVFQFFNLLPELTALENVAL--PLLLAG-VSRKERRERARELLERVGLGDRLDHRPSQ- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 182 firgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRysIFKLFDSLTLLA 260
Cdd:COG1136 145 ----LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPE--LAARADRVIRLR 218
|
....
gi 1149890125 261 SGRL 264
Cdd:COG1136 219 DGRI 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
59-264 |
1.56e-29 |
|
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: 116.44 E-value: 1.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 59 VEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP-------RPANFKCNS-GYVVQDDV 129
Cdd:cd03255 15 EKVQALKGVSLSIEKGeFVAIVGPSGSGKSTLLNILGGLDRPT--SGEVRVDGTDisklsekELAAFRRRHiGFVFQSFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 130 VMGTLTVRENLQFsaALRLATTmTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFL 209
Cdd:cd03255 93 LLPDLTALENVEL--PLLLAGV-PKKERRERAEELLERVGLGDRLNHYPSE-----LSGGQQQRVAIARALANDPKIILA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1149890125 210 DEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRysIFKLFDSLTLLASGRL 264
Cdd:cd03255 165 DEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPE--LAEYADRIIELRDGKI 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
64-214 |
4.37e-29 |
|
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: 112.74 E-value: 4.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRPAN----FKCNSGYVVQDDVVMGTLTVRE 138
Cdd:pfam00005 1 LKNVSLTLNPGeILALVGPNGAGKSTLLKLIAGLLSPT--EGTILLDGQDLTDDerksLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149890125 139 NLQFSAALRlatTMTNHEKNERINRVIQELGLDKVADSKVGtQFIRGVSGGERKRTSIGMELITDPSILFLDEPTT 214
Cdd:pfam00005 79 NLRLGLLLK---GLSKREKDARAEEALEKLGLGDLADRPVG-ERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
61-264 |
4.84e-29 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 113.65 E-value: 4.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 61 KEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP---RPANFKCNSGYVVQDDVVMGTLTV 136
Cdd:cd03230 13 KTALDDISLTVEKGeIYGLLGPNGAGKTTLIKIILGLLKPD--SGEIKVLGKDikkEPEEVKRRIGYLPEEPSLYENLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 137 RENLQFSaalrlattmtnheknerinrviqelgldkvadskvgtqfirgvsGGERKRTSIGMELITDPSILFLDEPTTGL 216
Cdd:cd03230 91 RENLKLS--------------------------------------------GGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1149890125 217 DSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRL 264
Cdd:cd03230 127 DPESRREFWELLRELKKEGKTILLSSHILE-EAERLCDRVAILNNGRI 173
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
60-245 |
5.43e-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: 114.50 E-value: 5.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpsGL----SGDVLINGAP---RPANFKCNSGYVVQDDVVM 131
Cdd:COG4133 14 ERLLFSGLSFTLAAGeALALTGPNGSGKTTLLRILA------GLlppsAGEVLWNGEPirdAREDYRRRLAYLGHADGLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 132 GTLTVRENLQFSAALRlattmTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDE 211
Cdd:COG4133 88 PELTVRENLRFWAALY-----GLRADREAIDEALEAVGLAGLADLPVRQ-----LSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190
....*....|....*....|....*....|....
gi 1149890125 212 PTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQP 245
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
72-268 |
2.62e-28 |
|
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: 112.85 E-value: 2.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 72 KPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING---APRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALR 147
Cdd:cd03266 29 KPGeVTGLLGPNGAGKTTTLRMLAGLLEPD--AGFATVDGfdvVKEPAEARRRLGFVSDSTGLYDRLTARENLEYFAGLY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 148 latTMTNHEKNERINRVIQELGLDKVADSKVGtqfirGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLL 227
Cdd:cd03266 107 ---GLKGDELTARLEELADRLGMEELLDRRVG-----GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1149890125 228 LKRMSKQGRTIIFSIHQpRYSIFKLFDSLTLLASGRLMFHG 268
Cdd:cd03266 179 IRQLRALGKCILFSTHI-MQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
61-268 |
3.26e-28 |
|
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: 112.63 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 61 KEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpsGL----SGDVLINGAPrPANFKCNSGYVVQDDVVMGT-- 133
Cdd:cd03235 12 HPVLEDVSFEVKPGeFLAIVGPNGAGKSTLLKAIL------GLlkptSGSIRVFGKP-LEKERKRIGYVPQRRSIDRDfp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 134 LTVREnlqfSAALRLATTM-----TNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILF 208
Cdd:cd03235 85 ISVRD----VVLMGLYGHKglfrrLSKADKAKVDEALERVGLSELADRQIGE-----LSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 209 LDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLAsGRLMFHG 268
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLG-LVLEYFDRVLLLN-RTVVASG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
60-272 |
4.53e-28 |
|
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: 112.60 E-value: 4.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRPAN-------FKCNSGYVVQDDVVM 131
Cdd:cd03261 12 GRTVLKGVDLDVRRGeILAIIGPSGSGKSTLLRLIVGLLRPD--SGEVLIDGEDISGLseaelyrLRRRMGMLFQSGALF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 132 GTLTVRENLQFSaaLRLATTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDE 211
Cdd:cd03261 90 DSLTVFENVAFP--LREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAE-----LSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149890125 212 PTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQpRYSIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHD-LDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
60-268 |
8.43e-28 |
|
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: 111.46 E-value: 8.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP---RPANfKCNSGYVVQDDVVMGTLT 135
Cdd:cd03259 12 SVRALDDLSLTVEPGeFLALLGPSGCGKTTLLRLIAGLERPD--SGEILIDGRDvtgVPPE-RRNIGMVFQDYALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 136 VRENLQFsaALRLATtMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTG 215
Cdd:cd03259 89 VAENIAF--GLKLRG-VPKAEIRARVRELLELVGLEGLLNRYPHE-----LSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1149890125 216 LDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHG 268
Cdd:cd03259 161 LDAKLREELREELKELQRElGITTIYVTHDQE-EALALADRIAVMNEGRIVQVG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
37-278 |
2.26e-27 |
|
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: 110.50 E-value: 2.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 37 LSFHNICYRVklksgflpcrkPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP-RP 114
Cdd:COG1122 1 IELENLSFSY-----------PGGTPALDDVSLSIEKGeFVAIIGPNGSGKSTLLRLLNGLLKPT--SGEVLVDGKDiTK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 115 ANFK---CNSGYV------------VQDDVVMGtLtvrENLQFSAAlrlattmtnhEKNERINRVIQELGLDKVADSKVG 179
Cdd:COG1122 68 KNLRelrRKVGLVfqnpddqlfaptVEEDVAFG-P---ENLGLPRE----------EIRERVEEALELVGLEHLADRPPH 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 180 TqfirgVSGGERKRTSI-GMeLITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYsIFKLFDSLTL 258
Cdd:COG1122 134 E-----LSGGQKQRVAIaGV-LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIV 206
|
250 260
....*....|....*....|
gi 1149890125 259 LASGRLMFHGPAQEALGYFE 278
Cdd:COG1122 207 LDDGRIVADGTPREVFSDYE 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
64-272 |
5.74e-27 |
|
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: 109.45 E-value: 5.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP---RPANFKCNSGyVV---QDDVVMGTLTV 136
Cdd:cd03219 16 LDDVSFSVRPGeIHGLIGPNGAGKTTLFNLISGFLRPT--SGSVLFDGEDitgLPPHEIARLG-IGrtfQIPRLFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 137 RENLQFSAALRLATTM-------TNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFL 209
Cdd:cd03219 93 LENVMVAAQARTGSGLllararrEEREARERAEELLERVGLADLADRPAGE-----LSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149890125 210 DEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:cd03219 168 DEPAAGLNPEETEELAELIRELRERGITVLLVEHDMD-VVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
60-274 |
1.12e-26 |
|
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: 108.91 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpsGL----SGDVLINGAPRPA-------NFKCNSGYVVQD 127
Cdd:COG1127 17 DRVVLDGVSLDVPRGeILAIIGGSGSGKSVLLKLII------GLlrpdSGEILVDGQDITGlsekelyELRRRIGMLFQG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 128 DVVMGTLTVRENLQFsaALRLATTMTNHEKNERINRVIQELGLDKVADskvgtQFIRGVSGGERKRTSIGMELITDPSIL 207
Cdd:COG1127 91 GALFDSLTVFENVAF--PLREHTDLSEAEIRELVLEKLELVGLPGAAD-----KMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149890125 208 FLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLD-SAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
77-272 |
1.25e-26 |
|
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: 110.56 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLING---APRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRlatTMT 153
Cdd:TIGR01188 23 GFLGPNGAGKTTTIRMLTTLLRPT--SGTARVAGydvVREPRKVRRSIGIVPQYASVDEDLTGRENLEMMGRLY---GLP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 154 NHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK 233
Cdd:TIGR01188 98 KDEAEERAEELLELFELGEAADRPVGT-----YSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRALKE 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1149890125 234 QGRTIIFSIHQpRYSIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:TIGR01188 173 EGVTILLTTHY-MEEADKLCDRIAIIDHGRIIAEGTPEE 210
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
37-243 |
1.38e-26 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 107.94 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 37 LSFHNICYRVKLKSGflpcrkpvEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP-RP 114
Cdd:cd03293 1 LEVRNVSKTYGGGGG--------AVTALEDISLSVEEGeFVALVGPSGCGKSTLLRIIAGLERPT--SGEVLVDGEPvTG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 115 ANFKCnsGYVVQDDVVMGTLTVRENLQFSAALRLATTMtnhEKNERINRVIQELGLDKVADSkvgtqFIRGVSGGERKRT 194
Cdd:cd03293 71 PGPDR--GYVFQQDALLPWLTVLDNVALGLELQGVPKA---EARERAEELLELVGLSGFENA-----YPHQLSGGMRQRV 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1149890125 195 SIGMELITDPSILFLDEPTTGLDSSTANAV-LLLLKRMSKQGRTIIFSIH 243
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLqEELLDIWRETGKTVLLVTH 190
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
16-274 |
2.42e-25 |
|
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: 110.62 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 16 NTNGFPATASNDLKAFTEGAVLSFHNICYRvklksgflpcrKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLA 94
Cdd:COG4988 316 DAPEPAAPAGTAPLPAAGPPSIELEDVSFS-----------YPGGRPALDGLSLTIPPGeRVALVGPSGAGKSTLLNLLL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 95 ARKDPSglSGDVLINGAP----RPANFKCNSGYVVQDDVVMGTlTVRENLQFSAalRLATtmtnhekNERINRVIQELGL 170
Cdd:COG4988 385 GFLPPY--SGSILINGVDlsdlDPASWRRQIAWVPQNPYLFAG-TIRENLRLGR--PDAS-------DEELEAALEAAGL 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 171 DKVA-------DSKVGTQFiRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIH 243
Cdd:COG4988 453 DEFVaalpdglDTPLGEGG-RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITH 530
|
250 260 270
....*....|....*....|....*....|.
gi 1149890125 244 QPrySIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:COG4988 531 RL--ALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
60-268 |
2.54e-25 |
|
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: 104.22 E-value: 2.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRPANFKCNS--GYVVQDDVVMGTLTV 136
Cdd:cd03268 12 KKRVLDDISLHVKKGeIYGFLGPNGAGKTTTMKIILGLIKPD--SGEITFDGKSYQKNIEALRriGALIEAPGFYPNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 137 RENLQFSAALRLAttmtnheKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGL 216
Cdd:cd03268 90 RENLRLLARLLGI-------RKKRIDEVLDVVGLKDSAKKKVKG-----FSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1149890125 217 DSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHG 268
Cdd:cd03268 158 DPDGIKELRELILSLRDQGITVLISSHLLS-EIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
60-263 |
7.71e-25 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 101.17 E-value: 7.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPrpanfkcnsgyvvqddvvmgtltvre 138
Cdd:cd00267 11 GRTALDNVSlTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT--SGEILIDGKD-------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 139 nlqfsaalrlattmtnheknerINRVIQELGLDKVAdskvgtqFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDS 218
Cdd:cd00267 63 ----------------------IAKLPLEELRRRIG-------YVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1149890125 219 STANAVLLLLKRMSKQGRTIIFSIHQPRYsIFKLFDSLTLLASGR 263
Cdd:cd00267 114 ASRERLLELLRELAEEGRTVIIVTHDPEL-AELAADRVIVLKDGK 157
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
60-263 |
7.83e-25 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 101.88 E-value: 7.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP------RPANFKCNSGYVVQDDVVMG 132
Cdd:cd03229 12 QKTVLNDVSLNIEAGeIVALLGPSGSGKSTLLRCIAGLEEPD--SGSILIDGEDltdledELPPLRRRIGMVFQDFALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 133 TLTVRENLQFsaalrlattmtnheknerinrviqelgldkvadskvgtqfirGVSGGERKRTSIGMELITDPSILFLDEP 212
Cdd:cd03229 90 HLTVLENIAL------------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1149890125 213 TTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYsIFKLFDSLTLLASGR 263
Cdd:cd03229 128 TSALDPITRREVRALLKSLQAQlGITVVLVTHDLDE-AARLADRVVVLRDGK 178
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
77-272 |
9.54e-25 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 102.83 E-value: 9.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLING---APRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRlatTMT 153
Cdd:cd03265 30 GLLGPNGAGKTTTIKMLTTLLKPT--SGRATVAGhdvVREPREVRRRIGIVFQDLSVDDELTGWENLYIHARLY---GVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 154 NHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK 233
Cdd:cd03265 105 GAERRERIDELLDFVGLLEAADRLVKT-----YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1149890125 234 -QGRTIIFSIHqprY--SIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:cd03265 180 eFGMTILLTTH---YmeEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
21-274 |
1.52e-24 |
|
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: 108.31 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 21 PATASNDLKAFTEGAVLSFHNICYRvklksgflpcRKPVEKEILSNINGIMKPG--LnAILGPTGGGKSSLLDVLAARKD 98
Cdd:COG4987 318 AVTEPAEPAPAPGGPSLELEDVSFR----------YPGAGRPVLDGLSLTLPPGerV-AIVGPSGSGKSTLLALLLRFLD 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 99 PSglSGDVLINGAP----RPANFKCNSGYVVQDDVVMGTlTVRENLQFsaALRLATtmtnhekNERINRVIQELGLDKVA 174
Cdd:COG4987 387 PQ--SGSITLGGVDlrdlDEDDLRRRIAVVPQRPHLFDT-TLRENLRL--ARPDAT-------DEELWAALERVGLGDWL 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 175 -------DSKVGTQFiRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSkQGRTIIFSIHQPry 247
Cdd:COG4987 455 aalpdglDTWLGEGG-RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRL-- 530
|
250 260
....*....|....*....|....*..
gi 1149890125 248 SIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:COG4987 531 AGLERMDRILVLEDGRIVEQGTHEELL 557
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
60-268 |
4.43e-24 |
|
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: 99.43 E-value: 4.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpsGL----SGDVLINGAPrpanfkcnsgyvvqddvvMGTL 134
Cdd:cd03214 11 GRTVLDDLSLSIEAGeIVGILGPNGAGKSTLLKTLA------GLlkpsSGEILLDGKD------------------LASL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 135 TVREnlqfsAALRLATtmtnheknerINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTT 214
Cdd:cd03214 67 SPKE-----LARKIAY----------VPQALELLGLAHLADRPFNE-----LSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1149890125 215 GLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQP----RYSifklfDSLTLLASGRLMFHG 268
Cdd:cd03214 127 HLDIAHQIELLELLRRLARErGKTVVMVLHDLnlaaRYA-----DRVILLKDGRIVAQG 180
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
61-264 |
5.92e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 100.51 E-value: 5.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 61 KEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP-------------RpanfkcNSGYVVQ 126
Cdd:COG2884 15 REALSDVSLEIEKGeFVFLTGPSGAGKSTLLKLLYGEERPT--SGQVLVNGQDlsrlkrreipylrR------RIGVVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 127 D-----DvvmgtLTVRENLQFsaALRlATTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELI 201
Cdd:COG2884 87 DfrllpD-----RTVYENVAL--PLR-VTGKSRKEIRRRVREVLDLVGLSDKAKALPHE-----LSGGEQQRVAIARALV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149890125 202 TDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQprYSIFKLFDSLTL-LASGRL 264
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHD--LELVDRMPKRVLeLEDGRL 215
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
37-274 |
8.07e-24 |
|
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: 106.46 E-value: 8.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 37 LSFHNICYRVKlksgflpcrkPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpsGL----SGDVLINGA 111
Cdd:COG2274 474 IELENVSFRYP----------GDSPPVLDNISLTIKPGeRVAIVGRSGSGKSTLLKLLL------GLyeptSGRILIDGI 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 112 PR----PANFKCNSGYVVQDDVVMGTlTVRENLQFSaalRLATTMtnheknERINRVIQELGLDKVA-------DSKVGT 180
Cdd:COG2274 538 DLrqidPASLRRQIGVVLQDVFLFSG-TIRENITLG---DPDATD------EEIIEAARLAGLHDFIealpmgyDTVVGE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 181 QFiRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMsKQGRTIIFSIHqpRYSIFKLFDSLTLLA 260
Cdd:COG2274 608 GG-SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAH--RLSTIRLADRIIVLD 683
|
250
....*....|....
gi 1149890125 261 SGRLMFHGPAQEAL 274
Cdd:COG2274 684 KGRIVEDGTHEELL 697
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
37-264 |
9.34e-24 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 99.51 E-value: 9.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 37 LSFHNICYRVKlksgflpcrkpvEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpsGL----SGDVLINGA 111
Cdd:COG4619 1 LELEGLSFRVG------------GKPILSPVSLTLEAGeCVAITGPSGSGKSTLLRALA------DLdpptSGEIYLDGK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 112 PR----PANFKCNSGYVVQDdVVMGTLTVRENLQFSAALRlattmTNHEKNERINRVIQELGLDK-VADSKVGTqfirgV 186
Cdd:COG4619 63 PLsampPPEWRRQVAYVPQE-PALWGGTVRDNLPFPFQLR-----ERKFDRERALELLERLGLPPdILDKPVER-----L 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149890125 187 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYsIFKLFDSLTLLASGRL 264
Cdd:COG4619 132 SGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQ-IERVADRVLTLEAGRL 209
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
74-268 |
9.54e-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: 99.68 E-value: 9.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 74 GLNAILGPTGGGKSSLLDVLAARKDPSGlsGDVLINGapRPANFKCNS----------GYVVQDDVVMGTLTVRENLQFs 143
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGLEKPDG--GTIVLNG--TVLFDSRKKinlppqqrkiGLVFQQYALFPHLNVRENLAF- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 144 aALRlatTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANA 223
Cdd:cd03297 99 -GLK---RKRNREDRISVDELLDLLGLDHLLNRYPAQ-----LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1149890125 224 VLLLLKRMSKQ-GRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHG 268
Cdd:cd03297 170 LLPELKQIKKNlNIPVIFVTHDLS-EAEYLADRIVVMEDGRLQYIG 214
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
57-264 |
1.01e-23 |
|
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: 99.97 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 57 KPVEKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP----RPANFKCNSGYVVQDdVVM 131
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKvAIIGRVGSGKSTLLKLLAGLYKPT--SGSVLLDGTDirqlDPADLRRNIGYVPQD-VTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 132 GTLTVRENLQFSAalRLATTmtnheknERINRVIQELGLDKVA-------DSKVGTQFiRGVSGGERKRTSIGMELITDP 204
Cdd:cd03245 90 FYGTLRDNITLGA--PLADD-------ERILRAAELAGVTDFVnkhpnglDLQIGERG-RGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 205 SILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGRL 264
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITH--RPSLLDLVDRIIVMDSGRI 216
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
32-240 |
1.36e-23 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 100.55 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 32 TEGAVLSFHNICYRVKLKSGflpcrkpvEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpsGL----SGDV 106
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGG--------GVTALDDVSLTVAAGeFVALVGPSGCGKSTLLRLIA------GLekptSGEV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 107 LINGAP--RPANfkcNSGYVVQDDVVMGTLTVRENLQFsaALRLATtMTNHEKNERINRVIQELGLDKVADSKVGTqfir 184
Cdd:COG1116 69 LVDGKPvtGPGP---DRGVVFQEPALLPWLTVLDNVAL--GLELRG-VPKAERRERARELLELVGLAGFEDAYPHQ---- 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1149890125 185 gVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTAnAVL--LLLKRMSKQGRTIIF 240
Cdd:COG1116 139 -LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTR-ERLqdELLRLWQETGKTVLF 194
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
64-243 |
2.59e-23 |
|
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: 98.63 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRpANFKCNS--------GYVVQDDVVMGTL 134
Cdd:cd03292 17 LDGINISISAGeFVFLVGPSGAGKSTLLKLIYKEELPT--SGTIRVNGQDV-SDLRGRAipylrrkiGVVFQDFRLLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 135 TVRENLQFsaALRLaTTMTNHEKNERINRVIQELGLDKVADSkvgtqFIRGVSGGERKRTSIGMELITDPSILFLDEPTT 214
Cdd:cd03292 94 NVYENVAF--ALEV-TGVPPREIRKRVPAALELVGLSHKHRA-----LPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180
....*....|....*....|....*....
gi 1149890125 215 GLDSSTANAVLLLLKRMSKQGRTIIFSIH 243
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
37-263 |
3.58e-23 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 96.68 E-value: 3.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 37 LSFHNICYRvklksgflpcRKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP--- 112
Cdd:cd03228 1 IEFKNVSFS----------YPGRPKPVLKDVSLTIKPGeKVAIVGPSGSGKSTLLKLLLRLYDPT--SGEILIDGVDlrd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 113 -RPANFKCNSGYVVQDDVVMGTlTVRENLqfsaalrlattmtnheknerinrviqelgldkvadskvgtqfirgVSGGER 191
Cdd:cd03228 69 lDLESLRKNIAYVPQDPFLFSG-TIRENI---------------------------------------------LSGGQR 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149890125 192 KRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGR 263
Cdd:cd03228 103 QRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK-GKTVIVIAH--RLSTIRDADRIIVLDDGR 171
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
56-280 |
5.23e-23 |
|
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: 98.72 E-value: 5.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 56 RKPVEKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAarkdpsGL----SGDVLINGAP----RPANFKCNSGYVVQ 126
Cdd:COG1124 13 QGGRRVPVLKDVSLEVAPGESfGLVGESGSGKSTLLRALA------GLerpwSGEVTFDGRPvtrrRRKAFRRRVQMVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 127 DdvVMGTL----TVRENLqfSAALRLaTTMTNHEknERINRVIQELGLDkvadSKVGTQFIRGVSGGERKRTSIGMELIT 202
Cdd:COG1124 87 D--PYASLhprhTVDRIL--AEPLRI-HGLPDRE--ERIAELLEQVGLP----PSFLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149890125 203 DPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYsIFKLFDSLTLLASGRLMFHGPAQEALGYFESA 280
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAV-VAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
77-274 |
7.60e-23 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 97.79 E-value: 7.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA---PRPANfKCNSGYVVQDDVVMGTLTVRENLQFsaALRLATTMt 153
Cdd:cd03299 29 VILGPTGSGKSVLLETIAGFIKPD--SGKILLNGKditNLPPE-KRDISYVPQNYALFPHMTVYKNIAY--GLKKRKVD- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 154 NHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK 233
Cdd:cd03299 103 KKEIERKVLEIAEMLGIDHLLNRKPET-----LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1149890125 234 QGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:cd03299 178 EFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
60-243 |
9.76e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 98.01 E-value: 9.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP-------RpanfkcnsGYVVQDDVVM 131
Cdd:COG4525 19 PQPALQDVSLTIESGeFVVALGASGCGKTTLLNLIAGFLAPS--SGEITLDGVPvtgpgadR--------GVVFQKDALL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 132 GTLTVRENLQFsaALRLATtMTNHEKNERINRVIQELGLDKVADskvgtQFIRGVSGGERKRTSIGMELITDPSILFLDE 211
Cdd:COG4525 89 PWLNVLDNVAF--GLRLRG-VPKAERRARAEELLALVGLADFAR-----RRIWQLSGGMRQRVGIARALAADPRFLLMDE 160
|
170 180 190
....*....|....*....|....*....|...
gi 1149890125 212 PTTGLDSSTANAV-LLLLKRMSKQGRTIIFSIH 243
Cdd:COG4525 161 PFGALDALTREQMqELLLDVWQRTGKGVFLITH 193
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
64-245 |
1.13e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.76 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRPAnfkcnsgYVVQDDVVMGTL--TVRENL 140
Cdd:NF040873 8 LHGVDLTIPAGsLTAVVGPNGSGKSTLLKVLAGVLRPT--SGTVRRAGGARVA-------YVPQRSEVPDSLplTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 141 QFSA-ALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSS 219
Cdd:NF040873 79 AMGRwARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGE-----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180
....*....|....*....|....*.
