|
Name |
Accession |
Description |
Interval |
E-value |
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-392 |
0e+00 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 600.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 2 SAIPMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQ 81
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 82 GIGMVHQHFKLVKSFTVAENIILGMKD-MGLLYDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGA 160
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLGLEPtKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 161 EILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGSTKTELASEEELTRWMVGR 240
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 241 NVPKQLDRTVTEPGAVVLELDNISCLNNRGQIAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGE 320
Cdd:COG3845 241 EVLLRVEKAPAEPGEVVLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGE 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2681003857 321 NHTISSARDMIRAGVSYVPEDRLGTGLVPGLNAIDNYILKGYDQ----KGWLINWQQALQKTQAAIDAFDIKMANI 392
Cdd:COG3845 321 DITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYRRppfsRGGFLDRKAIRAFAEELIEEFDVRTPGP 396
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-392 |
5.15e-148 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 428.28 E-value: 5.15e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQGIG 84
Cdd:COG1129 3 PLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 85 MVHQHFKLVKSFTVAENIILG--MKDMGLLyDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEI 162
Cdd:COG1129 83 IIHQELNLVPNLSVAENIFLGrePRRGGLI-DWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 163 LILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGSTKTELASEEELTRWMVGRNV 242
Cdd:COG1129 162 LILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGREL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 243 PKQLDRTVTEPGAVVLELDNISCLNnrgqiAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGENH 322
Cdd:COG1129 242 EDLFPKRAAAPGEVVLEVEGLSVGG-----VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2681003857 323 TISSARDMIRAGVSYVPEDRLGTGLVPGLNAIDNYILKGYDQ--KGWLINWQQALQKTQAAIDAFDIKMANI 392
Cdd:COG1129 317 RIRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRlsRGGLLDRRRERALAEEYIKRLRIKTPSP 388
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-391 |
8.56e-96 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 295.30 E-value: 8.56e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYrPD---EGEIYIKGQQVEMLSPKAAVMQ 81
Cdd:PRK13549 4 YLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 82 GIGMVHQHFKLVKSFTVAENIILGMKDM--GLL-YDQRKIEAQieQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFR 158
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLGNEITpgGIMdYDAMYLRAQ--KLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 159 GAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGSTKTELASEEELTRWMV 238
Cdd:PRK13549 161 QARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 239 GRNVPKQLDRTVTEPGAVVLELDNISCL--NNRGQIAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRP-VEDGQK 315
Cdd:PRK13549 241 GRELTALYPREPHTIGEVILEVRNLTAWdpVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEI 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2681003857 316 YVAGENHTISSARDMIRAGVSYVPEDRLGTGLVPGLNAIDNYILKGYDQ--KGWLINWQQALQKTQAAIDAFDIKMAN 391
Cdd:PRK13549 321 FIDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRftGGSRIDDAAELKTILESIQRLKVKTAS 398
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
11-356 |
9.67e-87 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 271.78 E-value: 9.67e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQGIGMVHQHF 90
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAIIYQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 91 KLVKSFTVAENIILGM--KDMGLLyDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEP 168
Cdd:PRK11288 89 HLVPEMTVAENLYLGQlpHKGGIV-NRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 169 TAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGsTKTELA--SEEELTRWMVGRNVPKQL 246
Cdd:PRK11288 168 TSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA-TFDDMAqvDRDQLVQAMVGREIGDIY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 247 DRTVTEPGAVVLELDNISclnnrGQiAVRH-ASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGENHTIS 325
Cdd:PRK11288 247 GYRPRPLGEVRLRLDGLK-----GP-GLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIR 320
|
330 340 350
....*....|....*....|....*....|.
gi 2681003857 326 SARDMIRAGVSYVPEDRLGTGLVPGLNAIDN 356
Cdd:PRK11288 321 SPRDAIRAGIMLCPEDRKAEGIIPVHSVADN 351
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-388 |
3.20e-83 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 262.63 E-value: 3.20e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQGIG 84
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 85 MVHQHFKLVKSFTVAENIILG---MKDMGLLyDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAE 161
Cdd:PRK10762 83 IIHQELNLIPQLTIAENIFLGrefVNRFGRI-DWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 162 ILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGSTKTELASEEELTRWMVGRN 241
Cdd:PRK10762 162 VIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGRK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 242 VPKQLDRTVTEPGAVVLELDNISCLnnrgqiAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGEN 321
Cdd:PRK10762 242 LEDQYPRLDKAPGEVRLKVDNLSGP------GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHE 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 322 HTISSARDMIRAGVSYVPEDRLGTGLVPGLNAIDNYILKGYDQ---KGWLINWQQALQKTQAAIDAFDIK 388
Cdd:PRK10762 316 VVTRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYfsrAGGSLKHADEQQAVSDFIRLFNIK 385
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-347 |
2.20e-80 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 255.36 E-value: 2.20e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 1 MSAIPMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVM 80
Cdd:PRK15439 6 TTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 81 QGIGMVHQHFKLVKSFTVAENIILGM-KDMGllyDQRKIEAQIEQFcnqyGMCIDPAAKVWQLTLGEQQRVEIIKALFRG 159
Cdd:PRK15439 86 LGIYLVPQEPLLFPNLSVKENILFGLpKRQA---SMQKMKQLLAAL----GCQLDLDSSAGSLEVADRQIVEILRGLMRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 160 AEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGSTKTELASEEELTRWMVG 239
Cdd:PRK15439 159 SRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAITP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 240 RNVPKQLD------------RTVTEPGAVVLELDNISclnnrGQiAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGL 307
Cdd:PRK15439 239 AAREKSLSasqklwlelpgnRRQQAAGAPVLTVEDLT-----GE-GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGL 312
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2681003857 308 RPVEDGQkyVAGENHTIS--SARDMIRAGVSYVPEDRLGTGL 347
Cdd:PRK15439 313 RPARGGR--IMLNGKEINalSTAQRLARGLVYLPEDRQSSGL 352
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-388 |
2.31e-78 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 249.65 E-value: 2.31e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 9 MVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQGIGMVHQ 88
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 89 HFKLVKSFTVAENIILGMKDM-GLLYDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDE 167
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYPTkGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 168 PTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGSTKTELASEEELTRWMVGRNVPKQLD 247
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQRFP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 248 RTVTEPGAVVLELDNISCLNnrgQIAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGENHTISSA 327
Cdd:PRK10982 241 DKENKPGEVILEVRNLTSLR---QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNA 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2681003857 328 RDMIRAGVSYVPEDRLGTGLVPGLNAIDNYI---LKGYDQKGWLINWQQALQKTQAAIDAFDIK 388
Cdd:PRK10982 318 NEAINHGFALVTEERRSTGIYAYLDIGFNSLisnIRNYKNKVGLLDNSRMKSDTQWVIDSMRVK 381
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-222 |
2.65e-77 |
|
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: 235.79 E-value: 2.65e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQGIGMV 86
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 87 HqhfklvksftvaeniilgmkdmgllydqrkieaqieqfcnqygmcidpaakvwQLTLGEQQRVEIIKALFRGAEILILD 166
Cdd:cd03216 81 Y-----------------------------------------------------QLSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2681003857 167 EPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGS 222
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-392 |
4.33e-77 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 247.01 E-value: 4.33e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 3 AIPMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQG 82
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 83 IGMVHQHFKLVKSFTVAENIILG----MKDMGL-LYDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALF 157
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIGrhltKKVCGVnIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 158 RGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGSTKTELASEEELTRWM 237
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 238 VGRNV----PKQLDRTVTEPGAVVLELDNISCLNNRgqiAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDG 313
Cdd:PRK09700 242 VGRELqnrfNAMKENVSNLAHETVFEVRNVTSRDRK---KVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 314 QKYVAGENHTISSARDMIRAGVSYVPEDRLGTGLVPGLN-----AIDNYILKGYDQKGW-LINWQQALQKTQAAIDAFDI 387
Cdd:PRK09700 319 EIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSiaqnmAISRSLKDGGYKGAMgLFHEVDEQRTAENQRELLAL 398
|
....*
gi 2681003857 388 KMANI 392
Cdd:PRK09700 399 KCHSV 403
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-348 |
1.10e-73 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 237.77 E-value: 1.10e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 8 QMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYrPD---EGEIYIKGQQVEMLSPKAAVMQGIG 84
Cdd:NF040905 3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKDIRDSEALGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 85 MVHQHFKLVKSFTVAENIILG--MKDMGLLyDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEI 162
Cdd:NF040905 82 IIHQELALIPYLSIAENIFLGneRAKRGVI-DWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 163 LILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGS--TKTELASEEELTRWMVGR 240
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETldCRADEVTEDRIIRGMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 241 NV----PkqlDRTVtEPGAVVLELDNISCLN--NRGQIAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGL---RPVE 311
Cdd:NF040905 241 DLedryP---ERTP-KIGEVVFEVKNWTVYHplHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRsygRNIS 316
|
330 340 350
....*....|....*....|....*....|....*..
gi 2681003857 312 dGQKYVAGENHTISSARDMIRAGVSYVPEDRLGTGLV 348
Cdd:NF040905 317 -GTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLN 352
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-391 |
9.24e-72 |
|
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: 232.79 E-value: 9.24e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYrPD---EGEIYIKGQQVEMLSPKAAVMQG 82
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 83 IGMVHQHFKLVKSFTVAENIILG--MKDMGLLYDQRKIEAQIEQFCNQYGMCIDPAAK-VWQLTLGEQQRVEIIKALFRG 159
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGneITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 160 AEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGSTKTELASEEELTRWMVG 239
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 240 RNVPKQLDRTVTEPGAVVLELDNISCLN--NRGQIAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVE-DGQKY 316
Cdd:TIGR02633 240 REITSLYPHEPHEIGDVILEARNLTCWDviNPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVF 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2681003857 317 VAGENHTISSARDMIRAGVSYVPEDRLGTGLVPGLNAIDNY---ILKGYDQKGwLINWQQALQKTQAAIDAFDIKMAN 391
Cdd:TIGR02633 320 INGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNItlsVLKSFCFKM-RIDAAAELQIIGSAIQRLKVKTAS 396
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
11-218 |
2.38e-54 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 179.49 E-value: 2.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEmlSPKAAVMQGIGMVHQHF 90
Cdd:COG1131 5 GLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA--RDPAEVRRRIGYVPQEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 91 KLVKSFTVAENIILgmkdMGLLY--DQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEP 168
Cdd:COG1131 83 ALYPDLTVRENLRF----FARLYglPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2681003857 169 TAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGR 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
11-218 |
7.30e-51 |
|
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: 170.31 E-value: 7.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQGIGMVHQHF 90
Cdd:cd03219 5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRTFQIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 91 KLVKSFTVAENIILG--------MKDMGLLYDQRKIEAQIEQFCNQYGMcidpaAKVW-----QLTLGEQQRVEIIKALF 157
Cdd:cd03219 85 RLFPELTVLENVMVAaqartgsgLLLARARREEREARERAEELLERVGL-----ADLAdrpagELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2681003857 158 RGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGR 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
11-218 |
9.55e-50 |
|
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: 165.26 E-value: 9.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQqvEMLSPKAAVMQGIGMVHQHF 90
Cdd:cd03230 5 NLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK--DIKKEPEEVKRRIGYLPEEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 91 KLVKSFTVAENIIL--GMKdmgllydqrkieaqieqfcnqygmcidpaakvwqltlgeqQRVEIIKALFRGAEILILDEP 168
Cdd:cd03230 83 SLYENLTVRENLKLsgGMK----------------------------------------QRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2681003857 169 TAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
5-218 |
2.75e-49 |
|
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: 167.14 E-value: 2.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQGIG 84
Cdd:COG0411 3 PLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 85 MVHQHFKLVKSFTVAENIILGM---------KDMGLLYDQRKIEAQIEQ-------FCNQYGMCIDPAAkvwQLTLGEQQ 148
Cdd:COG0411 83 RTFQNPRLFPELTVLENVLVAAharlgrgllAALLRLPRARREEREAREraeelleRVGLADRADEPAG---NLSYGQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2681003857 149 RVEIIKALFRGAEILILDEPTAVLTPQEAKDLYKTLR-LMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRrLRDERGITILLIEHDMDLVMGLADRIVVLDFGR 230
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-220 |
7.53e-47 |
|
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: 160.41 E-value: 7.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAavMQGIGM 85
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA--RRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 86 VHQHFKLVKSFTVAENI-----ILGMKDmgllydqRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGA 160
Cdd:COG4555 79 LPDERGLYDRLTVRENIryfaeLYGLFD-------EELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 161 EILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPA 220
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVV 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-341 |
4.81e-46 |
|
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: 165.08 E-value: 4.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFPG--VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPD---EGEIYIKGQQVEMLSPKAAV 79
Cdd:COG1123 3 PLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 80 mQGIGMVHQHFK--LVKSfTVAENIILGMKDMGLlyDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALF 157
Cdd:COG1123 83 -RRIGMVFQDPMtqLNPV-TVGDQIAEALENLGL--SRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 158 RGAEILILDEPTAVLTPQEAKDLYKTLR-LMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKP--AGSTKTELASEEELT 234
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLReLQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIveDGPPEEILAAPQALA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 235 RwMVGRNVPKQLDRTVTEPGAVVLELDNISC----LNNRGQIAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPV 310
Cdd:COG1123 239 A-VPRLGAARGRAAPAAAAAEPLLEVRNLSKrypvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRP 317
|
330 340 350
....*....|....*....|....*....|...
