|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
70-726 |
0e+00 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 599.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 70 FQNLSYSVKVRRRGSSLPENLTAEENggrVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKE-KLKGTVTL 148
Cdd:TIGR00955 11 FGRVAQDGSWKQLVSRLRGCFCRERP---RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvKGSGSVLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 149 NDEVLESALLKVISAYVMQDDLLFPMLTVEETLMFAAEFRLPRSLSKSKKKARVQALIDQLGLTTAANTVIGDEG-HRGV 227
Cdd:TIGR00955 88 NGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGrVKGL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 228 SGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYRILSLLDRLIFLSRGQTVY 307
Cdd:TIGR00955 168 SGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 308 SGSPAELSEFLADFGHPIPENENRTEFALDLVRDLEETAGGTRSMVEhnKSWQWKNKNHLKGHKIVRRNSSHRfhlclkd 387
Cdd:TIGR00955 248 LGSPDQAVPFFSDLGHPCPENYNPADFYVQVLAVIPGSENESRERIE--KICDSFAVSDIGRDMLVNTNLWSG------- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 388 aisasiSRGKLVSGApidsnRSSSFSKFSNPLWTEILVLAKRSITNSRRMPELFGIRLGAVLITGIILATMFWHLDNSPK 467
Cdd:TIGR00955 319 ------KAGGLVKDS-----ENMEGIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQK 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 468 GVKERLG-FFAFAMSTTFYTCAEAIPVFLQERYIFMRETAYNAYRRSSYVLAHSLISIPSLIILSLAFSGTTYFAVGLAG 546
Cdd:TIGR00955 388 GVQNINGaLFLFLTNMTFQNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 547 GFSGFLFFFAAVLAAFWAGSSFVTFLSGVVSHVMLGYTVVVAILAYFLLFSGFFLSRDRMPPYWIWFHYMSLVKYPYEAV 626
Cdd:TIGR00955 468 GATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 627 LQNEFEATGECFvrgvqMFDNTPLATVPaAAKVELLKSMGktlgfnitgstcvttgsdvlrqQGITDLskWNCIWISMAW 706
Cdd:TIGR00955 548 LINQWSDVDNIE-----CTSANTTGPCP-SSGEVILETLS----------------------FRNADL--YLDLIGLVIL 597
|
650 660
....*....|....*....|
gi 1281000366 707 GFFFRILFYFALLFGSKNKR 726
Cdd:TIGR00955 598 IFFFRLLAYFALRIRIRRKR 617
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
64-718 |
8.94e-85 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 281.38 E-value: 8.94e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 64 YPFKLSFQNLSYSVKV---RRRGSS------LPENLTAEENGGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALA 134
Cdd:PLN03211 36 YPITLKFMDVCYRVKFenmKNKGSNikrilgHKPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 135 DRIAKEKLKGTVTLNDEVLESALLKVIsAYVMQDDLLFPMLTVEETLMFAAEFRLPRSLSKSKKKARVQALIDQLGLTTA 214
Cdd:PLN03211 116 GRIQGNNFTGTILANNRKPTKQILKRT-GFVTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKC 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 215 ANTVIGDEGHRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYRILSLL 294
Cdd:PLN03211 195 ENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 295 DRLIFLSRGQTVYSGSPAELSEFLADFGHPIPENENRTEFALDLVRDLEETAGGTRSMVEHNKSWQWKNKNHLKGHKIVR 374
Cdd:PLN03211 275 DSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDLANGVCQTDGVSEREKPNVKQSLVASYNTLLAPKVKA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 375 RNSSHRFHLCLKDAISASISRgklVSGAPIDSNRSSSFSKFSnplwteilVLAKRSItNSRRMPELFGIRLGAVLITGII 454
Cdd:PLN03211 355 AIEMSHFPQANARFVGSASTK---EHRSSDRISISTWFNQFS--------ILLQRSL-KERKHESFNTLRVFQVIAAALL 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 455 LATMFWHLDNspKGVKERLGFFAF-AMSTTFYTCAEAIPVFLQERYIFMRETAYNAYRRSSYVLAHSLISIPSLIILSLA 533
Cdd:PLN03211 423 AGLMWWHSDF--RDVQDRLGLLFFiSIFWGVFPSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGDLPMELILPTI 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 534 FSGTTYFAVGLAGGFSGFLFFFAAVLAAFWAGSSFVTFLSGVVSHVMLGYTVVVAILAYFLLFSGFFLsrDRMPPYWIWF 613
Cdd:PLN03211 501 FLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGFYV--HKLPSCMAWI 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 614 HYMSLVKYPYEAVLQNEFeATGEcfvrgvqmfdntplatvpaaakvELLKSMGKTLGFNITGSTCVTTGSDVlrqqgITD 693
Cdd:PLN03211 579 KYISTTFYSYRLLINVQY-GEGK-----------------------RISSLLGCSLPHGSDRASCKFVEEDV-----AGQ 629
|
650 660
....*....|....*....|....*
gi 1281000366 694 LSKWNCIWISMAWGFFFRILFYFAL 718
Cdd:PLN03211 630 ISPATSVSVLIFMFVGYRLLAYLAL 654
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
95-309 |
8.72e-71 |
|
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: 230.24 E-value: 8.72e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 95 NGGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKLK-GTVTLNDEVLESALLKVISAYVMQDDLLFP 173
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTsGQILFNGQPRKPDQFQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 174 MLTVEETLMFAAEFRLPRSLSKSKKKARVqaliDQLGLTTAANTVIGDEGHRGVSGGERRRVSIGIDIIHDPILLFLDEP 253
Cdd:cd03234 95 GLTVRETLTYTAILRLPRKSSDAIRKKRV----EDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1281000366 254 TSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYRILSLLDRLIFLSRGQTVYSG 309
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
68-309 |
2.69e-70 |
|
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: 227.82 E-value: 2.69e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 68 LSFQNLSYSVKVRRRGSSlpenltaeenggrvKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKLKGTVT 147
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSG--------------KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 148 LNDEVLESALLKVISAYVMQDDLLFPMLTVEETLMFAAEFRlprslskskkkarvqalidqlglttaantvigdeghrGV 227
Cdd:cd03213 70 INGRPLDKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR-------------------------------------GL 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 228 SGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYRILSLLDRLIFLSRGQTVY 307
Cdd:cd03213 113 SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIY 192
|
..
gi 1281000366 308 SG 309
Cdd:cd03213 193 FG 194
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
69-627 |
7.01e-65 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 234.62 E-value: 7.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 69 SFQNLSYSVKVRrrgsslpenltaeengGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRiakeKLKGTVTL 148
Cdd:TIGR00956 761 HWRNLTYEVKIK----------------KEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAER----VTTGVITG 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 149 NDEV-----LESALLKvISAYVMQDDLLFPMLTVEETLMFAAEFRLPRSLSKSKKKARVQALIDQLGLTTAANTVIGDEG 223
Cdd:TIGR00956 821 GDRLvngrpLDSSFQR-SIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPG 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 224 hRGVSGGERRRVSIGIDIIHDP-ILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYRILSLLDRLIFLSR 302
Cdd:TIGR00956 900 -EGLNVEQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQK 978
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 303 G-QTVYSGSPAE----LSEFLADFG-HPIPENENRTEFALDLVrdleETAGGTRSMVEHNKSWqwknknhlkghkivrRN 376
Cdd:TIGR00956 979 GgQTVYFGDLGEnshtIINYFEKHGaPKCPEDANPAEWMLEVI----GAAPGAHANQDYHEVW---------------RN 1039
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 377 SSHRfhlclkDAISASISR-GKLVSGAPiDSNRSSSFSKFSNPLWTEILVLAKRSITNSRRMPELFGIRLGAVLITGIIL 455
Cdd:TIGR00956 1040 SSEY------QAVKNELDRlEAELSKAE-DDNDPDALSKYAASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFI 1112
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 456 ATMFWHLDNSPKGVKERLgfFAFAMSTTFYTCA--EAIPVFL-QERYIFMRETAYNAYRRSSYVLAHSLISIPSLIILSL 532
Cdd:TIGR00956 1113 GFTFFKVGTSLQGLQNQM--FAVFMATVLFNPLiqQYLPPFVaQRDLYEVRERPSRTFSWLAFIAAQITVEIPYNLVAGT 1190
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 533 AFSGTTYFAVGLAGGFSGFLFFFAAVLAAFWAGSSFVTFLSGVVSHVM-----LGYTVVVAILAY--FLLFSGFFLSRDR 605
Cdd:TIGR00956 1191 IFFFIWYYPVGFYWNASKTGQVHERGVLFWLLSTMFFLYFSTLGQMVIsfnpnADNAAVLASLLFtmCLSFCGVLAPPSR 1270
|
570 580
....*....|....*....|..
gi 1281000366 606 MPPYWIWFHYMSLVKYPYEAVL 627
Cdd:TIGR00956 1271 MPGFWIFMYRCSPFTYLVQALL 1292
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
102-633 |
3.88e-55 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 205.34 E-value: 3.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 102 LLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKLK--GTVTLNDEVLESAL--LKVISAYVMQDDLLFPMLTV 177
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGveGVITYDGITPEEIKkhYRGDVVYNAETDVHFPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 178 EETLMFAAEFRLPRS----LSKSKKKARVQALI-DQLGLTTAANTVIGDEGHRGVSGGERRRVSIGIDIIHDPILLFLDE 252
Cdd:TIGR00956 156 GETLDFAARCKTPQNrpdgVSREEYAKHIADVYmATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 253 PTSGLDSTSAFMVVKVLQRIAQ-SGSIVITSIHQPSYRILSLLDRLIFLSRGQTVYSGSPAELSEFLADFGHPIPENENR 331
Cdd:TIGR00956 236 ATRGLDSATALEFIRALKTSANiLDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFKCPDRQTT 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 332 TEFALDLVRDLEET--AGGT----RSMVEHNKSWqwknKNHLKGHKIVRRNSSHrfhlclKDAISASISRGKLV-SGAPI 404
Cdd:TIGR00956 316 ADFLTSLTSPAERQikPGYEkkvpRTPQEFETYW----RNSPEYAQLMKEIDEY------LDRCSESDTKEAYReSHVAK 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 405 DSNRSSSFSKFSNPLWTEILVLAKRSITNSRRMPELFGIRLGAVLITGIILATMFWHLDNSPKGVKERLGFFAFAMSTTF 484
Cdd:TIGR00956 386 QSKRTRPSSPYTVSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRGGALFFAILFNA 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 485 YTCAEAIPVFLQERYIFMRETAYNAYRRSSYVLAHSLISIPSLIILSLAFSGTTYFAVGLAGGFSGFLFFFAAVLAAFWA 564
Cdd:TIGR00956 466 FSSLLEIASMYEARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLILFICTLA 545
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1281000366 565 GSSFVTFLSGV---VSHVMLGYTVVVAILAyflLFSGFFLSRDRMPPYWIWFHYMSLVKYPYEAVLQNEFEA 633
Cdd:TIGR00956 546 MSHLFRSIGAVtktLSEAMTPAAILLLALS---IYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVNEFHG 614
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
68-309 |
2.20e-54 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 185.14 E-value: 2.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 68 LSFQNLSYSVKVrrrgsslpenltaeeNGGRvKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKLKGTVT 147
Cdd:cd03232 4 LTWKNLNYTVPV---------------KGGK-RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEIL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 148 LNDEVLESALLKvISAYVMQDDLLFPMLTVEETLMFAAEFRlprslskskkkarvqalidqlglttaantvigdeghrGV 227
Cdd:cd03232 68 INGRPLDKNFQR-STGYVEQQDVHSPNLTVREALRFSALLR-------------------------------------GL 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 228 SGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYRILSLLDRLIFLSR-GQTV 306
Cdd:cd03232 110 SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRgGKTV 189
|
...
gi 1281000366 307 YSG 309
Cdd:cd03232 190 YFG 192
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
7-621 |
3.41e-47 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 181.20 E-value: 3.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 7 DTFPRSWSYTNESELREFA-RRPTLGELLKQVEDAQSPDHRTVDVSYGcsyLAPPpvLYPFKLSFQNLSYSVkvrrrgsS 85
Cdd:PLN03140 811 DSIPRSLSSADGNNTREVAiQRMSNPEGLSKNRDSSLEAANGVAPKRG---MVLP--FTPLAMSFDDVNYFV-------D 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 86 LPENLTaEENGGRVKL-LLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKLKGTVTLNDEVLESALLKVISAY 164
Cdd:PLN03140 879 MPAEMK-EQGVTEDRLqLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFPKKQETFARISGY 957
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 165 VMQDDLLFPMLTVEETLMFAAEFRLPRSLSKSKKKARVQALIDQLGLTTAANTVIGDEGHRGVSGGERRRVSIGIDIIHD 244
Cdd:PLN03140 958 CEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVAN 1037
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 245 PILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYRILSLLDRLIFLSR-GQTVYSGSPAELSE-----FL 318
Cdd:PLN03140 1038 PSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRgGQVIYSGPLGRNSHkiieyFE 1117
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 319 ADFGHP-IPENENRTEFALDLVRDLEETAGGTrSMVEHNKSwqwknknhlkgHKIVRRNSShrfhlcLKDAISASISRGK 397
Cdd:PLN03140 1118 AIPGVPkIKEKYNPATWMLEVSSLAAEVKLGI-DFAEHYKS-----------SSLYQRNKA------LVKELSTPPPGAS 1179
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 398 LVSGAPIDSNrsSSFSKFSNPLWteilvlaKRSITnSRRMPELFGIRLGAVLITGIILATMFWHL----DNSPKGVKERL 473
Cdd:PLN03140 1180 DLYFATQYSQ--STWGQFKSCLW-------KQWWT-YWRSPDYNLVRFFFTLAAALMVGTIFWKVgtkrSNANDLTMVIG 1249
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 474 GFFAFAMSTTFYTCAEAIPVFLQERYIFMRETAYNAYRRSSYVLAHSLISIPSLIILSLAFSGTTYFAVGLAGGFSGFLF 553
Cdd:PLN03140 1250 AMYAAVLFVGINNCSTVQPMVAVERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFW 1329
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 554 FFaavlaafwagssFVTFLS-------GVVSHVMLGYTVVVAILA-----YFLLFSGFFLSRDRMPPYWIWFHYMSLVKY 621
Cdd:PLN03140 1330 FY------------FISFFSflyftyyGMMTVSLTPNQQVAAIFAaafygLFNLFSGFFIPRPKIPKWWVWYYWICPVAW 1397
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
103-320 |
5.96e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 163.70 E-value: 5.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVLESALLKVIS--AYVMQDDLLFPMLTVEET 180
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTS--GEVRVLGEDVARDPAEVRRriGYVPQEPALYPDLTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 181 LMFAAEFRlprSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDST 260
Cdd:COG1131 94 LRFFARLY---GLPRKEARERIDELLELFGLTDAADRKVGT-----LSGGMKQRLGLALALLHDPELLILDEPTSGLDPE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281000366 261 SAFMVVKVLQRIAQSGSIVITSIHqpsyrILS----LLDRLIFLSRGQTVYSGSPAEL-SEFLAD 320
Cdd:COG1131 166 ARRELWELLRELAAEGKTVLLSTH-----YLEeaerLCDRVAIIDKGRIVADGTPDELkARLLED 225
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
98-720 |
4.81e-45 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 174.65 E-value: 4.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 98 RVKL-LLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKE-KLKGTVTLNDEVLESALLKVISAYVMQDDLLFPML 175
Cdd:PLN03140 175 KTKLtILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlKVSGEITYNGYRLNEFVPRKTSAYISQNDVHVGVM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 176 TVEETLMFAAE-------FRLPRSLSKSKKKARV--QALIDQ----------------------LGLTTAANTVIGDEGH 224
Cdd:PLN03140 255 TVKETLDFSARcqgvgtrYDLLSELARREKDAGIfpEAEVDLfmkatamegvksslitdytlkiLGLDICKDTIVGDEMI 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 225 RGVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQ-SGSIVITSIHQPSYRILSLLDRLIFLSRG 303
Cdd:PLN03140 335 RGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHlTEATVLMSLLQPAPETFDLFDDIILLSEG 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 304 QTVYSGSPAELSEFLADFGHPIPENENRTEFaldlvrdLEETAggtrSMVEHNKSWQWKNK--NHLKGHKIVRRnsSHRF 381
Cdd:PLN03140 415 QIVYQGPRDHILEFFESCGFKCPERKGTADF-------LQEVT----SKKDQEQYWADRNKpyRYISVSEFAER--FKSF 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 382 HLCLKDAISASIsrgklvsgaPIDSNRSS----SFSKFSNP-------LWTEILVLAKRsitNSRrmpeLFGIRLGAVLI 450
Cdd:PLN03140 482 HVGMQLENELSV---------PFDKSQSHkaalVFSKYSVPkmellkaCWDKEWLLMKR---NAF----VYVFKTVQIII 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 451 TGIILATMF----WHLDNSPKGvKERLGFFAFAMSTTFYTCAEAIPVFLQERYIFMRETAYNAYRRSSYVLAHSLISIPS 526
Cdd:PLN03140 546 VAAIASTVFlrteMHTRNEEDG-ALYIGALLFSMIINMFNGFAELALMIQRLPVFYKQRDLLFHPPWTFTLPTFLLGIPI 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 527 LIILSLAFSGTTYFAVGLAGGFSGFLFFFAAVLAAFWAGSSFVTFLSGVVSHVMLGYTVVVAILAYFLLFSGFFLSRDRM 606
Cdd:PLN03140 625 SIIESVVWVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEI 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 607 PPYWIWFHYMSLVKYPYEAVLQNEFEATgecfvrgvqmfdntplatvpaaakvellKSMGKTLGFNITgstcvTTGSDVL 686
Cdd:PLN03140 705 PNWWEWAYWVSPLSYGFNALAVNEMFAP----------------------------RWMNKMASDNST-----RLGTAVL 751
|
650 660 670
....*....|....*....|....*....|....*.
gi 1281000366 687 RQQGITDLSKWNCIWISMAWGF--FFRILFYFALLF 720
Cdd:PLN03140 752 NIFDVFTDKNWYWIGVGALLGFtiLFNVLFTLALTY 787
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
100-316 |
1.55e-40 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 148.85 E-value: 1.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVLESALLKVIS--AYVMQDDLLFPMLTV 177
Cdd:COG4555 14 VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDS--GSILIDGEDVRKEPREARRqiGVLPDERGLYDRLTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 178 EETLMFAAEFRlprSLSKSKKKARVQALIDQLGLTTAANTVIGdeghrGVSGGERRRVSIGIDIIHDPILLFLDEPTSGL 257
Cdd:COG4555 92 RENIRYFAELY---GLFDEELKKRIEELIELLGLEEFLDRRVG-----ELSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1281000366 258 DSTSAFMVVKVLQRIAQSGSIVITSIHQPsYRILSLLDRLIFLSRGQTVYSGSPAELSE 316
Cdd:COG4555 164 DVMARRLLREILRALKKEGKTVLFSSHIM-QEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
96-314 |
3.76e-40 |
|
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: 146.88 E-value: 3.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 96 GGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLNDEVLESALLKV--ISAYVMQDDLLFP 173
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGEL--RPTSGTAYINGYSIRTDRKAArqSLGYCPQFDALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 174 MLTVEETLMFAAEFRlprSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLDEP 253
Cdd:cd03263 89 ELTVREHLRFYARLK---GLPKSEIKEEVELLLRVLGLTDKANKRART-----LSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1281000366 254 TSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYRILSllDRLIFLSRGQTVYSGSPAEL 314
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALC--DRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
96-304 |
1.41e-38 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 142.22 E-value: 1.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 96 GGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLNDEVLESALLKVIS---AYVMQD-DLL 171
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL--GPTSGEVLVDGKDLTKLSLKELRrkvGLVFQNpDDQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 172 FPMLTVEETLMFAAEFRlprSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLD 251
Cdd:cd03225 88 FFGPTVEEEVAFGLENL---GLPEEEIEERVEEALELVGLEGLRDRSPFT-----LSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1281000366 252 EPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYrILSLLDRLIFLSRGQ 304
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDL-LLELADRVIVLEDGK 211
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
426-629 |
1.80e-38 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 141.64 E-value: 1.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 426 LAKRSITNSRRMPELFGIRLGAVLITGIILATMFWHLDNSPKGVkERLGFFAFAMSTTFYT-CAEAIPVFLQERYIFMRE 504
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQGGL-NRPGLLFFSILFNAFSaLSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 505 TAYNAYRRSSYVLAHSLISIPSLIILSLAFSGTTYFAVGLAGGFSGFLFFFAAVLAAFWAGSSFVTFLSGVVSHVMLGYT 584
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1281000366 585 VVVAILAYFLLFSGFFLSRDRMPPYWIWFHYMSLVKYPYEAVLQN 629
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
89-309 |
5.25e-38 |
|
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: 140.48 E-value: 5.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 89 NLTAEENGGRVKL-LLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAK-EKLKGTVTLN----DEVLESALLKVIs 162
Cdd:cd03233 8 NISFTTGKGRSKIpILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnVSVEGDIHYNgipyKEFAEKYPGEII- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 163 aYVMQDDLLFPMLTVEETLMFAAEFRlprslskskkkarvqalidqlglttaantviGDEGHRGVSGGERRRVSIGIDII 242
Cdd:cd03233 87 -YVSEEDVHFPTLTVRETLDFALRCK-------------------------------GNEFVRGISGGERKRVSIAEALV 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1281000366 243 HDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQ-SGSIVITSIHQPSYRILSLLDRLIFLSRGQTVYSG 309
Cdd:cd03233 135 SRASVLCWDNSTRGLDSSTALEILKCIRTMADvLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
100-325 |
5.19e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 135.99 E-value: 5.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLNDEVLESALLKVisAYVMQD---DLLFPMlT 176
Cdd:COG1121 19 RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLL--PPTSGTVRLFGKPPRRARRRI--GYVPQRaevDWDFPI-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 177 VEETLM--FAAEFRLPRSLSKsKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLDEPT 254
Cdd:COG1121 94 VRDVVLmgRYGRRGLFRRPSR-ADREAVDEALERVGLEDLADRPIGE-----LSGGQQQRVLLARALAQDPDLLLLDEPF 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1281000366 255 SGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSyRILSLLDRLIFLSRGQtVYSGSPAEL--SEFLAD-FGHPI 325
Cdd:COG1121 168 AGVDAATEEALYELLRELRREGKTILVVTHDLG-AVREYFDRVLLLNRGL-VAHGPPEEVltPENLSRaYGGPV 239
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
88-314 |
3.33e-34 |
|
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: 130.53 E-value: 3.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGRVklLLNDISGEAREGEIMAVLGASGSGKSTLIDALAdRIAKEKlKGTVTLNDEVLESALLKVIS---AY 164
Cdd:COG1122 4 ENLSFSYPGGTP--ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLN-GLLKPT-SGEVLVDGKDITKKNLRELRrkvGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 165 VMQ--DDLLFpMLTVEETLMFAAEfrlPRSLSKSKKKARVQALIDQLGLTTAANTVIgdegHRgVSGGERRRVSI-GIdI 241
Cdd:COG1122 80 VFQnpDDQLF-APTVEEDVAFGPE---NLGLPREEIRERVEEALELVGLEHLADRPP----HE-LSGGQKQRVAIaGV-L 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1281000366 242 IHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYrILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
103-255 |
1.55e-33 |
|
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: 125.84 E-value: 1.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEklKGTVTLNDEVL---ESALLKVISAYVMQDDLLFPMLTVEE 179
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT--EGTILLDGQDLtddERKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1281000366 180 TLMFAAEFrlpRSLSKSKKKARVQALIDQLGLTTAANTVIGDEGHrGVSGGERRRVSIGIDIIHDPILLFLDEPTS 255
Cdd:pfam00005 79 NLRLGLLL---KGLSKREKDARAEEALEKLGLGDLADRPVGERPG-TLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
103-306 |
8.99e-33 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 126.31 E-value: 8.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALA--DRIAkeklKGTVTLNDEVL----ESALLKV----ISaYVMQDDLLF 172
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGglDRPT----SGEVLIDGQDIsslsERELARLrrrhIG-FVFQFFNLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 173 PMLTVEETLMFAAEFrlpRSLSKSKKKARVQALIDQLGLttaantvigdeGHRG------VSGGERRRVSIGIDIIHDPI 246
Cdd:COG1136 99 PELTALENVALPLLL---AGVSRKERRERARELLERVGL-----------GDRLdhrpsqLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1281000366 247 LLFLDEPTSGLDSTSAFMVVKVLQRIA-QSGSIVITSIHQPsyRILSLLDRLIFLSRGQTV 306
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDP--ELAARADRVIRLRDGRIV 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
96-325 |
6.01e-32 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 124.77 E-value: 6.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 96 GGRVklLLNDISGEAREGEIMAVLGASGSGKSTLIDALAdRIAKeKLKGTVTLNDEVLES----ALLKVIsAYVMQD-DL 170
Cdd:COG1120 12 GGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALA-GLLK-PSSGEVLLDGRDLASlsrrELARRI-AYVPQEpPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 171 LFPmLTVEETLMFAaefRLP--RSLSKSKKK--ARVQALIDQLGLTTAAntvigdegHRGV---SGGERRRVSIGIDIIH 243
Cdd:COG1120 87 PFG-LTVRELVALG---RYPhlGLFGRPSAEdrEAVEEALERTGLEHLA--------DRPVdelSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 244 DPILLFLDEPTSGLDSTSAFMVVKVLQRIAQS-GSIVITSIHQPSyriLSLL--DRLIFLSRGQTVYSGSPAEL--SEFL 318
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLN---LAARyaDRLVLLKDGRIVAQGPPEEVltPELL 231
|
....*...
gi 1281000366 319 AD-FGHPI 325
Cdd:COG1120 232 EEvYGVEA 239
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
94-304 |
1.50e-31 |
|
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: 122.60 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 94 ENGGRVKLLLNDISGEAREGEIMAVLGASGSGKSTL--IDALADRIAKeklkGTVTLNDEVL----ESALLKV----ISa 163
Cdd:cd03255 11 GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLlnILGGLDRPTS----GEVRVDGTDIsklsEKELAAFrrrhIG- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 164 YVMQDDLLFPMLTVEETLMFAAEFRlprSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIH 243
Cdd:cd03255 86 FVFQSFNLLPDLTALENVELPLLLA---GVPKKERRERAEELLERVGLGDRLNHYPSE-----LSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1281000366 244 DPILLFLDEPTSGLDSTSAFMVVKVLQRIA-QSG-SIVITSiHQPsyRILSLLDRLIFLSRGQ 304
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELNkEAGtTIVVVT-HDP--ELAEYADRIIELRDGK 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
103-304 |
2.02e-31 |
|
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: 120.58 E-value: 2.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVLESALLKVIS--AYVMQDDLLFPMLTVEET 180
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDS--GEIKVLGKDIKKEPEEVKRriGYLPEEPSLYENLTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 181 LMFaaefrlprslskskkkarvqalidqlglttaantvigdeghrgvSGGERRRVSIGIDIIHDPILLFLDEPTSGLDST 260
Cdd:cd03230 94 LKL--------------------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1281000366 261 SAFMVVKVLQRIAQSGSIVITSIHQPSyRILSLLDRLIFLSRGQ 304
Cdd:cd03230 130 SRREFWELLRELKKEGKTILLSSHILE-EAERLCDRVAILNNGR 172
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
58-316 |
2.81e-31 |
|
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: 129.11 E-value: 2.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 58 APPPVLYPFKLSFQNLSYSVKVRRRgsslpenltaeenggrvklLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRI 137
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSYPGGRP-------------------ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 138 AKEklKGTVTLNDEVL----ESALLKVIsAYVMQDDLLFPMlTVEETLMFAA----EFRLPRSLskskKKARVQALIDQL 209
Cdd:COG4988 388 PPY--SGSILINGVDLsdldPASWRRQI-AWVPQNPYLFAG-TIRENLRLGRpdasDEELEAAL----EAAGLDEFVAAL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 210 --GLttaaNTVIGDEGhRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQsGSIVITSIHQPS 287
Cdd:COG4988 460 pdGL----DTPLGEGG-RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLA 533
|
250 260
....*....|....*....|....*....
gi 1281000366 288 yrILSLLDRLIFLSRGQTVYSGSPAELSE 316
Cdd:COG4988 534 --LLAQADRILVLDDGRIVEQGTHEELLA 560
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
103-350 |
6.02e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 120.21 E-value: 6.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVLESALLKVIsAYvmqddL-----LFPMLTV 177
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDS--GEVLWDGEPLDPEDRRRI-GY-----LpeergLYPKMKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 178 EETLMFAAefRLpRSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLDEPTSGL 257
Cdd:COG4152 89 GEQLVYLA--RL-KGLSKAEAKRRADEWLERLGLGDRANKKVEE-----LSKGNQQKVQLIAALLHDPELLILDEPFSGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 258 DSTSAFMVVKVLQRIAQSGSIVITSIHQpsyriLS----LLDRLIFLSRGQTVYSGSpaeLSEFLADFGHP--IPENENR 331
Cdd:COG4152 161 DPVNVELLKDVIRELAAKGTTVIFSSHQ-----MElveeLCDRIVIINKGRKVLSGS---VDEIRRQFGRNtlRLEADGD 232
|
250 260
....*....|....*....|.