gi 1149890125 220 TANAVLLLLKRMSKQGRTIIFSIHQP 245
Cdd:NF040873 154 SRERIIALLAEEHARGATVVVVTHDL 179
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
61-272 |
1.90e-22 |
|
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: 96.87 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 61 KEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRPA-------NFKCNSGYVVQDDVVMG 132
Cdd:cd03256 14 KKALKDVSLSINPGeFVALIGPSGAGKSTLLRCLNGLVEPT--SGSVLIDGTDINKlkgkalrQLRRQIGMIFQQFNLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 133 TLTVRENLQFSAALRLAT--TMTNHEKNERINRVIQEL---GLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSIL 207
Cdd:cd03256 92 RLSVLENVLSGRLGRRSTwrSLFGLFPKEEKQRALAALervGLLDKAYQRADQ-----LSGGQQQRVAIARALMQQPKLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149890125 208 FLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYsIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:cd03256 167 LADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDL-AREYADRIVGLKDGRIVFDGPPAE 231
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
60-274 |
6.22e-22 |
|
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: 94.99 E-value: 6.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP-RpaNFKCNS-----GYVVQDDVVMG 132
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKvAIVGPSGSGKSTILRLLFRFYDVS--SGSILIDGQDiR--EVTLDSlrraiGVVPQDTVLFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 133 TlTVRENLQFSaalRLATT---MTNHEKNERINRVIqeLGLDKVADSKVGTqfiRGV--SGGERKRTSIGMELITDPSIL 207
Cdd:cd03253 89 D-TIGYNIRYG---RPDATdeeVIEAAKAAQIHDKI--MRFPDGYDTIVGE---RGLklSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149890125 208 FLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAH--RLSTIVNADKIIVLKDGRIVERGTHEELL 223
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
36-240 |
6.94e-22 |
|
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: 94.88 E-value: 6.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 36 VLSFHNIcyRVKLKSGFLPCRkpvekeILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRP 114
Cdd:cd03257 1 LLEVKNL--SVSFPTGGGSVK------ALDDVSFSIKKGETlGLVGESGSGKSTLARAILGLLKPT--SGSIIFDGKDLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 115 AN-------FKCNSGYVVQDdvVMGTL----TVREnlQFSAALRLATTMTNHEKNERInrviQELGLDKV-ADSKVGTQF 182
Cdd:cd03257 71 KLsrrlrkiRRKEIQMVFQD--PMSSLnprmTIGE--QIAEPLRIHGKLSKKEARKEA----VLLLLVGVgLPEEVLNRY 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1149890125 183 IRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIF 240
Cdd:cd03257 143 PHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLF 201
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
77-268 |
8.97e-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: 94.10 E-value: 8.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLING--------APRPANFkcnsgyVVQDDVVMGTLTVREN--LQFSAAL 146
Cdd:cd03298 28 AIVGPSGSGKSTLLNLIAGFETPQ--SGRVLINGvdvtaappADRPVSM------LFQENNLFAHLTVEQNvgLGLSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 147 RLattmtNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL- 225
Cdd:cd03298 100 KL-----TAEDRQAIEVALARVGLAGLEKRLPGE-----LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLd 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1149890125 226 LLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHG 268
Cdd:cd03298 170 LVLDLHAETKMTVLMVTHQPE-DAKRLAQRVVFLDNGRIAAQG 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
60-275 |
5.07e-21 |
|
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: 96.90 E-value: 5.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSG-LSGDVLING----APRPANFKCNSGYVVQD-DVVMG 132
Cdd:COG1123 18 DVPAVDGVSLTIAPGeTVALVGESGSGKSTLALALMGLLPHGGrISGEVLLDGrdllELSEALRGRRIGMVFQDpMTQLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 133 TLTVRENLQFsaALRLaTTMTNHEKNERINRVIQELGLDKVADskvgtQFIRGVSGGERKRTSIGMELITDPSILFLDEP 212
Cdd:COG1123 98 PVTVGDQIAE--ALEN-LGLSRAEARARVLELLEAVGLERRLD-----RYPHQLSGGQRQRVAIAMALALDPDLLIADEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149890125 213 TTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYsIFKLFDSLTLLASGRLMFHGPAQEALG 275
Cdd:COG1123 170 TTALDVTTQAEILDLLRELQRErGTTVLLITHDLGV-VAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
61-262 |
5.96e-21 |
|
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: 91.55 E-value: 5.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 61 KEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRPAN--FKCnSGYVVQD-DVVMGTLTV 136
Cdd:cd03226 13 TEILDDLSLDLYAGeIIALTGKNGAGKTTLAKILAGLIKES--SGSILLNGKPIKAKerRKS-IGYVMQDvDYQLFTDSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 137 RENLQFSAalrlattMTNHEKNERINRVIQELGLDKVADskvgtQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGL 216
Cdd:cd03226 90 REELLLGL-------KELDAGNEQAETVLKDLDLYALKE-----RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1149890125 217 DSSTANAVLLLLKRMSKQGRTIIFSIHQPRYsIFKLFDSLTLLASG 262
Cdd:cd03226 158 DYKNMERVGELIRELAAQGKAVIVITHDYEF-LAKVCDRVLLLANG 202
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
74-275 |
6.90e-21 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 94.79 E-value: 6.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 74 GLNAILGPTGGGKSSLLDVLAARKDPSG----LSGDVLINGAPR---PANfKCNSGYVVQDDVVMGTLTVRENLQFSAal 146
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGLTRPDEgeivLNGRTLFDSRKGiflPPE-KRRIGYVFQEARLFPHLSVRGNLRYGM-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 147 rlaTTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLL 226
Cdd:TIGR02142 101 ---KRARPSERRISFERVIELLGIGHLLGRLPGR-----LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1149890125 227 LLKRMSKQGRT-IIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQEALG 275
Cdd:TIGR02142 173 YLERLHAEFGIpILYVSHSLQ-EVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
60-268 |
7.74e-21 |
|
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: 90.06 E-value: 7.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRPANFKCNSGYvvqddvvMGTLTVRE 138
Cdd:cd03247 14 EQQVLKNLSLELKQGEKiALLGRSGSGKSTLLQLLTGDLKPQ--QGEITLDGVPVSDLEKALSSL-------ISVLNQRP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 139 NLqFSAALRlattmtnheknerinrviqelgldkvadSKVGTQFirgvSGGERKRTSIGMELITDPSILFLDEPTTGLDS 218
Cdd:cd03247 85 YL-FDTTLR----------------------------NNLGRRF----SGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1149890125 219 STANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGRLMFHG 268
Cdd:cd03247 132 ITERQLLSLIFEVLK-DKTLIWITH--HLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
60-264 |
9.28e-21 |
|
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: 89.97 E-value: 9.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP----RPANFKCNSGYVVQDDVVMGTl 134
Cdd:cd03246 14 EPPVLRNVSFSIEPGeSLAIIGPSGSGKSTLARLILGLLRPT--SGRVRLDGADisqwDPNELGDHVGYLPQDDELFSG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 135 TVRENLqfsaalrlattmtnheknerinrviqelgldkvadskvgtqfirgVSGGERKRTSIGMELITDPSILFLDEPTT 214
Cdd:cd03246 91 SIAENI---------------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1149890125 215 GLDSSTANAVLLLLKRMSKQGRTIIFSIHQPrySIFKLFDSLTLLASGRL 264
Cdd:cd03246 126 HLDVEGERALNQAIAALKAAGATRIVIAHRP--ETLASADRILVLEDGRV 173
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
44-268 |
9.48e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 91.63 E-value: 9.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 44 YRVKLKSGFLPC-------RKPVEKEILSNIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGApRPa 115
Cdd:cd03267 10 YRVYSKEPGLIGslkslfkRKYREVEALKGISfTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPT--SGEVRVAGL-VP- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 116 nFKCNSGYVVQDDVVMGT-------LTVRENLQFSAAL-RLATTmtnhEKNERINRVIQELGLDKVADSKVgtqfiRGVS 187
Cdd:cd03267 86 -WKRRKKFLRRIGVVFGQktqlwwdLPVIDSFYLLAAIyDLPPA----RFKKRLDELSELLDLEELLDTPV-----RQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 188 GGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRySIFKLFDSLTLLASGRLMF 266
Cdd:cd03267 156 LGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMK-DIEALARRVLVIDKGRLLY 234
|
..
gi 1149890125 267 HG 268
Cdd:cd03267 235 DG 236
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
56-245 |
1.06e-20 |
|
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: 95.89 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 56 RKPVEKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPsgLSGDVLINGAPRPANFKCNS----GYVVQDDVV 130
Cdd:TIGR02868 343 GYPGAPPVLDGVSLDLPPGERvAILGPSGSGKSTLLATLAGLLDP--LQGEVTLDGVPVSSLDQDEVrrrvSVCAQDAHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 131 MGTlTVRENLQFSAAlrlatTMTNHEKNERINRV-----IQEL--GLDkvadSKVGTQFIRgVSGGERKRTSIGMELITD 203
Cdd:TIGR02868 421 FDT-TVRENLRLARP-----DATDEELWAALERVgladwLRALpdGLD----TVLGEGGAR-LSGGERQRLALARALLAD 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1149890125 204 PSILFLDEPTTGLDSSTANAVL-LLLKRMSkqGRTIIFSIHQP 245
Cdd:TIGR02868 490 APILLLDEPTEHLDAETADELLeDLLAALS--GRTVVLITHHL 530
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
60-274 |
1.68e-20 |
|
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: 90.75 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP---RPANFKCNS-GYVVQDDVVMGTl 134
Cdd:cd03254 15 KKPVLKDINFSIKPGeTVAIVGPTGAGKTTLINLLMRFYDPQ--KGQILIDGIDirdISRKSLRSMiGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 135 TVRENLQFSaalrlattmTNHEKNERINRVIQELGLDkvadskvgtQFIR---------------GVSGGERKRTSIGME 199
Cdd:cd03254 92 TIMENIRLG---------RPNATDEEVIEAAKEAGAH---------DFIMklpngydtvlgenggNLSQGERQLLAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149890125 200 LITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAH--RLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
77-274 |
3.25e-20 |
|
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: 89.80 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLaarkdpSGL----SGDVLINGAP---RPANFKCNSG--YVVQDDVVMGTLTVRENLQFSAALR 147
Cdd:cd03224 30 ALLGRNGAGKTTLLKTI------MGLlpprSGSIRFDGRDitgLPPHERARAGigYVPEGRRIFPELTVEENLLLGAYAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 148 lattmTNHEKNERINRVIQEL-GLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLL 226
Cdd:cd03224 104 -----RRAKRKARLERVYELFpRLKERRKQLAGT-----LSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1149890125 227 LLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:cd03224 174 AIRELRDEGVTILLVEQNAR-FALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
60-272 |
1.29e-19 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 88.01 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLL-------DVLAARKDpsglSGDVLINGAP------RPANFKCNSGYVV 125
Cdd:cd03260 12 DKHALKDISLDIPKGeITALIGPSGCGKSTLLrllnrlnDLIPGAPD----EGEVLLDGKDiydldvDVLELRRRVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 126 QDDVVMgTLTVRENLqfSAALRLATTMTNHEKNERINRVIQELGL-DKVADSKVGtqfiRGVSGGERKRTSIGMELITDP 204
Cdd:cd03260 88 QKPNPF-PGSIYDNV--AYGLRLHGIKLKEELDERVEEALRKAALwDEVKDRLHA----LGLSGGQQQRLCLARALANEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149890125 205 SILFLDEPTTGLDSSTANAVLLLLKRMSKQgRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:cd03260 161 EVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQ-QAARVADRTAFLLNGRLVEFGPTEQ 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
63-274 |
1.69e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 92.58 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 63 ILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP----RPANFKCNSGYVVQD-DVVMGTLtv 136
Cdd:PRK11160 355 VLKGLSLQIKAGEKvALLGRTGCGKSTLLQLLTRAWDPQ--QGEILLNGQPiadySEAALRQAISVVSQRvHLFSATL-- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 137 RENLQFsaALRLATtmtnhekNERINRVIQELGLDKVADSKVG-TQFI----RGVSGGERKRTSIGMELITDPSILFLDE 211
Cdd:PRK11160 431 RDNLLL--AAPNAS-------DEALIEVLQQVGLEKLLEDDKGlNAWLgeggRQLSGGEQRRLGIARALLHDAPLLLLDE 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149890125 212 PTTGLDSSTANAVLLLLKRMSkQGRTIIFSIHqpRYSIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:PRK11160 502 PTEGLDAETERQILELLAEHA-QNKTVLMITH--RLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
73-274 |
2.17e-19 |
|
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: 90.16 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 73 PGLNAILGPTGGGKSSLLDVLAarkdpsGL----SGDVLINGAP--------------RPAnfkcnsGYVVQDDVVMGTL 134
Cdd:COG4148 25 RGVTALFGPSGSGKTTLLRAIA------GLerpdSGRIRLGGEVlqdsargiflpphrRRI------GYVFQEARLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 135 TVRENLQFsaALRLATTmtnHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTT 214
Cdd:COG4148 93 SVRGNLLY--GRKRAPR---AERRISFDEVVELLGIGHLLDRRPAT-----LSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149890125 215 GLDSSTANAVLLLLKRMSKQGRT-IIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:COG4148 163 ALDLARKAEILPYLERLRDELDIpILYVSHSLD-EVARLADHVVLLEQGRVVASGPLAEVL 222
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
57-274 |
3.12e-19 |
|
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: 87.16 E-value: 3.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 57 KPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING----APRPANFKCNSGYVVQDDVVM 131
Cdd:cd03252 11 KPDGPVILDNISLRIKPGeVVGIVGRSGSGKSTLTKLIQRFYVPE--NGRVLVDGhdlaLADPAWLRRQVGVVLQENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 132 GTlTVRENLQFS----------AALRLATTmtnHEknerinrVIQEL--GLDKVadskVGTQFIrGVSGGERKRTSIGME 199
Cdd:cd03252 89 NR-SIRDNIALAdpgmsmerviEAAKLAGA---HD-------FISELpeGYDTI----VGEQGA-GLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149890125 200 LITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:cd03252 153 LIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAH--RLSTVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
60-294 |
3.55e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 89.36 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING------APRPANFkcnsGYVVQDDVVMG 132
Cdd:COG3839 15 GVEALKDIDLDIEDGeFLVLLGPSGCGKSTLLRMIAGLEDPT--SGEILIGGrdvtdlPPKDRNI----AMVFQSYALYP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 133 TLTVRENLQFsaALRLATtMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEP 212
Cdd:COG3839 89 HMTVYENIAF--PLKLRK-VPKAEIDRRVREAAELLGLEDLLDRKPKQ-----LSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 213 TTGLDsstanAVL-----LLLKRMSKQ-GRTIIFSIHQPRysifklfDSLTL------LASGRLMFHGPAQealgyfesa 280
Cdd:COG3839 161 LSNLD-----AKLrvemrAEIKRLHRRlGTTTIYVTHDQV-------EAMTLadriavMNDGRIQQVGTPE--------- 219
|
250
....*....|....
gi 1149890125 281 gyhcEAYNNPADFF 294
Cdd:COG3839 220 ----ELYDRPANLF 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
36-274 |
3.71e-19 |
|
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: 91.12 E-value: 3.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 36 VLSFHNICYRvklksgfLPCRKPVEKEILSNINGIMKPG--LnAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP- 112
Cdd:COG1123 260 LLEVRNLSKR-------YPVRGKGGVRAVDDVSLTLRRGetL-GLVGESGSGKSTLARLLLGLLRPT--SGSILFDGKDl 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 113 ------RPANFKCNSGYVVQDdvVMGTL----TVRENLQFsaALRLATTMTNHEKNERINRVIQELGLDkvadSKVGTQF 182
Cdd:COG1123 330 tklsrrSLRELRRRVQMVFQD--PYSSLnprmTVGDIIAE--PLRLHGLLSRAERRERVAELLERVGLP----PDLADRY 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 183 IRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQ----PRYSifklfDSLT 257
Cdd:COG1123 402 PHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDlavvRYIA-----DRVA 476
|
250
....*....|....*..
gi 1149890125 258 LLASGRLMFHGPAQEAL 274
Cdd:COG1123 477 VMYDGRIVEDGPTEEVF 493
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
78-243 |
4.88e-19 |
|
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: 86.15 E-value: 4.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 78 ILGPTGGGKSSLLDVLAARKDPSglSGDVLING---APRPANfKCNSGYVVQDDVVMGTLTVRENLQFSAALRlatTMTN 154
Cdd:cd03301 31 LLGPSGCGKTTTLRMIAGLEEPT--SGRIYIGGrdvTDLPPK-DRDIAMVFQNYALYPHMTVYDNIAFGLKLR---KVPK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 155 HEKNERINRVIQELGLDKVADSKVgtqfiRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ 234
Cdd:cd03301 105 DEIDERVREVAELLQIEHLLDRKP-----KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQR 179
|
170
....*....|
gi 1149890125 235 -GRTIIFSIH 243
Cdd:cd03301 180 lGTTTIYVTH 189
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
35-246 |
5.33e-19 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 86.33 E-value: 5.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 35 AVLSFHNICYRVKLKSGFLpcrkpvekEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP- 112
Cdd:COG4181 7 PIIELRGLTKTVGTGAGEL--------TILKGISLEVEAGeSVAIVGASGSGKSTLLGLLAGLDRPT--SGTVRLAGQDl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 113 -----------RPANFkcnsGYVVQDDVVMGTLTVRENLQFSAALRlattmTNHEKNERINRVIQELGLDKVADskvgtQ 181
Cdd:COG4181 77 faldedararlRARHV----GFVFQSFQLLPTLTALENVMLPLELA-----GRRDARARARALLERVGLGHRLD-----H 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149890125 182 FIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK-QGRTIIFSIHQPR 246
Cdd:COG4181 143 YPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPA 208
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
56-264 |
6.56e-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: 85.87 E-value: 6.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 56 RKPVEKEILSNIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP-------RPANFKCNS-GYVVQ 126
Cdd:TIGR02211 13 EGKLDTRVLKGVSlSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPT--SGEVLFNGQSlsklssnERAKLRNKKlGFIYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 127 DDVVMGTLTVRENLQFSAalrLATTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSI 206
Cdd:TIGR02211 91 FHHLLPDFTALENVAMPL---LIGKKSVKEAKERAYEMLEKVGLEHRINHRPSE-----LSGGERQRVAIARALVNQPSL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1149890125 207 LFLDEPTTGLDSSTANAVL-LLLKRMSKQGRTIIFSIHQPRYSifKLFDSLTLLASGRL 264
Cdd:TIGR02211 163 VLADEPTGNLDNNNAKIIFdLMLELNRELNTSFLVVTHDLELA--KKLDRVLEMKDGQL 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
60-245 |
6.66e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 85.70 E-value: 6.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpsGL----SGDVLING-APRPANFKCNSGYVVQDDVVMGT 133
Cdd:PRK13539 14 GRVLFSGLSFTLAAGeALVLTGPNGSGKTTLLRLIA------GLlppaAGTIKLDGgDIDDPDVAEACHYLGHRNAMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 134 LTVRENLQFSAALRLATtmtnhekNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPT 213
Cdd:PRK13539 88 LTVAENLEFWAAFLGGE-------ELDIAAALEAVGLAPLAHLPFGY-----LSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180 190
....*....|....*....|....*....|..
gi 1149890125 214 TGLDSSTANAVLLLLKRMSKQGRTIIFSIHQP 245
Cdd:PRK13539 156 AALDAAAVALFAELIRAHLAQGGIVIAATHIP 187
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
58-245 |
8.26e-19 |
|
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: 90.04 E-value: 8.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 58 PVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGlsGDVLINGAP----RPANFKCNSGYVVQDDVVMG 132
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGeRVALVGPSGAGKSTLLNLLLGFVDPTE--GSIAVNGVPladaDADSWRDQIAWVPQHPFLFA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 133 TlTVRENLQFsaALRLATtmtnhekNERINRVIQELGLDK-VADSKVGTQFI-----RGVSGGERKRTSIGMELITDPSI 206
Cdd:TIGR02857 410 G-TIAENIRL--ARPDAS-------DAEIREALERAGLDEfVAALPQGLDTPigeggAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190
....*....|....*....|....*....|....*....
gi 1149890125 207 LFLDEPTTGLDSSTANAVLLLLKRMSkQGRTIIFSIHQP 245
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRL 517
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
60-274 |
1.01e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.22 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPsgLSGDVLINGAPRpANFKCNS-----GYVVQDDVVMGT 133
Cdd:PRK11231 14 TKRILNDLSLSLPTGkITALIGPNGCGKSTLLKCFARLLTP--QSGTVFLGDKPI-SMLSSRQlarrlALLPQHHLTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 134 LTVRENLQF--SAALRLATTMTNHEKnERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDE 211
Cdd:PRK11231 91 ITVRELVAYgrSPWLSLWGRLSAEDN-ARVNQAMEQTRINHLADRRLTD-----LSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149890125 212 PTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQ----PRYSifklfDSLTLLASGRLMFHGPAQEAL 274
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNTQGKTVVTVLHDlnqaSRYC-----DHLVVLANGHVMAQGTPEEVM 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
60-244 |
1.38e-18 |
|
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: 84.89 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING----APRPANFKCNS--GYVVQDDVVMG 132
Cdd:cd03262 12 DFHVLKGIDLTVKKGeVVVIIGPSGSGKSTLLRCINLLEEPD--SGTIIIDGlkltDDKKNINELRQkvGMVFQQFNLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 133 TLTVRENLQFsaALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEP 212
Cdd:cd03262 90 HLTVLENITL--APIKVKGMSKAEAEERALELLEKVGLADKADAYPAQ-----LSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190
....*....|....*....|....*....|..
gi 1149890125 213 TTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQ 244
Cdd:cd03262 163 TSALDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
63-246 |
1.81e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.83 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 63 ILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDpsGLSGDVLINGAP--------RPANFKCNSGYVVQDDVVMGT 133
Cdd:PRK10584 25 ILTGVELVVKRGETiALIGESGSGKSTLLAILAGLDD--GSSGEVSLVGQPlhqmdeeaRAKLRAKHVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 134 LTVRENLQFSAALRlatTMTNHEKNERINRVIQELGLDKVADsKVGTQfirgVSGGERKRTSIGMELITDPSILFLDEPT 213
Cdd:PRK10584 103 LNALENVELPALLR---GESSRQSRNGAKALLEQLGLGKRLD-HLPAQ----LSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190
....*....|....*....|....*....|....
gi 1149890125 214 TGLDSSTANAVLLLLKRMSK-QGRTIIFSIHQPR 246
Cdd:PRK10584 175 GNLDRQTGDKIADLLFSLNReHGTTLILVTHDLQ 208
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
77-243 |
2.11e-18 |
|
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: 83.63 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRPANFKC------NSGYVVQ--DDVVMGTlTVRENLQFSAalrL 148
Cdd:TIGR01166 22 ALLGANGAGKSTLLLHLNGLLRPQ--SGAVLIDGEPLDYSRKGllerrqRVGLVFQdpDDQLFAA-DVDQDVAFGP---L 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 149 ATTMTNHEKNERINRVIQELGLDKVADskvgtQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLL 228
Cdd:TIGR01166 96 NLGLSEAEVERRVREALTAVGASGLRE-----RPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQMLAIL 170
|
170
....*....|....*
gi 1149890125 229 KRMSKQGRTIIFSIH 243
Cdd:TIGR01166 171 RRLRAEGMTVVISTH 185
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
77-274 |
2.12e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 84.81 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLING--------APRPanfkcnsgyvV----QDDVVMGTLTVREN--LQF 142
Cdd:COG3840 29 AILGPSGAGKSTLLNLIAGFLPPD--SGRILWNGqdltalppAERP----------VsmlfQENNLFPHLTVAQNigLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 143 SAALRLattmtNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTAN 222
Cdd:COG3840 97 RPGLKL-----TAEQRAQVEQALERVGLAGLLDRLPGQ-----LSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1149890125 223 AVLLLLKRMSK-QGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:COG3840 167 EMLDLVDELCReRGLTVLMVTHDPE-DAARIADRVLLVADGRIAADGPTAALL 218
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
58-239 |
2.16e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 89.07 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 58 PVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP----RPANFKCNSGYVVQDdVVMG 132
Cdd:COG1132 350 PGDRPVLKDISLTIPPGeTVALVGPSGSGKSTLVNLLLRFYDPT--SGRILIDGVDirdlTLESLRRQIGVVPQD-TFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 133 TLTVRENLQFS----------AALRLAttmtnhekneRINRVIQEL--GLDkvadSKVGTqfiRGV--SGGERKRTSIGM 198
Cdd:COG1132 427 SGTIRENIRYGrpdatdeeveEAAKAA----------QAHEFIEALpdGYD----TVVGE---RGVnlSGGQRQRIAIAR 489
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1149890125 199 ELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTII 239
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTI 529
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
77-240 |
2.97e-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: 86.69 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAarkdpsGL----SGDVLING---APRPANfKCNSGYVVQDDVVMGTLTVRENLQFSaaLRLA 149
Cdd:COG3842 35 ALLGPSGCGKTTLLRMIA------GFetpdSGRILLDGrdvTGLPPE-KRNVGMVFQDYALFPHLTVAENVAFG--LRMR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 150 tTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLK 229
Cdd:COG3842 106 -GVPKAEIRARVAELLELVGLEGLADRYPHQ-----LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELR 179
|
170
....*....|..
