|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
105-726 |
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: 619.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 105 TKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSLK-GNVTLNGEVLNSKMQKAISAYVMQDDLLFPMLTV 183
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGsGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 184 EETLMFAAEFRLPRSLSKSKKSLRVQALIDQLGLRNAANTVIGDEG-HRGISGGERRRVSIGIDIIHDPILLFLDEPTSG 262
Cdd:TIGR00955 117 REHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 263 LDSTSALSVIKVLKRIAQSGSMVIMTLHQPSYRLLRLLDRLLFLSRGQTVFSGSPAMLPRFFAEFGHPIPEHENRTEFAL 342
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 343 DLIRELEGSAGGTRSLVEfnkgfRQRKAEPRSQTGLSLKEAISASISK-GKLVSGATTTTHSsgsspvstipTFANPFWV 421
Cdd:TIGR00955 277 QVLAVIPGSENESRERIE-----KICDSFAVSDIGRDMLVNTNLWSGKaGGLVKDSENMEGI----------GYNASWWT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 422 ELAVLAKRSMTNSRRQPELFGIRLGAVLVTGFILATMFWQLDNSPKGVQERLGC-FAFAMSTTFYTCADALPVFLQERFI 500
Cdd:TIGR00955 342 QFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGAlFLFLTNMTFQNVFPVINVFTAELPV 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 501 FMRETAYNAYRRSSYVLSHSLVALPSLIILSLAFAAITFWGVGLDGGLMGFLFYFLVILASFWAGSSFVTFLSGVVPHVM 580
Cdd:TIGR00955 422 FLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTS 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 581 LGYTIVVAILAYFLLFSGFFINRDRIPGYWIWFHYISLVKYPYEAVLLNEFGDPTKCFVrgvqiFDNTPLvavpqgmkvr 660
Cdd:TIGR00955 502 MALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVDNIEC-----TSANTT---------- 566
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15240660 661 llatmskslgmritsSTCLTTGYDILQQ--QGVTDLtkWNCLWVTVAWGFFFRILFYFSLLLGSKNKR 726
Cdd:TIGR00955 567 ---------------GPCPSSGEVILETlsFRNADL--YLDLIGLVILIFFFRLLAYFALRIRIRRKR 617
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
65-718 |
1.17e-84 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 281.00 E-value: 1.17e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 65 PFVLSFTDLTYSVKV---RRKFTWRRSVSSDPGAPSEGIFSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALAN 141
Cdd:PLN03211 37 PITLKFMDVCYRVKFenmKNKGSNIKRILGHKPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 142 RIAKGSLKGNVTLNGEVLNSKMQKAIsAYVMQDDLLFPMLTVEETLMFAAEFRLPRSLSKSKKSLRVQALIDQLGLRNAA 221
Cdd:PLN03211 117 RIQGNNFTGTILANNRKPTKQILKRT-GFVTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 222 NTVIGDEGHRGISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLHQPSYRLLRLLD 301
Cdd:PLN03211 196 NTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFD 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 302 RLLFLSRGQTVFSGSPAMLPRFFAEFGHPIPEHENRTEFALDLirelegsAGGTRSLvefnKGFRQRKAEPRSQTGLSLK 381
Cdd:PLN03211 276 SVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDL-------ANGVCQT----DGVSEREKPNVKQSLVASY 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 382 EAISASISKGKLVSGATTTTHSSGSSPVST------IPTFANPFWVELAVLAKRSMtNSRRQPELFGIRLGAVLVTGFIL 455
Cdd:PLN03211 345 NTLLAPKVKAAIEMSHFPQANARFVGSASTkehrssDRISISTWFNQFSILLQRSL-KERKHESFNTLRVFQVIAAALLA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 456 ATMFWQLDNspKGVQERLGCFAF-AMSTTFYTCADALPVFLQERFIFMRETAYNAYRRSSYVLSHSLVALPSLIILSLAF 534
Cdd:PLN03211 424 GLMWWHSDF--RDVQDRLGLLFFiSIFWGVFPSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGDLPMELILPTIF 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 535 AAITFWGVGLDGGLMGFLFYFLVILASFWAGSSFVTFLSGVVPHVMLGYTIVVAILAYFLLFSGFFINrdRIPGYWIWFH 614
Cdd:PLN03211 502 LTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGFYVH--KLPSCMAWIK 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 615 YISLVKYPYEAvllnefgdptkcfvrgvqifdntpLVAVPQGMKVRLLATMSKSLGMRITSSTClttgyDILQQQGVTDL 694
Cdd:PLN03211 580 YISTTFYSYRL------------------------LINVQYGEGKRISSLLGCSLPHGSDRASC-----KFVEEDVAGQI 630
|
650 660
....*....|....*....|....
gi 15240660 695 TKWNCLWVTVAWGFFFRILFYFSL 718
Cdd:PLN03211 631 SPATSVSVLIFMFVGYRLLAYLAL 654
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
54-658 |
8.57e-67 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 240.40 E-value: 8.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 54 DVDLASPDQSVPFVLSFTDLTYSV-----KVRRKFTWRRSVSSDPgapsegiFSSKTKTLLNGITGEARDGEILAVLGAS 128
Cdd:TIGR00956 726 DIEAGEVLGSTDLTDESDDVNDEKdmekeSGEDIFHWRNLTYEVK-------IKKEKRVILNNVDGWVKPGTLTALMGAS 798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 129 GSGKSTLIDALANRIAKGSL-KGNVTLNGEVLNSKMQKaISAYVMQDDLLFPMLTVEETLMFAAEFRLPRSLSKSKKSLR 207
Cdd:TIGR00956 799 GAGKTTLLNVLAERVTTGVItGGDRLVNGRPLDSSFQR-SIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEY 877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 208 VQALIDQLGLRNAANTVIGDEGHrGISGGERRRVSIGIDIIHDP-ILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVI 286
Cdd:TIGR00956 878 VEEVIKLLEMESYADAVVGVPGE-GLNVEQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAIL 956
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 287 MTLHQPSYRLLRLLDRLLFLSRG-QTVFSG-----SPAMLPRFFAEFGHPIPEHENRTEFALDLIreleGSAGGTRSLVE 360
Cdd:TIGR00956 957 CTIHQPSAILFEEFDRLLLLQKGgQTVYFGdlgenSHTIINYFEKHGAPKCPEDANPAEWMLEVI----GAAPGAHANQD 1032
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 361 FNKGFrqRKAEPRSQTGLSLKEaISASISKGKLVSgatttthssgssPVSTIPTFANPFWVELAVLAKRSMTNSRRQPEL 440
Cdd:TIGR00956 1033 YHEVW--RNSSEYQAVKNELDR-LEAELSKAEDDN------------DPDALSKYAASLWYQFKLVLWRTFQQYWRTPDY 1097
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 441 FGIRLGAVLVTGFILATMFWQLDNSPKGVQERLgcFAFAMSTTFYTCA--DALPVFL-QERFIFMRETAYNAYRRSSYVL 517
Cdd:TIGR00956 1098 LYSKFFLTIFAALFIGFTFFKVGTSLQGLQNQM--FAVFMATVLFNPLiqQYLPPFVaQRDLYEVRERPSRTFSWLAFIA 1175
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 518 SHSLVALPSLIILSLAFAAITFWGVGL--------DGGLMGFLFYFLVIlASFWAGSSFVTFLSGVVPHVMLGYTIVVAI 589
Cdd:TIGR00956 1176 AQITVEIPYNLVAGTIFFFIWYYPVGFywnasktgQVHERGVLFWLLST-MFFLYFSTLGQMVISFNPNADNAAVLASLL 1254
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 590 LAYFLLFSGFFINRDRIPGYWIWFHYISLVKYPYEAVLLNEFGD-PTKCFVRGVQIFDNtplvavPQGMK 658
Cdd:TIGR00956 1255 FTMCLSFCGVLAPPSRMPGFWIFMYRCSPFTYLVQALLSTGLADvPVTCKVKELLTFNP------PSGQT 1318
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
104-292 |
2.34e-63 |
|
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: 210.59 E-value: 2.34e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 104 KTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSLK-GNVTLNGEVLNSKMQKAISAYVMQDDLLFPMLT 182
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTsGQILFNGQPRKPDQFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 183 VEETLMFAAEFRLPRSLSKSKKSLRVqaliDQLGLRNAANTVIGDEGHRGISGGERRRVSIGIDIIHDPILLFLDEPTSG 262
Cdd:cd03234 98 VRETLTYTAILRLPRKSSDAIRKKRV----EDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190
....*....|....*....|....*....|
gi 15240660 263 LDSTSALSVIKVLKRIAQSGSMVIMTLHQP 292
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIHQP 203
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
67-294 |
1.95e-62 |
|
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: 207.02 E-value: 1.95e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 67 VLSFTDLTYSVKVRRkftwrrsvssdpgapsegifSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKG 146
Cdd:cd03213 3 TLSFRNLTVTVKSSP--------------------SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 147 SLKGNVTLNGEVLNSKMQKAISAYVMQDDLLFPMLTVEETLMFAAEFRlprslskskkslrvqalidqlglrnaantvig 226
Cdd:cd03213 63 GVSGEVLINGRPLDKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR-------------------------------- 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15240660 227 deghrGISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLHQPSY 294
Cdd:cd03213 111 -----GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSS 173
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
103-634 |
7.51e-58 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 213.43 E-value: 7.51e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 103 SKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRI--AKGSLKGNVTLNGEVLNS--KMQKAISAYVMQDDLLF 178
Cdd:TIGR00956 71 TKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgFHIGVEGVITYDGITPEEikKHYRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 179 PMLTVEETLMFAAEFRLPRS----LSKSKKSLRVQALI-DQLGLRNAANTVIGDEGHRGISGGERRRVSIGIDIIHDPIL 253
Cdd:TIGR00956 151 PHLTVGETLDFAARCKTPQNrpdgVSREEYAKHIADVYmATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 254 LFLDEPTSGLDSTSALSVIKVLKRIAQ-SGSMVIMTLHQPSYRLLRLLDRLLFLSRGQTVFSGSPAMLPRFFAEFGHPIP 332
Cdd:TIGR00956 231 QCWDNATRGLDSATALEFIRALKTSANiLDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFKCP 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 333 EHENRTEFALDLIRELE-----GSAGGT-RSLVEFNKGFRqrkaepRSQTGLSLKEAISA------SISKGKLVSGATTT 400
Cdd:TIGR00956 311 DRQTTADFLTSLTSPAErqikpGYEKKVpRTPQEFETYWR------NSPEYAQLMKEIDEyldrcsESDTKEAYRESHVA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 401 THSSGSSPVSTiptFANPFWVELAVLAKRSMTNSRRQPELFGIRLGAVLVTGFILATMFWQLDNSPKGVQERLGCFAFAM 480
Cdd:TIGR00956 385 KQSKRTRPSSP---YTVSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRGGALFFAI 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 481 STTFYTCADALPVFLQERFIFMRETAYNAYRRSSYVLSHSLVALPSLIILSLAFAAITFWGVGLDGGLMGFLFYFLVILA 560
Cdd:TIGR00956 462 LFNAFSSLLEIASMYEARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLILFI 541
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240660 561 SFWAGSSFVTFLSGVVPHVMLGYTIVVAILAYFLLFSGFFINRDRIPGYWIWFHYISLVKYPYEAVLLNEFGDP 634
Cdd:TIGR00956 542 CTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVNEFHGR 615
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
26-633 |
2.09e-52 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 196.99 E-value: 2.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 26 ASSSPTTFAQLLQNVDDSTRRSHHqhhvdvdlASPDQSVpfVLSFTDLTYSVKVRRKFtwrrsVSSDPGAPSEGIFSSKT 105
Cdd:PLN03140 829 AIQRMSNPEGLSKNRDSSLEAANG--------VAPKRGM--VLPFTPLAMSFDDVNYF-----VDMPAEMKEQGVTEDRL 893
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KtLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSLKGNVTLNGEVLNSKMQKAISAYVMQDDLLFPMLTVEE 185
Cdd:PLN03140 894 Q-LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVRE 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 186 TLMFAAEFRLPRSLSKSKKSLRVQALIDQLGLRNAANTVIGDEGHRGISGGERRRVSIGIDIIHDPILLFLDEPTSGLDS 265
Cdd:PLN03140 973 SLIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 266 TSALSVIKVLKRIAQSGSMVIMTLHQPSY-RLLRLLDRLLFLSRGQTVFSG-----SPAMLPRFFAEFGHP-IPEHENRT 338
Cdd:PLN03140 1053 RAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELLLMKRGGQVIYSGplgrnSHKIIEYFEAIPGVPkIKEKYNPA 1132
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 339 EFALdlirELEGSAGGTRSLVEFNKGFRQRKAEPRSQtglSLKEAISASISKGKLVSGATTTTHssgsspvSTIPTFANP 418
Cdd:PLN03140 1133 TWML----EVSSLAAEVKLGIDFAEHYKSSSLYQRNK---ALVKELSTPPPGASDLYFATQYSQ-------STWGQFKSC 1198
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 419 FWvelavlaKRSMTnSRRQPELFGIRLGAVLVTGFILATMFWQLDNSPKGVQERLGCFAFAMSTTFY----TCADALPVF 494
Cdd:PLN03140 1199 LW-------KQWWT-YWRSPDYNLVRFFFTLAAALMVGTIFWKVGTKRSNANDLTMVIGAMYAAVLFvginNCSTVQPMV 1270
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 495 LQERFIFMRETAYNAYRRSSYVLSHSLVALPSLIILSLAFAAITFWGVGLDGGLMGFLFYFLVILASFWAGSSFVTFLSG 574
Cdd:PLN03140 1271 AVERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFISFFSFLYFTYYGMMTVS 1350
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 15240660 575 VVPHVMLGYTIVVAILAYFLLFSGFFINRDRIPGYWIWFHYISLVKYPYEAVLLNEFGD 633
Cdd:PLN03140 1351 LTPNQQVAAIFAAAFYGLFNLFSGFFIPRPKIPKWWVWYYWICPVAWTVYGLIVSQYGD 1409
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
65-293 |
1.55e-48 |
|
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: 169.35 E-value: 1.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 65 PFVLSFTDLTYSVKVRRKftwrrsvssdpgapsegifsskTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIA 144
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGG----------------------KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKT 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 145 KGSLKGNVTLNGEVLNSKMQKaISAYVMQDDLLFPMLTVEETLMFAAEFRlprslskskkslrvqalidqlglrnaantv 224
Cdd:cd03232 59 AGVITGEILINGRPLDKNFQR-STGYVEQQDVHSPNLTVREALRFSALLR------------------------------ 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240660 225 igdeghrGISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLHQPS 293
Cdd:cd03232 108 -------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPS 169
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
426-629 |
1.78e-44 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 158.59 E-value: 1.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 426 LAKRSMTNSRRQPELFGIRLGAVLVTGFILATMFWQLDNSpKGVQERLGCFAFAMSTTFYT-CADALPVFLQERFIFMRE 504
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQ-QGGLNRPGLLFFSILFNAFSaLSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 505 TAYNAYRRSSYVLSHSLVALPSLIILSLAFAAITFWGVGLDGGLMGFLFYFLVILASFWAGSSFVTFLSGVVPHVMLGYT 584
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15240660 585 IVVAILAYFLLFSGFFINRDRIPGYWIWFHYISLVKYPYEAVLLN 629
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
104-290 |
6.94e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 144.05 E-value: 6.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 104 KTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGE--VLNSKMQKAISAYVMQDDLLFPML 181
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTS--GEVRVLGEdvARDPAEVRRRIGYVPQEPALYPDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 182 TVEETLMFAAEFR-LPRSLSKSkkslRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPT 260
Cdd:COG1131 89 TVRENLRFFARLYgLPRKEARE----RIDELLELFGLTDAADRKVGT-----LSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190
....*....|....*....|....*....|
gi 15240660 261 SGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:COG1131 160 SGLDPEARRELWELLRELAAEGKTVLLSTH 189
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
101-634 |
8.81e-37 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 148.84 E-value: 8.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 101 FSSKTK-TLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKgSLK--GNVTLNGEVLNSKMQKAISAYVMQDDLL 177
Cdd:PLN03140 172 LAKKTKlTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDP-SLKvsGEITYNGYRLNEFVPRKTSAYISQNDVH 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 178 FPMLTVEETLMFAAE-------FRLPRSLSKSKK------------------------SLRVQALIDQLGLRNAANTVIG 226
Cdd:PLN03140 251 VGVMTVKETLDFSARcqgvgtrYDLLSELARREKdagifpeaevdlfmkatamegvksSLITDYTLKILGLDICKDTIVG 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 227 DEGHRGISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQ-SGSMVIMTLHQPSYRLLRLLDRLLF 305
Cdd:PLN03140 331 DEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHlTEATVLMSLLQPAPETFDLFDDIIL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 306 LSRGQTVFSGSPAMLPRFFAEFGHPIPEHENRTEFALDLIRELEGS---AGGTR-----SLVEFNKGFRqrkaepRSQTG 377
Cdd:PLN03140 411 LSEGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTSKKDQEqywADRNKpyryiSVSEFAERFK------SFHVG 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 378 LSLKEAISASISKGKLVSGATTTTHSSgsspVSTIPTFANPFWVELAVLAKRSMTNSRRQPELfgIRLGAVLVTGFILAT 457
Cdd:PLN03140 485 MQLENELSVPFDKSQSHKAALVFSKYS----VPKMELLKACWDKEWLLMKRNAFVYVFKTVQI--IIVAAIASTVFLRTE 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 458 MfwQLDNSPKGvQERLGCFAFAMSTTFYTCADALPVFLQERFIFMRETAYNAYRRSSYVLSHSLVALPSLIILSLAFAAI 537
Cdd:PLN03140 559 M--HTRNEEDG-ALYIGALLFSMIINMFNGFAELALMIQRLPVFYKQRDLLFHPPWTFTLPTFLLGIPISIIESVVWVVI 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 538 TFWGVGLDGGLMGFLFYFLVILASFWAGSSFVTFLSGVVPHVMLGYTIVVAILAYFLLFSGFFINRDRIPGYWIWFHYIS 617
Cdd:PLN03140 636 TYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPNWWEWAYWVS 715
|
570
....*....|....*..
gi 15240660 618 LVKYPYEAVLLNEFGDP 634
Cdd:PLN03140 716 PLSYGFNALAVNEMFAP 732
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
100-290 |
3.09e-36 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 135.71 E-value: 3.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 100 IFSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKMQKA--ISAYVMQDDLL 177
Cdd:cd03263 9 TYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTS--GTAYINGYSIRTDRKAArqSLGYCPQFDAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 178 FPMLTVEETLMFAAEFRlprSLSKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLD 257
Cdd:cd03263 87 FDELTVREHLRFYARLK---GLPKSEIKEEVELLLRVLGLTDKANKRART-----LSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190
....*....|....*....|....*....|...
gi 15240660 258 EPTSGLDSTSALSVIKVLKRIaQSGSMVIMTLH 290
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEV-RKGRSIILTTH 190
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
101-294 |
3.23e-35 |
|
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: 132.59 E-value: 3.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 101 FSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIakGSLKGNVTLNGEVLNSKMQKAIS---AYVMQD-DL 176
Cdd:cd03225 9 YPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL--GPTSGEVLVDGKDLTKLSLKELRrkvGLVFQNpDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 177 LFPMLTVEETLMFAAEFRlprSLSKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFL 256
Cdd:cd03225 87 QFFGPTVEEEVAFGLENL---GLPEEEIEERVEEALELVGLEGLRDRSPFT-----LSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 15240660 257 DEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLHQPSY 294
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDL 196
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
101-293 |
6.69e-35 |
|
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: 133.06 E-value: 6.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 101 FSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVL---NSKMQKAISaYVMQDDLL 177
Cdd:COG4555 9 KKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDS--GSILIDGEDVrkePREARRQIG-VLPDERGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 178 FPMLTVEETLMFAAEFRlprSLSKSKKSLRVQALIDQLGLRNAANTVIGdeghrGISGGERRRVSIGIDIIHDPILLFLD 257
Cdd:COG4555 86 YDRLTVRENIRYFAELY---GLFDEELKKRIEELIELLGLEEFLDRRVG-----ELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 15240660 258 EPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLHQPS 293
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQ 193
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
105-293 |
2.23e-34 |
|
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: 130.08 E-value: 2.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 105 TKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAK-GSLKGNVTLNGEVL--NSKMQKAISAYVMQDDLLFPML 181
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnVSVEGDIHYNGIPYkeFAEKYPGEIIYVSEEDVHFPTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 182 TVEETLMFAAEFRlprslskskkslrvqalidqlglrnaantviGDEGHRGISGGERRRVSIGIDIIHDPILLFLDEPTS 261
Cdd:cd03233 99 TVRETLDFALRCK-------------------------------GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190
....*....|....*....|....*....|...
gi 15240660 262 GLDSTSALSVIKVLKRIAQ-SGSMVIMTLHQPS 293
Cdd:cd03233 148 GLDSSTALEILKCIRTMADvLKTTTFVSLYQAS 180
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
109-261 |
1.11e-31 |
|
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: 120.45 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKMQKAIS---AYVMQDDLLFPMLTVEE 185
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTE--GTILLDGQDLTDDERKSLRkeiGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15240660 186 TLMFAAEFrlpRSLSKSKKSLRVQALIDQLGLRNAANTVIGDEGHrGISGGERRRVSIGIDIIHDPILLFLDEPTS 261
Cdd:pfam00005 79 NLRLGLLL---KGLSKREKDARAEEALEKLGLGDLADRPVGERPG-TLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
109-290 |
1.34e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 120.15 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALanriakGSL----KGNVTLNGEVLNSKMQKAISA-------YVMQDDLL 177
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNIL------GGLdrptSGEVLIDGQDISSLSERELARlrrrhigFVFQFFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 178 FPMLTVEETLMFAAEFrlpRSLSKSKKSLRVQALIDQLGLRNAANtvigdegHRG--ISGGERRRVSIGIDIIHDPILLF 255
Cdd:COG1136 98 LPELTALENVALPLLL---AGVSRKERRERARELLERVGLGDRLD-------HRPsqLSGGQQQRVAIARALVNRPKLIL 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 15240660 256 LDEPTSGLDSTSALSVIKVLKRIA-QSGSMVIMTLH 290
Cdd:COG1136 168 ADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTH 203
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
104-290 |
3.78e-30 |
|
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: 116.73 E-value: 3.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 104 KTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKMQKAIS--AYVMQDDLLFPML 181
Cdd:cd03230 11 GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDS--GEIKVLGKDIKKEPEEVKRriGYLPEEPSLYENL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 182 TVEETLMFaaefrlprslskskkslrvqalidqlglrnaantvigdeghrgiSGGERRRVSIGIDIIHDPILLFLDEPTS 261
Cdd:cd03230 89 TVRENLKL--------------------------------------------SGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180
....*....|....*....|....*....
gi 15240660 262 GLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGKTILLSSH 153
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
103-293 |
4.63e-30 |
|
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: 118.36 E-value: 4.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 103 SKTKTLLNGITGEARDGEILAVLGASGSGKSTL--IDALANRIAKGSlkgnVTLNGEVLNSKMQKAISA-------YVMQ 173
Cdd:cd03255 14 GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLlnILGGLDRPTSGE----VRVDGTDISKLSEKELAAfrrrhigFVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 174 DDLLFPMLTVEETLMFAAEFRlprSLSKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPIL 253
Cdd:cd03255 90 SFNLLPDLTALENVELPLLLA---GVPKKERRERAEELLERVGLGDRLNHYPSE-----LSGGQQQRVAIARALANDPKI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15240660 254 LFLDEPTSGLDSTSALSVIKVLKRIA-QSGSMVIMTLHQPS 293
Cdd:cd03255 162 ILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPE 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
106-290 |
3.55e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 116.34 E-value: 3.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALAnriakGSLK---GNVTLNGEVLNsKMQKAIsAYVMQD---DLLFP 179
Cdd:COG1121 19 RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAIL-----GLLPptsGTVRLFGKPPR-RARRRI-GYVPQRaevDWDFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 180 MlTVEETLM--FAAEFRLPRSLSKSKKSlRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLD 257
Cdd:COG1121 92 I-TVRDVVLmgRYGRRGLFRRPSRADRE-AVDEALERVGLEDLADRPIGE-----LSGGQQQRVLLARALAQDPDLLLLD 164
|
170 180 190
....*....|....*....|....*....|...
gi 15240660 258 EPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:COG1121 165 EPFAGVDAATEEALYELLRELRREGKTILVVTH 197
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
106-291 |
4.26e-29 |
|
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: 115.89 E-value: 4.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALaNRIAKGSlKGNVTLNGEVLNSKMQKAIS---AYVMQ--DDLLFpM 180
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLL-NGLLKPT-SGEVLVDGKDITKKNLRELRrkvGLVFQnpDDQLF-A 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 181 LTVEETLMFAAEfrlPRSLSKSKKSLRVQALIDQLGLRNAANTVIgdegHRgISGGERRRVSI-GIdIIHDPILLFLDEP 259
Cdd:COG1122 91 PTVEEDVAFGPE---NLGLPREEIRERVEEALELVGLEHLADRPP----HE-LSGGQKQRVAIaGV-LAMEPEVLVLDEP 161
|
170 180 190
....*....|....*....|....*....|..
gi 15240660 260 TSGLDSTSALSVIKVLKRIAQSGSMVIMTLHQ 291
Cdd:COG1122 162 TAGLDPRGRRELLELLKRLNKEGKTVIIVTHD 193
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
109-290 |
9.71e-28 |
|
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: 111.35 E-value: 9.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKMQKAISAY------VMQDDLLFPMLT 182
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTS--GTIRVNGQDVSDLRGRAIPYLrrkigvVFQDFRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 183 VEETLMFAAE--FRLPRSLSKskkslRVQALIDQLGLRNAANTVigdegHRGISGGERRRVSIGIDIIHDPILLFLDEPT 260
Cdd:cd03292 95 VYENVAFALEvtGVPPREIRK-----RVPAALELVGLSHKHRAL-----PAELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190
....*....|....*....|....*....|
gi 15240660 261 SGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:cd03292 165 GNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
103-290 |
1.20e-27 |
|
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: 111.41 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 103 SKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKmQKAIsAYVMQDDLLFPMLT 182
Cdd:cd03293 14 GGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTS--GEVLVDGEPVTGP-GPDR-GYVFQQDALLPWLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 183 VEETLMFAAEFrlpRSLSKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPTSG 262
Cdd:cd03293 90 VLDNVALGLEL---QGVPKAEARERAEELLELVGLSGFENAYPHQ-----LSGGMRQRVALARALAVDPDVLLLDEPFSA 161
|
170 180
....*....|....*....|....*....
gi 15240660 263 LDSTSALSVIKVLKRI-AQSGSMVIMTLH 290
Cdd:cd03293 162 LDALTREQLQEELLDIwRETGKTVLLVTH 190
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
106-290 |
1.38e-27 |
|
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: 112.06 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAkgSLKGNVTLNGEVLNSKMQKAIS---AYVMQD-DLLFPmL 181
Cdd:COG1120 14 RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLK--PSSGEVLLDGRDLASLSRRELArriAYVPQEpPAPFG-L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 182 TVEETLMFAaefRLP--RSLSKSKKSLR--VQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLD 257
Cdd:COG1120 91 TVRELVALG---RYPhlGLFGRPSAEDReaVEEALERTGLEHLADRPVDE-----LSGGERQRVLIARALAQEPPLLLLD 162
|
170 180 190
....*....|....*....|....*....|....