gi 1281000366 332 TEFALDL--VRDLEETAGGTR 350
Cdd:COG4152 233 AGWLRALpgVTVVEEDGDGAE 253
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
10-314 |
1.22e-29 |
|
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: 124.49 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 10 PRSWSYTNESelREFARRptLGELLKQVEDAQSPDhrtvdvsygcsylAPPPVLYPFKLSFQNLSYsvkvRRRGSSLPen 89
Cdd:COG4987 293 PAAAQHLGRV--RAAARR--LNELLDAPPAVTEPA-------------EPAPAPGGPSLELEDVSF----RYPGAGRP-- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 90 ltaeenggrvklLLNDISGEAREGEIMAVLGASGSGKSTLIDALAdRIAkEKLKGTVTLND----EVLESALLKVIsAYV 165
Cdd:COG4987 350 ------------VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLL-RFL-DPQSGSITLGGvdlrDLDEDDLRRRI-AVV 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 166 MQDDLLFPMlTVEETLMFAA----EFRLPRSLskskKKARVQALIDQL--GLttaaNTVIGdEGHRGVSGGERRRVSIGI 239
Cdd:COG4987 415 PQRPHLFDT-TLRENLRLARpdatDEELWAAL----ERVGLGDWLAALpdGL----DTWLG-EGGRRLSGGERRRLALAR 484
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281000366 240 DIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSiHQPSyrILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLIT-HRLA--GLERMDRILVLEDGRIVEQGTHEEL 556
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
96-321 |
1.28e-29 |
|
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: 117.77 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 96 GGRVklLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEklKGTVTLNDEVL----ESALLKVIS--AYVMQDD 169
Cdd:COG1127 16 GDRV--VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPD--SGEILVDGQDItglsEKELYELRRriGMLFQGG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 170 LLFPMLTVEETLMFAAEFRlpRSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLF 249
Cdd:COG1127 92 ALFDSLTVFENVAFPLREH--TDLSEAEIRELVLEKLELVGLPGAADKMPSE-----LSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 250 LDEPTSGLDSTSAFMVVKVLQRIAQS---GSIVITsiHQ-PSyrILSLLDRLIFLSRGQTVYSGSPAEL----SEFLADF 321
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRELRDElglTSVVVT--HDlDS--AFAIADRVAVLADGKIIAEGTPEELlasdDPWVRQF 240
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
103-342 |
3.28e-29 |
|
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: 118.26 E-value: 3.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKLKGTVTLNDEVLESALLKVISAYVMQDDLLFPMLTVEETLM 182
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLTGRENLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 183 FAAEFRlprSLSKSKKKARVQALIDQLGLTTAANTVIGdeghrGVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSA 262
Cdd:TIGR01188 89 MMGRLY---GLPKDEAEERAEELLELFELGEAADRPVG-----TYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 263 FMVVKVLQRIAQSGSIVITSIHQpSYRILSLLDRLIFLSRGQTVYSGSPAELSEFLadfGHPIPENENRTEFALDLVRDL 342
Cdd:TIGR01188 161 RAIWDYIRALKEEGVTILLTTHY-MEEADKLCDRIAIIDHGRIIAEGTPEELKRRL---GKDTLESRPRDIQSLKVEVSM 236
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
88-316 |
4.71e-29 |
|
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: 116.13 E-value: 4.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGRVKLllNDISGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLNDEVLESALLKVI------ 161
Cdd:cd03256 4 ENLSKTYPNGKKAL--KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLV--EPTSGSVLIDGTDINKLKGKALrqlrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 162 SAYVMQDDLLFPMLTVEETLMFAAEFRLP--RSLSKSKKKARVQ---ALIDQLGLTTAANTVIGDeghrgVSGGERRRVS 236
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVLSGRLGRRStwRSLFGLFPKEEKQralAALERVGLLDKAYQRADQ-----LSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 237 IGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQS-GSIVITSIHQPSYrILSLLDRLIFLSRGQTVYSGSPAELS 315
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDL-AREYADRIVGLKDGRIVFDGPPAELT 233
|
.
gi 1281000366 316 E 316
Cdd:cd03256 234 D 234
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
94-258 |
6.94e-29 |
|
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: 114.88 E-value: 6.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 94 ENGGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALA--DRIAkeklKGTVTLNDEVLESALLKVisAYVMQDDLL 171
Cdd:cd03293 11 GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAglERPT----SGEVLVDGEPVTGPGPDR--GYVFQQDAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 172 FPMLTVEETLMFAAEFrlpRSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLD 251
Cdd:cd03293 85 LPWLTVLDNVALGLEL---QGVPKAEARERAEELLELVGLSGFENAYPHQ-----LSGGMRQRVALARALAVDPDVLLLD 156
|
....*..
gi 1281000366 252 EPTSGLD 258
Cdd:cd03293 157 EPFSALD 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
68-324 |
8.31e-29 |
|
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: 121.16 E-value: 8.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 68 LSFQNLSYSVKVRRRGSslpenLTAeenggrvkllLNDISGEAREGEIMAVLGASGSGKSTLIDALAdRIAKEKlKGTVT 147
Cdd:COG1123 261 LEVRNLSKRYPVRGKGG-----VRA----------VDDVSLTLRRGETLGLVGESGSGKSTLARLLL-GLLRPT-SGSIL 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 148 LNDEVLESALLKVISA------YVMQD--DLLFPMLTVEETLMFAAefRLPRSLSKSKKKARVQALIDQLGLttaantvi 219
Cdd:COG1123 324 FDGKDLTKLSRRSLRElrrrvqMVFQDpySSLNPRMTVGDIIAEPL--RLHGLLSRAERRERVAELLERVGL-------- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 220 gDEGHRGV-----SGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQS---GSIVITsiHQpsyriL 291
Cdd:COG1123 394 -PPDLADRyphelSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElglTYLFIS--HD-----L 465
|
250 260 270
....*....|....*....|....*....|....*..
gi 1281000366 292 SLL----DRLIFLSRGQTVYSGSPAELsefLADFGHP 324
Cdd:COG1123 466 AVVryiaDRVAVMYDGRIVEDGPTEEV---FANPQHP 499
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
88-314 |
9.79e-29 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 120.78 E-value: 9.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGRVKLLlNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKE-KLKGTVTLNDEVLESALLKVIS---A 163
Cdd:COG1123 8 RDLSVRYPGGDVPAV-DGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgRISGEVLLDGRDLLELSEALRGrriG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 164 YVMQD-DLLFPMLTVEETLMFAAEFRlprSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDII 242
Cdd:COG1123 87 MVFQDpMTQLNPVTVGDQIAEALENL---GLSRAEARARVLELLEAVGLERRLDRYPHQ-----LSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1281000366 243 HDPILLFLDEPTSGLDSTSAFMVVKVLQRI-AQSGSIVITSIHQPSYrILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGV-VAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
88-309 |
6.70e-28 |
|
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: 111.90 E-value: 6.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGRVkllLNDISGEAREGeIMAVLGASGSGKSTLIDALADriAKEKLKGTVTLNDE-VLES--ALLKVISaY 164
Cdd:cd03264 4 ENLTKRYGKKRA---LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILAT--LTPPSSGTIRIDGQdVLKQpqKLRRRIG-Y 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 165 VMQDDLLFPMLTVEETLMFAAefRLpRSLSKSKKKARVQALIDQLGLTTAANTVIGdeghrGVSGGERRRVSIGIDIIHD 244
Cdd:cd03264 77 LPQEFGVYPNFTVREFLDYIA--WL-KGIPSKEVKARVDEVLELVNLGDRAKKKIG-----SLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281000366 245 PILLFLDEPTSGLDSTSAFMVVKVLQRIAqSGSIVITSIHQPSyRILSLLDRLIFLSRGQTVYSG 309
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHIVE-DVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
102-306 |
9.44e-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: 9.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 102 LLNDISGEAREGEIMAVLGASGSGKSTLIDALA--DRIAkeklKGTVTLNDEVLESalLKVIS---AYVMQDDLLFPMLT 176
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAglERPD----SGEILIDGRDVTG--VPPERrniGMVFQDYALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 177 VEETLMFAAEFRLprsLSKSKKKARVQALIDQLGLTtaantvigDEGHR---GVSGGERRRVSIGIDIIHDPILLFLDEP 253
Cdd:cd03259 89 VAENIAFGLKLRG---VPKAEIRARVRELLELVGLE--------GLLNRyphELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1281000366 254 TSGLDS-TSAFMVVKVLQRIAQSGSIVITSIHQPSyRILSLLDRLIFLSRGQTV 306
Cdd:cd03259 158 LSALDAkLREELREELKELQRELGITTIYVTHDQE-EALALADRIAVMNEGRIV 210
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
96-316 |
1.03e-27 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 119.17 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 96 GGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALAdriakeKL----KGTVTLNDEVLESALLKVIS---AYVMQD 168
Cdd:COG2274 484 PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL------GLyeptSGRILIDGIDLRQIDPASLRrqiGVVLQD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 169 DLLFPMlTVEETLMFAAEfrlprSLSKSK-----KKARVQALIDQL--GLttaaNTVIGDEGhRGVSGGERRRVSIGIDI 241
Cdd:COG2274 558 VFLFSG-TIRENITLGDP-----DATDEEiieaaRLAGLHDFIEALpmGY----DTVVGEGG-SNLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281000366 242 IHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSiHQPSyrILSLLDRLIFLSRGQTVYSGSPAELSE 316
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIA-HRLS--TIRLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
96-314 |
1.29e-27 |
|
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: 111.82 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 96 GGRVklLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLN----DEVLESALLKVI--SAYVMQDD 169
Cdd:cd03261 11 GGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDS--GEVLIDgediSGLSEAELYRLRrrMGMLFQSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 170 LLFPMLTVEETLMFAaeFRLPRSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLF 249
Cdd:cd03261 87 ALFDSLTVFENVAFP--LREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAE-----LSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1281000366 250 LDEPTSGLDSTSAFMVVKVLQRIAQS---GSIVITSIHQPSYRIlslLDRLIFLSRGQTVYSGSPAEL 314
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKElglTSIMVTHDLDTAFAI---ADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
103-309 |
2.53e-27 |
|
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: 110.06 E-value: 2.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVLESALLKVIsAYVMQDDLLFPMLTVEETLM 182
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDS--GEVLFDGKPLDIAARNRI-GYLPEERGLYPKMKVIDQLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 183 FAAEFRlprSLSKSKKKARVQALIDQLGLTTAANTVIgdeghRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSA 262
Cdd:cd03269 93 YLAQLK---GLKKEEARRRIDEWLERLELSEYANKRV-----EELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1281000366 263 FMVVKVLQRIAQSGSIVITSIHQPSyRILSLLDRLIFLSRGQTVYSG 309
Cdd:cd03269 165 ELLKDVIRELARAGKTVILSTHQME-LVEELCDRVLLLNKGRAVLYG 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
68-296 |
3.21e-27 |
|
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: 109.49 E-value: 3.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 68 LSFQNLSysvkVRRrgsslpenltaeenGGRvkLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVT 147
Cdd:COG4133 3 LEAENLS----CRR--------------GER--LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSA--GEVL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 148 LNDEVLESALLKVIS--AYVMQDDLLFPMLTVEETLMFAAEFRlPRSLSKskkkARVQALIDQLGLTTAANTVIgdeghR 225
Cdd:COG4133 61 WNGEPIRDAREDYRRrlAYLGHADGLKPELTVRENLRFWAALY-GLRADR----EAIDEALEAVGLAGLADLPV-----R 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281000366 226 GVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQP----SYRILSLLDR 296
Cdd:COG4133 131 QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPlelaAARVLDLGDF 205
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
103-313 |
3.82e-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: 110.22 E-value: 3.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVL------ESALLKVISAYvmQDDLLFPMLT 176
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTS--GSVLFDGEDItglpphEIARLGIGRTF--QIPRLFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 177 VEETLMFAAEFRLPRSLS-----KSKKKARVQA--LIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLF 249
Cdd:cd03219 92 VLENVMVAAQARTGSGLLlararREEREARERAeeLLERVGLADLADRPAGE-----LSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281000366 250 LDEPTSGLDSTSAFMVVKVLQRIAQSG-SIVITSIHQPSyrILSLLDRLIFLSRGQTVYSGSPAE 313
Cdd:cd03219 167 LDEPAAGLNPEETEELAELIRELRERGiTVLLVEHDMDV--VMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
103-316 |
6.33e-27 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 109.45 E-value: 6.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALAD--RIAkeklKGTVTLNDEVLESALLKVIS----AYVMQDDLLFPMLT 176
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGllPPR----SGSIRFDGRDITGLPPHERAragiGYVPEGRRIFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 177 VEETLMFAAEFRlprslSKSKKKARVQALID---QLG--LTTAANTvigdeghrgVSGGERRRVSIGIDIIHDPILLFLD 251
Cdd:cd03224 92 VEENLLLGAYAR-----RRAKRKARLERVYElfpRLKerRKQLAGT---------LSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 252 EPTSGLdstsAFMVVK----VLQRIAQSG-SIVItsIHQPSYRILSLLDRLIFLSRGQTVYSGSPAELSE 316
Cdd:cd03224 158 EPSEGL----APKIVEeifeAIRELRDEGvTILL--VEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
100-304 |
8.57e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 108.36 E-value: 8.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVLESalLKVIS-----AYVMQDDLLFPM 174
Cdd:COG4619 13 KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTS--GEIYLDGKPLSA--MPPPEwrrqvAYVPQEPALWGG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 175 lTVEETLMFAAEFRlprslSKSKKKARVQALIDQLGLTTAA-NTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLDEP 253
Cdd:COG4619 89 -TVRDNLPFPFQLR-----ERKFDRERALELLERLGLPPDIlDKPVER-----LSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1281000366 254 TSGLDSTSAFMVVKVLQRIAQS--GSIVITSiHQPSYrILSLLDRLIFLSRGQ 304
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEegRAVLWVS-HDPEQ-IERVADRVLTLEAGR 208
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
88-309 |
1.11e-26 |
|
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: 108.75 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAE-ENGGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALAdRIAKeKLKGTVTLNDEVLESALLKVIS---- 162
Cdd:cd03257 5 KNLSVSfPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAIL-GLLK-PTSGSIIFDGKDLLKLSRRLRKirrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 163 --AYVMQDDL--LFPMLTVEETLMFAAEFRLPRSlSKSKKKARVQALIDQLGLttaantvigDEGH-----RGVSGGERR 233
Cdd:cd03257 83 eiQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLS-KKEARKEAVLLLLVGVGL---------PEEVlnrypHELSGGQRQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 234 RVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQS---GSIVITsiHQpsyriLSLL----DRLIFLSRGQTV 306
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElglTLLFIT--HD-----LGVVakiaDRVAVMYAGKIV 225
|
...
gi 1281000366 307 YSG 309
Cdd:cd03257 226 EEG 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
103-304 |
4.27e-26 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 106.46 E-value: 4.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALAdriAKEKL-KGTVTLNDEVL---ESALLKVIS--AYVMQDDLLFPMLT 176
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCIN---LLEEPdSGTIIIDGLKLtddKKNINELRQkvGMVFQQFNLFPHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 177 VEETLMFAAefRLPRSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLDEPTSG 256
Cdd:cd03262 93 VLENITLAP--IKVKGMSKAEAEERALELLEKVGLADKADAYPAQ-----LSGGQQQRVAIARALAMNPKVMLFDEPTSA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1281000366 257 LDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYrILSLLDRLIFLSRGQ 304
Cdd:cd03262 166 LDPELVGEVLDVMKDLAEEGMTMVVVTHEMGF-AREVADRVIFMDDGR 212
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
88-280 |
8.40e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 105.64 E-value: 8.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGgrvKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKE-KLKGTVTLNDEVLES--ALLKVIsAY 164
Cdd:COG4136 5 ENLTITLGG---RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfSASGEVLLNGRRLTAlpAEQRRI-GI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 165 VMQDDLLFPMLTVEETLMFAaefrLPRSLSKSKKKARVQALIDQLGLTTAANtvigdeghRGV---SGGERRRVSIGIDI 241
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFA----LPPTIGRAQRRARVEQALEEAGLAGFAD--------RDPatlSGGQRARVALLRAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1281000366 242 IHDPILLFLDEPTSGLDST-----SAFmvvkVLQRIAQSGSIVI 280
Cdd:COG4136 149 LAEPRALLLDEPFSKLDAAlraqfREF----VFEQIRQRGIPAL 188
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
105-314 |
1.96e-25 |
|
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: 108.65 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 105 DISGEAREGEIMAVLGASGSGKSTLIDALA--DRIAkeklKGTVTLNDEVLESALLKV--------IsAYVMQDDLLFPM 174
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAglERPD----SGRIRLGGEVLQDSARGIflpphrrrI-GYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 175 LTVEETLMFAAEfRLPRSLSkskkKARVQALIDQLGLttaantvigdeGH---RGV---SGGERRRVSIGIDIIHDPILL 248
Cdd:COG4148 92 LSVRGNLLYGRK-RAPRAER----RISFDEVVELLGI-----------GHlldRRPatlSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1281000366 249 FLDEPTSGLDSTSAFMVVKVLQRIAQSGSI-VITSIHQPSyRILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:COG4148 156 LMDEPLAALDLARKAEILPYLERLRDELDIpILYVSHSLD-EVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
112-309 |
2.20e-25 |
|
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: 104.68 E-value: 2.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 112 EGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVLESALLKVIS-------AYVMQDDLLFPMLTVEETLMFA 184
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDG--GTIVLNGTVLFDSRKKINLppqqrkiGLVFQQYALFPHLNVRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 185 AefrlpRSLSKSKKKARVQALIDQLGLTTaantvIGDEGHRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFM 264
Cdd:cd03297 100 L-----KRKRNREDRISVDELLDLLGLDH-----LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1281000366 265 VVKVLQRIAQSGSI-VITSIHQPSyRILSLLDRLIFLSRGQTVYSG 309
Cdd:cd03297 170 LLPELKQIKKNLNIpVIFVTHDLS-EAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
88-309 |
2.23e-25 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 104.54 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGRVkllLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLNDEVLESALLKVisAYVMQ 167
Cdd:cd03235 3 EDLTVSYGGHPV---LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLL--KPTSGSIRVFGKPLEKERKRI--GYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 168 D---DLLFPmLTVEETLM--FAAEFRLPRSLSKsKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDII 242
Cdd:cd03235 76 RrsiDRDFP-ISVRDVVLmgLYGHKGLFRRLSK-ADKAKVDEALERVGLSELADRQIGE-----LSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1281000366 243 HDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSyRILSLLDRLIFLSRGqTVYSG 309
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLG-LVLEYFDRVLLLNRT-VVASG 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
103-321 |
3.31e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 104.79 E-value: 3.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTL---IDALADRIAKEKLKGTVTLNDEVLESALLKVISAYVMQDDLLFPMLTVEE 179
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLlrcINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGMVFQQFYLFPHLTALE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 180 TLMFAAefRLPRSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDS 259
Cdd:PRK09493 97 NVMFGP--LRVRGASKEEAEKQARELLAKVGLAERAHHYPSE-----LSGGQQQRVAIARALAVKPKLMLFDEPTSALDP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1281000366 260 TSAFMVVKVLQRIAQSGSIVITSIHQPSY--RILSlldRLIFLSRGQTVYSGSPAEL-----SEFLADF 321
Cdd:PRK09493 170 ELRHEVLKVMQDLAEEGMTMVIVTHEIGFaeKVAS---RLIFIDKGRIAEDGDPQVLiknppSQRLQEF 235
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
88-314 |
3.63e-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: 104.37 E-value: 3.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGRVkllLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKLKGTVTLNDEVLESALLKVISAYVMQ 167
Cdd:cd03265 4 ENLVKKYGDFEA---VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 168 DDLLFPMLTVEETL-MFAAEFRLPRSlsksKKKARVQALIDQLGLTTAANTVIgdeghRGVSGGERRRVSIGIDIIHDPI 246
Cdd:cd03265 81 DLSVDDELTGWENLyIHARLYGVPGA----ERRERIDELLDFVGLLEAADRLV-----KTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 247 LLFLDEPTSGLDSTSAFMVVKVLQRI--AQSGSIVITSIHQPSYRILSllDRLIFLSRGQTVYSGSPAEL 314
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLkeEFGMTILLTTHYMEEAEQLC--DRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
103-284 |
5.28e-25 |
|
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: 103.64 E-value: 5.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLNDEVLES------ALLKVISAYVMQDDLLFPMLT 176
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEE--LPTSGTIRVNGQDVSDlrgraiPYLRRKIGVVFQDFRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 177 VEETLMFAAE--FRLPRSLSKskkkaRVQALIDQLGLTTAANTVigdegHRGVSGGERRRVSIGIDIIHDPILLFLDEPT 254
Cdd:cd03292 95 VYENVAFALEvtGVPPREIRK-----RVPAALELVGLSHKHRAL-----PAELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190
....*....|....*....|....*....|
gi 1281000366 255 SGLDSTSAFMVVKVLQRIAQSGSIVITSIH 284
Cdd:cd03292 165 GNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
88-314 |
5.55e-25 |
|
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: 103.80 E-value: 5.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGRVkllLNDISGEAREGEIMAVLGASGSGKSTLIDALA---DRIAKEKLKGTVTLNDEVLESALLKVIS-- 162
Cdd:cd03260 4 RDLNVYYGDKHA---LKDISLDIPKGEITALIGPSGCGKSTLLRLLNrlnDLIPGAPDEGEVLLDGKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 163 ---AYVMQDDLLFPMlTVEETLMFAAefRLPRSLSKSKKKARVQALIDQLGLTTAANtvigDEGH-RGVSGGERRRVSIG 238
Cdd:cd03260 81 rrvGMVFQKPNPFPG-SIYDNVAYGL--RLHGIKLKEELDERVEEALRKAALWDEVK----DRLHaLGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1281000366 239 IDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITS--IHQpsyrILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVThnMQQ----AARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
100-304 |
6.27e-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: 101.55 E-value: 6.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLNDEVLESALLKVISAYVmqddllfpmltvee 179
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLL--KPTSGEILIDGKDIAKLPLEELRRRI-------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 180 tlmfaaefrlprslskskkkarvqALIDQLglttaantvigdeghrgvSGGERRRVSIGIDIIHDPILLFLDEPTSGLDS 259
Cdd:cd00267 76 ------------------------GYVPQL------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1281000366 260 TSAFMVVKVLQRIAQSGSIVITSIHQPSYrILSLLDRLIFLSRGQ 304
Cdd:cd00267 114 ASRERLLELLRELAEEGRTVIIVTHDPEL-AELAADRVIVLKDGK 157
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
103-321 |
1.09e-24 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 106.34 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALA--DRIAkeklKGTVTLNDevlesallKVISA---------YVMQDDLL 171
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAgfETPD----SGRILLDG--------RDVTGlppekrnvgMVFQDYAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 172 FPMLTVEETLMFAAEFrlpRSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLD 251
Cdd:COG3842 89 FPHLTVAENVAFGLRM---RGVPKAEIRARVAELLELVGLEGLADRYPHQ-----LSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 252 EPTSGLDstsAFM------VVKVLQRiaQSGsivITSI---HQPSyRILSLLDRLIFLSRGQTVYSGSPAEL-----SEF 317
Cdd:COG3842 161 EPLSALD---AKLreemreELRRLQR--ELG---ITFIyvtHDQE-EALALADRIAVMNDGRIEQVGTPEEIyerpaTRF 231
|
....
gi 1281000366 318 LADF 321
Cdd:COG3842 232 VADF 235
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
88-309 |
3.94e-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: 99.82 E-value: 3.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEeNGGRVklLLNDISGEAREGEIMAVLGASGSGKSTLIDALAdRIAKEKlKGTVTLNDEVLESALLKVIS---AY 164
Cdd:cd03214 3 ENLSVG-YGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLA-GLLKPS-SGEILLDGKDLASLSPKELArkiAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 165 VMQddllfpmltveetlmfaaefrlprslskskkkarvqaLIDQLGLTtaantvigDEGHRGV---SGGERRRVSIGIDI 241
Cdd:cd03214 78 VPQ-------------------------------------ALELLGLA--------HLADRPFnelSGGERQRVLLARAL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1281000366 242 IHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQS-GSIVITSIHQPSyRILSLLDRLIFLSRGQTVYSG 309
Cdd:cd03214 113 AQEPPILLLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLN-LAARYADRVILLKDGRIVAQG 180
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
96-324 |
4.00e-24 |
|
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: 101.80 E-value: 4.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 96 GGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALAdRIAKEKlKGTVTLNDEVLESALLKVISA---YVMQDDL-- 170
Cdd:COG1124 14 GGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALA-GLERPW-SGEVTFDGRPVTRRRRKAFRRrvqMVFQDPYas 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 171 LFPMLTVEETLmfaAEfrlP-RSLSKSKKKARVQALIDQLGLttaantvigDEGHRG-----VSGGERRRVSIGIDIIHD 244
Cdd:COG1124 92 LHPRHTVDRIL---AE---PlRIHGLPDREERIAELLEQVGL---------PPSFLDryphqLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 245 PILLFLDEPTSGLDSTSAFMVVKVLQRIAQS---GSIVITsiHQPSYrILSLLDRLIFLSRGQTVysgSPAELSEFLADF 321
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDLREErglTYLFVS--HDLAV-VAHLCDRVAVMQNGRIV---EELTVADLLAGP 230
|
...
gi 1281000366 322 GHP 324
Cdd:COG1124 231 KHP 233
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
88-306 |
4.19e-24 |
|
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: 100.79 E-value: 4.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGRvkLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIaKEKlKGTVTLNDEVLESALLKVISAYVMQ 167
Cdd:cd03226 3 ENISFSYKKGT--EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLI-KES-SGSILLNGKPIKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 168 D--DLLFpMLTVEETLMFAAEfrlprslSKSKKKARVQALIDQLGLTTAAntvigdEGH-RGVSGGERRRVSIGIDIIHD 244
Cdd:cd03226 79 DvdYQLF-TDSVREELLLGLK-------ELDAGNEQAETVLKDLDLYALK------ERHpLSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1281000366 245 PILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYrILSLLDRLIFLSRGQTV 306
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEF-LAKVCDRVLLLANGAIV 205
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
103-317 |
1.12e-23 |
|
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.