gi 1149890125 230 RMSKQ-GRTIIF 240
Cdd:COG3842 180 RLQRElGITFIY 191
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
62-272 |
3.42e-18 |
|
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: 84.17 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 62 EILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING----APRPA---NFKCNSGYVVQDDVVMGT 133
Cdd:cd03258 19 TALKDVSLSVPKGeIFGIIGRSGAGKSTLIRCINGLERPT--SGSVLVDGtdltLLSGKelrKARRRIGMIFQHFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 134 LTVRENLQFsaALRLATtMTNHEKNERINRVIQELGLDKVADSkvgtqFIRGVSGGERKRTSIGMELITDPSILFLDEPT 213
Cdd:cd03258 97 RTVFENVAL--PLEIAG-VPKAEIEERVLELLELVGLEDKADA-----YPAQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 214 TGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:cd03258 169 SALDPETTQSILALLRDINRElGLTIVLITHEME-VVKRICDRVAVMEKGEVVEEGTVEE 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
77-272 |
3.50e-18 |
|
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: 84.13 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA-----PRPANFKCNSGYVVQDDVVMGTLTVRENLqfSAALRLaTT 151
Cdd:cd03218 30 GLLGPNGAGKTTTFYMIVGLVKPD--SGKILLDGQditklPMHKRARLGIGYLPQEASIFRKLTVEENI--LAVLEI-RG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 152 MTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRM 231
Cdd:cd03218 105 LSKKEREEKLEELLEEFHITHLRKSKASS-----LSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKIL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1149890125 232 SKQGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:cd03218 180 KDRGIGVLITDHNVR-ETLSITDRAYIIYEGKVLAEGTPEE 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
60-274 |
5.61e-18 |
|
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: 83.98 E-value: 5.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSgLSGDVLINGAPR----PANFKCNSGYV---VQDDVvM 131
Cdd:COG1119 15 GKTILDDISWTVKPGEHwAILGPNGAGKSTLLSLITGDLPPT-YGNDVRLFGERRggedVWELRKRIGLVspaLQLRF-P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 132 GTLTVRENLQ--FSAALRLATTMTNHEKnERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFL 209
Cdd:COG1119 93 RDETVLDVVLsgFFDSIGLYREPTDEQR-ERARELLELLGLAHLADRPFGT-----LSQGEQRRVLIARALVKDPELLIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149890125 210 DEPTTGLDSSTANAVLLLLKRMSKQG-RTIIFSIHQPRYsIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:COG1119 167 DEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEE-IPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
61-274 |
7.60e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 83.63 E-value: 7.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 61 KEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRPA-------------------NFkcn 120
Cdd:COG4559 14 RTLLDDVSLTLRPGeLTAIIGPNGAGKSTLLKLLTGELTPS--SGEVRLNGRPLAAwspwelarrravlpqhsslAF--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 121 sGYVVQDDVVMGtltvrenlqfsaalRLATTMTNHEKNERINRVIQELGLDKVADskvgtQFIRGVSGGERKRTSIGMEL 200
Cdd:COG4559 89 -PFTVEEVVALG--------------RAPHGSSAAQDRQIVREALALVGLAHLAG-----RSYQTLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 201 I-------TDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQP----RYSifklfDSLTLLASGRLMFHGP 269
Cdd:COG4559 149 AqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLnlaaQYA-----DRILLLHQGRLVAQGT 223
|
....*
gi 1149890125 270 AQEAL 274
Cdd:COG4559 224 PEEVL 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
77-268 |
7.75e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 82.33 E-value: 7.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRlatTMTNHE 156
Cdd:cd03269 30 GLLGPNGAGKTTTIRMILGIILPD--SGEVLFDGKPLDIAARNRIGYLPEERGLYPKMKVIDQLVYLAQLK---GLKKEE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 157 KNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGR 236
Cdd:cd03269 105 ARRRIDEWLERLELSEYANKRVEE-----LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGK 179
|
170 180 190
....*....|....*....|....*....|..
gi 1149890125 237 TIIFSIHQPRySIFKLFDSLTLLASGRLMFHG 268
Cdd:cd03269 180 TVILSTHQME-LVEELCDRVLLLNKGRAVLYG 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
77-272 |
1.41e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 83.62 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSL----LDVLAArkDpsglSGDVLINGAPRPANFKCNSGYvvqddvvM----G---TLTVRENLQFSAA 145
Cdd:COG4152 31 GLLGPNGAGKTTTiriiLGILAP--D----SGEVLWDGEPLDPEDRRRIGY-------LpeerGlypKMKVGEQLVYLAR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 146 LRlatTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL 225
Cdd:COG4152 98 LK---GLSKAEAKRRADEWLERLGLGDRANKKVEE-----LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1149890125 226 LLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:COG4152 170 DVIRELAAKGTTVIFSSHQME-LVEELCDRIVIINKGRKVLSGSVDE 215
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
60-276 |
1.99e-17 |
|
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: 81.89 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPrPANFKCNS-----GYVVQDdVVMGT 133
Cdd:cd03251 14 GPPVLRDISLDIPAGeTVALVGPSGSGKSTLVNLIPRFYDVD--SGRILIDGHD-VRDYTLASlrrqiGLVSQD-VFLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 134 LTVRENLQFS----------AALRLATTmtnHEknerinrVIQELglDKVADSKVGTqfiRGV--SGGERKRTSIGMELI 201
Cdd:cd03251 90 DTVAENIAYGrpgatreeveEAARAANA---HE-------FIMEL--PEGYDTVIGE---RGVklSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149890125 202 TDPSILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGRLMFHGPAQEALGY 276
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVIAH--RLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
61-217 |
2.38e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 80.99 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 61 KEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPS-GLSGDVLING---APRPANFKcNSGYVVQDDVVMGTLT 135
Cdd:COG4136 14 RPLLAPLSLTVAPGeILTLMGPSGSGKSTLLAAIAGTLSPAfSASGEVLLNGrrlTALPAEQR-RIGILFQDDLLFPHLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 136 VRENLQFSaalrLATTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTG 215
Cdd:COG4136 93 VGENLAFA----LPPTIGRAQRRARVEQALEEAGLAGFADRDPAT-----LSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
..
gi 1149890125 216 LD 217
Cdd:COG4136 164 LD 165
|
|
| urea_trans_UrtD |
TIGR03411 |
urea ABC transporter, ATP-binding protein UrtD; Members of this protein family are ABC ... |
64-239 |
3.70e-17 |
|
urea ABC transporter, ATP-binding protein UrtD; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274568 [Multi-domain] Cd Length: 242 Bit Score: 81.45 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA-------PRPANFkcNSGYVVQDDVVMGTLT 135
Cdd:TIGR03411 18 LNDLSLYVDPGeLRVIIGPNGAGKTTMMDVITGKTRPD--EGSVLFGGTdltglpeHQIARA--GIGRKFQKPTVFENLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 136 VRENLQFSAAL--RLATTMT---NHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLD 210
Cdd:TIGR03411 94 VFENLELALPRdkSVFASLFfrlSAEEKDRIEEVLETIGLADEADRLAGL-----LSHGQKQWLEIGMLLMQDPKLLLLD 168
|
170 180 190
....*....|....*....|....*....|...
gi 1149890125 211 EPTTGLD----SSTANavllLLKRMSKqGRTII 239
Cdd:TIGR03411 169 EPVAGMTdeetEKTAE----LLKSLAG-KHSVV 196
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
62-272 |
4.54e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 81.82 E-value: 4.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 62 EILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRP------ANFKCNSGYVVQD-DVVMGT 133
Cdd:PRK13636 20 HALKGININIKKGeVTAILGGNGAGKSTLFQNLNGILKPS--SGRILFDGKPIDysrkglMKLRESVGMVFQDpDNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 134 LTVRENLQFSAalrLATTMTNHEKNERINRVIQELGLDKVADSKVgtqfiRGVSGGERKRTSIGMELITDPSILFLDEPT 213
Cdd:PRK13636 98 ASVYQDVSFGA---VNLKLPEDEVRKRVDNALKRTGIEHLKDKPT-----HCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149890125 214 TGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQprYSIFKLF-DSLTLLASGRLMFHGPAQE 272
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEMQKElGLTIIIATHD--IDIVPLYcDNVFVMKEGRVILQGNPKE 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
78-272 |
4.90e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.96 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 78 ILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRPANFKCNS---GYVVQDDVVMGTLTVRENLQ-FSAALRLATtmt 153
Cdd:PRK13536 72 LLGPNGAGKSTIARMILGMTSPD--AGKITVLGVPVPARARLARariGVVPQFDNLDLEFTVRENLLvFGRYFGMST--- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 154 nHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK 233
Cdd:PRK13536 147 -REIEAVIPSLLEFARLESKADARVSD-----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLA 220
|
170 180 190
....*....|....*....|....*....|....*....
gi 1149890125 234 QGRTIIFSIHQPRYSIfKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK13536 221 RGKTILLTTHFMEEAE-RLCDRLCVLEAGRKIAEGRPHA 258
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
59-243 |
5.52e-17 |
|
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: 80.74 E-value: 5.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 59 VEKE-----ILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING---APRPANfKCNSGYVVQDDV 129
Cdd:cd03300 6 VSKFyggfvALDGVSLDIKEGeFFTLLGPSGCGKTTLLRLIAGFETPT--SGEILLDGkdiTNLPPH-KRPVNTVFQNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 130 VMGTLTVRENLQFsaALRLATTMTNhEKNERINRVIQELGLDKVADSKvgtqfIRGVSGGERKRTSIGMELITDPSILFL 209
Cdd:cd03300 83 LFPHLTVFENIAF--GLRLKKLPKA-EIKERVAEALDLVQLEGYANRK-----PSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1149890125 210 DEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIH 243
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKElGITFVFVTH 189
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
58-272 |
9.26e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 80.89 E-value: 9.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 58 PVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRP------ANFKCNSGYVVQ--DD 128
Cdd:PRK13639 12 PDGTEALKGINFKAEKGeMVALLGPNGAGKSTLFLHFNGILKPT--SGEVLIKGEPIKydkkslLEVRKTVGIVFQnpDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 129 VVMGTlTVRENLQFsAALRLATTMTNHEKneRINRVIQELGLDKVaDSKVGTQFirgvSGGERKRTSIGMELITDPSILF 208
Cdd:PRK13639 90 QLFAP-TVEEDVAF-GPLNLGLSKEEVEK--RVKEALKAVGMEGF-ENKPPHHL----SGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149890125 209 LDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQ----PRYSifklfDSLTLLASGRLMFHGPAQE 272
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDvdlvPVYA-----DKVYVMSDGKIIKEGTPKE 223
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
58-288 |
1.17e-16 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 83.61 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 58 PVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP----RPANFKCNSGYVVQDdVVMG 132
Cdd:TIGR02203 342 GRDRPALDSISLVIEPGeTVALVGRSGSGKSTLVNLIPRFYEPD--SGQILLDGHDladyTLASLRRQVALVSQD-VVLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 133 TLTVRENLQFSAalrlattmTNHEKNERINRVIQEL-------GLDKVADSKVGTQFIRgVSGGERKRTSIGMELITDPS 205
Cdd:TIGR02203 419 NDTIANNIAYGR--------TEQADRAEIERALAAAyaqdfvdKLPLGLDTPIGENGVL-LSGGQRQRLAIARALLKDAP 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 206 ILFLDEPTTGLDSSTANAVLLLLKRMsKQGRTIIFSIHqpRYSIFKLFDSLTLLASGRLMFHGPAQEALgyfESAGYHCE 285
Cdd:TIGR02203 490 ILILDEATSALDNESERLVQAALERL-MQGRTTLVIAH--RLSTIEKADRIVVMDDGRIVERGTHNELL---ARNGLYAQ 563
|
...
gi 1149890125 286 AYN 288
Cdd:TIGR02203 564 LHN 566
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
78-245 |
1.62e-16 |
|
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: 78.30 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 78 ILGPTGGGKSSLLDVLAARKDPsgLSGDVLINGAP---RPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALrlattmtn 154
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPP--LAGRVLLNGGPldfQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHAD-------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 155 hEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDsstANAVLLLLKRMS-- 232
Cdd:cd03231 101 -HSDEQVEEALARVGLNGFEDRPVAQ-----LSAGQQRRVALARLLLSGRPLWILDEPTTALD---KAGVARFAEAMAgh 171
|
170
....*....|....
gi 1149890125 233 -KQGRTIIFSIHQP 245
Cdd:cd03231 172 cARGGMVVLTTHQD 185
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
61-262 |
1.81e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 79.74 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 61 KEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP--RPAnfkCNSGYVVQDDVVMGTLTVR 137
Cdd:PRK11248 14 KPALEDINLTLESGeLLVVLGPSGCGKTTLLNLIAGFVPYQ--HGSITLDGKPveGPG---AERGVVFQNEGLLPWRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 138 ENLQFsaALRLATTmtnhEKNERINRVIQELGldKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:PRK11248 89 DNVAF--GLQLAGV----EKMQRLEIAHQMLK--KVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1149890125 218 SSTANAV-LLLLKRMSKQGRTIIFSIHQPRYSIFkLFDSLTLLASG 262
Cdd:PRK11248 161 AFTREQMqTLLLKLWQETGKQVLLITHDIEEAVF-MATELVLLSPG 205
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
78-275 |
2.10e-16 |
|
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: 79.24 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 78 ILGPTGGGKSSLLDVLAA--RKDpsglSGDVLING-----APRPANFKCNSGYVVQDDVVMGTLTVRENLQfsAALRLAT 150
Cdd:TIGR04406 32 LLGPNGAGKTTSFYMIVGlvRPD----AGKILIDGqdithLPMHERARLGIGYLPQEASIFRKLTVEENIM--AVLEIRK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 151 TMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKR 230
Cdd:TIGR04406 106 DLDRAEREERLEALLEEFQISHLRDNKAMS-----LSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVGDIKKIIKH 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1149890125 231 MSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQEALG 275
Cdd:TIGR04406 181 LKERGIGVLITDHNVR-ETLDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
78-272 |
2.85e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 80.23 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 78 ILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRPA---NFKCNSGYVVQDDVVMGTLTVRENLQ-FSAALrlatTMT 153
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLLGLTHPD--AGSISLCGEPVPSrarHARQRVGVVPQFDNLDPDFTVRENLLvFGRYF----GLS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 154 NHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK 233
Cdd:PRK13537 112 AAAARALVPPLLEFAKLENKADAKVGE-----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLA 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1149890125 234 QGRTIIFSIHqprysiF-----KLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK13537 187 RGKTILLTTH------FmeeaeRLCDRLCVIEEGRKIAEGAPHA 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
64-294 |
2.88e-16 |
|
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: 78.54 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING---APRPANfKCNSGYVVQDDVVMGTLTVREN 139
Cdd:cd03296 18 LDDVSLDIPSGeLVALLGPSGSGKTTLLRLIAGLERPD--SGTILFGGedaTDVPVQ-ERNVGFVFQHYALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 140 LQFSAALRLATTMTNH-EKNERINRVIQELGLDKVADSkvgtqFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDS 218
Cdd:cd03296 95 VAFGLRVKPRSERPPEaEIRAKVHELLKLVQLDWLADR-----YPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149890125 219 STANAVLLLLKRM-SKQGRTIIFSIHQPRYSIfKLFDSLTLLASGRLmfhgpaqealgyfESAGYHCEAYNNPADFF 294
Cdd:cd03296 170 KVRKELRRWLRRLhDELHVTTVFVTHDQEEAL-EVADRVVVMNKGRI-------------EQVGTPDEVYDHPASPF 232
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
77-272 |
3.13e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.06 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRPA----NFKCNSGYVVQDDVVMGTLTVRE-----NLQFSAAL- 146
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPS--EGEILLDAQPLESwsskAFARKVAYLPQQLPAAEGMTVRElvaigRYPWHGALg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 147 RLATtmtnhEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLL 226
Cdd:PRK10575 119 RFGA-----ADREKVEEAISLVGLKPLAHRLVDS-----LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1149890125 227 LLKRMSKQ-GRTIIFSIHQ----PRYSifklfDSLTLLASGRLMFHGPAQE 272
Cdd:PRK10575 189 LVHRLSQErGLTVIAVLHDinmaARYC-----DYLVALRGGEMIAQGTPAE 234
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
61-272 |
4.19e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 79.08 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 61 KEILSNINGIM-KPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP-RPANFK---CNSGYVVQ--DDVVMGT 133
Cdd:PRK13652 17 KEALNNINFIApRNSRIAVIGPNGAGKSTLFRHFNGILKPT--SGSVLIRGEPiTKENIRevrKFVGLVFQnpDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 134 lTVRENLQFSAA-LRLATTMTNHekneRINRVIQELGLDKVADskvgtQFIRGVSGGERKRTSIGMELITDPSILFLDEP 212
Cdd:PRK13652 95 -TVEQDIAFGPInLGLDEETVAH----RVSSALHMLGLEELRD-----RVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149890125 213 TTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYsIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDL-VPEMADYIYVMDKGRIVAYGTVEE 224
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
64-239 |
6.05e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 77.85 E-value: 6.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA-------PRPAN------FkcnsgyvvQDDV 129
Cdd:COG4674 26 LNDLSLYVDPGeLRVIIGPNGAGKTTLMDVITGKTRPD--SGSVLFGGTdltgldeHEIARlgigrkF--------QKPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 130 VMGTLTVRENLQFSAAL--RLATTMT---NHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDP 204
Cdd:COG4674 96 VFEELTVFENLELALKGdrGVFASLFarlTAEERDRIEEVLETIGLTDKADRLAGL-----LSHGQKQWLEIGMLLAQDP 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1149890125 205 SILFLDEPTTGL-DSSTANAVlLLLKRMSKQgRTII 239
Cdd:COG4674 171 KLLLLDEPVAGMtDAETERTA-ELLKSLAGK-HSVV 204
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
77-246 |
1.15e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 75.86 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPsgLSGDVLINGAPRP---ANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMT 153
Cdd:TIGR01189 30 QVTGPNGIGKTTLLRILAGLLRP--DSGEVRWNGTPLAeqrDEPHENILYLGHLPGLKPELSALENLHFWAAIHGGAQRT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 154 NHEKNERInrviqelGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDsstANAVLLLLKRMS- 232
Cdd:TIGR01189 108 IEDALAAV-------GLTGFEDLPAAQ-----LSAGQQRRLALARLWLSRRPLWILDEPTTALD---KAGVALLAGLLRa 172
|
170
....*....|....*.
gi 1149890125 233 --KQGRTIIFSIHQPR 246
Cdd:TIGR01189 173 hlARGGIVLLTTHQDL 188
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
122-217 |
1.40e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 76.61 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 122 GYVVQDDVVMGTLTVRENLQfsAALRLaTTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELI 201
Cdd:COG1137 81 GYLPQEASIFRKLTVEDNIL--AVLEL-RKLSKKEREERLEELLEEFGITHLRKSKAYS-----LSGGERRRVEIARALA 152
|
90
....*....|....*.
gi 1149890125 202 TDPSILFLDEPTTGLD 217
Cdd:COG1137 153 TNPKFILLDEPFAGVD 168
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
59-243 |
3.71e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 75.24 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 59 VEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP-------RPANFKCNS-GYVVQDDV 129
Cdd:PRK11629 20 VQTDVLHNVSFSIGEGeMMAIVGSSGSGKSTLLHLLGGLDTPT--SGDVIFNGQPmsklssaAKAELRNQKlGFIYQFHH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 130 VMGTLTVRENLqfsAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFL 209
Cdd:PRK11629 98 LLPDFTALENV---AMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSE-----LSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190
....*....|....*....|....*....|....*
gi 1149890125 210 DEPTTGLDSSTANAVLLLLKRMS-KQGRTIIFSIH 243
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNrLQGTAFLVVTH 204
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
74-272 |
7.43e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.45 E-value: 7.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 74 GLNAILGPTGGGKSSLLDVLAARKDP-SG---LSGDVL------INGAPRpanfKCNSGYVVQDDVVMGTLTVRENLQFS 143
Cdd:PRK11144 25 GITAIFGRSGAGKTSLINAISGLTRPqKGrivLNGRVLfdaekgICLPPE----KRRIGYVFQDARLFPHYKVRGNLRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 144 AAlrlattmtnHEKNERINRVIQELGLDKVADskvgtQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANA 223
Cdd:PRK11144 101 MA---------KSMVAQFDKIVALLGIEPLLD-----RYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1149890125 224 VLLLLKRMSKQGRT-IIFSIHqpryS---IFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK11144 167 LLPYLERLAREINIpILYVSH----SldeILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
38-268 |
9.66e-15 |
|
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: 73.72 E-value: 9.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 38 SFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRPAn 116
Cdd:cd03220 12 TYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERiGLIGRNGAGKSTLLRLLAGIYPPD--SGTVTVRGRVSSL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 117 FKCNSGyvvqddvVMGTLTVRENLQFSAALRlatTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSI 196
Cdd:cd03220 89 LGLGGG-------FNPELTGRENIYLNGRLL---GLSRKEIDEKIDEIIEFSELGDFIDLPVKT-----YSSGMKARLAF 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149890125 197 GMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHG 268
Cdd:cd03220 154 AIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPS-SIKRLCDRALVLEKGKIRFDG 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
58-231 |
1.14e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 74.35 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 58 PVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING-------APRPANFkcnSGYVVQDdV 129
Cdd:COG1101 16 VNEKRALDGLNLTIEEGdFVTVIGSNGAGKSTLLNAIAGSLPPD--SGSILIDGkdvtklpEYKRAKY---IGRVFQD-P 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 130 VMGT---LTVRENLQFSAA------LRLATTMTNHEK-NERINRViqELGLDKVADSKVGTqfirgVSGGERKRTSIGME 199
Cdd:COG1101 90 MMGTapsMTIEENLALAYRrgkrrgLRRGLTKKRRELfRELLATL--GLGLENRLDTKVGL-----LSGGQRQALSLLMA 162
|
170 180 190
....*....|....*....|....*....|..
gi 1149890125 200 LITDPSILFLDEPTTGLDSSTANAVLLLLKRM 231
Cdd:COG1101 163 TLTKPKLLLLDEHTAALDPKTAALVLELTEKI 194
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
80-243 |
1.24e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 75.84 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 80 GPTGGGKSSLLDVLAARKDPSglSGDVLI-----NGAPrPAnfKCNSGYVVQDDVVMGTLTVRENLQFsaALRLATTMTN 154
Cdd:PRK11000 36 GPSGCGKSTLLRMIAGLEDIT--SGDLFIgekrmNDVP-PA--ERGVGMVFQSYALYPHLSVAENMSF--GLKLAGAKKE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 155 hEKNERINRVIQELGLDKVADSKVgtqfiRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ 234
Cdd:PRK11000 109 -EINQRVNQVAEVLQLAHLLDRKP-----KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKR 182
|
170
....*....|
gi 1149890125 235 -GRTIIFSIH 243
Cdd:PRK11000 183 lGRTMIYVTH 192
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
62-244 |
1.28e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 73.89 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 62 EILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA----PRPANFKC------NSGYVVQDDVV 130
Cdd:COG4161 16 QALFDINLECPSGeTLVLLGPSGAGKSSLLRVLNLLETPD--SGQLNIAGHqfdfSQKPSEKAirllrqKVGMVFQQYNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 131 MGTLTVRENLqFSAALRLATtMTNHEKNERINRVIQELGLDKVADSkvgtqFIRGVSGGERKRTSIGMELITDPSILFLD 210
Cdd:COG4161 94 WPHLTVMENL-IEAPCKVLG-LSKEQAREKAMKLLARLRLTDKADR-----FPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190
....*....|....*....|....*....|....