gi 15240660 258 EPTSGLDSTSALSVIKVLKRIAQS-GSMVIMTLH 290
Cdd:COG1120 163 EPTSHLDLAHQLEVLELLRRLARErGRTVVMVLH 196
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
119-292 |
2.79e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 109.88 E-value: 2.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 119 GEILAVLGASGSGKSTLIDALANRIAKG-SLKGNVTLNGEVLNSK--MQKAIsAYVMQDDLLFPMLTVEETLMFAaefrL 195
Cdd:COG4136 27 GEILTLMGPSGSGKSTLLAAIAGTLSPAfSASGEVLLNGRRLTALpaEQRRI-GILFQDDLLFPHLSVGENLAFA----L 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 196 PRSLSKSKKSLRVQALIDQLGLrnaantviGDEGHRG---ISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSALSVI 272
Cdd:COG4136 102 PPTIGRAQRRARVEQALEEAGL--------AGFADRDpatLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFR 173
|
170 180
....*....|....*....|.
gi 15240660 273 K-VLKRIAQSGSMVIMTLHQP 292
Cdd:COG4136 174 EfVFEQIRQRGIPALLVTHDE 194
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
106-292 |
2.84e-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: 109.88 E-value: 2.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALAnriakGSLK---GNVTLNGEVLNSKMQKAIS--AYVMQDDLLFPM 180
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILA-----GLLPpsaGEVLWNGEPIRDAREDYRRrlAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 181 LTVEETLMFAAEFRlPRSLSKSkkslRVQALIDQLGLRNAANTVIgdeghRGISGGERRRVSIGIDIIHDPILLFLDEPT 260
Cdd:COG4133 90 LTVRENLRFWAALY-GLRADRE----AIDEALEAVGLAGLADLPV-----RQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|..
gi 15240660 261 SGLDSTSALSVIKVLKRIAQSGSMVIMTLHQP 292
Cdd:COG4133 160 TALDAAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
106-294 |
5.55e-27 |
|
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: 109.97 E-value: 5.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALaNRIAKGSlKGNVTLNGEVLNSKMQKAI------SAYVMQDDLLFP 179
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCL-NGLVEPT-SGSVLIDGTDINKLKGKALrqlrrqIGMIFQQFNLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 180 MLTVEETLMFAAEFRLP--RSL----SKSKKSLRVQALiDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPIL 253
Cdd:cd03256 92 RLSVLENVLSGRLGRRStwRSLfglfPKEEKQRALAAL-ERVGLLDKAYQRADQ-----LSGGQQQRVAIARALMQQPKL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15240660 254 LFLDEPTSGLDSTSALSVIKVLKRIAQS-GSMVIMTLHQPSY 294
Cdd:cd03256 166 ILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDL 207
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
106-293 |
6.29e-27 |
|
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: 109.15 E-value: 6.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALAN--RIAKGSlkgnVTLNGEVLNSKM--QKAIsAYVMQDDLLFPML 181
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGleRPDSGE----ILIDGRDVTGVPpeRRNI-GMVFQDYALFPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 182 TVEETLMFAAEFRLprsLSKSKKSLRVQALIDQLGLRNAANTVIgdeghRGISGGERRRVSIGIDIIHDPILLFLDEPTS 261
Cdd:cd03259 88 TVAENIAFGLKLRG---VPKAEIRARVRELLELVGLEGLLNRYP-----HELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190
....*....|....*....|....*....|...
gi 15240660 262 GLDSTSALSVIKVLKRI-AQSGSMVIMTLHQPS 293
Cdd:cd03259 160 ALDAKLREELREELKELqRELGITTIYVTHDQE 192
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
101-293 |
1.65e-26 |
|
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: 105.79 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 101 FSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKMQKAISAYVmqddllfpm 180
Cdd:cd00267 7 FRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTS--GEILIDGKDIAKLPLEELRRRI--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 181 ltveetlmfaaefrlprslskskkslrvqALIDQLglrnaantvigdeghrgiSGGERRRVSIGIDIIHDPILLFLDEPT 260
Cdd:cd00267 76 -----------------------------GYVPQL------------------SGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190
....*....|....*....|....*....|...
gi 15240660 261 SGLDSTSALSVIKVLKRIAQSGSMVIMTLHQPS 293
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPE 141
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
32-280 |
3.75e-26 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 113.07 E-value: 3.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 32 TFAQLLQNVDDSTRRSHHQHHVDVDLASPDQSVPfVLSFTDLTYSVKVRRKftwrrsvssdpgapsegifssKTKTLLNG 111
Cdd:COG1123 226 PPEEILAAPQALAAVPRLGAARGRAAPAAAAAEP-LLEVRNLSKRYPVRGK---------------------GGVRAVDD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 112 ITGEARDGEILAVLGASGSGKSTLIdalanRIAKGSLK---GNVTLNGEVLNSKMQKAISA------YVMQD--DLLFPM 180
Cdd:COG1123 284 VSLTLRRGETLGLVGESGSGKSTLA-----RLLLGLLRptsGSILFDGKDLTKLSRRSLRElrrrvqMVFQDpySSLNPR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 181 LTVEETLMFAAefRLPRSLSKSKKSLRVQALIDQLGLrnaantvigDEGHRG-----ISGGERRRVSIGIDIIHDPILLF 255
Cdd:COG1123 359 MTVGDIIAEPL--RLHGLLSRAERRERVAELLERVGL---------PPDLADrypheLSGGQRQRVAIARALALEPKLLI 427
|
250 260
....*....|....*....|....*
gi 15240660 256 LDEPTSGLDSTSALSVIKVLKRIAQ 280
Cdd:COG1123 428 LDEPTSALDVSVQAQILNLLRDLQR 452
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
106-293 |
1.26e-25 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 111.77 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKMQKAIS---AYVMQDDLLFPMlT 182
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYS--GSILINGVDLSDLDPASWRrqiAWVPQNPYLFAG-T 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 183 VEETLMFAA----EFRLPRSLskskKSLRVQALIDQL--GLrnaaNTVIGDEGhRGISGGERRRVSIGIDIIHDPILLFL 256
Cdd:COG4988 427 IRENLRLGRpdasDEELEAAL----EAAGLDEFVAALpdGL----DTPLGEGG-RGLSGGQAQRLALARALLRDAPLLLL 497
|
170 180 190
....*....|....*....|....*....|....*..
gi 15240660 257 DEPTSGLDSTSALSVIKVLKRIAQsGSMVIMTLHQPS 293
Cdd:COG4988 498 DEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLA 533
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
107-280 |
1.39e-25 |
|
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: 105.67 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 107 TLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNS---KMQKAIS---AYVMQDDL--LF 178
Cdd:cd03257 19 KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTS--GSIIFDGKDLLKlsrRLRKIRRkeiQMVFQDPMssLN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 179 PMLTVEETLMFAAEFRLPRSlSKSKKSLRVQALIDQLGLrnaantvigDEGH-----RGISGGERRRVSIGIDIIHDPIL 253
Cdd:cd03257 97 PRMTIGEQIAEPLRIHGKLS-KKEARKEAVLLLLVGVGL---------PEEVlnrypHELSGGQRQRVAIARALALNPKL 166
|
170 180
....*....|....*....|....*..
gi 15240660 254 LFLDEPTSGLDSTSALSVIKVLKRIAQ 280
Cdd:cd03257 167 LIADEPTSALDVSVQAQILDLLKKLQE 193
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
106-290 |
2.10e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 104.75 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALAnriakGSLK---GNVTLNGEVLnSKMQ-KAISAY------VMQDD 175
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLY-----GEERptsGQVLVNGQDL-SRLKrREIPYLrrrigvVFQDF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 176 LLFPMLTVEETLMFAAEFR-LPRSLSKSkkslRVQALIDQLGLRNAANTVIgDEghrgISGGERRRVSIGIDIIHDPILL 254
Cdd:COG2884 89 RLLPDRTVYENVALPLRVTgKSRKEIRR----RVREVLDLVGLSDKAKALP-HE----LSGGEQQRVAIARALVNRPELL 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 15240660 255 FLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATH 195
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
106-290 |
3.30e-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: 104.15 E-value: 3.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALAnriakGSLK---GNVTLNGEVLnSKMQKAIsAYVMQD---DLLFP 179
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIL-----GLLKptsGSIRVFGKPL-EKERKRI-GYVPQRrsiDRDFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 180 mLTVEETLM--FAAEFRLPRSLSKSKKSlRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLD 257
Cdd:cd03235 85 -ISVRDVVLmgLYGHKGLFRRLSKADKA-KVDEALERVGLSELADRQIGE-----LSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190
....*....|....*....|....*....|...
gi 15240660 258 EPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRREGMTILVVTH 190
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
105-288 |
5.10e-25 |
|
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: 103.38 E-value: 5.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 105 TKTLLNGITGEARDGEILAVLGASGSGKSTLIDALaNRIAKGSlKGNVTLNGEVLNSKMQKAIS-----AYVMQDDLLFP 179
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCI-NLLEEPD-SGTIIIDGLKLTDDKKNINElrqkvGMVFQQFNLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 180 MLTVEETLMFAAefRLPRSLSKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEP 259
Cdd:cd03262 90 HLTVLENITLAP--IKVKGMSKAEAEERALELLEKVGLADKADAYPAQ-----LSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190
....*....|....*....|....*....|
gi 15240660 260 TSGLDSTSALSVIKVLKRIAQSG-SMVIMT 288
Cdd:cd03262 163 TSALDPELVGEVLDVMKDLAEEGmTMVVVT 192
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
105-291 |
1.12e-24 |
|
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: 103.35 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 105 TKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKgsLKGNVTLNGE---VLNSKMQKAI---SAYVMQDDLLF 178
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRP--DSGEVLIDGEdisGLSEAELYRLrrrMGMLFQSGALF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 179 PMLTVEETLMFA--AEFRLPRSLSKSkkslRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFL 256
Cdd:cd03261 90 DSLTVFENVAFPlrEHTRLSEEEIRE----IVLEKLEAVGLRGAEDLYPAE-----LSGGMKKRVALARALALDPELLLY 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 15240660 257 DEPTSGLDSTSALSVIKVLKRIAQS-GSMVIMTLHQ 291
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHD 196
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
109-290 |
2.19e-24 |
|
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: 102.52 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKMQKAISAYVM----QDDLLFPMLTVE 184
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTS--GSVLFDGEDITGLPPHEIARLGIgrtfQIPRLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 185 ETLMFAAEFRLPRSLS-----KSKKSLRVQA--LIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLD 257
Cdd:cd03219 94 ENVMVAAQARTGSGLLlararREEREARERAeeLLERVGLADLADRPAGE-----LSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190
....*....|....*....|....*....|...
gi 15240660 258 EPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:cd03219 169 EPAAGLNPEETEELAELIRELRERGITVLLVEH 201
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
109-290 |
2.51e-24 |
|
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: 104.01 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNG-EVLN--SKMQKAISAyVMQDDLLFPMLTVEE 185
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTS--GTARVAGyDVVRepRKVRRSIGI-VPQYASVDEDLTGRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 186 TL-MFAAEFRLPRSLSKSkkslRVQALIDQLGLRNAANTVIGdeghrGISGGERRRVSIGIDIIHDPILLFLDEPTSGLD 264
Cdd:TIGR01188 86 NLeMMGRLYGLPKDEAEE----RAEELLELFELGEAADRPVG-----TYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLD 156
|
170 180
....*....|....*....|....*.
gi 15240660 265 STSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:TIGR01188 157 PRTRRAIWDYIRALKEEGVTILLTTH 182
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
106-294 |
2.72e-24 |
|
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: 100.34 E-value: 2.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALA--NRIAKGSLK-GNVTLNGEVLNSKMQKAISAYVMQDDLLFPMLT 182
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAglEEPDSGSILiDGEDLTDLEDELPPLRRRIGMVFQDFALFPHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 183 VEETLMFaaefrlprslskskkslrvqalidqlglrnaantvigdeghrGISGGERRRVSIGIDIIHDPILLFLDEPTSG 262
Cdd:cd03229 93 VLENIAL------------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSA 130
|
170 180 190
....*....|....*....|....*....|...
gi 15240660 263 LDSTSALSVIKVLKRI-AQSGSMVIMTLHQPSY 294
Cdd:cd03229 131 LDPITRREVRALLKSLqAQLGITVVLVTHDLDE 163
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
106-292 |
6.38e-24 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 99.43 E-value: 6.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALAnRIAKGSlKGNVTLNGEVLNSKMQKAIS---AYVMQddllfpmlt 182
Cdd:cd03214 12 RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLA-GLLKPS-SGEILLDGKDLASLSPKELArkiAYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 183 veetlmfaaefrlprslskskkslrvqaLIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPTSG 262
Cdd:cd03214 81 ----------------------------ALELLGLAHLADRPFNE-----LSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190
....*....|....*....|....*....|.
gi 15240660 263 LDSTSALSVIKVLKRIAQS-GSMVIMTLHQP 292
Cdd:cd03214 128 LDIAHQIELLELLRRLARErGKTVVMVLHDL 158
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
101-292 |
6.52e-24 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 100.28 E-value: 6.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 101 FSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSkmQKAIS-----AYVMQDD 175
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTS--GEIYLDGKPLSA--MPPPEwrrqvAYVPQEP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 176 LLFPMlTVEETLMFAAEFRlprslSKSKKSLRVQALIDQLGLrnaANTVIGDEGHRgISGGERRRVSIGIDIIHDPILLF 255
Cdd:COG4619 84 ALWGG-TVRDNLPFPFQLR-----ERKFDRERALELLERLGL---PPDILDKPVER-LSGGERQRLALIRALLLQPDVLL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 15240660 256 LDEPTSGLDSTSALSVIKVLKRIAQSGSM-VIMTLHQP 292
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRaVLWVSHDP 191
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
118-293 |
9.59e-24 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 100.06 E-value: 9.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 118 DGEILAVLGASGSGKSTLIdalanRIAKGSLK---GNVTLNGEVLNSKMQKAIS-------AYVMQDDLLFPMLTVEETL 187
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLL-----RCIAGLEKpdgGTIVLNGTVLFDSRKKINLppqqrkiGLVFQQYALFPHLNVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 188 MFAAefrlpRSLSKSKKSLRVQALIDQLGLrnaanTVIGDEGHRGISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTS 267
Cdd:cd03297 97 AFGL-----KRKRNREDRISVDELLDLLGL-----DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180
....*....|....*....|....*..
gi 15240660 268 ALSVIKVLKRIAQSGSM-VIMTLHQPS 293
Cdd:cd03297 167 RLQLLPELKQIKKNLNIpVIFVTHDLS 193
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
101-290 |
1.32e-23 |
|
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: 105.37 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 101 FSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRI-AKGSLKGNVTLNGEVLNSKMQKAIS---AYVMQD-D 175
Cdd:COG1123 14 YPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLpHGGRISGEVLLDGRDLLELSEALRGrriGMVFQDpM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 176 LLFPMLTVEETLMFAAEFRlprSLSKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLF 255
Cdd:COG1123 94 TQLNPVTVGDQIAEALENL---GLSRAEARARVLELLEAVGLERRLDRYPHQ-----LSGGQRQRVAIAMALALDPDLLI 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 15240660 256 LDEPTSGLDSTSALSVIKVLKRI-AQSGSMVIMTLH 290
Cdd:COG1123 166 ADEPTTALDVTTQAEILDLLRELqRERGTTVLLITH 201
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
106-290 |
2.62e-23 |
|
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: 99.28 E-value: 2.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALAnriakGSLK---GNVTLNGEVLNSKMQKAISA------YVMQDDL 176
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLII-----GLLRpdsGEILVDGQDITGLSEKELYElrrrigMLFQGGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 177 LFPMLTVEETLMFAAEFRlpRSLSKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFL 256
Cdd:COG1127 93 LFDSLTVFENVAFPLREH--TDLSEAEIRELVLEKLELVGLPGAADKMPSE-----LSGGMRKRVALARALALDPEILLY 165
|
170 180 190
....*....|....*....|....*....|....*
gi 15240660 257 DEPTSGLDSTSALSVIKVLKRIAQS-GSMVIMTLH 290
Cdd:COG1127 166 DEPTAGLDPITSAVIDELIRELRDElGLTSVVVTH 200
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
104-291 |
3.71e-23 |
|
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: 98.12 E-value: 3.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 104 KTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKMQKAIsAYVMQDDLLFPMLTV 183
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDS--GEVLFDGKPLDIAARNRI-GYLPEERGLYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 184 EETLMFAAEFRlprSLSKSKKSLRVQALIDQLGLRNAANTVIgdeghRGISGGERRRVSIGIDIIHDPILLFLDEPTSGL 263
Cdd:cd03269 88 IDQLVYLAQLK---GLKKEEARRRIDEWLERLELSEYANKRV-----EELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180
....*....|....*....|....*...
gi 15240660 264 DSTSALSVIKVLKRIAQSGSMVIMTLHQ 291
Cdd:cd03269 160 DPVNVELLKDVIRELARAGKTVILSTHQ 187
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
105-288 |
1.67e-22 |
|
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: 98.69 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 105 TKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGE-VL-NSKMQKAISAYVMQDDLLFPMLT 182
Cdd:TIGR03522 14 TQNALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDS--GSVQVCGEdVLqNPKEVQRNIGYLPEHNPLYLDMY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 183 VEETLMF-AAEFRLPRSLSKSkkslRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPTS 261
Cdd:TIGR03522 92 VREYLQFiAGIYGMKGQLLKQ----RVEEMIELVGLRPEQHKKIGQ-----LSKGYRQRVGLAQALIHDPKVLILDEPTT 162
|
170 180
....*....|....*....|....*..
gi 15240660 262 GLDSTSALSVIKVLKRIAQSGSMVIMT 288
Cdd:TIGR03522 163 GLDPNQLVEIRNVIKNIGKDKTIILST 189
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
105-291 |
3.64e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 97.49 E-value: 3.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 105 TKTLLNGITGEARDGEILAVLGASGSGKSTLIdalanRIAKGSLK---GNVTLNGEVLNSKMQKAIsAYvmqddL----- 176
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTI-----RIILGILApdsGEVLWDGEPLDPEDRRRI-GY-----Lpeerg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 177 LFPMLTVEETLMFAAefRLpRSLSKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFL 256
Cdd:COG4152 82 LYPKMKVGEQLVYLA--RL-KGLSKAEAKRRADEWLERLGLGDRANKKVEE-----LSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190
....*....|....*....|....*....|....*
gi 15240660 257 DEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLHQ 291
Cdd:COG4152 154 DEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQ 188
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
109-287 |
5.18e-22 |
|
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: 95.19 E-value: 5.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALA--NRIAKGSlkgnVTLNGEVLNSKMQKAIS----AYVMQDDLLFPMLT 182
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMglLPPRSGS----IRFDGRDITGLPPHERAragiGYVPEGRRIFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 183 VEETLMFAAEFRLPRslsKSKKSL-RVQALIDQLG--LRNAANTvigdeghrgISGGERRRVSIGIDIIHDPILLFLDEP 259
Cdd:cd03224 92 VEENLLLGAYARRRA---KRKARLeRVYELFPRLKerRKQLAGT---------LSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180
....*....|....*....|....*...
gi 15240660 260 TSGLDSTSALSVIKVLKRIAQSGSMVIM 287
Cdd:cd03224 160 SEGLAPKIVEEIFEAIRELRDEGVTILL 187
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
104-290 |
9.52e-22 |
|
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: 93.86 E-value: 9.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 104 KTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALA--NRIAKGSlkgnVTLNGEVLNSKMQKAISAYVMQD--DLLFp 179
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAglIKESSGS----ILLNGKPIKAKERRKSIGYVMQDvdYQLF- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 180 MLTVEETLMFAAEfrlprslSKSKKSLRVQALIDQLGLRNAAntvigdEGH-RGISGGERRRVSIGIDIIHDPILLFLDE 258
Cdd:cd03226 86 TDSVREELLLGLK-------ELDAGNEQAETVLKDLDLYALK------ERHpLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190
....*....|....*....|....*....|..
gi 15240660 259 PTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQGKAVIVITH 184
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
109-290 |
1.17e-21 |
|
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: 93.97 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNG-EVLN--SKMQKAISaYVMQDDLLFPMLTVEE 185
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTS--GRATVAGhDVVRepREVRRRIG-IVFQDLSVDDELTGWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 186 TL-MFAAEFRLPRSLSKSkkslRVQALIDQLGLRNAANTVIgdeghRGISGGERRRVSIGIDIIHDPILLFLDEPTSGLD 264
Cdd:cd03265 93 NLyIHARLYGVPGAERRE----RIDELLDFVGLLEAADRLV-----KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180
....*....|....*....|....*..
gi 15240660 265 STSALSVIKVLKRIAQSGSM-VIMTLH 290
Cdd:cd03265 164 PQTRAHVWEYIEKLKEEFGMtILLTTH 190
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
106-290 |
1.17e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 95.18 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLN--SKMQKAISAYVM-QD-DLLFPmL 181
Cdd:COG4559 14 RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSS--GEVRLNGRPLAawSPWELARRRAVLpQHsSLAFP-F 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 182 TVEETLMFAaefRLPRSLSKSKKSLRVQALIDQLGLRNAAntvigdegHR---GISGGERRRVS-------IGIDIIHDP 251
Cdd:COG4559 91 TVEEVVALG---RAPHGSSAAQDRQIVREALALVGLAHLA--------GRsyqTLSGGEQQRVQlarvlaqLWEPVDGGP 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 15240660 252 ILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:COG4559 160 RWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLH 198
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
58-293 |
1.69e-21 |
|
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: 99.07 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 58 ASPDQSVPFVLSFTDLTysvkvrrkFTWrrsvssdPGAPsegifssktKTLLNGITGEARDGEILAVLGASGSGKSTLID 137
Cdd:COG4987 324 EPAPAPGGPSLELEDVS--------FRY-------PGAG---------RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLA 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 138 ALANRIAkgSLKGNVTLNGEVLNSKMQKAIS---AYVMQDDLLFPMlTVEETLMFAA----EFRLPRSLSkskkslRVQ- 209
Cdd:COG4987 380 LLLRFLD--PQSGSITLGGVDLRDLDEDDLRrriAVVPQRPHLFDT-TLRENLRLARpdatDEELWAALE------RVGl 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 210 -ALIDQL--GLrnaaNTVIGdEGHRGISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVI 286
Cdd:COG4987 451 gDWLAALpdGL----DTWLG-EGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLL 525
|
....*..
gi 15240660 287 MTlHQPS 293
Cdd:COG4987 526 IT-HRLA 531
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-292 |
1.70e-21 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 98.97 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 11 MALPFFSPeFGNVSGASSSPTTFAQLLQNVDDSTRRSHHQHHVDVDLASPDQSVPFVLSFTDLTYSvkvrrkftWrrsvs 90
Cdd:TIGR02868 279 LPLAAFEA-FAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAG--------Y----- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 91 sdPGAPSegifssktktLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAkgSLKGNVTLNGEVLNSKMQKAISA- 169
Cdd:TIGR02868 345 --PGAPP----------VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD--PLQGEVTLDGVPVSSLDQDEVRRr 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 170 --YVMQDDLLFPMlTVEETLMFAAEFRLPRSLSKSKKSLRVQALIDqlGLRNAANTVIGDEGHRgISGGERRRVSIGIDI 247
Cdd:TIGR02868 411 vsVCAQDAHLFDT-TVRENLRLARPDATDEELWAALERVGLADWLR--ALPDGLDTVLGEGGAR-LSGGERQRLALARAL 486
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15240660 248 IHDPILLFLDEPTSGLDSTSALSVIKVLkRIAQSGSMVIMTLHQP 292
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADELLEDL-LAALSGRTVVLITHHL 530
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
109-278 |
1.75e-21 |
|
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: 93.94 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGE-VLNSKMQKAISAYVMQDDLLFPMLTVEETL 187
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDS--GKILLNGKdITNLPPEKRDISYVPQNYALFPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 188 MFAAEFRLPRSLSKSKKSLRVQAL--IDQLGLRNAANtvigdeghrgISGGERRRVSIGIDIIHDPILLFLDEPTSGLDS 265
Cdd:cd03299 93 AYGLKKRKVDKKEIERKVLEIAEMlgIDHLLNRKPET----------LSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170
....*....|...
gi 15240660 266 TSALSVIKVLKRI 278
Cdd:cd03299 163 RTKEKLREELKKI 175
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
103-280 |
2.01e-21 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 94.10 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 103 SKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALA--NRIAKGSlkgnVTLNGEVLNSKMQKAISA---YVMQDDL- 176
Cdd:COG1124 15 GRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAglERPWSGE----VTFDGRPVTRRRRKAFRRrvqMVFQDPYa 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 177 -LFPMLTVEETLmfaAEfrlP-RSLSKSKKSLRVQALIDQLGLrnaantvigDEGHRG-----ISGGERRRVSIGIDIIH 249
Cdd:COG1124 91 sLHPRHTVDRIL---AE---PlRIHGLPDREERIAELLEQVGL---------PPSFLDryphqLSGGQRQRVAIARALIL 155
|
170 180 190
....*....|....*....|....*....|..
gi 15240660 250 DPILLFLDEPTSGLD-STSALsVIKVLKRIAQ 280
Cdd:COG1124 156 EPELLLLDEPTSALDvSVQAE-ILNLLKDLRE 186
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
101-293 |
3.35e-21 |
|
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: 91.29 E-value: 3.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 101 FSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALAnRIAKGSlKGNVTLNGEVLN----SKMQKAIsAYVMQDDL 176
Cdd:cd03228 10 YPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLL-RLYDPT-SGEILIDGVDLRdldlESLRKNI-AYVPQDPF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 177 LFPMlTVEETLmfaaefrlprslskskkslrvqalidqlglrnaantvigdeghrgISGGERRRVSIGIDIIHDPILLFL 256
Cdd:cd03228 87 LFSG-TIRENI---------------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190
....*....|....*....|....*....|....*..