Pssm-ID: 132561 [Multi-domain] Cd Length: 301 Bit Score: 102.16 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDE-VLESAL-LKVISAYVMQDDLLFPMLTVEET 180
Cdd:TIGR03522 18 LDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDS--GSVQVCGEdVLQNPKeVQRNIGYLPEHNPLYLDMYVREY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 181 LMFAAEFRlprSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDST 260
Cdd:TIGR03522 96 LQFIAGIY---GMKGQLLKQRVEEMIELVGLRPEQHKKIGQ-----LSKGYRQRVGLAQALIHDPKVLILDEPTTGLDPN 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1281000366 261 SAFMVVKVLQRIAQSGSIVI-TSIHQpsyRILSLLDRLIFLSRGQTVYSGSPAELSEF 317
Cdd:TIGR03522 168 QLVEIRNVIKNIGKDKTIILsTHIMQ---EVEAICDRVIIINKGKIVADKKLDELSAA 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
100-304 |
1.14e-23 |
|
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: 98.41 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALA--DRIAKeklkGTVTLNDEVL-----ESALLKVISAYVMQDDLLF 172
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAglEEPDS----GSILIDGEDLtdledELPPLRRRIGMVFQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 173 PMLTVEETLMFaaefrlprslskskkkarvqalidqlglttaantvigdeghrGVSGGERRRVSIGIDIIHDPILLFLDE 252
Cdd:cd03229 89 PHLTVLENIAL------------------------------------------GLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1281000366 253 PTSGLDSTSAFMVVKVLQRI-AQSGSIVITSIHQPSYrILSLLDRLIFLSRGQ 304
Cdd:cd03229 127 PTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDE-AARLADRVVVLRDGK 178
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
96-325 |
1.44e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 100.58 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 96 GGRVklLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVLESALLKVISAY--VM-QD-DLL 171
Cdd:COG4559 12 GGRT--LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSS--GEVRLNGRPLAAWSPWELARRraVLpQHsSLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 172 FPmLTVEETLMFAaefRLPRSLSKSKKKARVQALIDQLGLTTAAntvigdegHR---GVSGGERRRVS-------IGIDI 241
Cdd:COG4559 88 FP-FTVEEVVALG---RAPHGSSAAQDRQIVREALALVGLAHLA--------GRsyqTLSGGEQQRVQlarvlaqLWEPV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 242 IHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQpsyriLSLL----DRLIFLSRGQTVYSGSPAEL--S 315
Cdd:COG4559 156 DGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHD-----LNLAaqyaDRILLLHQGRLVAQGTPEEVltD 230
|
250
....*....|.
gi 1281000366 316 EFLAD-FGHPI 325
Cdd:COG4559 231 ELLERvYGADL 241
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
103-314 |
2.27e-23 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 99.29 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIdALADRI--AKEklkGTVTLNDEVLESALLKVIS--AYVMQDDLLFPMLTVE 178
Cdd:TIGR03864 17 LDDVSFTVRPGRFVALLGPNGAGKSTLF-SLLTRLyvAQS---GQISVAGHDLRRAPRAALArlGVVFQQPTLDLDLSVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 179 ETLMF-AAEFRLPRSLSKskkkARVQALIDQLGLTTAAntvigDEGHRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGL 257
Cdd:TIGR03864 93 QNLRYhAALHGLSRAEAR----ARIAELLARLGLAERA-----DDKVRELNGGHRRRVEIARALLHRPALLLLDEPTVGL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1281000366 258 DSTSAFMVVKVLQRIAQSGSI-VITSIH-----QPSyrilsllDRLIFLSRGQTVYSGSPAEL 314
Cdd:TIGR03864 164 DPASRAAITAHVRALARDQGLsVLWATHlvdeiEAS-------DRLVVLHRGRVLADGAAAEL 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
103-306 |
2.85e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 98.59 E-value: 2.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALAdriAKEKL-KGTVTLNDEVLESALLKVISAY------VMQDDLLFPML 175
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLY---GEERPtSGQVLVNGQDLSRLKRREIPYLrrrigvVFQDFRLLPDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 176 TVEETLMFAAEFrlpRSLSKSKKKARVQALIDQLGLTTAANTVIgDEghrgVSGGERRRVSIGIDIIHDPILLFLDEPTS 255
Cdd:COG2884 95 TVYENVALPLRV---TGKSRKEIRRRVREVLDLVGLSDKAKALP-HE----LSGGEQQRVAIARALVNRPELLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1281000366 256 GLDSTSAFMVVKVLQRIAQSGSIVITSIHQpsyriLSLLD----RLIFLSRGQTV 306
Cdd:COG2884 167 NLDPETSWEIMELLEEINRRGTTVLIATHD-----LELVDrmpkRVLELEDGRLV 216
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
105-314 |
8.57e-23 |
|
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: 100.57 E-value: 8.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 105 DISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVLESALLKVIS-------AYVMQDDLLFPMLTV 177
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDE--GEIVLNGRTLFDSRKGIFLppekrriGYVFQEARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 178 EETLMFAAEFRLPrslskSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLDEPTSGL 257
Cdd:TIGR02142 93 RGNLRYGMKRARP-----SERRISFERVIELLGIGHLLGRLPGR-----LSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1281000366 258 DSTSAFMVVKVLQRIAQSGSIVITSI-HQPSyRILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:TIGR02142 163 DDPRKYEILPYLERLHAEFGIPILYVsHSLQ-EVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
102-321 |
9.45e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 100.22 E-value: 9.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 102 LLNDISGEAREGEIMAVLGASGSGKSTLIDALA-----DRiakeklkGTVTLNDEVLESAL----LKVisAYVMQDDLLF 172
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAgletpDS-------GRIVLNGRDLFTNLppreRRV--GFVFQHYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 173 PMLTVEETLMFAAEFRLPrslSKSKKKARVQALIDQLGLTtaantvigDEGHR---GVSGGERRRVSIGIDIIHDPILLF 249
Cdd:COG1118 88 PHMTVAENIAFGLRVRPP---SKAEIRARVEELLELVQLE--------GLADRypsQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 250 LDEPTSGLDSTsafmVVKVLQRiaqsgsiVITSIHQpSYRILSLL------------DRLIFLSRGQTVYSGSPAEL--- 314
Cdd:COG1118 157 LDEPFGALDAK----VRKELRR-------WLRRLHD-ELGGTTVFvthdqeealelaDRVVVMNQGRIEQVGTPDEVydr 224
|
....*....
gi 1281000366 315 --SEFLADF 321
Cdd:COG1118 225 paTPFVARF 233
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
100-314 |
2.25e-22 |
|
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: 96.46 E-value: 2.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDE------VLESALLKVIsaYVMQDDLLFP 173
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDS--GKILLDGQditklpMHKRARLGIG--YLPQEASIFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 174 MLTVEETLMFAAEFRlprSLSKSKKKARVQALIDQLGLTTAANTVIGdeghrGVSGGERRRVSIGIDIIHDPILLFLDEP 253
Cdd:cd03218 89 KLTVEENILAVLEIR---GLSKKEREEKLEELLEEFHITHLRKSKAS-----SLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1281000366 254 TSGLDSTSAFMVVKVLQRIAQSG-SIVITSiHQPSyRILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGiGVLITD-HNVR-ETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
88-309 |
2.33e-22 |
|
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: 95.90 E-value: 2.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLT-AEENGGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKLKGTVTLNDEVLESALLKVISAYVM 166
Cdd:cd03266 5 DALTkRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 167 QDDLLFPMLTVEETLMFAAEFRlprSLSKSKKKARVQALIDQLGLTTAANTVIGdeghrGVSGGERRRVSIGIDIIHDPI 246
Cdd:cd03266 85 DSTGLYDRLTARENLEYFAGLY---GLKGDELTARLEELADRLGMEELLDRRVG-----GFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1281000366 247 LLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSyRILSLLDRLIFLSRGQTVYSG 309
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQ-EVERLCDRVVVLHRGRVVYEG 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
68-325 |
2.39e-22 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 96.69 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 68 LSFQNlsysVKVRRRGsslpenltaeenggrvKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAK-------- 139
Cdd:COG1119 4 LELRN----VTVRRGG----------------KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtygndvrl 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 140 --EKLkGTVTLNDevlesalLK----VISAyVMQDDLLfPMLTVEETLM--FAAEFRLPRSLSKsKKKARVQALIDQLGL 211
Cdd:COG1119 64 fgERR-GGEDVWE-------LRkrigLVSP-ALQLRFP-RDETVLDVVLsgFFDSIGLYREPTD-EQRERARELLELLGL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 212 TTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGS---IVITsiHQPSY 288
Cdd:COG1119 133 AHLADRPFGT-----LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAptlVLVT--HHVEE 205
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1281000366 289 rILSLLDRLIFLSRGQTVYSGSPAEL--SEFLAD-FGHPI 325
Cdd:COG1119 206 -IPPGITHVLLLKDGRVVAAGPKEEVltSENLSEaFGLPV 244
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
103-321 |
3.43e-22 |
|
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: 95.87 E-value: 3.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDE-VLESALLKVISAYVMQDDLLFPMLTVEETL 181
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDS--GKILLNGKdITNLPPEKRDISYVPQNYALFPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 182 MFAAEFRLprsLSKSKKKARVQALIDQLGLTTaantvIGDEGHRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTS 261
Cdd:cd03299 93 AYGLKKRK---VDKKEIERKVLEIAEMLGIDH-----LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281000366 262 AFMVVKVLQRIAQSGSIVITSIHQPSYRILSLLDRLIFLSRGQTVYSGSPAEL-----SEFLADF 321
Cdd:cd03299 165 KEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVfkkpkNEFVAEF 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
101-314 |
4.06e-22 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 96.02 E-value: 4.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 101 LLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKLKGTVTLND-EVLESALLKVISAYVMQDDLLFPMlTVEE 179
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlALADPAWLRRQVGVVLQENVLFNR-SIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 180 TLMFAAEFRLPRSLSKSKKKARVQALIDQLGLttAANTVIGDEGhRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDS 259
Cdd:cd03252 95 NIALADPGMSMERVIEAAKLAGAHDFISELPE--GYDTIVGEQG-AGLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1281000366 260 TSAFMVVKVLQRIAqSGSIVITSIHQPSyrILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:cd03252 172 ESEHAIMRNMHDIC-AGRTVIIIAHRLS--TVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
96-304 |
9.38e-22 |
|
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: 92.83 E-value: 9.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 96 GGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALAdriakeKL----KGTVTLNDEVLE----SALLKVIsAYVMQ 167
Cdd:cd03228 11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLL------RLydptSGEILIDGVDLRdldlESLRKNI-AYVPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 168 DDLLFPMlTVEETLMfaaefrlprslskskkkarvqalidqlglttaantvigdeghrgvSGGERRRVSIGIDIIHDPIL 247
Cdd:cd03228 84 DPFLFSG-TIRENIL---------------------------------------------SGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1281000366 248 LFLDEPTSGLDSTSAFMVVKVLQRIAQ-SGSIVITsiHQPSYriLSLLDRLIFLSRGQ 304
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKgKTVIVIA--HRLST--IRDADRIIVLDDGR 171
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
88-286 |
1.29e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.40 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGgrvKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVLESALLKVISAYVMQ 167
Cdd:PRK13539 6 EDLACVRGG---RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAA--GTIKLDGGDIDDPDVAEACHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 168 DDLLFPMLTVEETLMFAAEFRLPRSLSkskkkarVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIG-IDIIHDPI 246
Cdd:PRK13539 81 RNAMKPALTVAENLEFWAAFLGGEELD-------IAAALEAVGLAPLAHLPFGY-----LSAGQKRRVALArLLVSNRPI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1281000366 247 LLfLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQP 286
Cdd:PRK13539 149 WI-LDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHIP 187
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
103-309 |
2.04e-21 |
|
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: 93.42 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALAD-RIAKEklkGTVTLND----EVLESALLKVISaYVMQDDLLFpMLTV 177
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGlYKPTS---GSVLLDGtdirQLDPADLRRNIG-YVPQDVTLF-YGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 178 EETLMFAAEFRLPRSLSKSKKKARVQALIDQL--GLttaaNTVIGdEGHRGVSGGERRRVSIGIDIIHDPILLFLDEPTS 255
Cdd:cd03245 95 RDNITLGAPLADDERILRAAELAGVTDFVNKHpnGL----DLQIG-ERGRGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1281000366 256 GLDSTSAFMVVKVLQRIAqSGSIVITSIHQPSyrILSLLDRLIFLSRGQTVYSG 309
Cdd:cd03245 170 AMDMNSEERLKERLRQLL-GDKTLIIITHRPS--LLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
100-309 |
2.31e-21 |
|
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: 92.67 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDE--VLESALLKVISAYVmQDDLLFPMLTV 177
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDS--GEITFDGKsyQKNIEALRRIGALI-EAPGFYPNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 178 EETLMFAAefRLPRslsksKKKARVQALIDQLGLttaantviGDEGHRGVSG---GERRRVSIGIDIIHDPILLFLDEPT 254
Cdd:cd03268 90 RENLRLLA--RLLG-----IRKKRIDEVLDVVGL--------KDSAKKKVKGfslGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1281000366 255 SGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSyRILSLLDRLIFLSRGQTVYSG 309
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQGITVLISSHLLS-EIQKVADRIGIINKGKLIEEG 208
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
88-314 |
4.25e-21 |
|
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: 92.68 E-value: 4.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGRvkLLLNDISGEAREGEIMAVLGASGSGKSTLIdaladriakeKL--------KGTVTLND----EVLES 155
Cdd:cd03253 4 ENVTFAYDPGR--PVLKDVSFTIPAGKKVAIVGPSGSGKSTIL----------RLlfrfydvsSGSILIDGqdirEVTLD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 156 ALLKVIsAYVMQDDLLFpmltvEETLMFAAEFRLPRS----LSKSKKKARVQALIdqLGLTTAANTVIGDEGHRgVSGGE 231
Cdd:cd03253 72 SLRRAI-GVVPQDTVLF-----NDTIGYNIRYGRPDAtdeeVIEAAKAAQIHDKI--MRFPDGYDTIVGERGLK-LSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 232 RRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQS-GSIVITsiHQPSYRILSllDRLIFLSRGQTVYSGS 310
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGrTTIVIA--HRLSTIVNA--DKIIVLKDGRIVERGT 218
|
....
gi 1281000366 311 PAEL 314
Cdd:cd03253 219 HEEL 222
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
103-313 |
5.32e-21 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 93.18 E-value: 5.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEklKGTVTLNDEVLESAllkviSAYVM---------QDDLLFP 173
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPT--SGRILFDGRDITGL-----PPHRIarlgiartfQNPRLFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 174 MLTVEETLMFAAEFRLPRSLSKSKKK------------ARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDI 241
Cdd:COG0411 93 ELTVLENVLVAAHARLGRGLLAALLRlprarreerearERAEELLERVGLADRADEPAGN-----LSYGQQRRLEIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1281000366 242 IHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSG--SIVIT----SIhqpsyrILSLLDRLIFLSRGQTVYSGSPAE 313
Cdd:COG0411 168 ATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILLIehdmDL------VMGLADRIVVLDFGRVIAEGTPAE 239
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
103-316 |
7.13e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 92.40 E-value: 7.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKST-------LIDAlaDriakeklKGTVTLNDEVL------ESALLKVisAYVMQDD 169
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTtfymivgLVKP--D-------SGRIFLDGEDIthlpmhKRARLGI--GYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 170 LLFPMLTVEETLMFAAEFRlprSLSKSKKKARVQALIDQLGLTTAANTvigdeghRG--VSGGERRRVSIGIDIIHDPIL 247
Cdd:COG1137 88 SIFRKLTVEDNILAVLELR---KLSKKEREERLEELLEEFGITHLRKS-------KAysLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281000366 248 LFLDEPTSGLDSTSafmvVKVLQRI----AQSG-SIVITSiHqpSYR-ILSLLDRLIFLSRGQTVYSGSPAELSE 316
Cdd:COG1137 158 ILLDEPFAGVDPIA----VADIQKIirhlKERGiGVLITD-H--NVReTLGICDRAYIISEGKVLAEGTPEEILN 225
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
88-320 |
9.76e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 91.88 E-value: 9.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGRVkllLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDE-----VLESALLKVIs 162
Cdd:PRK10895 7 KNLAKAYKGRRV---VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA--GNIIIDDEdisllPLHARARRGI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 163 AYVMQDDLLFPMLTVEETLMFAAEFRlpRSLSKSKKKARVQALIDQLGLTTAANTVigdegHRGVSGGERRRVSIGIDII 242
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIR--DDLSAEQREDRANELMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1281000366 243 HDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSyRILSLLDRLIFLSRGQTVYSGSPAELsefLAD 320
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVR-ETLAVCERAYIVSQGHLIAHGTPTEI---LQD 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
88-300 |
1.30e-20 |
|
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: 96.20 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGRVklLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLNDEVL----ESALLKVIsA 163
Cdd:TIGR02857 325 SGVSVAYPGRRP--ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFV--DPTEGSIAVNGVPLadadADSWRDQI-A 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 164 YVMQDDLLFPMlTVEETLMFAAEFRLPRSLSKSKKKARVQALIDQLGLTTaaNTVIGDEGhRGVSGGERRRVSIGIDIIH 243
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRLARPDASDAEIREALERAGLDEFVAALPQGL--DTPIGEGG-AGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1281000366 244 DPILLFLDEPTSGLDSTSAFMVVKVLQRIAQsGSIVITSIHQPSyrILSLLDRLIFL 300
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLA--LAALADRIVVL 529
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
72-309 |
1.52e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 91.24 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 72 NLSYSVKVRRRGSSLPENLTAEENGG-RVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLND 150
Cdd:cd03267 5 NLSKSYRVYSKEPGLIGSLKSLFKRKyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTS--GEVRVAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 151 EV---LESALLKVISAYVMQDDLLFPMLTVEETL-MFAAEFRLPrslsKSKKKARVQALIDQLGLTTAANTVIgdeghRG 226
Cdd:cd03267 83 LVpwkRRKKFLRRIGVVFGQKTQLWWDLPVIDSFyLLAAIYDLP----PARFKKRLDELSELLDLEELLDTPV-----RQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 227 VSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRI-AQSGSIVITSIHQpSYRILSLLDRLIFLSRGQT 305
Cdd:cd03267 154 LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHY-MKDIEALARRVLVIDKGRL 232
|
....
gi 1281000366 306 VYSG 309
Cdd:cd03267 233 LYDG 236
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
88-321 |
1.82e-20 |
|
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: 90.76 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGRVkllLNDISGEAREGEIMAVLGASGSGKSTLIDALAdriAKEKL-KGTVTLNDEVLESallkvISAY-- 164
Cdd:cd03300 4 ENVSKFYGGFVA---LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIA---GFETPtSGEILLDGKDITN-----LPPHkr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 165 ----VMQDDLLFPMLTVEETLMFAaeFRLpRSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGID 240
Cdd:cd03300 73 pvntVFQNYALFPHLTVFENIAFG--LRL-KKLPKAEIKERVAEALDLVQLEGYANRKPSQ-----LSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 241 IIHDPILLFLDEPTSGLDS---TSAFMVVKVLQRiaQSGSIVITSIHQPSyRILSLLDRLIFLSRGQTVYSGSPAELSE- 316
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLklrKDMQLELKRLQK--ELGITFVFVTHDQE-EALTMSDRIAVMNKGKIQQIGTPEEIYEe 221
|
....*....
gi 1281000366 317 ----FLADF 321
Cdd:cd03300 222 panrFVADF 230
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
103-286 |
2.04e-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: 95.51 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADriAKEKLKGTVTLND----EVLESALLKVISaYVMQDDLLFPMlTVE 178
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAG--LLDPLQGEVTLDGvpvsSLDQDEVRRRVS-VCAQDAHLFDT-TVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 179 ETLMFAAEFRLPRSLSKSKKKARVQALIDqlGLTTAANTVIGDEGHRgVSGGERRRVSIGIDIIHDPILLFLDEPTSGLD 258
Cdd:TIGR02868 427 ENLRLARPDATDEELWAALERVGLADWLR--ALPDGLDTVLGEGGAR-LSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
170 180
....*....|....*....|....*...
gi 1281000366 259 STSAFMVVKVLqRIAQSGSIVITSIHQP 286
Cdd:TIGR02868 504 AETADELLEDL-LAALSGRTVVLITHHL 530
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
100-314 |
3.00e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 95.23 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALAdriakeKL----KGTVTLND----EVLESALLKVIsAYVMQDDLL 171
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLL------RFydptSGRILIDGvdirDLTLESLRRQI-GVVPQDTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 172 FPMlTV------------EETLMFAAefrlprslskskKKARVQALIDQL--GLttaaNTVIGDEGHRgVSGGERRRVSI 237
Cdd:COG1132 426 FSG-TIrenirygrpdatDEEVEEAA------------KAAQAHEFIEALpdGY----DTVVGERGVN-LSGGQRQRIAI 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 238 GIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSG-SIVITsiHqpsyRiLSLL---DRLIFLSRGQTVYSGSPAE 313
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERLMKGRtTIVIA--H----R-LSTIrnaDRILVLDDGRIVEQGTHEE 560
|
.
gi 1281000366 314 L 314
Cdd:COG1132 561 L 561
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
90-306 |
3.35e-20 |
|
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: 90.19 E-value: 3.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 90 LTAEENGGRVKLLlNDISGEAREGEIMAVLGASGSGKSTLIDALA--DRIAkeklKGTVTLNDEVL----ESALLKVISA 163
Cdd:COG4181 16 KTVGTGAGELTIL-KGISLEVEAGESVAIVGASGSGKSTLLGLLAglDRPT----SGTVRLAGQDLfaldEDARARLRAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 164 ---YVMQDDLLFPMLTVEETLMFAAEFRlprslSKSKKKARVQALIDQLGLttaantvigdeGHR------GVSGGERRR 234
Cdd:COG4181 91 hvgFVFQSFQLLPTLTALENVMLPLELA-----GRRDARARARALLERVGL-----------GHRldhypaQLSGGEQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281000366 235 VSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRI-AQSGS--IVITsiHQPsyRILSLLDRLIFLSRGQTV 306
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTtlVLVT--HDP--ALAARCDRVLRLRAGRLV 225
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
100-314 |
4.94e-20 |
|
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: 90.03 E-value: 4.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVL------ESALLKVisAYVMQDDLLFP 173
Cdd:TIGR04406 14 RKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDA--GKILIDGQDIthlpmhERARLGI--GYLPQEASIFR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 174 MLTVEETLMFAAEFRlpRSLSKSKKKARVQALIDQLGLTTaantvIGDEGHRGVSGGERRRVSIGIDIIHDPILLFLDEP 253
Cdd:TIGR04406 90 KLTVEENIMAVLEIR--KDLDRAEREERLEALLEEFQISH-----LRDNKAMSLSGGERRRVEIARALATNPKFILLDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1281000366 254 TSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSyRILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:TIGR04406 163 FAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVR-ETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
96-314 |
6.28e-20 |
|
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: 89.21 E-value: 6.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 96 GGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDAL-------ADRIakeKLKGT----VTLNDevlesalLKVISAY 164
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvdSGRI---LIDGHdvrdYTLAS-------LRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 165 VMQDDLLFPMlTVEETLMFAAEFRLPRSLSKSKKKARVQALIDQL--GLttaaNTVIGDeghRGV--SGGERRRVSIGID 240
Cdd:cd03251 81 VSQDVFLFND-TVAENIAYGRPGATREEVEEAARAANAHEFIMELpeGY----DTVIGE---RGVklSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1281000366 241 IIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQS-GSIVITsiHQpsyriLSLL---DRLIFLSRGQTVYSGSPAEL 314
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERLMKNrTTFVIA--HR-----LSTIenaDRIVVLEDGKIVERGTHEEL 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
102-324 |
7.47e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 89.64 E-value: 7.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 102 LLNDISGEAREGEIMAVLGASGSGKSTLIDALadRIAKEKLKGTVTLNDEVL----------------ESALLKVISAYV 165
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCI--NFLEKPSEGSIVVNGQTInlvrdkdgqlkvadknQLRLLRTRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 166 MQDDLLFPMLTVEETLMFAAEFRLprSLSKSKKKARVQALIDQLGLTTAANtvigDEGHRGVSGGERRRVSIGIDIIHDP 245
Cdd:PRK10619 98 FQHFNLWSHMTVLENVMEAPIQVL--GLSKQEARERAVKYLAKVGIDERAQ----GKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 246 ILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSY-RILSllDRLIFLSRGQTVYSGSPAELsefladFGHP 324
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFaRHVS--SHVIFLHQGKIEEEGAPEQL------FGNP 243
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
100-344 |
8.88e-20 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 89.80 E-value: 8.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTL---IDAL----ADRIakeKLKGTVTLNDEVLESALLKVisAYVMQD-DLL 171
Cdd:TIGR04520 15 KPALKNVSLSIEKGEFVAIIGHNGSGKSTLaklLNGLllptSGKV---TVDGLDTLDEENLWEIRKKV--GMVFQNpDNQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 172 FPMLTVEETLMFAAE-FRLPRslskSKKKARVQALIDQLGLTTAANTvigdEGHRgVSGGERRRVSI-GIdIIHDPILLF 249
Cdd:TIGR04520 90 FVGATVEDDVAFGLEnLGVPR----EEMRKRVDEALKLVGMEDFRDR----EPHL-LSGGQKQRVAIaGV-LAMRPDIII 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 250 LDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSI-HQPSYRILSllDRLIFLSRGQTVYSGSPAEL---SEFLADFGHPI 325
Cdd:TIGR04520 160 LDEATSMLDPKGRKEVLETIRKLNKEEGITVISItHDMEEAVLA--DRVIVMNKGKIVAEGTPREIfsqVELLKEIGLDV 237
|
250
....*....|....*....
gi 1281000366 326 PenenrteFALDLVRDLEE 344
Cdd:TIGR04520 238 P-------FITELAKALKK 249
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
88-313 |
1.30e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.92 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAeenGGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALAdRIAKEKLkGTVTLNDEVLESALLKVISAYV-- 165
Cdd:PRK11231 6 ENLTV---GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA-RLLTPQS-GTVFLGDKPISMLSSRQLARRLal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 166 MQDDLLFPM-LTVEETLMFAaefrlpRS--------LSkSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVS 236
Cdd:PRK11231 81 LPQHHLTPEgITVRELVAYG------RSpwlslwgrLS-AEDNARVNQAMEQTRINHLADRRLTD-----LSGGQRQRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 237 IGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIH---QPS-YrilslLDRLIFLSRGQTVYSGSPA 312
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHdlnQASrY-----CDHLVVLANGHVMAQGTPE 223
|
.
gi 1281000366 313 E 313
Cdd:PRK11231 224 E 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
68-313 |
1.32e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.06 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 68 LSFQNLSYsvkvrRRGSslpenltaeenggrvKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEklKGTVT 147
Cdd:PRK13548 3 LEARNLSV-----RLGG---------------RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD--SGEVR 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 148 LNDEVLES---ALLKVISAyVM--QDDLLFPmLTVEETLMFAaefRLPRSLSKSKKKARVQALIDQLGLTTAAntvigDE 222
Cdd:PRK13548 61 LNGRPLADwspAELARRRA-VLpqHSSLSFP-FTVEEVVAMG---RAPHGLSRAEDDALVAAALAQVDLAHLA-----GR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 223 GHRGVSGGERRRV----------SIGidiiHDPILLFLDEPTSGLDSTSAFMVVKVLQRIA-QSGSIVITSIHQpsyriL 291
Cdd:PRK13548 131 DYPQLSGGEQQRVqlarvlaqlwEPD----GPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHD-----L 201
|
250 260
....*....|....*....|....*.
gi 1281000366 292 SLL----DRLIFLSRGQTVYSGSPAE 313
Cdd:PRK13548 202 NLAaryaDRIVLLHQGRLVADGTPAE 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
96-260 |
2.24e-19 |
|
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: 89.73 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 96 GGRVKLLlNDISGEAREGEIMAVLGASGSGKSTLIDALAdRIAKEKLK--GTVTLNDEVL----ESALLKV----IsAYV 165
Cdd:COG0444 15 RGVVKAV-DGVSFDVRRGETLGLVGESGSGKSTLARAIL-GLLPPPGItsGEILFDGEDLlklsEKELRKIrgreI-QMI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 166 MQDDL--LFPMLTVEETLMFAaeFRLPRSLSKSKKKARVQALIDQLGLTTAANtVIGDEGHRgVSGGERRRVSIGIDIIH 243
Cdd:COG0444 92 FQDPMtsLNPVMTVGDQIAEP--LRIHGGLSKAEARERAIELLERVGLPDPER-RLDRYPHE-LSGGMRQRVMIARALAL 167
|
170
....*....|....*..
gi 1281000366 244 DPILLFLDEPTSGLDST 260
Cdd:COG0444 168 EPKLLIADEPTTALDVT 184
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
113-309 |
2.62e-19 |
|
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: 87.16 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 113 GEIMAVLGASGSGKSTLIDALADRIAKEklKGTVTLNDE---VLESALLKVisAYVMQDDLLFPMLTVEETLMFAaefRL 189
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQ--SGRVLINGVdvtAAPPADRPV--SMLFQENNLFAHLTVEQNVGLG---LS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 190 PRSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHD-PILLfLDEPTSGLD-STSAFMVVK 267
Cdd:cd03298 97 PGLKLTAEDRQAIEVALARVGLAGLEKRLPGE-----LSGGERQRVALARVLVRDkPVLL-LDEPFAALDpALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1281000366 268 VLQRIAQSGSIVITSIHQPSyRILSLLDRLIFLSRGQTVYSG 309
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPE-DAKRLAQRVVFLDNGRIAAQG 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
94-281 |
1.01e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 86.45 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 94 ENGGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVLE--SALLKVisayVMQDDLL 171
Cdd:COG4525 14 PGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSS--GEITLDGVPVTgpGADRGV----VFQKDAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 172 FPMLTVEETLMFAaeFRLpRSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLD 251
Cdd:COG4525 88 LPWLNVLDNVAFG--LRL-RGVPKAERRARAEELLALVGLADFARRRIWQ-----LSGGMRQRVGIARALAADPRFLLMD 159
|
170 180 190
....*....|....*....|....*....|...