gi 1149890125 211 EPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQ 244
Cdd:COG4161 167 EPTAALDPEITAQVVEIIRELSQTGITQVIVTHE 200
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
77-274 |
1.56e-14 |
|
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: 73.48 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLaarkdpSGL----SGDVLINGAP---RPANFKCNSG--YVVQDDVVMGTLTVRENLQFSAALR 147
Cdd:COG0410 33 ALLGRNGAGKTTLLKAI------SGLlpprSGSIRFDGEDitgLPPHRIARLGigYVPEGRRIFPSLTVEENLLLGAYAR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 148 LATtmtnHEKNERINRV------IQELgldkvADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTA 221
Cdd:COG0410 107 RDR----AEVRADLERVyelfprLKER-----RRQRAGT-----LSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1149890125 222 NAVLLLLKRMSKQGRTIIFS---IHQprysIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:COG0410 173 EEIFEIIRRLNREGVTILLVeqnARF----ALEIADRAYVLERGRIVLEGTAAELL 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
60-272 |
1.83e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 73.58 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNIN-GIMKPGLNAILGPTGGGKSSLLDVLA--ARKDpsglSGDVLING-----------APRPANFKcnsgyvv 125
Cdd:COG4604 13 GKVVLDDVSlTIPKGGITALIGPNGAGKSTLLSMISrlLPPD----SGEVLVDGldvattpsrelAKRLAILR------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 126 QDDVVMGTLTVRENLQF-----SAAlRLattmtNHEKNERINRVIQELGLDKVADskvgtQFIRGVSGGERKRTSIGMEL 200
Cdd:COG4604 82 QENHINSRLTVRELVAFgrfpySKG-RL-----TAEDREIIDEAIAYLDLEDLAD-----RYLDELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149890125 201 ITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK-QGRTIIFSIHQ----PRYSifklfDSLTLLASGRLMFHGPAQE 272
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADeLGKTVVIVLHDinfaSCYA-----DHIVAMKDGRVVAQGTPEE 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
52-268 |
2.83e-14 |
|
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: 76.98 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 52 FLPCRKPVEKEIlsNINgIMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRPANF---KCNSGYVVQDD 128
Cdd:TIGR01257 938 FEPSGRPAVDRL--NIT-FYENQITAFLGHNGAGKTTTLSILTGLLPPT--SGTVLVGGKDIETNLdavRQSLGMCPQHN 1012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 129 VVMGTLTVRENLQFSAALRlatTMTNHEKNERINRVIQELGLDKVADSKVgtqfiRGVSGGERKRTSIGMELITDPSILF 208
Cdd:TIGR01257 1013 ILFHHLTVAEHILFYAQLK---GRSWEEAQLEMEAMLEDTGLHHKRNEEA-----QDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149890125 209 LDEPTTGLDSSTANAVL-LLLKRMSkqGRTIIFSIHQPRYSIFkLFDSLTLLASGRLMFHG 268
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWdLLLKYRS--GRTIIMSTHHMDEADL-LGDRIAIISQGRLYCSG 1142
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
77-274 |
3.06e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 72.69 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLING--------APRPANFkcnsgyVVQDDVVMGTLTVREN--LQFSAAL 146
Cdd:PRK10771 29 AILGPSGAGKSTLLNLIAGFLTPA--SGSLTLNGqdhtttppSRRPVSM------LFQENNLFSHLTVAQNigLGLNPGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 147 RLattmtNHEKNERINRVIQELGLDKVADsKVGTQfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLL 226
Cdd:PRK10771 101 KL-----NAAQREKLHAIARQMGIEDLLA-RLPGQ----LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1149890125 227 LLKRMSKQGR-TIIFSIHQ--------PRysifklfdSLtLLASGRLMFHGPAQEAL 274
Cdd:PRK10771 171 LVSQVCQERQlTLLMVSHSledaariaPR--------SL-VVADGRIAWDGPTDELL 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
35-274 |
4.11e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 72.88 E-value: 4.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 35 AVLSFHNICYRVKlksgflpcrkpvEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP- 112
Cdd:PRK13548 1 AMLEARNLSVRLG------------GRTLLDDVSLTLRPGeVVAILGPNGAGKSTLLRALSGELSPD--SGEVRLNGRPl 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 113 ---RPA---------------NFKCNsgyvVQDDVVMGtltvrenlqfsaalRLATTMTNHEKNERINRVIQELGLDKVA 174
Cdd:PRK13548 67 adwSPAelarrravlpqhsslSFPFT----VEEVVAMG--------------RAPHGLSRAEDDALVAAALAQVDLAHLA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 175 DSkvgtqFIRGVSGGERKRTSIGMELI------TDPSILFLDEPTTGLDSSTANAVLLLLKRM-SKQGRTIIFSIHQ--- 244
Cdd:PRK13548 129 GR-----DYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDlnl 203
|
250 260 270
....*....|....*....|....*....|.
gi 1149890125 245 -PRYSifklfDSLTLLASGRLMFHGPAQEAL 274
Cdd:PRK13548 204 aARYA-----DRIVLLHQGRLVADGTPAEVL 229
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
64-264 |
4.25e-14 |
|
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: 72.33 E-value: 4.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP----RPANFKCNSGYVVQDDVVMGTLTVRE 138
Cdd:cd03295 17 VNNLNLEIAKGeFLVLIGPSGSGKTTTMKMINRLIEPT--SGEIFIDGEDireqDPVELRRKIGYVIQQIGLFPHMTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 139 NLQFSAALrlattmtNHEKNERINRVIQEL----GLDkvaDSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTT 214
Cdd:cd03295 95 NIALVPKL-------LKWPKEKIRERADELlalvGLD---PAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1149890125 215 GLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYSiFKLFDSLTLLASGRL 264
Cdd:cd03295 165 ALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEA-FRLADRIAIMKNGEI 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
77-294 |
6.05e-14 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 73.64 E-value: 6.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAarkdpsGL----SGDVLING-------APRpanfKCNSGYVVQDDVVMGTLTVRENLQFsaA 145
Cdd:COG1118 32 ALLGPSGSGKTTLLRIIA------GLetpdSGRIVLNGrdlftnlPPR----ERRVGFVFQHYALFPHMTVAENIAF--G 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 146 LRLATTmTNHEKNERINRVIQELGLDKVADSKVgTQfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL 225
Cdd:COG1118 100 LRVRPP-SKAEIRARVEELLELVQLEGLADRYP-SQ----LSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELR 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149890125 226 LLLKRM-SKQGRTIIFSIHQP----RYSifklfDSLTLLASGRLMFHGPAQealgyfesagyhcEAYNNPADFF 294
Cdd:COG1118 174 RWLRRLhDELGGTTVFVTHDQeealELA-----DRVVVMNQGRIEQVGTPD-------------EVYDRPATPF 229
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
60-282 |
6.41e-14 |
|
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: 71.02 E-value: 6.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGaprpanfkcnsgyvvqddvvmgtltvrE 138
Cdd:cd03217 12 GKEILKGVNLTIKKGeVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKG---------------------------E 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 139 NLqfsaalrlattmTNHEKNERINRVI----QE----LGLdKVADskvgtqFIRGV----SGGERKRTSIGMELITDPSI 206
Cdd:cd03217 65 DI------------TDLPPEERARLGIflafQYppeiPGV-KNAD------FLRYVnegfSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149890125 207 LFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRysIFKLF--DSLTLLASGRLMFHGPAQEALgYFESAGY 282
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQR--LLDYIkpDRVHVLYDGRIVKSGDKELAL-EIEKKGY 200
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
63-263 |
7.57e-14 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 70.58 E-value: 7.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 63 ILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPsgLSGDVLINGaprpanfkcNSGYVVQDDVVMGTlTVRENLQ 141
Cdd:cd03250 20 TLKDINLEVPKGeLVAIVGPVGSGKSSLLSALLGELEK--LSGSVSVPG---------SIAYVSQEPWIQNG-TIRENIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 142 FSAALRlattmtnhekNERINRVIQELGLDKvaDSK---------VGtqfIRGV--SGGERKRTSIGMELITDPSILFLD 210
Cdd:cd03250 88 FGKPFD----------EERYEKVIKACALEP--DLEilpdgdlteIG---EKGInlSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1149890125 211 EPTTGLDSSTANAVL--LLLKRMsKQGRTIIFSIHQPRYsiFKLFDSLTLLASGR 263
Cdd:cd03250 153 DPLSAVDAHVGRHIFenCILGLL-LNNKTRILVTHQLQL--LPHADQIVVLDNGR 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
71-243 |
7.90e-14 |
|
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: 75.44 E-value: 7.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 71 MKPG-LNAILGPTGGGKSSLLDVLAArkDPSGLSGDVLINGAPRPANFK---CNSGYVVQDDVVMGTLTVRENLQFSAAL 146
Cdd:TIGR01257 1962 VRPGeCFGLLGVNGAGKTTTFKMLTG--DTTVTSGDATVAGKSILTNISdvhQNMGYCPQFDAIDDLLTGREHLYLYARL 2039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 147 RLATTmtnhEKNERI-NRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL 225
Cdd:TIGR01257 2040 RGVPA----EEIEKVaNWSIQSLGLSLYADRLAGT-----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLW 2110
|
170
....*....|....*...
gi 1149890125 226 LLLKRMSKQGRTIIFSIH 243
Cdd:TIGR01257 2111 NTIVSIIREGRAVVLTSH 2128
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
60-243 |
1.29e-13 |
|
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: 71.03 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPsgLSGDVLINGAP-RPAN---FKCNSGYVVQDDVVMGTl 134
Cdd:cd03249 15 DVPILKGLSLTIPPGKTvALVGSSGCGKSTVVSLLERFYDP--TSGEILLDGVDiRDLNlrwLRSQIGLVSQEPVLFDG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 135 TVRENLQFSAALRLATTMTNHEKNERINRVIQEL--GLDKVADSKvGTQfirgVSGGERKRTSIGMELITDPSILFLDEP 212
Cdd:cd03249 92 TIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLpdGYDTLVGER-GSQ----LSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190
....*....|....*....|....*....|.
gi 1149890125 213 TTGLDSSTANAVLLLLKRMSKqGRTIIFSIH 243
Cdd:cd03249 167 TSALDAESEKLVQEALDRAMK-GRTTIVIAH 196
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
60-246 |
1.34e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 70.87 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGA-------------------PRPANFKc 119
Cdd:COG0396 12 GKEILKGVNLTIKPGeVHAIMGPNGSGKSTLAKVLMGHPKYEVTSGSILLDGEdilelspderaragiflafQYPVEIP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 120 nsgyvvqddvvmGtLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKvadskvgtQFI-RGV----SGGERKRT 194
Cdd:COG0396 91 ------------G-VSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDE--------DFLdRYVnegfSGGEKKRN 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1149890125 195 SIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPR 246
Cdd:COG0396 150 EILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQR 201
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
77-272 |
1.39e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.17 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA--PRPANFKCNS--GYVVQDDVVMGTLTVREnlqFSAALRLAT-- 150
Cdd:PRK10253 37 AIIGPNGCGKSTLLRTLSRLMTPA--HGHVWLDGEhiQHYASKEVARriGLLAQNATTPGDITVQE---LVARGRYPHqp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 151 --TMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLL 228
Cdd:PRK10253 112 lfTRWRKEDEEAVTKAMQATGITHLADQSVDT-----LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1149890125 229 KRMSK-QGRTIIFSIHQ----PRYSIfklfdSLTLLASGRLMFHGPAQE 272
Cdd:PRK10253 187 SELNReKGYTLAAVLHDlnqaCRYAS-----HLIALREGKIVAQGAPKE 230
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
64-272 |
1.49e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 73.84 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 64 LSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP-RPANFKC---NSGYVVQDDVVMGTlTVRE 138
Cdd:PRK13657 351 VEDVSFEAKPGQTvAIVGPTGAGKSTLINLLQRVFDPQ--SGRILIDGTDiRTVTRASlrrNIAVVFQDAGLFNR-SIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 139 NLQF------SAALRLATTMTnhEKNERINRviQELGLDKVadskVGTqfiRG--VSGGERKRTSIGMELITDPSILFLD 210
Cdd:PRK13657 428 NIRVgrpdatDEEMRAAAERA--QAHDFIER--KPDGYDTV----VGE---RGrqLSGGERQRLAIARALLKDPPILILD 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149890125 211 EPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIHqpRYSIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK13657 497 EATSALDVETEAKVKAALDELMK-GRTTFIIAH--RLSTVRNADRILVFDNGRVVESGSFDE 555
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
78-297 |
1.65e-13 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 71.14 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 78 ILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP------------RPANFkcnsGYVVQDDVVMGTLTVRENLQFSAA 145
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPT--SGKVLIDGQDiaamsrkelrelRRKKI----SMVFQSFALLPHRTVLENVAFGLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 146 LRlatTMTNHEKNERINRVIQELGLDKVADSKvgtqfIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSstanavL 225
Cdd:cd03294 129 VQ---GVPRAEREERAAEALELVGLEGWEHKY-----PDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP------L 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 226 -------LLLKRMSKQGRTIIFSIHQPRYSIfKLFDSLTLLASGRLMFHGPAQEALgyfesagyhceayNNPAD-----F 293
Cdd:cd03294 195 irremqdELLRLQAELQKTIVFITHDLDEAL-RLGDRIAIMKDGRLVQVGTPEEIL-------------TNPANdyvreF 260
|
....
gi 1149890125 294 FLDI 297
Cdd:cd03294 261 FRGV 264
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
60-273 |
1.80e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.13 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP----RPANFKCNSGYVVQDDVVMGTl 134
Cdd:PRK10247 19 DAKILNNISFSLRAGeFKLITGPSGCGKSTLLKIVASLISPT--SGTLLFEGEDistlKPEIYRQQVSYCAQTPTLFGD- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 135 TVRENLQFSAALRlattmTNHEKNERINRVIQELGLDKvadsKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTT 214
Cdd:PRK10247 96 TVYDNLIFPWQIR-----NQQPDPAIFLDDLERFALPD----TILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1149890125 215 GLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGrlmfhGPAQEA 273
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHA-----GEMQEA 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
77-274 |
2.71e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.18 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP------RPANFKCNSgyVVQDDVVMGTLTVRENLQFSAALRLAT 150
Cdd:PRK09536 33 GLVGPNGAGKTTLLRAINGTLTPT--AGTVLVAGDDvealsaRAASRRVAS--VPQDTSLSFEFDVRQVVEMGRTPHRSR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 151 TMTNHEKNER-INRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLK 229
Cdd:PRK09536 109 FDTWTETDRAaVERAMERTGVAQFADRPVTS-----LSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1149890125 230 RMSKQGRTIIFSIHQ----PRYSifklfDSLTLLASGRLMFHGPAQEAL 274
Cdd:PRK09536 184 RLVDDGKTAVAAIHDldlaARYC-----DELVLLADGRVRAAGPPADVL 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
62-245 |
3.21e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.83 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 62 EILSNINGIMKPG-LNAILGPTGGGKSSLLDVLA------------ARKDPSGLSGDVLinGAPRPANFkcnsGYVVQDD 128
Cdd:PRK10535 22 EVLKGISLDIYAGeMVAIVGASGSGKSTLMNILGcldkptsgtyrvAGQDVATLDADAL--AQLRREHF----GFIFQRY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 129 VVMGTLTVRENLQFSAalrLATTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILF 208
Cdd:PRK10535 96 HLLSHLTAAQNVEVPA---VYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQ-----LSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 1149890125 209 LDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQP 245
Cdd:PRK10535 168 ADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
78-245 |
3.31e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.06 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 78 ILGPTGGGKSSLLDVLAARKDPsgLSGDVLINGAP----RPAnFKCNSGYV-----VQDDvvmgtLTVRENLQFSAALRL 148
Cdd:PRK13538 32 IEGPNGAGKTSLLRILAGLARP--DAGEVLWQGEPirrqRDE-YHQDLLYLghqpgIKTE-----LTALENLRFYQRLHG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 149 ATTmtnhekNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDsstANAVLLLL 228
Cdd:PRK13538 104 PGD------DEALWEALAQVGLAGFEDVPVRQ-----LSAGQQRRVALARLWLTRAPLWILDEPFTAID---KQGVARLE 169
|
170 180
....*....|....*....|
gi 1149890125 229 KRMS---KQGRTIIFSIHQP 245
Cdd:PRK13538 170 ALLAqhaEQGGMVILTTHQD 189
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
58-272 |
3.53e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 70.46 E-value: 3.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 58 PVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA-PRPANFKCNS-----GYVVQ---- 126
Cdd:PRK13637 17 PFEKKALDNVNIEIEDGeFVGLIGHTGSGKSTLIQHLNGLLKPT--SGKIIIDGVdITDKKVKLSDirkkvGLVFQypey 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 127 --------DDVVMGTltvrENLQFSaalrlattmtNHEKNERINRVIQELGLDKvADSKVGTQFirGVSGGERKRTSIGM 198
Cdd:PRK13637 95 qlfeetieKDIAFGP----INLGLS----------EEEIENRVKRAMNIVGLDY-EDYKDKSPF--ELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149890125 199 ELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSME-DVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
36-280 |
4.10e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 69.34 E-value: 4.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 36 VLSFHNI--CYRV------KLKSGFLPCRKP--VEKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAarkdpsGL-- 102
Cdd:COG1134 4 MIEVENVskSYRLyhepsrSLKELLLRRRRTrrEEFWALKDVSFEVERGESvGIIGRNGAGKSTLLKLIA------GIle 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 103 --SGDVLING--APrPANFkcNSGYvvqddvvMGTLTVRENLQFSAALRlatTMTNHEKNERINRVIQ--ELGldKVADS 176
Cdd:COG1134 78 ptSGRVEVNGrvSA-LLEL--GAGF-------HPELTGRENIYLNGRLL---GLSRKEIDEKFDEIVEfaELG--DFIDQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 177 KVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPT-TGlDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDS 255
Cdd:COG1134 143 PVKT-----YSSGMRARLAFAVATAVDPDILLVDEVLaVG-DAAFQKKCLARIRELRESGRTVIFVSHSMG-AVRRLCDR 215
|
250 260
....*....|....*....|....*
gi 1149890125 256 LTLLASGRLMFHGPAQEALGYFESA 280
Cdd:COG1134 216 AIWLEKGRLVMDGDPEEVIAAYEAL 240
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
77-272 |
4.28e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 69.66 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLaarkdpSGL-SGD--------VLINGAPRPANF-------KCNSGYVVQDDVVMGTLTVRENL 140
Cdd:PRK09984 34 ALLGPSGSGKSTLLRHL------SGLiTGDksagshieLLGRTVQREGRLardirksRANTGYIFQQFNLVNRLSVLENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 141 QFSAA-----LRLATTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTG 215
Cdd:PRK09984 108 LIGALgstpfWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVST-----LSGGQQQRVAIARALMQQAKVILADEPIAS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1149890125 216 LDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRYSIfKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK09984 183 LDPESARIVMDTLRDINQNdGITVVVTLHQVDYAL-RYCERIVALRQGHVFYDGSSQQ 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
60-217 |
5.53e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.63 E-value: 5.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPGlN--AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRpanfkcnSGYVVQDDVVMGTLTVR 137
Cdd:COG0488 10 GRPLLDDVSLSINPG-DriGLVGRNGAGKSTLLKILAGELEPD--SGEVSIPKGLR-------IGYLPQEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 138 ENLqFSAALRLATTMTNHEKNE------------------------------RINRVIQELGLDKV-ADSKVGTqfirgV 186
Cdd:COG0488 80 DTV-LDGDAELRALEAELEELEaklaepdedlerlaelqeefealggweaeaRAEEILSGLGFPEEdLDRPVSE-----L 153
|
170 180 190
....*....|....*....|....*....|.
gi 1149890125 187 SGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
64-262 |
5.61e-13 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 68.65 E-value: 5.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING----APRPANFkcnsgYVVQDDVVMGTLTVRE 138
Cdd:TIGR01184 1 LKGVNLTIQQGeFISLIGHSGCGKSTLLNLISGLAQPT--SGGVILEGkqitEPGPDRM-----VVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 139 NLQFsAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDS 218
Cdd:TIGR01184 74 NIAL-AVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ-----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1149890125 219 ST-ANAVLLLLKRMSKQGRTIIFSIHQPRYSIFkLFDSLTLLASG 262
Cdd:TIGR01184 148 LTrGNLQEELMQIWEEHRVTVLMVTHDVDEALL-LSDRVVMLTNG 191
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
60-280 |
8.36e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 68.84 E-value: 8.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP----RPAN-------------FKCNS 121
Cdd:PRK10619 17 EHEVLKGVSLQANAGdVISIIGSSGSGKSTFLRCINFLEKPS--EGSIVVNGQTinlvRDKDgqlkvadknqlrlLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 122 GYVVQDDVVMGTLTVRENLQFSAALRLAttMTNHEKNERINRVIQELGLDKVADSKVGTQfirgVSGGERKRTSIGMELI 201
Cdd:PRK10619 95 TMVFQHFNLWSHMTVLENVMEAPIQVLG--LSKQEARERAVKYLAKVGIDERAQGKYPVH----LSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149890125 202 TDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSiFKLFDSLTLLASGRLMFHGPAQEALGYFESA 280
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFA-RHVSSHVIFLHQGKIEEEGAPEQLFGNPQSP 246
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
61-243 |
1.11e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 69.98 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 61 KEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING-----AP---RPANfkcnsgYVVQDDVVM 131
Cdd:PRK09452 27 KEVISNLDLTINNGeFLTLLGPSGCGKTTVLRLIAGFETPD--SGRIMLDGqdithVPaenRHVN------TVFQSYALF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 132 GTLTVRENLQFsaALRLATTmTNHEKNERINRVIQELGLDKVADSKvgtqfIRGVSGGERKRTSIGMELITDPSILFLDE 211
Cdd:PRK09452 99 PHMTVFENVAF--GLRMQKT-PAAEITPRVMEALRMVQLEEFAQRK-----PHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190
....*....|....*....|....*....|...
gi 1149890125 212 PTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIH 243
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKlGITFVFVTH 203
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
60-244 |
1.16e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 71.29 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGlsGDVLINGAPRPaNFKCNS-----GYVVQDDVVMGT 133
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGeVVALVGPSGSGKSTVAALLQNLYQPTG--GQVLLDGVPLV-QYDHHYlhrqvALVGQEPVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 134 lTVRENLQFSAALRLATTMTNHEKNERINRVIQEL--GLDKVADSKvGTQfirgVSGGERKRTSIGMELITDPSILFLDE 211
Cdd:TIGR00958 570 -SVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFpnGYDTEVGEK-GSQ----LSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190
....*....|....*....|....*....|...
gi 1149890125 212 PTTGLDsstANAVLLLLKRMSKQGRTIIFSIHQ 244
Cdd:TIGR00958 644 ATSALD---AECEQLLQESRSRASRTVLLIAHR 673
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
48-243 |
1.31e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.50 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 48 LKSGFLPcRKPVEKEILSNINGIMKPGLN-AILGPTGGGKSS----LLDVLAARkdpsglsGDVLINGAP-------RPA 115
Cdd:PRK15134 287 IRKGILK-RTVDHNVVVKNISFTLRPGETlGLVGESGSGKSTtglaLLRLINSQ-------GEIWFDGQPlhnlnrrQLL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 116 NFKCNSGYVVQDDvvMGTLTVRENLQ--FSAALRL-ATTMTNHEKNERINRVIQELGLDKVADSKVGTQFirgvSGGERK 192
Cdd:PRK15134 359 PVRHRIQVVFQDP--NSSLNPRLNVLqiIEEGLRVhQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEF----SGGQRQ 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1149890125 193 RTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGR-TIIFSIH 243
Cdd:PRK15134 433 RIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISH 484
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
78-244 |
1.52e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 67.73 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 78 ILGPTGGGKSSLLDVLAARKDPSglSGDVLING-------APRP---ANFKCNSGYVVQDDVVMGTLTVRENLqFSAALR 147
Cdd:PRK11124 33 LLGPSGAGKSSLLRVLNLLEMPR--SGTLNIAGnhfdfskTPSDkaiRELRRNVGMVFQQYNLWPHLTVQQNL-IEAPCR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 148 LATtMTNHEKNERINRVIQELGLDKVADskvgtQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLL 227
Cdd:PRK11124 110 VLG-LSKDQALARAEKLLERLRLKPYAD-----RFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSI 183
|
170
....*....|....*..