gi 15240660 257 DEPTSGLDSTSALSVIKVLKRIAQsGSMVIMTLHQPS 293
Cdd:cd03228 121 DEATSALDPETEALILEALRALAK-GKTVIVIAHRLS 156
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
106-288 |
3.36e-21 |
|
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: 92.26 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGeILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKMQK--AISAYVMQDDLLFPMLTV 183
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSS--GTIRIDGQDVLKQPQKlrRRIGYLPQEFGVYPNFTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 184 EETLMFAAefRLpRSLSKSKKSLRVQALIDQLGLRNAANTVIGdeghrGISGGERRRVSIGIDIIHDPILLFLDEPTSGL 263
Cdd:cd03264 90 REFLDYIA--WL-KGIPSKEVKARVDEVLELVNLGDRAKKKIG-----SLSGGMRRRVGIAQALVGDPSILIVDEPTAGL 161
|
170 180
....*....|....*....|....*
gi 15240660 264 DSTSALSVIKVLKRIAQSGSMVIMT 288
Cdd:cd03264 162 DPEERIRFRNLLSELGEDRIVILST 186
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
101-293 |
1.05e-20 |
|
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: 97.21 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 101 FSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALAnRIAKGSlKGNVTLNG--------EVLNSKMqkaisAYVM 172
Cdd:COG2274 483 YPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL-GLYEPT-SGRILIDGidlrqidpASLRRQI-----GVVL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 173 QDDLLFPMlTVEETLMFAAEFRlprSLSKSKKSLR---VQALIDQL--GLrnaaNTVIGDEGhRGISGGERRRVSIGIDI 247
Cdd:COG2274 556 QDVFLFSG-TIRENITLGDPDA---TDEEIIEAARlagLHDFIEALpmGY----DTVVGEGG-SNLSGGQRQRLAIARAL 626
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15240660 248 IHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTlHQPS 293
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIA-HRLS 671
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
103-288 |
1.28e-20 |
|
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: 90.87 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 103 SKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALanriakGSL----KGNVTLNGEVLNSKMQKAISA-------YV 171
Cdd:TIGR02211 15 KLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLL------GGLdnptSGEVLFNGQSLSKLSSNERAKlrnkklgFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 172 MQDDLLFPMLTVEETLMFAAefrLPRSLSKSKKSLRVQALIDQLGLRNAANtvigdegHRG--ISGGERRRVSIGIDIIH 249
Cdd:TIGR02211 89 YQFHHLLPDFTALENVAMPL---LIGKKSVKEAKERAYEMLEKVGLEHRIN-------HRPseLSGGERQRVAIARALVN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15240660 250 DPILLFLDEPTSGLDSTSALSVIKVLKRI--AQSGSMVIMT 288
Cdd:TIGR02211 159 QPSLVLADEPTGNLDNNNAKIIFDLMLELnrELNTSFLVVT 199
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
115-280 |
1.73e-20 |
|
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: 93.63 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 115 EARDGEILAVLGASGSGKSTLIDALAnriakGSLK---GNVTLNGEVLNSKmQKAIS--------AYVMQDDLLFPMLTV 183
Cdd:COG4148 21 TLPGRGVTALFGPSGSGKTTLLRAIA-----GLERpdsGRIRLGGEVLQDS-ARGIFlpphrrriGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 184 EETLMFAAEfRLPRSLSKskksLRVQALIDQLGLrnaantvigdeGH------RGISGGERRRVSIGIDIIHDPILLFLD 257
Cdd:COG4148 95 RGNLLYGRK-RAPRAERR----ISFDEVVELLGI-----------GHlldrrpATLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180
....*....|....*....|...
gi 15240660 258 EPTSGLDSTSALSVIKVLKRIAQ 280
Cdd:COG4148 159 EPLAALDLARKAEILPYLERLRD 181
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
101-280 |
1.92e-20 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 92.81 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 101 FSSKTKTL--LNGITGEARDGEILAVLGASGSGKSTLIDALANRIAK-GSLKGNVTLNGEVLNSKMQKAIS-------AY 170
Cdd:COG0444 11 FPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpGITSGEILFDGEDLLKLSEKELRkirgreiQM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 171 VMQDDL--LFPMLTVEETLMFAaeFRLPRSLSKSKKSLRVQALIDQLGLRNAANtVIGDEGHRgISGGERRRVSIGIDII 248
Cdd:COG0444 91 IFQDPMtsLNPVMTVGDQIAEP--LRIHGGLSKAEARERAIELLERVGLPDPER-RLDRYPHE-LSGGMRQRVMIARALA 166
|
170 180 190
....*....|....*....|....*....|..
gi 15240660 249 HDPILLFLDEPTSGLDSTSALSVIKVLKRIAQ 280
Cdd:COG0444 167 LEPKLLIADEPTTALDVTIQAQILNLLKDLQR 198
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
101-291 |
3.31e-20 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 89.93 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 101 FSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALaNRIAKGSLK----GNVTLNGEVLNSKMQKAIS-----AYV 171
Cdd:cd03260 8 VYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLL-NRLNDLIPGapdeGEVLLDGKDIYDLDVDVLElrrrvGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 172 MQDDLLFPMlTVEETLMFAAefRLPRSLSKS------KKSLRVQALIDQLGLRNAAntvigdeghRGISGGERRRVSIGI 245
Cdd:cd03260 87 FQKPNPFPG-SIYDNVAYGL--RLHGIKLKEeldervEEALRKAALWDEVKDRLHA---------LGLSGGQQQRLCLAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15240660 246 DIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMT--LHQ 291
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVThnMQQ 202
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
109-280 |
3.35e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 90.87 E-value: 3.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALAnriakGSLK---GNVTLNGEVLNSKMQKAISAYVM----QDDLLFPML 181
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLIT-----GFYRptsGRILFDGRDITGLPPHRIARLGIartfQNPRLFPEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 182 TVEETLMFAAEFRLPRSLSKSKKSL------------RVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIH 249
Cdd:COG0411 95 TVLENVLVAAHARLGRGLLAALLRLprarreereareRAEELLERVGLADRADEPAGN-----LSYGQQRRLEIARALAT 169
|
170 180 190
....*....|....*....|....*....|.
gi 15240660 250 DPILLFLDEPTSGLDSTSALSVIKVLKRIAQ 280
Cdd:COG0411 170 EPKLLLLDEPAAGLNPEETEELAELIRRLRD 200
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
109-278 |
4.06e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 92.47 E-value: 4.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALA--NRIAKGSlkgnVTLNGEVLNskmqkAISAY------VMQDDLLFPM 180
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAgfETPDSGR----ILLDGRDVT-----GLPPEkrnvgmVFQDYALFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 181 LTVEETLMFAAEFrlpRSLSKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPT 260
Cdd:COG3842 92 LTVAENVAFGLRM---RGVPKAEIRARVAELLELVGLEGLADRYPHQ-----LSGGQQQRVALARALAPEPRVLLLDEPL 163
|
170
....*....|....*...
gi 15240660 261 SGLDSTSALSVIKVLKRI 278
Cdd:COG3842 164 SALDAKLREEMREELRRL 181
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
104-291 |
4.68e-20 |
|
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: 89.20 E-value: 4.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 104 KTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGevlnSKMQKAISAY-----VMQDDLLF 178
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDS--GEITFDG----KSYQKNIEALrrigaLIEAPGFY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 179 PMLTVEETL-MFAAEFRLPRSlskskkslRVQALIDQLGLRNaantvIGDEGHRGISGGERRRVSIGIDIIHDPILLFLD 257
Cdd:cd03268 85 PNLTARENLrLLARLLGIRKK--------RIDEVLDVVGLKD-----SAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190
....*....|....*....|....*....|....
gi 15240660 258 EPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLHQ 291
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHL 185
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
107-288 |
5.64e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 89.77 E-value: 5.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 107 TLLNGITGEARDGEILAVLGASGSGKSTL---IDALaNRIAKGSLK-GNVTLNGEVLNSKMQKAISAYVMQDDLLFPMLT 182
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLlrcINKL-EEITSGDLIvDGLKVNDPKVDERLIRQEAGMVFQQFYLFPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 183 VEETLMFAAefRLPRSLSKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPTSG 262
Cdd:PRK09493 94 ALENVMFGP--LRVRGASKEEAEKQARELLAKVGLAERAHHYPSE-----LSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180
....*....|....*....|....*..
gi 15240660 263 LDSTSALSVIKVLKRIAQSG-SMVIMT 288
Cdd:PRK09493 167 LDPELRHEVLKVMQDLAEEGmTMVIVT 193
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
104-290 |
2.74e-19 |
|
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: 87.60 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 104 KTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLnSKM------QKAISaYVMQDDLL 177
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDS--GKILLDGQDI-TKLpmhkraRLGIG-YLPQEASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 178 FPMLTVEETLMFAAEFRlprSLSKSKKSLRVQALIDQLGLRNAANTVIGdeghrGISGGERRRVSIGIDIIHDPILLFLD 257
Cdd:cd03218 87 FRKLTVEENILAVLEIR---GLSKKEREEKLEELLEEFHITHLRKSKAS-----SLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190
....*....|....*....|....*....|...
gi 15240660 258 EPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRGIGVLITDH 191
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
120-281 |
3.28e-19 |
|
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: 89.79 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 120 EILAVLGASGSGKSTLIDALANRIAKGslKGNVTLNGEVLNSKMQKAIS-------AYVMQDDLLFPMLTVEETLMFAAE 192
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGLTRPD--EGEIVLNGRTLFDSRKGIFLppekrriGYVFQEARLFPHLSVRGNLRYGMK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 193 FRLPrslskSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSALSVI 272
Cdd:TIGR02142 102 RARP-----SERRISFERVIELLGIGHLLGRLPGR-----LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
....*....
gi 15240660 273 KVLKRIAQS 281
Cdd:TIGR02142 172 PYLERLHAE 180
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
115-293 |
4.15e-19 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 91.19 E-value: 4.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 115 EARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVL---NSKMQKAISAYVMQDDLLFPMlTVEETLMFAa 191
Cdd:TIGR02857 344 TVPPGERVALVGPSGAGKSTLLNLLLGFVDPTE--GSIAVNGVPLadaDADSWRDQIAWVPQHPFLFAG-TIAENIRLA- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 192 efRLPRSLSKSKKSLRvQALIDQL--GLRNAANTVIGDEGhRGISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSAL 269
Cdd:TIGR02857 420 --RPDASDAEIREALE-RAGLDEFvaALPQGLDTPIGEGG-AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEA 495
|
170 180
....*....|....*....|....
gi 15240660 270 SVIKVLKRIAQsGSMVIMTLHQPS 293
Cdd:TIGR02857 496 EVLEALRALAQ-GRTVLLVTHRLA 518
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
106-290 |
6.21e-19 |
|
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: 86.58 E-value: 6.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIdALANRIaKGSLKGNVTLNGEVLNSKMQKAIS--AYVMQDDLLFPMLTV 183
Cdd:TIGR03864 14 RRALDDVSFTVRPGRFVALLGPNGAGKSTLF-SLLTRL-YVAQSGQISVAGHDLRRAPRAALArlGVVFQQPTLDLDLSV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 184 EETLMF-AAEFRLPRSLSKSkkslRVQALIDQLGLRNAAntvigDEGHRGISGGERRRVSIGIDIIHDPILLFLDEPTSG 262
Cdd:TIGR03864 92 RQNLRYhAALHGLSRAEARA----RIAELLARLGLAERA-----DDKVRELNGGHRRRVEIARALLHRPALLLLDEPTVG 162
|
170 180
....*....|....*....|....*....
gi 15240660 263 LDSTSALSVIKVLKRIAQSGSM-VIMTLH 290
Cdd:TIGR03864 163 LDPASRAAITAHVRALARDQGLsVLWATH 191
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
106-292 |
8.93e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 85.31 E-value: 8.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKgsLKGNVTLNGEVLNSKMQKAISAYVMQDDLLFPMLTVEE 185
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP--AAGTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 186 TLMFAAEFRLPRSLSkskkslrVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIG-IDIIHDPILLfLDEPTSGLD 264
Cdd:PRK13539 93 NLEFWAAFLGGEELD-------IAAALEAVGLAPLAHLPFGY-----LSAGQKRRVALArLLVSNRPIWI-LDEPTAALD 159
|
170 180
....*....|....*....|....*....
gi 15240660 265 STS-ALSVIKVLKRIAQsGSMVIMTLHQP 292
Cdd:PRK13539 160 AAAvALFAELIRAHLAQ-GGIVIAATHIP 187
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
109-290 |
1.05e-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: 84.78 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALAnriakGSLK---GNVTLNGEVLNSKMQKAIS-----AYVMQ--DDLLF 178
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLN-----GLLRpqsGAVLIDGEPLDYSRKGLLErrqrvGLVFQdpDDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 179 PMlTVEETLMFAaefrlPRSLSKSKKSL--RVQ---ALIDQLGLRNAANTVIgdeghrgiSGGERRRVSIGIDIIHDPIL 253
Cdd:TIGR01166 83 AA-DVDQDVAFG-----PLNLGLSEAEVerRVRealTAVGASGLRERPTHCL--------SGGEKKRVAIAGAVAMRPDV 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 15240660 254 LFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:TIGR01166 149 LLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
107-292 |
1.06e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.59 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 107 TLLNGITGEARDGEILAVLGASGSGKSTLIDALAnriakGSLKgnvTLNGEVlnSKMQKAISAYVMQ---DDLLFPmLTV 183
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLA-----GVLR---PTSGTV--RRAGGARVAYVPQrseVPDSLP-LTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 184 EETLMFA--AEFRLPRSLSKSKKSLRVQALiDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPTS 261
Cdd:NF040873 75 RDLVAMGrwARRGLWRRLTRDDRAAVDDAL-ERVGLADLAGRQLGE-----LSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190
....*....|....*....|....*....|.
gi 15240660 262 GLDSTSALSVIKVLKRIAQSGSMVIMTLHQP 292
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
102-290 |
2.50e-18 |
|
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: 85.02 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 102 SSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGE-VLNSKMQKAISA---YVMQDDLL 177
Cdd:TIGR04406 10 SYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDA--GKILIDGQdITHLPMHERARLgigYLPQEASI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 178 FPMLTVEETLMFAAEFRlpRSLSKSKKSLRVQALIDQLGLrnaanTVIGDEGHRGISGGERRRVSIGIDIIHDPILLFLD 257
Cdd:TIGR04406 88 FRKLTVEENIMAVLEIR--KDLDRAEREERLEALLEEFQI-----SHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190
....*....|....*....|....*....|...
gi 15240660 258 EPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHLKERGIGVLITDH 193
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
107-293 |
2.77e-18 |
|
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: 84.41 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 107 TLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKMQKAISA-------YVMQDDLLFP 179
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTS--GTVRLAGQDLFALDEDARARlrarhvgFVFQSFQLLP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 180 MLTVEETLMFAAEFrlpRSLSKSKKslRVQALIDQLGLrnaantvigdeGHR------GISGGERRRVSIGIDIIHDPIL 253
Cdd:COG4181 104 TLTALENVMLPLEL---AGRRDARA--RARALLERVGL-----------GHRldhypaQLSGGEQQRVALARAFATEPAI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15240660 254 LFLDEPTSGLDSTSALSVIKVLKRI-AQSGSMVIMTLHQPS 293
Cdd:COG4181 168 LFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPA 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
103-290 |
3.36e-18 |
|
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: 83.96 E-value: 3.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 103 SKTKTLLNGITGEARDGEILAVLGASGSGKSTLIdalanRIAKGSLK---GNVTLNG-EVLNSKMQ-KAISAYVMQDDLL 177
Cdd:cd03266 15 KKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTL-----RMLAGLLEpdaGFATVDGfDVVKEPAEaRRRLGFVSDSTGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 178 FPMLTVEETLMFAAEFRlprSLSKSKKSLRVQALIDQLGLRNAANTVIGdeghrGISGGERRRVSIGIDIIHDPILLFLD 257
Cdd:cd03266 90 YDRLTARENLEYFAGLY---GLKGDELTARLEELADRLGMEELLDRRVG-----GFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190
....*....|....*....|....*....|...
gi 15240660 258 EPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFSTH 194
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
107-265 |
3.89e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 86.35 E-value: 3.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 107 TLLNGITGEARDGEILAVLGASGSGKSTLIDALAnriakGSLK---GNVTLNGEVLNSKM---QKAIsAYVMQDDLLFPM 180
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIA-----GLETpdsGRIVLNGRDLFTNLpprERRV-GFVFQHYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 181 LTVEETLMFAAEFRLPrslSKSKKSLRVQALIDQLGLrnaantviGDEGHR---GISGGERRRVSIGIDIIHDPILLFLD 257
Cdd:COG1118 90 MTVAENIAFGLRVRPP---SKAEIRARVEELLELVQL--------EGLADRypsQLSGGQRQRVALARALAVEPEVLLLD 158
|
....*...
gi 15240660 258 EPTSGLDS 265
Cdd:COG1118 159 EPFGALDA 166
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
71-290 |
9.67e-18 |
|
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: 83.15 E-value: 9.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 71 TDLTYSVKVRRKFTWRrsvssdpGAPSEGIFSSKTKTL--LNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSl 148
Cdd:cd03267 4 SNLSKSYRVYSKEPGL-------IGSLKSLFKRKYREVeaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTS- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 149 kGNVTLNGEV---LNSKMQKAISAYVMQDDLLFPMLTVEETL-MFAAEFRLPRSLSKSkkslRVQALIDQLGLrnaanTV 224
Cdd:cd03267 76 -GEVRVAGLVpwkRRKKFLRRIGVVFGQKTQLWWDLPVIDSFyLLAAIYDLPPARFKK----RLDELSELLDL-----EE 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15240660 225 IGDEGHRGISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSALSVIKVLKRI-AQSGSMVIMTLH 290
Cdd:cd03267 146 LLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSH 212
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
106-287 |
1.51e-17 |
|
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: 82.83 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGN-VTLNGEVLNS----KMQKAIsAYV---MQDDLL 177
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTY--GNdVRLFGERRGGedvwELRKRI-GLVspaLQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 178 fPMLTVEETLM--FAAEFRLPRSLSKSKKSlRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLF 255
Cdd:COG1119 93 -RDETVLDVVLsgFFDSIGLYREPTDEQRE-RARELLELLGLAHLADRPFGT-----LSQGEQRRVLIARALVKDPELLI 165
|
170 180 190
....*....|....*....|....*....|..
gi 15240660 256 LDEPTSGLDSTSALSVIKVLKRIAQSGSMVIM 287
Cdd:COG1119 166 LDEPTAGLDLGARELLLALLDKLAAEGAPTLV 197
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
106-290 |
1.77e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 82.90 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLN--SKMQKAISAYVM--QDDLLFPmL 181
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDS--GEVRLNGRPLAdwSPAELARRRAVLpqHSSLSFP-F 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 182 TVEETLMFAaefRLPRSLSKSKKSLRVQALIDQLGLrnaanTVIGDEGHRGISGGERRRV----------SIGidiiHDP 251
Cdd:PRK13548 92 TVEEVVAMG---RAPHGLSRAEDDALVAAALAQVDL-----AHLAGRDYPQLSGGEQQRVqlarvlaqlwEPD----GPP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15240660 252 ILLFLDEPTSGLDSTSALSVIKVLKRIA-QSGSMVIMTLH 290
Cdd:PRK13548 160 RWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLH 199
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
106-290 |
1.80e-17 |
|
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: 82.28 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALAnRIAKgSLKGNVTLNG----EVLNSKMQKAIsAYVMQDDLLFpml 181
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLF-RFYD-VSSGSILIDGqdirEVTLDSLRRAI-GVVPQDTVLF--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 182 tvEETLMFAAEFRLPRS----LSKSKKSLRVQALIdqLGLRNAANTVIGDEGHRgISGGERRRVSIGIDIIHDPILLFLD 257
Cdd:cd03253 88 --NDTIGYNIRYGRPDAtdeeVIEAAKAAQIHDKI--MRFPDGYDTIVGERGLK-LSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190
....*....|....*....|....*....|...
gi 15240660 258 EPTSGLDSTSALSVIKVLKRIAQsGSMVIMTLH 290
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVSK-GRTTIVIAH 194
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
109-290 |
4.21e-17 |
|
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: 80.97 E-value: 4.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALANrIAKGSlKGNVTLNGEVLNS----KMqkaisaYVMQDDLLFPMLTVE 184
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISG-LAQPT-SGGVILEGKQITEpgpdRM------VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 185 ETLMFAAEfRLPRSLSKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPTSGLD 264
Cdd:TIGR01184 73 ENIALAVD-RVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ-----LSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180
....*....|....*....|....*..
gi 15240660 265 STSALSVIKVLKRIAQ-SGSMVIMTLH 290
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEeHRVTVLMVTH 173
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
108-293 |
5.17e-17 |
|
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: 80.99 E-value: 5.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 108 LLNGITGEARDGEILAVLGASGSGKSTLIDaLANRIAKGSlKGNVTLNGE---VLNSKMQKAISAYVMQDDLLFPMlTVE 184
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTK-LIQRFYVPE-NGRVLVDGHdlaLADPAWLRRQVGVVLQENVLFNR-SIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 185 ETLMFAAEFRLPRSLSKSKKSLRVQALIDQLglRNAANTVIGDEGhRGISGGERRRVSIGIDIIHDPILLFLDEPTSGLD 264
Cdd:cd03252 94 DNIALADPGMSMERVIEAAKLAGAHDFISEL--PEGYDTIVGEQG-AGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180
....*....|....*....|....*....
gi 15240660 265 STSALSVIKVLKRIAqSGSMVIMTLHQPS 293
Cdd:cd03252 171 YESEHAIMRNMHDIC-AGRTVIIIAHRLS 198
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
102-291 |
6.14e-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: 80.70 E-value: 6.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 102 SSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALaNRIAKGSlKGNVTLNGEVL----NSKMQKAIS--AYVMQDD 175
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI-NGLERPT-SGSVLVDGTDLtllsGKELRKARRriGMIFQHF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 176 LLFPMLTVEETLMFAAEFRlprSLSKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLF 255
Cdd:cd03258 92 NLLSSRTVFENVALPLEIA---GVPKAEIEERVLELLELVGLEDKADAYPAQ-----LSGGQKQRVGIARALANNPKVLL 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 15240660 256 LDEPTSGLDSTSALSVIKVLKRIAQS-GSMVIMTLHQ 291
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDINRElGLTIVLITHE 200
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
118-290 |
8.30e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 81.06 E-value: 8.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 118 DGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKmqKAISAYVMQDDLLFPMLTVEETLMFAaeFRLpR 197
Cdd:COG4525 32 SGEFVVALGASGCGKTTLLNLIAGFLAPSS--GEITLDGVPVTGP--GADRGVVFQKDALLPWLNVLDNVAFG--LRL-R 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 198 SLSKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSALSVIKVLKR 277
Cdd:COG4525 105 GVPKAERRARAEELLALVGLADFARRRIWQ-----LSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLD 179
|
170
....*....|....
gi 15240660 278 I-AQSGSMVIMTLH 290
Cdd:COG4525 180 VwQRTGKGVFLITH 193
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
119-293 |
1.85e-16 |
|
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: 78.69 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 119 GEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNG-EVLNSKMQKAISAYVMQDDLLFPMLTVEETLMFAaefRLPR 197
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQS--GRVLINGvDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLG---LSPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 198 SLSKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHD-PILLfLDEPTSGLDSTSALSVIK-VL 275
Cdd:cd03298 99 LKLTAEDRQAIEVALARVGLAGLEKRLPGE-----LSGGERQRVALARVLVRDkPVLL-LDEPFAALDPALRAEMLDlVL 172
|
170
....*....|....*...
gi 15240660 276 KRIAQSGSMVIMTLHQPS 293
Cdd:cd03298 173 DLHAETKMTVLMVTHQPE 190
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
104-290 |
2.03e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 79.55 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 104 KTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGE-----VLNSKMQKAIsAYVMQDDLLF 178
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA--GNIIIDDEdisllPLHARARRGI-GYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 179 PMLTVEETLMFAAEFRlpRSLSKSKKSLRVQALIDQLGLRNAANTVigdegHRGISGGERRRVSIGIDIIHDPILLFLDE 258
Cdd:PRK10895 91 RRLSVYDNLMAVLQIR--DDLSAEQREDRANELMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190
....*....|....*....|....*....|..
gi 15240660 259 PTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDH 195
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
101-293 |
2.18e-16 |
|
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: 78.81 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 101 FS-SKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDaLANRIAKGSlKGNVTLNGEVLNSKMQKAIS---AYVMQDDL 176
Cdd:cd03254 10 FSyDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLIN-LLMRFYDPQ-KGQILIDGIDIRDISRKSLRsmiGVVLQDTF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 177 LFPMlTVEETLmfaaefRLPRSLSKSKKSLRV--QALIDQLG--LRNAANTVIGDEGHrGISGGERRRVSIGIDIIHDPI 252
Cdd:cd03254 88 LFSG-TIMENI------RLGRPNATDEEVIEAakEAGAHDFImkLPNGYDTVLGENGG-NLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15240660 253 LLFLDEPTSGLDSTSALSVIKVLKRIaQSGSMVIMTLHQPS 293
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLS 199
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
104-264 |
2.69e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 78.92 E-value: 2.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 104 KTKTLLNGITGEARDGEILAVLGASGSGKST-------LI--DAlanriakgslkGNVTLNGEVLnSKM------QKAIS 168
Cdd:COG1137 14 GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTtfymivgLVkpDS-----------GRIFLDGEDI-THLpmhkraRLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 169 aYVMQDDLLFPMLTVEETLMFAAEFRlprSLSKSKKSLRVQALIDQLGLRNAANTvigdeghRGI--SGGERRRVSIGID 246
Cdd:COG1137 82 -YLPQEASIFRKLTVEDNILAVLELR---KLSKKEREERLEELLEEFGITHLRKS-------KAYslSGGERRRVEIARA 150
|
170
....*....|....*...
gi 15240660 247 IIHDPILLFLDEPTSGLD 264
Cdd:COG1137 151 LATNPKFILLDEPFAGVD 168
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
119-292 |
2.82e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 78.64 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 119 GEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSK--MQKAISAyVMQDDLLFPMLTVEETLMFAaeFRLP 196
Cdd:COG3840 25 GERVAILGPSGAGKSTLLNLIAGFLPPDS--GRILWNGQDLTALppAERPVSM-LFQENNLFPHLTVAQNIGLG--LRPG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 197 RSLSKSKKSlRVQALIDQLGLRNaantvIGDEGHRGISGGERRRVSIGIDIIHD-PILLfLDEPTSGLDstSAL--SVIK 273
Cdd:COG3840 100 LKLTAEQRA-QVEQALERVGLAG-----LLDRLPGQLSGGQRQRVALARCLVRKrPILL-LDEPFSALD--PALrqEMLD 170
|
170 180
....*....|....*....|
gi 15240660 274 VLKRIAQS-GSMVIMTLHQP 292
Cdd:COG3840 171 LVDELCRErGLTVLMVTHDP 190
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
109-290 |
3.55e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 79.35 E-value: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALaNRIAKGSlKGNVTLNGEVLNSKMQKAISA-----YVMQ--DDLLF-Pm 180
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHF-NGILKPT-SGEVLIKGEPIKYDKKSLLEVrktvgIVFQnpDDQLFaP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 181 lTVEETLMFAAefrLPRSLSKSKKSLRVQALIDQLGLRNAANTVigdeGHRgISGGERRRVSIGIDIIHDPILLFLDEPT 260
Cdd:PRK13639 95 -TVEEDVAFGP---LNLGLSKEEVEKRVKEALKAVGMEGFENKP----PHH-LSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190
....*....|....*....|....*....|
gi 15240660 261 SGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLNKEGITIIISTH 195
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
106-290 |
3.62e-16 |
|
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: 78.43 E-value: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNG-EVLNSKMQKAISAYVMQDDLLFPMLTVE 184
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTS--GEILLDGkDITNLPPHKRPVNTVFQNYALFPHLTVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 185 ETLMFAaeFRLpRSLSKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPTSGLD 264
Cdd:cd03300 91 ENIAFG--LRL-KKLPKAEIKERVAEALDLVQLEGYANRKPSQ-----LSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180
....*....|....*....|....*..