gi 1281000366 252 EPTSGLDS-TSAFMVVKVLQRIAQSGSIV--IT 281
Cdd:COG4525 160 EPFGALDAlTREQMQELLLDVWQRTGKGVflIT 192
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
103-333 |
1.11e-18 |
|
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: 85.60 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADrIAKEKLKGTVTLNDEVLESALLKVIsayVMQDDLLFPMLTVEETLM 182
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISG-LAQPTSGGVILEGKQITEPGPDRMV---VFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 183 FAAEfRLPRSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSA 262
Cdd:TIGR01184 77 LAVD-RVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ-----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1281000366 263 FMVVKVLQRIAQSGSIVITSIHQPSYRILSLLDRLIFLSRGQTVYSGSPAELsefladfghPIPENENRTE 333
Cdd:TIGR01184 151 GNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV---------PFPRPRDRLE 212
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
103-316 |
1.67e-18 |
|
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: 85.47 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADriAKEKLKGTVTLNDE-VLESALLKVISAYVMQDDLLFPMLTVEETL 181
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAG--LERPDSGTILFGGEdATDVPVQERNVGFVFQHYALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 182 MFAAEFRlPRSL--SKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDS 259
Cdd:cd03296 96 AFGLRVK-PRSErpPEAEIRAKVHELLKLVQLDWLADRYPAQ-----LSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1281000366 260 TsafmVVKVLQRIAQS--GSIVITSI---HQPSyRILSLLDRLIFLSRGQTVYSGSPAELSE 316
Cdd:cd03296 170 K----VRKELRRWLRRlhDELHVTTVfvtHDQE-EALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
103-314 |
1.97e-18 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 85.28 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIdALADRIAkEKLKGTVTLNDEVLES----ALLKVIsAYVMQDDLLFPMlTVE 178
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVV-SLLERFY-DPTSGEILLDGVDIRDlnlrWLRSQI-GLVSQEPVLFDG-TIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 179 ETLMFAAEfrlPRSLSKSKKKARvQALIDQL--GLTTAANTVIGDEGHRgVSGGERRRVSIGIDIIHDPILLFLDEPTSG 256
Cdd:cd03249 95 ENIRYGKP---DATDEEVEEAAK-KANIHDFimSLPDGYDTLVGERGSQ-LSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1281000366 257 LDSTSAFMVVKVLQRIAQsGSIVITSIHQpsyriLSLL---DRLIFLSRGQTVYSGSPAEL 314
Cdd:cd03249 170 LDAESEKLVQEALDRAMK-GRTTIVIAHR-----LSTIrnaDLIAVLQNGQVVEQGTHDEL 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
100-326 |
2.21e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 85.84 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEklKGTVTLNDEVLESALLKVISA---YVMQD-DLLFPML 175
Cdd:PRK13635 20 TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPE--AGTITVGGMVLSEETVWDVRRqvgMVFQNpDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 176 TVEETLMFAAEFR-LPRslskSKKKARVQALIDQLGLTTAANtvigDEGHRgVSGGERRRVSI-GIdIIHDPILLFLDEP 253
Cdd:PRK13635 98 TVQDDVAFGLENIgVPR----EEMVERVDQALRQVGMEDFLN----REPHR-LSGGQKQRVAIaGV-LALQPDIIILDEA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1281000366 254 TSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYRILSlLDRLIFLSRGQTVYSGSPAE---LSEFLADFGHPIP 326
Cdd:PRK13635 168 TSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEifkSGHMLQEIGLDVP 242
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
109-314 |
2.96e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 84.42 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 109 EAREGEIMAVLGASGSGKSTLIDALADRIAKEklKGTVTLNDE---VLESALLKVisAYVMQDDLLFPMLTVEETLMFAa 185
Cdd:COG3840 21 TIAAGERVAILGPSGAGKSTLLNLIAGFLPPD--SGRILWNGQdltALPPAERPV--SMLFQENNLFPHLTVAQNIGLG- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 186 eFRLPRSLSkSKKKARVQALIDQLGLTTaantvIGDEGHRGVSGGERRRVSIGIDIIHD-PILLfLDEPTSGLD-STSAF 263
Cdd:COG3840 96 -LRPGLKLT-AEQRAQVEQALERVGLAG-----LLDRLPGQLSGGQRQRVALARCLVRKrPILL-LDEPFSALDpALRQE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1281000366 264 MVVKVLQRIAQSGSIVITSIHQPSyRILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:COG3840 168 MLDLVDELCRERGLTVLMVTHDPE-DAARIADRVLLVADGRIAADGPTAAL 217
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
94-284 |
3.42e-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: 83.24 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 94 ENGGRVkllLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVLE---SALLKVIS--AYVMQ- 167
Cdd:TIGR01166 2 PGGPEV---LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQS--GAVLIDGEPLDysrKGLLERRQrvGLVFQd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 168 -DDLLFPMlTVEETLMFAaefrlPRSLSKSKkkARVQALIDQlglttaANTVIGDEGHRG-----VSGGERRRVSIGIDI 241
Cdd:TIGR01166 77 pDDQLFAA-DVDQDVAFG-----PLNLGLSE--AEVERRVRE------ALTAVGASGLRErpthcLSGGEKKRVAIAGAV 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1281000366 242 IHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIH 284
Cdd:TIGR01166 143 AMRPDVLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
80-314 |
3.46e-18 |
|
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: 88.62 E-value: 3.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 80 RRRGSSLPENLTAEEnGGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIdALADRIAkEKLKGTVTLNDEVLESALLK 159
Cdd:TIGR02203 326 RARGDVEFRNVTFRY-PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLV-NLIPRFY-EPDSGQILLDGHDLADYTLA 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 160 VIS---AYVMQDDLLFPMlTVEETLMFAAEFRLPRS-LSKSKKKARVQALIDQLGLttAANTVIGDEGHRgVSGGERRRV 235
Cdd:TIGR02203 403 SLRrqvALVSQDVVLFND-TIANNIAYGRTEQADRAeIERALAAAYAQDFVDKLPL--GLDTPIGENGVL-LSGGQRQRL 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 236 SIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQS-GSIVITsiHQpsyriLSLL---DRLIFLSRGQTVYSGSP 311
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAALERLMQGrTTLVIA--HR-----LSTIekaDRIVVMDDGRIVERGTH 551
|
...
gi 1281000366 312 AEL 314
Cdd:TIGR02203 552 NEL 554
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
88-323 |
4.59e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 84.35 E-value: 4.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGgrvKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKLKGTVTLNDEVL------ESALLKVi 161
Cdd:COG0396 4 KNLHVSVEG---KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEVTSGSILLDGEDIlelspdERARAGI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 162 sAYVMQDDLLFPMLTVEETLMFAAEFRLPRSLSKSKKKARVQALIDQLGLttaantvigDEG--HRGV----SGGERRRV 235
Cdd:COG0396 80 -FLAFQYPVEIPGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGL---------DEDflDRYVnegfSGGEKKRN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 236 SIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGS--IVITsiHQPsyRILSLL--DRLIFLSRGQTVYSGSP 311
Cdd:COG0396 150 EILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRgiLIIT--HYQ--RILDYIkpDFVHVLVDGRIVKSGGK 225
|
250
....*....|..
gi 1281000366 312 aELSEFLADFGH 323
Cdd:COG0396 226 -ELALELEEEGY 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
88-314 |
6.31e-18 |
|
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: 83.43 E-value: 6.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGrvKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLND----EVLESALLKVIsA 163
Cdd:cd03254 6 ENVNFSYDEK--KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQK--GQILIDGidirDISRKSLRSMI-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 164 YVMQDDLLFPMlTVEETLMFAAEFRLPRSLSKSKKKARVQALIDQL--GLttaaNTVIGDEGHrGVSGGERRRVSIGIDI 241
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLpnGY----DTVLGENGG-NLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1281000366 242 IHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQS-GSIVITsiHQPSyrILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKLMKGrTSIIIA--HRLS--TIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
103-314 |
1.22e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 84.52 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVLES--------------------ALLKVIS 162
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKY--GTIQVGDIYIGDkknnhelitnpyskkiknfkELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 163 aYVMQddllFPML-----TVEETLMFAaefrlPRSLSKSKKKARVQA--LIDQLGLTTAantvIGDEGHRGVSGGERRRV 235
Cdd:PRK13631 120 -MVFQ----FPEYqlfkdTIEKDIMFG-----PVALGVKKSEAKKLAkfYLNKMGLDDS----YLERSPFGLSGGQKRRV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 236 SI-GIDIIHDPILLFlDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSyRILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:PRK13631 186 AIaGILAIQPEILIF-DEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTME-HVLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
100-316 |
1.28e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.09 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVLES----ALLKVisAYVMQDDLLFPML 175
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDA--GSISLCGEPVPSrarhARQRV--GVVPQFDNLDPDF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 176 TVEETLM-FAAEFrlprSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLDEPT 254
Cdd:PRK13537 96 TVRENLLvFGRYF----GLSAAAARALVPPLLEFAKLENKADAKVGE-----LSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1281000366 255 SGLDSTSAFMVVKVLQRIAQSGSIVITSIH--QPSYRilsLLDRLIFLSRGQTVYSGSPAELSE 316
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLARGKTILLTTHfmEEAER---LCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
96-286 |
1.31e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.51 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 96 GGRVklLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKekLKGTVTlndevlESALLKVisAYVMQ---DDLLF 172
Cdd:NF040873 3 GGRP--VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRP--TSGTVR------RAGGARV--AYVPQrseVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 173 PmLTVEETLMFA--AEFRLPRSLSKSKKKARVQALiDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFL 250
Cdd:NF040873 71 P-LTVRDLVAMGrwARRGLWRRLTRDDRAAVDDAL-ERVGLADLAGRQLGE-----LSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190
....*....|....*....|....*....|....*.
gi 1281000366 251 DEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQP 286
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
94-324 |
1.32e-17 |
|
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: 82.63 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 94 ENGGRVKLLLNDISGEAREGEIMAVLGASGSGKSTL---IDALadriakEK-LKGTVTLNDEVL----ESALLKVIS--A 163
Cdd:cd03258 12 GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLircINGL------ERpTSGSVLVDGTDLtllsGKELRKARRriG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 164 YVMQDDLLFPMLTVEETLMFAAEFRlprSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIH 243
Cdd:cd03258 86 MIFQHFNLLSSRTVFENVALPLEIA---GVPKAEIEERVLELLELVGLEDKADAYPAQ-----LSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 244 DPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSI-HQPSYrILSLLDRLIFLSRGQTVYSGSPAELsefladFG 322
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLItHEMEV-VKRICDRVAVMEKGEVVEEGTVEEV------FA 230
|
..
gi 1281000366 323 HP 324
Cdd:cd03258 231 NP 232
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
103-309 |
1.69e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 82.37 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDAL-----AD----RIAKEKLKGTVTLNDEVLESALLKVisAYVMQDDLLFP 173
Cdd:COG4161 18 LFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletPDsgqlNIAGHQFDFSQKPSEKAIRLLRQKV--GMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 174 MLTVEETLMFAaefrlP-RSLSKSKKKARVQA--LIDQLGLTtaantvigDEGHR---GVSGGERRRVSIGIDIIHDP-I 246
Cdd:COG4161 96 HLTVMENLIEA-----PcKVLGLSKEQAREKAmkLLARLRLT--------DKADRfplHLSGGQQQRVAIARALMMEPqV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1281000366 247 LLFlDEPTSGLDSTSAFMVVKVLQRIAQSG--SIVITsiHQPSY--RILSlldRLIFLSRGQTVYSG 309
Cdd:COG4161 163 LLF-DEPTAALDPEITAQVVEIIRELSQTGitQVIVT--HEVEFarKVAS---QVVYMEKGRIIEQG 223
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
88-321 |
2.24e-17 |
|
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: 82.35 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGRVklLLNDISGEAREGEIMAVLGASGSGKSTLIdALADRIAkEKLKGTVTLND----EVLESALLKVIsA 163
Cdd:cd03295 4 ENVTKRYGGGKK--AVNNLNLEIAKGEFLVLIGPSGSGKTTTM-KMINRLI-EPTSGEIFIDGedirEQDPVELRRKI-G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 164 YVMQDDLLFPMLTVEETLMFaaefrLPRSL--SKSKKKARVQALIDQLGLTTAAntvIGDEGHRGVSGGERRRVSIGIDI 241
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIAL-----VPKLLkwPKEKIRERADELLALVGLDPAE---FADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 242 IHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQ-SGSIVITSIH--QPSYRilsLLDRLIFLSRGQTVYSGSPAEL---- 314
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQeLGKTIVFVTHdiDEAFR---LADRIAIMKNGEIVQVGTPDEIlrsp 227
|
....*...
gi 1281000366 315 -SEFLADF 321
Cdd:cd03295 228 aNDFVAEF 235
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
103-314 |
3.47e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 82.43 E-value: 3.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALaDRIAKEKlKGTVTLNDEVLE---SALLKV--ISAYVMQ--DDLLF-Pm 174
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHF-NGILKPT-SGEVLIKGEPIKydkKSLLEVrkTVGIVFQnpDDQLFaP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 175 lTVEETLMFAAefrLPRSLSKSKKKARVQALIDQLGLTTAANTVigdeGHRgVSGGERRRVSIGIDIIHDPILLFLDEPT 254
Cdd:PRK13639 95 -TVEEDVAFGP---LNLGLSKEEVEKRVKEALKAVGMEGFENKP----PHH-LSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1281000366 255 SGLDSTSAFMVVKVLQRIAQSGSIVITSIHQ----PSYRilsllDRLIFLSRGQTVYSGSPAEL 314
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLNKEGITIIISTHDvdlvPVYA-----DKVYVMSDGKIIKEGTPKEV 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
103-316 |
3.68e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.07 E-value: 3.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALA-----DRiakeklkGTVTLNDEVLE-----SALLKVISAyVMQDDLLF 172
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSgvyqpDS-------GEILLDGEPVRfrsprDAQAAGIAI-IHQELNLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 173 PMLTVEETLMFAAEFRLPRSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLDE 252
Cdd:COG1129 92 PNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGD-----LSVAQQQLVEIARALSRDARVLILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1281000366 253 PTSGLDSTSAFMVVKVLQRIAQSG-SIVITSiHqpsyR---ILSLLDRLIFLSRGQTVYSGSPAELSE 316
Cdd:COG1129 167 PTASLTEREVERLFRIIRRLKAQGvAIIYIS-H----RldeVFEIADRVTVLRDGRLVGTGPVAELTE 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
112-343 |
3.85e-17 |
|
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: 86.61 E-value: 3.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 112 EGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVLESALLKVISAYVM--QDDLLFPMLTVEETLMFAAEFRl 189
Cdd:TIGR01257 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTS--GTVLVGGKDIETNLDAVRQSLGMcpQHNILFHHLTVAEHILFYAQLK- 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 190 prSLSKSKKKARVQALIDQLGLTTAANtvigdEGHRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVL 269
Cdd:TIGR01257 1032 --GRSWEEAQLEMEAMLEDTGLHHKRN-----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281000366 270 QRIAQSGSIVITSIHQPSYRILSllDRLIFLSRGQTVYSGSPAelseFLAD-FGhpipenenrTEFALDLVRDLE 343
Cdd:TIGR01257 1105 LKYRSGRTIIMSTHHMDEADLLG--DRIAIISQGRLYCSGTPL----FLKNcFG---------TGFYLTLVRKMK 1164
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
88-337 |
4.07e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 81.72 E-value: 4.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGRVkllLNDISGEAREGEIMAVLGASGSGKSTLIDALadRIAKEKLKGTVTLNDEVLESAL---------- 157
Cdd:PRK11264 7 KNLVKKFHGQTV---LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI--NLLEQPEAGTIRVGDITIDTARslsqqkglir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 158 -LKVISAYVMQDDLLFPMLTVEETLMFAaefrlPRSLSKSKKK---ARVQALIDQLGLTTAANTVigdegHRGVSGGERR 233
Cdd:PRK11264 82 qLRQHVGFVFQNFNLFPHRTVLENIIEG-----PVIVKGEPKEeatARARELLAKVGLAGKETSY-----PRRLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 234 RVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYrILSLLDRLIFLSRGQTVYSGSPAE 313
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSF-ARDVADRAIFMDQGRIVEQGPAKA 230
|
250 260
....*....|....*....|....
gi 1281000366 314 LsefladFGHPipeNENRTEFALD 337
Cdd:PRK11264 231 L------FADP---QQPRTRQFLE 245
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
88-304 |
7.26e-17 |
|
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: 80.09 E-value: 7.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGRVKL-LLNDISGEAREGEIMAVLGASGSGKSTLIDALADriAKEKLKGTVTLNDEVLESALLKVISA--- 163
Cdd:TIGR02211 5 ENLGKRYQEGKLDTrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGG--LDNPTSGEVLFNGQSLSKLSSNERAKlrn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 164 ----YVMQDDLLFPMLTVEETLMFAAefrLPRSLSKSKKKARVQALIDQLGLTTAANtvigdegHRG--VSGGERRRVSI 237
Cdd:TIGR02211 83 kklgFIYQFHHLLPDFTALENVAMPL---LIGKKSVKEAKERAYEMLEKVGLEHRIN-------HRPseLSGGERQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 238 GIDIIHDPILLFLDEPTSGLDSTSA---FMVVKVLQRIAQSGSIVITsiHQPsyRILSLLDRLIFLSRGQ 304
Cdd:TIGR02211 153 ARALVNQPSLVLADEPTGNLDNNNAkiiFDLMLELNRELNTSFLVVT--HDL--ELAKKLDRVLEMKDGQ 218
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
89-304 |
7.28e-17 |
|
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: 79.82 E-value: 7.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 89 NLTAEENGGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLNDEVlesallkvisAYVMQD 168
Cdd:cd03250 7 SFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGEL--EKLSGSVSVPGSI----------AYVSQE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 169 DLLFPMlTVEETLMFAAEFRLPRslskSKKKARVQAL---IDQL--GLttaaNTVIGDeghRGV--SGGERRRVSIGIDI 241
Cdd:cd03250 75 PWIQNG-TIRENILFGKPFDEER----YEKVIKACALepdLEILpdGD----LTEIGE---KGInlSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1281000366 242 IHDPILLFLDEPTSGLDS-TSAFMVVKVLQRIAQSGSIVITSIHQPSYriLSLLDRLIFLSRGQ 304
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAhVGRHIFENCILGLLLNNKTRILVTHQLQL--LPHADQIVVLDNGR 204
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
103-310 |
7.66e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.21 E-value: 7.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKLKGTVT--LNDEVLESALL-------KVISAYVMQDDLLFP 173
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIelLGRTVQREGRLardirksRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 174 MLTVEETLMFAAEFRLP------RSLSKSKKKARVQALIdQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPIL 247
Cdd:PRK09984 100 RLSVLENVLIGALGSTPfwrtcfSWFTREQKQRALQALT-RVGMVHFAHQRVST-----LSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1281000366 248 LFLDEPTSGLDSTSAFMVVKVLQRIAQSGSI-VITSIHQPSYrILSLLDRLIFLSRGQTVYSGS 310
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQNDGItVVVTLHQVDY-ALRYCERIVALRQGHVFYDGS 236
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
88-316 |
8.22e-17 |
|
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: 79.49 E-value: 8.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGRVkllLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKLKGTVTLNDEVL------ESALLKVI 161
Cdd:cd03217 4 KDLHVSVGGKEI---LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKGEDItdlppeERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 162 SAyvMQDDLLFPMLTVEETLmfaaefrlpRSLSKskkkarvqalidqlglttaantvigdeghrGVSGGERRRVSIGIDI 241
Cdd:cd03217 81 LA--FQYPPEIPGVKNADFL---------RYVNE------------------------------GFSGGEKKRNEILQLL 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1281000366 242 IHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGS--IVITsiHQPsyRILSLL--DRLIFLSRGQTVYSGsPAELSE 316
Cdd:cd03217 120 LLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKsvLIIT--HYQ--RLLDYIkpDRVHVLYDGRIVKSG-DKELAL 193
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
96-304 |
9.34e-17 |
|
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: 78.41 E-value: 9.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 96 GGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLNDEVLES---ALLKVISAYVMQDDLLF 172
Cdd:cd03246 11 PGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLL--RPTSGRVRLDGADISQwdpNELGDHVGYLPQDDELF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 173 PmltveetlmfaaefrlprslskskkkarvqalidqlGlTTAANTVigdeghrgvSGGERRRVSIGIDIIHDPILLFLDE 252
Cdd:cd03246 89 S------------------------------------G-SIAENIL---------SGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1281000366 253 PTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSyrILSLLDRLIFLSRGQ 304
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDGR 172
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
100-314 |
1.40e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.80 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKLKGTVtLNDEVLESA-LLKVISAYVMQDDLLFPMLTVE 178
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV-LGVPVPARArLARARIGVVPQFDNLDLEFTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 179 ETLM-FAAEFRLprslSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLDEPTSGL 257
Cdd:PRK13536 133 ENLLvFGRYFGM----STREIEAVIPSLLEFARLESKADARVSD-----LSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1281000366 258 DSTSAFMVVKVLQRIAQSGSIVITSIH--QPSYRilsLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:PRK13536 204 DPHARHLIWERLRSLLARGKTILLTTHfmEEAER---LCDRLCVLEAGRKIAEGRPHAL 259
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
102-350 |
1.51e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.58 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 102 LLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVLESALLKVIS---AYVMQDDLLFPMLTVE 178
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTA--GTVLVAGDDVEALSARAASrrvASVPQDTSLSFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 179 ETLMFAAEFRLPR-SLSKSKKKARVQALIDQLGLTTAAntvigDEGHRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGL 257
Cdd:PRK09536 96 QVVEMGRTPHRSRfDTWTETDRAAVERAMERTGVAQFA-----DRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 258 DSTSAFMVVKVLQRIAQSGSIVITSIHQpsyriLSL----LDRLIFLSRGQTVYSGSPAEL--SEFLAD-FG-------H 323
Cdd:PRK09536 171 DINHQVRTLELVRRLVDDGKTAVAAIHD-----LDLaaryCDELVLLADGRVRAAGPPADVltADTLRAaFDartavgtD 245
|
250 260
....*....|....*....|....*..
gi 1281000366 324 PIPENENRTEFALDlvrDLEETAGGTR 350
Cdd:PRK09536 246 PATGAPTVTPLPDP---DRTEAAADTR 269
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
103-321 |
2.01e-16 |
|
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: 80.00 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLNDEVL----ESALLKVIS---AYVMQDDLLFPML 175
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLI--EPTSGKVLIDGQDIaamsRKELRELRRkkiSMVFQSFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 176 TVEETLMFAAEFrlpRSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLDEPTS 255
Cdd:cd03294 118 TVLENVAFGLEV---QGVPRAEREERAAEALELVGLEGWEHKYPDE-----LSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1281000366 256 GLDST-SAFMVVKVLQRIAQSGSIVITSIHQPSyRILSLLDRLIFLSRGQTVYSGSPAEL-----SEFLADF 321
Cdd:cd03294 190 ALDPLiRREMQDELLRLQAELQKTIVFITHDLD-EALRLGDRIAIMKDGRLVQVGTPEEIltnpaNDYVREF 260
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
77-321 |
2.02e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.81 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 77 VKVRRRGSSLPE--NLTAEENGgrvKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADriAKEKLKGTVtlndeVLE 154
Cdd:PRK11607 10 AKTRKALTPLLEirNLTKSFDG---QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG--FEQPTAGQI-----MLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 155 SALLKVISAY------VMQDDLLFPMLTVEETLMFAAEfrlPRSLSKSKKKARVQALIDQLGLTTAANTvigdEGHRgVS 228
Cdd:PRK11607 80 GVDLSHVPPYqrpinmMFQSYALFPHMTVEQNIAFGLK---QDKLPKAEIASRVNEMLGLVHMQEFAKR----KPHQ-LS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 229 GGERRRVSIGIDIIHDPILLFLDEPTSGLDST----SAFMVVKVLQRIaqsGSIVITSIHQPSyRILSLLDRLIFLSRGQ 304
Cdd:PRK11607 152 GGQRQRVALARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV---GVTCVMVTHDQE-EAMTMAGRIAIMNRGK 227
|
250 260
....*....|....*....|..
gi 1281000366 305 TVYSGSPAELSE-----FLADF 321
Cdd:PRK11607 228 FVQIGEPEEIYEhpttrYSAEF 249
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
103-315 |
2.13e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 83.23 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALA--D-------RIAKEKLkgtVTLNDEVLeSALLKVISAYVMQDDLLFP 173
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGclDkptsgtyRVAGQDV---ATLDADAL-AQLRREHFGFIFQRYHLLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 174 MLTVEETLMFAAEFrlpRSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLDEP 253
Cdd:PRK10535 100 HLTAAQNVEVPAVY---AGLERKQRLLRAQELLQRLGLEDRVEYQPSQ-----LSGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1281000366 254 TSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPsyRILSLLDRLIFLSRGQTVySGSPAELS 315
Cdd:PRK10535 172 TGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP--QVAAQAERVIEIRDGEIV-RNPPAQEK 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
88-340 |
2.22e-16 |
|
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: 82.93 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGRVkllLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKLKGTVTLNDEVLESALLKVISAYVMQ 167
Cdd:TIGR03269 4 KNLTKKFDGKEV---LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHVALCEKCGYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 168 -------------------DDLLFPMLTVEETLMFAAEFRL----------PRSLSK---SKKKA--RVQALIDQLGLTT 213
Cdd:TIGR03269 81 pcpvcggtlepeevdfwnlSDKLRRRIRKRIAIMLQRTFALygddtvldnvLEALEEigyEGKEAvgRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 214 AANTVIgdeghRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQR--IAQSGSIVITSiHQPSYrIL 291
Cdd:TIGR03269 161 RITHIA-----RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTS-HWPEV-IE 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1281000366 292 SLLDRLIFLSRGQTVYSGSPAELSE-FLADFghPIPENENRTEFALDLVR 340
Cdd:TIGR03269 234 DLSDKAIWLENGEIKEEGTPDEVVAvFMEGV--SEVEKECEVEVGEPIIK 281
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
89-314 |
3.46e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 79.78 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 89 NLTAEENGGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLNDEVLESA---------LLK 159
Cdd:PRK13643 8 NYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLL--QPTEGKVTVGDIVVSSTskqkeikpvRKK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 160 VISAYVMQDDLLFpmltvEETLMFAAEFRlPRSLSKSKKKARVQAL--IDQLGLTTAantvIGDEGHRGVSGGERRRVSI 237
Cdd:PRK13643 86 VGVVFQFPESQLF-----EETVLKDVAFG-PQNFGIPKEKAEKIAAekLEMVGLADE----FWEKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1281000366 238 GIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSyRILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMD-DVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
103-320 |
5.34e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 79.36 E-value: 5.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRI------------AKEKLKGTVTLNDEVLESALLKVISAYVMQ-DD 169
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLlpdtgtiewifkDEKNKKKTKEKEKVLEKLVIQKTRFKKIKKiKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 170 L--------------LFPMlTVEETLMFAaefrlPRSLSKSKKKARVQAL--IDQLGLttaantvigDEGHR-----GVS 228
Cdd:PRK13651 103 IrrrvgvvfqfaeyqLFEQ-TIEKDIIFG-----PVSMGVSKEEAKKRAAkyIELVGL---------DESYLqrspfELS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 229 GGERRRVSI-GIdIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSyRILSLLDRLIFLSRGQTVY 307
Cdd:PRK13651 168 GGQKRRVALaGI-LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD-NVLEWTKRTIFFKDGKIIK 245
|
250
....*....|....*.
gi 1281000366 308 SGSPAEL---SEFLAD 320
Cdd:PRK13651 246 DGDTYDIlsdNKFLIE 261
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
102-322 |
7.77e-16 |
|
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: 78.31 E-value: 7.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 102 LLNDISGEAREGEIMAVLGASGSGKSTLIDALadrIAKEK-LKGTVTLNDEVLesALLKVISAYVMQDD--LLF------ 172
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLL---LGLEKpAQGTVSFRGQDL--YQLDRKQRRAFRRDvqLVFqdspsa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 173 --PMLTVEETLmfAAEFRLPRSLSKSKKKARVQALIDQLGLTTAantvIGDEGHRGVSGGERRRVSIGIDIIHDPILLFL 250
Cdd:TIGR02769 101 vnPRMTVRQII--GEPLRHLTSLDESEQKARIAELLDMVGLRSE----DADKLPRQLSGGQLQRINIARALAVKPKLIVL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1281000366 251 DEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYRILSLLDRLIFLSRGQTVYSGSPAELSEFLADFG 322
Cdd:TIGR02769 175 DEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSFKHPAG 246
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
68-309 |
1.56e-15 |
|
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: 75.04 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 68 LSFQNLSYSvkvrrrgssLPENltaeenggrVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVT 147
Cdd:cd03247 1 LSINNVSFS---------YPEQ---------EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDL--KPQQGEIT 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 148 LNDE---VLESALLKVISaYVMQDDLLFpmltveetlmfaaefrlprslskskkkarvqalidqlglttaaNTVIGDEGH 224
Cdd:cd03247 61 LDGVpvsDLEKALSSLIS-VLNQRPYLF-------------------------------------------DTTLRNNLG 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 225 RGVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSyriLSLLDRLIFLSRGQ 304
Cdd:cd03247 97 RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTG---IEHMDKILFLENGK 173
|
....*
gi 1281000366 305 TVYSG 309
Cdd:cd03247 174 IIMQG 178
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
71-323 |
2.06e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.82 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 71 QNLSYSVKVRRRGSSLPENLTA----EEnggRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIdaladriakeKL---- 142
Cdd:COG4586 5 ENLSKTYRVYEKEPGLKGALKGlfrrEY---REVEAVDDISFTIEPGEIVGFIGPNGAGKSTTI----------KMltgi 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 143 ----KGTVTLNDEV---LESALLKVISAyVM-QDDLLFPMLTVEETL-MFAAEFRLPrslsKSKKKARVQALIDQLGLTT 213
Cdd:COG4586 72 lvptSGEVRVLGYVpfkRRKEFARRIGV-VFgQRSQLWWDLPAIDSFrLLKAIYRIP----DAEYKKRLDELVELLDLGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 214 AANTVIgdeghRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRI-AQSGSIVI-TSiHqpsY--R 289
Cdd:COG4586 147 LLDTPV-----RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILlTS-H---DmdD 217
|
250 260 270
....*....|....*....|....*....|....
gi 1281000366 290 ILSLLDRLIFLSRGQTVYSGSpaeLSEFLADFGH 323
Cdd:COG4586 218 IEALCDRVIVIDHGRIIYDGS---LEELKERFGP 248
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
106-313 |
2.33e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 76.51 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 106 ISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEklkGTVTLNDEVLES---ALLKVISAYVMQDDLLFPMLTVEETLM 182
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS---GSIQFAGQPLEAwsaAELARHRAYLSQQQTPPFAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 183 FAaefrLPRSLSKSKKKARVQALIDQLGLTtaantvigDEGHRGV---SGGERRRVSIGIDI--IHDPI-----LLFLDE 252
Cdd:PRK03695 92 LH----QPDKTRTEAVASALNEVAEALGLD--------DKLGRSVnqlSGGEWQRVRLAAVVlqVWPDInpagqLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1281000366 253 PTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSyRILSLLDRLIFLSRGQTVYSGSPAE 313
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLN-HTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
88-344 |
3.28e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 76.62 E-value: 3.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGR--VKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLNDEVL--ESALLKVIS- 162
Cdd:PRK13637 6 ENLTHIYMEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLL--KPTSGKIIIDGVDItdKKVKLSDIRk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 163 --AYVMQ--DDLLFpmltvEETLMFAAEFRlPRSL--SKSKKKARVQALIDQLGLTTaanTVIGDEGHRGVSGGERRRVS 236
Cdd:PRK13637 84 kvGLVFQypEYQLF-----EETIEKDIAFG-PINLglSEEEIENRVKRAMNIVGLDY---EDYKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 237 IGIDIIHDPILLFLDEPTSGLDSTS---AFMVVKVLQRiaQSGSIVITSIHQPSyRILSLLDRLIFLSRGQTVYSGSPAE 313
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGrdeILNKIKELHK--EYNMTIILVSHSME-DVAKLADRIIVMNKGKCELQGTPRE 231
|
250 260 270
....*....|....*....|....*....|....