gi 1149890125 228 LKRMSKQGRTIIFSIHQ 244
Cdd:PRK11124 184 IRELAETGITQVIVTHE 200
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
77-269 |
1.66e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 68.95 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP---------RPAnfKCNSGYVVQDDVVMGTLTVRENLQFsaALR 147
Cdd:COG1135 35 GIIGYSGAGKSTLIRCINLLERPT--SGSVLVDGVDltalserelRAA--RRKIGMIFQHFNLLSSRTVAENVAL--PLE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 148 LAttmtNHEKNERINRViQEL----GL-DKvADSkvgtqFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTAN 222
Cdd:COG1135 109 IA----GVPKAEIRKRV-AELlelvGLsDK-ADA-----YPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1149890125 223 AVLLLLKRMSKQ-GRTIIFSIHQP---RysifKLFDSLTLLASGRLMFHGP 269
Cdd:COG1135 178 SILDLLKDINRElGLTIVLITHEMdvvR----RICDRVAVLENGRIVEQGP 224
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
63-274 |
1.97e-12 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 70.16 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 63 ILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAarkdpsGL----SGDVLINGAP----RPANFKCNSGYVVQDdvVmgT 133
Cdd:COG4618 347 ILRGVSFSLEPGeVLGVIGPSGSGKSTLARLLV------GVwpptAGSVRLDGADlsqwDREELGRHIGYLPQD--V--E 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 134 L---TVRENL-QFS--------AALRLATTmtnHEknerinrVIQEL--GLD-KVADSkvGTqfirGVSGGERKRtsIGM 198
Cdd:COG4618 417 LfdgTIAENIaRFGdadpekvvAAAKLAGV---HE-------MILRLpdGYDtRIGEG--GA----RLSGGQRQR--IGL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149890125 199 E--LITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHqpRYSIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:COG4618 479 AraLYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITH--RPSLLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
78-274 |
3.28e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.88 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 78 ILGPTGGGKSSLLDVLAarkdpsGL---SGDVLINGAP----RPANFKCNSGYVVQDDVVMGTLTVRENLqfsaALRLAT 150
Cdd:PRK03695 27 LVGPNGAGKSTLLARMA------GLlpgSGSIQFAGQPleawSAAELARHRAYLSQQQTPPFAMPVFQYL----TLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 151 TMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSI-GMELITDPSI------LFLDEPTTGLDSSTANA 223
Cdd:PRK03695 97 KTRTEAVASALNEVAEALGLDDKLGRSVNQ-----LSGGEWQRVRLaAVVLQVWPDInpagqlLLLDEPMNSLDVAQQAA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1149890125 224 VLLLLKRMSKQGRTIIFSIHQPRYSiFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:PRK03695 172 LDRLLSELCQQGIAVVMSSHDLNHT-LRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
63-264 |
4.08e-12 |
|
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: 66.34 E-value: 4.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 63 ILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGlsGDVLINGAPRPANFKCNSGYVV----QDDVVMGTlTVR 137
Cdd:cd03248 29 VLQDVSFTLHPGeVTALVGPSGSGKSTVVALLENFYQPQG--GQVLLDGKPISQYEHKYLHSKVslvgQEPVLFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 138 ENLQFsaALRLATTMTNHEKNERIN--RVIQEL--GLDKVADSKvGTQfirgVSGGERKRTSIGMELITDPSILFLDEPT 213
Cdd:cd03248 106 DNIAY--GLQSCSFECVKEAAQKAHahSFISELasGYDTEVGEK-GSQ----LSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1149890125 214 TGLDSSTANAVLLLLkRMSKQGRTIIFSIHqpRYSIFKLFDSLTLLASGRL 264
Cdd:cd03248 179 SALDAESEQQVQQAL-YDWPERRTVLVIAH--RLSTVERADQILVLDGGRI 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
78-274 |
4.33e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.46 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 78 ILGPTGGGKSSLLDV---LAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQfsAALRLATTMTN 154
Cdd:PRK10895 34 LLGPNGAGKTTTFYMvvgIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEASIFRRLSVYDNLM--AVLQIRDDLSA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 155 HEKNERINRVIQELGLDKVADSkVGtqfiRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ 234
Cdd:PRK10895 112 EQREDRANELMEEFHIEHLRDS-MG----QSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDS 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1149890125 235 GRTIIFSIHQPRYSIfKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:PRK10895 187 GLGVLITDHNVRETL-AVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
60-239 |
4.34e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 69.08 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP---------RPAnfkcnSGYVVQDdV 129
Cdd:COG5265 370 ERPILKGVSFEVPAGKTvAIVGPSGAGKSTLARLLFRFYDVT--SGRILIDGQDirdvtqaslRAA-----IGIVPQD-T 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 130 VMGTLTVRENLQFS----------AALRLAttmtnhekneRINRVIQEL--GLDkvadSKVGTqfiRGV--SGGERKRTS 195
Cdd:COG5265 442 VLFNDTIAYNIAYGrpdaseeeveAAARAA----------QIHDFIESLpdGYD----TRVGE---RGLklSGGEKQRVA 504
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1149890125 196 IGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSkQGRTII 239
Cdd:COG5265 505 IARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTL 547
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
58-243 |
4.58e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.42 E-value: 4.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 58 PVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRPANFKCNSGYVVQDDVVMGtLTV 136
Cdd:PRK13651 17 PTELKALDNVSVEINQGeFIAIIGQTGSGKTTFIEHLNALLLPD--TGTIEWIFKDEKNKKKTKEKEKVLEKLVIQ-KTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 137 RENLQFSAALR---------------------------LATTMTNHEKNERINRVIQELGLDKVADSKvgTQFirGVSGG 189
Cdd:PRK13651 94 FKKIKKIKEIRrrvgvvfqfaeyqlfeqtiekdiifgpVSMGVSKEEAKKRAAKYIELVGLDESYLQR--SPF--ELSGG 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1149890125 190 ERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIH 243
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
44-269 |
5.84e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.42 E-value: 5.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 44 YRVKLK-SGFLPC------RKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLaarkdpSGL----SGDVLINGA 111
Cdd:COG4586 11 YRVYEKePGLKGAlkglfrREYREVEAVDDISFTIEPGeIVGFIGPNGAGKSTTIKML------TGIlvptSGEVRVLGY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 112 pRPanFKCNSGYVVQDDVVMGT-------LTVRENLQFSAAL-RLattmTNHEKNERINRVIQELGLDKVADskvgtQFI 183
Cdd:COG4586 85 -VP--FKRRKEFARRIGVVFGQrsqlwwdLPAIDSFRLLKAIyRI----PDAEYKKRLDELVELLDLGELLD-----TPV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 184 RGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHqprYS--IFKLFDSLTLLA 260
Cdd:COG4586 153 RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSH---DMddIEALCDRVIVID 229
|
....*....
gi 1149890125 261 SGRLMFHGP 269
Cdd:COG4586 230 HGRIIYDGS 238
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
60-287 |
7.60e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.20 E-value: 7.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRPAnfkcnsgyvVQDDVVMGTLTVRE 138
Cdd:PRK10789 327 DHPALENVNFTLKPGqMLGICGPTGSGKSTLLSLIQRHFDVS--EGDIRFHDIPLTK---------LQLDSWRSRLAVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 139 NLQF--------SAAL-RLATTMTNHEKNERINRVIQE-LGLDKVADSKVGTqfiRGV--SGGERKRTSIGMELITDPSI 206
Cdd:PRK10789 396 QTPFlfsdtvanNIALgRPDATQQEIEHVARLASVHDDiLRLPQGYDTEVGE---RGVmlSGGQKQRISIARALLLNAEI 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 207 LFLDEPTTGLDSSTANAVLLLLKRMSkQGRTIIFSIHqpRYSIFKLFDSLTLLASGRLMFHGPAQEALgyfESAGYHCEA 286
Cdd:PRK10789 473 LILDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAH--RLSALTEASEILVMQHGHIAQRGNHDQLA---QQSGWYRDM 546
|
.
gi 1149890125 287 Y 287
Cdd:PRK10789 547 Y 547
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
77-240 |
9.77e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 67.74 E-value: 9.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLaarkdpSGL----SGDVLINGA------PRPANfKCNSGYVVQDDVVMGTLTVRENLQFSAAL 146
Cdd:COG3845 35 ALLGENGAGKSTLMKIL------YGLyqpdSGEILIDGKpvrirsPRDAI-ALGIGMVHQHFMLVPNLTVAENIVLGLEP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 147 RLATTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLL 226
Cdd:COG3845 108 TKGGRLDRKAARARIRELSERYGLDVDPDAKVED-----LSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFE 182
|
170
....*....|....
gi 1149890125 227 LLKRMSKQGRTIIF 240
Cdd:COG3845 183 ILRRLAAEGKSIIF 196
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
63-274 |
1.69e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.23 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 63 ILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLS------GDVLINGAP----RPANFKCNSGYVVQDDVVM 131
Cdd:PRK13547 16 ILRDLSLRIEPGrVTALLGRNGAGKSTLLKALAGDLTGGGAPrgarvtGDVTLNGEPlaaiDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 132 GTLTVRENL---QFSAALRLATTmtNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMEL-------- 200
Cdd:PRK13547 96 FAFSAREIVllgRYPHARRAGAL--THRDGEIAWQALALAGATALVGRDVTT-----LSGGELARVQFARVLaqlwpphd 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 201 -ITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSI-HQP----RYSifklfDSLTLLASGRLMFHGPAQEAL 274
Cdd:PRK13547 169 aAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIvHDPnlaaRHA-----DRIAMLADGAIVAHGAPADVL 243
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
62-272 |
1.90e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.00 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 62 EILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPR----PANFKCNSGYVV-QDDVVMGTLT 135
Cdd:PRK15439 25 EVLKGIDFTLHAGeVHALLGGNGAGKSTLMKIIAGIVPPD--SGTLEIGGNPCarltPAKAHQLGIYLVpQEPLLFPNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 136 VRENLQFSaalrlattMTNHEKN-ERINRVIQELGLDKVADSKVGTQFIrgvsgGERKRTSIGMELITDPSILFLDEPTT 214
Cdd:PRK15439 103 VKENILFG--------LPKRQASmQKMKQLLAALGCQLDLDSSAGSLEV-----ADRQIVEILRGLMRDSRILILDEPTA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1149890125 215 GLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK15439 170 SLTPAETERLFSRIRELLAQGVGIVFISHKLP-EIRQLADRISVMRDGTIALSGKTAD 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
61-272 |
2.04e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 64.77 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 61 KEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLS---GDVLINGApRPAN--------FKCNSGYVVQDD 128
Cdd:PRK11264 16 QTVLHGIDLEVKPGeVVAIIGPSGSGKTTLLRCINLLEQPEAGTirvGDITIDTA-RSLSqqkglirqLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 129 VVMGTLTVRENLqfsaaLRLATTMTNHEKNERINRViQELgLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILF 208
Cdd:PRK11264 95 NLFPHRTVLENI-----IEGPVIVKGEPKEEATARA-REL-LAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149890125 209 LDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSiFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFA-RDVADRAIFMDQGRIVEQGPAKA 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
77-240 |
2.73e-11 |
|
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: 65.07 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKS----SLLDVLaarKDPSGLSGDVLING-----APRPA--NFKCNS-GYVVQDdvVMGTL----TVREnl 140
Cdd:COG0444 35 GLVGESGSGKStlarAILGLL---PPPGITSGEILFDGedllkLSEKElrKIRGREiQMIFQD--PMTSLnpvmTVGD-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 141 QFSAALRLATTMTNHEKNERINRVIQELGLD---KVADSKVGtQFirgvSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:COG0444 108 QIAEPLRIHGGLSKAEARERAIELLERVGLPdpeRRLDRYPH-EL----SGGMRQRVMIARALALEPKLLIADEPTTALD 182
|
170 180
....*....|....*....|....
gi 1149890125 218 SSTANAVLLLLKRMSKQ-GRTIIF 240
Cdd:COG0444 183 VTIQAQILNLLKDLQRElGLAILF 206
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
61-243 |
4.34e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 62.97 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 61 KEILSNINGIMKPGLNAIL-GPTGGGKSSLLDVLAARKDPSglSGDVLING------APRPANF-KCNSGYVVQDDVVMG 132
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLtGHSGAGKSTLLKLICGIERPS--AGKIWFSGhditrlKNREVPFlRRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 133 TLTVRENLQFSAALRLATTmtnheknERINRVIQElGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEP 212
Cdd:PRK10908 93 DRTVYDNVAIPLIIAGASG-------DDIRRRVSA-ALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190
....*....|....*....|....*....|.
gi 1149890125 213 TTGLDSSTANAVLLLLKRMSKQGRTIIFSIH 243
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
58-220 |
4.35e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.73 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 58 PVEKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAarkdpsGLSGDvlINGAPRPA-NFKCnsGYVVQDDVVMGTLT 135
Cdd:TIGR03719 15 PPKKEILKDISLSFFPGAKiGVLGLNGAGKSTLLRIMA------GVDKD--FNGEARPQpGIKV--GYLPQEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 136 VRENL---------------QFSAAL--------RLATTMTN----------HEKNERINRVIQELGLDKvADSKVGTqf 182
Cdd:TIGR03719 85 VRENVeegvaeikdaldrfnEISAKYaepdadfdKLAAEQAElqeiidaadaWDLDSQLEIAMDALRCPP-WDADVTK-- 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1149890125 183 irgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSST 220
Cdd:TIGR03719 162 ---LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
64-264 |
4.69e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.70 E-value: 4.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGapRPANFK-----CNSGYVV--QDDVVMGTLT 135
Cdd:PRK11288 20 LDDISFDCRAGqVHALMGENGAGKSTLLKILSGNYQPD--AGSILIDG--QEMRFAsttaaLAAGVAIiyQELHLVPEMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 136 VRENL---QFSAALRLAttmtnHEK--NERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLD 210
Cdd:PRK11288 96 VAENLylgQLPHKGGIV-----NRRllNYEAREQLEHLGVDIDPDTPLKY-----LSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1149890125 211 EPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRL 264
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRME-EIFALCDAITVFKDGRY 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
61-277 |
5.28e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 65.59 E-value: 5.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 61 KEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLIN----------------GAPRPanfKCNSGY 123
Cdd:TIGR03269 13 KEVLKNISFTIEEGeVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHvalcekcgyverpskvGEPCP---VCGGTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 124 VVQD-DVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQ---ELG-------------LDKVADSKVGTQFIRGV 186
Cdd:TIGR03269 90 EPEEvDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEaleEIGyegkeavgravdlIEMVQLSHRITHIARDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 187 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL-LLLKRMSKQGRTIIFSIHQPRYsIFKLFDSLTLLASGRLM 265
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHnALEEAVKASGISMVLTSHWPEV-IEDLSDKAIWLENGEIK 248
|
250
....*....|..
gi 1149890125 266 FHGPAQEALGYF 277
Cdd:TIGR03269 249 EEGTPDEVVAVF 260
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
60-282 |
5.56e-11 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 63.05 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLING---APRPANFKCNSGYVV--QDDVVMGT 133
Cdd:TIGR01978 12 DKEILKGVNLTVKKGeIHAIMGPNGSGKSTLSKTIAGHPSYEVTSGTILFKGqdlLELEPDERARAGLFLafQYPEEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 134 LTVRENLQFSA-ALRLA---TTMTNHEKNERINRVIQELGLDK-VADSKVGTQFirgvSGGERKRTSIGMELITDPSILF 208
Cdd:TIGR01978 92 VSNLEFLRSALnARRSArgeEPLDLLDFEKLLKEKLALLDMDEeFLNRSVNEGF----SGGEKKRNEILQMALLEPKLAI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149890125 209 LDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRysIFKLF--DSLTLLASGRLMFHGPAQEALgYFESAGY 282
Cdd:TIGR01978 168 LDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQR--LLNYIkpDYVHVLLDGRIVKSGDVELAK-ELEAKGY 240
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
77-272 |
5.74e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.42 E-value: 5.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAA--RKDpsglSGDVLINGAP-RPANFK--CNSGYVV--QDDVVMGTLTVRENLqfsaAL-RL 148
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGvyQPD----SGEILLDGEPvRFRSPRdaQAAGIAIihQELNLVPNLSVAENI----FLgRE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 149 ATT--MTNHEK-NERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL 225
Cdd:COG1129 106 PRRggLIDWRAmRRRARELLARLGLDIDPDTPVGD-----LSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLF 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1149890125 226 LLLKRMSKQGRTIIFsIhqpryS-----IFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:COG1129 181 RIIRRLKAQGVAIIY-I-----ShrldeVFEIADRVTVLRDGRLVGTGPVAE 226
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
35-265 |
7.87e-11 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 63.29 E-value: 7.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 35 AVLSFHNICYRVKlKSGFLpcRKPVEKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP- 112
Cdd:TIGR02769 1 SLLEVRDVTHTYR-TGGLF--GAKQRAPVLTNVSLSIEEGETvGLLGRSGCGKSTLARLLLGLEKPA--QGTVSFRGQDl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 113 ---RPAN---FKCNSGYVVQD--DVVMGTLTVRENLqfSAALRLATTMTNHEKNERINRVIQELGLDkvadSKVGTQFIR 184
Cdd:TIGR02769 76 yqlDRKQrraFRRDVQLVFQDspSAVNPRMTVRQII--GEPLRHLTSLDESEQKARIAELLDMVGLR----SEDADKLPR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 185 GVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRySIFKLFDSLTLLASGR 263
Cdd:TIGR02769 150 QLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLR-LVQSFCQRVAVMDKGQ 228
|
..
gi 1149890125 264 LM 265
Cdd:TIGR02769 229 IV 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
64-262 |
8.24e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 8.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRPA-----NFKCNSGYVVQDDVVMGTLTVR 137
Cdd:PRK09700 21 LKSVNLTVYPGeIHALLGENGAGKSTLMKVLSGIHEPT--KGTITINNINYNKldhklAAQLGIGIIYQELSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 138 ENLQFSaalRLAT-------TMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLD 210
Cdd:PRK09700 99 ENLYIG---RHLTkkvcgvnIIDWREMRVRAAMMLLRVGLKVDLDEKVAN-----LSISHKQMLEIAKTLMLDAKVIIMD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1149890125 211 EPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASG 262
Cdd:PRK09700 171 EPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLA-EIRRICDRYTVMKDG 221
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
60-284 |
1.01e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 62.74 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAP---RPANFKCNSG------YVVQDDV 129
Cdd:CHL00131 19 ENEILKGLNLSINKGeIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKGESildLEPEERAHLGiflafqYPIEIPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 130 VmgtltvrENLQFsaaLRLATTMTNHEKN----------ERINRVIQELGLDKVadskvgtqFI-----RGVSGGERKRT 194
Cdd:CHL00131 99 V-------SNADF---LRLAYNSKRKFQGlpeldpleflEIINEKLKLVGMDPS--------FLsrnvnEGFSGGEKKRN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 195 SIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDYVHVMQNGKIIKTGDAELAK 240
|
250
....*....|
gi 1149890125 275 gYFESAGYHC 284
Cdd:CHL00131 241 -ELEKKGYDW 249
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
64-274 |
1.73e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 62.31 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 64 LSNIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRPANFKCNS-----GYVVQD-DVVMGTLTV 136
Cdd:PRK13644 18 LENINlVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ--KGKVLVSGIDTGDFSKLQGirklvGIVFQNpETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 137 RENLQFSAA-LRLATTmtnhEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTG 215
Cdd:PRK13644 96 EEDLAFGPEnLCLPPI----EIRKRVDRALAEIGLEKYRHRSPKT-----LSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1149890125 216 LDSSTANAVLLLLKRMSKQGRTIIFSIHQprYSIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHEKGKTIVYITHN--LEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
77-217 |
2.12e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.99 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLA-ARKDPSG----LSGDVLING-----APRPAnfkcnsgYVVQddvvmG-------TLTVREN 139
Cdd:NF033858 31 GLIGPDGVGKSSLLSLIAgARKIQQGrvevLGGDMADARhrravCPRIA-------YMPQ-----GlgknlypTLSVFEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 140 LQFSAalRL----AttmtnHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTG 215
Cdd:NF033858 99 LDFFG--RLfgqdA-----AERRRRIDELLRATGLAPFADRPAGK-----LSGGMKQKLGLCCALIHDPDLLILDEPTTG 166
|
..
gi 1149890125 216 LD 217
Cdd:NF033858 167 VD 168
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
77-243 |
2.26e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 61.68 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLING-APRPANFK---CNSGYVVQD-DVVMGTLTVRENLQFSAalrLATT 151
Cdd:PRK13647 35 ALLGPNGAGKSTLLLHLNGIYLPQ--RGRVKVMGrEVNAENEKwvrSKVGLVFQDpDDQVFSSTVWDDVAFGP---VNMG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 152 MTNHEKNERINRVIQELGLDKVADSKVgtqfiRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRM 231
Cdd:PRK13647 110 LDKDEVERRVEEALKAVRMWDFRDKPP-----YHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRL 184
|
170
....*....|..
gi 1149890125 232 SKQGRTIIFSIH 243
Cdd:PRK13647 185 HNQGKTVIVATH 196
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
62-272 |
2.63e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.47 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 62 EILSNINGIMKPG-LNAILGPTGGGKSSLLDV---LAARKDPSGLSGDVLINGAprpANFKCN-------SGYVVQDDVV 130
Cdd:PRK14247 17 EVLDGVNLEIPDNtITALMGPSGSGKSTLLRVfnrLIELYPEARVSGEVYLDGQ---DIFKMDvielrrrVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 131 MGTLTVRENLQFSAAL-RLATTmtNHEKNERINRVIQELGL-DKVADsKVGTQFIRgVSGGERKRTSIGMELITDPSILF 208
Cdd:PRK14247 94 IPNLSIFENVALGLKLnRLVKS--KKELQERVRWALEKAQLwDEVKD-RLDAPAGK-LSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149890125 209 LDEPTTGLD-SSTANAVLLLLKRmsKQGRTIIFSIHQPRYSIfKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK14247 170 ADEPTANLDpENTAKIESLFLEL--KKDMTIVLVTHFPQQAA-RISDYVAFLYKGQIVEWGPTRE 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
58-272 |
3.17e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 61.77 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 58 PVEKEILSNIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING---APRPAN-----FKCNSGYVVQ-D 127
Cdd:PRK13641 17 PMEKKGLDNISfELEEGSFVALVGHTGSGKSTLMQHFNALLKPS--SGTITIAGyhiTPETGNknlkkLRKKVSLVFQfP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 128 DVVMGTLTVRENLQFSAalrLATTMTNHEKNERINRVIQELGLDKVADSKvgTQFirGVSGGERKRTSIGMELITDPSIL 207
Cdd:PRK13641 95 EAQLFENTVLKDVEFGP---KNFGFSEDEAKEKALKWLKKVGLSEDLISK--SPF--ELSGGQMRRVAIAGVMAYEPEIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149890125 208 FLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK13641 168 CLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMD-DVAEYADDVLVLEHGKLIKHASPKE 231
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
62-274 |
3.80e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 60.49 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 62 EILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGlsGDVLING--APRPANFKCN----SGYVVQDDVVMGTL 134
Cdd:PRK09493 15 QVLHNIDLNIDQGeVVVIIGPSGSGKSTLLRCINKLEEITS--GDLIVDGlkVNDPKVDERLirqeAGMVFQQFYLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 135 TVRENLQFsaalrlATTMTNHEKNERINRVIQELgLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTT 214
Cdd:PRK09493 93 TALENVMF------GPLRVRGASKEEAEKQAREL-LAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 215 GLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSiFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:PRK09493 166 ALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFA-EKVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
60-229 |
8.46e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 59.79 E-value: 8.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKP-GLNAILGPTGGGKSSLLDVLAARKD--PS-GLSGDVLING----APR--PANFKCNSGYVVQDDV 129
Cdd:PRK14239 17 KKKALNSVSLDFYPnEITALIGPSGSGKSTLLRSINRMNDlnPEvTITGSIVYNGhniySPRtdTVDLRKEIGMVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 130 VMgTLTVRENLQFsaALRLATTMTNHEKNERINRVIQELGL-----DKVADSKVGtqfirgVSGGERKRTSIGMELITDP 204
Cdd:PRK14239 97 PF-PMSIYENVVY--GLRLKGIKDKQVLDEAVEKSLKGASIwdevkDRLHDSALG------LSGGQQQRVCIARVLATSP 167
|
170 180
....*....|....*....|....*...