gi 15240660 265 STSALSVIKVLKRIAQS-GSMVIMTLH 290
Cdd:cd03300 163 LKLRKDMQLELKRLQKElGITFVFVTH 189
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
108-291 |
4.34e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.86 E-value: 4.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 108 LLNGITGEARDGEILAVLGASGSGKSTLIDALaNRIAKGSlKGNVTLNGEVLNS----------------KMQKAISAYV 171
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEKPS-EGSIVVNGQTINLvrdkdgqlkvadknqlRLLRTRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 172 MQDDLLFPMLTVEETLMFAAEFRLprSLSKSKKSLRVQALIDQLGLrnaantvigDEGHRG-----ISGGERRRVSIGID 246
Cdd:PRK10619 98 FQHFNLWSHMTVLENVMEAPIQVL--GLSKQEARERAVKYLAKVGI---------DERAQGkypvhLSGGQQQRVSIARA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15240660 247 IIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLHQ 291
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
93-290 |
8.58e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 77.82 E-value: 8.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 93 PGAPSEgifssktKTLLNGITGEARDGEILAVLGASGSGKSTLIDALAnriakGSLK---GNVTLNGEVLNSKMQKAISA 169
Cdd:COG1101 13 PGTVNE-------KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIA-----GSLPpdsGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 170 Y---VMQDDLL--FPMLTVEETLMFAAEFRLPRSLSKSKKSLRVQALIDQL-----GLRNAANTVIGDeghrgISGGERR 239
Cdd:COG1101 81 YigrVFQDPMMgtAPSMTIEENLALAYRRGKRRGLRRGLTKKRRELFRELLatlglGLENRLDTKVGL-----LSGGQRQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15240660 240 RVSIGIDIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSM-VIMTLH 290
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLtTLMVTH 207
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
106-290 |
9.02e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 78.69 E-value: 9.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKMQKAIS--AYVMQDDLLFPMLTV 183
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDA--GSISLCGEPVPSRARHARQrvGVVPQFDNLDPDFTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 184 EETLM-FAAEFrlprSLSKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPTSG 262
Cdd:PRK13537 98 RENLLvFGRYF----GLSAAAARALVPPLLEFAKLENKADAKVGE-----LSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180
....*....|....*....|....*...
gi 15240660 263 LDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:PRK13537 169 LDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
106-282 |
1.50e-15 |
|
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: 77.15 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANrIAKGSlKGNVTLNGEVLnSKMQKAISAYVMQD-DLLF------ 178
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLG-LEKPA-QGTVSFRGQDL-YQLDRKQRRAFRRDvQLVFqdspsa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 179 --PMLTVEETLmfAAEFRLPRSLSKSKKSLRVQALIDQLGLRNAantvIGDEGHRGISGGERRRVSIGIDIIHDPILLFL 256
Cdd:TIGR02769 101 vnPRMTVRQII--GEPLRHLTSLDESEQKARIAELLDMVGLRSE----DADKLPRQLSGGQLQRINIARALAVKPKLIVL 174
|
170 180
....*....|....*....|....*.
gi 15240660 257 DEPTSGLDSTSALSVIKVLKRIAQSG 282
Cdd:TIGR02769 175 DEAVSNLDMVLQAVILELLRKLQQAF 200
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
118-291 |
1.50e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 81.21 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 118 DGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKMQKAISAYVM--QDDLLFPMLTVEETLMFAAEFRl 195
Cdd:TIGR01257 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTS--GTVLVGGKDIETNLDAVRQSLGMcpQHNILFHHLTVAEHILFYAQLK- 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 196 prSLSKSKKSLRVQALIDQLGLRNAANtvigdEGHRGISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSALSVIKVL 275
Cdd:TIGR01257 1032 --GRSWEEAQLEMEAMLEDTGLHHKRN-----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170
....*....|....*.
gi 15240660 276 KRIaQSGSMVIMTLHQ 291
Cdd:TIGR01257 1105 LKY-RSGRTIIMSTHH 1119
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
104-294 |
1.89e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 76.71 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 104 KTKTLLNGITGEARDGEILAVLGASGSGKSTLIDA--LANRIAKGSLK-GNVTLNGEVLNSKMQKAISA------YVMQD 174
Cdd:PRK11264 14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCinLLEQPEAGTIRvGDITIDTARSLSQQKGLIRQlrqhvgFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 175 DLLFPMLTVEETLMFAaefrlPRSLSKSKKS---LRVQALIDQLGLRNAANTVigdegHRGISGGERRRVSIGIDIIHDP 251
Cdd:PRK11264 94 FNLFPHRTVLENIIEG-----PVIVKGEPKEeatARARELLAKVGLAGKETSY-----PRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15240660 252 ILLFLDEPTSGLDSTSALSVIKVLKRIAQSG-SMVIMTlHQPSY 294
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVT-HEMSF 206
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
109-294 |
2.21e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.98 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSLKG-NVTLNGEVLNS--------KMQKAISAYVMQDDLLFP 179
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGsHIELLGRTVQRegrlardiRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 180 MLTVEETLMFAAEFRLP------RSLSKSKKSLRVQALIdQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPIL 253
Cdd:PRK09984 100 RLSVLENVLIGALGSTPfwrtcfSWFTREQKQRALQALT-RVGMVHFAHQRVST-----LSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15240660 254 LFLDEPTSGLDSTSALSVIKVLKRIAQS-GSMVIMTLHQPSY 294
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDY 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
109-292 |
2.48e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.77 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALA--NRIAKGSLK---GNV-TLNGEVLnSKMQKAISAYVMQDDLLFPMLT 182
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGclDKPTSGTYRvagQDVaTLDADAL-AQLRREHFGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 183 VEETLMFAAEFRlprSLSKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPTSG 262
Cdd:PRK10535 103 AAQNVEVPAVYA---GLERKQRLLRAQELLQRLGLEDRVEYQPSQ-----LSGGQQQRVSIARALMNGGQVILADEPTGA 174
|
170 180 190
....*....|....*....|....*....|
gi 15240660 263 LDSTSALSVIKVLKRIAQSGSMVIMTLHQP 292
Cdd:PRK10535 175 LDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
109-280 |
2.60e-15 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 75.73 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALAnRIAKGSlKGNVTLNG----EVLNSKMQKAIsAYVMQDDLLFPMlTVE 184
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIP-RFYDVD-SGRILIDGhdvrDYTLASLRRQI-GLVSQDVFLFND-TVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 185 ETLMFAAEFRLPRSLSKSKKSLRVQALIDQLglRNAANTVIGDEGHRgISGGERRRVSIGIDIIHDPILLFLDEPTSGLD 264
Cdd:cd03251 94 ENIAYGRPGATREEVEEAARAANAHEFIMEL--PEGYDTVIGERGVK-LSGGQRQRIAIARALLKDPPILILDEATSALD 170
|
170
....*....|....*.
gi 15240660 265 STSALSVIKVLKRIAQ 280
Cdd:cd03251 171 TESERLVQAALERLMK 186
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
119-293 |
2.81e-15 |
|
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: 75.32 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 119 GEILAVLGASGSGKSTLidalaNRIAKGSLK---GNVTLNG----EVLNSKMQKAISaYVMQDDLLFpMLTVEETLMFAA 191
Cdd:cd03245 30 GEKVAIIGRVGSGKSTL-----LKLLAGLYKptsGSVLLDGtdirQLDPADLRRNIG-YVPQDVTLF-YGTLRDNITLGA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 192 efrlprSLSKSKKSLRVQAL--IDQLGLRNAA--NTVIGdEGHRGISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTS 267
Cdd:cd03245 103 ------PLADDERILRAAELagVTDFVNKHPNglDLQIG-ERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNS 175
|
170 180
....*....|....*....|....*.
gi 15240660 268 ALSVIKVLKRIAQSGSMVIMTlHQPS 293
Cdd:cd03245 176 EERLKERLRQLLGDKTLIIIT-HRPS 200
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
109-282 |
2.98e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.91 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSK-----MQKAISAyVMQDDLLFPMLTV 183
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDS--GEILLDGEPVRFRsprdaQAAGIAI-IHQELNLVPNLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 184 EETLMFAAEFRLPRSLSKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPTSGL 263
Cdd:COG1129 97 AENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGD-----LSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170
....*....|....*....
gi 15240660 264 DSTSALSVIKVLKRIAQSG 282
Cdd:COG1129 172 TEREVERLFRIIRRLKAQG 190
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
109-264 |
3.03e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 77.81 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALA--NRIAKGSlkgnVTLNGEVLNSKMQKA--IsAYVMQDDLLFPMLTVE 184
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAglEDPTSGE----ILIGGRDVTDLPPKDrnI-AMVFQSYALYPHMTVY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 185 ETLMFAAEFrlpRSLSKSKKSLRVQALIDQLGL-----RNAANtvigdeghrgISGGERRRVSIGIDIIHDPILLFLDEP 259
Cdd:COG3839 94 ENIAFPLKL---RKVPKAEIDRRVREAAELLGLedlldRKPKQ----------LSGGQRQRVALGRALVREPKVFLLDEP 160
|
....*
gi 15240660 260 TSGLD 264
Cdd:COG3839 161 LSNLD 165
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
119-290 |
3.20e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 77.95 E-value: 3.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 119 GEILAVLGASGSGKSTLIDALANriAKGSLKGNVTLNGEVLNS--KMQKAISAyVMQDDLLFPMLTVEETLMFAAEfrlP 196
Cdd:PRK11607 45 GEIFALLGASGCGKSTLLRMLAG--FEQPTAGQIMLDGVDLSHvpPYQRPINM-MFQSYALFPHMTVEQNIAFGLK---Q 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 197 RSLSKSKKSLRVQALIDQLGLRNAANTvigdEGHRgISGGERRRVSIGIDIIHDPILLFLDEPTSGLDST----SALSVI 272
Cdd:PRK11607 119 DKLPKAEIASRVNEMLGLVHMQEFAKR----KPHQ-LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVV 193
|
170
....*....|....*...
gi 15240660 273 KVLKRIaqsGSMVIMTLH 290
Cdd:PRK11607 194 DILERV---GVTCVMVTH 208
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
109-265 |
5.31e-15 |
|
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: 75.07 E-value: 5.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIdalanRIAKG---SLKGNVTLNGE-VLNSKMQKAISAYVMQDDLLFPMLTVE 184
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLL-----RLIAGlerPDSGTILFGGEdATDVPVQERNVGFVFQHYALFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 185 ETLMFAAEFRlPRSL--SKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPTSG 262
Cdd:cd03296 93 DNVAFGLRVK-PRSErpPEAEIRAKVHELLKLVQLDWLADRYPAQ-----LSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
...
gi 15240660 263 LDS 265
Cdd:cd03296 167 LDA 169
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
93-290 |
5.98e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 76.02 E-value: 5.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 93 PGAPSEgifsskTKTLLNgITGEARDGEILAVLGASGSGKSTLIDALaNRIAKGSlKGNVTLNGEVLNS--------KMQ 164
Cdd:PRK13641 14 PGTPME------KKGLDN-ISFELEEGSFVALVGHTGSGKSTLMQHF-NALLKPS-SGTITIAGYHITPetgnknlkKLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 165 KAIS-AYVMQDDLLFpmltvEETLMFAAEFRlPRSLSKSKKSLRVQAL--IDQLGLrnaaNTVIGDEGHRGISGGERRRV 241
Cdd:PRK13641 85 KKVSlVFQFPEAQLF-----ENTVLKDVEFG-PKNFGFSEDEAKEKALkwLKKVGL----SEDLISKSPFELSGGQMRRV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15240660 242 SIGIDIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
100-293 |
8.03e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.81 E-value: 8.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 100 IFSSKTKTLlNGITGEARDGEILAVLGASGSGKSTLIDALaNRIakGSLKGNVTLNGEVL-NSK-----------MQKAI 167
Cdd:PRK14239 13 VYYNKKKAL-NSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRM--NDLNPEVTITGSIVyNGHniysprtdtvdLRKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 168 sAYVMQDDLLFPMlTVEETLMFAaeFRLPRSLSKSK------KSLRVQALIDQLGLRNAANTVigdeghrGISGGERRRV 241
Cdd:PRK14239 89 -GMVFQQPNPFPM-SIYENVVYG--LRLKGIKDKQVldeaveKSLKGASIWDEVKDRLHDSAL-------GLSGGQQQRV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15240660 242 SIGIDIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMT--LHQPS 293
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTrsMQQAS 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
94-264 |
8.11e-15 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 75.37 E-value: 8.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 94 GAPSEGIFSSKTKTL-LNGITGEARDGEILAVLGASGSGKSTLIDALaNRIAKGSLkGNVTLNGEVLNSKMQKAIS---- 168
Cdd:cd03294 24 GKSKEEILKKTGQTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCI-NRLIEPTS-GKVLIDGQDIAAMSRKELRelrr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 169 ---AYVMQDDLLFPMLTVEETLMFAAEFrlpRSLSKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGI 245
Cdd:cd03294 102 kkiSMVFQSFALLPHRTVLENVAFGLEV---QGVPRAEREERAAEALELVGLEGWEHKYPDE-----LSGGMQQRVGLAR 173
|
170
....*....|....*....
gi 15240660 246 DIIHDPILLFLDEPTSGLD 264
Cdd:cd03294 174 ALAVDPDILLMDEAFSALD 192
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
102-294 |
8.76e-15 |
|
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: 73.66 E-value: 8.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 102 SSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKgsLKGNVTLNGEVlnskmqkaisAYVMQDDLLFPMl 181
Cdd:cd03250 14 EQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEK--LSGSVSVPGSI----------AYVSQEPWIQNG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 182 TVEETLMFAAEFRLPRslskSKKSLRVQAL---IDQLGLRNaaNTVIGDeghRGI--SGGERRRVSIGIDIIHDPILLFL 256
Cdd:cd03250 81 TIRENILFGKPFDEER----YEKVIKACALepdLEILPDGD--LTEIGE---KGInlSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 15240660 257 DEPTSGLDSTSALSVI-KVLKRIAQSGSMVIMTLHQPSY 294
Cdd:cd03250 152 DDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQL 190
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
106-293 |
9.43e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 77.90 E-value: 9.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDaLANR---IAKGSlkgnVTLNG--------EVLNSKMqkaisAYVMQD 174
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVN-LLLRfydPTSGR----ILIDGvdirdltlESLRRQI-----GVVPQD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 175 DLLFPMlTVEETLMFAaefRLPRSLSKSKKSLR-VQA--LIDQL--GLrnaaNTVIGDEGHRgISGGERRRVSIGIDIIH 249
Cdd:COG1132 423 TFLFSG-TIRENIRYG---RPDATDEEVEEAAKaAQAheFIEALpdGY----DTVVGERGVN-LSGGQRQRIAIARALLK 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15240660 250 DPILLFLDEPTSGLDSTSALSVIKVLKRIAQsGSMVIMTLHQPS 293
Cdd:COG1132 494 DPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLS 536
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
106-290 |
1.34e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 75.64 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKMQKAIS--AYVMQDDLLFPMLTV 183
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA--GKITVLGVPVPARARLARAriGVVPQFDNLDLEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 184 EETLM-FAAEFRLprslSKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPTSG 262
Cdd:PRK13536 132 RENLLvFGRYFGM----STREIEAVIPSLLEFARLESKADARVSD-----LSGGMKRRLTLARALINDPQLLILDEPTTG 202
|
170 180
....*....|....*....|....*...
gi 15240660 263 LDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:PRK13536 203 LDPHARHLIWERLRSLLARGKTILLTTH 230
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
101-286 |
1.49e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 73.98 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 101 FSSKTKTL----LNGITGEARDGEILAVLGASGSGKSTLIDALAnriakGSLK---GNVTLNGEVLNSKMQKAISAYVMq 173
Cdd:cd03237 3 YPTMKKTLgeftLEVEGGSISESEVIGILGPNGIGKTTFIKMLA-----GVLKpdeGDIEIELDTVSYKPQYIKADYEG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 174 ddllfpmlTVEETLMFAAEFRLPRSLSKSK--KSLRVQALIDQLgLRNaantvigdeghrgISGGERRRVSIGIDIIHDP 251
Cdd:cd03237 77 --------TVRDLLSSITKDFYTHPYFKTEiaKPLQIEQILDRE-VPE-------------LSGGELQRVAIAACLSKDA 134
|
170 180 190
....*....|....*....|....*....|....*...
gi 15240660 252 ILLFLDEPTSGLDSTSALSVIKVLKRIA---QSGSMVI 286
Cdd:cd03237 135 DIYLLDEPSAYLDVEQRLMASKVIRRFAennEKTAFVV 172
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
100-278 |
1.71e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 75.50 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 100 IFSSKTKTL--LNGITGEARDGEILAVLGASGSGKSTLIDALaNRIAKGSlKGNVTLNGEVLNS-------KMQKAISaY 170
Cdd:COG1135 10 TFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI-NLLERPT-SGSVLVDGVDLTAlserelrAARRKIG-M 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 171 VMQDDLLFPMLTVEETLMFAAEFrlpRSLSKSKKSLRVQALIDQLGLrnaantvigdEGHRG-----ISGGERRRVSIGI 245
Cdd:COG1135 87 IFQHFNLLSSRTVAENVALPLEI---AGVPKAEIRKRVAELLELVGL----------SDKADaypsqLSGGQKQRVGIAR 153
|
170 180 190
....*....|....*....|....*....|...
gi 15240660 246 DIIHDPILLFLDEPTSGLDSTSALSVIKVLKRI 278
Cdd:COG1135 154 ALANNPKVLLCDEATSALDPETTRSILDLLKDI 186
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
100-291 |
1.81e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.81 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 100 IFSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALAnriakGSL--KGNVTLNGEVLN----SKMQKAIsAYVMQ 173
Cdd:PRK11174 357 ILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALL-----GFLpyQGSLKINGIELReldpESWRKHL-SWVGQ 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 174 DDLLFPMlTVEETLMF----AAEFRLPRSLSKSKkslrVQALIDQL--GLrnaaNTVIGDEGhRGISGGERRRVSIGIDI 247
Cdd:PRK11174 431 NPQLPHG-TLRDNVLLgnpdASDEQLQQALENAW----VSEFLPLLpqGL----DTPIGDQA-AGLSVGQAQRLALARAL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15240660 248 IHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQsGSMVIMTLHQ 291
Cdd:PRK11174 501 LQPCQLLLLDEPTASLDAHSEQLVMQALNAASR-RQTTLMVTHQ 543
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
99-280 |
2.61e-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: 76.26 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 99 GIFSSKTKTL--LNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGslkGNVTLNGEVLNSKMQKAISAY------ 170
Cdd:COG4172 290 GLFRRTVGHVkaVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE---GEIRFDGQDLDGLSRRALRPLrrrmqv 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 171 VMQDDL--LFPMLTVEETLmfaAE-FRL-PRSLSKSKKSLRVQALIDQLGLrnaantvigDEGHRG-----ISGGERRRV 241
Cdd:COG4172 367 VFQDPFgsLSPRMTVGQII---AEgLRVhGPGLSAAERRARVAEALEEVGL---------DPAARHrypheFSGGQRQRI 434
|
170 180 190
....*....|....*....|....*....|....*....
gi 15240660 242 SIGIDIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQ 280
Cdd:COG4172 435 AIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQR 473
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
106-290 |
2.69e-14 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 73.10 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIdALANRIAKGSlKGNVTLNGEVLNS----KMQKAIsAYVMQDDLLFPML 181
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTM-KMINRLIEPT-SGEIFIDGEDIREqdpvELRRKI-GYVIQQIGLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 182 TVEETLMFaaefrLPRSL--SKSKKSLRVQALIDQLGLRNAAntvIGDEGHRGISGGERRRVSIGIDIIHDPILLFLDEP 259
Cdd:cd03295 91 TVEENIAL-----VPKLLkwPKEKIRERADELLALVGLDPAE---FADRYPHELSGGQQQRVGVARALAADPPLLLMDEP 162
|
170 180 190
....*....|....*....|....*....|..
gi 15240660 260 TSGLDSTSALSVIKVLKRIAQ-SGSMVIMTLH 290
Cdd:cd03295 163 FGALDPITRDQLQEEFKRLQQeLGKTIVFVTH 194
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
105-293 |
3.48e-14 |
|
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: 71.09 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 105 TKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNS--KMQK-AISAYVMQDDLLFPML 181
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTS--GRVRLDGADISQwdPNELgDHVGYLPQDDELFSGS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 182 TVEETLmfaaefrlprslskskkslrvqalidqlglrnaantvigdeghrgiSGGERRRVSIGIDIIHDPILLFLDEPTS 261
Cdd:cd03246 92 IAENIL----------------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190
....*....|....*....|....*....|..
gi 15240660 262 GLDSTSALSVIKVLKRIAQSGSMVIMTLHQPS 293
Cdd:cd03246 126 HLDVEGERALNQAIAALKAAGATRIVIAHRPE 157
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
99-294 |
3.60e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.90 E-value: 3.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 99 GIFSSKT--KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKgslKGNVTLNGEVLNSKMQKAISAY------ 170
Cdd:PRK15134 290 GILKRTVdhNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS---QGEIWFDGQPLHNLNRRQLLPVrhriqv 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 171 VMQD--DLLFPMLTVEETLMFAAEFRLPrSLSKSKKSLRVQALIDQLGLRNAANtvigdegHR---GISGGERRRVSIGI 245
Cdd:PRK15134 367 VFQDpnSSLNPRLNVLQIIEEGLRVHQP-TLSAAQREQQVIAVMEEVGLDPETR-------HRypaEFSGGQRQRIAIAR 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15240660 246 DIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSgsmvimtlHQPSY 294
Cdd:PRK15134 439 ALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQK--------HQLAY 479
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
104-264 |
4.30e-14 |
|
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: 71.90 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 104 KTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALA--NRIAKGslkgNVTLNGEVLN--SKMQKAIsAYVMQDDLLFP 179
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAglEEPTSG----RIYIGGRDVTdlPPKDRDI-AMVFQNYALYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 180 MLTVEETLMFAAEFRlprSLSKSKKSLRVQALIDQLGLRNaantvIGDEGHRGISGGERRRVSIGIDIIHDPILLFLDEP 259
Cdd:cd03301 86 HMTVYDNIAFGLKLR---KVPKDEIDERVREVAELLQIEH-----LLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
....*
gi 15240660 260 TSGLD 264
Cdd:cd03301 158 LSNLD 162
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
93-264 |
4.54e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 73.16 E-value: 4.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 93 PGAPSEgifssktKTLLNGITGEARDGEILAVLGASGSGKSTLIDALaNRIAKGSlKGNVTLNGEVLNSKMQKAIS---- 168
Cdd:PRK13637 14 EGTPFE-------KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHL-NGLLKPT-SGKIIIDGVDITDKKVKLSDirkk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 169 -AYVMQ--DDLLFpmltvEETLMFAAEFRlPRSL--SKSKKSLRVQALIDQLGLrnaANTVIGDEGHRGISGGERRRVSI 243
Cdd:PRK13637 85 vGLVFQypEYQLF-----EETIEKDIAFG-PINLglSEEEIENRVKRAMNIVGL---DYEDYKDKSPFELSGGQKRRVAI 155
|
170 180
....*....|....*....|.
gi 15240660 244 GIDIIHDPILLFLDEPTSGLD 264
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLD 176
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
109-290 |
5.49e-14 |
|
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: 72.19 E-value: 5.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIdALANRIAkGSLKGNVTLNGE---VLNSKMQKAISAYVMQDDLLFPMlTVEE 185
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVV-SLLERFY-DPTSGEILLDGVdirDLNLRWLRSQIGLVSQEPVLFDG-TIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 186 TLMFAAEfrlPRSLSKSKKSLRvQALIDQL--GLRNAANTVIGDEGHRgISGGERRRVSIGIDIIHDPILLFLDEPTSGL 263
Cdd:cd03249 96 NIRYGKP---DATDEEVEEAAK-KANIHDFimSLPDGYDTLVGERGSQ-LSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180
....*....|....*....|....*..
gi 15240660 264 DSTSALSVIKVLKRIAQsGSMVIMTLH 290
Cdd:cd03249 171 DAESEKLVQEALDRAMK-GRTTIVIAH 196
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
101-290 |
5.65e-14 |
|
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: 70.80 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 101 FSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAkgSLKGNVTLNGEVLnSKMQKAISAYVM---QDDLL 177
Cdd:cd03247 10 YPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLK--PQQGEITLDGVPV-SDLEKALSSLISvlnQRPYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 178 FpmltvEETLMfaaefrlprslskskkslrvqaliDQLGLRnaantvigdeghrgISGGERRRVSIGIDIIHDPILLFLD 257
Cdd:cd03247 87 F-----DTTLR------------------------NNLGRR--------------FSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190
....*....|....*....|....*....|...
gi 15240660 258 EPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:cd03247 124 EPTVGLDPITERQLLSLIFEVLKDKTLIWITHH 156
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
101-290 |
7.29e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.51 E-value: 7.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 101 FSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKMQKAIS---AYVMQDDLL 177
Cdd:PRK10575 19 FRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSE--GEILLDAQPLESWSSKAFArkvAYLPQQLPA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 178 FPMLTVEEtlmFAAEFRLP--RSLSK--SKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPIL 253
Cdd:PRK10575 97 AEGMTVRE---LVAIGRYPwhGALGRfgAADREKVEEAISLVGLKPLAHRLVDS-----LSGGERQRAWIAMLVAQDSRC 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 15240660 254 LFLDEPTSGLDSTSALSVIKVLKRIAQS-GSMVIMTLH 290
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLH 206
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
107-292 |
9.34e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 70.47 E-value: 9.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 107 TLLNGITGEARDGEILAVLGASGSGKSTLIdalanRIAKG---SLKGNVTLNGEVLNSKMQKAI--SAYVMQDDLLFPML 181
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLL-----RILAGllrPDSGEVRWNGTPLAEQRDEPHenILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 182 TVEETLMFAAEFRLPRSLSkskkslrVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPTS 261
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQRT-------IEDALAAVGLTGFEDLPAAQ-----LSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|.
gi 15240660 262 GLDSTSALSVIKVLKRIAQSGSMVIMTLHQP 292
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
103-284 |
1.00e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.03 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 103 SKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANriAKGSLKGNVTLNGEVLNSKMQKAISAY------VMQDDL 176
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVG--LESPSQGNVSWRGEPLAKLNRAQRKAFrrdiqmVFQDSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 177 --LFPMLTVEETLmfAAEFRLPRSLSKSKKSLRVQALIDQLGLRNAantvIGDEGHRGISGGERRRVSIGIDIIHDPILL 254
Cdd:PRK10419 100 saVNPRKTVREII--REPLRHLLSLDKAERLARASEMLRAVDLDDS----VLDKRPPQLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190
....*....|....*....|....*....|
gi 15240660 255 FLDEPTSGLDSTSALSVIKVLKRIAQSGSM 284
Cdd:PRK10419 174 ILDEAVSNLDLVLQAGVIRLLKKLQQQFGT 203
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
109-288 |
1.54e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 70.81 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALaN----------RIAKGSLKGNVTLNGEVLNSKMQKAisAYVMQDDLLF 178
Cdd:COG4161 18 LFDINLECPSGETLVLLGPSGAGKSSLLRVL-NlletpdsgqlNIAGHQFDFSQKPSEKAIRLLRQKV--GMVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 179 PMLTVEETLMfAAEFRLpRSLSKSKKSLRVQALIDQLGLRNAAntvigDEGHRGISGGERRRVSIGIDIIHDP-ILLFlD 257
Cdd:COG4161 95 PHLTVMENLI-EAPCKV-LGLSKEQAREKAMKLLARLRLTDKA-----DRFPLHLSGGQQQRVAIARALMMEPqVLLF-D 166
|
170 180 190
....*....|....*....|....*....|..