gi 2681003857 311 EDGQKYVAGENHTISSARDM--IRAGVSYVPED 341
Cdd:COG1123 318 TSGSILFDGKDLTKLSRRSLreLRRRVQMVFQD 350
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
11-218 |
4.23e-44 |
|
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: 151.90 E-value: 4.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAavmQGIGMVHQHF 90
Cdd:cd03259 5 GLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER---RNIGMVFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 91 KLVKSFTVAENIILGMKDMGLlyDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTA 170
Cdd:cd03259 82 ALFPHLTVAENIAFGLKLRGV--PKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2681003857 171 VLTPQEAKDLYKTLR-LMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03259 160 ALDAKLREELREELKeLQRELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
11-235 |
9.58e-44 |
|
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: 151.72 E-value: 9.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFP-GVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKaAVMQGIGMVHQH 89
Cdd:COG1122 5 NLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLR-ELRRKVGLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 90 -----FklvkSFTVAENIILGMKDMGLlyDQRKIEAQIEQFCNQYGMcIDPAAK-VWQLTLGEQQRVEIIKALFRGAEIL 163
Cdd:COG1122 84 pddqlF----APTVEEDVAFGPENLGL--PREEIRERVEEALELVGL-EHLADRpPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2681003857 164 ILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPA--GSTKTELASEEELTR 235
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVadGTPREVFSDYELLEE 230
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-218 |
3.63e-43 |
|
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: 149.54 E-value: 3.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 8 QMVNVTKRFPGVVAN--DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAaVMQGIGM 85
Cdd:cd03225 1 ELKNLSFSYPDGARPalDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE-LRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 86 V-----HQHFKLvksfTVAENIILGMKDMGLlyDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGA 160
Cdd:cd03225 80 VfqnpdDQFFGP----TVEEEVAFGLENLGL--PEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2681003857 161 EILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-218 |
4.92e-42 |
|
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: 147.34 E-value: 4.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFPG----VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKA--AV 79
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 80 MQGIGMVHQHFKLVKSFTVAENIILGMKDMGllYDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRG 159
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAG--VPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 160 AEILILDEPTAVLTPQEAKDLYKTLR-LMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRdINRELGLTIVLITHEMEVVKRICDRVAVMEKGE 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
5-218 |
1.16e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 145.96 E-value: 1.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFP----GVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVM 80
Cdd:COG1136 3 PLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 81 ---QGIGMVHQHFKLVKSFTVAENIILGMKDMGLlyDQRKIEAQIEQFCNQYGM--CIDpaAKVWQLTLGEQQRVEIIKA 155
Cdd:COG1136 83 lrrRHIGFVFQFFNLLPELTALENVALPLLLAGV--SRKERRERARELLERVGLgdRLD--HRPSQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2681003857 156 LFRGAEILILDEPTAVLTPQEAKDLYKTLR-LMAEQGKAVIVISHKLsEVLEGTDKISVLRGGK 218
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTGEEVLELLReLNRELGTTIVMVTHDP-ELAARADRVIRLRDGR 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-218 |
1.19e-41 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 146.74 E-value: 1.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFP-GVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKA--AVMQ 81
Cdd:COG3638 1 PMLELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 82 GIGMVHQHFKLVKSFTVAENIILG-MKDMGLLY---------DQRKIEAQIEQFcnqyGMcidpAAKVWQ----LTLGEQ 147
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLAGrLGRTSTWRsllglfppeDRERALEALERV----GL----ADKAYQradqLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2681003857 148 QRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYKTLRLMA-EQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIArEDGITVVVNLHQVDLARRYADRIIGLRDGR 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-235 |
1.53e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 143.69 E-value: 1.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 1 MSAIPMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKaavm 80
Cdd:COG1121 1 MMMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 81 qgIGMVHQHFKLVKSF--TVAENIILG-MKDMGLLY-----DQRKIEAQIEQFcnqyGMciDPAAK--VWQLTLGEQQRV 150
Cdd:COG1121 77 --IGYVPQRAEVDWDFpiTVRDVVLMGrYGRRGLFRrpsraDREAVDEALERV----GL--EDLADrpIGELSGGQQQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 151 EIIKALFRGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGSTKTELASE 230
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLTP 228
|
....*
gi 2681003857 231 EELTR 235
Cdd:COG1121 229 ENLSR 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-218 |
1.55e-40 |
|
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: 143.01 E-value: 1.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPG----VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPK---AAV 79
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 80 MQGIGMVHQHFKLVKSFTVAENIILGMKDMGLLYDQRKieAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRG 159
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERR--ERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 160 AEILILDEPTAVLTPQEAKDLYKTLRLMAEQ-GKAVIVISHKLsEVLEGTDKISVLRGGK 218
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDP-ELAEYADRIIELRDGK 217
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-170 |
2.97e-40 |
|
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: 140.09 E-value: 2.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKaAVMQGIGMVHQHFKLVKSFTVAENI 102
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERK-SLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2681003857 103 ILGMKDMGLlyDQRKIEAQIEQFCNQYGMcIDPAAKVW-----QLTLGEQQRVEIIKALFRGAEILILDEPTA 170
Cdd:pfam00005 81 RLGLLLKGL--SKREKDARAEEALEKLGL-GDLADRPVgerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-218 |
3.26e-39 |
|
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: 139.27 E-value: 3.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVmqgIGMV 86
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR---IGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 87 HQHFKLVKSFTVAENIILGMKDMGLLYdqrkieAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILD 166
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGIRK------KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2681003857 167 EPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-220 |
7.73e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 139.84 E-value: 7.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 1 MSAI-PMVQMVNVTKRFP----GVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSP 75
Cdd:COG1116 1 MSAAaPALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 76 KaavmqgIGMVHQHFKLVKSFTVAENIILGMKDMGLLYDQRKieAQIEQFCNQYGMciDPAAKVW--QLTLGEQQRVEII 153
Cdd:COG1116 81 D------RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERR--ERARELLELVGL--AGFEDAYphQLSGGMRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2681003857 154 KALFRGAEILILDEPTA---VLTPQEAKDLykTLRLMAEQGKAVIVISHKLSE-VLEGtDKISVLRGGkPA 220
Cdd:COG1116 151 RALANDPEVLLMDEPFGaldALTRERLQDE--LLRLWQETGKTVLFVTHDVDEaVFLA-DRVVVLSAR-PG 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-239 |
8.69e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 145.16 E-value: 8.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 17 PGVVANdhVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQGIGMV---HQHFKLV 93
Cdd:COG1129 265 GGVVRD--VSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIAYVpedRKGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 94 KSFTVAENIILG----MKDMGLLyDQRKIEAQIEQFCNQYGM-CIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEP 168
Cdd:COG1129 343 LDLSIRENITLAsldrLSRGGLL-DRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2681003857 169 TA---VltpqEAK-DLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGSTKTELASEEELTRWMVG 239
Cdd:COG1129 422 TRgidV----GAKaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEATEEAIMAAATG 492
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-218 |
1.75e-38 |
|
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: 135.45 E-value: 1.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 8 QMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKaAVMQGIGMVH 87
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE-ELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 88 qhfklvksftvaeniilgmkdmgllydqrkieaqieqfcnqygmcidpaakvwQLTLGEQQRVEIIKALFRGAEILILDE 167
Cdd:cd00267 80 -----------------------------------------------------QLSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2681003857 168 PTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-199 |
2.15e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 137.49 E-value: 2.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFP-GVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPK--AAVMQG 82
Cdd:COG2884 1 MIRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReiPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 83 IGMVHQHFKLVKSFTVAENIILGMKDMGllYDQRKIEAQIEQFCNQYGMcidpAAKVW----QLTLGEQQRVEIIKALFR 158
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTG--KSRKEIRRRVREVLDLVGL----SDKAKalphELSGGEQQRVAIARALVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2681003857 159 GAEILILDEPTAVLTPQEAKDLyktLRLMAE---QGKAVIVISH 199
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEI---MELLEEinrRGTTVLIATH 195
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-218 |
2.89e-38 |
|
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: 135.78 E-value: 2.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVM-QGIGM 85
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLrRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 86 VHQHFKLVKSFTVAENIILGmkdmgllydqrkieaqieqfcnqygmcidpaakvwqLTLGEQQRVEIIKALFRGAEILIL 165
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG------------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2681003857 166 DEPTAVLTPQEAKDLYKTLR-LMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03229 125 DEPTSALDPITRREVRALLKsLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
11-214 |
8.74e-38 |
|
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: 135.35 E-value: 8.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKaavmqgIGMVHQHF 90
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR------IGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 91 KLVKSF--TVAENIILG-MKDMGLLY-----DQRKIEA-----QIEQFCNQygmcidpaaKVWQLTLGEQQRVEIIKALF 157
Cdd:cd03235 78 SIDRDFpiSVRDVVLMGlYGHKGLFRrlskaDKAKVDEalervGLSELADR---------QIGELSGGQQQRVLLARALV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2681003857 158 RGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVL 214
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-218 |
9.52e-38 |
|
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: 142.35 E-value: 9.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFP-----GVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKA-- 77
Cdd:COG1123 259 PLLEVRNLSKRYPvrgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlr 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 78 AVMQGIGMVHQH-FK-LVKSFTVAENIILGMKDMGLLyDQRKIEAQIEQFCNQYGMciDPAAK---VWQLTLGEQQRVEI 152
Cdd:COG1123 339 ELRRRVQMVFQDpYSsLNPRMTVGDIIAEPLRLHGLL-SRAERRERVAELLERVGL--PPDLAdryPHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2681003857 153 IKALFRGAEILILDEPTA---------VLtpqeakDLYKTLRlmAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:COG1123 416 ARALALEPKLLILDEPTSaldvsvqaqIL------NLLRDLQ--RELGLTYLFISHDLAVVRYIADRVAVMYDGR 482
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-218 |
1.99e-37 |
|
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: 133.28 E-value: 1.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPGVVAN--DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPkAAVMQGIGMVHQ 88
Cdd:cd03228 5 NVSFSYPGRPKPvlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDL-ESLRKNIAYVPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 89 HFKLVkSFTVAENIILGmkdmgllydqrkieaqieqfcnqygmcidpaakvwqltlGEQQRVEIIKALFRGAEILILDEP 168
Cdd:cd03228 84 DPFLF-SGTIRENILSG---------------------------------------GQRQRIAIARALLRDPPILILDEA 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2681003857 169 TAVLTPQEAKDLYKTLRLMAeQGKAVIVISHKLSEVLEGtDKISVLRGGK 218
Cdd:cd03228 124 TSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-218 |
2.30e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 137.90 E-value: 2.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFPG----VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKA--AV 79
Cdd:COG1135 1 MIELENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElrAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 80 MQGIGMVHQHFKLVKSFTVAENIILGMKDMGllYDQRKIEAQIEQ---------FCNQYgmcidPAakvwQLTLGEQQRV 150
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAG--VPKAEIRKRVAEllelvglsdKADAY-----PS----QLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2681003857 151 EIIKALFRGAEILILDEPTAVLTPQEAK---DLYKTLRlmAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRsilDLLKDIN--RELGLTIVLITHEMDVVRRICDRVAVLENGR 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
11-218 |
2.68e-37 |
|
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: 135.00 E-value: 2.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFP-GVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKA--AVMQGIGMVH 87
Cdd:cd03256 5 NLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrQLRRQIGMIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 88 QHFKLVKSFTVAENIILGMKD--------MGLLYDQRKIEAQieQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRG 159
Cdd:cd03256 85 QQFNLIERLSVLENVLSGRLGrrstwrslFGLFPKEEKQRAL--AALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 160 AEILILDEPTAVLTPQEAKDLYKTLR-LMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03256 163 PKLILADEPVASLDPASSRQVMDLLKrINREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-220 |
3.10e-36 |
|
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: 131.44 E-value: 3.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPG----VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKaavmqg 82
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 83 IGMVHQHFKLVKSFTVAENIILGMKDMGLLYDQRKIEAQ-------IEQFCNQYgmcidPaakvWQLTLGEQQRVEIIKA 155
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEellelvgLSGFENAY-----P----HQLSGGMRQRVALARA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2681003857 156 LFRGAEILILDEPTAVLTPQEAKDLYKTL-RLMAEQGKAVIVISHKLSEVLEGTDKISVLrGGKPA 220
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTREQLQEELlDIWRETGKTVLLVTHDIDEAVFLADRVVVL-SARPG 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-218 |
3.67e-36 |
|
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: 132.08 E-value: 3.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAavmQGIGMV 86
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE---RNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 87 HQHFKLVKSFTVAENIILG--MKDMGLLYDQRKIEA---------QIEQFCNQYgmcidPAakvwQLTLGEQQRVEIIKA 155
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGlrVKPRSERPPEAEIRAkvhellklvQLDWLADRY-----PA----QLSGGQRQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2681003857 156 LFRGAEILILDEPTAVLTPQEAKDLYKTLR-LMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRrLHDELHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-218 |
6.32e-36 |
|
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: 130.48 E-value: 6.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEmlspkAAVMQGIGMV 86
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-----IAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 87 HQHFKLVKSFTVAENII-LG-MKDMGLlydqRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILI 164
Cdd:cd03269 76 PEERGLYPKMKVIDQLVyLAqLKGLKK----EEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2681003857 165 LDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
254-359 |
1.88e-35 |
|
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: 128.32 E-value: 1.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 254 GAVVLELDNISclnnrGQIAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGENHTISSARDMIRA 333
Cdd:cd03215 1 GEPVLEVRGLS-----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRA 75
|
90 100
....*....|....*....|....*.
gi 2681003857 334 GVSYVPEDRLGTGLVPGLNAIDNYIL 359
Cdd:cd03215 76 GIAYVPEDRKREGLVLDLSVAENIAL 101
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-218 |
2.97e-35 |
|
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: 130.16 E-value: 2.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQgIGM 85
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 86 VHQHFKLVKSFTVAENIILG----MKDMGLL--YDQRKIEA-----QIEQFCNQYgmcidpaakVWQLTLGEQQRVEIIK 154
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGryphLGLFGRPsaEDREAVEEalertGLEHLADRP---------VDELSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2681003857 155 ALFRGAEILILDEPTAVLtpqeakDLYKTLRLM-------AEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHL------DLAHQLEVLellrrlaRERGRTVVMVLHDLNLAARYADRLVLLKDGR 215
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
6-202 |
4.54e-35 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 128.52 E-value: 4.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFP-GVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPK--AAVMQG 82
Cdd:TIGR02673 1 MIEFHNVSKAYPgGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRqlPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 83 IGMVHQHFKLVKSFTVAENIILGMKDMGLlyDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEI 162
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGK--KEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2681003857 163 LILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLS 202
Cdd:TIGR02673 159 LLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLS 198
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-218 |
5.89e-35 |
|
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: 128.14 E-value: 5.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAavmQGIGMV 86
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD---RDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 87 HQHFKLVKSFTVAENIILGMKDMGllYDQRKIEA---------QIEQFCNQYgmcidPAakvwQLTLGEQQRVEIIKALF 157
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRK--VPKDEIDErvrevaellQIEHLLDRK-----PK----QLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2681003857 158 RGAEILILDEPtavLTPQEAKDLYKTL----RLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03301 147 REPKVFLMDEP---LSNLDAKLRVQMRaelkRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-218 |
6.00e-35 |
|
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: 128.77 E-value: 6.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKA--AVMQGIG 84
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 85 MVHQHFKLVKSFTVAENIILGMKDMGLLyDQRKIEAQIEQFCNQYGmcIDPAAKVW--QLTLGEQQRVEIIKALFRGAEI 162
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRL-SEEEIREIVLEKLEAVG--LRGAEDLYpaELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2681003857 163 LILDEPTAVLTPQEAK---DLYKTLRlmAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03261 158 LLYDEPTAGLDPIASGvidDLIRSLK--KELGLTSIMVTHDLDTAFAIADRIAVLYDGK 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-218 |
8.78e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 131.04 E-value: 8.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 1 MSaipmVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVE-MLSPKAav 79
Cdd:COG1118 1 MS----IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRE-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 80 mQGIGMVHQHFKLVKSFTVAENIILGMKDMGLlyDQRKIEA---------QIEQFCNQYgmcidPAakvwQLTLGEQQRV 150
Cdd:COG1118 75 -RRVGFVFQHYALFPHMTVAENIAFGLRVRPP--SKAEIRArveellelvQLEGLADRY-----PS----QLSGGQRQRV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2681003857 151 EIIKALFRGAEILILDEPTAVLTPQEAKDLYKTLR-LMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRrLHDELGGTTVFVTHDQEEALELADRVVVMNQGR 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-218 |
1.46e-34 |
|
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: 135.35 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPGVVAN--DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPkAAVMQGIG 84
Cdd:COG2274 474 IELENVSFRYPGDSPPvlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDP-ASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 85 MVHQHFKLvksF--TVAENIILGMKDMgllyDQRKIE-----AQIEQFCNQ----YGMCIDPAAKvwQLTLGEQQRVEII 153
Cdd:COG2274 553 VVLQDVFL---FsgTIRENITLGDPDA----TDEEIIeaarlAGLHDFIEAlpmgYDTVVGEGGS--NLSGGQRQRLAIA 623
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2681003857 154 KALFRGAEILILDEPTAVLTPQEAKDLYKTLRLMAeQGKAVIVISHKLSeVLEGTDKISVLRGGK 218
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLS-TIRLADRIIVLDKGR 686
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
5-235 |
3.95e-34 |
|
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: 126.63 E-value: 3.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKA--AVMQG 82
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 83 IGMVHQHFKLVKSFTVAENIILGMKdMGLLYDQRKIEAQI---------EQFCNQYgmcidPAakvwQLTLGEQQRVEII 153
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLR-EHTDLSEAEIRELVleklelvglPGAADKM-----PS----ELSGGMRKRVALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 154 KALfrgA---EILILDEPTAVLTPQEAKDLYKTLR-LMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPA--GSTKTEL 227
Cdd:COG1127 154 RAL---AldpEILLYDEPTAGLDPITSAVIDELIReLRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIaeGTPEELL 230
|
....*...