gi 1281000366 314 L---SEFLADFGHPIPEnenrtefALDLVRDLEE 344
Cdd:PRK13637 232 VfkeVETLESIGLAVPQ-------VTYLVRKLRK 258
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
100-307 |
3.31e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 76.28 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVL----ESALLKVISaYVMQDDLL--FP 173
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDS--GSILIDGKDVtklpEYKRAKYIG-RVFQDPMMgtAP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 174 MLTVEETLMFAAEFRLPRSLSKSKKKARVQALIDQL-----GLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILL 248
Cdd:COG1101 96 SMTIEENLALAYRRGKRRGLRRGLTKKRRELFRELLatlglGLENRLDTKVGL-----LSGGQRQALSLLMATLTKPKLL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1281000366 249 FLDEPTSGLDSTSAFMVVKVLQRIAQSGSI---VIT-SIHQPsyriLSLLDRLIFLSRGQTVY 307
Cdd:COG1101 171 LLDEHTAALDPKTAALVLELTEKIVEENNLttlMVThNMEQA----LDYGNRLIMMHEGRIIL 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
103-283 |
3.50e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 75.82 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDAL-----AD----RIAKEKLKGTVTLNDEvlESALLKVISAYVMQDDLLFP 173
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemPRsgtlNIAGNHFDFSKTPSDK--AIRELRRNVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 174 MLTVEETLMfAAEFRLpRSLSKSKKKARVQALIDQLGLTTAAntvigDEGHRGVSGGERRRVSIGIDIIHDPILLFLDEP 253
Cdd:PRK11124 96 HLTVQQNLI-EAPCRV-LGLSKDQALARAEKLLERLRLKPYA-----DRFPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190
....*....|....*....|....*....|
gi 1281000366 254 TSGLDSTSAFMVVKVLQRIAQSGsivITSI 283
Cdd:PRK11124 169 TAALDPEITAQIVSIIRELAETG---ITQV 195
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
100-314 |
4.82e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 75.80 E-value: 4.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADrIAKEKlKGTVTLNDEVLESALLKVISAY---VMQD-DLLFPML 175
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTG-LLKPQ-SGEIKIDGITISKENLKEIRKKigiIFQNpDNQFIGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 176 TVEETLMFAAEFR-LPRSlskskkkaRVQALIDQLGLTTAANTVIGDEGHRgVSGGERRRVSIGIDIIHDPILLFLDEPT 254
Cdd:PRK13632 100 TVEDDIAFGLENKkVPPK--------KMKDIIDDLAKKVGMEDYLDKEPQN-LSGGQKQRVAIASVLALNPEIIIFDEST 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1281000366 255 SGLDSTSAFMVVKVLQRIAQSGSIVITSI-HQPSYRILSllDRLIFLSRGQTVYSGSPAEL 314
Cdd:PRK13632 171 SMLDPKGKREIKKIMVDLRKTRKKTLISItHDMDEAILA--DKVIVFSEGKLIAQGKPKEI 229
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
97-314 |
6.24e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.59 E-value: 6.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 97 GRVklLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVLESALLKVIS---AYVMQDDLLFP 173
Cdd:PRK10575 23 GRT--LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSE--GEILLDAQPLESWSSKAFArkvAYLPQQLPAAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 174 MLTVEEtlmFAAEFRLP--RSLSK--SKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLF 249
Cdd:PRK10575 99 GMTVRE---LVAIGRYPwhGALGRfgAADREKVEEAISLVGLKPLAHRLVDS-----LSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1281000366 250 LDEPTSGLDSTSAFMVVKVLQRIAQS-GSIVITSIHQPSYRIlSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:PRK10575 171 LDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAA-RYCDYLVALRGGEMIAQGTPAEL 235
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
103-346 |
6.25e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 76.66 E-value: 6.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTL---IDALadriakEK-LKGTVTLNDEVL----ESALLKV---ISaYVMQDDLL 171
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLircINLL------ERpTSGSVLVDGVDLtalsERELRAArrkIG-MIFQHFNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 172 FPMLTVEETLMFAAEFrlpRSLSKSKKKARVQALIDQLGLttaantvigdEGHRGV-----SGGERRRVSIGIDIIHDPI 246
Cdd:COG1135 94 LSSRTVAENVALPLEI---AGVPKAEIRKRVAELLELVGL----------SDKADAypsqlSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 247 LLFLDEPTSGLD--STSAfmVVKVLQRIAQS-G-SIV-ITsiHQPSYrILSLLDRLIFLSRGQTVYSGSPAELsefladF 321
Cdd:COG1135 161 VLLCDEATSALDpeTTRS--ILDLLKDINRElGlTIVlIT--HEMDV-VRRICDRVAVLENGRIVEQGPVLDV------F 229
|
250 260
....*....|....*....|....*
gi 1281000366 322 GHPipenenRTEFALDLVRDLEETA 346
Cdd:COG1135 230 ANP------QSELTRRFLPTVLNDE 248
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
100-347 |
1.09e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 75.06 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLNDEVLESAL----LKVIS---AYVMQddllF 172
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLL--QPTSGTVTIGERVITAGKknkkLKPLRkkvGIVFQ----F 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 173 P--ML---TVEETLMFAaefrlPRS--LSKSKKKARVQALIDQLGLTTAantvIGDEGHRGVSGGERRRVSIGIDIIHDP 245
Cdd:PRK13634 94 PehQLfeeTVEKDICFG-----PMNfgVSEEDAKQKAREMIELVGLPEE----LLARSPFELSGGQMRRVAIAGVLAMEP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 246 ILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSI-VITSIHQ----PSYRilsllDRLIFLSRGQTVYSGSPAEL---SEF 317
Cdd:PRK13634 165 EVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLtTVLVTHSmedaARYA-----DQIVVMHKGTVFLQGTPREIfadPDE 239
|
250 260 270
....*....|....*....|....*....|
gi 1281000366 318 LADFGHPIPENenrTEFAldlvRDLEETAG 347
Cdd:PRK13634 240 LEAIGLDLPET---VKFK----RALEEKFG 262
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
100-310 |
1.19e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.44 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEklkGTVTLNDEVLES----ALLKVIS--AYVMQD--DLL 171
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ---GEIWFDGQPLHNlnrrQLLPVRHriQVVFQDpnSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 172 FPMLTVEETLMFAAEFRLPrSLSKSKKKARVQALIDQLGLTTAANtvigdegHR---GVSGGERRRVSIGIDIIHDPILL 248
Cdd:PRK15134 376 NPRLNVLQIIEEGLRVHQP-TLSAAQREQQVIAVMEEVGLDPETR-------HRypaEFSGGQRQRIAIARALILKPSLI 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 249 FLDEPTSGLDSTSAFMVVKVLQRIAQSgsivitsiHQPSYRILS--------LLDRLIFLSRGQTVYSGS 310
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLQQK--------HQLAYLFIShdlhvvraLCHQVIVLRQGEVVEQGD 509
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
115-310 |
1.75e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 75.68 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 115 IMAVLGASGSGKSTLIDALADRIAKEklKGTVTLNDEVLESALLKVISA-------YVMQDDLLFPMLTVEETLMFAAef 187
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQ--KGRIVLNGRVLFDAEKGICLPpekrrigYVFQDARLFPHYKVRGNLRYGM-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 188 rlprslsKSKKKARVQALIDQLGLttaantvigdeGH------RGVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTS 261
Cdd:PRK11144 102 -------AKSMVAQFDKIVALLGI-----------EPlldrypGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1281000366 262 AFMVVKVLQRIAQSGSIVITSIHQPSYRILSLLDRLIFLSRGQTVYSGS 310
Cdd:PRK11144 164 KRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
103-314 |
1.91e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.79 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALAdRiAKEKLKGTVTLNDEVL----ESALLKVISaYVMQDDLLFPMlTVE 178
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT-R-AWDPQQGEILLNGQPIadysEAALRQAIS-VVSQRVHLFSA-TLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 179 ETLMFAAEfrlprslskskkKARVQALID---QLGLTTAA------NTVIGdEGHRGVSGGERRRVSIGIDIIHD-PILL 248
Cdd:PRK11160 432 DNLLLAAP------------NASDEALIEvlqQVGLEKLLeddkglNAWLG-EGGRQLSGGEQRRLGIARALLHDaPLLL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1281000366 249 fLDEPTSGLDSTSAFMVVKVLQRIAQSGS-IVITsihqpsYRILSL--LDRLIFLSRGQTVYSGSPAEL 314
Cdd:PRK11160 499 -LDEPTEGLDAETERQILELLAEHAQNKTvLMIT------HRLTGLeqFDRICVMDNGQIIEQGTHQEL 560
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
88-322 |
2.38e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 73.58 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGRVkllLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVLE--SALLKVisayV 165
Cdd:PRK11248 5 SHLYADYGGKPA---LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQH--GSITLDGKPVEgpGAERGV----V 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 166 MQDDLLFPMLTVEETLMFAAEFRlprSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDP 245
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLA---GVEKMQRLEIAHQMLKKVGLEGAEKRYIWQ-----LSGGQRQRVGIARALAANP 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1281000366 246 ILLFLDEPTSGLDS-TSAFMVVKVLQRIAQSGSIVITSIHQpsyrilslLDRLIFLSRGQTVYSGSPAELSEFLA-DFG 322
Cdd:PRK11248 148 QLLLLDEPFGALDAfTREQMQTLLLKLWQETGKQVLLITHD--------IEEAVFMATELVLLSPGPGRVVERLPlNFA 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
103-324 |
3.52e-14 |
|
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: 75.88 E-value: 3.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEklkGTVTLNDEVL----ESALLKVISAY--VMQDDL--LFPM 174
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE---GEIRFDGQDLdglsRRALRPLRRRMqvVFQDPFgsLSPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 175 LTVEETLmfaAE-FRL-PRSLSKSKKKARVQALIDQLGLTTAAntvigdeGHR---GVSGGERRRVSIGIDIIHDPILLF 249
Cdd:COG4172 379 MTVGQII---AEgLRVhGPGLSAAERRARVAEALEEVGLDPAA-------RHRyphEFSGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 250 LDEPTSGLDSTSAFMVVKVLQRIAQSgsivitsiHQPSY----------RILSllDRLIFLSRGQTVYSGSPAELsefla 319
Cdd:COG4172 449 LDEPTSALDVSVQAQILDLLRDLQRE--------HGLAYlfishdlavvRALA--HRVMVMKDGKVVEQGPTEQV----- 513
|
....*
gi 1281000366 320 dFGHP 324
Cdd:COG4172 514 -FDAP 517
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
103-333 |
4.69e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.45 E-value: 4.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDAL-----ADriakeklKGTVTLNDEVLEsallkvIS----------AYVMQ 167
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILyglyqPD-------SGEILIDGKPVR------IRsprdaialgiGMVHQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 168 DDLLFPMLTVEETLMFAAEFRLPRSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSI------GIDI 241
Cdd:COG3845 88 HFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVED-----LSVGEQQRVEIlkalyrGARI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 242 ihdpilLFLDEPTSGL--DSTSAFMvvKVLQRIAQSG-SIVITS--IHQpsyrILSLLDRLIFLSRGQTVYSGSPAELS- 315
Cdd:COG3845 163 ------LILDEPTAVLtpQEADELF--EILRRLAAEGkSIIFIThkLRE----VMAIADRVTVLRRGKVVGTVDTAETSe 230
|
250 260
....*....|....*....|
gi 1281000366 316 EFLAD--FGHPIPENENRTE 333
Cdd:COG3845 231 EELAElmVGREVLLRVEKAP 250
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
96-258 |
5.96e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.10 E-value: 5.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 96 GGRVklLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEklKGTVTLNDEvlesalLKVisAYVMQDDLLFPML 175
Cdd:COG0488 9 GGRP--LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPD--SGEVSIPKG------LRI--GYLPQEPPLDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 176 TVEETLM-------------FAAEFRLPRSLSKSKKKARVQALIDQLGLTTA---ANTVI------GDEGHRGV---SGG 230
Cdd:COG0488 77 TVLDTVLdgdaelraleaelEELEAKLAEPDEDLERLAELQEEFEALGGWEAearAEEILsglgfpEEDLDRPVselSGG 156
|
170 180
....*....|....*....|....*...
gi 1281000366 231 ERRRVSIGIDIIHDPILLFLDEPTSGLD 258
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
70-315 |
5.98e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 75.38 E-value: 5.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 70 FQNLSYSVKVRRRGsslpenltaeenggrvkllLNDISGEAREGEIMAVLGASGSGKSTLIdALADRiAKEKLKGTVTLN 149
Cdd:PRK13657 337 FDDVSFSYDNSRQG-------------------VEDVSFEAKPGQTVAIVGPTGAGKSTLI-NLLQR-VFDPQSGRILID 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 150 DE----VLESALLKVIsAYVMQDDLLFPMlTVEETLMFAAEFRLPRSLSKSKKKARVQALIDQ--LGLttaaNTVIGDEG 223
Cdd:PRK13657 396 GTdirtVTRASLRRNI-AVVFQDAGLFNR-SIEDNIRVGRPDATDEEMRAAAERAQAHDFIERkpDGY----DTVVGERG 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 224 hRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSiHQpsyriLSLL---DRLIFL 300
Cdd:PRK13657 470 -RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIA-HR-----LSTVrnaDRILVF 542
|
250
....*....|....*
gi 1281000366 301 SRGQTVYSGSPAELS 315
Cdd:PRK13657 543 DNGRVVESGSFDELV 557
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
88-297 |
6.66e-14 |
|
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: 75.11 E-value: 6.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAE-ENGGRVKLLLNDISGEAREGEIMAVLGASGSGKS----TLIDALADRIAKekLKGTVTLNDEVL----ESALL 158
Cdd:COG4172 10 EDLSVAfGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAH--PSGSILFDGQDLlglsERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 159 KV----IsAYVMQDDL--LFPMLTVE----ETLmfaaefRLPRSLSKSKKKARVQALIDQLGLTTAAnTVIGDEGHRgVS 228
Cdd:COG4172 88 RIrgnrI-AMIFQEPMtsLNPLHTIGkqiaEVL------RLHRGLSGAAARARALELLERVGIPDPE-RRLDAYPHQ-LS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1281000366 229 GGERRRVSIGIDIIHDPILLFLDEPTSGLDSTsafmvvkvLQriAQsgsivitsihqpsyrILSLLDRL 297
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVT--------VQ--AQ---------------ILDLLKDL 202
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
100-326 |
7.61e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 72.53 E-value: 7.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKST---LIDA--LADRIAKEKLK-GTVTLNDEVLESALLKVisAYVMQD-DLLF 172
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGllLPDDNPNSKITvDGITLTAKTVWDIREKV--GIVFQNpDNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 173 PMLTVEETLMFAAEfrlPRSLSKSKKKARVQALIDQLGLTTAAntvigDEGHRGVSGGERRRVSI-GIDIIhDPILLFLD 251
Cdd:PRK13640 98 VGATVGDDVAFGLE---NRAVPRPEMIKIVRDVLADVGMLDYI-----DSEPANLSGGQKQRVAIaGILAV-EPKIIILD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 252 EPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIhqpSYRI--LSLLDRLIFLSRGQTVYSGSPAEL---SEFLADFGHPIP 326
Cdd:PRK13640 169 ESTSMLDPAGKEQILKLIRKLKKKNNLTVISI---THDIdeANMADQVLVLDDGKLLAQGSPVEIfskVEMLKEIGLDIP 245
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
89-326 |
1.09e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 72.63 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 89 NLTAEENG--GRVKLLlNDISGEAREGEIMAVLGASGSGKSTLIDALADrIAKEKLKGTV---TLNDEVL----ESALLK 159
Cdd:COG4170 8 NLTIEIDTpqGRVKAV-DRVSLTLNEGEIRGLVGESGSGKSLIAKAICG-ITKDNWHVTAdrfRWNGIDLlklsPRERRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 160 VIS---AYVMQDDL--LFPMLTVEETLMFAaefrLPRSLSKSK-------KKARVQALIDQLGlttaantvIGDegHRGV 227
Cdd:COG4170 86 IIGreiAMIFQEPSscLDPSAKIGDQLIEA----IPSWTFKGKwwqrfkwRKKRAIELLHRVG--------IKD--HKDI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 228 --------SGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYRILSLLDRLIF 299
Cdd:COG4170 152 mnsyphelTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITV 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 1281000366 300 LSRGQTVYSGSPAELSE------------FLADFGHPIP 326
Cdd:COG4170 232 LYCGQTVESGPTEQILKsphhpytkallrSMPDFRQPLP 270
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
89-345 |
1.14e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 72.07 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 89 NLTAEENGGRVKLLLNDISGEAREGEIMAVLGASGSGKST---LIDALAdriakEKLKGTVTLNDEVLESA----LLKVI 161
Cdd:PRK13650 9 NLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLL-----EAESGQIIIDGDLLTEEnvwdIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 162 SAYVMQDDLLFPMLTVEETLMFAAEfrlPRSLSKSKKKARVQALIDQLGLTTAANTvigdEGHRgVSGGERRRVSIGIDI 241
Cdd:PRK13650 84 GMVFQNPDNQFVGATVEDDVAFGLE---NKGIPHEEMKERVNEALELVGMQDFKER----EPAR-LSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 242 IHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSI-HQPSYRILSllDRLIFLSRGQTVYSGSPAEL---SEF 317
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISItHDLDEVALS--DRVLVMKNGQVESTSTPRELfsrGND 233
|
250 260
....*....|....*....|....*...
gi 1281000366 318 LADFGHPIPenenrteFALDLVRDLEET 345
Cdd:PRK13650 234 LLQLGLDIP-------FTTSLVQSLRQN 254
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
103-314 |
1.16e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.17 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLI---DALAdriakEKLKGTVTLNDEVLES--------ALLKVIS-AYVMQDDL 170
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMqhfNALL-----KPSSGTITIAGYHITPetgnknlkKLRKKVSlVFQFPEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 171 LFpmltvEETLMFAAEFRlPRSLSKSKKKARVQAL--IDQLGLTTAantvIGDEGHRGVSGGERRRVSIGIDIIHDPILL 248
Cdd:PRK13641 98 LF-----ENTVLKDVEFG-PKNFGFSEDEAKEKALkwLKKVGLSED----LISKSPFELSGGQMRRVAIAGVMAYEPEIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1281000366 249 FLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSyRILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:PRK13641 168 CLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMD-DVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
103-258 |
1.34e-13 |
|
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: 70.36 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLNDEV---LESALLKVisAYVMQDDLLFPMLTVEE 179
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLE--EPTSGRIYIGGRDvtdLPPKDRDI--AMVFQNYALYPHMTVYD 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1281000366 180 TLMFAAEFRlprSLSKSKKKARVQALIDQLGLTTaantvIGDEGHRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGLD 258
Cdd:cd03301 92 NIAFGLKLR---KVPKDEIDERVREVAELLQIEH-----LLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
100-315 |
1.42e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.11 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIakeKLKGTVTLNDEVL----ESALLKVIsAYVMQDDLLFPMl 175
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL---PYQGSLKINGIELreldPESWRKHL-SWVGQNPQLPHG- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 176 TVEETLMFAAEFRLPRSLSKSKKKARVQALIDQL--GLttaaNTVIGDEGhRGVSGGERRRVSIGIDIIHDPILLFLDEP 253
Cdd:PRK11174 438 TLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLpqGL----DTPIGDQA-AGLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1281000366 254 TSGLDSTSAFMVVKVLQRIAQSGS-IVITsiHQPSYriLSLLDRLIFLSRGQTVYSGSPAELS 315
Cdd:PRK11174 513 TASLDAHSEQLVMQALNAASRRQTtLMVT--HQLED--LAQWDQIWVMQDGQIVQQGDYAELS 571
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
103-342 |
1.64e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 71.66 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKST---LIDALAdriakEKLKGTVTLNDEVLESA----LLKVISAYVMQDDLLFPML 175
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTtarLIDGLF-----EEFEGKVKIDGELLTAEnvwnLRRKIGMVFQNPDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 176 TVEETLMFAAEFR-LPRSlSKSKKKARVQALIDQLGLTTAantvigdEGHRgVSGGERRRVSIGIDIIHDPILLFLDEPT 254
Cdd:PRK13642 98 TVEDDVAFGMENQgIPRE-EMIKRVDEALLAVNMLDFKTR-------EPAR-LSGGQKQRVAVAGIIALRPEIIILDEST 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 255 SGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYRILSlLDRLIFLSRGQTVYSGSPAEL---SEFLADFGHPIPenenr 331
Cdd:PRK13642 169 SMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELfatSEDMVEIGLDVP----- 242
|
250
....*....|.
gi 1281000366 332 teFALDLVRDL 342
Cdd:PRK13642 243 --FSSNLMKDL 251
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
103-304 |
2.59e-13 |
|
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: 69.77 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDAL-------ADRIAKEKLKGTVTLND----EVLesALLKVISAYVMQddll 171
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIygnylpdSGSILVRHDGGWVDLAQasprEIL--ALRRRTIGYVSQ---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 172 F----PMLTveeTLMFAAEFRLPRSLSKSKKKARVQALIDQLGL-----TTAANTVigdeghrgvSGGERRRVSIGIDII 242
Cdd:COG4778 101 FlrviPRVS---ALDVVAEPLLERGVDREEARARARELLARLNLperlwDLPPATF---------SGGEQQRVNIARGFI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1281000366 243 HDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYRiLSLLDRLIFLSRGQ 304
Cdd:COG4778 169 ADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVR-EAVADRVVDVTPFS 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
89-310 |
7.40e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.81 E-value: 7.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 89 NLTAEENGGRVKLLLNdISGEAREGEIMAVLGASGSGKStlIDALADRIAKEKLKGTVTLNDEVLESALLKVIS------ 162
Cdd:PRK10261 19 NIAFMQEQQKIAAVRN-LSFSLQRGETLAIVGESGSGKS--VTALALMRLLEQAGGLVQCDKMLLRRRSRQVIElseqsa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 163 -----------AYVMQDDL--LFPMLTVEETLmfAAEFRLPRSLSKSKKKARVQALIDQLGLTTAaNTVIGDEGHRgVSG 229
Cdd:PRK10261 96 aqmrhvrgadmAMIFQEPMtsLNPVFTVGEQI--AESIRLHQGASREEAMVEAKRMLDQVRIPEA-QTILSRYPHQ-LSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 230 GERRRVSIGIDIIHDPILLFLDEPTSGLDST---SAFMVVKVLQRIAQSGSIVITsiHQPSYrILSLLDRLIFLSRGQTV 306
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTiqaQILQLIKVLQKEMSMGVIFIT--HDMGV-VAEIADRVLVMYQGEAV 248
|
....
gi 1281000366 307 YSGS 310
Cdd:PRK10261 249 ETGS 252
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
100-311 |
8.27e-13 |
|
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: 68.29 E-value: 8.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALAdRIAkEKLKGTVTLND--------EVLESALlkvisAYVMQDDLL 171
Cdd:cd03244 17 PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALF-RLV-ELSSGSILIDGvdiskiglHDLRSRI-----SIIPQDPVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 172 FPMlTVEETLMF---AAEFRLPRSLSKSKKKARVQALIDQLglttaaNTVIgDEGHRGVSGGERRRVSIGIDIIHDPILL 248
Cdd:cd03244 90 FSG-TIRSNLDPfgeYSDEELWQALERVGLKEFVESLPGGL------DTVV-EEGGENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281000366 249 FLDEPTSGLDSTSAFMVVKVLQRiAQSGSIVITSIHqpsyRILSLL--DRLIFLSRGQTVYSGSP 311
Cdd:cd03244 162 VLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAH----RLDTIIdsDRILVLDKGRVVEFDSP 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
113-315 |
8.90e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.24 E-value: 8.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 113 GEIMAVLGASGSGKSTLIDALADRIAKEklKGTVTLNDEV---LESALLKVISAY-VMQDDLLFPMLTVEETLMfaaeFR 188
Cdd:PRK15439 37 GEVHALLGGNGAGKSTLMKIIAGIVPPD--SGTLEIGGNPcarLTPAKAHQLGIYlVPQEPLLFPNLSVKENIL----FG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 189 LPRS-LSKSKKKARVQALIDQLGLTTAANTV-IGDeghrgvsggeRRRVSIGIDIIHDPILLFLDEPTSGL---DSTSAF 263
Cdd:PRK15439 111 LPKRqASMQKMKQLLAALGCQLDLDSSAGSLeVAD----------RQIVEILRGLMRDSRILILDEPTASLtpaETERLF 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1281000366 264 MVVKVLQriAQSGSIVITSIHQPSYRILSllDRLIFLSRGQTVYSGSPAELS 315
Cdd:PRK15439 181 SRIRELL--AQGVGIVFISHKLPEIRQLA--DRISVMRDGTIALSGKTADLS 228
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
108-313 |
1.02e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 68.59 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 108 GEAREGEIMAVLGASGSGKSTLIDALADRIAKeklkgtvtlnDEVLESALLKVIS---AYVMQDdllFPMlTVEETLMFa 184
Cdd:cd03237 20 GSISESEVIGILGPNGIGKTTFIKMLAGVLKP----------DEGDIEIELDTVSykpQYIKAD---YEG-TVRDLLSS- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 185 aefRLPRSLSKSKKKARVqalIDQLGLTTaantvIGDEGHRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFM 264
Cdd:cd03237 85 ---ITKDFYTHPYFKTEI---AKPLQIEQ-----ILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1281000366 265 VVKVLQRIAQSGSIVITSIHQPSYRILSLLDRLIflsrgqtVYSGSPAE 313
Cdd:cd03237 154 ASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLI-------VFEGEPSV 195
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
104-324 |
1.51e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 69.67 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 104 NDISGEAREGEIMAVLGASGSGKSTL---IDALADRIAKEKLKGTVTLNDevLESALLKVisAYVMQDDLLFPMLTVEET 180
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLlrmIAGLEDITSGDLFIGEKRMND--VPPAERGV--GMVFQSYALYPHLSVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 181 LMFAAEfrlprsLSKSKK---KARVQALIDQLGLttaantvigdeGH------RGVSGGERRRVSIGIDIIHDPILLFLD 251
Cdd:PRK11000 96 MSFGLK------LAGAKKeeiNQRVNQVAEVLQL-----------AHlldrkpKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 252 EPTSGLDstsAFMVVKVLQRIA----QSGSIVITSIHQpSYRILSLLDRLIFLSRGQTVYSGSPAEL-----SEFLADF- 321
Cdd:PRK11000 159 EPLSNLD---AALRVQMRIEISrlhkRLGRTMIYVTHD-QVEAMTLADKIVVLDAGRVAQVGKPLELyhypaNRFVAGFi 234
|
...
gi 1281000366 322 GHP 324
Cdd:PRK11000 235 GSP 237
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
98-304 |
1.71e-12 |
|
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: 66.30 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 98 RVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADriAKEKLKGTVTLNDEvlESALLKVISAyvmqddllfpmltV 177
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFG--LRPPASGEITLDGK--PVTRRSPRDA-------------I 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 178 EETLMFAAEFRlprslskskkkaRVQALIdqLGLTTAANTVIGdeghRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGL 257
Cdd:cd03215 74 RAGIAYVPEDR------------KREGLV--LDLSVAENIALS----SLLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1281000366 258 D-STSAFmVVKVLQRIAQSG-SIVITSIHQPSyrILSLLDRLIFLSRGQ 304
Cdd:cd03215 136 DvGAKAE-IYRLIRELADAGkAVLLISSELDE--LLGLCDRILVMYEGR 181
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
103-308 |
1.75e-12 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 65.91 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEvlesallkvisayvmqddllfpmltveetlm 182
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDS--GEILVDGK------------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 183 fAAEFRLPRSlsksKKKARVqALIDQLglttaantvigdeghrgvSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSA 262
Cdd:cd03216 63 -EVSFASPRD----ARRAGI-AMVYQL------------------SVGERQMVEIARALARNARLLILDEPTAALTPAEV 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1281000366 263 FMVVKVLQRIAQSG-SIVITSiHQPSyRILSLLDRLIFLSRGQTVYS 308
Cdd:cd03216 119 ERLFKVIRRLRAQGvAVIFIS-HRLD-EVFEIADRVTVLRDGRVVGT 163
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
103-284 |
2.18e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.99 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALAD--RIAKeklkGTVTLNDEVLESALLKVISAYVMQD---DLLFPMLtV 177
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGfvRLAS----GKISILGQPTRQALQKNLVAYVPQSeevDWSFPVL-V 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 178 EETLMFA-----AEFRLPrslsKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLDE 252
Cdd:PRK15056 98 EDVVMMGryghmGWLRRA----KKRDRQIVTAALARVDMVEFRHRQIGE-----LSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190
....*....|....*....|....*....|..