gi 15240660 258 EPTSGLDSTSALSVIKVLKRIAQSG-SMVIMT 288
Cdd:COG4161 167 EPTAALDPEITAQVVEIIRELSQTGiTQVIVT 198
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
100-290 |
1.56e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 72.04 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 100 IFSSKTKT---LLNGITGEARDGEILAVLGASGSGKSTLIDAL----------ANRIAKGSLKGNVTLNGEVLNSK--MQ 164
Cdd:PRK13651 11 IFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLnalllpdtgtIEWIFKDEKNKKKTKEKEKVLEKlvIQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 165 KAISAYVMQ-DDL--------------LFPMlTVEETLMFAaefrlPRSLSKSKKSLRVQAL--IDQLGLrnaantvigD 227
Cdd:PRK13651 91 KTRFKKIKKiKEIrrrvgvvfqfaeyqLFEQ-TIEKDIIFG-----PVSMGVSKEEAKKRAAkyIELVGL---------D 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240660 228 EGHR-----GISGGERRRVSI-GIdIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:PRK13651 156 ESYLqrspfELSGGQKRRVALaGI-LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
114-286 |
1.74e-13 |
|
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: 73.67 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 114 GEARDGEILAVLGASGSGKSTLIDALANRIA--KGSLKGNVTLngevlnS-KMQkaisaYVMQDdllFPMlTVEETLMFA 190
Cdd:COG1245 361 GEIREGEVLGIVGPNGIGKTTFAKILAGVLKpdEGEVDEDLKI------SyKPQ-----YISPD---YDG-TVEEFLRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 191 AEFRLPRSLSKSKkslrvqaLIDQLGLRNaantvIGDEGHRGISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSALS 270
Cdd:COG1245 426 NTDDFGSSYYKTE-------IIKPLGLEK-----LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 493
|
170
....*....|....*....
gi 15240660 271 VIKVLKRIAQS---GSMVI 286
Cdd:COG1245 494 VAKAIRRFAENrgkTAMVV 512
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
107-292 |
1.86e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.19 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 107 TLLNGITGEARDGEILAVLGASGSGKSTLIDALANrIAKGSlKGNVTLNGEVLnSKMQKAISA--------YVMQDDLLF 178
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAG-LDDGS-SGEVSLVGQPL-HQMDEEARAklrakhvgFVFQSFMLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 179 PMLTVEETLMFAAefrLPRSLSKSKKSLRVQALIDQLGLrnaantvigdeGHR------GISGGERRRVSIGIDIIHDPI 252
Cdd:PRK10584 101 PTLNALENVELPA---LLRGESSRQSRNGAKALLEQLGL-----------GKRldhlpaQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15240660 253 LLFLDEPTSGLDSTSALSVIKVLKRIAQS-GSMVIMTLHQP 292
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDL 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
105-264 |
1.92e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.56 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 105 TKTLLNGITGEARDGEILAVLGASGSGKSTLIdalanRIAKGSLK---GNVTLNGEVlnsKMqkaisAYVMQDDLLFPML 181
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLL-----KILAGELEpdsGEVSIPKGL---RI-----GYLPQEPPLDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 182 TVEETLM-------------FAAEFRLPRSLSKSKKSLRVQALIDQLGLRNA---ANTVI------GDEGHRGI---SGG 236
Cdd:COG0488 77 TVLDTVLdgdaelraleaelEELEAKLAEPDEDLERLAELQEEFEALGGWEAearAEEILsglgfpEEDLDRPVselSGG 156
|
170 180
....*....|....*....|....*...
gi 15240660 237 ERRRVSIGIDIIHDPILLFLDEPTSGLD 264
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
104-290 |
2.41e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 71.66 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 104 KTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALAnriakGSL---KGNVTLNGEV---LNSKMQKAISAyVM-QDDL 176
Cdd:COG4586 33 REVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLT-----GILvptSGEVRVLGYVpfkRRKEFARRIGV-VFgQRSQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 177 LFPMLTVEETL-MFAAEFRLPRSLSKSkkslRVQALIDQLGLRNAANTVIgdeghRGISGGERRRVSIGIDIIHDPILLF 255
Cdd:COG4586 107 LWWDLPAIDSFrLLKAIYRIPDAEYKK----RLDELVELLDLGELLDTPV-----RQLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 15240660 256 LDEPTSGLDSTSALSVIKVLKRI-AQSGSMVIMTLH 290
Cdd:COG4586 178 LDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSH 213
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
106-290 |
2.45e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 70.50 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKmqKAISAYVMQDDLLFPMLTVEE 185
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQH--GSITLDGKPVEGP--GAERGVVFQNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 186 TLMFAAEFRlprSLSKSKKSLRVQALIDQLGLRNAantvigdeGHRGI---SGGERRRVSIGIDIIHDPILLFLDEPTSG 262
Cdd:PRK11248 90 NVAFGLQLA---GVEKMQRLEIAHQMLKKVGLEGA--------EKRYIwqlSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180
....*....|....*....|....*....
gi 15240660 263 LDSTSALSVIKVLKRI-AQSGSMVIMTLH 290
Cdd:PRK11248 159 LDAFTREQMQTLLLKLwQETGKQVLLITH 187
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
109-288 |
2.95e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 70.04 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALanRIAKGSLKGNVTLNGEVLNSKMQ---KAISA------YVMQDDLLFP 179
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRVL--NLLEMPRSGTLNIAGNHFDFSKTpsdKAIRElrrnvgMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 180 MLTVEETLMfAAEFRLpRSLSKSKKSLRVQALIDQLGLRNAAntvigDEGHRGISGGERRRVSIGIDIIHDPILLFLDEP 259
Cdd:PRK11124 96 HLTVQQNLI-EAPCRV-LGLSKDQALARAEKLLERLRLKPYA-----DRFPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190
....*....|....*....|....*....|
gi 15240660 260 TSGLDSTSALSVIKVLKRIAQSG-SMVIMT 288
Cdd:PRK11124 169 TAALDPEITAQIVSIIRELAETGiTQVIVT 198
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
109-290 |
3.19e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.81 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSK----MQKAIsAYVMQD-DLLFPMLTV 183
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEA--GTITVGGMVLSEEtvwdVRRQV-GMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 184 EETLMFAAEFR-LPRSLSKSkkslRVQALIDQLGLRNAANtvigDEGHRgISGGERRRVSI-GIdIIHDPILLFLDEPTS 261
Cdd:PRK13635 100 QDDVAFGLENIgVPREEMVE----RVDQALRQVGMEDFLN----REPHR-LSGGQKQRVAIaGV-LALQPDIIILDEATS 169
|
170 180 190
....*....|....*....|....*....|
gi 15240660 262 GLDSTSALSVIKVLKRI-AQSGSMVIMTLH 290
Cdd:PRK13635 170 MLDPRGRREVLETVRQLkEQKGITVLSITH 199
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
108-290 |
3.32e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.84 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 108 LLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNsKMQKAISA--------YVMQDDLLFP 179
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTS--GDVIFNGQPMS-KLSSAAKAelrnqklgFIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 180 MLTVEETLMfaaefrLPRSLSKSKKSL---RVQALIDQLGLRNAANtvigdegHRG--ISGGERRRVSIGIDIIHDPILL 254
Cdd:PRK11629 101 DFTALENVA------MPLLIGKKKPAEinsRALEMLAAVGLEHRAN-------HRPseLSGGERQRVAIARALVNNPRLV 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 15240660 255 FLDEPTSGLDSTSALSVIKVLKRI-AQSGSMVIMTLH 290
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTH 204
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
115-264 |
3.33e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 69.61 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 115 EARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGE--VLNSKMQKAISAyVMQDDLLFPMLTVEETLMFAAE 192
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNLIAGFLTPAS--GSLTLNGQdhTTTPPSRRPVSM-LFQENNLFSHLTVAQNIGLGLN 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240660 193 FRLprSLSKSKKsLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDII-HDPILLfLDEPTSGLD 264
Cdd:PRK10771 98 PGL--KLNAAQR-EKLHAIARQMGIEDLLARLPGQ-----LSGGQRQRVALARCLVrEQPILL-LDEPFSALD 161
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
107-290 |
4.50e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 70.30 E-value: 4.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 107 TLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKMQKAISAYVMQD---DLLFPMLtV 183
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLAS--GKISILGQPTRQALQKNLVAYVPQSeevDWSFPVL-V 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 184 EETLMFA-----AEFRLPrslsKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDE 258
Cdd:PRK15056 98 EDVVMMGryghmGWLRRA----KKRDRQIVTAALARVDMVEFRHRQIGE-----LSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190
....*....|....*....|....*....|..
gi 15240660 259 PTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRDEGKTMLVSTH 200
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
109-290 |
5.71e-13 |
|
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: 69.77 E-value: 5.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTL---IDALanriakgsLK---GNVTLNG-EVLNSKM-----QKAisAYVMQD-D 175
Cdd:TIGR04520 18 LKNVSLSIEKGEFVAIIGHNGSGKSTLaklLNGL--------LLptsGKVTVDGlDTLDEENlweirKKV--GMVFQNpD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 176 LLFPMLTVEETLMFAAE-FRLPRSLSKSkkslRVQALIDQLGLRNAANTvigdEGHRgISGGERRRVSI-GIdIIHDPIL 253
Cdd:TIGR04520 88 NQFVGATVEDDVAFGLEnLGVPREEMRK----RVDEALKLVGMEDFRDR----EPHL-LSGGQKQRVAIaGV-LAMRPDI 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 15240660 254 LFLDEPTSGLDSTSALSVIKVLKRIAQSGSM-VIMTLH 290
Cdd:TIGR04520 158 IILDEATSMLDPKGRKEVLETIRKLNKEEGItVISITH 195
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
100-291 |
5.86e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 70.65 E-value: 5.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 100 IFSSKTK---TLLNGITGEARDGEILAVLGASGSGKSTLI-----------------DALANRIAKGSLKGNVTLNGEVL 159
Cdd:PRK13631 30 VFDEKQEnelVALNNISYTFEKNKIYFIIGNSGSGKSTLVthfnglikskygtiqvgDIYIGDKKNNHELITNPYSKKIK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 160 NSKMQKAISAYVMQddllFPML-----TVEETLMFAaefrlPRSLSKSKKSLRVQA--LIDQLGLRNAantvIGDEGHRG 232
Cdd:PRK13631 110 NFKELRRRVSMVFQ----FPEYqlfkdTIEKDIMFG-----PVALGVKKSEAKKLAkfYLNKMGLDDS----YLERSPFG 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 233 ISGGERRRVSI-GIDIIHDPILLFlDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLHQ 291
Cdd:PRK13631 177 LSGGQKRRVAIaGILAIQPEILIF-DEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT 235
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
107-290 |
5.91e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.41 E-value: 5.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 107 TLLNGITGEARDGEILAVLGASGSGKSTLIdalanRIAKGSLK---GNVTLNGEVLNSKMQKAIS---AYVMQDDLLFPM 180
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLL-----RAINGTLTptaGTVLVAGDDVEALSARAASrrvASVPQDTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 181 LTVEETLmfaaefRLPRSLSKSKKSLRVQAliDQLGLRNAANTV----IGDEGHRGISGGERRRVSIGIDIIHDPILLFL 256
Cdd:PRK09536 92 FDVRQVV------EMGRTPHRSRFDTWTET--DRAAVERAMERTgvaqFADRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190
....*....|....*....|....*....|....
gi 15240660 257 DEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRLVDDGKTAVAAIH 197
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
109-280 |
9.89e-13 |
|
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: 71.29 E-value: 9.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIdALANRIAKGSlKGNVTLNG-EVLNSKMQ--KAISAYVMQDDLLFPMlTVEE 185
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLV-NLIPRFYEPD-SGQILLDGhDLADYTLAslRRQVALVSQDVVLFND-TIAN 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 186 TLMFAAEFRLPRS-LSKSKKSLRVQALIDQLGlrNAANTVIGDEGHRgISGGERRRVSIGIDIIHDPILLFLDEPTSGLD 264
Cdd:TIGR02203 425 NIAYGRTEQADRAeIERALAAAYAQDFVDKLP--LGLDTPIGENGVL-LSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
170
....*....|....*.
gi 15240660 265 STSALSVIKVLKRIAQ 280
Cdd:TIGR02203 502 NESERLVQAALERLMQ 517
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
105-290 |
1.09e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.50 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 105 TKTLLNGITGEARDGEILAVLGASGSGKSTLIDALAnRIAKgSLKGNVTLNGEVLNSKMQKAISAYV--MQDDLLFPM-L 181
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA-RLLT-PQSGTVFLGDKPISMLSSRQLARRLalLPQHHLTPEgI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 182 TVEETLMFAaefrlpRS--------LSKSKKSLrVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPIL 253
Cdd:PRK11231 92 TVRELVAYG------RSpwlslwgrLSAEDNAR-VNQAMEQTRINHLADRRLTD-----LSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 15240660 254 LFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLH 196
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
109-287 |
1.27e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.83 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALAnriakGSLK---GNVTLNGEVLN-SKMQKAISA---YVMQDDLLFPML 181
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILY-----GLYQpdsGEILIDGKPVRiRSPRDAIALgigMVHQHFMLVPNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 182 TVEETLMFAAEFRLPRSLSKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSI------GIDIihdpilLF 255
Cdd:COG3845 96 TVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVED-----LSVGEQQRVEIlkalyrGARI------LI 164
|
170 180 190
....*....|....*....|....*....|..
gi 15240660 256 LDEPTSGLDSTSALSVIKVLKRIAQSGSMVIM 287
Cdd:COG3845 165 LDEPTAVLTPQEADELFEILRRLAAEGKSIIF 196
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
102-290 |
1.68e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 68.60 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 102 SSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIdalanRIAKGSLK---GNVTLNGEVLNSK----MQKAISAYVMQD 174
Cdd:PRK13650 16 EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTV-----RLIDGLLEaesGQIIIDGDLLTEEnvwdIRHKIGMVFQNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 175 DLLFPMLTVEETLMFAAEFR-LPRSLSKSkkslRVQALIDQLGLRNAANTvigdEGHRgISGGERRRVSIGIDIIHDPIL 253
Cdd:PRK13650 91 DNQFVGATVEDDVAFGLENKgIPHEEMKE----RVNEALELVGMQDFKER----EPAR-LSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 15240660 254 LFLDEPTSGLDSTSALSVIKVLKRIAQSGSM-VIMTLH 290
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDYQMtVISITH 199
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
109-287 |
1.79e-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: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALANriAKGSLKGNVTLNGE-VLNSKMQKAIS---AYVMQD---DLLFPML 181
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFG--LRPPASGEITLDGKpVTRRSPRDAIRagiAYVPEDrkrEGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 182 TVEEtlmfaaefrlprslskskkslrvqalidqlglrnaaNTVIGdeghRGISGGERRRVSIGIDIIHDPILLFLDEPTS 261
Cdd:cd03215 94 SVAE------------------------------------NIALS----SLLSGGNQQKVVLARWLARDPRVLILDEPTR 133
|
170 180
....*....|....*....|....*.
gi 15240660 262 GLDSTSALSVIKVLKRIAQSGSMVIM 287
Cdd:cd03215 134 GVDVGAKAEIYRLIRELADAGKAVLL 159
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
121-264 |
1.84e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.13 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 121 ILAVLGASGSGKSTLIDALANRIAKGslKGNVTLNGEVLNsKMQKAIS--------AYVMQDDLLFPMLTVEETLMFAAe 192
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQ--KGRIVLNGRVLF-DAEKGIClppekrriGYVFQDARLFPHYKVRGNLRYGM- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 193 frlprslsksKKSLRVQ--ALIDQLGLrnaantvigdeGH------RGISGGERRRVSIGIDIIHDPILLFLDEPTSGLD 264
Cdd:PRK11144 102 ----------AKSMVAQfdKIVALLGI-----------EPlldrypGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
109-290 |
1.86e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 70.62 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIdALANRiAKGSLKGNVTLNGevlnskmqKAISAYVMQDdlLFPMLTV--EET 186
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLL-QLLTR-AWDPQQGEILLNG--------QPIADYSEAA--LRQAISVvsQRV 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 187 LMFAAEFRLPRSLSKSKKS-LRVQALIDQLGLRNAA------NTVIGdEGHRGISGGERRRVSIGIDIIHD-PILLfLDE 258
Cdd:PRK11160 424 HLFSATLRDNLLLAAPNASdEALIEVLQQVGLEKLLeddkglNAWLG-EGGRQLSGGEQRRLGIARALLHDaPLLL-LDE 501
|
170 180 190
....*....|....*....|....*....|..
gi 15240660 259 PTSGLDSTSALSVIKVLKRIAQsGSMVIMTLH 290
Cdd:PRK11160 502 PTEGLDAETERQILELLAEHAQ-NKTVLMITH 532
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
109-265 |
3.62e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 69.60 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIdALANRIAKGSLkGNVTLNGE----VLNSKMQKAIsAYVMQDDLLF------ 178
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLI-NLLQRVFDPQS-GRILIDGTdirtVTRASLRRNI-AVVFQDAGLFnrsied 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 179 ------PMLTVEEtLMFAAEfrlprslskskkslRVQALIDQLGLRNAANTVIGDEGhRGISGGERRRVSIGIDIIHDPI 252
Cdd:PRK13657 428 nirvgrPDATDEE-MRAAAE--------------RAQAHDFIERKPDGYDTVVGERG-RQLSGGERQRLAIARALLKDPP 491
|
170
....*....|...
gi 15240660 253 LLFLDEPTSGLDS 265
Cdd:PRK13657 492 ILILDEATSALDV 504
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
104-287 |
5.14e-12 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 68.94 E-value: 5.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 104 KTKTLLNGITGEARDGEILAVLGASGSGKS----TLIDALANRIAKGSlkGNVTLNGEVLNSKMQKAIS-------AYVM 172
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPS--GSILFDGQDLLGLSERELRrirgnriAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 173 QDDL--LFPMLTVE----ETLmfaaefRLPRSLSKSKKSLRVQALIDQLGLRNAAnTVIGDEGHRgISGGERRRVSIGID 246
Cdd:COG4172 99 QEPMtsLNPLHTIGkqiaEVL------RLHRGLSGAAARARALELLERVGIPDPE-RRLDAYPHQ-LSGGQRQRVMIAMA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15240660 247 IIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIM 287
Cdd:COG4172 171 LANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALL 211
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
106-292 |
5.55e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 65.59 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKgsLKGNVTLNGEVLNSK---MQKAIsAYVMQDDLLFPMLT 182
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPP--LAGRVLLNGGPLDFQrdsIARGL-LYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 183 VEETLMFAAEFrlprslskSKKSLRVQALiDQLGLRNaantvIGDEGHRGISGGERRRVSIGIDIIHDPILLFLDEPTSG 262
Cdd:cd03231 90 VLENLRFWHAD--------HSDEQVEEAL-ARVGLNG-----FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180 190
....*....|....*....|....*....|
gi 15240660 263 LDSTSALSVIKVLKRIAQSGSMVIMTLHQP 292
Cdd:cd03231 156 LDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
107-290 |
7.80e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.06 E-value: 7.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 107 TLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAK-GSLKGNVTLNG-EVLN------SKMQKAISAYVMQDDL-- 176
Cdd:PRK09473 30 TAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAnGRIGGSATFNGrEILNlpekelNKLRAEQISMIFQDPMts 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 177 LFPMLTVEETLMfaAEFRLPRSLSKSK---KSLRvqaLIDQLGLRNAANTvIGDEGHRgISGGERRRVSIGIDIIHDPIL 253
Cdd:PRK09473 110 LNPYMRVGEQLM--EVLMLHKGMSKAEafeESVR---MLDAVKMPEARKR-MKMYPHE-FSGGMRQRVMIAMALLCRPKL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15240660 254 LFLDEPTSGLDST---SALSVIKVLKRiaQSGSMVIMTLH 290
Cdd:PRK09473 183 LIADEPTTALDVTvqaQIMTLLNELKR--EFNTAIIMITH 220
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
114-286 |
8.86e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.30 E-value: 8.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 114 GEARDGEILAVLGASGSGKSTLIDALANRI--AKGSLKGNVTLNgevlnSKMQkaisaYVMQDdllFPMlTVEETLMFAA 191
Cdd:PRK13409 360 GEIYEGEVIGIVGPNGIGKTTFAKLLAGVLkpDEGEVDPELKIS-----YKPQ-----YIKPD---YDG-TVEDLLRSIT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 192 EfRLPRSLSKSKkslrvqaLIDQLGLRNaantvIGDEGHRGISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSALSV 271
Cdd:PRK13409 426 D-DLGSSYYKSE-------IIKPLQLER-----LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 492
|
170
....*....|....*...
gi 15240660 272 IKVLKRIA---QSGSMVI 286
Cdd:PRK13409 493 AKAIRRIAeerEATALVV 510
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
107-277 |
8.87e-12 |
|
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: 67.93 E-value: 8.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 107 TLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSLKGNVTLNGEVLNSK----MQKAISAYVMQDDLLFPMLT 182
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASnirdTERAGIVIIHQELTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 183 VEETLMFAAEFRLPRSLSK-SKKSLRVQALIDQLGLRNAANT-VIGDEGhrgisGGERRRVSIGIDIIHDPILLFLDEPT 260
Cdd:TIGR02633 95 VAENIFLGNEITLPGGRMAyNAMYLRAKNLLRELQLDADNVTrPVGDYG-----GGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180
....*....|....*....|
gi 15240660 261 SGL---DSTSALSVIKVLKR 277
Cdd:TIGR02633 170 SSLtekETEILLDIIRDLKA 189
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
93-290 |
9.01e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 66.30 E-value: 9.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 93 PGAPsegiFSSKTktlLNGITGEARDGEILAVLGASGSGKSTLIDALANRI--AKGSLK-GNVTlngeVLNSKMQKAISA 169
Cdd:PRK13643 13 PNSP----FASRA---LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqpTEGKVTvGDIV----VSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 170 YVMQDDLLFPM---LTVEETLMFAAEFRlPRSLSKSKKSLRVQAL--IDQLGLRNAantvIGDEGHRGISGGERRRVSIG 244
Cdd:PRK13643 82 VRKKVGVVFQFpesQLFEETVLKDVAFG-PQNFGIPKEKAEKIAAekLEMVGLADE----FWEKSPFELSGGQMRRVAIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15240660 245 IDIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
106-291 |
1.02e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 64.47 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSLKGNVTLNGEVLNSkmqkaisayvmqddllfpmLTVEE 185
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKGEDITD-------------------LPPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 186 ------TLMFAAEFRLPrslskskkSLRVQALidqlgLRNAantvigDEGhrgISGGERRRVSIGIDIIHDPILLFLDEP 259
Cdd:cd03217 74 rarlgiFLAFQYPPEIP--------GVKNADF-----LRYV------NEG---FSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190
....*....|....*....|....*....|...
gi 15240660 260 TSGLDSTSALSVIKVLKRIAQSG-SMVIMTLHQ 291
Cdd:cd03217 132 DSGLDIDALRLVAEVINKLREEGkSVLIITHYQ 164
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
112-290 |
1.06e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.72 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 112 ITGEARDGEILAVLGASGSGKSTLIDALAnriakGSL--KGNVTLNGEVLNSKMQKAIS---AYVMQDDLLFPMLTVEET 186
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMA-----GLLpgSGSIQFAGQPLEAWSAAELArhrAYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 187 LMFAaefrLPRSLSKSKKSLRVQALIDQLGLrnaantviGDEGHRGI---SGGERRRVSIGIDI--IHDPI-----LLFL 256
Cdd:PRK03695 90 LTLH----QPDKTRTEAVASALNEVAEALGL--------DDKLGRSVnqlSGGEWQRVRLAAVVlqVWPDInpagqLLLL 157
|
170 180 190
....*....|....*....|....*....|....
gi 15240660 257 DEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSH 191
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
75-265 |
1.31e-11 |
|
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: 68.43 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 75 YSVKVRR-KFTWRRSvssDPgaPSegifssktktlLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKgsLKGNVT 153
Cdd:TIGR00957 635 NSITVHNaTFTWARD---LP--PT-----------LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK--VEGHVH 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 154 LNGEVLNSKMQKAIsayvmQDDllfpmlTVEETLMFAAEFRLPRslskSKKSLRVQALIDQLG-LRNAANTVIGDEGhRG 232
Cdd:TIGR00957 697 MKGSVAYVPQQAWI-----QND------SLRENILFGKALNEKY----YQQVLEACALLPDLEiLPSGDRTEIGEKG-VN 760
|
170 180 190
....*....|....*....|....*....|...
gi 15240660 233 ISGGERRRVSIGIDIIHDPILLFLDEPTSGLDS 265
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
105-284 |
1.36e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.42 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 105 TKTLLNGITGEARDGEILAVLGASGSGKStlIDALAN-RIAKGS----LKGNVTLNGE-VLNSKMQKAIS------AYVM 172
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKS--VTALSIlRLLPSPpvvyPSGDIRFHGEsLLHASEQTLRGvrgnkiAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 173 QDDL--LFPMLTVEETLmfAAEFRLPRSLSKSKKSLRVQALIDQLGLRNAANTvIGDEGHRgISGGERRRVSIGIDIIHD 250
Cdd:PRK15134 99 QEPMvsLNPLHTLEKQL--YEVLSLHRGMRREAARGEILNCLDRVGIRQAAKR-LTDYPHQ-LSGGERQRVMIAMALLTR 174
|
170 180 190
....*....|....*....|....*....|....
gi 15240660 251 PILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSM 284
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRELQQELNM 208
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
106-292 |
1.71e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.05 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIdalanRIAKG---SLKGNVTLNGEvlnsKMQKAISAYvmQDDLLF---- 178
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLL-----RILAGlarPDAGEVLWQGE----PIRRQRDEY--HQDLLYlghq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 179 ----PMLTVEETLMFAAefRLPRSLSKSKkslRVQALiDQLGLRNAANTVIgdeghRGISGGERRRVSIGIDIIHDPILL 254
Cdd:PRK13538 83 pgikTELTALENLRFYQ--RLHGPGDDEA---LWEAL-AQVGLAGFEDVPV-----RQLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 15240660 255 FLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLHQP 292
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQD 189
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
103-291 |
2.19e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 65.21 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 103 SKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALaNRIAKGSlKGNVTLNGEVLNSKMQKAISAYV-----MQDDLL 177
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHF-NGILKPT-SGSVLIRGEPITKENIREVRKFVglvfqNPDDQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 178 FPMlTVEETLMFAaefrlPRSLSKSKKSL--RVQALIDQLGLRNAANTVigdeGHRgISGGERRRVSIGIDIIHDPILLF 255
Cdd:PRK13652 92 FSP-TVEQDIAFG-----PINLGLDEETVahRVSSALHMLGLEELRDRV----PHH-LSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 15240660 256 LDEPTSGLDSTSALSVIKVLKRIAQS-GSMVIMTLHQ 291
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQ 197
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
101-278 |
2.96e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 65.50 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 101 FSSKTKTL--LNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVL----NSKMQKAISAYVM-- 172
Cdd:PRK15079 27 FWQPPKTLkaVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATD--GEVAWLGKDLlgmkDDEWRAVRSDIQMif 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 173 QDDL--LFPMLTVEETLMFAAEFRLPRsLSKSKKSLRVQALIDQLGLRNaanTVIGDEGHRgISGGERRRVSIGIDIIHD 250
Cdd:PRK15079 105 QDPLasLNPRMTIGEIIAEPLRTYHPK-LSRQEVKDRVKAMMLKVGLLP---NLINRYPHE-FSGGQCQRIGIARALILE 179
|
170 180
....*....|....*....|....*...
gi 15240660 251 PILLFLDEPTSGLDSTSALSVIKVLKRI 278
Cdd:PRK15079 180 PKLIICDEPVSALDVSIQAQVVNLLQQL 207
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
109-290 |
3.76e-11 |
|
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: 62.06 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNskmqkaisayvmqddllfpmltveetlm 188
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDS--GEILVDGKEVS---------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 189 faaefrlPRSLSKSKKsLRVqALIDQLglrnaantvigdeghrgiSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSA 268
Cdd:cd03216 66 -------FASPRDARR-AGI-AMVYQL------------------SVGERQMVEIARALARNARLLILDEPTAALTPAEV 118
|
170 180
....*....|....*....|..