gi 2681003857 228 ASEEELTR 235
Cdd:COG1127 231 ASDDPWVR 238
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-218 |
5.77e-34 |
|
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: 125.70 E-value: 5.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPG--VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQqvEMLSPKAAVMQGIG 84
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY--SIRTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 85 MVHQHFKLVKSFTVAENIILgmkdMGLL--YDQRKIEAQIEQFCNQYGM--CIDPAAKvwQLTLGEQQRVEIIKALFRGA 160
Cdd:cd03263 79 YCPQFDALFDELTVREHLRF----YARLkgLPKSEIKEEVELLLRVLGLtdKANKRAR--TLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2681003857 161 EILILDEPTAVLTPQEAKDLYKTLRLMAeQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-218 |
7.40e-34 |
|
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: 124.08 E-value: 7.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTkrFPGVVANdhVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQGIG 84
Cdd:cd03215 3 PVLEVRGLS--VKGAVRD--VSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 85 MV---HQHFKLVKSFTVAENIILGmkdmgllydqrkieaqieqfcnqygmcidpaakvWQLTLGEQQRVEIIKALFRGAE 161
Cdd:cd03215 79 YVpedRKREGLVLDLSVAENIALS----------------------------------SLLSGGNQQKVVLARWLARDPR 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2681003857 162 ILILDEPTA---VltpqEAK-DLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03215 125 VLILDEPTRgvdV----GAKaEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-218 |
7.44e-34 |
|
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: 125.17 E-value: 7.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRF----PGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGqqVEMLSPKAAVMQ 81
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 82 GIGMVHQHFKLVKSFTVAENIILGMKDMGLLYDQrkIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAE 161
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDE--LTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2681003857 162 ILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGR 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-218 |
9.34e-34 |
|
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: 124.61 E-value: 9.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPGVVANDHVSLTIEAGqIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVemLSPKAAVMQGIGMV 86
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV--LKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 87 HQHFKLVKSFTVAE--NIILGMKDMgllyDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILI 164
Cdd:cd03264 78 PQEFGVYPNFTVREflDYIAWLKGI----PSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2681003857 165 LDEPTAVLTPQEAkdlYKTLRLMAEQGKAVIVI--SHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03264 154 VDEPTAGLDPEER---IRFRNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGK 206
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-218 |
2.11e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 127.52 E-value: 2.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 1 MSAiPMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAavm 80
Cdd:COG3842 1 MAM-PALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 81 QGIGMVHQHFKLvksF---TVAENIILGMKDMGLlyDQRKIEAQIEQFCNQYGMciDPAA--KVWQLTLGEQQRVEIIKA 155
Cdd:COG3842 77 RNVGMVFQDYAL---FphlTVAENVAFGLRMRGV--PKAEIRARVAELLELVGL--EGLAdrYPHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2681003857 156 LFRGAEILILDEPTAVLTPQEAKDLYKTLR-LMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRrLQRELGITFIYVTHDQEEALALADRIAVMNDGR 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-218 |
3.56e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 125.61 E-value: 3.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVemlspKAAVMQGIGM 85
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-----DPEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 86 VHQHFKLVKSFTVAENII-LGM-KDMGLLYDQRKIEAQIEQFcnqyGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEIL 163
Cdd:COG4152 76 LPEERGLYPKMKVGEQLVyLARlKGLSKAEAKRRADEWLERL----GLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2681003857 164 ILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGR 206
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-218 |
5.08e-33 |
|
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: 123.42 E-value: 5.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 9 MVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQGIGMVHQ 88
Cdd:cd03218 3 AENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 89 HFKLVKSFTVAENIILGMKDMGLLYDQR--KIEAQIEQFcnqygmCIDPAAKVWQLTL--GEQQRVEIIKALFRGAEILI 164
Cdd:cd03218 83 EASIFRKLTVEENILAVLEIRGLSKKEReeKLEELLEEF------HITHLRKSKASSLsgGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2681003857 165 LDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGK 210
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-219 |
9.82e-33 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 123.18 E-value: 9.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 1 MSAiPMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVM 80
Cdd:PRK11300 1 MSQ-PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 81 QGIGMVHQHFKLVKSFTVAENIILGMK---DMGLLYDQRKIEAqieqFCNQYGMCIDPAAkVW---------------QL 142
Cdd:PRK11300 80 MGVVRTFQHVRLFREMTVIENLLVAQHqqlKTGLFSGLLKTPA----FRRAESEALDRAA-TWlervgllehanrqagNL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2681003857 143 TLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYKTL-RLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKP 219
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIaELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTP 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-317 |
1.49e-32 |
|
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: 128.00 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGL--YRPDEGEI-----------YI------------ 65
Cdd:TIGR03269 5 NLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgYVerpskvgepcpv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 66 -----KGQQVEMLSP----KAAVMQGIG-MVHQHFKLVKSFTVAENIILGMKDMGLLYD---QRKIEAqIEQFcnQYGMC 132
Cdd:TIGR03269 85 cggtlEPEEVDFWNLsdklRRRIRKRIAiMLQRTFALYGDDTVLDNVLEALEEIGYEGKeavGRAVDL-IEMV--QLSHR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 133 IDPAAKvwQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEG-TDKI 211
Cdd:TIGR03269 162 ITHIAR--DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDlSDKA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 212 SVLRGgkpaGSTKTELASEEELTRWMVGRNVPKQldRTVTEPGAVVLELDNIS---CLNNRGQI-AVRHASLCIRAGEIV 287
Cdd:TIGR03269 240 IWLEN----GEIKEEGTPDEVVAVFMEGVSEVEK--ECEVEVGEPIIKVRNVSkryISVDRGVVkAVDNVSLEVKEGEIF 313
|
330 340 350
....*....|....*....|....*....|
gi 2681003857 288 GIAGVAGNGQTELAEVVAGLRPVEDGQKYV 317
Cdd:TIGR03269 314 GIVGTSGAGKTTLSKIIAGVLEPTSGEVNV 343
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-199 |
1.50e-32 |
|
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: 121.43 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEmlSPKAAVMQGIG 84
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR--DAREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 85 MVHQHFKLVKSFTVAENIILGMKDMGLLYDQRKIEAQIEQFcnqyGM--CID-PAAkvwQLTLGEQQRVEIIKALFRGAE 161
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAV----GLagLADlPVR---QLSAGQKRRVALARLLLSPAP 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 2681003857 162 ILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISH 199
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
12-218 |
3.41e-32 |
|
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: 122.37 E-value: 3.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 12 VTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKA--AVM-QGIGMVHQ 88
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrELRrKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 89 HFKLVKSFTVAENIILGMKDMGLLYDQRkiEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEP 168
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAER--EERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2681003857 169 TAVLTPQEAKDLYKT-LRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03294 188 FSALDPLIRREMQDElLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGR 238
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
9-211 |
3.62e-32 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 120.41 E-value: 3.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 9 MVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEML-SPKAAVMQ--GIGM 85
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLnSKKASKFRreKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 86 VHQHFKLVKSFTVAENIILGMKDMGLlyDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILIL 165
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKL--SKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2681003857 166 DEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLsEVLEGTDKI 211
Cdd:TIGR03608 159 DEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDP-EVAKQADRV 203
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
11-218 |
6.01e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 119.92 E-value: 6.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQgIGMVHQHF 90
Cdd:COG4619 5 GLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQ-VAYVPQEP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 91 KLVKSfTVAENIILGMKDMGLLYDQRKIEAQIEQFCnqygmcIDPAAKVWQ---LTLGEQQRVEIIKALFRGAEILILDE 167
Cdd:COG4619 84 ALWGG-TVRDNLPFPFQLRERKFDRERALELLERLG------LPPDILDKPverLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2681003857 168 PTAVLTPqEAKDLYKTL--RLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:COG4619 157 PTSALDP-ENTRRVEELlrEYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
23-218 |
1.01e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 126.43 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPkAAVMQGIGMVHQHFKLVkSFTVAENI 102
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTL-ESLRRQIGVVPQDTFLF-SGTIRENI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 103 ILGMKDmgllYDQRKIE-----AQ----IEQFCNQYGMCIDPAAKvwQLTLGEQQRVEIIKALFRGAEILILDEPTAVLT 173
Cdd:COG1132 435 RYGRPD----ATDEEVEeaakaAQahefIEALPDGYDTVVGERGV--NLSGGQRQRIAIARALLKDPPILILDEATSALD 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2681003857 174 PQEAKDLYKTL-RLMaeQGKAVIVISHKLSEVlEGTDKISVLRGGK 218
Cdd:COG1132 509 TETEALIQEALeRLM--KGRTTIVIAHRLSTI-RNADRILVLDDGR 551
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-218 |
1.50e-31 |
|
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: 119.53 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFPG----VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQ 81
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 82 G--IGMVHQH--FKLVKSFTVAENIILGMKDMGLLYDQRKIEAQI----------EQFCNQYgmcidPAakvwQLTLGEQ 147
Cdd:cd03257 81 RkeIQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVllllvgvglpEEVLNRY-----PH----ELSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2681003857 148 QRVEIIKALFRGAEILILDEPTA---VLTPQEAKDLYKTLRlmAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSaldVSVQAQILDLLKKLQ--EELGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-218 |
1.77e-31 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 119.71 E-value: 1.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFP-GVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKA--AVMQG 82
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 83 IGMVHQHFKLVKSFTVAENII---LGMKD-----MGLLYDQRKIEAQieQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIK 154
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLhgrLGYKPtwrslLGRFSEEDKERAL--SALERVGLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2681003857 155 ALFRGAEILILDEPTAVLTPQEAKDLYKTL-RLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLkRINKEDGITVIINLHQVDLAKKYADRIVGLKAGE 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-239 |
1.82e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 124.75 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 18 GVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQGIGMVH---QHFKLVK 94
Cdd:COG3845 270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAYIPedrLGRGLVP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 95 SFTVAENIILG------MKDMGLLyDQRKIEAQIEQFCNQYG-MCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDE 167
Cdd:COG3845 350 DMSVAENLILGryrrppFSRGGFL-DRKAIRAFAEELIEEFDvRTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2681003857 168 PTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGSTKTELASEEELTRWMVG 239
Cdd:COG3845 429 PTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEATREEIGLLMAG 500
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
25-218 |
2.37e-31 |
|
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: 118.69 E-value: 2.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQGIGMVHQHFKLVKSFTVAENIIL 104
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVPEGRRIFPELTVEENLLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 105 GmkdmGLLYDQRKIEAQIE----------QFCNQygmcidpaaKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTP 174
Cdd:cd03224 99 G----AYARRRAKRKARLErvyelfprlkERRKQ---------LAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2681003857 175 QEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03224 166 KIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-218 |
2.59e-31 |
|
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: 118.88 E-value: 2.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAavmQGIGMV 86
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK---RPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 87 HQHFKLVKSFTVAENIILGMKDMGLlyDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILD 166
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKL--PKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2681003857 167 EPTAVLTPQEAKDLYKTL-RLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03300 156 EPLGALDLKLRKDMQLELkRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGK 208
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-218 |
8.67e-31 |
|
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: 116.86 E-value: 8.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVemLSPKAAVM---QGI 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL--TDDKKNINelrQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 84 GMVHQHFKLVKSFTVAENIILG-MKDMGLlyDQRKIEAQIEQFCNQYGMciDPAAKVW--QLTLGEQQRVEIIKALFRGA 160
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLApIKVKGM--SKAEAEERALELLEKVGL--ADKADAYpaQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2681003857 161 EILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-231 |
1.25e-30 |
|
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: 122.94 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 2 SAIPMVQMVNVTKRFP-GVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPkAAVM 80
Cdd:COG4988 332 AGPPSIELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDP-ASWR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 81 QGIGMVHQHFKLVKSfTVAENIILGMKDMGllydqrkiEAQIEQFCNQygmcidpaAKVWQLT----------LGEQ--- 147
Cdd:COG4988 411 RQIAWVPQNPYLFAG-TIRENLRLGRPDAS--------DEELEAALEA--------AGLDEFVaalpdgldtpLGEGgrg 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 148 ------QRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYKTLRLMAeQGKAVIVISHKLSeVLEGTDKISVLRGGKPAG 221
Cdd:COG4988 474 lsggqaQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLA-LLAQADRILVLDDGRIVE 551
|
250
....*....|.