gi 1149890125 205 SILFLDEPTTGLDSSTANAV---LLLLK 229
Cdd:PRK14239 168 KIILLDEPTSALDPISAGKIeetLLGLK 195
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
58-243 |
1.22e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 59.79 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 58 PVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP----------RPANFKCnsGYVVQ 126
Cdd:PRK13646 17 PYEHQAIHDVNTEFEQGkYYAIVGQTGSGKSTLIQNINALLKPT--TGTVTVDDITithktkdkyiRPVRKRI--GMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 127 -------DDvvmgtlTVRENLQFSAAlrlATTMTNHEKNERINRVIQELGLDKVADSKVGTQfirgVSGGERKRTSIGME 199
Cdd:PRK13646 93 fpesqlfED------TVEREIIFGPK---NFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQ----MSGGQMRKIAIVSI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1149890125 200 LITDPSILFLDEPTTGLDSSTANAVLLLLKRMS-KQGRTIIFSIH 243
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSH 204
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
181-278 |
1.46e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 59.25 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 181 QFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYsIFKLFDSLTLLA 260
Cdd:PRK13638 132 QPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLR 210
|
90
....*....|....*...
gi 1149890125 261 SGRLMFHGPAQEALGYFE 278
Cdd:PRK13638 211 QGQILTHGAPGEVFACTE 228
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
77-244 |
1.55e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 61.01 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLaarkdpSGL---SGDVLINGAPR----PANFKCNSGYVVQDDVVM-GTLtvRENL-------- 140
Cdd:PRK11174 380 ALVGPSGAGKTSLLNAL------LGFlpyQGSLKINGIELreldPESWRKHLSWVGQNPQLPhGTL--RDNVllgnpdas 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 141 --QFSAALRLAttmtnhEKNERINRviQELGLdkvaDSKVGTQFIrGVSGGERKRTSIGMELITDPSILFLDEPTTGLDS 218
Cdd:PRK11174 452 deQLQQALENA------WVSEFLPL--LPQGL----DTPIGDQAA-GLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180
....*....|....*....|....*.
gi 1149890125 219 STANAVLLLLKRMSkQGRTIIFSIHQ 244
Cdd:PRK11174 519 HSEQLVMQALNAAS-RRQTTLMVTHQ 543
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
61-272 |
1.64e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 59.34 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 61 KEILSNIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDP-SGL--SGDVLINGAP-----RPANFKCNSGYVVQDDVVM 131
Cdd:PRK14271 34 KTVLDQVSmGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvSGYrySGDVLLGGRSifnyrDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 132 gTLTVRENLQfsAALRLATTMTNHEKNERINRVIQELGL-DKVADSKVGTQFirGVSGGERKRTSIGMELITDPSILFLD 210
Cdd:PRK14271 114 -PMSIMDNVL--AGVRAHKLVPRKEFRGVAQARLTEVGLwDAVKDRLSDSPF--RLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149890125 211 EPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSifKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAA--RISDRAALFFDGRLVEEGPTEQ 248
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
62-279 |
2.35e-09 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 60.52 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 62 EILSNIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRpANFKCNS-----GYVVQDDVVMgTLT 135
Cdd:TIGR01193 488 NILSDISlTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR--SGEILLNGFSL-KDIDRHTlrqfiNYLPQEPYIF-SGS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 136 VRENLQFSA-----------ALRLATTMTNHEKnerinrviQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDP 204
Cdd:TIGR01193 564 ILENLLLGAkenvsqdeiwaACEIAEIKDDIEN--------MPLGYQTELSEEGSS-----ISGGQKQRIALARALLTDS 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149890125 205 SILFLDEPTTGLDSSTANAVLLLLKRMskQGRTIIFSIHqpRYSIFKLFDSLTLLASGRLMFHGPAQEAL---GYFES 279
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVNNLLNL--QDKTIIFVAH--RLSVAKQSDKIIVLDHGKIIEQGSHDELLdrnGFYAS 704
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
62-272 |
2.69e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 58.31 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 62 EILSNIN-GIMKPGLNAILGPTGGGKSSLL---DVLAARKDPSGLSGDVLING----APR--PANFKCNSGYVVQDDVVM 131
Cdd:PRK14267 18 HVIKGVDlKIPQNGVFALMGPSGCGKSTLLrtfNRLLELNEEARVEGEVRLFGrniySPDvdPIEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 132 GTLTVRENLQFSAALRlATTMTNHEKNERINRVIQELGL-DKVADSKvgTQFIRGVSGGERKRTSIGMELITDPSILFLD 210
Cdd:PRK14267 98 PHLTIYDNVAIGVKLN-GLVKSKKELDERVEWALKKAALwDEVKDRL--NDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149890125 211 EPTTGLDSSTANAVLLLLKRMsKQGRTIIFSIHQPRYSIfKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPAQAA-RVSDYVAFLYLGKLIEVGPTRK 234
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
77-264 |
3.01e-09 |
|
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: 56.28 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGapRPANFkcnsgyvvqddvvmgtLTVREnlqfsaALRLattmtnhe 156
Cdd:cd03216 30 ALLGENGAGKSTLMKILSGLYKPD--SGEILVDG--KEVSF----------------ASPRD------ARRA-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 157 kneRINRVIQelgldkvadskvgtqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGR 236
Cdd:cd03216 76 ---GIAMVYQ-------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGV 133
|
170 180
....*....|....*....|....*...
gi 1149890125 237 TIIFSIHQPRySIFKLFDSLTLLASGRL 264
Cdd:cd03216 134 AVIFISHRLD-EVFEIADRVTVLRDGRV 160
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
77-231 |
3.26e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.01 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLING-------------APRPANFKCNSGYVVQDDvvmgtltvRENL--Q 141
Cdd:PRK11701 36 GIVGESGSGKTTLLNALSARLAPD--AGEVHYRMrdgqlrdlyalseAERRRLLRTEWGFVHQHP--------RDGLrmQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 142 FSA----ALRLATTMTNHEKNER------INRViqELGLDKVADskVGTQFirgvSGGERKRTSIGMELITDPSILFLDE 211
Cdd:PRK11701 106 VSAggniGERLMAVGARHYGDIRatagdwLERV--EIDAARIDD--LPTTF----SGGMQQRLQIARNLVTHPRLVFMDE 177
|
170 180
....*....|....*....|
gi 1149890125 212 PTTGLDSSTANAVLLLLKRM 231
Cdd:PRK11701 178 PTGGLDVSVQARLLDLLRGL 197
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
185-272 |
3.71e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 58.71 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 185 GVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGRL 264
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTME-HVLEVADEVIVMDKGKI 254
|
....*...
gi 1149890125 265 MFHGPAQE 272
Cdd:PRK13631 255 LKTGTPYE 262
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
187-271 |
3.81e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.72 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 187 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQPRySIFKLFDSLTLLASGRLM 265
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLS-IVRKLADRVAVMQNGRCV 236
|
....*.
gi 1149890125 266 FHGPAQ 271
Cdd:PRK15134 237 EQNRAA 242
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
60-272 |
5.24e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 57.36 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNIN-GIMKPGLNAILGPTGGGKSSLLDVL----AARKDPSGLSGDVLINGAP----RPANFKCNSGYVVQDDVV 130
Cdd:PRK14246 22 DKAILKDITiKIPNNSIFGIMGPSGSGKSTLLKVLnrliEIYDSKIKVDGKVLYFGKDifqiDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 131 MGTLTVRENLQFSaaLRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRgVSGGERKRTSIGMELITDPSILFLD 210
Cdd:PRK14246 102 FPHLSIYDNIAYP--LKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQ-LSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149890125 211 EPTTGLDSSTANAVLLLLKRMSKQgRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQ-QVARVADYVAFLYNGELVEWGSSNE 238
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
243-300 |
5.34e-09 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 58.76 E-value: 5.34e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1149890125 243 HQPRYSIFKLFDSLTLLASGRLM-FHGPAQEALGYFESAGYHCEAYNNPADFFLDIING 300
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGLTvYHGPVKKVEEYFAGLGINVPERVNPPDHFIDILEG 59
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
46-272 |
7.15e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.22 E-value: 7.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 46 VKLKSGFLPCRKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLSGdVLINGAprpanfkcnSGYV 124
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGsLVAIVGGTGEGKTSLISAMLGELSHAETSS-VVIRGS---------VAYV 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 125 VQDDVVMGTlTVRENLQFSAALrlattmtnheKNERINRVIQELGLDKVADSKVGTQFI----RGV--SGGERKRTSIGM 198
Cdd:PLN03232 685 PQVSWIFNA-TVRENILFGSDF----------ESERYWRAIDVTALQHDLDLLPGRDLTeigeRGVniSGGQKQRVSMAR 753
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149890125 199 ELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYsiFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PLN03232 754 AVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHF--LPLMDRIILVSEGMIKEEGTFAE 825
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
56-237 |
7.52e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 57.00 E-value: 7.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 56 RKPVEKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSGlsGDVLINGAP-------RPANFKCNSGYVVQD 127
Cdd:PRK10419 20 GKHQHQTVLNNVSLSLKSGETvALLGRSGCGKSTLARLLVGLESPSQ--GNVSWRGEPlaklnraQRKAFRRDIQMVFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 128 DV--VMGTLTVRENLqfSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQfirgVSGGERKRTSIGMELITDPS 205
Cdd:PRK10419 98 SIsaVNPRKTVREII--REPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQ----LSGGQLQRVCLARALAVEPK 171
|
170 180 190
....*....|....*....|....*....|..
gi 1149890125 206 ILFLDEPTTGLDSSTANAVLLLLKRMSKQGRT 237
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKKLQQQFGT 203
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
187-272 |
8.12e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.82 E-value: 8.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 187 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIhQPRYSIFKLFDSLTLLASGRLMF 266
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTT-QYMEEAEQLAHELTVIDRGRVIA 224
|
....*.
gi 1149890125 267 HGPAQE 272
Cdd:NF000106 225 DGKVDE 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
63-303 |
8.14e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.81 E-value: 8.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 63 ILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAprpaNFKCNSgyVVQDDVVM--------GT 133
Cdd:PRK11432 21 VIDNLNLTIKQGtMVTLLGPSGCGKTTVLRLVAGLEKPT--EGQIFIDGE----DVTHRS--IQQRDICMvfqsyalfPH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 134 LTVRENLQFsaALRlattMTNHEKNERINRVIQELGLdkVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPT 213
Cdd:PRK11432 93 MSLGENVGY--GLK----MLGVPKEERKQRVKEALEL--VDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 214 TGLDsstANavllLLKRMSKQGRTIifsihQPRYSIFKLF------------DSLTLLASGRLMFHGPAQealgyfesag 281
Cdd:PRK11432 165 SNLD---AN----LRRSMREKIREL-----QQQFNITSLYvthdqseafavsDTVIVMNKGKIMQIGSPQ---------- 222
|
250 260
....*....|....*....|..
gi 1149890125 282 yhcEAYNNPADFFLDIINGDST 303
Cdd:PRK11432 223 ---ELYRQPASRFMASFMGDAN 241
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
77-240 |
8.17e-09 |
|
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: 55.52 E-value: 8.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRPAN-----FKCNSGYVVQD---DVVMGTLTVRENLQFSAALrl 148
Cdd:cd03215 30 GIAGLVGNGQTELAEALFGLRPPA--SGEITLDGKPVTRRsprdaIRAGIAYVPEDrkrEGLVLDLSVAENIALSSLL-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 149 attmtnheknerinrviqelgldkvadskvgtqfirgvSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLL 228
Cdd:cd03215 106 --------------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLI 147
|
170
....*....|..
gi 1149890125 229 KRMSKQGRTIIF 240
Cdd:cd03215 148 RELADAGKAVLL 159
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
78-240 |
9.87e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.11 E-value: 9.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 78 ILGPTG--G-GKSSLLDVL--AARKDpsglSGDVLINGapRPANFKCNS-------GYVVQD---DVVMGTLTVRENLQF 142
Cdd:COG1129 280 ILGIAGlvGaGRTELARALfgADPAD----SGEIRLDG--KPVRIRSPRdairagiAYVPEDrkgEGLVLDLSIRENITL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 143 SAALRLATTMTNHEKNER--INRVIQELGLdKVADSKvgtQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSST 220
Cdd:COG1129 354 ASLDRLSRGGLLDRRRERalAEEYIKRLRI-KTPSPE---QPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGA 429
|
170 180
....*....|....*....|
gi 1149890125 221 ANAVLLLLKRMSKQGRTIIF 240
Cdd:COG1129 430 KAEIYRLIRELAAEGKAVIV 449
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
187-239 |
1.11e-08 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 55.90 E-value: 1.11e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1149890125 187 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTII 239
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
64-247 |
1.28e-08 |
|
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: 55.80 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 64 LSNINGIMKPG-LNAILGPTGGGKSSLLdvLAARKDPSGLSGDVLINGAPRPANFKCNS--------GYVVQDDVVMGTl 134
Cdd:cd03290 17 LSNINIRIPTGqLTMIVGQVGCGKSSLL--LAILGEMQTLEGKVHWSNKNESEPSFEATrsrnrysvAYAAQKPWLLNA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 135 TVRENLQFSAALrlattmtnheKNERINRVIQELGLDKVAD-------SKVGTQFIrGVSGGERKRTSIGMELITDPSIL 207
Cdd:cd03290 94 TVEENITFGSPF----------NKQRYKAVTDACSLQPDIDllpfgdqTEIGERGI-NLSGGQRQRICVARALYQNTNIV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1149890125 208 FLDEPTTGLDSSTANAVLL--LLKRMSKQGRTIIFSIHQPRY 247
Cdd:cd03290 163 FLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
78-239 |
1.49e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.87 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 78 ILGPTGGGKSSLLDVLAARKDPSG--LSGDVLINGAPRpanfkcnsgYVVQDdvvmGTLTVRENLQFSAALRLATTMTNH 155
Cdd:COG1245 371 IVGPNGIGKTTFAKILAGVLKPDEgeVDEDLKISYKPQ---------YISPD----YDGTVEEFLRSANTDDFGSSYYKT 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 156 EknerinrVIQELGLDKVADSKVgtqfiRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMS-KQ 234
Cdd:COG1245 438 E-------IIKPLGLEKLLDKNV-----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAeNR 505
|
....*
gi 1149890125 235 GRTII 239
Cdd:COG1245 506 GKTAM 510
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
60-229 |
2.13e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 57.00 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG--LnAILGPTGGGKSSLLDVLAARKDPsgLSGDVLInGAprpanfKCNSGYVVQD-DVVMGTLTV 136
Cdd:COG0488 327 DKTLLDDLSLRIDRGdrI-GLIGPNGAGKSTLLKLLAGELEP--DSGTVKL-GE------TVKIGYFDQHqEELDPDKTV 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 137 RENLQfsaalRLATTMTNHEknerinrVIQELGL-----DKVaDSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDE 211
Cdd:COG0488 397 LDELR-----DGAPGGTEQE-------VRGYLGRflfsgDDA-FKPVGV-----LSGGEKARLALAKLLLSPPNVLLLDE 458
|
170
....*....|....*...
gi 1149890125 212 PTTGLDSSTANAVLLLLK 229
Cdd:COG0488 459 PTNHLDIETLEALEEALD 476
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
78-230 |
2.25e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 55.49 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 78 ILGPTGGGKSSLLDVLAARKDPSGlsGDVLING---APRPANFKCNSgyvvqddvvmgTLTVRENLqfSAALRLATTmTN 154
Cdd:cd03237 30 ILGPNGIGKTTFIKMLAGVLKPDE--GDIEIELdtvSYKPQYIKADY-----------EGTVRDLL--SSITKDFYT-HP 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149890125 155 HEKNErinrVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKR 230
Cdd:cd03237 94 YFKTE----IAKPLQIEQILDREVPE-----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
58-217 |
2.86e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 58 PVEKEILSNINGIMKPGlnA---ILGPTGGGKSSLLDVLAarkdpsGLsgDVLINGAPRPA-NFKCnsGYVVQDDVVMGT 133
Cdd:PRK11819 17 PPKKQILKDISLSFFPG--AkigVLGLNGAGKSTLLRIMA------GV--DKEFEGEARPApGIKV--GYLPQEPQLDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 134 LTVRENLQFSAALRLAttmtnheKNERINRVIQELG-----LDKVA------------------DSKV-----------G 179
Cdd:PRK11819 85 KTVRENVEEGVAEVKA-------ALDRFNEIYAAYAepdadFDALAaeqgelqeiidaadawdlDSQLeiamdalrcppW 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1149890125 180 TQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:PRK11819 158 DAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
70-217 |
2.90e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 56.38 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 70 IMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING------AP--RPANFkcnsgyVVQDDVVMGTLTVRENLQ 141
Cdd:PRK11607 42 IYKGEIFALLGASGCGKSTLLRMLAGFEQPT--AGQIMLDGvdlshvPPyqRPINM------MFQSYALFPHMTVEQNIA 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149890125 142 FSAAL-RLAttmtnheKNERINRVIQELGLdkVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:PRK11607 114 FGLKQdKLP-------KAEIASRVNEMLGL--VHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
56-272 |
2.99e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.41 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 56 RKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDP-SGLS--GDVLINGAPRPANFKC---NSGYV---- 124
Cdd:PRK13634 15 KTPFERRALYDVNVSIPSGsYVAIIGHTGSGKSTLLQHLNGLLQPtSGTVtiGERVITAGKKNKKLKPlrkKVGIVfqfp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 125 --------VQDDVVMGTLT--VREnlqfSAALRLATTMtnheknerinrvIQELGLDKvadsKVGTQFIRGVSGGERKRT 194
Cdd:PRK13634 95 ehqlfeetVEKDICFGPMNfgVSE----EDAKQKAREM------------IELVGLPE----ELLARSPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 195 SIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK-QGRTIIFSIHQ----PRYSifklfDSLTLLASGRLMFHGP 269
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSmedaARYA-----DQIVVMHKGTVFLQGT 229
|
...
gi 1149890125 270 AQE 272
Cdd:PRK13634 230 PRE 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
78-266 |
3.26e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.89 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 78 ILGPTGGGKSSLLDVLAArkDPSGLSGDVLINGA-----PRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALrlattM 152
Cdd:PRK11614 36 LIGANGAGKTTLLGTLCG--DPRATSGRIVFDGKditdwQTAKIMREAVAIVPEGRRVFSRMTVEENLAMGGFF-----A 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 153 TNHEKNERINRVIQELG-LDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRM 231
Cdd:PRK11614 109 ERDQFQERIKWVYELFPrLHERRIQRAGT-----MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL 183
|
170 180 190
....*....|....*....|....*....|....*
gi 1149890125 232 SKQGRTiIFSIHQPRYSIFKLFDSLTLLASGRLMF 266
Cdd:PRK11614 184 REQGMT-IFLVEQNANQALKLADRGYVLENGHVVL 217
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
69-242 |
3.94e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 55.14 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 69 GIMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP-RPANFK---CNSGYVVQ--DDVVMGTLtvrenLQF 142
Cdd:PRK13648 31 NIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK--SGEIFYNNQAiTDDNFEklrKHIGIVFQnpDNQFVGSI-----VKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 143 SAALRLATTMTNHEK-NERINRVIQELGLDKVADSKVgtqfiRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTA 221
Cdd:PRK13648 104 DVAFGLENHAVPYDEmHRRVSEALKQVDMLERADYEP-----NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180
....*....|....*....|.
gi 1149890125 222 NAVLLLLKRMSKQGRTIIFSI 242
Cdd:PRK13648 179 QNLLDLVRKVKSEHNITIISI 199
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
78-295 |
5.31e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 55.42 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 78 ILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP---------RPANFKcNSGYVVQDDVVMGTLTVRENLQFSAALrl 148
Cdd:PRK10070 59 IMGLSGSGKSTMVRLLNRLIEPT--RGQVLIDGVDiakisdaelREVRRK-KIAMVFQSFALMPHMTVLDNTAFGMEL-- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 149 aTTMTNHEKNERINRVIQELGLDKVADSkvgtqFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL-LL 227
Cdd:PRK10070 134 -AGINAEERREKALDALRQVGLENYAHS-----YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdEL 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149890125 228 LKRMSKQGRTIIFSIHQPRYSIfKLFDSLTLLASGRLMFHGPAQEALgyfesagyhceayNNPADFFL 295
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDLDEAM-RIGDRIAIMQNGEVVQVGTPDEIL-------------NNPANDYV 261
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
62-218 |
5.53e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 55.09 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 62 EILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLING--APRPANFKCNSGYVVQDDVVMGTLTVRE 138
Cdd:PRK10851 16 QVLNDISLDIPSGqMVALLGPSGSGKTTLLRIIAGLEHQT--SGHIRFHGtdVSRLHARDRKVGFVFQHYALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 139 NLQFSAalrlaTTMTNHEKNER--INRVIQELgLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGL 216
Cdd:PRK10851 94 NIAFGL-----TVLPRRERPNAaaIKAKVTQL-LEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
..
gi 1149890125 217 DS 218
Cdd:PRK10851 168 DA 169
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
78-244 |
6.10e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 55.19 E-value: 6.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 78 ILGPTGGGKSSLLdvlaaRkdpsglsgdvLINGAPRPAnfkcnSGYVVQDDVVMGTL----------------------- 134
Cdd:PRK11153 36 VIGASGAGKSTLI-----R----------CINLLERPT-----SGRVLVDGQDLTALsekelrkarrqigmifqhfnlls 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 135 --TVRENLQFsaALRLATTmtnhEKNErINRVIQELgLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEP 212
Cdd:PRK11153 96 srTVFDNVAL--PLELAGT----PKAE-IKARVTEL-LELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEA 167
|
170 180 190
....*....|....*....|....*....|...
gi 1149890125 213 TTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQ 244
Cdd:PRK11153 168 TSALDPATTRSILELLKDINRElGLTIVLITHE 200
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
58-243 |
6.42e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 54.74 E-value: 6.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 58 PVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLS---GDVLINGAPRPANFKC---NSGYVVQ-DDV 129
Cdd:PRK13643 16 PFASRALFDIDLEVKKGsYTALIGHTGSGKSTLLQHLNGLLQPTEGKvtvGDIVVSSTSKQKEIKPvrkKVGVVFQfPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 130 VMGTLTVRENLQFSAAlrlaTTMTNHEKNERIN-RVIQELGLDKVADSKVGTQfirgVSGGERKRTSIGMELITDPSILF 208
Cdd:PRK13643 96 QLFEETVLKDVAFGPQ----NFGIPKEKAEKIAaEKLEMVGLADEFWEKSPFE----LSGGQMRRVAIAGILAMEPEVLV 167
|
170 180 190
....*....|....*....|....*....|....*
gi 1149890125 209 LDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIH 243
Cdd:PRK13643 168 LDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
77-240 |
8.65e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.03 E-value: 8.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGapRPANFKcNSGY-------VVQDDVVmgTLTVRENLQ--FSAALR 147
Cdd:PRK15112 43 AIIGENGSGKSTLAKMLAGMIEPT--SGELLIDD--HPLHFG-DYSYrsqrirmIFQDPST--SLNPRQRISqiLDFPLR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 148 LATTMTNHEKNERINRVIQELGLdkVADSkvGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL-L 226
Cdd:PRK15112 116 LNTDLEPEQREKQIIETLRQVGL--LPDH--ASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLInL 191
|
170
....*....|....