gi 15240660 269 LSVIKVLKRIAQSGSMVIMTLH 290
Cdd:cd03216 119 ERLFKVIRRLRAQGVAVIFISH 140
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
106-292 |
3.89e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 63.93 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSLKGNVTLNGEVLNSkM------QKAISaYVMQDDLLFP 179
Cdd:COG0396 13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEVTSGSILLDGEDILE-LspderaRAGIF-LAFQYPVEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 180 MLTVEETLMFAAEFRLPRSLSKSKKSLRVQALIDQLGLRNaantvigDEGHR----GISGGERRRVSIGIDIIHDPILLF 255
Cdd:COG0396 91 GVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDE-------DFLDRyvneGFSGGEKKRNEILQMLLLEPKLAI 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 15240660 256 LDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLHQP 292
Cdd:COG0396 164 LDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQ 200
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
109-277 |
4.18e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.11 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSLKGNVTLNGEVLNSKM-----QKAIsAYVMQDDLLFPMLTV 183
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGEELQASNirdteRAGI-AIIHQELALVKELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 184 EETLMFAAEFRLPRSLSKSKKSLRVQALIDQLGLRNAANTVIGDEGhrgisGGERRRVSIGIDIIHDPILLFLDEPTSGL 263
Cdd:PRK13549 100 LENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLG-----LGQQQLVEIAKALNKQARLLILDEPTASL 174
|
170
....*....|....*..
gi 15240660 264 ---DSTSALSVIKVLKR 277
Cdd:PRK13549 175 tesETAVLLDIIRDLKA 191
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
104-291 |
4.58e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.89 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 104 KTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSLKGNVTLNGEVLNSKMQKAIS------AYvmQDDLL 177
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKGESILDLEPEERAhlgiflAF--QYPIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 178 FPMLTVEETLMFAAEFRLPRSLSKSKKSLRVQALI-DQLGLRNAANTVIGDEGHRGISGGERRRVSIGIDIIHDPILLFL 256
Cdd:CHL00131 96 IPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIInEKLKLVGMDPSFLSRNVNEGFSGGEKKRNEILQMALLDSELAIL 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 15240660 257 DEPTSGLDsTSALSVI-KVLKRIAQSG-SMVIMTLHQ 291
Cdd:CHL00131 176 DETDSGLD-IDALKIIaEGINKLMTSEnSIILITHYQ 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
105-264 |
5.04e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 64.97 E-value: 5.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 105 TKTLLNGITGEARDGEILAVLGASGSGKSTLIdalanRIAKG---SLKGNVTLNGEVLN--SKMQKAISAyVMQDDLLFP 179
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVL-----RLIAGfetPDSGRIMLDGQDIThvPAENRHVNT-VFQSYALFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 180 MLTVEETLMF--------AAEFRlPRSLskskKSLR-VQalIDQLGLRNAANtvigdeghrgISGGERRRVSIGIDIIHD 250
Cdd:PRK09452 100 HMTVFENVAFglrmqktpAAEIT-PRVM----EALRmVQ--LEEFAQRKPHQ----------LSGGQQQRVAIARAVVNK 162
|
170
....*....|....
gi 15240660 251 PILLFLDEPTSGLD 264
Cdd:PRK09452 163 PKVLLLDESLSALD 176
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
109-263 |
8.05e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 8.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLN----SKMQKAISAYVMQDDLLFPMLTVE 184
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDS--GTLEIGGNPCArltpAKAHQLGIYLVPQEPLLFPNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 185 ETLMfaaeFRLPRSLSKSKKslrVQALIDQLG----LRNAANTV-IGDeghrgisggeRRRVSIGIDIIHDPILLFLDEP 259
Cdd:PRK15439 105 ENIL----FGLPKRQASMQK---MKQLLAALGcqldLDSSAGSLeVAD----------RQIVEILRGLMRDSRILILDEP 167
|
....
gi 15240660 260 TSGL 263
Cdd:PRK15439 168 TASL 171
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
109-290 |
8.43e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 63.22 E-value: 8.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALaNRIAKGSlKGNVTLNGEVLNSKMQKAISA---YVMQD--DLLFPMlTV 183
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHL-NGIYLPQ-RGRVKVMGREVNAENEKWVRSkvgLVFQDpdDQVFSS-TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 184 EETLMFAaefrlPRSLSKSKKSL--RVQALIDQLGLRNAAntvigDEGHRGISGGERRRVSIGIDIIHDPILLFLDEPTS 261
Cdd:PRK13647 98 WDDVAFG-----PVNMGLDKDEVerRVEEALKAVRMWDFR-----DKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMA 167
|
170 180
....*....|....*....|....*....
gi 15240660 262 GLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:PRK13647 168 YLDPRGQETLMEILDRLHNQGKTVIVATH 196
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
109-289 |
9.48e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 63.19 E-value: 9.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKST---LIDALANRiakgsLKGNVTLNGEVLNSK----MQKAISAYVMQDDLLFPML 181
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTtarLIDGLFEE-----FEGKVKIDGELLTAEnvwnLRRKIGMVFQNPDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 182 TVEETLMFAAEFR-LPRS--LSKSKKSLRVQALIDqLGLRNAANtvigdeghrgISGGERRRVSIGIDIIHDPILLFLDE 258
Cdd:PRK13642 98 TVEDDVAFGMENQgIPREemIKRVDEALLAVNMLD-FKTREPAR----------LSGGQKQRVAVAGIIALRPEIIILDE 166
|
170 180 190
....*....|....*....|....*....|.
gi 15240660 259 PTSGLDSTSALSVIKVLKRIAQSGSMVIMTL 289
Cdd:PRK13642 167 STSMLDPTGRQEIMRVIHEIKEKYQLTVLSI 197
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
103-290 |
9.52e-11 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 62.45 E-value: 9.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 103 SKTKTL----------LNGITGEARDGEILAVLGASGSGKSTLIDAL-AN-RIAKGSL-----KGNVTLNG----EVLNs 161
Cdd:COG4778 11 SKTFTLhlqggkrlpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIyGNyLPDSGSIlvrhdGGWVDLAQasprEILA- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 162 kMQKAISAYVMQddllF----PMLTveeTLMFAAEFRLPRSLSKSKKSLRVQALIDQLGL-----RNAANTvigdeghrg 232
Cdd:COG4778 90 -LRRRTIGYVSQ----FlrviPRVS---ALDVVAEPLLERGVDREEARARARELLARLNLperlwDLPPAT--------- 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15240660 233 ISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:COG4778 153 FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFH 210
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
117-290 |
1.17e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.88 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 117 RDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKMQKAIS-----------------AYVMQDDL--L 177
Cdd:PRK10261 40 QRGETLAIVGESGSGKSVTALALMRLLEQAG--GLVQCDKMLLRRRSRQVIElseqsaaqmrhvrgadmAMIFQEPMtsL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 178 FPMLTVEETLmfAAEFRLPRSLSKSKKSLRVQALIDQLGLRNAaNTVIGDEGHRgISGGERRRVSIGIDIIHDPILLFLD 257
Cdd:PRK10261 118 NPVFTVGEQI--AESIRLHQGASREEAMVEAKRMLDQVRIPEA-QTILSRYPHQ-LSGGMRQRVMIAMALSCRPAVLIAD 193
|
170 180 190
....*....|....*....|....*....|....
gi 15240660 258 EPTSGLDSTSALSVIKVLKRIAQSGSM-VIMTLH 290
Cdd:PRK10261 194 EPTTALDVTIQAQILQLIKVLQKEMSMgVIFITH 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
109-290 |
1.22e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 62.94 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALaNRIAKGSlKGNVTLNGEVLNS------KMQKAIsAYVMQ--DDLLFPM 180
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNL-NGILKPS-SGRILFDGKPIDYsrkglmKLRESV-GMVFQdpDNQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 181 LTVEETLMFAAEFRLPrslsKSKKSLRVQALIDQLGLRNaantvIGDEGHRGISGGERRRVSIGIDIIHDPILLFLDEPT 260
Cdd:PRK13636 99 SVYQDVSFGAVNLKLP----EDEVRKRVDNALKRTGIEH-----LKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190
....*....|....*....|....*....|.
gi 15240660 261 SGLDSTSALSVIKVLKRIAQS-GSMVIMTLH 290
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEMQKElGLTIIIATH 200
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
100-290 |
1.24e-10 |
|
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: 65.42 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 100 IFSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKMQKAIS--AYVMQDDLL 177
Cdd:TIGR01257 1946 VYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTS--GDATVAGKSILTNISDVHQnmGYCPQFDAI 2023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 178 FPMLTVEETLMFAAEFR-LPrslskSKKSLRVQAL-IDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLF 255
Cdd:TIGR01257 2024 DDLLTGREHLYLYARLRgVP-----AEEIEKVANWsIQSLGLSLYADRLAGT-----YSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190
....*....|....*....|....*....|....*
gi 15240660 256 LDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
109-291 |
1.50e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.82 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALANriAKGSLKGNVTLNGEVLNS-----KMQKAIsAYVMQDDLLFPMLTV 183
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG--DPRATSGRIVFDGKDITDwqtakIMREAV-AIVPEGRRVFSRMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 184 EETLMFAAEFrlPRSLSKSKKSLRVQALIDQLGLRNA--ANTvigdeghrgISGGERRRVSIGIDIIHDPILLFLDEPTS 261
Cdd:PRK11614 98 EENLAMGGFF--AERDQFQERIKWVYELFPRLHERRIqrAGT---------MSGGEQQMLAIGRALMSQPRLLLLDEPSL 166
|
170 180 190
....*....|....*....|....*....|
gi 15240660 262 GLDSTSALSVIKVLKRIAQSGsMVIMTLHQ 291
Cdd:PRK11614 167 GLAPIIIQQIFDTIEQLREQG-MTIFLVEQ 195
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
92-290 |
1.65e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.76 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 92 DPGAPS----EGIFSSKTK----TLLNgITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlKGNVTLNGEVlnskm 163
Cdd:PLN03130 609 EPGLPAisikNGYFSWDSKaerpTLSN-INLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRS-DASVVIRGTV----- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 164 qkaisAYVMQDDLLFPMlTVEETLMFAAEFRLPRSlsksKKSLRVQALIDQLGLRNAAN-TVIGDEGhRGISGGERRRVS 242
Cdd:PLN03130 682 -----AYVPQVSWIFNA-TVRDNILFGSPFDPERY----ERAIDVTALQHDLDLLPGGDlTEIGERG-VNISGGQKQRVS 750
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15240660 243 IGIDIIHDPILLFLDEPTSGLDSTSALSVI-KVLKRIAQSGSMVIMT--LH 290
Cdd:PLN03130 751 MARAVYSNSDVYIFDDPLSALDAHVGRQVFdKCIKDELRGKTRVLVTnqLH 801
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
106-264 |
1.90e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.93 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIA--KGSLKGNVTLNgevlnskmqkaiSAYVMQD-DLLFPMLT 182
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEpdSGTVKLGETVK------------IGYFDQHqEELDPDKT 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 183 VEETLmfaaefrlpRSLSKSKKSLRVQALIDQLGLRNA-ANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPTS 261
Cdd:COG0488 396 VLDEL---------RDGAPGGTEQEVRGYLGRFLFSGDdAFKPVGV-----LSGGEKARLALAKLLLSPPNVLLLDEPTN 461
|
...
gi 15240660 262 GLD 264
Cdd:COG0488 462 HLD 464
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
112-271 |
3.07e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 62.74 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 112 ITGEARDGEILAVLGASGSGKSTLIDALA--NRIAKGSLK-GNVTLNgEVLNSKmqKAIsAYVMQDDLLFPMLTVEETLM 188
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAglEDITSGDLFiGEKRMN-DVPPAE--RGV-GMVFQSYALYPHLSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 189 FAAEfrlprsLSKSKKS---LRVQALIDQLGLrnaantvigdeGH------RGISGGERRRVSIGIDIIHDPILLFLDEP 259
Cdd:PRK11000 98 FGLK------LAGAKKEeinQRVNQVAEVLQL-----------AHlldrkpKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170
....*....|..
gi 15240660 260 TSGLDstSALSV 271
Cdd:PRK11000 161 LSNLD--AALRV 170
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
117-290 |
3.82e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 61.23 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 117 RDGEILAVLGASGSGKSTLIDALAnriakGSLKGNVTLNG------EVLN----SKMQKAISAyvMQDDLLFPMLTVEET 186
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILA-----GKLKPNLGKFDdppdwdEILDefrgSELQNYFTK--LLEGDVKVIVKPQYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 187 lmfaaeFRLPRS--------LSKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDE 258
Cdd:cd03236 97 ------DLIPKAvkgkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQ-----LSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190
....*....|....*....|....*....|..
gi 15240660 259 PTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:cd03236 166 PSSYLDIKQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
108-292 |
3.95e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.08 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 108 LLNGITGEARDGEILAVLGASGSGKSTLIDALaNRI----AKGSLKGNVTLNGE--------VLNSKMQkaisaYVMQDD 175
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVF-NRLielyPEARVSGEVYLDGQdifkmdviELRRRVQ-----MVFQIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 176 LLFPMLTVEETLmfAAEFRLPRsLSKSKKSL--RVQALIDQLGLRNAANTVIGDEGHRgISGGERRRVSIGIDIIHDPIL 253
Cdd:PRK14247 92 NPIPNLSIFENV--ALGLKLNR-LVKSKKELqeRVRWALEKAQLWDEVKDRLDAPAGK-LSGGQQQRLCIARALAFQPEV 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 15240660 254 LFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTlHQP 292
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKDMTIVLVT-HFP 205
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
106-293 |
4.87e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.85 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGS---LKGNVTLNGEVLNSKMqkaisayVMQDDLLFPMLT 182
Cdd:PRK11247 25 RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAgelLAGTAPLAEAREDTRL-------MFQDARLLPWKK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 183 VEET--LMFAAEFRlPRSLskskkslrvQALiDQLGLRNAANtvigdEGHRGISGGERRRVSIGIDIIHDPILLFLDEPT 260
Cdd:PRK11247 98 VIDNvgLGLKGQWR-DAAL---------QAL-AAVGLADRAN-----EWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 15240660 261 SGLDstsALSVIKVLKRIA----QSGSMVIMTLHQPS 293
Cdd:PRK11247 162 GALD---ALTRIEMQDLIEslwqQHGFTVLLVTHDVS 195
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
101-280 |
6.15e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 60.11 E-value: 6.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 101 FSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGE---VLNSKMQKAISAYVMQDDLL 177
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTS--GTLLFEGEdisTLKPEIYRQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 178 FPMlTVEETLMFAAEFRlprslsksKKSLRVQALIDQLGLRNAANTVIgDEGHRGISGGERRRVSIGIDIIHDPILLFLD 257
Cdd:PRK10247 93 FGD-TVYDNLIFPWQIR--------NQQPDPAIFLDDLERFALPDTIL-TKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180
....*....|....*....|...
gi 15240660 258 EPTSGLDSTSALSVIKVLKRIAQ 280
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVR 185
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
106-292 |
6.21e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.45 E-value: 6.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALaNRI-----AKGSLKGNVTLNG----EVLNSKMQKAIsAYVMQDDL 176
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL-NRLieiydSKIKVDGKVLYFGkdifQIDAIKLRKEV-GMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 177 LFPMLTVEETLMFAaefrLPRSLSKSKKSLR--VQALIDQLGLRNAANTVIGDEGHRgISGGERRRVSIGIDIIHDPILL 254
Cdd:PRK14246 101 PFPHLSIYDNIAYP----LKSHGIKEKREIKkiVEECLRKVGLWKEVYDRLNSPASQ-LSGGQQQRLTIARALALKPKVL 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 15240660 255 FLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTlHQP 292
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVS-HNP 212
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
101-283 |
6.46e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 60.77 E-value: 6.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 101 FSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLidalaNRIAKGSLK---GNVTLNGEVLNS----KMQKAISAYVMQ 173
Cdd:PRK13632 17 YPNSENNALKNVSFEINEGEYVAILGHNGSGKSTI-----SKILTGLLKpqsGEIKIDGITISKenlkEIRKKIGIIFQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 174 DDLLFPMLTVEETLMFAAEFR-LPRSlskskkslRVQALIDQLGLRNAANTVIGDEGHRgISGGERRRVSIGIDIIHDPI 252
Cdd:PRK13632 92 PDNQFIGATVEDDIAFGLENKkVPPK--------KMKDIIDDLAKKVGMEDYLDKEPQN-LSGGQKQRVAIASVLALNPE 162
|
170 180 190
....*....|....*....|....*....|.
gi 15240660 253 LLFLDEPTSGLDSTSALSVIKVLKRIAQSGS 283
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRK 193
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
95-290 |
6.50e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.79 E-value: 6.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 95 APSEGIFSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGslKGNVTLNGEVLNSKMQKAIS-----A 169
Cdd:PRK13638 3 ATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQ--KGAVLWQGKPLDYSKRGLLAlrqqvA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 170 YVMQD-DLLFPMLTVEETLMFA------AEFRLPRSLSKSkkslrvQALIDQLGLRNaantvigdEGHRGISGGERRRVS 242
Cdd:PRK13638 81 TVFQDpEQQIFYTDIDSDIAFSlrnlgvPEAEITRRVDEA------LTLVDAQHFRH--------QPIQCLSHGQKKRVA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15240660 243 IGIDIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:PRK13638 147 IAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSH 194
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
101-293 |
1.04e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.05 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 101 FSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALaNRIAKgsLKGNVTLNGEV-------------LNsKMQKAI 167
Cdd:PRK14258 15 FYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNE--LESEVRVEGRVeffnqniyerrvnLN-RLRRQV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 168 SAyVMQDDLLFPMlTVEETLMFAAEfrlprsLSKSKKSLRVQALIDQlGLRNAAN-TVIGDEGHRG---ISGGERRRVSI 243
Cdd:PRK14258 91 SM-VHPKPNLFPM-SVYDNVAYGVK------IVGWRPKLEIDDIVES-ALKDADLwDEIKHKIHKSaldLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15240660 244 GIDIIHDPILLFLDEPTSGLDSTSALSVIKVLK--RIAQSGSMVIMT--LHQPS 293
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVShnLHQVS 215
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
117-287 |
1.30e-09 |
|
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: 61.38 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 117 RDGEILAVLGASGSGKSTLIDALANrIAKGSLKGNVTLNGEVLNSKM-QKAIS---AYVMQD---DLLFPMLTVEETLMF 189
Cdd:TIGR02633 284 RRGEILGVAGLVGAGRTELVQALFG-AYPGKFEGNVFINGKPVDIRNpAQAIRagiAMVPEDrkrHGIVPILGVGKNITL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 190 AA--EFRLPRSLSKSKKSLRVQALIDQLGLRNAANTV-IGdeghrGISGGERRRVSIGIDIIHDPILLFLDEPTSGLDST 266
Cdd:TIGR02633 363 SVlkSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLpIG-----RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVG 437
|
170 180
....*....|....*....|.
gi 15240660 267 SALSVIKVLKRIAQSGSMVIM 287
Cdd:TIGR02633 438 AKYEIYKLINQLAQEGVAIIV 458
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
109-290 |
1.33e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 59.62 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLidALANRIAKGSLKGNVTLNGEVLN--SKMQ--KAISAYVMQD-DLLFPMLTV 183
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTL--ALHLNGLLRPQKGKVLVSGIDTGdfSKLQgiRKLVGIVFQNpETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 184 EETLMFAAE-FRLPrslskskkSLRVQALIDqlglRNAANTVIGDEGHRG---ISGGERRRVSIGIDIIHDPILLFLDEP 259
Cdd:PRK13644 96 EEDLAFGPEnLCLP--------PIEIRKRVD----RALAEIGLEKYRHRSpktLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190
....*....|....*....|....*....|.
gi 15240660 260 TSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHEKGKTIVYITH 194
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
117-287 |
1.45e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 60.30 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 117 RDGEILAVLGASGSGKSTLIDALAnriakGSLKGN--VT-----LNGEVL----NSKMQKAIS---AYVMQDDL--LFPM 180
Cdd:COG4170 31 NEGEIRGLVGESGSGKSLIAKAIC-----GITKDNwhVTadrfrWNGIDLlklsPRERRKIIGreiAMIFQEPSscLDPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 181 LTVEETLMFAaefrLPRSLSKSK-------KSLRVQALIDQLGLRNaantvigdegHRGI--------SGGERRRVSIGI 245
Cdd:COG4170 106 AKIGDQLIEA----IPSWTFKGKwwqrfkwRKKRAIELLHRVGIKD----------HKDImnsyphelTEGECQKVMIAM 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15240660 246 DIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIM 287
Cdd:COG4170 172 AIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSIL 213
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
108-271 |
1.72e-09 |
|
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: 58.64 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 108 LLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAkgSLKGNVTLNGEVLNS---KMQKAISAYVMQDDLLFPMlTVE 184
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQ--PQGGQVLLDGKPISQyehKYLHSKVSLVGQEPVLFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 185 ETLMFAaefrLPRSLSKSKKSLRVQALIDQL--GLRNAANTVIGDEGHRgISGGERRRVSIGIDIIHDPILLFLDEPTSG 262
Cdd:cd03248 106 DNIAYG----LQSCSFECVKEAAQKAHAHSFisELASGYDTEVGEKGSQ-LSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
....*....
gi 15240660 263 LDSTSALSV 271
Cdd:cd03248 181 LDAESEQQV 189
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
67-264 |
1.86e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 59.98 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 67 VLSFTDLTYSVKVRRkftwrrsvssdpgapseGIFSsKTKTL--LNGITGEARDGEILAVLGASGSGKSTLIDALAnRIA 144
Cdd:PRK11308 5 LLQAIDLKKHYPVKR-----------------GLFK-PERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLT-MIE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 145 KGSlKGNVTLNGE-----------VLNSKMQkaisaYVMQDDL--LFPMLTVEETLmfAAEFRLPRSLSKSKKSLRVQAL 211
Cdd:PRK11308 66 TPT-GGELYYQGQdllkadpeaqkLLRQKIQ-----IVFQNPYgsLNPRKKVGQIL--EEPLLINTSLSAAERREKALAM 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15240660 212 IDQLGLRNAantvigdegHRG-----ISGGERRRVSIGIDIIHDPILLFLDEPTSGLD 264
Cdd:PRK11308 138 MAKVGLRPE---------HYDryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
92-271 |
2.26e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.15 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 92 DPGAPS----EGIFSSKTKT---LLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlKGNVTLNGEVlnskmq 164
Cdd:PLN03232 609 QPGAPAisikNGYFSWDSKTskpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-TSSVVIRGSV------ 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 165 kaisAYVMQDDLLFPMlTVEETLMFAAEFRLPRSLskskKSLRVQALIDQLGLRNAAN-TVIGDEGhRGISGGERRRVSI 243
Cdd:PLN03232 682 ----AYVPQVSWIFNA-TVRENILFGSDFESERYW----RAIDVTALQHDLDLLPGRDlTEIGERG-VNISGGQKQRVSM 751
|
170 180
....*....|....*....|....*...
gi 15240660 244 GIDIIHDPILLFLDEPTSGLDSTSALSV 271
Cdd:PLN03232 752 ARAVYSNSDIYIFDDPLSALDAHVAHQV 779
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
109-273 |
2.28e-09 |
|
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: 60.59 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSLKGNVTLNGE--------VLNSKMQKAISAYVMQDDLLFPM 180
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEwvdmtkpgPDGRGRAKRYIGILHQEYDLYPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 181 LTVEETLMFAAEFRLPRSLSKSKKSLRVQALidqlGLRNAANTVIGDEGHRGISGGERRRVSIGIDIIHDPILLFLDEPT 260
Cdd:TIGR03269 380 RTVLDNLTEAIGLELPDELARMKAVITLKMV----GFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPT 455
|
170
....*....|...
gi 15240660 261 SGLDSTSALSVIK 273
Cdd:TIGR03269 456 GTMDPITKVDVTH 468
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
119-264 |
2.44e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.91 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 119 GEILAVLGASGSGKST-------LIDALAnriakgslkGNVTLNGEVLNSK----------MQKAISayvmqddlLFPML 181
Cdd:NF033858 292 GEIFGFLGSNGCGKSTtmkmltgLLPASE---------GEAWLFGQPVDAGdiatrrrvgyMSQAFS--------LYGEL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 182 TVEETLMFAAE-FRLPRSLSKSkkslRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPT 260
Cdd:NF033858 355 TVRQNLELHARlFHLPAAEIAA----RVAEMLERFDLADVADALPDS-----LPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
....
gi 15240660 261 SGLD 264
Cdd:NF033858 426 SGVD 429
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
119-264 |
2.75e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.40 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 119 GEILAVLGASGSGKSTLIDALANRIAKGSlkgnvtlnGEVLnskmqkaisaYVMQDDLLFPMLTVEEtlmfaAEFRLprs 198
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDA--------GEVH----------YRMRDGQLRDLYALSE-----AERRR--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 199 LSKSKKSLRVQALIDqlGLRNA----ANtvIG--------------------------------DEGHRGISGGERRRVS 242
Cdd:PRK11701 86 LLRTEWGFVHQHPRD--GLRMQvsagGN--IGerlmavgarhygdiratagdwlerveidaariDDLPTTFSGGMQQRLQ 161
|
170 180
....*....|....*....|..
gi 15240660 243 IGIDIIHDPILLFLDEPTSGLD 264
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLD 183
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
106-293 |
3.44e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.30 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSLKGNVTLNGEV-LNSKMQKAISAYVM---------QDD 175
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVtLNGEPLAAIDAPRLarlravlpqAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 176 LLFPmLTVEETLMFAaefRLPRSLSKSKKSLRVQALIDQLGLRNAANTVIGDEgHRGISGGERRRVSIGI---------D 246
Cdd:PRK13547 94 PAFA-FSAREIVLLG---RYPHARRAGALTHRDGEIAWQALALAGATALVGRD-VTTLSGGELARVQFARvlaqlwpphD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15240660 247 IIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSM-VIMTLHQPS 293
Cdd:PRK13547 169 AAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPN 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
106-292 |
3.52e-09 |
|
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: 59.82 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSLKGNVTLN----------------GE---VLNSKMQKA 166
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHvalcekcgyverpskvGEpcpVCGGTLEPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 167 ISAYVMQDDLLFPMLTVEETLMFAAEFRL----------PRSLS----KSKKSL-RVQALIDQLGLRNAANTVIgdeghR 231
Cdd:TIGR03269 93 EVDFWNLSDKLRRRIRKRIAIMLQRTFALygddtvldnvLEALEeigyEGKEAVgRAVDLIEMVQLSHRITHIA-----R 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240660 232 GISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSM-VIMTLHQP 292
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIsMVLTSHWP 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
102-287 |
3.95e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.80 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 102 SSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDAL--ANRIAKGSlkgnVTLNGEVLNSK-----MQKAIsAYVMQ- 173
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLfgVDKRAGGE----IRLNGKDISPRspldaVKKGM-AYITEs 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 174 --DDLLFPMLTVEETLMFAAEFRLPR-----SLSKSKKSLRV-QALIDQLGLRNAA-NTVIGDeghrgISGGERRRVSIG 244
Cdd:PRK09700 347 rrDNGFFPNFSIAQNMAISRSLKDGGykgamGLFHEVDEQRTaENQRELLALKCHSvNQNITE-----LSGGNQQKVLIS 421
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15240660 245 IDIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIM 287
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILM 464
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
108-277 |
4.18e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 58.94 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 108 LLNGITGEARDGEILAVLGASGSGKSTLIdalanRIAKG---SLKGNVTLNGE---VLNSKMQKAisAYVMQDDLLFPML 181
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLL-----RIIAGlehQTSGHIRFHGTdvsRLHARDRKV--GFVFQHYALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 182 TVEETLMFAAEFrLPRSLSKSKKSLR--VQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEP 259
Cdd:PRK10851 90 TVFDNIAFGLTV-LPRRERPNAAAIKakVTQLLEMVQLAHLADRYPAQ-----LSGGQKQRVALARALAVEPQILLLDEP 163
|
170
....*....|....*...