gi 2681003857 222 S-TKTELASEE 231
Cdd:COG4988 552 QgTHEELLAKN 562
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
11-218 |
1.79e-30 |
|
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: 114.84 E-value: 1.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKaAVMQGIGMVHQhf 90
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPK-ELARKIAYVPQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 91 klvksftvaeniilGMKDMGllydqrkieaqIEQFCNQYgmcidpaakVWQLTLGEQQRVEIIKALFRGAEILILDEPTA 170
Cdd:cd03214 81 --------------ALELLG-----------LAHLADRP---------FNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2681003857 171 VLTPQEAKDLYKTLR-LMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03214 127 HLDIAHQIELLELLRrLARERGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-218 |
1.94e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 119.17 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEmlSPKAAVMQGIGMV 86
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP--ARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 87 HQHFKLVKSFTVAENIILGMKDMGLlyDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILD 166
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVFGRYFGM--STREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2681003857 167 EPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-218 |
2.77e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 119.02 E-value: 2.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAavmQGIGM 85
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---RNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 86 VHQHFKLVKSFTVAENIILGMKDMGLlyDQRKIEAQIEQfcnqygmcidpAAKVWQLT---------L--GEQQRVEIIK 154
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRKV--PKAEIDRRVRE-----------AAELLGLEdlldrkpkqLsgGQRQRVALGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2681003857 155 ALFRGAEILILDEPTAVLtpqEAKdlyktLR---------LMAEQGKAVIVISHKLSEVLegT--DKISVLRGGK 218
Cdd:COG3839 147 ALVREPKVFLLDEPLSNL---DAK-----LRvemraeikrLHRRLGTTTIYVTHDQVEAM--TlaDRIAVMNDGR 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
11-218 |
5.51e-30 |
|
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: 114.99 E-value: 5.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPG--VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPkAAVMQGIGMVHQ 88
Cdd:cd03245 7 NVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDP-ADLRRNIGYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 89 HFKLVKSfTVAENIILGmkdMGLLYDQRKIEAQ----IEQFCNQY--GMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEI 162
Cdd:cd03245 86 DVTLFYG-TLRDNITLG---APLADDERILRAAelagVTDFVNKHpnGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2681003857 163 LILDEPTAVLTPQEAKDLYKTLRLMAEqGKAVIVISHKLSeVLEGTDKISVLRGGK 218
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPS-LLDLVDRIIVMDSGR 215
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-218 |
8.22e-30 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 117.59 E-value: 8.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFPG----VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKA--AV 79
Cdd:PRK11153 1 MIELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 80 MQGIGMVHQHFKLVKSFTVAENIILGMKDMGLlyDQRKIEAQIEQFC---------NQYgmcidPAakvwQLTLGEQQRV 150
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGT--PKAEIKARVTELLelvglsdkaDRY-----PA----QLSGGQKQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2681003857 151 EIIKALFRGAEILILDEPTAVLTPQEAKDLYKTLR-LMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKdINRELGLTIVLITHEMDVVKRICDRVAVIDAGR 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-218 |
1.20e-29 |
|
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: 114.04 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFP-GVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAA--VMQGI 83
Cdd:cd03292 1 IEFINVTKTYPnGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIpyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 84 GMVHQHFKLVKSFTVAENIILGMKDMGllYDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEIL 163
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTG--VPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2681003857 164 ILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-218 |
1.62e-29 |
|
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: 114.52 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFP----GVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAvMQ 81
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAF-RR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 82 GIGMVHQHFKLvkSF----TVAENIILGMKDMGLlydqRKIEAQIEQFCNQYGMCID-----PAakvwQLTLGEQQRVEI 152
Cdd:COG1124 80 RVQMVFQDPYA--SLhprhTVDRILAEPLRIHGL----PDREERIAELLEQVGLPPSfldryPH----QLSGGQRQRVAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2681003857 153 IKALFRGAEILILDEPTA---VLTPQEAKDLYKTLRlmAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:COG1124 150 ARALILEPELLLLDEPTSaldVSVQAEILNLLKDLR--EERGLTYLFVSHDLAVVAHLCDRVAVMQNGR 216
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-236 |
8.12e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 112.90 E-value: 8.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKA-----AVM 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElarrrAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 81 QgigmvhQHFKLVKSFTVAENIILGMkdMGLLYDQRKIEAQIEQfcnqygmCIDpAAKVWQL------TL--GEQQRVEI 152
Cdd:COG4559 81 P------QHSSLAFPFTVEEVVALGR--APHGSSAAQDRQIVRE-------ALA-LVGLAHLagrsyqTLsgGEQQRVQL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 153 IKAL-------FRGAEILILDEPTAVLtpqeakDLY---KTLRL---MAEQGKAVIVISHKLSEVLEGTDKISVLRGGKP 219
Cdd:COG4559 145 ARVLaqlwepvDGGPRWLFLDEPTSAL------DLAhqhAVLRLarqLARRGGGVVAVLHDLNLAAQYADRILLLHQGRL 218
|
250
....*....|....*...
gi 2681003857 220 AGS-TKTELASEEELTRW 236
Cdd:COG4559 219 VAQgTPEEVLTDELLERV 236
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
25-235 |
1.38e-28 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 111.61 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQGIGMVHQHFKLVKSFTVAENIIL 104
Cdd:COG0410 22 VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYVPEGRRIFPSLTVEENLLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 105 GMKdmgLLYDQRKIEAQIEQ----FcnqygmcidP--AAKVWQL--TL--GEQQRVEIIKALFRGAEILILDEPTAVLTP 174
Cdd:COG0410 102 GAY---ARRDRAEVRADLERvyelF---------PrlKERRRQRagTLsgGEQQMLAIGRALMSRPKLLLLDEPSLGLAP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2681003857 175 QEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGS-TKTELASEEELTR 235
Cdd:COG0410 170 LIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEgTAAELLADPEVRE 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
23-218 |
1.88e-28 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 110.42 E-value: 1.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQV---EMLSPKAAVMQGIGmvHQHFklvkSFTVA 99
Cdd:cd03226 17 DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkakERRKSIGYVMQDVD--YQLF----TDSVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 100 ENIILGMKDMGLlyDQRKIEAQIEQFCNQYGMCIDPaakvWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKD 179
Cdd:cd03226 91 EELLLGLKELDA--GNEQAETVLKDLDLYALKERHP----LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMER 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 2681003857 180 LYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03226 165 VGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
25-218 |
2.91e-28 |
|
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: 110.39 E-value: 2.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLsPKAAVMQGIGMVHQHFKLVkSFTVAENIIL 104
Cdd:cd03254 22 INFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI-SRKSLRSMIGVVLQDTFLF-SGTIMENIRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 105 G-----MKDMGLLYDQRKIEAQIEQFCNQYGMCIDPAAKVwqLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKD 179
Cdd:cd03254 100 GrpnatDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGN--LSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2681003857 180 LYKTL-RLMaeQGKAVIVISHKLSEVLEgTDKISVLRGGK 218
Cdd:cd03254 178 IQEALeKLM--KGRTSIIIAHRLSTIKN-ADKILVLDDGK 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
25-218 |
4.18e-28 |
|
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: 110.50 E-value: 4.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKaavMQGIGMVHQHFKLVKSFTVAENIIL 104
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE---KRDISYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 105 GMKDmgLLYDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYKTL 184
Cdd:cd03299 95 GLKK--RKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREEL 172
|
170 180 190
....*....|....*....|....*....|....*
gi 2681003857 185 -RLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03299 173 kKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGK 207
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-214 |
4.47e-28 |
|
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: 115.46 E-value: 4.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 4 IPMVQMVNVTKRFPGV-VANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPkAAVMQG 82
Cdd:TIGR02857 319 ASSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA-DSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 83 IGMVHQHFKLVKSfTVAENIILGMKDMGllydqrkiEAQIEQFCNQYGM--CIDPAAKVWQ---------LTLGEQQRVE 151
Cdd:TIGR02857 398 IAWVPQHPFLFAG-TIAENIRLARPDAS--------DAEIREALERAGLdeFVAALPQGLDtpigeggagLSGGQAQRLA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2681003857 152 IIKALFRGAEILILDEPTAVLTPQEAKDLYKTLRLMAeQGKAVIVISHKLsEVLEGTDKISVL 214
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRL-ALAALADRIVVL 529
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
11-218 |
5.53e-28 |
|
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: 110.08 E-value: 5.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPGV-VANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPkAAVMQGIGMVHQH 89
Cdd:cd03295 5 NVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP-VELRRKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 90 FKLVKSFTVAENIILGMKDMGllYDQRKIEAQIEQFCNQYGMciDPAAKV----WQLTLGEQQRVEIIKALFRGAEILIL 165
Cdd:cd03295 84 IGLFPHMTVEENIALVPKLLK--WPKEKIRERADELLALVGL--DPAEFAdrypHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2681003857 166 DEPTAVLTPQEAKDLYKT-LRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03295 160 DEPFGALDPITRDQLQEEfKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGE 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-236 |
5.83e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 110.63 E-value: 5.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKA-----AV 79
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElarrrAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 80 MQgigmvhQHFKLVKSFTVAENIILGMKDMGLLYDQRK--IEAQIEQfcnqygmcidpaAKVWQL------TL--GEQQR 149
Cdd:PRK13548 81 LP------QHSSLSFPFTVEEVVAMGRAPHGLSRAEDDalVAAALAQ------------VDLAHLagrdypQLsgGEQQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 150 VEIIKALFRGAE------ILILDEPTAVLtpqeakDLY---KTLRLM----AEQGKAVIVISHKLSEVLEGTDKISVLRG 216
Cdd:PRK13548 143 VQLARVLAQLWEpdgpprWLLLDEPTSAL------DLAhqhHVLRLArqlaHERGLAVIVVLHDLNLAARYADRIVLLHQ 216
|
250 260
....*....|....*....|.
gi 2681003857 217 GKP-AGSTKTELASEEELTRW 236
Cdd:PRK13548 217 GRLvADGTPAEVLTPETLRRV 237
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-199 |
1.03e-27 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 109.31 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEmLSPK--AAVMQGI 83
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKdiNKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 84 GMVHQHFKLVKSFTVAENIILG-MKDMGLLYDQRKIEAQ-------IEQFCNQYgmcidPAakvwQLTLGEQQRVEIIKA 155
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLApIKVKKMSKAEAEERAMellervgLADKADAY-----PA----QLSGGQQQRVAIARA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2681003857 156 LFRGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISH 199
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTH 194
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-227 |
1.46e-26 |
|
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: 105.91 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVemLSPKAAVMQGIGMVHQHF 90
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV--VREPREVRRRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 91 KLVKSFTVAENIILGMKDMGLLYDQRKieAQIEQFCNQYGMcIDPAAK-VWQLTLGEQQRVEIIKALFRGAEILILDEPT 169
Cdd:cd03265 83 SVDDELTGWENLYIHARLYGVPGAERR--ERIDELLDFVGL-LEAADRlVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 170 AVLTPQEAKDLYKTLRLM-AEQGKAVIVISHKLSEVLEGTDKISVLRGGK-PAGSTKTEL 227
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRiIAEGTPEEL 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-230 |
2.12e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 105.61 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFPGVVAndHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAavmQGIGM 85
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE---RPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 86 VHQHFKLVKSFTVAENIILGMK-DMGLLYDQRkieAQIEQFCNQYGM--CID--PAakvwQLTLGEQQRVEIIKALFRGA 160
Cdd:COG3840 76 LFQENNLFPHLTVAQNIGLGLRpGLKLTAEQR---AQVEQALERVGLagLLDrlPG----QLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2681003857 161 EILILDEPTAVLTP---QEAKDLYKTLRlmAEQGKAVIVISHKLSEVLEGTDKISVLRGGK--PAGSTKTELASE 230
Cdd:COG3840 149 PILLLDEPFSALDPalrQEMLDLVDELC--RERGLTVLMVTHDPEDAARIADRVLLVADGRiaADGPTAALLDGE 221
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
11-218 |
2.75e-26 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 108.20 E-value: 2.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAavmQGIGMVHQHF 90
Cdd:TIGR03265 9 NIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQK---RDYGIVFQSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 91 KLVKSFTVAENIILGMKDMGllYDQRKIEAQIEQFCNQYGmcIDPAAKVW--QLTLGEQQRVEIIKALFRGAEILILDEP 168
Cdd:TIGR03265 86 ALFPNLTVADNIAYGLKNRG--MGRAEVAERVAELLDLVG--LPGSERKYpgQLSGGQQQRVALARALATSPGLLLLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2681003857 169 TAVLTPQEAKDLYKTLR-LMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:TIGR03265 162 LSALDARVREHLRTEIRqLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGV 212
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-199 |
7.48e-26 |
|
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: 104.05 E-value: 7.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 2 SAIPMVQMVNVTKRFPG----VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLS--P 75
Cdd:COG4181 4 SSAPIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 76 KAAVM-QGIGMVHQHFKLVKSFTVAENIIL-----GMKDmgllyDQRKIEAQIEQF-----CNQYgmcidPAakvwQLTL 144
Cdd:COG4181 84 RARLRaRHVGFVFQSFQLLPTLTALENVMLplelaGRRD-----ARARARALLERVglghrLDHY-----PA----QLSG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2681003857 145 GEQQRVEIIKALFRGAEILILDEPTAVL---TPQEAKDLYKTLRlmAEQGKAVIVISH 199
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLdaaTGEQIIDLLFELN--RERGTTLVLVTH 205
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-321 |
1.12e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 108.23 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVemlspkaavmqgIGMVHQHF 90
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLR------------IGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 91 KLVKSFTVAENIILGMKDMGLLYDQRK------------------------------IEAQIEQFCNQYGM-CIDPAAKV 139
Cdd:COG0488 71 PLDDDLTVLDTVLDGDAELRALEAELEeleaklaepdedlerlaelqeefealggweAEARAEEILSGLGFpEEDLDRPV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 140 WQLTLGEQQRVEIIKALFRGAEILILDEPTAVLtpqeakDLYKTLRL---MAEQGKAVIVISHK---LSEVlegTDKISV 213
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHL------DLESIEWLeefLKNYPGTVLVVSHDryfLDRV---ATRILE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 214 LRGGK----PAGSTKTELASEEELTRWMV------------------------------GR---------NVPKQLDRTV 250
Cdd:COG0488 222 LDRGKltlyPGNYSAYLEQRAERLEQEAAayakqqkkiakeeefirrfrakarkakqaqSRikaleklerEEPPRRDKTV 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2681003857 251 -------TEPGAVVLELDNISCLNNrGQIAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGqKYVAGEN 321
Cdd:COG0488 302 eirfpppERLGKKVLELEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSG-TVKLGET 377
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2-218 |
1.63e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 106.46 E-value: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 2 SAIPMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPkaaVMQ 81
Cdd:PRK11607 15 ALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP---YQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 82 GIGMVHQHFKLVKSFTVAENIILGMKDMGLLYDQrkIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAE 161
Cdd:PRK11607 92 PINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAE--IASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2681003857 162 ILILDEPTAVLTpqeaKDLYKTLRL-----MAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK11607 170 LLLLDEPMGALD----KKLRDRMQLevvdiLERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
11-218 |
2.26e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 105.55 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPGV-VANDhVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAavmQGIGMVHQH 89
Cdd:PRK10851 7 NIKKSFGRTqVLND-ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD---RKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 90 FKLVKSFTVAENIILGM----------------KDMGLLYdqrkiEAQIEQFCNQYgmcidPAakvwQLTLGEQQRVEII 153
Cdd:PRK10851 83 YALFRHMTVFDNIAFGLtvlprrerpnaaaikaKVTQLLE-----MVQLAHLADRY-----PA----QLSGGQKQRVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2681003857 154 KALFRGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIV-ISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVfVTHDQEEAMEVADRVVVMSQGN 214
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-218 |
2.90e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 104.12 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 4 IPMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAavMQGI 83
Cdd:PRK13537 5 VAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA--RQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 84 GMVHQHFKLVKSFTVAENIILGMKDMGLLYDQrkIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEIL 163
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAA--ARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2681003857 164 ILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
7-218 |
3.45e-25 |
|
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: 102.31 E-value: 3.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPGVVAN--DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQgIG 84
Cdd:cd03251 1 VEFKNVTFRYPGDGPPvlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ-IG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 85 MVHQHFKLVkSFTVAENIILGMKDMGllyDQRKIEAQ--------IEQFCNQYGMCI-DPAAKvwqLTLGEQQRVEIIKA 155
Cdd:cd03251 80 LVSQDVFLF-NDTVAENIAYGRPGAT---REEVEEAAraanahefIMELPEGYDTVIgERGVK---LSGGQRQRIAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2681003857 156 LFRGAEILILDEPTAVLTPQEAKDLYKTL-RLMaeQGKAVIVISHKLSEVlEGTDKISVLRGGK 218
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALeRLM--KNRTTFVIAHRLSTI-ENADRIVVLEDGK 213
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-226 |
4.54e-25 |
|
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: 104.81 E-value: 4.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQ------QVEMLSPKAavmQGIGMVHQHFKLVKSFTV 98
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrKGIFLPPEK---RRIGYVFQEARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 99 AENIILGMKD-MGllyDQRKI-EAQIEQFCNqygmcIDPAAK--VWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTP 174
Cdd:TIGR02142 93 RGNLRYGMKRaRP---SERRIsFERVIELLG-----IGHLLGrlPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2681003857 175 QEAKDLYKTL-RLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGSTKTE 226
Cdd:TIGR02142 165 PRKYEILPYLeRLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIA 217
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-218 |
5.01e-25 |
|
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: 101.85 E-value: 5.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 17 PGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKaAVMQGIGMVHQHFKLVkSF 96
Cdd:cd03249 14 PDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLR-WLRSQIGLVSQEPVLF-DG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 97 TVAENIILGMKDMGLLYDQR-----KIEAQIEQFCNQYGMCIDPAAKvwQLTLGEQQRVEIIKALFRGAEILILDEPTAV 171
Cdd:cd03249 92 TIAENIRYGKPDATDEEVEEaakkaNIHDFIMSLPDGYDTLVGERGS--QLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2681003857 172 LTPQEAKDLYKTL-RLMaeQGKAVIVISHKLSEVlEGTDKISVLRGGK 218
Cdd:cd03249 170 LDAESEKLVQEALdRAM--KGRTTIVIAHRLSTI-RNADLIAVLQNGQ 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
10-222 |
7.80e-25 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 100.83 E-value: 7.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 10 VNVTKRFPGVVANdhVSLTIEaGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKG------QQVEMLSPKAavmQGI 83
Cdd:cd03297 4 VDIEKRLPDFTLK--IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsRKKINLPPQQ---RKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 84 GMVHQHFKLVKSFTVAENIILGMKDMGLLYDQRKIEAQIEQfcnqygMCIDP--AAKVWQLTLGEQQRVEIIKALFRGAE 161
Cdd:cd03297 78 GLVFQQYALFPHLNVRENLAFGLKRKRNREDRISVDELLDL------LGLDHllNRYPAQLSGGEKQRVALARALAAQPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2681003857 162 ILILDEPTAVLTPQEAKDLYKTLRLMAEQ-GKAVIVISHKLSEVLEGTDKISVLRGGKPAGS 222
Cdd:cd03297 152 LLLLDEPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-218 |
1.00e-24 |
|
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: 105.65 E-value: 1.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRF----PGVV-ANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIK-GQQ-VEMLSP-- 75
Cdd:TIGR03269 278 PIIKVRNVSKRYisvdRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEwVDMTKPgp 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 76 --KAAVMQGIGMVHQHFKLVKSFTVAENI-----------------ILGMKDMGllYDQRKIEAQIEQFCNqygmcidpa 136
Cdd:TIGR03269 358 dgRGRAKRYIGILHQEYDLYPHRTVLDNLteaiglelpdelarmkaVITLKMVG--FDEEKAEEILDKYPD--------- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 137 akvwQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYKT-LRLMAEQGKAVIVISHKLSEVLEGTDKISVLR 215
Cdd:TIGR03269 427 ----ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSiLKAREEMEQTFIIVSHDMDFVLDVCDRAALMR 502
|
...