gi 1281000366 253 PTSGLDSTSAFMVVKVLQRIAQSGSIVITSIH 284
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRDEGKTMLVSTH 200
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
109-258 |
5.20e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.14 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 109 EAREGEIMAVLGASGSGKSTLIDALADRIAKEklKGTVTLN--DEVLESALLKVISAyVMQDDLLFPMLTVEET--LMFA 184
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNLIAGFLTPA--SGSLTLNgqDHTTTPPSRRPVSM-LFQENNLFSHLTVAQNigLGLN 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281000366 185 AEFRLprslsKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDII-HDPILLfLDEPTSGLD 258
Cdd:PRK10771 98 PGLKL-----NAAQREKLHAIARQMGIEDLLARLPGQ-----LSGGQRQRVALARCLVrEQPILL-LDEPFSALD 161
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
79-360 |
5.68e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.42 E-value: 5.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 79 VRRRGSSLPENLTAEENGGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADriakeklkgtvtlNDEVLESALL 158
Cdd:PTZ00243 652 TSERSAKTPKMKTDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLS-------------QFEISEGRVW 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 159 KVIS-AYVMQDDLLFPMlTVEETLMFAAEFRLPRsLSKSKKKARVQALIDQLGltTAANTVIGDEGhRGVSGGERRRVSI 237
Cdd:PTZ00243 719 AERSiAYVPQQAWIMNA-TVRGNILFFDEEDAAR-LADAVRVSQLEADLAQLG--GGLETEIGEKG-VNLSGGQKARVSL 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 238 GIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQpsYRILSLLDRLIFLSRGQTVYSGSPAEL--S 315
Cdd:PTZ00243 794 ARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQ--VHVVPRADYVVALGDGRVEFSGSSADFmrT 871
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1281000366 316 EFLADFGHPIPENENRTEFALDLVRDLEETAGGTRSMVEHNKSWQ 360
Cdd:PTZ00243 872 SLYATLAAELKENKDSKEGDADAEVAEVDAAPGGAVDHEPPVAKQ 916
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
103-318 |
5.79e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 68.68 E-value: 5.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKLKGTVTLNDE--------VLESALLKVISAYVMQDDLLFPM 174
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEwvdmtkpgPDGRGRAKRYIGILHQEYDLYPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 175 LTVEETLMFAAEFRLPRSLskskkkARVQALI--DQLGLTTAANTVIGDEGHRGVSGGERRRVSIGIDIIHDPILLFLDE 252
Cdd:TIGR03269 380 RTVLDNLTEAIGLELPDEL------ARMKAVItlKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDE 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1281000366 253 PTSGLDSTSAFMVVKVL--QRIAQSGSIVITSiHQPSYrILSLLDRLIFLSRGQTVYSGSPAELSEFL 318
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSIlkAREEMEQTFIIVS-HDMDF-VLDVCDRAALMRDGKIVKIGDPEEIVEEL 519
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
100-314 |
7.05e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 66.34 E-value: 7.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTL---IDALADRIAKEKLKGTVTLNDEVLESA------LLKVIsAYVMQDDL 170
Cdd:PRK14239 18 KKALNSVSLDFYPNEITALIGPSGSGKSTLlrsINRMNDLNPEVTITGSIVYNGHNIYSPrtdtvdLRKEI-GMVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 171 LFPMlTVEETLMFAAEfrlprsLSKSKKKARVQALIDQlGLTTAAntvIGDE-------GHRGVSGGERRRVSIGIDIIH 243
Cdd:PRK14239 97 PFPM-SIYENVVYGLR------LKGIKDKQVLDEAVEK-SLKGAS---IWDEvkdrlhdSALGLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1281000366 244 DPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVIT--SIHQPSyRIlslLDRLIFLSRGQTVYSGSPAEL 314
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVtrSMQQAS-RI---SDRTGFFLDGDLIEYNDTKQM 234
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
103-314 |
7.10e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 66.75 E-value: 7.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALaDRIAKEKlKGTVTLNDEVLESALLKVISAYV-----MQDDLLFPMlTV 177
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHF-NGILKPT-SGSVLIRGEPITKENIREVRKFVglvfqNPDDQIFSP-TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 178 EETLMFAAefrLPRSLSKSKKKARVQALIDQLGLTTaantvIGDEGHRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGL 257
Cdd:PRK13652 97 EQDIAFGP---INLGLDEETVAHRVSSALHMLGLEE-----LRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1281000366 258 DSTSAFMVVKVLQRIAQS-GSIVITSIHQPSYrILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:PRK13652 169 DPQGVKELIDFLNDLPETyGMTVIFSTHQLDL-VPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
113-258 |
8.15e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.57 E-value: 8.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 113 GEIMAVLGASGSGKSTLIDALA---DRIAKE-KLKG-TVTLNDEVLESALLKVISAYVMQDDLLFPMLTVEETLMFAAef 187
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAgldDGSSGEvSLVGqPLHQMDEEARAKLRAKHVGFVFQSFMLIPTLNALENVELPA-- 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1281000366 188 rLPRSLSKSKKKARVQALIDQLGLttaantvigdeGHR------GVSGGERRRVSIGIDIIHDPILLFLDEPTSGLD 258
Cdd:PRK10584 114 -LLRGESSRQSRNGAKALLEQLGL-----------GKRldhlpaQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
100-314 |
8.66e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 66.22 E-value: 8.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRI----AKEKLKGTVT-LNDEVLESALLKVIS--AYVMQDDLLF 172
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydSKIKVDGKVLyFGKDIFQIDAIKLRKevGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 173 PMLTVEETLMFaaefrlPRSLSKSKKKARVQALIDQ----LGLTTAANTVIGDEGHRgVSGGERRRVSIGIDIIHDPILL 248
Cdd:PRK14246 103 PHLSIYDNIAY------PLKSHGIKEKREIKKIVEEclrkVGLWKEVYDRLNSPASQ-LSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1281000366 249 FLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSiHQPSyRILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVS-HNPQ-QVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
102-297 |
9.17e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.61 E-value: 9.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 102 LLNDISGEAREGEIMAVLGASGSGKSTLIDALADRiakeklkGTVTLNDEVLESALLKVISA------------YVMQDD 169
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-------DTPTSGDVIFNGQPMSKLSSaakaelrnqklgFIYQFH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 170 LLFPMLTVEETLMfaaefrLPRSLSKSKKK---ARVQALIDQLGLTTAANtvigdegHRG--VSGGERRRVSIGIDIIHD 244
Cdd:PRK11629 97 HLLPDFTALENVA------MPLLIGKKKPAeinSRALEMLAAVGLEHRAN-------HRPseLSGGERQRVAIARALVNN 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1281000366 245 PILLFLDEPTSGLDSTSAFMVVKVLQRI-AQSGSIVITSIHQpsyriLSLLDRL 297
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHD-----LQLAKRM 212
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
100-306 |
9.70e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 65.86 E-value: 9.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALadrIAKEK-LKGTVTLNDEVLESALLKVISAY------VMQDDL-- 170
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLL---VGLESpSQGNVSWRGEPLAKLNRAQRKAFrrdiqmVFQDSIsa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 171 LFPMLTVEETLmfAAEFRLPRSLSKSKKKARVQALIDQLGLTTAantvIGDEGHRGVSGGERRRVSIGIDIIHDPILLFL 250
Cdd:PRK10419 102 VNPRKTVREII--REPLRHLLSLDKAERLARASEMLRAVDLDDS----VLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1281000366 251 DEPTSGLD---STSAFMVVKVLQRiaQSGSIVITSIHQpsyriLSLLD----RLIFLSRGQTV 306
Cdd:PRK10419 176 DEAVSNLDlvlQAGVIRLLKKLQQ--QFGTACLFITHD-----LRLVErfcqRVMVMDNGQIV 231
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
103-314 |
1.36e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.90 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADriAKEKLKGTVTLNDEVLE----SALLKVISAYVMQDDLLFPMLTVE 178
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG--DPRATSGRIVFDGKDITdwqtAKIMREAVAIVPEGRRVFSRMTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 179 ETLMFAAEFrlPRSLSKSKKKARVQALIDQLGLTTA--ANTVigdeghrgvSGGERRRVSIGIDIIHDPILLFLDEPTSG 256
Cdd:PRK11614 99 ENLAMGGFF--AERDQFQERIKWVYELFPRLHERRIqrAGTM---------SGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1281000366 257 LDSTSAFMVVKVLQRIAQSGsIVITSIHQPSYRILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:PRK11614 168 LAPIIIQQIFDTIEQLREQG-MTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDAL 224
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
103-360 |
1.47e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 65.96 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLN---------DEVLESALLKVISAYVMQDDLLFP 173
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALL--KPTTGTVTVDditithktkDKYIRPVRKRIGMVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 174 MlTVEETLMFAAE-FRLPRSlsksKKKARVQALIDQLGLTTAantvIGDEGHRGVSGGERRRVSIGIDIIHDPILLFLDE 252
Cdd:PRK13646 101 D-TVEREIIFGPKnFKMNLD----EVKNYAHRLLMDLGFSRD----VMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 253 PTSGLDSTSAFMVVKVLQRIA--QSGSIVITSiHQPSyRILSLLDRLIFLSRGQTVYSGSPAEL---SEFLADFGHPIPE 327
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQtdENKTIILVS-HDMN-EVARYADEVIVMKEGSIVSQTSPKELfkdKKKLADWHIGLPE 249
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1281000366 328 nenrtefALDLVRDLEE--------TAGGTRSMVEHNKSWQ 360
Cdd:PRK13646 250 -------IVQLQYDFEQkyqtklkdIALTEEEFVSLYKEWQ 283
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
67-304 |
1.55e-11 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 64.80 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 67 KLSFQNLSYSVKVRrrgsslPEnltaeenggrvKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTV 146
Cdd:cd03248 11 IVKFQNVTFAYPTR------PD-----------TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQG--GQV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 147 TLNDEVL---ESALLKVISAYVMQDDLLFPMlTVEETLMFAAEFRLPRSLSKSKKKARVQALIDqlGLTTAANTVIGDEG 223
Cdd:cd03248 72 LLDGKPIsqyEHKYLHSKVSLVGQEPVLFAR-SLQDNIAYGLQSCSFECVKEAAQKAHAHSFIS--ELASGYDTEVGEKG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 224 HRgVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHqpsyriLSLL---DRLIFL 300
Cdd:cd03248 149 SQ-LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHR------LSTVeraDQILVL 221
|
....
gi 1281000366 301 SRGQ 304
Cdd:cd03248 222 DGGR 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
103-340 |
1.60e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 65.39 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKLKGTVTLNDEVLESAL--LKVISAYVMQD-DLLFPMLTVEE 179
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLqgIRKLVGIVFQNpETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 180 TLMFAAEfrlPRSLSKSKKKARVQALIDQLGLttaantviGDEGHRG---VSGGERRRVSIGIDIIHDPILLFLDEPTSG 256
Cdd:PRK13644 98 DLAFGPE---NLCLPPIEIRKRVDRALAEIGL--------EKYRHRSpktLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 257 LDSTSAFMVVKVLQRIAQSGSIVITSIHqpSYRILSLLDRLIFLSRGQTVYSGSPA-------------------ELSEF 317
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHEKGKTIVYITH--NLEELHDADRIIVMDRGKIVLEGEPEnvlsdvslqtlgltppsliELAEN 244
|
250 260
....*....|....*....|....*
gi 1281000366 318 LADFGHPIP-ENENR-TEFALDLVR 340
Cdd:PRK13644 245 LKMHGVVIPwENTSSpSSFAEEICR 269
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
88-323 |
1.63e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.05 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGgrvKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKLKGTVTLNDEVL------ESALLKVI 161
Cdd:CHL00131 11 KNLHASVNE---NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKGESIldlepeERAHLGIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 162 SAYvmQDDLLFPMLTVEETLMFAAefrlprslsKSKKKARVQALIDQLG----LTTAANTVIGDEG--HR----GVSGGE 231
Cdd:CHL00131 88 LAF--QYPIEIPGVSNADFLRLAY---------NSKRKFQGLPELDPLEfleiINEKLKLVGMDPSflSRnvneGFSGGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 232 RRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSG-SIVITSIHQpsyrilSLLDRLI-----FLSRGQT 305
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEnSIILITHYQ------RLLDYIKpdyvhVMQNGKI 230
|
250
....*....|....*...
gi 1281000366 306 VYSGSpAELSEFLADFGH 323
Cdd:CHL00131 231 IKTGD-AELAKELEKKGY 247
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
103-314 |
1.76e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 65.80 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVLESALLKVISAYVMQDDL----LFPML--- 175
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISET--GQTIVGDYAIPANLKKIKEVKRLRKEIglvfQFPEYqlf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 176 --TVEETLMFAaefrlPRSLSKSKKKA--RVQALIDQLGLTTaantvigDEGHRG---VSGGERRRVSIGIDIIHDPILL 248
Cdd:PRK13645 105 qeTIEKDIAFG-----PVNLGENKQEAykKVPELLKLVQLPE-------DYVKRSpfeLSGGQKRRVALAGIIAMDGNTL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1281000366 249 FLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYRILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:PRK13645 173 VLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
88-304 |
1.88e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGrvkllLNDISGEAREGEIMAVLGASGSGKSTLIDALADriAKEKLKGTVTLND-EVLESALLKVIS---A 163
Cdd:PRK10982 254 RNLTSLRQPS-----IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFG--IREKSAGTITLHGkKINNHNANEAINhgfA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 164 YVMQDDL---LFPMLTVEETLMFA------AEFRLprsLSKSKKKARVQALIDQLGLTTAAN-TVIGDeghrgVSGGERR 233
Cdd:PRK10982 327 LVTEERRstgIYAYLDIGFNSLISnirnykNKVGL---LDNSRMKSDTQWVIDSMRVKTPGHrTQIGS-----LSGGNQQ 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1281000366 234 RVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGS-IVITSIHQPsyRILSLLDRLIFLSRGQ 304
Cdd:PRK10982 399 KVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKgIIIISSEMP--ELLGITDRILVMSNGL 468
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
88-316 |
1.96e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.97 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAeenGGRVKlllnDISGEAREGEIMAVLGASGSGKSTLIDAL--ADRIAkeklKGTVTLNDEVLE-----SALLKV 160
Cdd:COG1129 260 EGLSV---GGVVR----DVSFSVRAGEILGIAGLVGAGRTELARALfgADPAD----SGEIRLDGKPVRirsprDAIRAG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 161 IsAYVMQDDL---LFPMLTVEETLMFAAEFRLPRS--LSKSKKKARVQALIDQLGLTTA-ANTVIGDeghrgVSGGERRR 234
Cdd:COG1129 329 I-AYVPEDRKgegLVLDLSIRENITLASLDRLSRGglLDRRRERALAEEYIKRLRIKTPsPEQPVGN-----LSGGNQQK 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 235 VSIGIDIIHDPILLFLDEPTSGLDstsafmvV-------KVLQRIAQSGS--IVITS-IHQpsyrILSLLDRLIFLSRGQ 304
Cdd:COG1129 403 VVLAKWLATDPKVLILDEPTRGID-------VgakaeiyRLIRELAAEGKavIVISSeLPE----LLGLSDRILVMREGR 471
|
250
....*....|..
gi 1281000366 305 TVYSGSPAELSE 316
Cdd:COG1129 472 IVGELDREEATE 483
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
72-309 |
2.36e-11 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 64.09 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 72 NLSYSVKVRRRGSSLPENLTAEENGGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEklKGTVTLNDE 151
Cdd:cd03220 7 SKSYPTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPD--SGTVTVRGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 152 VleSALLKVisAYVMQddllfPMLTVEETLMFAAEFrlpRSLSKSKKKARVQALIDQLGLttaantviGDEGHRGV---S 228
Cdd:cd03220 85 V--SSLLGL--GGGFN-----PELTGRENIYLNGRL---LGLSRKEIDEKIDEIIEFSEL--------GDFIDLPVktyS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 229 GGERRRVSIGIDIIHDPILLFLDEPTSGLDstSAFM--VVKVLQRIAQSGSIVITSIHQPSYrILSLLDRLIFLSRGQTV 306
Cdd:cd03220 145 SGMKARLAFAIATALEPDILLIDEVLAVGD--AAFQekCQRRLRELLKQGKTVILVSHDPSS-IKRLCDRALVLEKGKIR 221
|
...
gi 1281000366 307 YSG 309
Cdd:cd03220 222 FDG 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
107-313 |
2.49e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 66.73 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 107 SGEAREGEIMAVLGASGSGKSTLIDALADRIA--KEKLKGTVTlndevlesallkvIS---AYVMQDdllFPMlTVEETL 181
Cdd:COG1245 360 GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKpdEGEVDEDLK-------------ISykpQYISPD---YDG-TVEEFL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 182 MFAAEFRLPRSLSKSKkkarvqaLIDQLGLTTaantvIGDEGHRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTS 261
Cdd:COG1245 423 RSANTDDFGSSYYKTE-------IIKPLGLEK-----LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1281000366 262 AFMVVKVLQRIAQSGSIVITSIHQPSYRILSLLDRLIflsrgqtVYSGSPAE 313
Cdd:COG1245 491 RLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM-------VFEGEPGV 535
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
100-258 |
2.83e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 66.63 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLNDevlesallKVISAYVMQD-DLLFPMLTVE 178
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGEL--EPDSGTVKLGE--------TVKIGYFDQHqEELDPDKTVL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 179 ETLmfaaefrlpRSLSKSKKKARVQALIDQLGLTtaantviGDEGHRGV---SGGERRRVSIGIDIIHDPILLFLDEPTS 255
Cdd:COG0488 398 DEL---------RDGAPGGTEQEVRGYLGRFLFS-------GDDAFKPVgvlSGGEKARLALAKLLLSPPNVLLLDEPTN 461
|
...
gi 1281000366 256 GLD 258
Cdd:COG0488 462 HLD 464
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
98-314 |
4.29e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.08 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 98 RVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKE------KLKGTVTLNDEVLES------ALLKVISAYV 165
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgaRVTGDVTLNGEPLAAidaprlARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 166 MQDDLLFpmlTVEETLMFAaefRLPRSLSKSKKKARVQALIDQLGLTTAANTVIGdeghRGV---SGGERRRVSIGI--- 239
Cdd:PRK13547 92 AQPAFAF---SAREIVLLG---RYPHARRAGALTHRDGEIAWQALALAGATALVG----RDVttlSGGELARVQFARvla 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 240 ------DIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSI-VITSIHQPSYRIlSLLDRLIFLSRGQTVYSGSPA 312
Cdd:PRK13547 162 qlwpphDAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAA-RHADRIAMLADGAIVAHGAPA 240
|
..
gi 1281000366 313 EL 314
Cdd:PRK13547 241 DV 242
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
103-315 |
5.01e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.58 E-value: 5.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADriAKEKLKGTVTLNDEVLeSALLKVISA-----YVMQDDLLFPMLTV 177
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSG--IHEPTKGTITINNINY-NKLDHKLAAqlgigIIYQELSVIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 178 EETLMFAaefRLPRS-------LSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFL 250
Cdd:PRK09700 98 LENLYIG---RHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVAN-----LSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281000366 251 DEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSyRILSLLDRLIFLSRGQTVYSGSPAELS 315
Cdd:PRK09700 170 DEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLA-EIRRICDRYTVMKDGSSVCSGMVSDVS 233
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
57-316 |
5.05e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 65.90 E-value: 5.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 57 LAPPPVlyPFKLSFQNLSYSVKVRrrgsslPEnltaeenggrvKLLLNDISGEAREGEIMAVLGASGSGKSTLIdALADR 136
Cdd:TIGR00958 470 LAPLNL--EGLIEFQDVSFSYPNR------PD-----------VPVLKGLTFTLHPGEVVALVGPSGSGKSTVA-ALLQN 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 137 IAkEKLKGTVTLNDEVL---ESALLKVISAYVMQDDLLFPMlTVEETLMFAAEFRLPRSLSKSKKKARVQALIdqLGLTT 213
Cdd:TIGR00958 530 LY-QPTGGQVLLDGVPLvqyDHHYLHRQVALVGQEPVLFSG-SVRENIAYGLTDTPDEEIMAAAKAANAHDFI--MEFPN 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 214 AANTVIGDEGHRgVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAfmvvKVLQRIAQSGSIVITSI-HQpsyriLS 292
Cdd:TIGR00958 606 GYDTEVGEKGSQ-LSGGQKQRIAIARALVRKPRVLILDEATSALDAECE----QLLQESRSRASRTVLLIaHR-----LS 675
|
250 260
....*....|....*....|....*..
gi 1281000366 293 LL---DRLIFLSRGQTVYSGSPAELSE 316
Cdd:TIGR00958 676 TVeraDQILVLKKGSVVEMGTHKQLME 702
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
105-309 |
5.72e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.41 E-value: 5.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 105 DISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEklKGTVT--LNDEVLES----------ALLKVISAYVMQD--DL 170
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPD--AGEVHyrMRDGQLRDlyalseaerrRLLRTEWGFVHQHprDG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 171 LFPMLT----VEETLMFAAEfrlpRSLSKSKKKA-----RVQalIDQLGLttaantvigDEGHRGVSGGERRRVSIGIDI 241
Cdd:PRK11701 102 LRMQVSaggnIGERLMAVGA----RHYGDIRATAgdwleRVE--IDAARI---------DDLPTTFSGGMQQRLQIARNL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 242 IHDPILLFLDEPTSGLD-STSAFMVVKVLQRIAQSGSIVITSIHQPSY-RILSllDRLIFLSRGQTVYSG 309
Cdd:PRK11701 167 VTHPRLVFMDEPTGGLDvSVQARLLDLLRGLVRELGLAVVIVTHDLAVaRLLA--HRLLVMKQGRVVESG 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
88-274 |
6.60e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.50 E-value: 6.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLT-AEENGGRVKLLLNDISGEAREGEIMAVLGASGSGKStlIDALAD-RI----AKEKLKGTVTLNDEVL----ESAL 157
Cdd:PRK15134 9 ENLSvAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKS--VTALSIlRLlpspPVVYPSGDIRFHGESLlhasEQTL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 158 LKVIS---AYVMQDDL--LFPMLTVEETLmfAAEFRLPRSLSKSKKKARVQALIDQLGLTTAANTvIGDEGHRgVSGGER 232
Cdd:PRK15134 87 RGVRGnkiAMIFQEPMvsLNPLHTLEKQL--YEVLSLHRGMRREAARGEILNCLDRVGIRQAAKR-LTDYPHQ-LSGGER 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1281000366 233 RRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQ 274
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQ 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
111-284 |
7.40e-11 |
|
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: 66.19 E-value: 7.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 111 REGEIMAVLGASGSGKSTLIDALADriakeklKGTVTLNDE-VLESALLKVIS------AYVMQDDLLFPMLTVEETLMF 183
Cdd:TIGR01257 1963 RPGECFGLLGVNGAGKTTTFKMLTG-------DTTVTSGDAtVAGKSILTNISdvhqnmGYCPQFDAIDDLLTGREHLYL 2035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 184 AAEFR-LPrslskSKKKARVQAL-IDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTS 261
Cdd:TIGR01257 2036 YARLRgVP-----AEEIEKVANWsIQSLGLSLYADRLAGT-----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
|
170 180
....*....|....*....|...
gi 1281000366 262 AFMVVKVLQRIAQSGSIVITSIH 284
Cdd:TIGR01257 2106 RRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
89-304 |
9.29e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 9.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 89 NLTAEENGgRVKlllnDISGEAREGEIMAVLGASGSGKSTLIDAL--ADRIAKeklkGTVTLNDEVLE-----SALLKVI 161
Cdd:PRK09700 270 NVTSRDRK-KVR----DISFSVCRGEILGFAGLVGSGRTELMNCLfgVDKRAG----GEIRLNGKDISprsplDAVKKGM 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 162 sAYVMQ---DDLLFPMLTVEETLMFAAEFRLPRS------LSKSKKKARVQALIDQLGLTTAA-NTVIGDeghrgVSGGE 231
Cdd:PRK09700 341 -AYITEsrrDNGFFPNFSIAQNMAISRSLKDGGYkgamglFHEVDEQRTAENQRELLALKCHSvNQNITE-----LSGGN 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1281000366 232 RRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSG-SIVITSIHQPsyRILSLLDRLIFLSRGQ 304
Cdd:PRK09700 415 QQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGkVILMVSSELP--EIITVCDRIAVFCEGR 486
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
103-363 |
1.04e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 63.33 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALaDRIAKEKlKGTVTLNDEVLE---SALLKVISAYVM----QDDLLFPML 175
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNL-NGILKPS-SGRILFDGKPIDysrKGLMKLRESVGMvfqdPDNQLFSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 176 TVEETLMFAAEFRLPrslsKSKKKARVQALIDQLGLTTaantvIGDEGHRGVSGGERRRVSIGIDIIHDPILLFLDEPTS 255
Cdd:PRK13636 100 VYQDVSFGAVNLKLP----EDEVRKRVDNALKRTGIEH-----LKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 256 GLDSTSAFMVVKVLQRIAQSGSIVITsIHQPSYRILSLL-DRLIFLSRGQTVYSGSPAEL---SEF-------LADFGHP 324
Cdd:PRK13636 171 GLDPMGVSEIMKLLVEMQKELGLTII-IATHDIDIVPLYcDNVFVMKEGRVILQGNPKEVfaeKEMlrkvnlrLPRIGHL 249
|
250 260 270
....*....|....*....|....*....|....*....
gi 1281000366 325 IPENENRTEFALDlvrDLEETAGGTRSMVehnKSWQWKN 363
Cdd:PRK13636 250 MEILKEKDGFVFD---ELDLTISQARKTL---NSWKNKI 282
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
107-312 |
1.08e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.83 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 107 SGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLNdevlesalLKVisAYVMQ---DDllFPMlTVEETLMF 183
Cdd:PRK13409 359 GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVL--KPDEGEVDPE--------LKI--SYKPQyikPD--YDG-TVEDLLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 184 AAEfRLPRSLSKSKkkarvqaLIDQLGLTTaantvIGDEGHRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAF 263
Cdd:PRK13409 424 ITD-DLGSSYYKSE-------IIKPLQLER-----LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1281000366 264 MVVKVLQRIAQSGSIVITSIHQPSYRILSLLDRLIflsrgqtVYSGSPA 312
Cdd:PRK13409 491 AVAKAIRRIAEEREATALVVDHDIYMIDYISDRLM-------VFEGEPG 532
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
103-314 |
1.17e-10 |
|
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: 64.84 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIdaladriakeKL--------KGTVTLND----EVLESALLKVIsAYVMQDDL 170
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLA----------RLlfrfydvtSGRILIDGqdirDVTQASLRAAI-GIVPQDTV 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 171 LF------------PMLTVEEtLMFAAefrlprslskskKKARVQALIDQL--GLttaaNTVIGDeghRGV--SGGERRR 234
Cdd:COG5265 443 LFndtiayniaygrPDASEEE-VEAAA------------RAAQIHDFIESLpdGY----DTRVGE---RGLklSGGEKQR 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 235 VSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQS-GSIVI-----TSIHQpsyrilsllDRLIFLSRGQTVYS 308
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGrTTLVIahrlsTIVDA---------DEILVLEAGRIVER 573
|
....*.
gi 1281000366 309 GSPAEL 314
Cdd:COG5265 574 GTHAEL 579
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
82-304 |
1.18e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.77 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 82 RGSSLPENLTAEENGGRVklLLNDISGEAREGEIMAVLGASGSGKSTLIDALA---DRIAKEKLKGTVTLNDEVLESALL 158
Cdd:PRK11247 9 QGTPLLLNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAgleTPSAGELLAGTAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 159 kvisayvMQDDLLFPMLTVEETLMFAaefrlprsLSKSKKKARVQALiDQLGLTTAANtvigdEGHRGVSGGERRRVSIG 238
Cdd:PRK11247 87 -------FQDARLLPWKKVIDNVGLG--------LKGQWRDAALQAL-AAVGLADRAN-----EWPAALSGGQKQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1281000366 239 IDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRI-AQSGSIVITSIHQPSYRIlSLLDRLIFLSRGQ 304
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAV-AMADRVLLIEEGK 211
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
103-316 |
1.41e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.00 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEK-----LKGTVtlndevlesallkvisAYVMQDDLLFPMlTV 177
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtssvvIRGSV----------------AYVPQVSWIFNA-TV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 178 EETLMFAAEFRLPRSLskskKKARVQALIDQLGLTTAAN-TVIGDEGhRGVSGGERRRVSIGIDIIHDPILLFLDEPTSG 256
Cdd:PLN03232 696 RENILFGSDFESERYW----RAIDVTALQHDLDLLPGRDlTEIGERG-VNISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 257 LDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYriLSLLDRLIFLSRGQTVYSGSPAELSE 316
Cdd:PLN03232 771 LDAHVAHQVFDSCMKDELKGKTRVLVTNQLHF--LPLMDRIILVSEGMIKEEGTFAELSK 828
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
106-314 |
1.42e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 63.22 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 106 ISGEAREGEIMAVLGASGSGKST-------LIDaLADRIAKEKLKGTVTLNDEVLESALLKVISAYV---MQDDL--LFP 173
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVsslaimgLID-YPGRVMAEKLEFNGQDLQRISEKERRNLVGAEVamiFQDPMtsLNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 174 MLTVEETLMFAaeFRLPRSLSKSKKKARVQALIDQLGLTTAANTVigDEGHRGVSGGERRRVSIGIDIIHDPILLFLDEP 253
Cdd:PRK11022 105 CYTVGFQIMEA--IKVHQGGNKKTRRQRAIDLLNQVGIPDPASRL--DVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1281000366 254 TSGLDSTSAFMVVKV---LQRIAQSGSIVITsiHQpsyriLSLL----DRLIFLSRGQTVYSGSPAEL 314
Cdd:PRK11022 181 TTALDVTIQAQIIELlleLQQKENMALVLIT--HD-----LALVaeaaHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
97-314 |
1.51e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 64.27 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 97 GRVKLLLNDISGEAREGEIMAVLGASGSGKST---LIDALADRIAKEKLKGTVTLNDEVLESalLKVISAYVMQDDLLFP 173
Cdd:PRK11176 353 GKEVPALRNINFKIPAGKTVALVGRSGSGKSTianLLTRFYDIDEGEILLDGHDLRDYTLAS--LRNQVALVSQNVHLFN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 174 MlTVEETLMFAAEFRLPR-SLSKSKKKARVQALIDQL--GLttaaNTVIGDEGhRGVSGGERRRVSIGIDIIHDPILLFL 250
Cdd:PRK11176 431 D-TIANNIAYARTEQYSReQIEEAARMAYAMDFINKMdnGL----DTVIGENG-VLLSGGQRQRIAIARALLRDSPILIL 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1281000366 251 DEPTSGLDSTSAFMVVKVLQRIAQS-GSIVITsiHQpsyriLSLL---DRLIFLSRGQTVYSGSPAEL 314
Cdd:PRK11176 505 DEATSALDTESERAIQAALDELQKNrTSLVIA--HR-----LSTIekaDEILVVEDGEIVERGTHAEL 565
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
86-314 |
1.69e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 63.51 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 86 LPENLTAEENGgrVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLN--------DEVLESAL 157
Cdd:PRK10070 29 LSKEQILEKTG--LSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLI--EPTRGQVLIDgvdiakisDAELREVR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 158 LKVIsAYVMQDDLLFPMLTVEETLMFAAEFrlpRSLSKSKKKARVQALIDQLGLTTAANTViGDEghrgVSGGERRRVSI 237
Cdd:PRK10070 105 RKKI-AMVFQSFALMPHMTVLDNTAFGMEL---AGINAEERREKALDALRQVGLENYAHSY-PDE----LSGGMRQRVGL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1281000366 238 GIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYRILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:PRK10070 176 ARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
97-321 |
1.84e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 63.18 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 97 GRVKLLlNDISGEAREGEIMAVLGASGSGKSTLIDALA----DRIAKEKLKGT----VTLNDEvlesallKVisAYVMQD 168
Cdd:PRK10851 13 GRTQVL-NDISLDIPSGQMVALLGPSGSGKTTLLRIIAglehQTSGHIRFHGTdvsrLHARDR-------KV--GFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 169 DLLFPMLTVEETLMFAAEFrLPRSLSKSKK--KARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPI 246
Cdd:PRK10851 83 YALFRHMTVFDNIAFGLTV-LPRRERPNAAaiKAKVTQLLEMVQLAHLADRYPAQ-----LSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 247 LLFLDEPTSGLDStsafMVVKVLQRIAQS-------GSIVITSIHQPSyriLSLLDRLIFLSRGQTVYSGSPAEL----- 314
Cdd:PRK10851 157 ILLLDEPFGALDA----QVRKELRRWLRQlheelkfTSVFVTHDQEEA---MEVADRVVVMSQGNIEQAGTPDQVwrepa 229
|
....*..