gi 1149890125 227 LLKRMSKQGRTIIF 240
Cdd:PRK15112 192 MLELQEKQGISYIY 205
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
46-224 |
1.48e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.13 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 46 VKLKSGFLPCRKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDV----LAARKDpsglsGDVLINGAprpanfkcn 120
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGsLVAIVGSTGEGKTSLISAmlgeLPPRSD-----ASVVIRGT--------- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 121 SGYVVQDDVVMGTlTVRENLQFSAALrlattmtnheKNERINRVIQELGLDKVADSKVGTQFI----RGV--SGGERKRT 194
Cdd:PLN03130 681 VAYVPQVSWIFNA-TVRDNILFGSPF----------DPERYERAIDVTALQHDLDLLPGGDLTeigeRGVniSGGQKQRV 749
|
170 180 190
....*....|....*....|....*....|
gi 1149890125 195 SIGMELITDPSILFLDEPTTGLDSSTANAV 224
Cdd:PLN03130 750 SMARAVYSNSDVYIFDDPLSALDAHVGRQV 779
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
58-243 |
1.52e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.21 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 58 PVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDvlaarkdpsglsgdvLINGAPRPanfkcNSGYVVQDDVVMGTLTV 136
Cdd:PRK13649 17 PFEGRALFDVNLTIEDGsYTAFIGHTGSGKSTIMQ---------------LLNGLHVP-----TQGSVRVDDTLITSTSK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 137 RENL-----------QFSAALRLATTM------------TNHEKNERINRviQELGLDKVADSkvgtQFIRG---VSGGE 190
Cdd:PRK13649 77 NKDIkqirkkvglvfQFPESQLFEETVlkdvafgpqnfgVSQEEAEALAR--EKLALVGISES----LFEKNpfeLSGGQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1149890125 191 RKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIH 243
Cdd:PRK13649 151 MRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
37-243 |
1.58e-07 |
|
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: 52.50 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 37 LSFHNIC--YRvklksgflpcrkPVEKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP- 112
Cdd:cd03244 3 IEFKNVSlrYR------------PNLPPVLKNISFSIKPGEKvGIVGRTGSGKSSLLLALFRLVELS--SGSILIDGVDi 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 113 ---RPANFKCNSGYVVQDDVVMgTLTVRENL----QFSaalrlattmtnhekNERINRVIQELGLDKVADSKVG---TQF 182
Cdd:cd03244 69 skiGLHDLRSRISIIPQDPVLF-SGTIRSNLdpfgEYS--------------DEELWQALERVGLKEFVESLPGgldTVV 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149890125 183 IRG---VSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKqGRTIIFSIH 243
Cdd:cd03244 134 EEGgenLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFK-DCTVLTIAH 196
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
77-272 |
1.58e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.16 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKS----SLLDVLaarkdPSG---LSGDVLINGAP-RPANFKcnsGYVVQddvvmgtlTVRENLQfsAALRL 148
Cdd:PRK10418 33 ALVGGSGSGKSltcaAALGIL-----PAGvrqTAGRVLLDGKPvAPCALR---GRKIA--------TIMQNPR--SAFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 149 ATTMTNHEK-----------NERINRVIQELGLDKVAdsKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:PRK10418 95 LHTMHTHARetclalgkpadDATLTAALEAVGLENAA--RVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1149890125 218 SSTANAVLLLLKR-MSKQGRTIIFSIHQPRYsIFKLFDSLTLLASGRLMFHGPAQE 272
Cdd:PRK10418 173 VVAQARILDLLESiVQKRALGMLLVTHDMGV-VARLADDVAVMSHGRIVEQGDVET 227
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
70-274 |
1.89e-07 |
|
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: 54.57 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 70 IMKPGLNAILGPTGGGKSSLLDVLAARKDPsgLSGDVLINGAprpanfkcnSGYVVQDDVVMGTlTVRENLQFSAALrla 149
Cdd:TIGR00957 661 IPEGALVAVVGQVGCGKSSLLSALLAEMDK--VEGHVHMKGS---------VAYVPQQAWIQND-SLRENILFGKAL--- 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 150 ttmtnheKNERINRVIQELGLdkVAD---------SKVGTQFIRgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSST 220
Cdd:TIGR00957 726 -------NEKYYQQVLEACAL--LPDleilpsgdrTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHV 795
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1149890125 221 ANAVL--LLLKRMSKQGRTIIFSIHQPRYsiFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:TIGR00957 796 GKHIFehVIGPEGVLKNKTRILVTHGISY--LPQVDVIIVMSGGKISEMGSYQELL 849
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
60-268 |
2.08e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.49 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLING------APRPanfKCNSGYVV--QDDVV 130
Cdd:PRK09580 13 DKAILRGLNLEVRPGeVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGkdllelSPED---RAGEGIFMafQYPVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 131 MGTLTVRENLQFSA-ALRlattmtNHEKNERINRV-IQELGLDKVADSKVGTQFIR-----GVSGGERKRTSIGMELITD 203
Cdd:PRK09580 90 IPGVSNQFFLQTALnAVR------SYRGQEPLDRFdFQDLMEEKIALLKMPEDLLTrsvnvGFSGGEKKRNDILQMAVLE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149890125 204 PSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHG 268
Cdd:PRK09580 164 PELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSG 228
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
428-648 |
2.48e-07 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 51.74 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 428 GVLFFLTTNQCFSSVSAVelFVVEKKL-FIHEYISGYYRVSSYFLGKLLSDLLPMrMLPSIIFTCIVYFMLGLKPKADAF 506
Cdd:COG0842 8 GLLAMSLLFTALMLTALS--IAREREQgTLERLLVTPVSRLEILLGKVLAYLLRG-LLQALLVLLVALLFFGVPLRGLSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 507 FVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQhnef 586
Cdd:COG0842 85 LLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEALR---- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149890125 587 lgqnfcpglnatgnnpcnyatctgeeYLVKQGIDLSPwgLWKNHVALACMIVIFLTIAYLKL 648
Cdd:COG0842 161 --------------------------ALFLGGAGLAD--VWPSLLVLLAFAVVLLALALRLF 194
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
66-245 |
2.68e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 50.82 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 66 NINGIMKPGLNAILGPTGGGKSSLLDvlaarkdpsglsgdvlingaprpanfkcnsgyvvqddvvmgtltvrenlqfsaA 145
Cdd:cd03227 14 NDVTFGEGSLTIITGPNGSGKSTILD-----------------------------------------------------A 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 146 LRLATTMTNHEKNERINRVIQELgldkVADSKVGTQFIR-GVSGGERKRTSIGMEL----ITDPSILFLDEPTTGLDSST 220
Cdd:cd03227 41 IGLALGGAQSATRRRSGVKAGCI----VAAVSAELIFTRlQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRD 116
|
170 180
....*....|....*....|....*
gi 1149890125 221 ANAVLLLLKRMSKQGRTIIFSIHQP 245
Cdd:cd03227 117 GQALAEAILEHLVKGAQVIVITHLP 141
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
77-271 |
3.72e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.19 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRPANFKCN-SGYV-------------VQDDVVMGtltvreNLQF 142
Cdd:PRK15056 37 ALVGVNGSGKSTLFKALMGFVRLA--SGKISILGQPTRQALQKNlVAYVpqseevdwsfpvlVEDVVMMG------RYGH 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 143 SAALRLATTMtnhekneriNRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTAN 222
Cdd:PRK15056 109 MGWLRRAKKR---------DRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1149890125 223 AVLLLLKRMSKQGRTIIFSIHQprYSIFKLFDSLTLLASGRLMFHGPAQ 271
Cdd:PRK15056 180 RIISLLRELRDEGKTMLVSTHN--LGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
64-263 |
3.96e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAA--RKDpsglSGDVLINGapRPANFKcNSGYVVQDDVVMgtltVRENL 140
Cdd:PRK10982 14 LDNVNLKVRPHsIHALMGENGAGKSTLLKCLFGiyQKD----SGSILFQG--KEIDFK-SSKEALENGISM----VHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 141 QFsaaLRLATTMTN--------------HEKNERINRVI-QELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPS 205
Cdd:PRK10982 83 NL---VLQRSVMDNmwlgryptkgmfvdQDKMYRDTKAIfDELDIDIDPRAKVAT-----LSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1149890125 206 ILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGR 263
Cdd:PRK10982 155 IVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKME-EIFQLCDEITILRDGQ 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
78-217 |
3.99e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 78 ILGPTGGGKSSLLDVLAARKDPSG--LSGDVLINGAPRpanfkcnsgYVvQDDVVMgtlTVRENLqFSAALRLATTMTNH 155
Cdd:PRK13409 370 IVGPNGIGKTTFAKLLAGVLKPDEgeVDPELKISYKPQ---------YI-KPDYDG---TVEDLL-RSITDDLGSSYYKS 435
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149890125 156 EknerinrVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:PRK13409 436 E-------IIKPLQLERLLDKNVKD-----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
59-268 |
4.66e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.24 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 59 VEKEILSNIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLingAPRpanfkcNSGYVVQDDVVMGTlTVR 137
Cdd:PTZ00243 671 EPKVLLRDVSvSVPRGKLTVVLGATGSGKSTLLQSLLSQFEIS--EGRVW---AER------SIAYVPQQAWIMNA-TVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 138 ENLQF---SAALRLATTMtnheknerinRVIQ-ELGLDKVA---DSKVGTqfiRGV--SGGERKRTSIGMELITDPSILF 208
Cdd:PTZ00243 739 GNILFfdeEDAARLADAV----------RVSQlEADLAQLGgglETEIGE---KGVnlSGGQKARVSLARAVYANRDVYL 805
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149890125 209 LDEPTTGLDSSTANAVL--LLLKRMSkqGRTIIFSIHQprYSIFKLFDSLTLLASGRLMFHG 268
Cdd:PTZ00243 806 LDDPLSALDAHVGERVVeeCFLGALA--GKTRVLATHQ--VHVVPRADYVVALGDGRVEFSG 863
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
58-274 |
4.85e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 51.53 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 58 PVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPsgLSGDVLING-APRPANFK---CNSGYVVQ--DDVV 130
Cdd:PRK13632 19 NSENNALKNVSFEINEGeYVAILGHNGSGKSTISKILTGLLKP--QSGEIKIDGiTISKENLKeirKKIGIIFQnpDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 131 MGtLTVRENLQFSaalrLATTMTNHEK-NERINRVIQELGLDKVADSKvgTQFIrgvSGGERKRTSIGMELITDPSILFL 209
Cdd:PRK13632 97 IG-ATVEDDIAFG----LENKKVPPKKmKDIIDDLAKKVGMEDYLDKE--PQNL---SGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149890125 210 DEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSI-HQPRYSIfkLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKTRKKTLISItHDMDEAI--LADKVIVFSEGKLIAQGKPKEIL 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
156-234 |
5.13e-07 |
|
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: 52.76 E-value: 5.13e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149890125 156 EKNERINRVIQELGLDKVADSKVGTQFirgvSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ 234
Cdd:COG4172 400 ERRARVAEALEEVGLDPAARHRYPHEF----SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQRE 474
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
60-217 |
7.28e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.88 E-value: 7.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRpanfkcnSGYVVQD---DVVMgTLT 135
Cdd:PRK09544 16 QRRVLSDVSLELKPGkILTLLGPNGAGKSTLVRVVLGLVAPD--EGVIKRNGKLR-------IGYVPQKlylDTTL-PLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 136 VRENLQFSAALRLATTMTnheknerinrviqelGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTG 215
Cdd:PRK09544 86 VNRFLRLRPGTKKEDILP---------------ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
..
gi 1149890125 216 LD 217
Cdd:PRK09544 151 VD 152
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
56-268 |
7.42e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.16 E-value: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 56 RKPVEKEILSNIN-GIMKPGLNAILGPTGGGKSSLLDVlaarkdPSGL----SGDVLINGAPRPANFKC---------NS 121
Cdd:PRK13645 19 KTPFEFKALNNTSlTFKKNKVTCVIGTTGSGKSTMIQL------TNGLiiseTGQTIVGDYAIPANLKKikevkrlrkEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 122 GYVVQ-DDVVMGTLTVRENLQFsaalrlATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRgVSGGERKRTSIGMEL 200
Cdd:PRK13645 93 GLVFQfPEYQLFQETIEKDIAF------GPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFE-LSGGQKRRVALAGII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149890125 201 ITDPSILFLDEPTTGLDSSTANAVLLLLKRMSK-QGRTIIFSIHQPRySIFKLFDSLTLLASGRLMFHG 268
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeYKKRIIMVTHNMD-QVLRIADEVIVMHEGKVISIG 233
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
64-263 |
7.88e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.24 E-value: 7.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKdPSG-LSGDVLINGAPRPANFKCNS---GYVV--QDDVVMGTLTV 136
Cdd:PRK13549 21 LDNVSLKVRAGeIVSLCGENGAGKSTLMKVLSGVY-PHGtYEGEIIFEGEELQASNIRDTeraGIAIihQELALVKELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 137 RENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGL 216
Cdd:PRK13549 100 LENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGN-----LGLGQQQLVEIAKALNKQARLLILDEPTASL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1149890125 217 DSSTANAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASGR 263
Cdd:PRK13549 175 TESETAVLLDIIRDLKAHGIACIYISHKLN-EVKAISDTICVIRDGR 220
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
78-217 |
8.44e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 51.38 E-value: 8.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 78 ILGPTGGGKSSLLDVLAarkdpsGL----SGDVLINGAprpanfkcnsgyVVQD------DVVM--------GTLTVREN 139
Cdd:PRK11650 35 LVGPSGCGKSTLLRMVA------GLeritSGEIWIGGR------------VVNElepadrDIAMvfqnyalyPHMSVREN 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149890125 140 LQFsaALRLATtMTNHEKNERINRVIQELGLDKVADSKVgtqfiRGVSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:PRK11650 97 MAY--GLKIRG-MPKAEIEERVAEAARILELEPLLDRKP-----RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
77-242 |
1.18e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 50.40 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP------------------RPAN-FkcnSGYVVQDDVVMGTltvr 137
Cdd:PRK13635 37 AIVGHNGSGKSTLAKLLNGLLLPE--AGTITVGGMVlseetvwdvrrqvgmvfqNPDNqF---VGATVQDDVAFGL---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 138 ENLQfsaalrlattMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:PRK13635 108 ENIG----------VPREEMVERVDQALRQVGMEDFLNREPHR-----LSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
170 180
....*....|....*....|....*
gi 1149890125 218 SSTANAVLLLLKRMSKQGRTIIFSI 242
Cdd:PRK13635 173 PRGRREVLETVRQLKEQKGITVLSI 197
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
187-272 |
1.23e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 50.88 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 187 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMF 266
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTME 242
|
....*.
gi 1149890125 267 HGPAQE 272
Cdd:PRK09473 243 YGNARD 248
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
60-239 |
1.26e-06 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 49.99 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRPANFKC------NSGYVVQD----- 127
Cdd:COG1126 13 DLEVLKGISLDVEKGeVVVIIGPSGSGKSTLLRCINLLEEPD--SGTITVDGEDLTDSKKDinklrrKVGMVFQQfnlfp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 128 DvvmgtLTVRENLqfSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSIL 207
Cdd:COG1126 91 H-----LTVLENV--TLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQ-----LSGGQQQRVAIARALAMEPKVM 158
|
170 180 190
....*....|....*....|....*....|..
gi 1149890125 208 FLDEPTTGLDSSTANAVLLLLKRMSKQGRTII 239
Cdd:COG1126 159 LFDEPTSALDPELVGEVLDVMRDLAKEGMTMV 190
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
78-272 |
1.43e-06 |
|
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: 51.36 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 78 ILGPTGGGKSSLLDVLAARKdPSGLSGDVLINGapRPANFKcNSGYVVQDDVVM-----------GTLTVRENLQFSAAL 146
Cdd:TIGR02633 291 VAGLVGAGRTELVQALFGAY-PGKFEGNVFING--KPVDIR-NPAQAIRAGIAMvpedrkrhgivPILGVGKNITLSVLK 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 147 RLATTMTNHEKNER--INRVIQELGLdkvadsKVGTQF--IRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTAN 222
Cdd:TIGR02633 367 SFCFKMRIDAAAELqiIGSAIQRLKV------KTASPFlpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKY 440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1149890125 223 AVLLLLKRMSKQGRTIIFsIHQPRYSIFKLFDSLTLLASGRL----MFHGPAQE 272
Cdd:TIGR02633 441 EIYKLINQLAQEGVAIIV-VSSELAEVLGLSDRVLVIGEGKLkgdfVNHALTQE 493
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
63-289 |
1.48e-06 |
|
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: 51.83 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 63 ILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGaprpanfkcNSGYVVQDDVVMGTlTVRENLQ 141
Cdd:TIGR01271 441 VLKNISFKLEKGqLLAVAGSTGSGKSSLLMMIMGELEPS--EGKIKHSG---------RISFSPQTSWIMPG-TIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 142 FSAA---LRLATTMTNHEKNERINRVIQElglDKVADSKVGTQfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDS 218
Cdd:TIGR01271 509 FGLSydeYRYTSVIKACQLEEDIALFPEK---DKTVLGEGGIT----LSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149890125 219 STANAVL--LLLKRMSKQGRTIIFSihqpRYSIFKLFDSLTLLASGRLMFHGPAQEALGY---FESAGYHCEAYNN 289
Cdd:TIGR01271 582 VTEKEIFesCLCKLMSNKTRILVTS----KLEHLKKADKILLLHEGVCYFYGTFSELQAKrpdFSSLLLGLEAFDN 653
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
132-243 |
1.55e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.66 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 132 GTLTVRENLQFSAAL-RLATTmtnhEKNERINRVIQELGLDKVADSKVGtqfirGVSGGERKRTSIGMELITDPSILFLD 210
Cdd:NF033858 352 GELTVRQNLELHARLfHLPAA----EIAARVAEMLERFDLADVADALPD-----SLPLGIRQRLSLAVAVIHKPELLILD 422
|
90 100 110
....*....|....*....|....*....|....
gi 1149890125 211 EPTTGLDSSTANAVLLLLKRMS-KQGRTIIFSIH 243
Cdd:NF033858 423 EPTSGVDPVARDMFWRLLIELSrEDGVTIFISTH 456
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
80-264 |
3.24e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.17 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 80 GPTGGGKSSLLDVLAArKDPSgLSGDVLINGA---PRPA--NFKCNSGYVVQ---DDVVMGTLTVRENLQFSAALRL--- 148
Cdd:PRK09700 296 GLVGSGRTELMNCLFG-VDKR-AGGEIRLNGKdisPRSPldAVKKGMAYITEsrrDNGFFPNFSIAQNMAISRSLKDggy 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 149 --ATTMTNHEKNERINRVIQELGLDKVADSKvgtQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLL 226
Cdd:PRK09700 374 kgAMGLFHEVDEQRTAENQRELLALKCHSVN---QNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYK 450
|
170 180 190
....*....|....*....|....*....|....*....
gi 1149890125 227 LLKRMSKQGRTIIF-SIHQPRysIFKLFDSLTLLASGRL 264
Cdd:PRK09700 451 VMRQLADDGKVILMvSSELPE--IITVCDRIAVFCEGRL 487
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
160-243 |
3.58e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 160 RINRVIQELGLDkvADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKrmSKQGrTII 239
Cdd:PRK11147 138 RINEVLAQLGLD--PDAALSS-----LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK--TFQG-SII 207
|
....
gi 1149890125 240 FSIH 243
Cdd:PRK11147 208 FISH 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
187-240 |
4.34e-06 |
|
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: 49.68 E-value: 4.34e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1149890125 187 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIF 240
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLL 212
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
60-274 |
4.48e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 49.72 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGapRP------ANFKCNSGYVVQDDVVMG 132
Cdd:PRK10790 353 DNLVLQNINlSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT--EGEIRLDG--RPlsslshSVLRQGVAMVQQDPVVLA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 133 TlTVRENLqfsaalrlatTMTNHEKNERINRVIQELGLDKVA-------DSKVGTQFiRGVSGGERKRTSIGMELITDPS 205
Cdd:PRK10790 429 D-TFLANV----------TLGRDISEEQVWQALETVQLAELArslpdglYTPLGEQG-NNLSVGQKQLLALARVLVQTPQ 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149890125 206 ILFLDEPTTGLDSSTANAVLLLLkRMSKQGRTIIFSIHqpRYSIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQAL-AAVREHTTLVVIAH--RLSTIVEADTILVLHRGQAVEQGTHQQLL 562
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
60-242 |
4.66e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 48.64 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPG-LNAILGPTGGGKSS---LLD-VLAARKDP-SGLSGDVLINGAPRPANFKCNSGYVVQ--DDVVM 131
Cdd:PRK13640 19 KKPALNDISFSIPRGsWTALIGHNGSGKSTiskLINgLLLPDDNPnSKITVDGITLTAKTVWDIREKVGIVFQnpDNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 132 GTlTVRENLQFSaalrLATTMTNHEKNERI-NRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLD 210
Cdd:PRK13640 99 GA-TVGDDVAFG----LENRAVPRPEMIKIvRDVLADVGMLDYIDSEPAN-----LSGGQKQRVAIAGILAVEPKIIILD 168
|
170 180 190
....*....|....*....|....*....|..
gi 1149890125 211 EPTTGLDSSTANAVLLLLKRMSKQGRTIIFSI 242
Cdd:PRK13640 169 ESTSMLDPAGKEQILKLIRKLKKKNNLTVISI 200
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
77-217 |
4.76e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 48.45 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSGlsGDVLINGAP---RPANFKCNSGYV--VQDDVVMGTLTVRENLQFSAALRLATT 151
Cdd:PRK11300 35 SLIGPNGAGKTTVFNCLTGFYKPTG--GTILLRGQHiegLPGHQIARMGVVrtFQHVRLFREMTVIENLLVAQHQQLKTG 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149890125 152 M------------TNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:PRK11300 113 LfsgllktpafrrAESEALDRAATWLERVGLLEHANRQAGN-----LAYGQQRRLEIARCMVTQPEILMLDEPAAGLN 185
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
64-244 |
6.32e-06 |
|
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: 49.05 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 64 LSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNS---GYVV--QDDVVMGTLTVR 137
Cdd:TIGR02633 17 LDGIDLEVRPGeCVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNIRDTeraGIVIihQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 138 ENLQFSAALRLATTMTNH-EKNERINRVIQELGLDKVADSKVGTQFirgvSGGERKRTSIGMELITDPSILFLDEPTTGL 216
Cdd:TIGR02633 97 ENIFLGNEITLPGGRMAYnAMYLRAKNLLRELQLDADNVTRPVGDY----GGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180
....*....|....*....|....*...
gi 1149890125 217 DSSTANAVLLLLKRMSKQGRTIIFSIHQ 244
Cdd:TIGR02633 173 TEKETEILLDIIRDLKAHGVACVYISHK 200
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
181-240 |
6.90e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.89 E-value: 6.90e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 181 QFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIF 240
Cdd:PRK15439 399 QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLF 458
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
59-245 |
9.41e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 47.26 E-value: 9.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 59 VEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVL--AARKDPSGLSGDVLINgaprpanfKCNSGYVVQDDVVMgtlt 135
Cdd:COG2401 41 VERYVLRDLNLEIEPGeIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDN--------QFGREASLIDAIGR---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 136 vreNLQFSAALrlattmtnheknERINRViqelGL-DKVAdskvgtqFIRGV---SGGERKRTSIGMELITDPSILFLDE 211
Cdd:COG2401 109 ---KGDFKDAV------------ELLNAV----GLsDAVL-------WLRRFkelSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190
....*....|....*....|....*....|....*
gi 1149890125 212 PTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQP 245
Cdd:COG2401 163 FCSHLDRQTAKRVARNLQKLARRaGITLVVATHHY 197
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
63-254 |
1.03e-05 |
|
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: 45.99 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 63 ILSNINGIMKPGLNA-ILGPTGGGKSSLLDVLAarkdpsGL----SGDVlinGAPRPAN--FKCNSGYVVQddvvmGTLt 135
Cdd:cd03223 16 LLKDLSFEIKPGDRLlITGPSGTGKSSLFRALA------GLwpwgSGRI---GMPEGEDllFLPQRPYLPL-----GTL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 136 vREnlqfsaALRLAttmtnheknerinrviqelgLDKVadskvgtqfirgVSGGERKRTSIGMELITDPSILFLDEPTTG 215
Cdd:cd03223 81 -RE------QLIYP--------------------WDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1149890125 216 LDSSTANAVLLLLKRMSkqgrTIIFSI-HQPrySIFKLFD 254
Cdd:cd03223 122 LDEESEDRLYQLLKELG----ITVISVgHRP--SLWKFHD 155
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
78-275 |
2.30e-05 |
|
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: 47.49 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 78 ILGPTGGGKSSLLDVLAARKDPSG-----LSGDVLIN-GAPRPAN---FKCNSGYVVQDDVVMGTLTVRENLQFSAALRL 148
Cdd:TIGR03269 315 IVGTSGAGKTTLSKIIAGVLEPTSgevnvRVGDEWVDmTKPGPDGrgrAKRYIGILHQEYDLYPHRTVLDNLTEAIGLEL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 149 ATTMTNHekneRINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL-LL 227
Cdd:TIGR03269 395 PDELARM----KAVITLKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVThSI 470
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1149890125 228 LKRMSKQGRTIIFSIHQPRYsIFKLFDSLTLLASGRLMFHGPAQEALG 275
Cdd:TIGR03269 471 LKAREEMEQTFIIVSHDMDF-VLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
78-243 |
2.37e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 46.21 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 78 ILGPTGGGKSSLLDVLAARKDP------SGLSGDVLINgaprpaNFKcnsGYVVQD---DVVMGTLTVRENLQFSAALRL 148
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPnlgkfdDPPDWDEILD------EFR---GSELQNyftKLLEGDVKVIVKPQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 149 ATT------MTNHEKNERINRVIQELGLDKVADSKvgtqfIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTAN 222
Cdd:cd03236 102 AVKgkvgelLKKKDERGKLDELVDQLELRHVLDRN-----IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180
....*....|....*....|.