gi 2681003857 216 GGK 218
Cdd:TIGR03269 503 DGK 505
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
11-236 |
1.01e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 105.64 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPGVVANdhVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQGIGMVHQHF 90
Cdd:PRK09700 270 NVTSRDRKKVRD--ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESR 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 91 K---LVKSFTVAENIILG--MKD------MGLLYD---QRKIEAQIEQFCNQygmCIDPAAKVWQLTLGEQQRVEIIKAL 156
Cdd:PRK09700 348 RdngFFPNFSIAQNMAISrsLKDggykgaMGLFHEvdeQRTAENQRELLALK---CHSVNQNITELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 157 FRGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGS-TKTELASEEELTR 235
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQIlTNRDDMSEEEIMA 504
|
.
gi 2681003857 236 W 236
Cdd:PRK09700 505 W 505
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-233 |
1.06e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 101.99 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFPGVVAN--DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAvMQG 82
Cdd:PRK13632 6 VMIKVENVSFSYPNSENNalKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI-RKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 83 IGMVHQH--FKLVKSfTVAENIILGMKDMglLYDQRKIEAQIEQFCNQYGMcIDPAAKVWQ-LTLGEQQRVEIIKALFRG 159
Cdd:PRK13632 85 IGIIFQNpdNQFIGA-TVEDDIAFGLENK--KVPPKKMKDIIDDLAKKVGM-EDYLDKEPQnLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2681003857 160 AEILILDEPTAVLTPQEAKDLYKTLRLMAEQG-KAVIVISHKLSEVLEGtDKISVLRGGK--PAGSTKTELASEEEL 233
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAILA-DKVIVFSEGKliAQGKPKEILNNKEIL 236
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
25-199 |
1.11e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 101.24 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEM---LSPKA--AVMQGIGMVHQHFKLVKSFTVA 99
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFsktPSDKAirELRRNVGMVFQQYNLWPHLTVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 100 ENIILG-MKDMGLLYDQRKIEA-------QIEQFCNQYGMcidpaakvwQLTLGEQQRVEIIKALFRGAEILILDEPTAV 171
Cdd:PRK11124 101 QNLIEApCRVLGLSKDQALARAekllerlRLKPYADRFPL---------HLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180
....*....|....*....|....*...
gi 2681003857 172 LTPQEAKDLYKTLRLMAEQGKAVIVISH 199
Cdd:PRK11124 172 LDPEITAQIVSIIRELAETGITQVIVTH 199
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-218 |
1.38e-24 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 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. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 102.96 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 37 LLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKaavMQGIGMVHQHFKLVKSFTVAENIILGMKDMGLlyDQR 116
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH---LRHINMVFQSYALFPHMTVEENVAFGLKMRKV--PRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 117 KIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQ-GKAVI 195
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITFV 155
|
170 180
....*....|....*....|...
gi 2681003857 196 VISHKLSEVLEGTDKISVLRGGK 218
Cdd:TIGR01187 156 FVTHDQEEAMTMSDRIAIMRKGK 178
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-230 |
1.71e-24 |
|
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: 100.93 E-value: 1.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFPGVVANDHVSLTIEAGQiH-GLLGENGAGKSTLMSILTGLYRPDEG-EIYIKGQQ-----VEMLSPKa 77
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGE-HwAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERrggedVWELRKR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 78 avmqgIGMV--HQHFKLVKSFTVAENIILGMKDMGLLY------DQRKIEAQIEQFcnqyGMcIDPAAKVW-QLTLGEQQ 148
Cdd:COG1119 80 -----IGLVspALQLRFPRDETVLDVVLSGFFDSIGLYreptdeQRERARELLELL----GL-AHLADRPFgTLSQGEQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 149 RVEIIKALFRGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQG-KAVIVISHKLSEVLEGTDKISVLRGGKP--AGSTKT 225
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVvaAGPKEE 229
|
....*
gi 2681003857 226 ELASE 230
Cdd:COG1119 230 VLTSE 234
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
25-233 |
2.03e-24 |
|
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: 100.38 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQ---QVEMLSPKAAvmqgIGMVHQHFKLVKSfTVAEN 101
Cdd:cd03253 20 VSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirEVTLDSLRRA----IGVVPQDTVLFND-TIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 102 IILGMKDMGllyDQRKIEA--------QIEQFCNQYgmcidpAAKVWQ----LTLGEQQRVEIIKALFRGAEILILDEPT 169
Cdd:cd03253 95 IRYGRPDAT---DEEVIEAakaaqihdKIMRFPDGY------DTIVGErglkLSGGEKQRVAIARAILKNPPILLLDEAT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2681003857 170 AVLTPQEAKDLYKTLRLMAeQGKAVIVISHKLSEVLeGTDKISVLRGGKPAgstktELASEEEL 233
Cdd:cd03253 166 SALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIV-NADKIIVLKDGRIV-----ERGTHEEL 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
11-218 |
4.19e-24 |
|
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: 97.67 E-value: 4.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPG----VVANdhVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPkAAVMQGIGMV 86
Cdd:cd03246 5 NVSFRYPGaeppVLRN--VSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDP-NELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 87 HQHFKLVkSFTVAENIILGmkdmgllydqrkieaqieqfcnqygmcidpaakvwqltlGEQQRVEIIKALFRGAEILILD 166
Cdd:cd03246 82 PQDDELF-SGSIAENILSG---------------------------------------GQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2681003857 167 EPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLsEVLEGTDKISVLRGGK 218
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGR 172
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-202 |
5.33e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 99.40 E-value: 5.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVemLSPKA---AVMQG 82
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV--NDPKVderLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 83 IGMVHQHFKLVKSFTVAENIILG-MKDMGLLYDQRKIEAQ-------IEQFCNQYgmcidPAakvwQLTLGEQQRVEIIK 154
Cdd:PRK09493 79 AGMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARellakvgLAERAHHY-----PS----ELSGGQQQRVAIAR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2681003857 155 ALFRGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLS 202
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIG 197
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-220 |
6.58e-24 |
|
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: 98.33 E-value: 6.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 24 HVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAavmQGIGMVHQHFKLVKSFTVAENII 103
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD---RPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 104 LGMK-DMGLLYDQRKieaQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTP---QEAKD 179
Cdd:cd03298 93 LGLSpGLKLTAEDRQ---AIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPalrAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2681003857 180 LYKTLRlmAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPA 220
Cdd:cd03298 170 LVLDLH--AETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-205 |
7.72e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 99.17 E-value: 7.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFPG----VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVm 80
Cdd:COG4525 2 SMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 81 qgigmVHQHFKLVKSFTVAENIILGMKDMGLLYDQRkiEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGA 160
Cdd:COG4525 81 -----VFQKDALLPWLNVLDNVAFGLRLRGVPKAER--RARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2681003857 161 EILILDEPTAVL---TPQEAKDLykTLRLMAEQGKAVIVISHKLSEVL 205
Cdd:COG4525 154 RFLLMDEPFGALdalTREQMQEL--LLDVWQRTGKGVFLITHSVEEAL 199
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-218 |
7.86e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 99.70 E-value: 7.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFPGV--VANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQvemLSPKAA--VM 80
Cdd:PRK13635 4 EIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEETVwdVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 81 QGIGMVHQH--FKLVKSfTVAENIILGMKDMGLLYDQ--RKIEAQIEQFCNQYGMCIDPAakvwQLTLGEQQRVEIIKAL 156
Cdd:PRK13635 81 RQVGMVFQNpdNQFVGA-TVQDDVAFGLENIGVPREEmvERVDQALRQVGMEDFLNREPH----RLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2681003857 157 FRGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKA-VIVISHKLSEVLEgTDKISVLRGGK 218
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGItVLSITHDLDEAAQ-ADRVIVMNKGE 217
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-202 |
8.53e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 98.55 E-value: 8.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEM---LSPKAAVM--Q 81
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFsqkPSEKAIRLlrQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 82 GIGMVHQHFKLVKSFTVAENIILG-MKDMGLLYDQRKIEAQieQFCNQYGmcIDPAAKVWQLTL--GEQQRVEIIKALFR 158
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQAREKAM--KLLARLR--LTDKADRFPLHLsgGQQQRVAIARALMM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2681003857 159 GAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLS 202
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVE 202
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-235 |
9.06e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 99.38 E-value: 9.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFP-GVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMlSPKA--AVMQG 82
Cdd:PRK13639 1 ILETRDLKYSYPdGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY-DKKSllEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 83 IGMVHQH-----FklvkSFTVAENIILGMKDMGLLYDQrkIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALF 157
Cdd:PRK13639 80 VGIVFQNpddqlF----APTVEEDVAFGPLNLGLSKEE--VEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2681003857 158 RGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK-PAGSTKTELASEEELTR 235
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKiIKEGTPKEVFSDIETIR 232
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
11-218 |
1.24e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 98.18 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPG--VVanDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSpkaavM-----QGI 83
Cdd:COG1137 8 NLVKSYGKrtVV--KDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP-----MhkrarLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 84 GMVHQH---F-KLvksfTVAENI--ILGMKDMGLLYDQRKIEAQIEQF-----CNQYGMcidpaakvwQLTLGEQQRVEI 152
Cdd:COG1137 81 GYLPQEasiFrKL----TVEDNIlaVLELRKLSKKEREERLEELLEEFgithlRKSKAY---------SLSGGERRRVEI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2681003857 153 IKALFRGAEILILDEPTAVLTP---QEAKDLYKTLRlmaEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDPiavADIQKIIRHLK---ERGIGVLITDHNVRETLGICDRAYIISEGK 213
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
7-233 |
1.97e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 98.65 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFP-GVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAaVMQGIGM 85
Cdd:PRK13647 5 IEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW-VRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 86 VHQH-FKLVKSFTVAENIILGMKDMGLlyDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILI 164
Cdd:PRK13647 84 VFQDpDDQVFSSTVWDDVAFGPVNMGL--DKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2681003857 165 LDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGSTKTELASEEEL 233
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDI 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-386 |
2.06e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 100.69 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQgIG 84
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 85 MVHQHFKLVKSFTVAENIILG----------MKDMGllydqrkiEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIK 154
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGrtphrsrfdtWTETD--------RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 155 ALFRGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK------PAGSTKTELA 228
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRvraagpPADVLTADTL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 229 SEEELTRWMVGRNvPKQLDRTVTE-PGAVVLEL--DNISCLNNRGQIAVRHASLCIRAGEIVGIAGV-AGNGQTELAEVV 304
Cdd:PRK09536 233 RAAFDARTAVGTD-PATGAPTVTPlPDPDRTEAaaDTRVHVVGGGQPAARAVSRLVAAGASVSVGPVpEGDTAAETAARV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 305 AglRPVEDGQKYVAGENHTISSARDMIRAG--VSYVPEDRLGTGLVPGLNAIDNYILKGYDqkgwlinwqqALQKTQAAI 382
Cdd:PRK09536 312 G--CEAVTVPPFKPIEDSTRAEATDLIIAAdaVVAAGVAAAARSGVIGLLAGNAPTLTVTD----------AAAAPEWAD 379
|
....