gi 1281000366 315 SEFLADF 321
Cdd:PRK10851 230 TRFVLEF 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
88-316 |
1.89e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.89 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGRVKLllNDISGEAREGEIMAVLGASGSGKSTLIDALA--DRIAkeklKGTVTLNDEVLESA------LLK 159
Cdd:COG3845 261 ENLSVRDDRGVPAL--KDVSLEVRAGEILGIAGVAGNGQSELAEALAglRPPA----SGSIRLDGEDITGLsprerrRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 160 VisAYVMQDDL---LFPMLTVEETLMFAAEFRLPRS----LSKSKKKARVQALIDQLGL-TTAANTVIgdeghRGVSGGE 231
Cdd:COG3845 335 V--AYIPEDRLgrgLVPDMSVAENLILGRYRRPPFSrggfLDRKAIRAFAEELIEEFDVrTPGPDTPA-----RSLSGGN 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 232 RRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVL--QRIAQSGSIVItsihqpSY---RILSLLDRLIFLSRGQTV 306
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLleLRDAGAAVLLI------SEdldEILALSDRIAVMYEGRIV 481
|
250
....*....|
gi 1281000366 307 YSGSPAELSE 316
Cdd:COG3845 482 GEVPAAEATR 491
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
103-321 |
1.96e-10 |
|
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: 64.58 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLNDEVlesallkvisAYV-----MQDDllfpmlTV 177
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEM--DKVEGHVHMKGSV----------AYVpqqawIQND------SL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 178 EETLMFAaefrlpRSLSKSKKKARVQA---LIDQLGLTTAANTVIGDEGhRGVSGGERRRVSIGIDIIHDPILLFLDEPT 254
Cdd:TIGR00957 716 RENILFG------KALNEKYYQQVLEAcalLPDLEILPSGDRTEIGEKG-VNLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1281000366 255 SGLDSTSAFM----VVKVLQRIAQSGSIVITsiHQPSYriLSLLDRLIFLSRGQTVYSGSPAEL-------SEFLADF 321
Cdd:TIGR00957 789 SAVDAHVGKHifehVIGPEGVLKNKTRILVT--HGISY--LPQVDVIIVMSGGKISEMGSYQELlqrdgafAEFLRTY 862
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
88-293 |
2.32e-10 |
|
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: 60.58 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEEnGGRVklLLNDISGEAREGEIMAVLGASGSGKSTLIDALADriAKEKLKGTVTLNDEVLESALLKVISA--YV 165
Cdd:cd03231 4 DELTCER-DGRA--LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAG--LSPPLAGRVLLNGGPLDFQRDSIARGllYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 166 MQDDLLFPMLTVEETLMFAAEFRlprslskskKKARVQALIDQLGLTTaantvIGDEGHRGVSGGERRRVSIGIDIIHDP 245
Cdd:cd03231 79 GHAPGIKTTLSVLENLRFWHADH---------SDEQVEEALARVGLNG-----FEDRPVAQLSAGQQRRVALARLLLSGR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1281000366 246 ILLFLDEPTSGLDSTSafmVVKVLQRIA---QSGSIVITSIHQP------SYRILSL 293
Cdd:cd03231 145 PLWILDEPTTALDKAG---VARFAEAMAghcARGGMVVLTTHQDlglseaGARELDL 198
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
102-314 |
3.30e-10 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 63.61 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 102 LLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLN----DEVLESALLKVISaYVMQDDLLFPMLTV 177
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARS--GEILLNgfslKDIDRHTLRQFIN-YLPQEPYIFSGSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 178 EETLMFAAEFRLPRSLSKSKKKARVQALIDQLGLttAANTVIGDEGHrGVSGGERRRVSIGIDIIHDPILLFLDEPTSGL 257
Cdd:TIGR01193 566 ENLLLGAKENVSQDEIWAACEIAEIKDDIENMPL--GYQTELSEEGS-SISGGQKQRIALARALLTDSKVLILDESTSNL 642
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1281000366 258 DSTSAFMVVKVLQRIAQSGSIVITsiHQPSyrILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:TIGR01193 643 DTITEKKIVNNLLNLQDKTIIFVA--HRLS--VAKQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
103-324 |
4.86e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.78 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALA--DRIAKeklkGTVTLNDEV---LESALLKVisAYVMQDDLLFPMLTV 177
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAglERITS----GEIWIGGRVvneLEPADRDI--AMVFQNYALYPHMSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 178 EETLMFAAEFRlprSLSKSKKKARVQAlidqlglttAANTV-IG---DEGHRGVSGGERRRVSIGIDIIHDPILLFLDEP 253
Cdd:PRK11650 94 RENMAYGLKIR---GMPKAEIEERVAE---------AARILeLEpllDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 254 TSGLDST-SAFMVV--KVLQRIAQSGSIVITsiH-QpsYRILSLLDRLIFLSRGQTVYSGSPAEL-----SEFLADF-GH 323
Cdd:PRK11650 162 LSNLDAKlRVQMRLeiQRLHRRLKTTSLYVT--HdQ--VEAMTLADRVVVMNGGVAEQIGTPVEVyekpaSTFVASFiGS 237
|
.
gi 1281000366 324 P 324
Cdd:PRK11650 238 P 238
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
97-314 |
5.77e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.31 E-value: 5.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 97 GRVKLLlNDISGEAREGEIMAVLGASGSGKSTLI---DALADRIAKEKLKGTVTLNDE---VLESALLKVISAYVMQDDL 170
Cdd:PRK14247 14 GQVEVL-DGVNLEIPDNTITALMGPSGSGKSTLLrvfNRLIELYPEARVSGEVYLDGQdifKMDVIELRRRVQMVFQIPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 171 LFPMLTVEETLmfAAEFRLPRsLSKSKKK--ARVQALIDQLGLTTAANTVIGDEGHRgVSGGERRRVSIGIDIIHDPILL 248
Cdd:PRK14247 93 PIPNLSIFENV--ALGLKLNR-LVKSKKElqERVRWALEKAQLWDEVKDRLDAPAGK-LSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1281000366 249 FLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSiHQPSyRILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKDMTIVLVT-HFPQ-QAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
115-314 |
6.26e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.79 E-value: 6.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 115 IMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVLESA-----LLKVISAYVMQD-DLLFPMLTVEETLMFAAefr 188
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQK--GAVLWQGKPLDYSkrgllALRQQVATVFQDpEQQIFYTDIDSDIAFSL--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 189 lpRSLSKSKkkARVQALIDQlglttaANTVIGDEGHRG-----VSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAF 263
Cdd:PRK13638 104 --RNLGVPE--AEITRRVDE------ALTLVDAQHFRHqpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1281000366 264 MVVKVLQRIAQSGSIVITSIHQPSYrILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:PRK13638 174 QMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
88-293 |
7.17e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.43 E-value: 7.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEEnGGRVklLLNDISGEAREGEIMAVLGASGSGKSTL---IDALADRIAkeklkGTVTLNDEvlesALLKVISAY 164
Cdd:PRK13538 5 RNLACER-DERI--LFSGLSFTLNAGELVQIEGPNGAGKTSLlriLAGLARPDA-----GEVLWQGE----PIRRQRDEY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 165 vmQDDLLF--------PMLTVEETLMFAAefRLPRSLSkskKKARVQALiDQLGLT----TAANTvigdeghrgVSGGER 232
Cdd:PRK13538 73 --HQDLLYlghqpgikTELTALENLRFYQ--RLHGPGD---DEALWEAL-AQVGLAgfedVPVRQ---------LSAGQQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1281000366 233 RRVSIGIDIIHDPILLFLDEPTSGLDSTSafmvVKVLQRI----AQSGSIVITSIHQP------SYRILSL 293
Cdd:PRK13538 136 RRVALARLWLTRAPLWILDEPFTAIDKQG----VARLEALlaqhAEQGGMVILTTHQDlpvasdKVRKLRL 202
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
100-321 |
7.58e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 61.50 E-value: 7.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALAdriAKEKL-KGTVTLNDEVLESallkvISA------YVMQDDLLF 172
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIA---GFETPdSGRIMLDGQDITH-----VPAenrhvnTVFQSYALF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 173 PMLTVEETLMFAaeFRLpRSLSKSKKKARVqalIDQLGLTTAANTviGDEGHRGVSGGERRRVSIGIDIIHDPILLFLDE 252
Cdd:PRK09452 99 PHMTVFENVAFG--LRM-QKTPAAEITPRV---MEALRMVQLEEF--AQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 253 PTSGLD---STSAFMVVKVLQRiaQSGsivITSI---HQPSyRILSLLDRLIFLSRGQTVYSGSPAELSE-----FLADF 321
Cdd:PRK09452 171 SLSALDyklRKQMQNELKALQR--KLG---ITFVfvtHDQE-EALTMSDRIVVMRDGRIEQDGTPREIYEepknlFVARF 244
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
88-304 |
9.83e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 61.76 E-value: 9.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADrIAKEKLKGTVTLNDEVLE-SALLKVIS---A 163
Cdd:TIGR02633 261 RNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKFEGNVFINGKPVDiRNPAQAIRagiA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 164 YVMQD---DLLFPMLTVEETLMFAA--EFRLPRSLSKSKKKARVQALIDQLGLTTAANTV-IGdeghrGVSGGERRRVSI 237
Cdd:TIGR02633 340 MVPEDrkrHGIVPILGVGKNITLSVlkSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLpIG-----RLSGGNQQKAVL 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1281000366 238 GIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSG-SIVITSIHQPsyRILSLLDRLIFLSRGQ 304
Cdd:TIGR02633 415 AKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGvAIIVVSSELA--EVLGLSDRVLVIGEGK 480
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
100-316 |
1.69e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.39 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVL----ESALLKVISAYVM--QDDLLFP 173
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDH--GEILFDGENIpamsRSRLYTVRKRMSMlfQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 174 MLTVEETLMFA--AEFRLPRSLSKSKKKARVQALidqlGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLD 251
Cdd:PRK11831 98 DMNVFDNVAYPlrEHTQLPAPLLHSTVMMKLEAV----GLRGAAKLMPSE-----LSGGMARRAALARAIALEPDLIMFD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281000366 252 EPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYRILSLLDRLIFLSRGQTVYSGSPAELSE 316
Cdd:PRK11831 169 EPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
75-258 |
2.09e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 59.59 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 75 YSVKvrrRGSSLPEnltaeengGRVKLLlNDISGEAREGEIMAVLGASGSGKSTLIDALAdrIAKEKLKGTVTLNDEVL- 153
Cdd:PRK11308 15 YPVK---RGLFKPE--------RLVKAL-DGVSFTLERGKTLAVVGESGCGKSTLARLLT--MIETPTGGELYYQGQDLl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 154 -----ESALLKVISAYVMQDDL--LFPMLTVEETLmfAAEFRLPRSLSKSKKKARVQALIDQLGLTTAantvigdegHRG 226
Cdd:PRK11308 81 kadpeAQKLLRQKIQIVFQNPYgsLNPRKKVGQIL--EEPLLINTSLSAAERREKALAMMAKVGLRPE---------HYD 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 1281000366 227 -----VSGGERRRVSIGIDIIHDPILLFLDEPTSGLD 258
Cdd:PRK11308 150 ryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
102-280 |
2.09e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.19 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 102 LLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVLES----ALLKVISaYVMQDDLLFPMlTV 177
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTS--GTLLFEGEDISTlkpeIYRQQVS-YCAQTPTLFGD-TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 178 EETLMFAAEFRlprslsksKKKARVQALIDQLGLTTAANTVIgDEGHRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGL 257
Cdd:PRK10247 98 YDNLIFPWQIR--------NQQPDPAIFLDDLERFALPDTIL-TKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180
....*....|....*....|...
gi 1281000366 258 DSTSAFMVVKVLQRIAQSGSIVI 280
Cdd:PRK10247 169 DESNKHNVNEIIHRYVREQNIAV 191
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
103-304 |
2.28e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.40 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVL-----ESALLKVIsAYVMQD---DLLFPM 174
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTS--GYVTLDGHEVvtrspQDGLANGI-VYISEDrkrDGLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 175 LTVEETLMFAAEFRLPRSLSKSKKKARVQALIDQLGL----TTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFL 250
Cdd:PRK10762 345 MSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRLfnikTPSMEQAIGL-----LSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1281000366 251 DEPTSGLDSTSAFMVVKVLQRIAQSG-SIVITSIHQPsyRILSLLDRLIFLSRGQ 304
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLINQFKAEGlSIILVSSEMP--EVLGMSDRILVMHEGR 472
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
100-282 |
2.53e-09 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 56.30 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEklKGTVTLNDevlesallKVISAYVmqddllfpmltvee 179
Cdd:cd03221 13 KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPD--EGIVTWGS--------TVKIGYF-------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 180 tlmfaaefrlprslskskkkarvqaliDQLglttaantvigdeghrgvSGGERRRVSIGIDIIHDPILLFLDEPTSGLDS 259
Cdd:cd03221 69 ---------------------------EQL------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
170 180
....*....|....*....|....*
gi 1281000366 260 TSafmvVKVLQR--IAQSGSIVITS 282
Cdd:cd03221 104 ES----IEALEEalKEYPGTVILVS 124
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
104-260 |
3.02e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 59.35 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 104 NDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKE-KLKGTVTLN-DEVL---ESALLKVIS---AYVMQDDL--LFP 173
Cdd:PRK09473 33 NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgRIGGSATFNgREILnlpEKELNKLRAeqiSMIFQDPMtsLNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 174 MLTVEETLMfaAEFRLPRSLSKSKKKARVQALIDQLGLTTAANTvIGDEGHRgVSGGERRRVSIGIDIIHDPILLFLDEP 253
Cdd:PRK09473 113 YMRVGEQLM--EVLMLHKGMSKAEAFEESVRMLDAVKMPEARKR-MKMYPHE-FSGGMRQRVMIAMALLCRPKLLIADEP 188
|
....*..
gi 1281000366 254 TSGLDST 260
Cdd:PRK09473 189 TTALDVT 195
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
88-275 |
3.35e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.17 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGgrvkLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAK--EKLKGTVTLNDEVLESALLKVIS-AY 164
Cdd:PRK10418 8 RNIALQAAQ----PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvRQTAGRVLLDGKPVAPCALRGRKiAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 165 VMQD--DLLFPMLT----VEETLmfaaefrlpRSLSKSKKKARVQALIDQLGLttaantvigDEGHR-------GVSGGE 231
Cdd:PRK10418 84 IMQNprSAFNPLHTmhthARETC---------LALGKPADDATLTAALEAVGL---------ENAARvlklypfEMSGGM 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1281000366 232 RRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQS 275
Cdd:PRK10418 146 LQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQK 189
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
103-288 |
4.62e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 57.34 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLNDEVLESALLKVIS-------AYVMQDDLLFPMl 175
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEM--QTLEGKVHWSNKNESEPSFEATRsrnrysvAYAAQKPWLLNA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 176 TVEETLMFAAEFrlprslskskKKARVQALIDQLGLTTAANTV-IGDE---GHRGV--SGGERRRVSIGIDIIHDPILLF 249
Cdd:cd03290 94 TVEENITFGSPF----------NKQRYKAVTDACSLQPDIDLLpFGDQteiGERGInlSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1281000366 250 LDEPTSGLDS--TSAFMVVKVLQRIAQSGSIVITSIHQPSY 288
Cdd:cd03290 164 LDDPFSALDIhlSDHLMQEGILKFLQDDKRTLVLVTHKLQY 204
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
101-258 |
4.63e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 57.69 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 101 LLLNDISGEAREGEIMAVLGASGSGKSTLIDALADriAKEKLKGTVTLNDEVLES------ALLKVISAYvmQDDLLFPM 174
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTG--FYKPTGGTILLRGQHIEGlpghqiARMGVVRTF--QHVRLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 175 LTVEETLM-----------FAAEFRLPrSLSKSKKKARVQAL--IDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDI 241
Cdd:PRK11300 95 MTVIENLLvaqhqqlktglFSGLLKTP-AFRRAESEALDRAAtwLERVGLLEHANRQAGN-----LAYGQQRRLEIARCM 168
|
170
....*....|....*..
gi 1281000366 242 IHDPILLFLDEPTSGLD 258
Cdd:PRK11300 169 VTQPEILMLDEPAAGLN 185
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
103-340 |
4.72e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 58.22 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlkGTVTLNDEVLES-ALLKVISAYVMQDDLLF--PMLTV-E 178
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQ--GSVRVDDTLITStSKNKDIKQIRKKVGLVFqfPESQLfE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 179 ETLMFAAEFRlPRSLSKSKKKARVQALiDQLGLTTAANTVIgDEGHRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGLD 258
Cdd:PRK13649 101 ETVLKDVAFG-PQNFGVSQEEAEALAR-EKLALVGISESLF-EKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 259 STSAFMVVKVLQRIAQSGSIVITSIHQPSyRILSLLDRLIFLSRGQTVYSGSPAEL---SEFLADFGHPIPEnenRTEFA 335
Cdd:PRK13649 178 PKGRKELMTLFKKLHQSGMTIVLVTHLMD-DVANYADFVYVLEKGKLVLSGKPKDIfqdVDFLEEKQLGVPK---ITKFA 253
|
....*
gi 1281000366 336 LDLVR 340
Cdd:PRK13649 254 QRLAD 258
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
103-326 |
6.15e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 57.45 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTlIDALADRIAKEKlKGTVTLNDEVLESALLKVISAY---VMQD-DLLFPMLTVE 178
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKST-IAKLMIGIEKVK-SGEIFYNNQAITDDNFEKLRKHigiVFQNpDNQFVGSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 179 ETLMFAAEfrlPRSLSKSKKKARVQALIDQLGLTTAANtvigDEGHrGVSGGERRRVSIGIDIIHDPILLFLDEPTSGLD 258
Cdd:PRK13648 103 YDVAFGLE---NHAVPYDEMHRRVSEALKQVDMLERAD----YEPN-ALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1281000366 259 STSAFMVVKVLQRIAQSGSIVITSI-HQPSYRILSllDRLIFLSRGqTVY-SGSPAEL---SEFLADFGHPIP 326
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEHNITIISItHDLSEAMEA--DHVIVMNKG-TVYkEGTPTEIfdhAEELTRIGLDLP 244
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
68-313 |
6.50e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 57.01 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 68 LSFQNLS--YSVKVRRRGSSLPENLTAEENGGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALAdRIAKEKlKGT 145
Cdd:COG1134 5 IEVENVSksYRLYHEPSRSLKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIA-GILEPT-SGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 146 VTLNDEVleSALLKVISAYVmqddllfPMLTVEETLMFAAefRLpRSLSKSKKKARVQALIDQLGlttaantvIGDEGHR 225
Cdd:COG1134 83 VEVNGRV--SALLELGAGFH-------PELTGRENIYLNG--RL-LGLSRKEIDEKFDEIVEFAE--------LGDFIDQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 226 GV---SGGERRR----VSIGIDiiHDpILLfLDEPTSGLDstSAFMvVKVLQRI----AQSGSIVITSiHQPSYrILSLL 294
Cdd:COG1134 143 PVktySSGMRARlafaVATAVD--PD-ILL-VDEVLAVGD--AAFQ-KKCLARIrelrESGRTVIFVS-HSMGA-VRRLC 213
|
250
....*....|....*....
gi 1281000366 295 DRLIFLSRGQTVYSGSPAE 313
Cdd:COG1134 214 DRAIWLEKGRLVMDGDPEE 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
88-304 |
6.56e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.79 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDAL--ADRIAKEklkGTVTLNDEVLE-SALLKVIS-- 162
Cdd:PRK13549 263 RNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfgAYPGRWE---GEIFIDGKPVKiRNPQQAIAqg 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 163 -AYVMQD---DLLFPMLTVEETLMFAA--EFRLPRSLSKSKKKARVQALIDQLGLTTAANTV-IGdeghrGVSGGERRRV 235
Cdd:PRK13549 340 iAMVPEDrkrDGIVPVMGVGKNITLAAldRFTGGSRIDDAAELKTILESIQRLKVKTASPELaIA-----RLSGGNQQKA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 236 SIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSG-SIVITSIHQPsyRILSLLDRLIFLSRGQ 304
Cdd:PRK13549 415 VLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGvAIIVISSELP--EVLGLSDRVLVMHEGK 482
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
111-297 |
7.75e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.99 E-value: 7.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 111 REGEIMAVLGASGSGKSTLIDALAdriakeklkGTVTLN----------DEVLE----SALLKVISAyvMQDDLLFPMLT 176
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILA---------GKLKPNlgkfddppdwDEILDefrgSELQNYFTK--LLEGDVKVIVK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 177 VEETlmfaaeFRLPRS--------LSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILL 248
Cdd:cd03236 93 PQYV------DLIPKAvkgkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQ-----LSGGELQRVAIAAALARDADFY 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1281000366 249 FLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQpsyriLSLLDRL 297
Cdd:cd03236 162 FFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHD-----LAVLDYL 205
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
100-314 |
9.72e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.03 E-value: 9.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALA---DRIAKEKLKGTVTLND-------EVLEsalLKVISAYVMQDD 169
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNrmnDKVSGYRYSGDVLLGGrsifnyrDVLE---FRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 170 LLFPMLTVEETLmfaAEFRLPRSLSKSKKKARVQALIDQLGLTTAANTVIGDEGHRgVSGGERRRVSIGIDIIHDPILLF 249
Cdd:PRK14271 111 NPFPMSIMDNVL---AGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFR-LSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281000366 250 LDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYRILSllDRLIFLSRGQTVYSGSPAEL 314
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARIS--DRAALFFDGRLVEEGPTEQL 249
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
103-315 |
1.04e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 57.05 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDAL-ADRIAKeklKGTVTLNDEVLESALLKVISA---YVMQD--DLLFPMlT 176
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLnGIYLPQ---RGRVKVMGREVNAENEKWVRSkvgLVFQDpdDQVFSS-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 177 VEETLMFAaefrlPRS--LSKSKKKARVQALIDQLGLTTAAntvigDEGHRGVSGGERRRVSIGIDIIHDPILLFLDEPT 254
Cdd:PRK13647 97 VWDDVAFG-----PVNmgLDKDEVERRVEEALKAVRMWDFR-----DKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1281000366 255 SGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYrILSLLDRLIFLSRGQTVYSGSPAELS 315
Cdd:PRK13647 167 AYLDPRGQETLMEILDRLHNQGKTVIVATHDVDL-AAEWADQVIVLKEGRVLAEGDKSLLT 226
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
112-272 |
1.16e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 57.41 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 112 EGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLNDEVL----ESALLKVISAYVM--QDDL--LFPMLTVEETLMF 183
Cdd:PRK15079 46 EGETLGVVGESGCGKSTFARAIIGLV--KATDGEVAWLGKDLlgmkDDEWRAVRSDIQMifQDPLasLNPRMTIGEIIAE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 184 AAEFRLPRsLSKSKKKARVQALIDQLGLTTaanTVIGDEGHRgVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAF 263
Cdd:PRK15079 124 PLRTYHPK-LSRQEVKDRVKAMMLKVGLLP---NLINRYPHE-FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 198
|
....*....
gi 1281000366 264 MVVKVLQRI 272
Cdd:PRK15079 199 QVVNLLQQL 207
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
89-326 |
1.20e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.50 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 89 NLTAE--ENGGRVKLLlNDISGEAREGEIMAVLGASGSGKSTLIDALADrIAKEKLKGT---VTLND----EVLESALLK 159
Cdd:PRK15093 8 NLTIEfkTSDGWVKAV-DRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTadrMRFDDidllRLSPRERRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 160 VIS---AYVMQD--DLLFPMLTVEETLMFAaefrLPRSLSKSK-------KKARVQALIDQLGlttaantvIGDegHRGV 227
Cdd:PRK15093 86 LVGhnvSMIFQEpqSCLDPSERVGRQLMQN----IPGWTYKGRwwqrfgwRKRRAIELLHRVG--------IKD--HKDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 228 SG--------GERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYRILSLLDRLIF 299
Cdd:PRK15093 152 MRsfpyelteGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINV 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 1281000366 300 LSRGQTVYSGSPAE------------LSEFLADFGHPIP 326
Cdd:PRK15093 232 LYCGQTVETAPSKElvttphhpytqaLIRAIPDFGSAMP 270
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
104-258 |
1.30e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.60 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 104 NDISGEAREGEIMAVLGASGSGKST-------LIDALAdriakeklkGTVTLNDEVLESallKVISA-----YVMQDDLL 171
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTtmkmltgLLPASE---------GEAWLFGQPVDA---GDIATrrrvgYMSQAFSL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 172 FPMLTVEETLMFAAE-FRLPrslsKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFL 250
Cdd:NF033858 351 YGELTVRQNLELHARlFHLP----AAEIAARVAEMLERFDLADVADALPDS-----LPLGIRQRLSLAVAVIHKPELLIL 421
|
....*...
gi 1281000366 251 DEPTSGLD 258
Cdd:NF033858 422 DEPTSGVD 429
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
103-280 |
1.32e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.00 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALA-DRIAKEklkGTVTLNDEVLE-----SALLKVIsAYVMQDDLLFPMLT 176
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSgNYQPDA---GSILIDGQEMRfasttAALAAGV-AIIYQELHLVPEMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 177 VEETLMFAaefRLPRS---LSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLDEP 253
Cdd:PRK11288 96 VAENLYLG---QLPHKggiVNRRLLNYEAREQLEHLGVDIDPDTPLKY-----LSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180
....*....|....*....|....*..
gi 1281000366 254 TSGLDSTSAFMVVKVLQRIAQSGSIVI 280
Cdd:PRK11288 168 TSSLSAREIEQLFRVIRELRAEGRVIL 194
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
102-323 |
1.55e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 56.28 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 102 LLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEklKGTVTLNDEvlesalLKVisAYVMQD---DLLFPmLTVE 178
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPD--EGVIKRNGK------LRI--GYVPQKlylDTTLP-LTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 179 ETLMFAAEFRLPRSLSKSKkkaRVQA--LIDQlglttaantvigdeGHRGVSGGERRRVSIGIDIIHDPILLFLDEPTSG 256
Cdd:PRK09544 88 RFLRLRPGTKKEDILPALK---RVQAghLIDA--------------PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 257 LDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYRILSLLDRLIFLSRgQTVYSGSPAELS---EFLADFGH 323
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSlhpEFISMFGP 219
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
187-314 |
1.60e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.05 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 187 FRLPRSLSKSKKKARVQA--LIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFM 264
Cdd:NF000106 108 YMIGR*LDLSRKDARARAdeLLERFSLTEAAGRAAAK-----YSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNE 182
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1281000366 265 VVKVLQRIAQSGSIVITSIhQPSYRILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:NF000106 183 VWDEVRSMVRDGATVLLTT-QYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
100-261 |
1.62e-08 |
|
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: 57.64 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADrIAKEklkgtvtLNDEVLESALLKVisAYVMQDDLLFPMLTVEE 179
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKD-------FNGEARPQPGIKV--GYLPQEPQLDPTKTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 180 TLM---------------FAAEFRLPRSLSKS--KKKARVQALIDQLGLTTAANTV----------IGDEGHRGVSGGER 232
Cdd:TIGR03719 88 NVEegvaeikdaldrfneISAKYAEPDADFDKlaAEQAELQEIIDAADAWDLDSQLeiamdalrcpPWDADVTKLSGGER 167
|
170 180
....*....|....*....|....*....