gi 15240660 260 TSGLDStsalSVIKVLKR 277
Cdd:PRK10851 164 FGALDA----QVRKELRR 177
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
117-291 |
4.63e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 58.11 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 117 RDGEILAVLGASGSGKSTLIDALaNRIAKGSlKGNVTLNGEVL-NSKMQKAISAY------VMQddllFP--ML---TVE 184
Cdd:PRK13634 31 PSGSYVAIIGHTGSGKSTLLQHL-NGLLQPT-SGTVTIGERVItAGKKNKKLKPLrkkvgiVFQ----FPehQLfeeTVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 185 ETLMFAaefrlPRS--LSKSKKSLRVQALIDQLGLRNAantvIGDEGHRGISGGERRRVSIGIDIIHDPILLFLDEPTSG 262
Cdd:PRK13634 105 KDICFG-----PMNfgVSEEDAKQKAREMIELVGLPEE----LLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190
....*....|....*....|....*....|
gi 15240660 263 LDSTSALSVIKVLKRIAQSGSM-VIMTLHQ 291
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGLtTVLVTHS 205
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
98-281 |
4.93e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 57.79 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 98 EGIFSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKG--SLKGNVTLNGE-VLNSKMQKAISAYVMQD 174
Cdd:PRK10418 8 RNIALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrQTAGRVLLDGKpVAPCALRGRKIATIMQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 175 --DLLFPMLT----VEETLmfaaefrlpRSLSKSKKSLRVQALIDQLGLRNAAnTVIGDEGHRgISGGERRRVSIGIDII 248
Cdd:PRK10418 88 prSAFNPLHTmhthARETC---------LALGKPADDATLTAALEAVGLENAA-RVLKLYPFE-MSGGMLQRMMIALALL 156
|
170 180 190
....*....|....*....|....*....|...
gi 15240660 249 HDPILLFLDEPTSGLDSTSALSVIKVLKRIAQS 281
Cdd:PRK10418 157 CEAPFIIADEPTTDLDVVAQARILDLLESIVQK 189
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
121-293 |
5.02e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.54 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 121 ILAVLGASGSGKSTLIDAL-----ANRIAKgsLKGNVTLNGEVLNSKMQKAIS-----AYVMQDDLLFPMLTVEETLMFA 190
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRTFnrlleLNEEAR--VEGEVRLFGRNIYSPDVDPIEvrrevGMVFQYPNPFPHLTIYDNVAIG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 191 AEFRlprSLSKSKKSL--RVQALIDQLGLRNAANTVIGDEGHRgISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSA 268
Cdd:PRK14267 110 VKLN---GLVKSKKELdeRVEWALKKAALWDEVKDRLNDYPSN-LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGT 185
|
170 180
....*....|....*....|....*
gi 15240660 269 LSVIKVLKRIAQSGSMVIMTlHQPS 293
Cdd:PRK14267 186 AKIEELLFELKKEYTIVLVT-HSPA 209
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
109-290 |
6.50e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.87 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALaNRIAKGSlKGNVTLNGEVLNSK--------MQKAIsAYVMQddllFPM 180
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNI-NALLKPT-TGTVTVDDITITHKtkdkyirpVRKRI-GMVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 181 L-----TVEETLMFAAE-FRLPRSLSKSkkslRVQALIDQLGL-RNaantvIGDEGHRGISGGERRRVSIGIDIIHDPIL 253
Cdd:PRK13646 96 SqlfedTVEREIIFGPKnFKMNLDEVKN----YAHRLLMDLGFsRD-----VMSQSPFQMSGGQMRKIAIVSILAMNPDI 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 15240660 254 LFLDEPTSGLDSTSALSVIKVLKRIA-QSGSMVIMTLH 290
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSH 204
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
97-289 |
7.79e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 7.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 97 SEGIFS-SKTKTL-LNGITGEArdGEILAVLGASGSGKSTLIDALANRIakgslkgnVTLNGEVLNS----------KMQ 164
Cdd:PRK10938 7 SQGTFRlSDTKTLqLPSLTLNA--GDSWAFVGANGSGKSALARALAGEL--------PLLSGERQSQfshitrlsfeQLQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 165 KAISAyVMQD---DLLFPmlTVEETLMFAAEFrlprSLSKSKKSLRVQALIDQLGLrnaanTVIGDEGHRGISGGERRRV 241
Cdd:PRK10938 77 KLVSD-EWQRnntDMLSP--GEDDTGRTTAEI----IQDEVKDPARCEQLAQQFGI-----TALLDRRFKYLSTGETRKT 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15240660 242 SIGIDIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGsmviMTL 289
Cdd:PRK10938 145 LLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSG----ITL 188
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
109-264 |
9.34e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.93 E-value: 9.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALA--NRIAKGSlkgnVTLNGEVLNsKMQKA---IsAYVMQDDLLFPMLTV 183
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAglERITSGE----IWIGGRVVN-ELEPAdrdI-AMVFQNYALYPHMSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 184 EETLMFAAEFRlprSLSKSKKSLRVQAlidqlglrnAANTV-IG---DEGHRGISGGERRRVSIGIDIIHDPILLFLDEP 259
Cdd:PRK11650 94 RENMAYGLKIR---GMPKAEIEERVAE---------AARILeLEpllDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEP 161
|
....*
gi 15240660 260 TSGLD 264
Cdd:PRK11650 162 LSNLD 166
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
109-280 |
9.60e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 58.68 E-value: 9.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLI-------DALANRIakgslkgnvTLNG----EVLNSKMQKAIsAYVMQDDLL 177
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLArllfrfyDVTSGRI---------LIDGqdirDVTQASLRAAI-GIVPQDTVL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 178 F------------PMLTVEEtLMFAAEfrlprslskskkslrvQALIDQ--LGLRNAANTVIGDeghRG--ISGGERRRV 241
Cdd:COG5265 444 FndtiayniaygrPDASEEE-VEAAAR----------------AAQIHDfiESLPDGYDTRVGE---RGlkLSGGEKQRV 503
|
170 180 190
....*....|....*....|....*....|....*....
gi 15240660 242 SIGIDIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQ 280
Cdd:COG5265 504 AIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR 542
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
118-264 |
1.11e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 57.74 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 118 DGEILAVLGASGSGKSTLIdALANRIAKGSlKGNVTLNG----EVLNSKMQKAIS---AYVMQDDLLFPMLTVEETLMFA 190
Cdd:PRK10070 53 EGEIFVIMGLSGSGKSTMV-RLLNRLIEPT-RGQVLIDGvdiaKISDAELREVRRkkiAMVFQSFALMPHMTVLDNTAFG 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240660 191 AEFRLPRSLSKSKKSLRVqalIDQLGLRNAANTViGDEghrgISGGERRRVSIGIDIIHDPILLFLDEPTSGLD 264
Cdd:PRK10070 131 MELAGINAEERREKALDA---LRQVGLENYAHSY-PDE----LSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
115-287 |
1.12e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.11 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 115 EARDGEILAVLGASGSGKSTLIDAL--ANRIAKGSlkgnVTLNGEVLNSK-MQKAIS---AYVMQDDL---LFPMLTVEE 185
Cdd:COG1129 274 SVRAGEILGIAGLVGAGRTELARALfgADPADSGE----IRLDGKPVRIRsPRDAIRagiAYVPEDRKgegLVLDLSIRE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 186 TLMFAAEFRLPRS--LSKSKKSLRVQALIDQLGLR-NAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPTSG 262
Cdd:COG1129 350 NITLASLDRLSRGglLDRRRERALAEEYIKRLRIKtPSPEQPVGN-----LSGGNQQKVVLAKWLATDPKVLILDEPTRG 424
|
170 180
....*....|....*....|....*
gi 15240660 263 LDSTSALSVIKVLKRIAQSGSMVIM 287
Cdd:COG1129 425 IDVGAKAEIYRLIRELAAEGKAVIV 449
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
100-278 |
1.77e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 56.73 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 100 IFSSKTKTL--LNGITGEARDGEILAVLGASGSGKSTLIdALANRIAKGSlKGNVTLNGEVLNSKMQKAISAY------V 171
Cdd:PRK11153 10 VFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLI-RCINLLERPT-SGRVLVDGQDLTALSEKELRKArrqigmI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 172 MQDdllFPML---TVEETLMFAAEF-RLPRSLSKSkkslRVQALIDQLGL---RNA--ANtvigdeghrgISGGERRRVS 242
Cdd:PRK11153 88 FQH---FNLLssrTVFDNVALPLELaGTPKAEIKA----RVTELLELVGLsdkADRypAQ----------LSGGQKQRVA 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 15240660 243 IGIDIIHDPILLFLDEPTSGLDSTSALSVIKVLKRI 278
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDI 186
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
97-294 |
1.83e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 55.41 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 97 SEGIFS--SKTKTLLNgITGEARDGEILAVLGASGSGKSTLIDALANRIAKgsLKGNVTLNGEVLNSKMQKAIS------ 168
Cdd:cd03290 4 TNGYFSwgSGLATLSN-INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQT--LEGKVHWSNKNESEPSFEATRsrnrys 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 169 -AYVMQDDLLFPMlTVEETLMFAAEFrlprslskskKSLRVQALIDQLGLRNAANTV-IGDE---GHRGI--SGGERRRV 241
Cdd:cd03290 81 vAYAAQKPWLLNA-TVEENITFGSPF----------NKQRYKAVTDACSLQPDIDLLpFGDQteiGERGInlSGGQRQRI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15240660 242 SIGIDIIHDPILLFLDEPTSGLDS--TSALSVIKVLKRIAQSGSMVIMTLHQPSY 294
Cdd:cd03290 150 CVARALYQNTNIVFLDDPFSALDIhlSDHLMQEGILKFLQDDKRTLVLVTHKLQY 204
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
106-276 |
1.85e-08 |
|
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: 53.61 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkgnvtlnGEVlnskmqkaisayvmqddllfpmltvee 185
Cdd:cd03221 13 KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDE--------GIV--------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 186 tlmfaaefrlprslsKSKKSLRVqALIDQLglrnaantvigdeghrgiSGGERRRVSIGIDIIHDPILLFLDEPTSGLDS 265
Cdd:cd03221 58 ---------------TWGSTVKI-GYFEQL------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
170
....*....|.
gi 15240660 266 TSALSVIKVLK 276
Cdd:cd03221 104 ESIEALEEALK 114
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
106-288 |
1.93e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 56.26 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALA---NRIAKGSLKGNVTLNG-------EVLNSKMQKAIsayVMQDD 175
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNrmnDKVSGYRYSGDVLLGGrsifnyrDVLEFRRRVGM---LFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 176 LLFPMLTVEETLMFAAEFRL-PRslskskKSLR--VQALIDQLGLRNAANTVIGDEGHRgISGGERRRVSIGIDIIHDPI 252
Cdd:PRK14271 111 NPFPMSIMDNVLAGVRAHKLvPR------KEFRgvAQARLTEVGLWDAVKDRLSDSPFR-LSGGQQQLLCLARTLAVNPE 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 15240660 253 LLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMT 288
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVT 219
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
109-267 |
2.10e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 57.81 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKMQKAIS---AYVMQDDLLFPMlTVEE 185
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTG--GQVLLDGVPLVQYDHHYLHrqvALVGQEPVLFSG-SVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 186 TLMFAAEFRLPRSLSKSKKSLRVQALIdqLGLRNAANTVIGDEGHRgISGGERRRVSIGIDIIHDPILLFLDEPTSGLDS 265
Cdd:TIGR00958 574 NIAYGLTDTPDEEIMAAAKAANAHDFI--MEFPNGYDTEVGEKGSQ-LSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
..
gi 15240660 266 TS 267
Cdd:TIGR00958 651 EC 652
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
109-290 |
2.17e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 55.27 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALANrIAKGSlKGNVTLNGEVLNSKMQKAIS------AYVMQDDLLFPMLT 182
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG-IERPS-AGKIWFSGHDITRLKNREVPflrrqiGMIFQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 183 VEETLMFAAefrLPRSLSKSKKSLRVQALIDQLGLRNAA-NTVIGdeghrgISGGERRRVSIGIDIIHDPILLFLDEPTS 261
Cdd:PRK10908 96 VYDNVAIPL---IIAGASGDDIRRRVSAALDKVGLLDKAkNFPIQ------LSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180
....*....|....*....|....*....
gi 15240660 262 GLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:PRK10908 167 NLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
119-275 |
2.50e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 57.34 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 119 GEILAVLGASGSGKSTlIDALANRIAKGSlKGNVTLNGEVLN----SKMQKAIsAYVMQDDLLFPMlTVEETLMFAAEFR 194
Cdd:PRK11176 369 GKTVALVGRSGSGKST-IANLLTRFYDID-EGEILLDGHDLRdytlASLRNQV-ALVSQNVHLFND-TIANNIAYARTEQ 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 195 LPR-SLSKSKKSLRVQALIDQLglRNAANTVIGDEGhRGISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSALSVIK 273
Cdd:PRK11176 445 YSReQIEEAARMAYAMDFINKM--DNGLDTVIGENG-VLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQA 521
|
..
gi 15240660 274 VL 275
Cdd:PRK11176 522 AL 523
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
109-290 |
4.07e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.46 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLN-SKMQKAISAYVM---QDDLLFPMLTVE 184
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDA--GSILIDGQEMRfASTTAALAAGVAiiyQELHLVPEMTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 185 ETLMFAaefRLPRSLSKSKKSL---RVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPTS 261
Cdd:PRK11288 98 ENLYLG---QLPHKGGIVNRRLlnyEAREQLEHLGVDIDPDTPLKY-----LSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180
....*....|....*....|....*....
gi 15240660 262 GLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:PRK11288 170 SLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
109-291 |
4.10e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.33 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALANriAKGSLKGNVTLNGEVLNsKMQKAISA-----YVMQDDLLFPMLTV 183
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSG--IHEPTKGTITINNINYN-KLDHKLAAqlgigIIYQELSVIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 184 EETLMFAaefRLPRS-------LSKSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFL 256
Cdd:PRK09700 98 LENLYIG---RHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVAN-----LSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190
....*....|....*....|....*....|....*
gi 15240660 257 DEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLHQ 291
Cdd:PRK09700 170 DEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHK 204
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
110-264 |
4.54e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 55.00 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 110 NGITGEARDGEILAVLGASGSGKSTLIDALAnriakGSLK---GNVTLNGEVLNSKMQKAISAYVM----QDDLLFPMLT 182
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLT-----GFYKptgGTILLRGQHIEGLPGHQIARMGVvrtfQHVRLFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 183 VEETLM-----------FAAEFRLPRSLSKSKKSL-RVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHD 250
Cdd:PRK11300 97 VIENLLvaqhqqlktglFSGLLKTPAFRRAESEALdRAATWLERVGLLEHANRQAGN-----LAYGQQRRLEIARCMVTQ 171
|
170
....*....|....
gi 15240660 251 PILLFLDEPTSGLD 264
Cdd:PRK11300 172 PEILMLDEPAAGLN 185
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
117-287 |
4.73e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 117 RDGEILAVLGASGSGKSTLIDALANrIAKGSLKGNVTLNGEVLN-SKMQKAIS---AYVMQD---DLLFPMLTVEETLMF 189
Cdd:PRK13549 286 RRGEILGIAGLVGAGRTELVQCLFG-AYPGRWEGEIFIDGKPVKiRNPQQAIAqgiAMVPEDrkrDGIVPVMGVGKNITL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 190 AA--EFRLPRSLSKSKKSLRVQALIDQLGLRNAANTV-IGdeghrGISGGERRRVSIGIDIIHDPILLFLDEPTSGLDST 266
Cdd:PRK13549 365 AAldRFTGGSRIDDAAELKTILESIQRLKVKTASPELaIA-----RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVG 439
|
170 180
....*....|....*....|.
gi 15240660 267 SALSVIKVLKRIAQSGSMVIM 287
Cdd:PRK13549 440 AKYEIYKLINQLVQQGVAIIV 460
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
117-290 |
4.78e-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: 56.33 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 117 RDGEILAVLGASGSGKSTLIDALAnriakGSLK---GNVTLNG---EVLN----SKMQ---KAISA----------YVmq 173
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILS-----GELKpnlGDYDEEPswdEVLKrfrgTELQdyfKKLANgeikvahkpqYV-- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 174 dDLLfPML---TVEETLMFAAEfrlprslsksKKSLRvqALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHD 250
Cdd:COG1245 170 -DLI-PKVfkgTVRELLEKVDE----------RGKLD--ELAEKLGLENILDRDISE-----LSGGELQRVAIAAALLRD 230
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15240660 251 PILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:COG1245 231 ADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
117-286 |
6.28e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 117 RDGEILAVLGASGSGKSTLIDALAnriakGSLK---GNVTLNG---EVLN----SKMQ--------KAISA-----YVmq 173
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKILS-----GELIpnlGDYEEEPswdEVLKrfrgTELQnyfkklynGEIKVvhkpqYV-- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 174 dDLLfPML---TVEETLMFAAEfrlprslsksKKSLRvqALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHD 250
Cdd:PRK13409 170 -DLI-PKVfkgKVRELLKKVDE----------RGKLD--EVVERLGLENILDRDISE-----LSGGELQRVAIAAALLRD 230
|
170 180 190
....*....|....*....|....*....|....*.
gi 15240660 251 PILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVI 286
Cdd:PRK13409 231 ADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLV 266
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
101-264 |
7.18e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.39 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 101 FSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVL----NSKMQKAISAYVM--QD 174
Cdd:PRK11831 15 FTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDH--GEILFDGENIpamsRSRLYTVRKRMSMlfQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 175 DLLFPMLTVEETLMFA--AEFRLPRSLSKSKKSLRVQALidqlGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPI 252
Cdd:PRK11831 93 GALFTDMNVFDNVAYPlrEHTQLPAPLLHSTVMMKLEAV----GLRGAAKLMPSE-----LSGGMARRAALARAIALEPD 163
|
170
....*....|..
gi 15240660 253 LLFLDEPTSGLD 264
Cdd:PRK11831 164 LIMFDEPFVGQD 175
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
112-287 |
7.23e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.75 E-value: 7.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 112 ITGEARDGEILAVLGASGSGKST-------LIDaLANRIAKGSLkgnvTLNGEVLNSKMQK-------AISAYVMQDDL- 176
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVsslaimgLID-YPGRVMAEKL----EFNGQDLQRISEKerrnlvgAEVAMIFQDPMt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 177 -LFPMLTVEETLMFAaefrLPRSLSKSKKSLRVQA--LIDQLGLRNAANTVigDEGHRGISGGERRRVSIGIDIIHDPIL 253
Cdd:PRK11022 101 sLNPCYTVGFQIMEA----IKVHQGGNKKTRRQRAidLLNQVGIPDPASRL--DVYPHQLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190
....*....|....*....|....*....|....
gi 15240660 254 LFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIM 287
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLLELQQKENMALV 208
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
94-290 |
7.63e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 54.37 E-value: 7.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 94 GAPSEGifssktkTLLNGITGEARDGEILAVLGASGSGKSTLIDALaNRIAKGSlKGNVTLNGEVLNSKMQ-KAISAYVM 172
Cdd:PRK13649 15 GTPFEG-------RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLL-NGLHVPT-QGSVRVDDTLITSTSKnKDIKQIRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 173 QDDLLF--PMLTV-EETLMFAAEFRlPRSLSKSKK--------SLRVQALIDQLGLRNAANtvigdeghrgISGGERRRV 241
Cdd:PRK13649 86 KVGLVFqfPESQLfEETVLKDVAFG-PQNFGVSQEeaealareKLALVGISESLFEKNPFE----------LSGGQMRRV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15240660 242 SIGIDIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLH 290
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
109-290 |
7.92e-08 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 53.65 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALAnRIAKGSlKGNVTLNGEVLNS----KMQKAISaYVMQDDLLFPMlTVE 184
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALF-RLVELS-SGSILIDGVDISKiglhDLRSRIS-IIPQDPVLFSG-TIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 185 ETLMF---AAEFRLPRSLSKSKKSLRVQALIDQLglrnaaNTVIgDEGHRGISGGERRRVSIGIDIIHDPILLFLDEPTS 261
Cdd:cd03244 96 SNLDPfgeYSDEELWQALERVGLKEFVESLPGGL------DTVV-EEGGENLSVGQRQLLCLARALLRKSKILVLDEATA 168
|
170 180
....*....|....*....|....*....
gi 15240660 262 GLDSTSALSVIKVLKRiAQSGSMVIMTLH 290
Cdd:cd03244 169 SVDPETDALIQKTIRE-AFKDCTVLTIAH 196
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
124-288 |
8.42e-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: 55.33 E-value: 8.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 124 VLGASGSGKSTLIdalanRIAKGSLKgnvTLNGEVLNSKMQKAisAYVMQDDLLFPMLTVEETLM--------------- 188
Cdd:TIGR03719 36 VLGLNGAGKSTLL-----RIMAGVDK---DFNGEARPQPGIKV--GYLPQEPQLDPTKTVRENVEegvaeikdaldrfne 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 189 FAAEFRLPRSLSKS--KKSLRVQALIDQLGLRNAANTV----------IGDEGHRGISGGERRRVSIGIDIIHDPILLFL 256
Cdd:TIGR03719 106 ISAKYAEPDADFDKlaAEQAELQEIIDAADAWDLDSQLeiamdalrcpPWDADVTKLSGGERRRVALCRLLLSKPDMLLL 185
|
170 180 190
....*....|....*....|....*....|..
gi 15240660 257 DEPTSGLDSTSALSVIKVLKRIAqsGSMVIMT 288
Cdd:TIGR03719 186 DEPTNHLDAESVAWLERHLQEYP--GTVVAVT 215
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
155-289 |
1.03e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 155 NGEVL---------NSKMQKAISAYVMQDDLLFPMlTVEETLMFAAEFRLPRSLSKSKKSLRVQALIDQLglRNAANTVI 225
Cdd:PTZ00265 1276 SGKILldgvdicdyNLKDLRNLFSIVSQEPMLFNM-SIYENIKFGKEDATREDVKRACKFAAIDEFIESL--PNKYDTNV 1352
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240660 226 GDEGhRGISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTL 289
Cdd:PTZ00265 1353 GPYG-KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITI 1415
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
117-264 |
2.21e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.24 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 117 RDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKM-QKAIS---AYVMQD---DLLFPMLTVEETLMF 189
Cdd:PRK10762 276 RKGEILGVSGLMGAGRTELMKVLYGALPRTS--GYVTLDGHEVVTRSpQDGLAngiVYISEDrkrDGLVLGMSVKENMSL 353
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240660 190 AAEFRLPRSLSKSKKSLRVQALIDQLGLRN----AANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPTSGLD 264
Cdd:PRK10762 354 TALRYFSRAGGSLKHADEQQAVSDFIRLFNiktpSMEQAIGL-----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
106-290 |
2.33e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.68 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKMQKAIS---AYVMQDDLLFPMLT 182
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAH--GHVWLDGEHIQHYASKEVArriGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 183 VEEtlmFAAEFRLPRSLSKSKKSLRVQALIDQlGLRNAANTVIGDEGHRGISGGERRRVSIGIDIIHDPILLFLDEPTSG 262
Cdd:PRK10253 98 VQE---LVARGRYPHQPLFTRWRKEDEEAVTK-AMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180
....*....|....*....|....*....
gi 15240660 263 LDSTSALSVIKVLKRIAQS-GSMVIMTLH 290
Cdd:PRK10253 174 LDISHQIDLLELLSELNREkGYTLAAVLH 202
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
108-275 |
2.58e-07 |
|
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: 53.98 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 108 LLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNS----KMQKAISaYVMQDDLLFPMLTV 183
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARS--GEILLNGFSLKDidrhTLRQFIN-YLPQEPYIFSGSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 184 EETLMFAAEFRLPRSLSKSKKSLRVQALIDQLGLrnAANTVIGDEGHrGISGGERRRVSIGIDIIHDPILLFLDEPTSGL 263
Cdd:TIGR01193 566 ENLLLGAKENVSQDEIWAACEIAEIKDDIENMPL--GYQTELSEEGS-SISGGQKQRIALARALLTDSKVLILDESTSNL 642
|
170
....*....|..
gi 15240660 264 DSTSALSVIKVL 275
Cdd:TIGR01193 643 DTITEKKIVNNL 654
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
93-291 |
2.61e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.40 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 93 PGAPSEGIFSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIdalanriakGSLKGNVTLN-GEVLnskMQKAIsAYV 171
Cdd:PTZ00243 660 PKMKTDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLL---------QSLLSQFEISeGRVW---AERSI-AYV 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 172 MQDDLLFPMlTVEETLMFAAEFRLPRsLSKSKKSLRVQALIDQLGlrNAANTVIGDEGhRGISGGERRRVSIGIDIIHDP 251
Cdd:PTZ00243 727 PQQAWIMNA-TVRGNILFFDEEDAAR-LADAVRVSQLEADLAQLG--GGLETEIGEKG-VNLSGGQKARVSLARAVYANR 801
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15240660 252 ILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLHQ 291
Cdd:PTZ00243 802 DVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQ 841
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
96-287 |
3.19e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 96 PSEGIFSSKTKTLLN-----GITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNG-EVLNSKMQKAIS- 168
Cdd:PRK10982 246 PGEVILEVRNLTSLRqpsirDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSA--GTITLHGkKINNHNANEAINh 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 169 --AYVMQDDL---LFPMLTVEETLMFA------AEFRLprsLSKSKKSLRVQALIDQLGLRNAAN-TVIGDeghrgISGG 236
Cdd:PRK10982 324 gfALVTEERRstgIYAYLDIGFNSLISnirnykNKVGL---LDNSRMKSDTQWVIDSMRVKTPGHrTQIGS-----LSGG 395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15240660 237 ERRRVSIGIDIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIM 287
Cdd:PRK10982 396 NQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIII 446
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
106-289 |
3.23e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 52.49 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTlIDALANRI--AKGSLKGNVTLNGEVLNSKMQKAIS---AYVMQD-DLLFP 179
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKST-ISKLINGLllPDDNPNSKITVDGITLTAKTVWDIRekvGIVFQNpDNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 180 MLTVEETLMFAAEfrlPRSLSKSKKSLRVQALIDQLGLRNAAntvigDEGHRGISGGERRRVSI-GIDIIhDPILLFLDE 258
Cdd:PRK13640 99 GATVGDDVAFGLE---NRAVPRPEMIKIVRDVLADVGMLDYI-----DSEPANLSGGQKQRVAIaGILAV-EPKIIILDE 169
|
170 180 190
....*....|....*....|....*....|.
gi 15240660 259 PTSGLDSTSALSVIKVLKRIAQSGSMVIMTL 289
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLKKKNNLTVISI 200
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
193-288 |
4.43e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.82 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 193 FRLPRSLSKSKKSLRVQA--LIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSALS 270
Cdd:NF000106 108 YMIGR*LDLSRKDARARAdeLLERFSLTEAAGRAAAK-----YSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNE 182
|
90
....*....|....*...