gi 2681003857 383 DAFD 386
Cdd:PRK09536 380 DTVD 383
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-218 |
2.31e-23 |
|
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: 102.78 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 4 IPMVQMVNVTKRFP--GVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEmlSPKAAVMQ 81
Cdd:TIGR01257 926 VPGVCVKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE--TNLDAVRQ 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 82 GIGMVHQHFKLVKSFTVAENIILGMKDMGLLYDQRKIEaqIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAE 161
Cdd:TIGR01257 1004 SLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLE--MEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAK 1081
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2681003857 162 ILILDEPTAVLTPQEAKDLYKTLrLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWDLL-LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-218 |
3.88e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 97.07 E-value: 3.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 1 MSaiPMVQMVNVTKRFP----------------------GVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRP 58
Cdd:COG1134 1 MS--SMIEVENVSKSYRlyhepsrslkelllrrrrtrreEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 59 DEGEIYIKGQQVEMLSPkaavmqGIGMVHQhfklvksFTVAENIILGMKDMGLLYDQ--RKIE-----AQIEQFCNQ--- 128
Cdd:COG1134 79 TSGRVEVNGRVSALLEL------GAGFHPE-------LTGRENIYLNGRLLGLSRKEidEKFDeivefAELGDFIDQpvk 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 129 -Y--GM----------CIDPaakvwqltlgeqqrveiikalfrgaEILILDEPTAVltpqeaKDLY---KTLRLMAE--- 189
Cdd:COG1134 146 tYssGMrarlafavatAVDP-------------------------DILLVDEVLAV------GDAAfqkKCLARIRElre 194
|
250 260
....*....|....*....|....*....
gi 2681003857 190 QGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:COG1134 195 SGRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-205 |
3.89e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 97.08 E-value: 3.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEmlSPKAAVmqgiGM 85
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GPGAER----GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 86 VHQHFKLVKSFTVAENIILGMKDMGLLYDQRKIEAQieQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILIL 165
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAH--QMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2681003857 166 DEPTAVL---TPQEAKDLYktLRLMAEQGKAVIVISHKLSEVL 205
Cdd:PRK11248 153 DEPFGALdafTREQMQTLL--LKLWQETGKQVLLITHDIEEAV 193
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
25-201 |
5.06e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 96.96 E-value: 5.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQ------------GIGMVHQHFKL 92
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKvadknqlrllrtRLTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 93 VKSFTVAENIILG-MKDMGLLYDQRKIEAqiEQFCNQYGmcIDPAAKV---WQLTLGEQQRVEIIKALFRGAEILILDEP 168
Cdd:PRK10619 104 WSHMTVLENVMEApIQVLGLSKQEARERA--VKYLAKVG--IDERAQGkypVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190
....*....|....*....|....*....|...
gi 2681003857 169 TAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKL 201
Cdd:PRK10619 180 TSALDPELVGEVLRIMQQLAEEGKTMVVVTHEM 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-233 |
7.18e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 99.99 E-value: 7.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQGI----------GMVHQHfklvk 94
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGImlcpedrkaeGIIPVH----- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 95 sfTVAENIILGMK----DMGLLYDQRKIEAQIEQFCNQygMCI---DPAAKVWQLTLGEQQRVEIIKALFRGAEILILDE 167
Cdd:PRK11288 347 --SVADNINISARrhhlRAGCLINNRWEAENADRFIRS--LNIktpSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2681003857 168 PTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGSTKTELASEEEL 233
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQATERQA 488
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
25-220 |
7.27e-23 |
|
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: 94.93 E-value: 7.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGL--YRPDEGEIYIKGQQVEMLSPKAAvmqgIGMVHQHFKLVKSFTVAENi 102
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFRKI----IGYVPQDDILHPTLTVRET- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 103 ilgmkdmgLLYdqrkieaqieqfcnqygmcidpAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYK 182
Cdd:cd03213 103 --------LMF----------------------AAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 2681003857 183 TLRLMAEQGKAVIVISHKLS-EVLEGTDKISVLRGGKPA 220
Cdd:cd03213 153 LLRRLADTGRTIICSIHQPSsEIFELFDKLLLLSQGRVI 191
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-218 |
9.14e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 98.48 E-value: 9.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 1 MSAIPMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAavm 80
Cdd:PRK09452 9 SSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 81 QGIGMVHQHFKLVKSFTVAENIILGMKDMGLLYDQ---RKIEA----QIEQFCNQygmcidpaaKVWQLTLGEQQRVEII 153
Cdd:PRK09452 86 RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEitpRVMEAlrmvQLEEFAQR---------KPHQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2681003857 154 KALFRGAEILILDEPTAVL-------TPQEAKDLYKTLrlmaeqGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALdyklrkqMQNELKALQRKL------GITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
11-239 |
9.23e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 95.73 E-value: 9.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQGIGMVHQHF 90
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 91 KLVKSFTVAENI--ILGMKDmGLLYDQRKIEAQ-------IEQFCNQYGMcidpaakvwQLTLGEQQRVEIIKALFRGAE 161
Cdd:PRK10895 88 SIFRRLSVYDNLmaVLQIRD-DLSAEQREDRANelmeefhIEHLRDSMGQ---------SLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2681003857 162 ILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK-PAGSTKTELASEEELTRWMVG 239
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHlIAHGTPTEILQDEHVKRVYLG 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-330 |
1.02e-22 |
|
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: 99.76 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 1 MSAIPMVQMVNVTKRFPG----VVANDHVSLTIEAGQIHGLLGENGAGKS-TLMSIL----TGLYRPDeGEIYIKGQqvE 71
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILrllpDPAAHPS-GSILFDGQ--D 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 72 MLSPKAAVMQG-----IGMVHQ--------HFKLVKSftVAENIIL--GMkdmgllyDQRKIEAQIEQFCNQYGmcI-DP 135
Cdd:COG4172 78 LLGLSERELRRirgnrIAMIFQepmtslnpLHTIGKQ--IAEVLRLhrGL-------SGAAARARALELLERVG--IpDP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 136 AAKV----WQLTLGEQQRVEIIKALFRGAEILILDEPTAVL--TPQeAK--DLYKTLRlmAEQGKAVIVISHKLSEVLEG 207
Cdd:COG4172 147 ERRLdaypHQLSGGQRQRVMIAMALANEPDLLIADEPTTALdvTVQ-AQilDLLKDLQ--RELGMALLLITHDLGVVRRF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 208 TDKISVLRGGK--PAGSTKTELAS-EEELTRWMVGRnVPKQLDRTVTEPGAVVLELDNISC-------LNNRGQI---AV 274
Cdd:COG4172 224 ADRVAVMRQGEivEQGPTAELFAApQHPYTRKLLAA-EPRGDPRPVPPDAPPLLEARDLKVwfpikrgLFRRTVGhvkAV 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2681003857 275 RHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEdGQKYVAGENHTISSARDM 330
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSRRAL 357
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
23-231 |
1.91e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 98.85 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYR-PDEGEIYIKGQQVEMLSPKAAVMQGIGMV---HQHFKLVKSFTV 98
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQGIAMVpedRKRDGIVPVMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 99 AENIILGMKD---MGLLYDQRKIEAQIEQFCNQygMCI---DPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVL 172
Cdd:PRK13549 359 GKNITLAALDrftGGSRIDDAAELKTILESIQR--LKVktaSPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2681003857 173 TPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGSTKTELASEE 231
Cdd:PRK13549 437 DVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHNLTQE 495
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
26-238 |
2.36e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 99.03 E-value: 2.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 26 SLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKaavmqgigMVHQHFKLVK------SFTVA 99
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHH--------YLHRQVALVGqepvlfSGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 100 ENIILGMKDmgllYDQRKIEAQ---------IEQFCNQYGMCIDPAAKvwQLTLGEQQRVEIIKALFRGAEILILDEPTA 170
Cdd:TIGR00958 573 ENIAYGLTD----TPDEEIMAAakaanahdfIMEFPNGYDTEVGEKGS--QLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2681003857 171 VLTPQEAKDLYKtlrLMAEQGKAVIVISHKLSEVlEGTDKISVLRGGKPA-GSTKTELASEEELTRWMV 238
Cdd:TIGR00958 647 ALDAECEQLLQE---SRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVeMGTHKQLMEDQGCYKHLV 711
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-218 |
2.79e-22 |
|
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: 94.14 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 19 VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPkaavmqGIGMvhqhfklVKSFTV 98
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGL------GGGF-------NPELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 99 AENIILGMKDMGLLYDQ-RKIEAQIEQFCnQYGMCIDpaAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEA 177
Cdd:cd03220 102 RENIYLNGRLLGLSRKEiDEKIDEIIEFS-ELGDFID--LPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2681003857 178 KDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:cd03220 179 EKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-206 |
3.07e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 94.77 E-value: 3.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRF-PG----VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSP-KAAV 79
Cdd:COG1101 1 MLELKNLSKTFnPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEyKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 80 MqgIGMVHQHFKL--VKSFTVAENIILGMK-------DMGLLYDQRKI-EAQIEQFcnqyGMCID--PAAKVWQLTLGEQ 147
Cdd:COG1101 81 Y--IGRVFQDPMMgtAPSMTIEENLALAYRrgkrrglRRGLTKKRRELfRELLATL----GLGLEnrLDTKVGLLSGGQR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 148 QRVEIIKALFRGAEILILDEPTAVLTPQEAKD-LYKTLRLMAEQGKAVIVISHKLSEVLE 206
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALvLELTEKIVEENNLTTLMVTHNMEQALD 214
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-217 |
5.32e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 94.31 E-value: 5.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPD---EGEIYIKGQQVEMLSPKAAVMQG 82
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksaGSHIELLGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 83 ----IGMVHQHFKLVKSFTVAENIILGMkdMG--------LLYDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRV 150
Cdd:PRK09984 84 sranTGYIFQQFNLVNRLSVLENVLIGA--LGstpfwrtcFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2681003857 151 EIIKALFRGAEILILDEPTAVLTPQEAKDLYKTLR-LMAEQGKAVIVISHKLSEVLEGTDKISVLRGG 217
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRdINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-235 |
7.96e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.04 E-value: 7.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 24 HVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQGIgmVH-----QHFKLVKSFTV 98
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGL--VYlpedrQSSGLYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 99 AENII-LGMKDMGLLYDQRKIEAQIEQFCNQYGM-CIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQE 176
Cdd:PRK15439 359 AWNVCaLTHNRRGFWIKPARENAVLERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2681003857 177 AKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGSTKTELASEEELTR 235
Cdd:PRK15439 439 RNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTIMR 497
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
23-218 |
8.05e-22 |
|
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: 91.61 E-value: 8.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGqqVEMLSPKAAVMQGIGMVHQHFKLVkSFTVAENI 102
Cdd:cd03247 19 KNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG--VPVSDLEKALSSLISVLNQRPYLF-DTTLRNNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 103 ilgmkdmGLlydqrkieaqieqfcnqygmcidpaakvwQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPqeaKDLYK 182
Cdd:cd03247 96 -------GR-----------------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDP---ITERQ 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 2681003857 183 TLRLMAEQ--GKAVIVISHKLSEVlEGTDKISVLRGGK 218
Cdd:cd03247 137 LLSLIFEVlkDKTLIWITHHLTGI-EHMDKILFLENGK 173
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-204 |
9.97e-22 |
|
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: 92.78 E-value: 9.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 19 VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKG-----QQVEMLSPKAAVMQgigmvhQHFKLV 93
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwkRRKKFLRRIGVVFG------QKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 94 KSFTVAENIILgMKDMgllYDQRKIEAQ--IEQFCN--QYGMCIDpaAKVWQLTLGEQQRVEIIKALFRGAEILILDEPT 169
Cdd:cd03267 108 WDLPVIDSFYL-LAAI---YDLPPARFKkrLDELSEllDLEELLD--TPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190
....*....|....*....|....*....|....*.
gi 2681003857 170 AVLTPQEAKDLYKTLR-LMAEQGKAVIVISHKLSEV 204
Cdd:cd03267 182 IGLDVVAQENIRNFLKeYNRERGTTVLLTSHYMKDI 217
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-220 |
1.28e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 95.10 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAavmQGIGMV 86
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE---RGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 87 HQHFKLVKSFTVAENIILGMKDMGLlyDQRKIEAQIEQFCN--QYGMCIDPAAKvwQLTLGEQQRVEIIKALFRGAEILI 164
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGA--KKEEINQRVNQVAEvlQLAHLLDRKPK--ALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2681003857 165 LDEP----TAVLTPQ---EAKDLYKTLrlmaeqGKAVIVISHKLSEVLEGTDKISVLRGGKPA 220
Cdd:PRK11000 157 LDEPlsnlDAALRVQmriEISRLHKRL------GRTMIYVTHDQVEAMTLADKIVVLDAGRVA 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-220 |
1.39e-21 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 92.14 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVmqgigmVHQHFKLVKSFTVAENI 102
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV------VFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 103 ILGMKDmgLLYDQRKIEAQ--IEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVL---TPQEA 177
Cdd:TIGR01184 76 ALAVDR--VLPDLSKSERRaiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALdalTRGNL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2681003857 178 KDlyKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPA 220
Cdd:TIGR01184 154 QE--ELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAA 194
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-218 |
2.51e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 92.97 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEM-LSPKA--AVMQGIGMVHQhFKLVKSF--T 97
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPeTGNKNlkKLRKKVSLVFQ-FPEAQLFenT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 98 VAENIILGMKDMGLLYDQRKIEAQieQFCNQYGMCIDPAAKV-WQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQE 176
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDEAKEKAL--KWLKKVGLSEDLISKSpFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2681003857 177 AKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK13641 181 RKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGK 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-233 |
2.57e-21 |
|
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: 95.28 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPD-EGEIYIKGQQVEMLSPKAAVMQGIGMVHQHFK---LVKSFTV 98
Cdd:TIGR02633 277 DDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKrhgIVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 99 AENIILGMKDMglLYDQRKIEAQIEQFCNQYGM------CIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVL 172
Cdd:TIGR02633 357 GKNITLSVLKS--FCFKMRIDAAAELQIIGSAIqrlkvkTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2681003857 173 TPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGS-TKTELASEEEL 233
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDfVNHALTQEQVL 496
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-199 |
3.56e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.56 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFPG----VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVM 80
Cdd:PRK10535 3 ALLELKDIRRSYPSgeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 81 ---QGIGMVHQHFKLVKSFTVAENIILGMKDMGLLYDQRKIEAQieQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALF 157
Cdd:PRK10535 83 lrrEHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQ--ELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2681003857 158 RGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISH 199
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-199 |
3.70e-21 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 90.17 E-value: 3.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 16 FP-GVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMlSPKA--AVMQGIGMVHQH--- 89
Cdd:TIGR01166 1 YPgGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDY-SRKGllERRQRVGLVFQDpdd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 90 --FklvkSFTVAENIILGMKDMGLLYDQrkIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDE 167
Cdd:TIGR01166 80 qlF----AADVDQDVAFGPLNLGLSEAE--VERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDE 153
|
170 180 190
....*....|....*....|....*....|..