gi 1281000366 233 RRVSIGIDIIHDPILLFLDEPTSGLDSTS 261
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
88-287 |
1.66e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 57.89 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEENGGRVklLLNDISGEAREGEIMAVLGASGSGKSTLIDALADriakekL----KGTVTLNDevlesallkvisa 163
Cdd:COG4178 366 EDLTLRTPDGRP--LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG------LwpygSGRIARPA------------- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 164 yvmQDDLLF-------PMLTVEETLMFAAEfrlPRSLSkskkKARVQALIDQLGLTTAANTVigDEG---HRGVSGGERR 233
Cdd:COG4178 425 ---GARVLFlpqrpylPLGTLREALLYPAT---AEAFS----DAELREALEAVGLGHLAERL--DEEadwDQVLSLGEQQ 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1281000366 234 RVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRiAQSGSIVItSI-HQPS 287
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVI-SVgHRST 545
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
103-315 |
1.67e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.21 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKlKGTVTLNDEVlesallkvisAYVMQDDLLFPMlTVEETLM 182
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRS-DASVVIRGTV----------AYVPQVSWIFNA-TVRDNIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 183 FAAEFRLPRSlsksKKKARVQALIDQLGLTTAAN-TVIGDeghRGV--SGGERRRVSIGIDIIHDPILLFLDEPTSGLDS 259
Cdd:PLN03130 701 FGSPFDPERY----ERAIDVTALQHDLDLLPGGDlTEIGE---RGVniSGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1281000366 260 TSAFMVV-KVLQRIAQSGS--IVITSIHqpsyrILSLLDRLIFLSRGQTVYSGSPAELS 315
Cdd:PLN03130 774 HVGRQVFdKCIKDELRGKTrvLVTNQLH-----FLSQVDRIILVHEGMIKEEGTYEELS 827
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
57-258 |
2.36e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.49 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 57 LAPPPVLYPFKLSFqnlsysvkvrRRGSSLPENLTAEEN---GGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDAL 133
Cdd:PRK10636 289 IAPAHVDNPFHFSF----------RAPESLPNPLLKMEKvsaGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 134 ADRIAKekLKGTVtlndevlesALLKVIS-AYVMQDDLLFpmLTVEETLMfaaefrlpRSLSKSKKKARVQALIDQLGLT 212
Cdd:PRK10636 359 AGELAP--VSGEI---------GLAKGIKlGYFAQHQLEF--LRADESPL--------QHLARLAPQELEQKLRDYLGGF 417
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1281000366 213 TAANTVIGDEGHRgVSGGERRRVSIGIDIIHDPILLFLDEPTSGLD 258
Cdd:PRK10636 418 GFQGDKVTEETRR-FSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
102-303 |
2.44e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.96 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 102 LLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKLKGTVTLNDEVL--ESALLKvisayvmqddllfpmltvee 179
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFgrEASLID-------------------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 180 tlmfaaefRLPRSLSKSKKKarvqALIDQLGLTTAANTVigdEGHRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDS 259
Cdd:COG2401 105 --------AIGRKGDFKDAV----ELLNAVGLSDAVLWL---RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1281000366 260 TSAFMVVKVLQRIAQSGSI--VITSIHqpsYRILSLL--DRLIFLSRG 303
Cdd:COG2401 170 QTAKRVARNLQKLARRAGItlVVATHH---YDVIDDLqpDLLIFVGYG 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
158-293 |
2.99e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.35 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 158 LKVISAYVMQDDLLFPMlTVEETLMFAAEFRLPRSLSKSKKKARVQALIDQLglTTAANTVIGDEGhRGVSGGERRRVSI 237
Cdd:PTZ00265 1294 LRNLFSIVSQEPMLFNM-SIYENIKFGKEDATREDVKRACKFAAIDEFIESL--PNKYDTNVGPYG-KSLSGGQKQRIAI 1369
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1281000366 238 GIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIhqpSYRILSL 293
Cdd:PTZ00265 1370 ARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITI---AHRIASI 1422
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
102-321 |
4.68e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 55.25 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 102 LLNDISGEAREGEIMAVLGASGSGKSTLI----DALADRIAKEKLKGTVTLNDEVlesallkvisAYVMQDdllfpmlTV 177
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLmlilGELEPSEGKIKHSGRISFSSQF----------SWIMPG-------TI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 178 EETLMFAAEFRLPRSLSKSKKkarVQALIDQLGLTTAANTVIGdEGHRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGL 257
Cdd:cd03291 115 KENIIFGVSYDEYRYKSVVKA---CQLEEDITKFPEKDNTVLG-EGGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1281000366 258 DSTSAFMVVK--VLQRIAQSGSIVITSihqpSYRILSLLDRLIFLSRGQTVYSGSPAELSEFLADF 321
Cdd:cd03291 191 DVFTEKEIFEscVCKLMANKTRILVTS----KMEHLKKADKILILHEGSSYFYGTFSELQSLRPDF 252
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
100-314 |
5.18e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 56.26 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEklKGTVTLNDEVLES---ALLKVISAYVMQDdllfPMLT 176
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT--EGEIRLDGRPLSSlshSVLRQGVAMVQQD----PVVL 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 177 VEEtlmFAAEFRLPRSLSKSKKKARVQALidQL-----GLTTAANTVIGDEGHRgVSGGERRRVSIGIDIIHDPILLFLD 251
Cdd:PRK10790 428 ADT---FLANVTLGRDISEEQVWQALETV--QLaelarSLPDGLYTPLGEQGNN-LSVGQKQLLALARVLVQTPQILILD 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1281000366 252 EPTSGLDSTSAFMVVKVLQRIAQSGSIVITSiHQPSYRILSllDRLIFLSRGQTVYSGSPAEL 314
Cdd:PRK10790 502 EATANIDSGTEQAIQQALAAVREHTTLVVIA-HRLSTIVEA--DTILVLHRGQAVEQGTHQQL 561
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
111-297 |
6.03e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.95 E-value: 6.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 111 REGEIMAVLGASGSGKSTLIDALAdriakeklkGTVTLN----------DEVLE----SAL-----------LKVI--SA 163
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILS---------GELKPNlgdydeepswDEVLKrfrgTELqdyfkklangeIKVAhkPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 164 YVmqdDLLfPML---TVEETLMFAAEfrlprslskskkKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGID 240
Cdd:COG1245 168 YV---DLI-PKVfkgTVRELLEKVDE------------RGKLDELAEKLGLENILDRDISE-----LSGGELQRVAIAAA 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1281000366 241 IIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQpsyriLSLLDRL 297
Cdd:COG1245 227 LLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHD-----LAILDYL 278
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
92-338 |
8.60e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 54.32 E-value: 8.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 92 AEENGGRVKLLLNDISGEAREGEIMAVLGASGSGKSTL---IDALAdrIAKEklkGTVTLN--DEVLESALLKVISA--Y 164
Cdd:PRK13633 15 ESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALL--IPSE---GKVYVDglDTSDEENLWDIRNKagM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 165 VMQ--DDLLFPMLtVEETLMFAaefrlPRSLSKSKK--KARVQALIDQLGLTTAAntvigDEGHRGVSGGERRRVSI-GI 239
Cdd:PRK13633 90 VFQnpDNQIVATI-VEEDVAFG-----PENLGIPPEeiRERVDESLKKVGMYEYR-----RHAPHLLSGGQKQRVAIaGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 240 DIIHdPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSI-HQPSYRILSllDRLIFLSRGQTVYSGSPAEL---S 315
Cdd:PRK13633 159 LAMR-PECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILItHYMEEAVEA--DRIIVMDSGKVVMEGTPKEIfkeV 235
|
250 260
....*....|....*....|...
gi 1281000366 316 EFLADFGHPIPEnenRTEFALDL 338
Cdd:PRK13633 236 EMMKKIGLDVPQ---VTELAYEL 255
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
103-321 |
1.24e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 54.34 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALAdriAKEK-LKGTVTLNDE-VLESALLKVISAYVMQDDLLFPMLTVEET 180
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVA---GLEKpTEGQIFIDGEdVTHRSIQQRDICMVFQSYALFPHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 181 LMFAAEFRlprSLSKSKKKARVQ---ALIDQLGLttaantviGDEGHRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGL 257
Cdd:PRK11432 99 VGYGLKML---GVPKEERKQRVKealELVDLAGF--------EDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281000366 258 DST---SAFMVVKVLQRiaqsgSIVITSI---HQPSyRILSLLDRLIFLSRGQTVYSGSPAEL-----SEFLADF 321
Cdd:PRK11432 168 DANlrrSMREKIRELQQ-----QFNITSLyvtHDQS-EAFAVSDTVIVMNKGKIMQIGSPQELyrqpaSRFMASF 236
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
94-343 |
1.79e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 53.65 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 94 ENGGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIdaladRIAK--EK-LKGTV--------TLNDEVLESALLKVis 162
Cdd:PRK11153 12 PQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLI-----RCINllERpTSGRVlvdgqdltALSEKELRKARRQI-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 163 AYVMQDdllFPML---TVEETLMFAAEFrlpRSLSKSKKKARVQALIDQLGLTtaantvigDEGHR---GVSGGERRRVS 236
Cdd:PRK11153 85 GMIFQH---FNLLssrTVFDNVALPLEL---AGTPKAEIKARVTELLELVGLS--------DKADRypaQLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 237 IGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSI-HQPSYrILSLLDRLIFLSRGQTVYSGSPAELs 315
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLItHEMDV-VKRICDRVAVIDAGRLVEQGTVSEV- 228
|
250 260
....*....|....*....|....*...
gi 1281000366 316 efladFGHPipenenRTEFALDLVRDLE 343
Cdd:PRK11153 229 -----FSHP------KHPLTREFIQSTL 245
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
96-293 |
3.08e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 51.80 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 96 GGRVKLllNDISGEAREGEIMAVLGASGSGKSTLIDALA--DRIAKEKL--KGTVTLNDEVLESALLKVISAYVMQDDLL 171
Cdd:PRK10908 13 GGRQAL--QGVTFHMRPGEMAFLTGHSGAGKSTLLKLICgiERPSAGKIwfSGHDITRLKNREVPFLRRQIGMIFQDHHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 172 FPMLTVEETLMFAAefrLPRSLSKSKKKARVQALIDQLGL-TTAANTVIGdeghrgVSGGERRRVSIGIDIIHDPILLFL 250
Cdd:PRK10908 91 LMDRTVYDNVAIPL---IIAGASGDDIRRRVSAALDKVGLlDKAKNFPIQ------LSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1281000366 251 DEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIH------QPSYRILSL 293
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHdiglisRRSYRMLTL 210
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
103-316 |
4.51e-07 |
|
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: 52.90 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKLKGTVTLNDEVLESALLKVIS----AYVMQDDLLFPMLTVE 178
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNIRDTEragiVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 179 ETLMFAAEFRLPRSLSKSKKKA-RVQALIDQLGLTTAANT-VIGDEGhrgvsGGERRRVSIGIDIIHDPILLFLDEPTSG 256
Cdd:TIGR02633 97 ENIFLGNEITLPGGRMAYNAMYlRAKNLLRELQLDADNVTrPVGDYG-----GGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 257 LDSTSAFMVVKVLQRIAQSGSIVITSIHQPSyRILSLLDRLIFLSRGQTVYSGSPAELSE 316
Cdd:TIGR02633 172 LTEKETEILLDIIRDLKAHGVACVYISHKLN-EVKAVCDTICVIRDGQHVATKDMSTMSE 230
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
102-321 |
5.17e-07 |
|
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: 53.38 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 102 LLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLNDEVLESALLKVISAYVMQDDLLFPmLTVEEtl 181
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGEL--EPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFG-LSYDE-- 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 182 mfaaeFRLpRSLSKSkkkarVQALIDQLGLTTAANTVIGdEGHRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTS 261
Cdd:TIGR01271 516 -----YRY-TSVIKA-----CQLEEDIALFPEKDKTVLG-EGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1281000366 262 AFMVVK--VLQRIAQSGSIVITSihqpSYRILSLLDRLIFLSRGQTVYSGSPAELSEFLADF 321
Cdd:TIGR01271 584 EKEIFEscLCKLMSNKTRILVTS----KLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDF 641
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
115-316 |
6.28e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.38 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 115 IMAVLGASGSGKSTLIDA---LADRIAKEKLKGTVTLNDEVLESALLKVIS-----AYVMQDDLLFPMLTVEETLMFAAE 186
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRTfnrLLELNEEARVEGEVRLFGRNIYSPDVDPIEvrrevGMVFQYPNPFPHLTIYDNVAIGVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 187 FRlprSLSKSKKK--ARVQALIDQLGLTTAANTVIGDEGHRgVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFM 264
Cdd:PRK14267 112 LN---GLVKSKKEldERVEWALKKAALWDEVKDRLNDYPSN-LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAK 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1281000366 265 VVKVLQRIAQSGSIVITSiHQPS-------YRILSLLDRLIFLSRGQTVYSGSPAELSE 316
Cdd:PRK14267 188 IEELLFELKKEYTIVLVT-HSPAqaarvsdYVAFLYLGKLIEVGPTRKVFENPEHELTE 245
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
103-257 |
6.34e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKLKGTVTLNDEVLESALLK-------VIsayVMQDDLLFPML 175
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGEELQASNIRdteragiAI---IHQELALVKEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 176 TVEETLMFAAEFRLPRSLSKSKKKARVQALIDQLGLTTAANTVIGDEGhrgvsGGERRRVSIGIDIIHDPILLFLDEPTS 255
Cdd:PRK13549 98 SVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLG-----LGQQQLVEIAKALNKQARLLILDEPTA 172
|
..
gi 1281000366 256 GL 257
Cdd:PRK13549 173 SL 174
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
80-314 |
6.58e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.53 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 80 RRRGsslpENLTAeenGGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKekLKGTVTLNDEVLESALLK 159
Cdd:PRK10253 7 RLRG----EQLTL---GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP--AHGHVWLDGEHIQHYASK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 160 VIS---AYVMQDDLLFPMLTVEEtlmFAAEFRLPRS--LSKSKKK--ARVQALIDQLGLTTAANTVIGDeghrgVSGGER 232
Cdd:PRK10253 78 EVArriGLLAQNATTPGDITVQE---LVARGRYPHQplFTRWRKEdeEAVTKAMQATGITHLADQSVDT-----LSGGQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 233 RRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYRILSLLDRLIFLSRGQTVYSGSPA 312
Cdd:PRK10253 150 QRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPK 229
|
..
gi 1281000366 313 EL 314
Cdd:PRK10253 230 EI 231
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
103-309 |
7.68e-07 |
|
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: 50.01 E-value: 7.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLidaladriakeklkgtvtlndevlesallkvisayvmqddllfpmltVEETLM 182
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL-----------------------------------------------VNEGLY 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 183 FAAEFRLPRSLSKSKKKARVqaLIDQLGLTTAANtvIG----DEGHRGVSGGERRRVSIG--IDIIHDPILLFLDEPTSG 256
Cdd:cd03238 44 ASGKARLISFLPKFSRNKLI--FIDQLQFLIDVG--LGyltlGQKLSTLSGGELQRVKLAseLFSEPPGTLFILDEPSTG 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1281000366 257 LDSTSAFMVVKVLQRIAQSGSIVITSIHQPsyRILSLLDRLIFLSRGQTVYSG 309
Cdd:cd03238 120 LHQQDINQLLEVIKGLIDLGNTVILIEHNL--DVLSSADWIIDFGPGSGKSGG 170
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
111-280 |
1.90e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 111 REGEIMAVLGASGSGKSTLIDALAdriakeklkGTVTLN----------DEVLE----SAL-----------LKVI--SA 163
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKILS---------GELIPNlgdyeeepswDEVLKrfrgTELqnyfkklyngeIKVVhkPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 164 YVmqdDLLfPML---TVEETLMfaaefrlprslsKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGID 240
Cdd:PRK13409 168 YV---DLI-PKVfkgKVRELLK------------KVDERGKLDEVVERLGLENILDRDISE-----LSGGELQRVAIAAA 226
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1281000366 241 IIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVI 280
Cdd:PRK13409 227 LLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLV 266
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
228-287 |
2.90e-06 |
|
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: 47.92 E-value: 2.90e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 228 SGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFmvvKVLQRIAQSGSIVITSIHQPS 287
Cdd:cd03223 93 SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED---RLYQLLKELGITVISVGHRPS 149
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
100-261 |
3.51e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADrIAKEklkgtvtLNDEVLESALLKVisAYVMQDDLLFPMLTVEE 179
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKE-------FEGEARPAPGIKV--GYLPQEPQLDPEKTVRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 180 TLM---------------FAAEFRLPRSLSKS--KKKARVQALIDQLGLTTAANTV----------IGDEGHRGVSGGER 232
Cdd:PRK11819 90 NVEegvaevkaaldrfneIYAAYAEPDADFDAlaAEQGELQEIIDAADAWDLDSQLeiamdalrcpPWDAKVTKLSGGER 169
|
170 180
....*....|....*....|....*....
gi 1281000366 233 RRVSIGIDIIHDPILLFLDEPTSGLDSTS 261
Cdd:PRK11819 170 RRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
216-287 |
7.78e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 7.78e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1281000366 216 NTVIGDEGHRgVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRI-AQSGSIVITSIHQPS 287
Cdd:PTZ00265 570 ETLVGSNASK-LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLS 641
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
114-314 |
8.17e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.59 E-value: 8.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 114 EIMAVLGASGSGKSTLIDALAdRIAkEKLKGTVTLND-EVLESAL--LKVISAYVMQDDLLFPMlTVEETLMFAAEFRlP 190
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALF-RIV-ELEKGRIMIDDcDVAKFGLtdLRRVLSIIPQSPVLFSG-TVRFNIDPFSEHN-D 1338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 191 RSLSKSKKKARVQALIDQLGLTTAANTVigdEGHRGVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQ 270
Cdd:PLN03232 1339 ADLWEALERAHIKDVIDRNPFGLDAEVS---EGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIR 1415
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1281000366 271 RIAQSGSIVITsihqpSYRILSLL--DRLIFLSRGQTVYSGSPAEL 314
Cdd:PLN03232 1416 EEFKSCTMLVI-----AHRLNTIIdcDKILVLSSGQVLEYDSPQEL 1456
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
103-258 |
1.21e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.97 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIDALADriAKEKLKGTVtlndEVL---------ESALLKVIsAYvMQDDL--- 170
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAG--ARKIQQGRV----EVLggdmadarhRRAVCPRI-AY-MPQGLgkn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 171 LFPMLTVEETLMFAAefRLpRSLSKSKKKARVQALIDQLGLTTAANTVIGDeghrgVSGGERRRVSIGIDIIHDPILLFL 250
Cdd:NF033858 89 LYPTLSVFENLDFFG--RL-FGQDAAERRRRIDELLRATGLAPFADRPAGK-----LSGGMKQKLGLCCALIHDPDLLIL 160
|
....*...
gi 1281000366 251 DEPTSGLD 258
Cdd:NF033858 161 DEPTTGVD 168
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
112-306 |
2.80e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 112 EGEIMAVLGASGSGKSTLIDALAD-------RIAKEK--------------LKGTVTlnDEVLE-----SALLK---VIS 162
Cdd:PRK11147 28 DNERVCLVGRNGAGKSTLMKILNGevllddgRIIYEQdlivarlqqdpprnVEGTVY--DFVAEgieeqAEYLKryhDIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 163 AYVMQD---DLLFPMLTVEETLMFAAEFRLprslskskkKARVQALIDQLGLTtaANTVIGDeghrgVSGGERRRVSIGI 239
Cdd:PRK11147 106 HLVETDpseKNLNELAKLQEQLDHHNLWQL---------ENRINEVLAQLGLD--PDAALSS-----LSGGWLRKAALGR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1281000366 240 DIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIaqSGSIVITSiHQPSYrILSLLDRLIFLSRGQTV 306
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF--QGSIIFIS-HDRSF-IRNMATRIVDLDRGKLV 232
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
66-321 |
4.10e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.81 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 66 FKLSFQNLSYSVKVRRRGSSLPENLTAEENGGRVKLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEklKGT 145
Cdd:PRK13545 3 YKVKFEHVTKKYKMYNKPFDKLKDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPN--KGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 146 VtlndEVLESALLKVISAYvmqddlLFPMLTVEETLMFAAefrLPRSLSKSKKKARVQALIDQLGLTTAANTVIgdeghR 225
Cdd:PRK13545 81 V----DIKGSAALIAISSG------LNGQLTGIENIELKG---LMMGLTKEKIKEIIPEIIEFADIGKFIYQPV-----K 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 226 GVSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSyRILSLLDRLIFLSRGQT 305
Cdd:PRK13545 143 TYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLS-QVKSFCTKALWLHYGQV 221
|
250
....*....|....*.
gi 1281000366 306 VYSGSPAELSEFLADF 321
Cdd:PRK13545 222 KEYGDIKEVVDHYDEF 237
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
100-272 |
9.89e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.78 E-value: 9.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 100 KLLLNDISGEAREGEIMAVLGASGSGKSTLIDALADRIAKEKLKGTVTLNDEVL------ESALLKVISAYvmQDDLLFP 173
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLlelspeDRAGEGIFMAF--QYPVEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 174 MLTVEETLMFAA----EFRLPRSLSKSKKKARVQALIDQLG-----LTTAANTvigdeghrGVSGGERRRVSIGIDIIHD 244
Cdd:PRK09580 92 GVSNQFFLQTALnavrSYRGQEPLDRFDFQDLMEEKIALLKmpedlLTRSVNV--------GFSGGEKKRNDILQMAVLE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1281000366 245 PILLFLDEPTSGLD----------------STSAFMVVKVLQRI 272
Cdd:PRK09580 164 PELCILDESDSGLDidalkivadgvnslrdGKRSFIIVTHYQRI 207
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
199-319 |
2.18e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 199 KARVQALIDqLGLT-----TAANTVigdeghrgvSGGERRRVSI----GIDIIHdpILLFLDEPTSGLDSTSAFMVVKVL 269
Cdd:PRK00635 454 KSRLSILID-LGLPyltpeRALATL---------SGGEQERTALakhlGAELIG--ITYILDEPSIGLHPQDTHKLINVI 521
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1281000366 270 QRIAQSGSIVITSIHQPsyRILSLLDRLIFLSR------GQTVYSGSPAelsEFLA 319
Cdd:PRK00635 522 KKLRDQGNTVLLVEHDE--QMISLADRIIDIGPgagifgGEVLFNGSPR---EFLA 572
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
113-258 |
2.21e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.46 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 113 GEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLN----DEVLESAL--LKVISAYVMQDDL--LFPMLTVEETLMfa 184
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLV--ESQGGEIIFNgqriDTLSPGKLqaLRRDIQFIFQDPYasLDPRQTVGDSIM-- 425
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1281000366 185 AEFRLPRSLSKSKKKARVQALIDQLGLTTAANTVIGDEghrgVSGGERRRVSIGIDIIHDPILLFLDEPTSGLD 258
Cdd:PRK10261 426 EPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
105-314 |
3.04e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 43.24 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 105 DISGEAREGEIMAVLGASGSGKSTLIDALADRIakEKLKGTVTLNDEVLE-------SALLKVIsayvMQD--DLLFPML 175
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMI--EPTSGELLIDDHPLHfgdysyrSQRIRMI----FQDpsTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 176 TVEETLMFAaeFRLPRSLSKSKKKARVQALIDQLGLTTaantvigDEGH---RGVSGGERRRVSIGIDIIHDPILLFLDE 252
Cdd:PRK15112 105 RISQILDFP--LRLNTDLEPEQREKQIIETLRQVGLLP-------DHASyypHMLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1281000366 253 PTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYRILSLLDRLIFLSRGQTVYSGSPAEL 314
Cdd:PRK15112 176 ALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
226-298 |
3.68e-04 |
|
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: 41.58 E-value: 3.68e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1281000366 226 GVSGGERRRVSIGIDIIH----DPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPsyRILSLLDRLI 298
Cdd:cd03227 77 QLSGGEKELSALALILALaslkPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLP--ELAELADKLI 151
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
284-330 |
3.76e-04 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 43.36 E-value: 3.76e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1281000366 284 HQPSYRILSLLDRLIFLSR-GQTVYSGSPAELSEFLADFGHPIPENEN 330
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKgGLTVYHGPVKKVEEYFAGLGINVPERVN 48
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
101-314 |
4.46e-04 |
|
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: 43.78 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 101 LLLNDISGEAREGEIMAVLGASGSGKSTL----------------IDALadRIAKEKL-----KGTVTLNDEVLESALLK 159
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLtlglfrinesaegeiiIDGL--NIAKIGLhdlrfKITIIPQDPVLFSGSLR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 160 visayvMQDDlLFPMLTVEETLMfaaefrlprSLSKSKKKARVQALIDQLGLTTAantvigdEGHRGVSGGERRRVSIGI 239
Cdd:TIGR00957 1378 ------MNLD-PFSQYSDEEVWW---------ALELAHLKTFVSALPDKLDHECA-------EGGENLSVGQRQLVCLAR 1434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1281000366 240 DIIHDPILLFLDEPTSGLDSTSAFMVVKVLqRIAQSGSIVITSIHqpsyRILSLLD--RLIFLSRGQTVYSGSPAEL 314
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVDLETDNLIQSTI-RTQFEDCTVLTIAH----RLNTIMDytRVIVLDKGEVAEFGAPSNL 1506
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
88-312 |
6.51e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.12 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 88 ENLTAEenGGRvklllnDISGEAREGEIMAVLGASGSGKSTLIDALAD-RIAKeklKGTVTLNDEVlesallkvISAYVM 166
Cdd:PRK15439 272 EDLTGE--GFR------NISLEVRAGEILGLAGVVGAGRTELAETLYGlRPAR---GGRIMLNGKE--------INALST 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 167 QDDLLFPMLTVEE------------------TLMFAaefRLPRSLSKSKKKARVQALIDQLGLTTAAntviGDEGHRGVS 228
Cdd:PRK15439 333 AQRLARGLVYLPEdrqssglyldaplawnvcALTHN---RRGFWIKPARENAVLERYRRALNIKFNH----AEQAARTLS 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 229 GGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITsIHQPSYRILSLLDRLIFLSRGQtvYS 308
Cdd:PRK15439 406 GGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLF-ISSDLEEIEQMADRVLVMHQGE--IS 482
|
....
gi 1281000366 309 GSPA 312
Cdd:PRK15439 483 GALT 486
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
109-224 |
7.61e-04 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 42.08 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 109 EAREGeIMAVLGASGSGKSTLIDALADRIAKEklkgtvtlndevlesallkVISAYVmqddlLFPMLTVEETL-MFAAEF 187
Cdd:COG3267 40 AQGGG-FVVLTGEVGTGKTTLLRRLLERLPDD-------------------VKVAYI-----PNPQLSPAELLrAIADEL 94
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1281000366 188 RLPrsLSKSKKKARVQALIDQLGLTTAANT---VIGDEGH 224
Cdd:COG3267 95 GLE--PKGASKADLLRQLQEFLLELAAAGRrvvLIIDEAQ 132
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
227-318 |
1.21e-03 |
|
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: 40.63 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 227 VSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAFMVVKVLQRIAQSGSIVITSIHQPSYRILSLLDRLIflsrgqtV 306
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIH-------V 144
|
90
....*....|..
gi 1281000366 307 YSGSPAELSEFL 318
Cdd:cd03222 145 FEGEPGVYGIAS 156
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
111-134 |
1.48e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.58 E-value: 1.48e-03
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
103-316 |
1.61e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 41.62 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 103 LNDISGEAREGEIMAVLGASGSGKSTLIdALADR--------IAKEKLKGTvTLNDEVLESALlkvisAYVMQDDLLFPM 174
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLL-SLIQRhfdvsegdIRFHDIPLT-KLQLDSWRSRL-----AVVSQTPFLFSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 175 lTVEETLMFAAEFRLPRSLSKSKKKARVQAliDQLGLTTAANTVIGDeghRGV--SGGERRRVSIGIDIIHDPILLFLDE 252
Cdd:PRK10789 404 -TVANNIALGRPDATQQEIEHVARLASVHD--DILRLPQGYDTEVGE---RGVmlSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1281000366 253 PTSGLDSTSAFMVVKVLQRIAQsGSIVITSIHQPSyrILSLLDRLIFLSRGQTVYSGSPAELSE 316
Cdd:PRK10789 478 ALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLS--ALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
102-304 |
6.01e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 39.89 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 102 LLNDISGEAREGEIMAVLGASGSGKSTLIDAL--ADRIAkeklKGTVTLNDEVLESALLK-VISAYVM------QDDLLF 172
Cdd:PRK11288 268 LREPISFSVRAGEIVGLFGLVGAGRSELMKLLygATRRT----AGQVYLDGKPIDIRSPRdAIRAGIMlcpedrKAEGII 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281000366 173 PMLTVEETLMFAAE--FRLPRSLSKSKKKAR-VQALIDQLGLTTA-ANTVIGDeghrgVSGGERRRVSIGIDIIHDPILL 248
Cdd:PRK11288 344 PVHSVADNINISARrhHLRAGCLINNRWEAEnADRFIRSLNIKTPsREQLIMN-----LSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1281000366 249 FLDEPTSGLDSTSAFMVVKVLQRIAQSG-SIVITSIHQPsyRILSLLDRLIFLSRGQ 304
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVIYELAAQGvAVLFVSSDLP--EVLGVADRIVVMREGR 473
|
|
| PRK06547 |
PRK06547 |
hypothetical protein; Provisional |
101-136 |
6.05e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235825 Cd Length: 172 Bit Score: 38.18 E-value: 6.05e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1281000366 101 LLLNDISGEAREGEIMAVL--GASGSGKSTLIDALADR 136
Cdd:PRK06547 1 MLVALIAARLCGGGMITVLidGRSGSGKTTLAGALAAR 38
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
113-134 |
9.96e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 9.96e-03
|
| |