gi 15240660 271 VIKVLKRIAQSGSMVIMT 288
Cdd:NF000106 183 VWDEVRSMVRDGATVLLT 200
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
106-290 |
4.89e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 51.65 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIA--KGSLKGNVTLNgevlnskmqkaiSAYVMQD---DLLFPm 180
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVApdEGVIKRNGKLR------------IGYVPQKlylDTTLP- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 181 LTVEETLMFAAEFRLPRSLSKSKkslRVQA--LIDQlglrnaantvigdeGHRGISGGERRRVSIGIDIIHDPILLFLDE 258
Cdd:PRK09544 84 LTVNRFLRLRPGTKKEDILPALK---RVQAghLIDA--------------PMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190
....*....|....*....|....*....|...
gi 15240660 259 PTSGLDSTSALSVIKVLKRIAQS-GSMVIMTLH 290
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRRElDCAVLMVSH 179
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
109-290 |
1.16e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.78 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIdalanRIAKGSLkgnVTLNGEVL--------NSKMQKAISAYVMQDDLLFPM 180
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMI-----QLTNGLI---ISETGQTIvgdyaipaNLKKIKEVKRLRKEIGLVFQF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 181 L-------TVEETLMFAaefrlPRSLSKSKKSL--RVQALIDQLGLRNaantvigDEGHRG---ISGGERRRVSIGIDII 248
Cdd:PRK13645 99 PeyqlfqeTIEKDIAFG-----PVNLGENKQEAykKVPELLKLVQLPE-------DYVKRSpfeLSGGQKRRVALAGIIA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15240660 249 HDPILLFLDEPTSGLDSTSALSVIKVLKRIAQS-GSMVIMTLH 290
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTH 209
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
101-291 |
1.35e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.56 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 101 FSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGslKGNVTLNGEvlnsKMQKAISAYvmQDDLLF-- 178
Cdd:PRK13540 9 FDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPE--KGEILFERQ----SIKKDLCTY--QKQLCFvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 179 ------PMLTVEETLMFAAEFrlprslskSKKSLRVQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPI 252
Cdd:PRK13540 81 hrsginPYLTLRENCLYDIHF--------SPGAVGITELCRLFSLEHLIDYPCGL-----LSSGQKRQVALLRLWMSKAK 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 15240660 253 LLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLHQ 291
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
119-265 |
1.46e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 50.87 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 119 GEILAVLGASGSGKSTLIdalanRIAKGSLK---GNVTLNGE-VLNSKMQKAISAYVMQDDLLFPMLTVEETLMFAAEFR 194
Cdd:PRK11432 32 GTMVTLLGPSGCGKTTVL-----RLVAGLEKpteGQIFIDGEdVTHRSIQQRDICMVFQSYALFPHMSLGENVGYGLKML 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240660 195 lprSLSKSKKSLRVQ---ALIDQLGLrnaantviGDEGHRGISGGERRRVSIGIDIIHDPILLFLDEPTSGLDS 265
Cdd:PRK11432 107 ---GVPKEERKQRVKealELVDLAGF--------EDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
102-291 |
1.51e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.17 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 102 SSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSLKGNVTLNGEVLN--SKMQKAISAYVMQddLLFP 179
Cdd:PRK09580 10 SVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLelSPEDRAGEGIFMA--FQYP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 180 MltveETLMFAAEFRLPRSLSKSKKsLRVQALID----------QLGLRNAANTVIGDEGHRGISGGERRRVSIGIDIIH 249
Cdd:PRK09580 88 V----EIPGVSNQFFLQTALNAVRS-YRGQEPLDrfdfqdlmeeKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15240660 250 DPILLFLDEPTSGLDstsalsvIKVLKRIAQ--------SGSMVIMTLHQ 291
Cdd:PRK09580 163 EPELCILDESDSGLD-------IDALKIVADgvnslrdgKRSFIIVTHYQ 205
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
106-293 |
2.18e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 50.96 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALAnriakgSL----KGNVTLNGevlnskmqkaisayvmQDDLLF--- 178
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIA------GLwpygSGRIARPA----------------GARVLFlpq 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 179 ----PMLTVEETLMFAAEfrlPRSLSKSkkslRVQALIDQLGLRNAANTVigDEG---HRGISGGERRRVSIGIDIIHDP 251
Cdd:COG4178 434 rpylPLGTLREALLYPAT---AEAFSDA----ELREALEAVGLGHLAERL--DEEadwDQVLSLGEQQRLAFARLLLHKP 504
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15240660 252 ILLFLDEPTSGLDSTSALSVIKVLKRiAQSGSMVIMTLHQPS 293
Cdd:COG4178 505 DWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHRST 545
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
102-290 |
3.86e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 49.32 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 102 SSKTKTLLNGITGEARDGEILAVLGASGSGKSTL---IDAL-ANRIAKGSLKGNVTLNGEVLNSKMQKAISAYVMQDDLL 177
Cdd:PRK13633 19 ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALlIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNPDNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 178 FPMLtVEETLMFAaefrlPRSLSKSKKSLR--VQALIDQLGL----RNAANTvigdeghrgISGGERRRVSI-GIDIIHd 250
Cdd:PRK13633 99 VATI-VEEDVAFG-----PENLGIPPEEIRerVDESLKKVGMyeyrRHAPHL---------LSGGQKQRVAIaGILAMR- 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15240660 251 PILLFLDEPTSGLDSTSALSVIKVLKRI-AQSGSMVIMTLH 290
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITH 203
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
106-264 |
5.91e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAkgSLKGNVTLngevlnskmQKAIS-AYVMQDDLLFpmLTVE 184
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELA--PVSGEIGL---------AKGIKlGYFAQHQLEF--LRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 185 ETLMFAAEFRLPRSLSkskkslrvQALIDQLGLRNAANTVIGDEGHRgISGGERRRVSIGIDIIHDPILLFLDEPTSGLD 264
Cdd:PRK10636 392 ESPLQHLARLAPQELE--------QKLRDYLGGFGFQGDKVTEETRR-FSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
112-287 |
6.41e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.28 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 112 ITGEARDGEILAVLGASGSGKSTLIDALAN-RIAKGslkGNVTLNGEVLNS-----KMQKAIsAYVMQDDL---LF---P 179
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGlRPARG---GRIMLNGKEINAlstaqRLARGL-VYLPEDRQssgLYldaP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 180 MLTVEETLMFAaefRLPRSLSKSKKSLRVQALIDQLGLRNAAntviGDEGHRGISGGERRRVSIGIDIIHDPILLFLDEP 259
Cdd:PRK15439 358 LAWNVCALTHN---RRGFWIKPARENAVLERYRRALNIKFNH----AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180
....*....|....*....|....*...
gi 15240660 260 TSGLDSTSALSVIKVLKRIAQSGSMVIM 287
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQNVAVLF 458
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
119-275 |
6.55e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.47 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 119 GEILAVLGASGSGKSTLIDALANRIAkgSLKGNVTLNGEVLN----SKMQ--KAISAYVMQDDL--LFPMLTVEETLMfa 190
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVE--SQGGEIIFNGQRIDtlspGKLQalRRDIQFIFQDPYasLDPRQTVGDSIM-- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 191 AEFRLPRSLSKSKKSLRVQALIDQLGLRNAANTVIGDEghrgISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSALS 270
Cdd:PRK10261 426 EPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQ 501
|
....*
gi 15240660 271 VIKVL 275
Cdd:PRK10261 502 IINLL 506
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
109-264 |
6.71e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.74 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIdAL---ANRIAKGSLkgnvtlngEVLNSKMQKA---------IsAYvMQDDL 176
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLL-SLiagARKIQQGRV--------EVLGGDMADArhrravcprI-AY-MPQGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 177 ---LFPMLTVEETLMFAAefRLpRSLSKSKKSLRVQALIDQLGL-----RNAANtvigdeghrgISGGERRRVSIGIDII 248
Cdd:NF033858 86 gknLYPTLSVFENLDFFG--RL-FGQDAAERRRRIDELLRATGLapfadRPAGK----------LSGGMKQKLGLCCALI 152
|
170
....*....|....*.
gi 15240660 249 HDPILLFLDEPTSGLD 264
Cdd:NF033858 153 HDPDLLILDEPTTGVD 168
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
109-293 |
6.76e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.93 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLidalanriakgslkgnvtlngevlnskmqkaisayvmqddllfpmltVEETLM 188
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL-----------------------------------------------VNEGLY 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 189 FAAEFRLPRSLSKSKKSLRV-----QALIDQ----LGLRNAANTvigdeghrgISGGERRRVSIG--IDIIHDPILLFLD 257
Cdd:cd03238 44 ASGKARLISFLPKFSRNKLIfidqlQFLIDVglgyLTLGQKLST---------LSGGELQRVKLAseLFSEPPGTLFILD 114
|
170 180 190
....*....|....*....|....*....|....*.
gi 15240660 258 EPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLHQPS 293
Cdd:cd03238 115 EPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLD 150
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
118-292 |
7.01e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.58 E-value: 7.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 118 DGEILAVLGASGSGKSTLIDALANriakgslkgNVTLNGEVLNSKMQKAISAYVMQddllfpmltVEETLMFaaefrlpr 197
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIGL---------ALGGAQSATRRRSGVKAGCIVAA---------VSAELIF-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 198 slskskkslrvqaLIDQLglrnaantvigdeghrgiSGGERRRVSIGIDIIH----DPILLFLDEPTSGLDSTSALSVIK 273
Cdd:cd03227 74 -------------TRLQL------------------SGGEKELSALALILALaslkPRPLYILDEIDRGLDPRDGQALAE 122
|
170
....*....|....*....
gi 15240660 274 VLKRIAQSGSMVIMTLHQP 292
Cdd:cd03227 123 AILEHLVKGAQVIVITHLP 141
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
124-267 |
7.17e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 124 VLGASGSGKSTLIdalanRIAKGSLKGNvtlNGEVlnsKMQKAIS-AYVMQDDLLFPMLTVEETLM-------------- 188
Cdd:PRK11819 38 VLGLNGAGKSTLL-----RIMAGVDKEF---EGEA---RPAPGIKvGYLPQEPQLDPEKTVRENVEegvaevkaaldrfn 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 189 -FAAEFRLPRSLSKS--KKSLRVQALIDQLGLRNAANTV----------IGDEGHRGISGGERRRVSIGIDIIHDPILLF 255
Cdd:PRK11819 107 eIYAAYAEPDADFDAlaAEQGELQEIIDAADAWDLDSQLeiamdalrcpPWDAKVTKLSGGERRRVALCRLLLEKPDMLL 186
|
170
....*....|..
gi 15240660 256 LDEPTSGLDSTS 267
Cdd:PRK11819 187 LDEPTNHLDAES 198
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
77-264 |
8.16e-06 |
|
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: 48.31 E-value: 8.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 77 VKVRRKFTWRRSVSSDPGApSEGIFSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNG 156
Cdd:cd03291 22 EKAKQENNDRKHSSDDNNL-FFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSE--GKIKHSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 157 EVlnskmqkaisAYVMQDDLLFPMlTVEETLMFAAEFRLPRSLSKSKKslrVQALIDQLGLRNAANTVIGdEGHRGISGG 236
Cdd:cd03291 99 RI----------SFSSQFSWIMPG-TIKENIIFGVSYDEYRYKSVVKA---CQLEEDITKFPEKDNTVLG-EGGITLSGG 163
|
170 180
....*....|....*....|....*...
gi 15240660 237 ERRRVSIGIDIIHDPILLFLDEPTSGLD 264
Cdd:cd03291 164 QRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
109-264 |
8.52e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.87 E-value: 8.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTLIDALAN--RIAKGSlkgnVTLNGEVLN----SKMQKAISAYVMQDDL---LFP 179
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGlrPPASGS----IRLDGEDITglspRERRRLGVAYIPEDRLgrgLVP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 180 MLTVEETLMFAAEFRLPRS----LSKSKKSLRVQALIDQLGLRNA-ANTVIgdeghRGISGGERRRVSIGIDIIHDPILL 254
Cdd:COG3845 350 DMSVAENLILGRYRRPPFSrggfLDRKAIRAFAEELIEEFDVRTPgPDTPA-----RSLSGGNQQKVILARELSRDPKLL 424
|
170
....*....|
gi 15240660 255 FLDEPTSGLD 264
Cdd:COG3845 425 IAAQPTRGLD 434
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
101-293 |
9.94e-06 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 47.14 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 101 FSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEV-----LNSKMQkaisayvmqdd 175
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDS--GTVTVRGRVssllgLGGGFN----------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 176 llfPMLTVEETLMFAAEFrlpRSLSKSKKSLRVQALIDQLGLRNAANTVIgdeghRGISGGERRRVSIGIDIIHDPILLF 255
Cdd:cd03220 97 ---PELTGRENIYLNGRL---LGLSRKEIDEKIDEIIEFSELGDFIDLPV-----KTYSSGMKARLAFAIATALEPDILL 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 15240660 256 LDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLHQPS 293
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPS 203
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
234-293 |
1.52e-05 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 45.99 E-value: 1.52e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 234 SGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSALSVIKVLKriaQSGSMVIMTLHQPS 293
Cdd:cd03223 93 SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK---ELGITVISVGHRPS 149
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
119-276 |
1.77e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.08 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 119 GEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSK----MQKAISAYVMQDDLLFPMLTVEETLMFAAEFR 194
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDA--GSILYLGKEVTFNgpksSQEAGIGIIHQELNLIPQLTIAENIFLGREFV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 195 LPRSLSKSKKSLR-VQALIDQLGLRNAANTVIGDeghrgISGGERRRVSIGIDIIHDPILLFLDEPTSGLDST---SALS 270
Cdd:PRK10762 108 NRFGRIDWKKMYAeADKLLARLNLRFSSDKLVGE-----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTeteSLFR 182
|
....*.
gi 15240660 271 VIKVLK 276
Cdd:PRK10762 183 VIRELK 188
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
101-267 |
2.09e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 48.37 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 101 FSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGslKGNVTLNGEVLNSKMQKAISAYVMQDDLLFPm 180
Cdd:TIGR01271 434 FSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPS--EGKIKHSGRISFSPQTSWIMPGTIKDNIIFG- 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 181 LTVEetlmfaaEFRLpRSLSKSkkslrVQALIDQLGLRNAANTVIGdEGHRGISGGERRRVSIGIDIIHDPILLFLDEPT 260
Cdd:TIGR01271 511 LSYD-------EYRY-TSVIKA-----CQLEEDIALFPEKDKTVLG-EGGITLSGGQRARISLARAVYKDADLYLLDSPF 576
|
....*..
gi 15240660 261 SGLDSTS 267
Cdd:TIGR01271 577 THLDVVT 583
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
104-280 |
2.29e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 46.10 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 104 KTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGSLKGNVTLngevlnskmqkaisayvmqDDLLFPmltv 183
Cdd:COG2401 41 VERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDV-------------------PDNQFG---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 184 eetlmfaaefrlprslskskkslRVQALIDQLGLRNAANTVIGDEGHRGI-------------SGGERRRVSIGIDIIHD 250
Cdd:COG2401 98 -----------------------REASLIDAIGRKGDFKDAVELLNAVGLsdavlwlrrfkelSTGQKFRFRLALLLAER 154
|
170 180 190
....*....|....*....|....*....|
gi 15240660 251 PILLFLDEPTSGLDSTSAlsviKVLKRIAQ 280
Cdd:COG2401 155 PKLLVIDEFCSHLDRQTA----KRVARNLQ 180
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
120-288 |
2.43e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 46.70 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 120 EILAVLGASGSGKSTLI---DALANRIAKGSLKGNVTLNGEVLNSKMQKAIS-----AYVMQDDLLFPMlTVEETLMFAA 191
Cdd:PRK14243 37 QITAFIGPSGCGKSTILrcfNRLNDLIPGFRVEGKVTFHGKNLYAPDVDPVEvrrriGMVFQKPNPFPK-SIYDNIAYGA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 192 EFR-LPRSLSK-SKKSLRVQALIDQLG--LRNAANTvigdeghrgISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTS 267
Cdd:PRK14243 116 RINgYKGDMDElVERSLRQAALWDEVKdkLKQSGLS---------LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPIS 186
|
170 180
....*....|....*....|.
gi 15240660 268 ALSVIKVLKRIAQSGSMVIMT 288
Cdd:PRK14243 187 TLRIEELMHELKEQYTIIIVT 207
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
114-282 |
6.37e-05 |
|
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: 44.10 E-value: 6.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 114 GEARDGEILAVLGASGSGKSTLIDALAnriakGSLKGNvtlngevlnskmqkaisayvmQDDLLFPMLTVeetlmfaaef 193
Cdd:cd03222 20 GVVKEGEVIGIVGPNGTGKTTAVKILA-----GQLIPN---------------------GDNDEWDGITP---------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 194 rlprSLSKSKKSLrvqalidqlglrnaantvigdeghrgiSGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSALSVIK 273
Cdd:cd03222 64 ----VYKPQYIDL---------------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAAR 112
|
....*....
gi 15240660 274 VLKRIAQSG 282
Cdd:cd03222 113 AIRRLSEEG 121
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
67-158 |
8.50e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 44.69 E-value: 8.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 67 VLSFTDLT--YSVKVRRKFTWRRSVSSDPGAPSEgifsskTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALAnria 144
Cdd:COG1134 4 MIEVENVSksYRLYHEPSRSLKELLLRRRRTRRE------EFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIA---- 73
|
90
....*....|....*..
gi 15240660 145 kGSLK---GNVTLNGEV 158
Cdd:COG1134 74 -GILEptsGRVEVNGRV 89
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
236-337 |
8.59e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 45.18 E-value: 8.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 236 GERRRVSIGIDIIHDPILLFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIMTLHQPSYRLLRLLDRLLFLSRGQTVFSG 315
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETA 241
|
90 100 110
....*....|....*....|....*....|....
gi 15240660 316 SP------------AMLPRFFAEFGHPIPeHENR 337
Cdd:PRK15093 242 PSkelvttphhpytQALIRAIPDFGSAMP-HKSR 274
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
199-293 |
8.92e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 199 LSKSKKSL---RVQALIDQLglrnaaNTVIGDEGHRgISGGERRRVSIGIDIIHDPILLFLDEPTSGLDSTSALSVIKVL 275
Cdd:PTZ00265 550 VDVSKKVLihdFVSALPDKY------ETLVGSNASK-LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
90
....*....|....*....
gi 15240660 276 KRI-AQSGSMVIMTLHQPS 293
Cdd:PTZ00265 623 NNLkGNENRITIIIAHRLS 641
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
511-616 |
1.25e-04 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 44.69 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 511 RRSSYVLSHSLVALPSLIILSLAFAAITFwGVGLDggLMGFLFYFLVILASFWAGSSFVTFLSGVVPHVMLGYTIVVAIL 590
Cdd:pfam12698 201 SPLQYWLGKILGDFLVGLLQLLIILLLLF-GIGIP--FGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVI 277
|
90 100
....*....|....*....|....*.
gi 15240660 591 AYFLLFSGFFINRDRIPGYWIWFHYI 616
Cdd:pfam12698 278 LLLSGFFGGLFPLEDPPSFLQWIFSI 303
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
101-291 |
1.46e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 45.29 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 101 FSSKTKTLLNGITGEARDGEILAVLGASGSGKSTLIDALAnRIAkgSLKGNVTLNGEVLNS-KMQKAISAYVMQDDLLFp 179
Cdd:TIGR01271 1227 YTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLL--STEGEIQIDGVSWNSvTLQTWRKAFGVIPQKVF- 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 180 mltveetlMFAAEFRLPRSLSKSKKSLRVQALIDQLGLRNAA-------NTVIGDEGHRgISGGERRRVSIGIDIIHDPI 252
Cdd:TIGR01271 1303 --------IFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIeqfpdklDFVLVDGGYV-LSNGHKQLMCLARSILSKAK 1373
|
170 180 190
....*....|....*....|....*....|....*....
gi 15240660 253 LLFLDEPTSGLDSTSALSVIKVLKRiAQSGSMVIMTLHQ 291
Cdd:TIGR01271 1374 ILLLDEPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEHR 1411
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
109-289 |
2.84e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 43.20 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 109 LNGITGEARDGEILAVLGASGSGKSTlIDALANRIAKGSlKGNVTLNGEVLN----SKMQKAISAYVMQDDLLFPMLTVE 184
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKST-IAKLMIGIEKVK-SGEIFYNNQAITddnfEKLRKHIGIVFQNPDNQFVGSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 185 ETLMFAAEfrlPRSLSKSKKSLRVQALIDQLGLRNAANtvigDEGHrGISGGERRRVSIGIDIIHDPILLFLDEPTSGLD 264
Cdd:PRK13648 103 YDVAFGLE---NHAVPYDEMHRRVSEALKQVDMLERAD----YEPN-ALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180
....*....|....*....|....*
gi 15240660 265 STSALSVIKVLKRIAQSGSMVIMTL 289
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEHNITIISI 199
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
107-291 |
4.10e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 42.92 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 107 TLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIakgSLKGNVTLNGEVLNS-KMQKAISAyvmqddllFPMLTvEE 185
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL---NTEGDIQIDGVSWNSvPLQKWRKA--------FGVIP-QK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 186 TLMFAAEFRL---PRSLSKSKKSLRVQaliDQLGLRNAANTVIGD------EGHRGISGGERRRVSIGIDIIHDPILLFL 256
Cdd:cd03289 86 VFIFSGTFRKnldPYGKWSDEEIWKVA---EEVGLKSVIEQFPGQldfvlvDGGCVLSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190
....*....|....*....|....*....|....*
gi 15240660 257 DEPTSGLDSTSALSVIKVLKRiAQSGSMVIMTLHQ 291
Cdd:cd03289 163 DEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHR 196
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
511-617 |
5.22e-04 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 41.72 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 511 RRSSYVLSHSLVALPSLIILSLAFAAITFWGVGLDGGLMGFLFYFLVILASFWAGSSFVTFLSGVVPHVMLGYTIVVAIL 590
Cdd:COG0842 44 SRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGLSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVI 123
|
90 100
....*....|....*....|....*..
gi 15240660 591 AYFLLFSGFFINRDRIPGYWIWFHYIS 617
Cdd:COG0842 124 LPLTFLSGAFFPIESLPGWLQAIAYLN 150
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
106-287 |
5.52e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 43.17 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 106 KTLLNGITGEARDGEILAVLGASGSGKSTLIDALANRIAKGslKGNVTLNGEVLNSKMQKAIS---AYVMQDdllfPMLT 182
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT--EGEIRLDGRPLSSLSHSVLRqgvAMVQQD----PVVL 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 183 VEEtlmFAAEFRLPRSLSKSK--KSLRVQALIDQL-GLRNAANTVIGDEGHRgISGGERRRVSIGIDIIHDPILLFLDEP 259
Cdd:PRK10790 428 ADT---FLANVTLGRDISEEQvwQALETVQLAELArSLPDGLYTPLGEQGNN-LSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180
....*....|....*....|....*...
gi 15240660 260 TSGLDSTSALSVIKVLKRIAQSGSMVIM 287
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAVREHTTLVVI 531
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
112-287 |
1.05e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.21 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 112 ITGEARDGEILAVLGASGSGKSTLIDAL--ANRIAKGSlkgnVTLNGEVLN-SKMQKAISAYVM------QDDLLFPMLT 182
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLygATRRTAGQ----VYLDGKPIDiRSPRDAIRAGIMlcpedrKAEGIIPVHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 183 VEETLmfaaefrlprSLSKSKKSLRVQALIDQLGLRNAANTVI---------GDEGHRGISGGERRRVSIGIDIIHDPIL 253
Cdd:PRK11288 348 VADNI----------NISARRHHLRAGCLINNRWEAENADRFIrslniktpsREQLIMNLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190
....*....|....*....|....*....|....
gi 15240660 254 LFLDEPTSGLDSTSALSVIKVLKRIAQSGSMVIM 287
Cdd:PRK11288 418 ILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLF 451
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
120-292 |
1.25e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 40.72 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 120 EILAVLGASGSGKSTLIDALANriakgSLKGNVTLNGEVLNSKMQKAisayvmqddllfpmlTVEETLMFAAEFRLprsl 199
Cdd:cd03279 29 GLFLICGPTGAGKSTILDAITY-----ALYGKTPRYGRQENLRSVFA---------------PGEDTAEVSFTFQL---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 200 skSKKSLRVqalIDQLGL--RNAANTVIGDEGH---------RGISGGERRRVSIGI-----DIIHDPI-----LLFLDE 258
Cdd:cd03279 85 --GGKKYRV---ERSRGLdyDQFTRIVLLPQGEfdrflarpvSTLSGGETFLASLSLalalsEVLQNRGgarleALFIDE 159
|
170 180 190
....*....|....*....|....*....|....
gi 15240660 259 PTSGLDSTSALSVIKVLKRIAQSGSMVIMTLHQP 292
Cdd:cd03279 160 GFGTLDPEALEAVATALELIRTENRMVGVISHVE 193
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
119-161 |
3.89e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.51 E-value: 3.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 15240660 119 GEILAVLGASGSGKSTLIDALANRIAKGSlKGNVTLNGEVLNS 161
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPG-GGVIYIDGEDILE 43
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
123-141 |
3.95e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.04 E-value: 3.95e-03
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
118-264 |
3.97e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.32 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 118 DGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLNSKMQK-----------------------------AIS 168
Cdd:PRK11147 28 DNERVCLVGRNGAGKSTLMKILNGEVLLDD--GRIIYEQDLIVARLQQdpprnvegtvydfvaegieeqaeylkryhDIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 169 AYVMQD---DLLFPMLTVEETLMFAAEFRLPRslskskkslRVQALIDQLGLrnAANTVIGDeghrgISGGERRRVSIGI 245
Cdd:PRK11147 106 HLVETDpseKNLNELAKLQEQLDHHNLWQLEN---------RINEVLAQLGL--DPDAALSS-----LSGGWLRKAALGR 169
|
170
....*....|....*....
gi 15240660 246 DIIHDPILLFLDEPTSGLD 264
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLD 188
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
117-264 |
5.43e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 39.39 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 117 RDGEILAVLGASGSGKSTLIDALANRIAKGSlkGNVTLNGEVLN----SKMQKAISAyVMQD--DLLFPMLTVEETLMFA 190
Cdd:PRK15112 37 REGQTLAIIGENGSGKSTLAKMLAGMIEPTS--GELLIDDHPLHfgdySYRSQRIRM-IFQDpsTSLNPRQRISQILDFP 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15240660 191 aeFRLPRSLSKSKKSLRVQALIDQLGLRNaantvigDEGH---RGISGGERRRVSIGIDIIHDPILLFLDEPTSGLD 264
Cdd:PRK15112 114 --LRLNTDLEPEQREKQIIETLRQVGLLP-------DHASyypHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
118-140 |
5.68e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 5.68e-03
10 20
....*....|....*....|...
gi 15240660 118 DGEILAVLGASGSGKSTLIDALA 140
Cdd:COG4913 23 DGRGTLLTGDNGSGKSTLLDAIQ 45
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
107-230 |
7.84e-03 |
|
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: 38.62 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240660 107 TLLNGItgeARDGEILAVLGASGSGKSTLIDALANRiakgsLKGNVTLngevlnskmqkaisAYVmqddlLFPMLTVEET 186
Cdd:COG3267 34 RLEYAL---AQGGGFVVLTGEVGTGKTTLLRRLLER-----LPDDVKV--------------AYI-----PNPQLSPAEL 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15240660 187 L-MFAAEFRLPRSlSKSKKSLrVQALIDQLGLRNAANT---VIGDEGH 230
Cdd:COG3267 87 LrAIADELGLEPK-GASKADL-LRQLQEFLLELAAAGRrvvLIIDEAQ 132
|
|
| |