gi 2681003857 168 PTAVLTPQEAKDLYKTLRLMAEQGKAVIVISH 199
Cdd:TIGR01166 154 PTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
7-218 |
4.64e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 93.25 E-value: 4.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEmlspKAAVMQ-GIGM 85
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT----HRSIQQrDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 86 VHQHFKLVKSFTVAENIILGMKDMGLLYDQRKI---EA----QIEQFCNQYgmcidpaakVWQLTLGEQQRVEIIKALFR 158
Cdd:PRK11432 83 VFQSYALFPHMSLGENVGYGLKMLGVPKEERKQrvkEAlelvDLAGFEDRY---------VDQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2681003857 159 GAEILILDEPTAVLTPQEAKDLYKTLRLMAEQ-GKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-218 |
4.84e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 92.03 E-value: 4.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 20 VANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGqqVEMLSPKAA---VMQGIGMVHQH--FKLVK 94
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG--VDITDKKVKlsdIRKKVGLVFQYpeYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 95 SfTVAENIILGMKDMGLlyDQRKIEAQIEQFCNQYGMCIDPAA--KVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVL 172
Cdd:PRK13637 99 E-TIEKDIAFGPINLGL--SEEEIENRVKRAMNIVGLDYEDYKdkSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2681003857 173 TPQEAKDLYKTLRLMAEQGK-AVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-239 |
5.14e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 92.15 E-value: 5.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 20 VANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQV------EMLSPkaaVMQGIGMVHQhFKLV 93
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkdKYIRP---VRKRIGMVFQ-FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 94 KSF--TVAENIILGMKDMGLLYDQRKIEAQieQFCNQYGMCIDPAAKV-WQLTLGEQQRVEIIKALFRGAEILILDEPTA 170
Cdd:PRK13646 97 QLFedTVEREIIFGPKNFKMNLDEVKNYAH--RLLMDLGFSRDVMSQSpFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2681003857 171 VLTPQEAKDLYKTLR-LMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK--PAGSTKTELASEEELTRWMVG 239
Cdd:PRK13646 175 GLDPQSKRQVMRLLKsLQTDENKTIILVSHDMNEVARYADEVIVMKEGSivSQTSPKELFKDKKKLADWHIG 246
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
11-169 |
5.47e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 95.19 E-value: 5.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEmlsPK-AAVMQGIGMVHQH 89
Cdd:NF033858 271 GLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGdIATRRRVGYMSQA 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 90 FKLVKSFTVAENIILGMKdmglLYD--QRKIEAQIEQFCNQYGM--CID--PAAkvwqLTLGEQQRVEIIKALFRGAEIL 163
Cdd:NF033858 348 FSLYGELTVRQNLELHAR----LFHlpAAEIAARVAEMLERFDLadVADalPDS----LPLGIRQRLSLAVAVIHKPELL 419
|
....*.
gi 2681003857 164 ILDEPT 169
Cdd:NF033858 420 ILDEPT 425
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
23-230 |
6.36e-21 |
|
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: 90.62 E-value: 6.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQgIGMVHQHFKLVkSFTVAENI 102
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQ-VGVVLQENVLF-NRSIRDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 103 ILGMKDMGLlydQRKIEAQ--------IEQFCNQYGMCIDPAAKvwQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTP 174
Cdd:cd03252 97 ALADPGMSM---ERVIEAAklagahdfISELPEGYDTIVGEQGA--GLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2681003857 175 QEAKDLYKTLRLMAEqGKAVIVISHKLSEVLEGtDKISVLRGGK--PAGSTKTELASE 230
Cdd:cd03252 172 ESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNA-DRIIVMEKGRivEQGSHDELLAEN 227
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-218 |
6.50e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 90.67 E-value: 6.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYrPDEGEIYIKGQQVEMLSPKA-AVMQgiGMVHQHFKLVKSFTVAENII 103
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAElARHR--AYLSQQQSPPFAMPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 104 LGMKDMGllyDQRKIEAQIEQFCNQYGMcidpAAK----VWQLTLGEQQRVEIIKALFR-------GAEILILDEPTAVL 172
Cdd:COG4138 92 LHQPAGA---SSEAVEQLLAQLAEALGL----EDKlsrpLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2681003857 173 -TPQEAKdLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:COG4138 165 dVAQQAA-LDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGK 210
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-226 |
7.09e-21 |
|
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: 90.32 E-value: 7.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLY-----RPDEGEIYIKGQQV-EMLSPKAAVM 80
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIyDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 81 QGIGMVHQH---FKLvksfTVAENIILGMKDMGLLyDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTL--GEQQRVEIIKA 155
Cdd:cd03260 81 RRVGMVFQKpnpFPG----SIYDNVAYGLRLHGIK-LKEELDERVEEALRKAALWDEVKDRLHALGLsgGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2681003857 156 LFRGAEILILDEPTAVLTPQEAKDLYktlRLMAEQGK--AVIVISHKLSEVLEGTDKISVLRGGKPAGSTKTE 226
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIE---ELIAELKKeyTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTE 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
6-218 |
8.24e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.20 E-value: 8.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFP-GVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQGIG 84
Cdd:PRK13644 1 MIRLENVSYSYPdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 85 MVHQHFKlvKSF---TVAENIILGMKDMGL-------LYDQRKIEAQIEQFCNQygmciDPAAkvwqLTLGEQQRVEIIK 154
Cdd:PRK13644 81 IVFQNPE--TQFvgrTVEEDLAFGPENLCLppieirkRVDRALAEIGLEKYRHR-----SPKT----LSGGQGQCVALAG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2681003857 155 ALFRGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEvLEGTDKISVLRGGK 218
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGK 212
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-218 |
1.13e-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: 91.65 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFP---GVV-ANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRP---DEGEIYIKGQQVEMLSPKAavMQ-- 81
Cdd:COG0444 6 NLKVYFPtrrGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKE--LRki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 82 ---GIGMVHQhfklvkS--------FTVAENIILGMKDMGLLyDQRKIEAQIEQFCNQYGmcIDPAAKV-----WQLTLG 145
Cdd:COG0444 84 rgrEIQMIFQ------DpmtslnpvMTVGDQIAEPLRIHGGL-SKAEARERAIELLERVG--LPDPERRldrypHELSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2681003857 146 EQQRVEIIKALFRGAEILILDEPTAVL--TPQeAK--DLYKTLRlmAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALdvTIQ-AQilNLLKDLQ--RELGLAILFITHDLGVVAEIADRVAVMYAGR 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
25-220 |
1.35e-20 |
|
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: 89.64 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDE---GEIYIKGQQVEmlspKAAVMQGIGMVHQHFKLVKSFTVAEN 101
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRK----PDQFQKCVAYVRQDDILLPGLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 102 I--ILGMKdMGLLYDQRKIEAQIEQFC-NQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAK 178
Cdd:cd03234 102 LtyTAILR-LPRKSSDAIRKKRVEDVLlRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2681003857 179 DLYKTLRLMAEQGKAVIVISHK-LSEVLEGTDKISVLRGGKPA 220
Cdd:cd03234 181 NLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-243 |
1.51e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.20 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMlSPKAAVMQGIGMVHQH--FKLVKSfTVAE 100
Cdd:PRK13648 26 KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD-DNFEKLRKHIGIVFQNpdNQFVGS-IVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 101 NIILGMKDMGLLYDqrKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDL 180
Cdd:PRK13648 104 DVAFGLENHAVPYD--EMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNL 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2681003857 181 YKTLR-LMAEQGKAVIVISHKLSEVLEGtDKISVLRGGK--PAGSTKTELASEEELTRwmVGRNVP 243
Cdd:PRK13648 182 LDLVRkVKSEHNITIISITHDLSEAMEA-DHVIVMNKGTvyKEGTPTEIFDHAEELTR--IGLDLP 244
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
23-235 |
1.58e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.07 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAaVMQGIGMVHQHFKLVKSFTVAENI 102
Cdd:PRK11231 19 NDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-LARRLALLPQHHLTPEGITVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 103 ILGMKDMGLLY------DQRKIEAQIEQfcnqygMCIDPAA--KVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTP 174
Cdd:PRK11231 98 AYGRSPWLSLWgrlsaeDNARVNQAMEQ------TRINHLAdrRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2681003857 175 QEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK-PAGSTKTELASEEELTR 235
Cdd:PRK11231 172 NHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHvMAQGTPEEVMTPGLLRT 233
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-202 |
1.77e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 89.49 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRF-PGVVAND---HVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVM 80
Cdd:PRK11629 4 ILLQCDNLCKRYqEGSVQTDvlhNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 81 ---QGIGMVHQHFKLVKSFTVAENIIlgmkdMGLLYDQRKiEAQIEQFCNQYGMCIDPAAKVW----QLTLGEQQRVEII 153
Cdd:PRK11629 84 lrnQKLGFIYQFHHLLPDFTALENVA-----MPLLIGKKK-PAEINSRALEMLAAVGLEHRANhrpsELSGGERQRVAIA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2681003857 154 KALFRGAEILILDEPTAVLTPQEAKDLYKTL-RLMAEQGKAVIVISHKLS 202
Cdd:PRK11629 158 RALVNNPRLVLADEPTGNLDARNADSIFQLLgELNRLQGTAFLVVTHDLQ 207
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
23-218 |
1.84e-20 |
|
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: 93.35 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPkAAVMQGIGMVHQHFKLvksF--TVAE 100
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQ-ASLRAAIGIVPQDTVL---FndTIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 101 NIILGMKDMgllyDQRKIE-----AQIEQFcnqygmcIDPAAKVWQ-------LTL--GEQQRVEIIKALFRGAEILILD 166
Cdd:COG5265 451 NIAYGRPDA----SEEEVEaaaraAQIHDF-------IESLPDGYDtrvgergLKLsgGEKQRVAIARTLLKNPPILIFD 519
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2681003857 167 EPTAVLTPQEAKDLYKTLRLMAeQGKAVIVISHKLSEVLEGtDKISVLRGGK 218
Cdd:COG5265 520 EATSALDSRTERAIQAALREVA-RGRTTLVIAHRLSTIVDA-DEILVLEAGR 569
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
7-218 |
1.99e-20 |
|
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: 89.07 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVT---KRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQgI 83
Cdd:cd03248 12 VKFQNVTfayPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK-V 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 84 GMVHQHFKLVkSFTVAENIILGMKDMGllyDQRKIEAQ--------IEQFcnQYGMCIDPAAKVWQLTLGEQQRVEIIKA 155
Cdd:cd03248 91 SLVGQEPVLF-ARSLQDNIAYGLQSCS---FECVKEAAqkahahsfISEL--ASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2681003857 156 LFRGAEILILDEPTAVLTPQEAKDLYKTLRlMAEQGKAVIVISHKLSEVlEGTDKISVLRGGK 218
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALY-DWPERRTVLVIAHRLSTV-ERADQILVLDGGR 225
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-218 |
2.12e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 92.97 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSpKAAVMQGIGMVHQHFKLVkSFTVAENI 102
Cdd:PRK11160 357 KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS-EAALRQAISVVSQRVHLF-SATLRDNL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 103 ILGMKDmgllydqrKIEAQIEQFCNQYGMC----IDPAAKVW------QLTLGEQQRVEIIKALFRGAEILILDEPTAVL 172
Cdd:PRK11160 435 LLAAPN--------ASDEALIEVLQQVGLEklleDDKGLNAWlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2681003857 173 ---TPQEakdlykTLRLMAE--QGKAVIVISHKLSEvLEGTDKISVLRGGK 218
Cdd:PRK11160 507 daeTERQ------ILELLAEhaQNKTVLMITHRLTG-LEQFDRICVMDNGQ 550
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-237 |
2.21e-20 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 92.55 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTL-MSILTGLY-RPDEGEIYIKGQQVEMLSPKAAVMQGIGMV---HQHFKLVKSFT 97
Cdd:NF040905 277 DDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYgRNISGTVFKDGKEVDVSTVSDAIDAGLAYVtedRKGYGLNLIDD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 98 VAENIIL----GMKDMGLLYDQRKIEAQiEQFCNQygMCIDpAAKVWQLTL----GEQQRVEIIKALFRGAEILILDEPT 169
Cdd:NF040905 357 IKRNITLanlgKVSRRGVIDENEEIKVA-EEYRKK--MNIK-TPSVFQKVGnlsgGNQQKVVLSKWLFTDPDVLILDEPT 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2681003857 170 A---VltpqEAK-DLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGSTKTELASEEELTRWM 237
Cdd:NF040905 433 RgidV----GAKyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPREEASQERIMRLI 500
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-218 |
2.41e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 90.15 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 20 VANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQGIGMVHQH--FKLVKSFt 97
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNpdNQIVATI- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 98 VAENIILGMKDMGLlyDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEA 177
Cdd:PRK13633 103 VEEDVAFGPENLGI--PPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2681003857 178 KDLYKTLR-LMAEQGKAVIVISHKLSEVLEGtDKISVLRGGK 218
Cdd:PRK13633 181 REVVNTIKeLNKKYGITIILITHYMEEAVEA-DRIIVMDSGK 221
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
11-218 |
5.14e-20 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 91.73 E-value: 5.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPG----VVANdhVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPkAAVMQGIGMV 86
Cdd:COG4618 335 NLTVVPPGskrpILRG--VSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR-EELGRHIGYL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 87 HQHFKLvksF--TVAENI----------------ILGMKDMgllydqrkieaqIEQFCNQYGMCIDPAAKVwqLTLGEQQ 148
Cdd:COG4618 412 PQDVEL---FdgTIAENIarfgdadpekvvaaakLAGVHEM------------ILRLPDGYDTRIGEGGAR--LSGGQRQ 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 149 RVEIIKALFRGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSeVLEGTDKISVLRGGK 218
Cdd:COG4618 475 RIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGR 543
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-199 |
5.25e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.66 E-value: 5.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIkGQQVEmlspkaavmqgIG 84
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-----------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 85 MVHQHFK-LVKSFTVAENIILGMKDMGllydqrkiEAQIEQFCNQYGMcidPAAKVWQL--TL--GEQQRVEIIKALFRG 159
Cdd:COG0488 382 YFDQHQEeLDPDKTVLDELRDGAPGGT--------EQEVRGYLGRFLF---SGDDAFKPvgVLsgGEKARLALAKLLLSP 450
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2681003857 160 AEILILDEPTAVLtpqeakDLyKTLRLMAE-----QGkAVIVISH 199
Cdd:COG0488 451 PNVLLLDEPTNHL------DI-ETLEALEEalddfPG-TVLLVSH 487
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-238 |
5.94e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.91 E-value: 5.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMlSPKA--AVMQGIGMVHQHFKLVKSFT-VAEN 101
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY-SKRGllALRQQVATVFQDPEQQIFYTdIDSD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 102 IILGMKDMGLLYDQ--RKIEAQI-----EQFCNQYGMCidpaakvwqLTLGEQQRVEIIKALFRGAEILILDEPTAVLTP 174
Cdd:PRK13638 99 IAFSLRNLGVPEAEitRRVDEALtlvdaQHFRHQPIQC---------LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2681003857 175 QEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK--PAGS-----TKTELASEEELTR-WMV 238
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQilTHGApgevfACTEAMEQAGLTQpWLV 241
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-218 |
8.65e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.14 E-value: 8.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 19 VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIK----GQQVEMLSPKAAVMQG-----------I 83
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELITNPYSKkiknfkelrrrV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 84 GMVHQ--HFKLVKSfTVAENIILGMKDMGllydQRKIEAQieQFCNQY--GMCIDPA---AKVWQLTLGEQQRVEIIKAL 156
Cdd:PRK13631 119 SMVFQfpEYQLFKD-TIEKDIMFGPVALG----VKKSEAK--KLAKFYlnKMGLDDSyleRSPFGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2681003857 157 FRGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGK 253
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-235 |
1.63e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 87.11 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKA-------A 78
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSqqkglirQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 79 VMQGIGMVHQHFKLVKSFTVAENIILG---MKDMgllyDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKA 155
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGpviVKGE----PKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 156 LFRGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK--PAGSTKTELAS-EEE 232
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRivEQGPAKALFADpQQP 238
|
...