gi 1149890125 223 AVLLLLKRMSKQGRTIIFSIH 243
Cdd:cd03236 177 NAARLIRELAEDDNYVLVVEH 197
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
56-220 |
2.39e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 56 RKPVEkeILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP--RPANFK---CNSGYVVQDDV 129
Cdd:PTZ00265 395 RKDVE--IYKDLNFTLTEGKTyAFVGESGCGKSTILKLIERLYDPT--EGDIIINDSHnlKDINLKwwrSKIGVVSQDPL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 130 VMGTlTVRENLQFSA-ALRLATTMTNH----------EKNER----------INRVIQELGLDKVADSKVGTQFIRG--- 185
Cdd:PTZ00265 471 LFSN-SIKNNIKYSLySLKDLEALSNYynedgndsqeNKNKRnscrakcagdLNDMSNTTDSNELIEMRKNYQTIKDsev 549
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149890125 186 ------------------------------VSGGERKRTSIGMELITDPSILFLDEPTTGLDSST 220
Cdd:PTZ00265 550 vdvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
45-245 |
2.45e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 45.72 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 45 RVKLKsGFLPCRKPVEkeilSNINGIMKPGLNAILGPTGGGKSSLLDVLAArkdpsGLSGDVlingaPRPANfkcnsgyV 124
Cdd:cd03279 5 KLELK-NFGPFREEQV----IDFTGLDNNGLFLICGPTGAGKSTILDAITY-----ALYGKT-----PRYGR-------Q 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 125 VQDDVVMGT--LTVRENLQFSAalrlattmtnhekNERINRVIQELGLDKvadskvgTQFIRGV---------------- 186
Cdd:cd03279 63 ENLRSVFAPgeDTAEVSFTFQL-------------GGKKYRVERSRGLDY-------DQFTRIVllpqgefdrflarpvs 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149890125 187 --SGGERKRTSIGMELITDPSI----------LFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQP 245
Cdd:cd03279 123 tlSGGETFLASLSLALALSEVLqnrggarleaLFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVE 193
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
124-285 |
2.56e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 124 VVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELglDKVADSKVGTqFIRGVSGGERKRTSIGMELITD 203
Cdd:PTZ00265 1300 IVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESL--PNKYDTNVGP-YGKSLSGGQKQRIAIARALLRE 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 204 PSILFLDEPTTGLDSstaNAVLLLLKRM----SKQGRTIIFSIHqpRYSIFKLFDSLtllasgrLMFHGPAQEAlGYFES 279
Cdd:PTZ00265 1377 PKILLLDEATSSLDS---NSEKLIEKTIvdikDKADKTIITIAH--RIASIKRSDKI-------VVFNNPDRTG-SFVQA 1443
|
....*.
gi 1149890125 280 AGYHCE 285
Cdd:PTZ00265 1444 HGTHEE 1449
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
60-217 |
2.67e-05 |
|
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: 44.36 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPRPanfkcnsGYVVQddvvmgtltvre 138
Cdd:cd03221 12 GKLLLKDISLTINPGDRiGLVGRNGAGKSTLLKLIAGELEPD--EGIVTWGSTVKI-------GYFEQ------------ 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149890125 139 nlqfsaalrlattmtnheknerinrviqelgldkvadskvgtqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:cd03221 71 -----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
73-246 |
3.18e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 45.29 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 73 PGLNAILGPTGGGKSSLLDVLAArkdpsGLSGDvlinGAPRpanfkCNSGYVVQDDVVMGTLTVRENLQFSaaLRLATTM 152
Cdd:cd03240 22 SPLTLIVGQNGAGKTTIIEALKY-----ALTGE----LPPN-----SKGGAHDPKLIREGEVRAQVKLAFE--NANGKKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 153 TNHEKNERINRVI---QElGLDKVADSKVGTqfirgVSGGERK------RTSIGMELITDPSILFLDEPTTGLDSSTANA 223
Cdd:cd03240 86 TITRSLAILENVIfchQG-ESNWPLLDMRGR-----CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEE 159
|
170 180
....*....|....*....|....*
gi 1149890125 224 VLL-LLKRMSKQG-RTIIFSIHQPR 246
Cdd:cd03240 160 SLAeIIEERKSQKnFQLIVITHDEE 184
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
67-240 |
3.72e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.83 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 67 INGIMKPGLNA----------ILG---PTGGGKSSLLDVL--AARKDpsglSGDVLINGAPRPANfkcNSGYVVQDDVVM 131
Cdd:PRK11288 260 LDGLKGPGLREpisfsvrageIVGlfgLVGAGRSELMKLLygATRRT----AGQVYLDGKPIDIR---SPRDAIRAGIML 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 132 -----------GTLTVRENLQFSA---ALRLATTMTNHEKNERINRVIQELgldkvadsKVGT----QFIRGVSGGERKR 193
Cdd:PRK11288 333 cpedrkaegiiPVHSVADNINISArrhHLRAGCLINNRWEAENADRFIRSL--------NIKTpsreQLIMNLSGGNQQK 404
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1149890125 194 TSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIF 240
Cdd:PRK11288 405 AILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLF 451
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
187-246 |
6.55e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.85 E-value: 6.55e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149890125 187 SGGERKRTSIGMELI--TDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPR 246
Cdd:cd03238 89 SGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLD 150
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
62-239 |
6.67e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 62 EILSnINGIMkpglnailgptGGGKSSLLDVL--AARKDpsglSGDVLING---APRPANFKCNSGYVV------QDDVV 130
Cdd:PRK10762 279 EILG-VSGLM-----------GAGRTELMKVLygALPRT----SGYVTLDGhevVTRSPQDGLANGIVYisedrkRDGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 131 MGtLTVRENLQFSAALRLATTM--TNH-EKNERINRVIQELgldkvadsKVGT----QFIRGVSGGERKRTSIGMELITD 203
Cdd:PRK10762 343 LG-MSVKENMSLTALRYFSRAGgsLKHaDEQQAVSDFIRLF--------NIKTpsmeQAIGLLSGGNQQKVAIARGLMTR 413
|
170 180 190
....*....|....*....|....*....|....*.
gi 1149890125 204 PSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTII 239
Cdd:PRK10762 414 PKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSII 449
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
186-243 |
7.05e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.00 E-value: 7.05e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1149890125 186 VSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIH 243
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITH 227
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
183-239 |
7.86e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 7.86e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1149890125 183 IRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTII 239
Cdd:PRK10982 389 IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGII 445
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
77-228 |
9.48e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 44.96 E-value: 9.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAprpaNFKCNSGYVVQD---DVVM------GTLTVRENL--QFSAA 145
Cdd:PRK11308 45 AVVGESGCGKSTLARLLTMIETPT--GGELYYQGQ----DLLKADPEAQKLlrqKIQIvfqnpyGSLNPRKKVgqILEEP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 146 LRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFirgvSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVL 225
Cdd:PRK11308 119 LLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMF----SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVL 194
|
...
gi 1149890125 226 LLL 228
Cdd:PRK11308 195 NLM 197
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
70-292 |
1.44e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 43.87 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 70 IMKPGLNAILGPTGGGKSSLLDVLAARKDpsgLSGDVLINGA--------------------------PRPANFKCNsgy 123
Cdd:PRK14258 30 IYQSKVTAIIGPSGCGKSTFLKCLNRMNE---LESEVRVEGRveffnqniyerrvnlnrlrrqvsmvhPKPNLFPMS--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 124 vVQDDVVMGTLTV--RENLQFSAALRLAttMTNHEKNERINRVIQELGLDkvadskvgtqfirgVSGGERKRTSIGMELI 201
Cdd:PRK14258 104 -VYDNVAYGVKIVgwRPKLEIDDIVESA--LKDADLWDEIKHKIHKSALD--------------LSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 202 TDPSILFLDEPTTGLDSSTANAVLLLLK--RMSKQGRTIIFSIHQPRYSIFKLFDSLtllasgrlmFHGpAQEALGYFES 279
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSDFTAF---------FKG-NENRIGQLVE 236
|
250
....*....|...
gi 1149890125 280 AGYHCEAYNNPAD 292
Cdd:PRK14258 237 FGLTKKIFNSPHD 249
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
60-274 |
1.56e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 44.62 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP----RPANFKCNSGYVVQ-----DDV 129
Cdd:PRK11176 355 EVPALRNINFKIPAGKTvALVGRSGSGKSTIANLLTRFYDID--EGEILLDGHDlrdyTLASLRNQVALVSQnvhlfNDT 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 130 VMGTLTVRENLQFS-----AALRLATTMtnheknERINRViqELGLDKVadskVGTQfirGV--SGGERKRTSIGMELIT 202
Cdd:PRK11176 433 IANNIAYARTEQYSreqieEAARMAYAM------DFINKM--DNGLDTV----IGEN---GVllSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149890125 203 DPSILFLDEPTTGLDSSTANAVLLLLKRMSKQgRTIIFSIHqpRYSIFKLFDSLTLLASGRLMFHGPAQEAL 274
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAH--RLSTIEKADEILVVEDGEIVERGTHAELL 566
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
158-239 |
1.63e-04 |
|
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: 44.78 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 158 NER--INRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQG 235
Cdd:COG1245 188 DERgkLDELAEKLGLENILDRDISE-----LSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEG 262
|
....
gi 1149890125 236 RTII 239
Cdd:COG1245 263 KYVL 266
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
178-239 |
2.04e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.62 E-value: 2.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149890125 178 VGTQFIR------GVSGGERKRTSIGMEL---ITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTII 239
Cdd:TIGR00630 816 VGLGYIRlgqpatTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVV 886
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
103-240 |
2.25e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.15 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 103 SGDVLINGAP----RPAN-FKCNSGYVVQD---DVVMGTLTVRENLQFSAALRLAT-TMTNHEKNER-INRVIQELgldk 172
Cdd:PRK13549 317 EGEIFIDGKPvkirNPQQaIAQGIAMVPEDrkrDGIVPVMGVGKNITLAALDRFTGgSRIDDAAELKtILESIQRL---- 392
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149890125 173 vadsKVGT----QFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIF 240
Cdd:PRK13549 393 ----KVKTaspeLAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIV 460
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
77-240 |
2.27e-04 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 43.95 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAP---------RPanFKCNSGYVVQDDvvMGTL----TVRENLqfS 143
Cdd:COG4608 48 GLVGESGCGKSTLGRLLLRLEEPT--SGEILFDGQDitglsgrelRP--LRRRMQMVFQDP--YASLnprmTVGDII--A 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 144 AALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFirgvSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANA 223
Cdd:COG4608 120 EPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEF----SGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQ 195
|
170
....*....|....*...
gi 1149890125 224 VLLLLKRMSKQ-GRTIIF 240
Cdd:COG4608 196 VLNLLEDLQDElGLTYLF 213
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
134-244 |
2.46e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 43.37 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 134 LTVRENLQFsaalrlattMTNHEKNERINRVIQELGLDKVadsKVGtQFIRGVSGGERKRTSIGMELI---TDPSILFLD 210
Cdd:cd03271 131 MTVEEALEF---------FENIPKIARKLQTLCDVGLGYI---KLG-QPATTLSGGEAQRIKLAKELSkrsTGKTLYILD 197
|
90 100 110
....*....|....*....|....*....|....
gi 1149890125 211 EPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQ 244
Cdd:cd03271 198 EPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN 231
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
60-244 |
3.04e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 42.24 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEILSNIN-GIMKPGLNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGA---PRPANFKCNSGYVVQDDVVMGTLT 135
Cdd:PRK13540 13 DQPLLQQISfHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPE--KGEILFERQsikKDLCTYQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 136 VRENLQFSaalrLATTMTNHEknerINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTG 215
Cdd:PRK13540 91 LRENCLYD----IHFSPGAVG----ITELCRLFSLEHLIDYPCGL-----LSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
170 180
....*....|....*....|....*....
gi 1149890125 216 LDSSTANAVLLLLKRMSKQGRTIIFSIHQ 244
Cdd:PRK13540 158 LDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
181-242 |
3.82e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.79 E-value: 3.82e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149890125 181 QFIRgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSI 242
Cdd:cd03222 68 QYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVV 128
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
158-217 |
3.84e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.64 E-value: 3.84e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149890125 158 NER--INRVIQELGLDKVADSKvgtqfIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:PRK13409 188 DERgkLDEVVERLGLENILDRD-----ISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
187-290 |
4.72e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 42.77 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 187 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIHQprYSIFKLFDSLTLlasgrLM 265
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHD--LAVVKHISDRVL-----VM 235
|
90 100
....*....|....*....|....*
gi 1149890125 266 FHGPAQEaLGYFEsagyhcEAYNNP 290
Cdd:PRK15079 236 YLGHAVE-LGTYD------EVYHNP 253
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
186-243 |
5.13e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 5.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149890125 186 VSGGERKRTSIGMELIT---DPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIH 243
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
286-646 |
6.52e-04 |
|
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: 42.38 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 286 AYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQ---DKPLIEKLAEIYVNSSFYKETKAELHQLSGgeKKKKIT 362
Cdd:pfam12698 25 AVNDPEELPVAVVDEDNSSLSRQLVRALEASPTVNLVQYvdsEEEAKEALKNGKIDGLLVIPKGFSKDLLKG--ESATVT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 363 VFKEISYTTS---FCHQLRWVSKRSFKNLLGNPQASIAQIIVtvvlglvIGAIYFGLKNDSTGIQNraGVLFFLTTNQCF 439
Cdd:pfam12698 103 VYINSSNLLVsklILNALQSLLQQLNASALVLLLEALSTSAP-------IPVESTPLFNPQSGYAY--YLVGLILMIIIL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 440 SSVSAVELFVVEKKL--FIHEYISGYYRVSSYFLGKLLSDLLpmRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVA 517
Cdd:pfam12698 174 IGAAIIAVSIVEEKEsrIKERLLVSGVSPLQYWLGKILGDFL--VGLLQLLIILLLLFGIGIPFGNLGLLLLLFLLYGLA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 518 YSASSMALAIAAGQSvvSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFsIPrygftalqhneflgqNFCPGlna 597
Cdd:pfam12698 252 YIALGYLLGSLFKNS--EDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSI-IP---------------FFSPI--- 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1149890125 598 tgnnpcnyatctgeEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYL 646
Cdd:pfam12698 311 --------------DGLLRLIYGDSLWEIAPSLIILLLFAVVLLLLALL 345
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
80-217 |
7.82e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 41.37 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 80 GPTGGGKSSLLDVLAARKDPSglSGDVLINGAP-RPANFKCNSGYVVQDDVVMGTLTVRENLQFSAAL--RLATTMTNHe 156
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVE--SGQIQIDGKTaTRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLhgRRAKQMPGS- 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149890125 157 knerinrVIQELGLDKVADSkvgtqFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLD 217
Cdd:PRK13543 121 -------ALAIVGLAGYEDT-----LVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
61-244 |
7.84e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 42.98 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 61 KEILSNINGIMKPGLN-AILGPTGGGKSSLLDVLAARkdpSGLSGDVLINGAPRPA----NFKCNSGyVVQDDVVMGTLT 135
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRvGLLGRTGSGKSTLLSALLRL---LSTEGEIQIDGVSWNSvtlqTWRKAFG-VIPQKVFIFSGT 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 136 VRENLQfsaalrlattmtNHEK--NERINRVIQELGLDKVADS---KVGTQFIRG---VSGGERKRTSIGMELITDPSIL 207
Cdd:TIGR01271 1308 FRKNLD------------PYEQwsDEEIWKVAEEVGLKSVIEQfpdKLDFVLVDGgyvLSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1149890125 208 FLDEPTTGLDSSTanavLLLLKRMSKQGR---TIIFSIHQ 244
Cdd:TIGR01271 1376 LLDEPSAHLDPVT----LQIIRKTLKQSFsncTVILSEHR 1411
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
47-243 |
8.56e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.57 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 47 KLKSGFLPCRKPVEKEILSNINGIMKPG-LNAILGPTGGGKSSLLDVLAARKDPSglSGDVLINGAPrpANFKCNSGyvv 125
Cdd:PRK13545 23 KLKDLFFRSKDGEYHYALNNISFEVPEGeIVGIIGLNGSGKSTLSNLIAGVTMPN--KGTVDIKGSA--ALIAISSG--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 126 qddvVMGTLTVRENLQFSAalrLATTMTNHEKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPS 205
Cdd:PRK13545 96 ----LNGQLTGIENIELKG---LMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKT-----YSSGMKSRLGFAISVHINPD 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 1149890125 206 ILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIH 243
Cdd:PRK13545 164 ILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISH 201
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
77-262 |
1.09e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.91 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAA--RKDpsglSGDVLINGapRPANFK-------CNSGYVVQDDVVMGTLTVRENLqFsaalr 147
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGiyTRD----AGSILYLG--KEVTFNgpkssqeAGIGIIHQELNLIPQLTIAENI-F----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 148 LATTMTNH-------EKNERINRVIQELGLDKVADSKVGTqfirgVSGGERKRTSIGMELITDPSILFLDEPTTGL-DSS 219
Cdd:PRK10762 102 LGREFVNRfgridwkKMYAEADKLLARLNLRFSSDKLVGE-----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1149890125 220 TAnAVLLLLKRMSKQGRTIIFSIHQPRySIFKLFDSLTLLASG 262
Cdd:PRK10762 177 TE-SLFRVIRELKSQGRGIVYISHRLK-EIFEICDDVTVFRDG 217
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
70-273 |
1.11e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 41.31 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 70 IMKPGLNAILGPTGGGKSSLLDVLAARKD--PSG-LSGDVLING----APR--PANFKCNSGYVVQDDVVMGTlTVRENL 140
Cdd:PRK14243 33 IPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrVEGKVTFHGknlyAPDvdPVEVRRRIGMVFQKPNPFPK-SIYDNI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 141 QFSAALrlattmtNHEK---NERINRVIQELGL-----DKVADSKVGtqfirgVSGGERKRTSIGMELITDPSILFLDEP 212
Cdd:PRK14243 112 AYGARI-------NGYKgdmDELVERSLRQAALwdevkDKLKQSGLS------LSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149890125 213 TTGLDSSTANAVLLLLKRMSKQgRTIIFSIHQ----PRYSIFKLFDSLTLLASG------------RLMFHGPAQEA 273
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQ-YTIIIVTHNmqqaARVSDMTAFFNVELTEGGgrygylvefdrtEKIFNSPQQQA 254
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
77-239 |
1.19e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 77 AILGPTGGGKSSLLDVLAARKDPsgLSGDvLINGAPRPAN-------------FKCNSGYVVQDDVVMGTLTVRENLQfs 143
Cdd:PRK10938 33 AFVGANGSGKSALARALAGELPL--LSGE-RQSQFSHITRlsfeqlqklvsdeWQRNNTDMLSPGEDDTGRTTAEIIQ-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 144 aalrlattmTNHEKNERINRVIQELGLDKVADSKvgtqFIRgVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANA 223
Cdd:PRK10938 108 ---------DEVKDPARCEQLAQQFGITALLDRR----FKY-LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
170
....*....|....*.
gi 1149890125 224 VLLLLKRMSKQGRTII 239
Cdd:PRK10938 174 LAELLASLHQSGITLV 189
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
189-274 |
2.08e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.94 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 189 GERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHG 268
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETA 241
|
....*.
gi 1149890125 269 PAQEAL 274
Cdd:PRK15093 242 PSKELV 247
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
60-242 |
2.63e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 40.08 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 60 EKEI-LSNING----IMKPGLNAILGPTGGGKSS---LLDVLAARkdpsgLSGDVLINGAPRPA----NFKCNSGYVVQ- 126
Cdd:PRK13642 15 EKESdVNQLNGvsfsITKGEWVSIIGQNGSGKSTtarLIDGLFEE-----FEGKVKIDGELLTAenvwNLRRKIGMVFQn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 127 -DDVVMGTlTVRENLQFSaalrlattMTNH--EKNERINRVIQELGLDKVADSKvgTQFIRGVSGGERKRTSIGMELITD 203
Cdd:PRK13642 90 pDNQFVGA-TVEDDVAFG--------MENQgiPREEMIKRVDEALLAVNMLDFK--TREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1149890125 204 PSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSI 242
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSI 197
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
186-274 |
2.74e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 186 VSGGERKRTSI----GMELITDPSILflDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQ--------------PRY 247
Cdd:PRK00635 477 LSGGEQERTALakhlGAELIGITYIL--DEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDeqmisladriidigPGA 554
|
90 100
....*....|....*....|....*..
gi 1149890125 248 SIFklfdsltllaSGRLMFHGPAQEAL 274
Cdd:PRK00635 555 GIF----------GGEVLFNGSPREFL 571
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
34-222 |
3.00e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. 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: 213255 [Multi-domain] Cd Length: 257 Bit Score: 39.89 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 34 GAVLSFHNICYRvklksgFLPCRKPVekeiLSNINGIMKPGLN-AILGPTGGGKSSLldVLAARKDPSGLSGDVLING-- 110
Cdd:cd03288 17 GGEIKIHDLCVR------YENNLKPV----LKHVKAYIKPGQKvGICGRTGSGKSSL--SLAFFRMVDIFDGKIVIDGid 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 111 -APRPANFKCNSGYVVQDDVVMGTLTVRENLQfsaALRLATTMTNHEKNE--RINRVIQEL--GLDKVAdSKVGTQFirg 185
Cdd:cd03288 85 iSKLPLHTLRSRLSIILQDPILFSGSIRFNLD---PECKCTDDRLWEALEiaQLKNMVKSLpgGLDAVV-TEGGENF--- 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 1149890125 186 vSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTAN 222
Cdd:cd03288 158 -SVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN 193
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
144-245 |
3.17e-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: 40.07 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 144 AALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITD---PSILFLDEPTTGLDSST 220
Cdd:pfam13304 195 ADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLAALLSAlpkGGLLLIDEPESGLHPKL 274
|
90 100
....*....|....*....|....*
gi 1149890125 221 ANAVLLLLKRMSKQGRTIIFSIHQP 245
Cdd:pfam13304 275 LRRLLELLKELSRNGAQLILTTHSP 299
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
186-243 |
4.34e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 39.72 E-value: 4.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1149890125 186 VSGGERKRTSIGMELITDPSILFLDEPTTGLDSS-TANAVLLLLKRMSKQGRTIIFSIH 243
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTiQAQIIELLLELQQKENMALVLITH 212
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
187-243 |
4.39e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 4.39e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1149890125 187 SGGERKRTSIGMELITDPSILFLDEPTTGLDsstANAVLLLLKRMSKQGRTIIFSIH 243
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSH 399
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
187-245 |
5.16e-03 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 38.78 E-value: 5.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149890125 187 SGGERKR----TSIGMELItdpSILF-LDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQP 245
Cdd:cd03270 139 SGGEAQRirlaTQIGSGLT---GVLYvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDE 199
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
187-243 |
5.89e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 39.30 E-value: 5.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1149890125 187 SGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQ-GRTIIFSIH 243
Cdd:PRK13633 146 SGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITH 203
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
83-273 |
5.95e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 39.62 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 83 GGGKSSLLDVLaarkdpSGL----SGDVLINGAP----RPANF-KCNSGYVVQD---DVVMGTLTVRENLqfsaalrlat 150
Cdd:COG3845 294 GNGQSELAEAL------AGLrppaSGSIRLDGEDitglSPRERrRLGVAYIPEDrlgRGLVPDMSVAENL---------- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 151 TMTNHEKNE-----RINR-VIQELGLDKVADSKVGT----QFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSST 220
Cdd:COG3845 358 ILGRYRRPPfsrggFLDRkAIRAFAEELIEEFDVRTpgpdTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGA 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1149890125 221 ANAVLLLLKRMSKQGRTIIFSihqpryS-----IFKLFDSLTLLASGRLMFHGPAQEA 273
Cdd:COG3845 438 IEFIHQRLLELRDAGAAVLLI------SedldeILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
36-243 |
8.77e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 39.07 E-value: 8.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 36 VLSFHNICYRVKLKSGFLPcRKPVEKEILSNINGIMKPGLN-AILGPTGGGKS----SLLDVLAARKDPSGLSG---DVL 107
Cdd:PRK10261 313 ILQVRNLVTRFPLRSGLLN-RVTREVHAVEKVSFDLWPGETlSLVGESGSGKSttgrALLRLVESQGGEIIFNGqriDTL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149890125 108 INGAPRPanFKCNSGYVVQDDvvMGTLTVRENLQFS--AALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFirg 185
Cdd:PRK10261 392 SPGKLQA--LRRDIQFIFQDP--YASLDPRQTVGDSimEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEF--- 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1149890125 186 vSGGERKRTSIGMELITDPSILFLDEPTTGLDSST-ANAVLLLLKRMSKQGRTIIFSIH 243
Cdd:PRK10261 465 -SGGQRQRICIARALALNPKVIIADEAVSALDVSIrGQIINLLLDLQRDFGIAYLFISH 522
|
|
| |