gi 2681003857 233 LTR 235
Cdd:PRK11264 239 RTR 241
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
5-218 |
2.39e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 86.09 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQGIG 84
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 85 MVHQHFKLVKSFTVAENIILGmkdmGLLYDQRKIEAQIEQFCNQYGMCID-PAAKVWQLTLGEQQRVEIIKALFRGAEIL 163
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMG----GFFAERDQFQERIKWVYELFPRLHErRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2681003857 164 ILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGH 214
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-199 |
2.43e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 86.68 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQV-----EMLSPKAAVM 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVattpsRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 81 QgigmvhQHFKLVKSFTVAENIILGMkdmgllY----------DQRKIEAQIEQF-----CNQYgmcIDpaakvwQLTLG 145
Cdd:COG4604 81 R------QENHINSRLTVRELVAFGR------FpyskgrltaeDREIIDEAIAYLdledlADRY---LD------ELSGG 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2681003857 146 EQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYKTLRLMA-EQGKAVIVISH 199
Cdd:COG4604 140 QRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdELGKTVVIVLH 194
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
21-235 |
4.45e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.40 E-value: 4.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 21 ANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAaVMQGIGMVHQHFK-LVKSFTVA 99
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRE-VRKFVGLVFQNPDdQIFSPTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 100 ENIILGMKDMGLlyDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKD 179
Cdd:PRK13652 98 QDIAFGPINLGL--DEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2681003857 180 LYKTLR-LMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGS-TKTELASEEELTR 235
Cdd:PRK13652 176 LIDFLNdLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYgTVEEIFLQPDLLA 233
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-201 |
5.58e-19 |
|
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: 88.57 E-value: 5.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 12 VTKRFPG-VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSpKAAVMQGIGMVHQHF 90
Cdd:TIGR02868 340 LSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLD-QDEVRRRVSVCAQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 91 KLVKSfTVAENIILGMKD-----MGLLYDQRKIEAQIEQFCNQYGMCIDPAAKvwQLTLGEQQRVEIIKALFRGAEILIL 165
Cdd:TIGR02868 419 HLFDT-TVRENLRLARPDatdeeLWAALERVGLADWLRALPDGLDTVLGEGGA--RLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*.
gi 2681003857 166 DEPTAVLTPQEAKDLYKTLrLMAEQGKAVIVISHKL 201
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDL-LAALSGRTVVLITHHL 530
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
23-232 |
8.99e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 85.55 E-value: 8.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQvemLSPKAA--VMQGIGMVHQH--FKLVKSfTV 98
Cdd:PRK13650 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL---LTEENVwdIRHKIGMVFQNpdNQFVGA-TV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 99 AENIILGMKDMGLLYDQRKieAQIEQFCNQYGMCI----DPAakvwQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTP 174
Cdd:PRK13650 100 EDDVAFGLENKGIPHEEMK--ERVNEALELVGMQDfkerEPA----RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 175 QEAKDLYKTLRLMAEQ-GKAVIVISHKLSEVLEgTDKISVLRGGK-PAGSTKTELASEEE 232
Cdd:PRK13650 174 EGRLELIKTIKGIRDDyQMTVISITHDLDEVAL-SDRVLVMKNGQvESTSTPRELFSRGN 232
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
6-235 |
1.02e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 85.28 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFP-GVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMlSPKA--AVMQG 82
Cdd:PRK13636 5 ILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDY-SRKGlmKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 83 IGMV-----HQHFklvkSFTVAENIILGMKDMGLLYDQrkIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALF 157
Cdd:PRK13636 84 VGMVfqdpdNQLF----SASVYQDVSFGAVNLKLPEDE--VRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 158 RGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQ-GKAVIVISHKLSEVLEGTDKISVLRGGKPA-GSTKTELASEEELTR 235
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVIlQGNPKEVFAEKEMLR 237
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
25-230 |
1.28e-18 |
|
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: 83.35 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGL--YRPDEGEIYIKGQQVEMLSPKAAVMQGIGMVHQHfklvksftVAEni 102
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIFLAFQY--------PPE-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 103 ILGMKDMGLLydqrkieaqieQFCNqYGmcidpaakvwqLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYK 182
Cdd:cd03217 89 IPGVKNADFL-----------RYVN-EG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2681003857 183 TLRLMAEQGKAVIVISH--KLSEVLEgTDKISVLRGGKPAGSTKTELASE 230
Cdd:cd03217 146 VINKLREEGKSVLIITHyqRLLDYIK-PDRVHVLYDGRIVKSGDKELALE 194
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
11-218 |
1.41e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 87.38 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPG--VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQgIGMVHQ 88
Cdd:PRK11176 346 NVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQ-VALVSQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 89 HFKLVKSfTVAENIILGMKDMgllYDQRKIEAQIEQfcnQYGMciDPAAKVWQ------------LTLGEQQRVEIIKAL 156
Cdd:PRK11176 425 NVHLFND-TIANNIAYARTEQ---YSREQIEEAARM---AYAM--DFINKMDNgldtvigengvlLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2681003857 157 FRGAEILILDEPTAVLTPQEAKDLYKTLRLMaEQGKAVIVISHKLSEVlEGTDKISVLRGGK 218
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTI-EKADEILVVEDGE 555
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-235 |
2.45e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 83.44 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYrPDEGEIYIKGQQVEMLS-PKAAVMQGigMVHQHFKLVKSFTVAENII 103
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSaAELARHRA--YLSQQQTPPFAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 104 LGMKDMGLLYDqrkIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRV-------EIIKALFRGAEILILDEPTAVLTPQE 176
Cdd:PRK03695 92 LHQPDKTRTEA---VASALNEVAEALGLDDKLGRSVNQLSGGEWQRVrlaavvlQVWPDINPAGQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2681003857 177 AKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK--PAGSTKtELASEEELTR 235
Cdd:PRK03695 169 QAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKllASGRRD-EVLTPENLAQ 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-218 |
3.71e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 86.17 E-value: 3.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPGVV-ANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSpKAAVMQGIGM 85
Cdd:PRK13657 335 VEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT-RASLRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 86 VHQHFKLVKSfTVAENIILGMKDMGL--LYDQRKIeAQIEQFCNQYGMCIDPAA--KVWQLTLGEQQRVEIIKALFRGAE 161
Cdd:PRK13657 414 VFQDAGLFNR-SIEDNIRVGRPDATDeeMRAAAER-AQAHDFIERKPDGYDTVVgeRGRQLSGGERQRLAIARALLKDPP 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 162 ILILDEPTAVL---TPQEAKDLYKTLRlmaeQGKAVIVISHKLSEVLEGtDKISVLRGGK 218
Cdd:PRK13657 492 ILILDEATSALdveTEAKVKAALDELM----KGRTTFIIAHRLSTVRNA-DRILVFDNGR 546
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-242 |
4.96e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.44 E-value: 4.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 17 PGVvanDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQGIGMVHQHFK---LV 93
Cdd:PRK10762 266 PGV---NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRKrdgLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 94 KSFTVAENIILGM-----KDMGLLYDQRKIEAqIEQFCNQYGM-CIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDE 167
Cdd:PRK10762 343 LGMSVKENMSLTAlryfsRAGGSLKHADEQQA-VSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2681003857 168 PTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGSTKTELASEEELTRWMVGRNV 242
Cdd:PRK10762 422 PTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQATQEKLMAAAVGKLN 496
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-201 |
9.03e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 81.55 E-value: 9.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 24 HVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKaavMQGIGMVHQHFKLVKSFTVAENII 103
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS---RRPVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 104 LGMkDMGL-LYDQRKieAQIEQFCNQYGM--CID--PAakvwQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTP---Q 175
Cdd:PRK10771 94 LGL-NPGLkLNAAQR--EKLHAIARQMGIedLLArlPG----QLSGGQRQRVALARCLVREQPILLLDEPFSALDPalrQ 166
|
170 180
....*....|....*....|....*.
gi 2681003857 176 EAKDLYKTlrLMAEQGKAVIVISHKL 201
Cdd:PRK10771 167 EMLTLVSQ--VCQERQLTLLMVSHSL 190
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-218 |
1.08e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.93 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 26 SLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSP---KAAVMQGIGMVHQHFKLVKSFTVAENI 102
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelREVRRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 103 ILGMKDMGLLYDQRKIEAQieQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYK 182
Cdd:PRK10070 128 AFGMELAGINAEERREKAL--DALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
|
170 180 190
....*....|....*....|....*....|....*..
gi 2681003857 183 TL-RLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK10070 206 ELvKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGE 242
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
24-218 |
1.74e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 84.00 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 24 HVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSpKAAVMQGIGMVHQHfKLVKSFTVAENII 103
Cdd:PRK10790 359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSVLRQGVAMVQQD-PVVLADTFLANVT 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 104 LGmkdmgllydqRKI-EAQIEQfcnqygmcidpAAKVWQLT-------------LGEQ---------QRVEIIKALFRGA 160
Cdd:PRK10790 437 LG----------RDIsEEQVWQ-----------ALETVQLAelarslpdglytpLGEQgnnlsvgqkQLLALARVLVQTP 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2681003857 161 EILILDEPTAVLTPQEAKDLYKTLRLMAEQgKAVIVISHKLSEVLEGtDKISVLRGGK 218
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREH-TTLVVIAHRLSTIVEA-DTILVLHRGQ 551
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-218 |
1.99e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 82.44 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 19 VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGqqvemLSP---KAAVMQGIGMV-------HQ 88
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG-----YVPfkrRKEFARRIGVVfgqrsqlWW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 89 HFKLVKSFTVaeniilgmkdMGLLY--DQRKIEAQIEQFCNQYGmcIDPAAK--VWQLTLGEQQRVEIIKALFRGAEILI 164
Cdd:COG4586 110 DLPAIDSFRL----------LKAIYriPDAEYKKRLDELVELLD--LGELLDtpVRQLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2681003857 165 LDEPTA---VLTPQEAKDLYKTLRlmAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:COG4586 178 LDEPTIgldVVSKEAIREFLKEYN--RERGTTILLTSHDMDDIEALCDRVIVIDHGR 232
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-218 |
2.01e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 83.74 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGlYRPDEGEIYIKGQQVEMLSPkAAVMQGIGMVHQHFKLVKSfTVAENIIL 104
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRELDP-ESWRKHLSWVGQNPQLPHG-TLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 105 GMKDMGllydqrkiEAQIEQFCNQYGMC--IDPAAKVWQLTLGEQ---------QRVEIIKALFRGAEILILDEPTAVLT 173
Cdd:PRK11174 446 GNPDAS--------DEQLQQALENAWVSefLPLLPQGLDTPIGDQaaglsvgqaQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2681003857 174 PQEAKDLYKTLRlMAEQGKAVIVISHKLSEvLEGTDKISVLRGGK 218
Cdd:PRK11174 518 AHSEQLVMQALN-AASRRQTTLMVTHQLED-LAQWDQIWVMQDGQ 560
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
25-218 |
7.65e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 79.79 E-value: 7.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSpkaaVMQGIGMVHQHFKLVKSF-------- 96
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTS----KNKDIKQIRKKVGLVFQFpesqlfee 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 97 TVAENIILGMKDMGLlyDQRKIEAQIEQFCNQYGMCIDPAAK-VWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQ 175
Cdd:PRK13649 102 TVLKDVAFGPQNFGV--SQEEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2681003857 176 EAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK13649 180 GRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-240 |
1.80e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.42 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYR--PD---EGEIYIKGQQVEMLsPKAAVMQGIGMVHQHFKLVKSFT 97
Cdd:PRK14247 20 DGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKM-DVIELRRRVQMVFQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 98 VAENIILGMKDMGLLYDQRKIEAQIEQFCNQYGMCID-------PAAKvwqLTLGEQQRVEIIKALFRGAEILILDEPTA 170
Cdd:PRK14247 99 IFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEvkdrldaPAGK---LSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2681003857 171 VLTPQEAKDLyKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK--PAGSTKTELAS-EEELT-RWMVGR 240
Cdd:PRK14247 176 NLDPENTAKI-ESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQivEWGPTREVFTNpRHELTeKYVTGR 248
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-218 |
1.95e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 79.36 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 21 ANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYI---------KGQQVEMLSPKAAVMQG--------- 82
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkKTKEKEKVLEKLVIQKTrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 83 -----IGMVHQ--HFKLVKSfTVAENIILGMKDMGLlydqRKIEAqiEQFCNQY----GMCIDPAAKV-WQLTLGEQQRV 150
Cdd:PRK13651 102 eirrrVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGV----SKEEA--KKRAAKYielvGLDESYLQRSpFELSGGQKRRV 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2681003857 151 EIIKALFRGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
25-247 |
2.09e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 80.79 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPkAAVMQGIGMVHQHFKLV------KSFTV 98
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQP-EDYRKLFSAVFTDFHLFdqllgpEGKPA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 99 AENII------LGMKDmgllydqrKIEAQIEQFCNQygmcidpaakvwQLTLGEQQRVEIIKALFRGAEILILDEPTAVL 172
Cdd:PRK10522 421 NPALVekwlerLKMAH--------KLELEDGRISNL------------KLSKGQKKRLALLLALAEERDILLLDEWAADQ 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2681003857 173 TPQEAKDLY-KTLRLMAEQGKAVIVISHKlSEVLEGTDKISVLRGGKpagstKTELASEEeltRWMVGRNVPKQLD 247
Cdd:PRK10522 481 DPHFRREFYqVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ-----LSELTGEE---RDAASRDAVARTA 547
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
5-199 |
2.28e-16 |
|
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: 77.47 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRF----------PGVvanDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIK--GQQVEM 72
Cdd:COG4778 3 TLLEVENLSKTFtlhlqggkrlPVL---DGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 73 LSPKAAVM-----QGIGMVHQHFKLVKSFT----VAENIIlgmkDMGllYDQRKIEAQIEQFCNQygMCIDPaaKVWQL- 142
Cdd:COG4778 80 AQASPREIlalrrRTIGYVSQFLRVIPRVSaldvVAEPLL----ERG--VDREEARARARELLAR--LNLPE--RLWDLp 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2681003857 143 --TL--GEQQRVEIIKALFRGAEILILDEPTAVLTPQeAKDlyKTLRLMAE---QGKAVIVISH 199
Cdd:COG4778 150 paTFsgGEQQRVNIARGFIADPPLLLLDEPTASLDAA-NRA--VVVELIEEakaRGTAIIGIFH 210
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
25-199 |
2.76e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 76.76 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPK-AAVMQGIGmvhqHFKLVKS-FTVAENI 102
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLG----HAPGIKTtLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 103 ILGMKDMGllydqrkiEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYK 182
Cdd:cd03231 95 RFWHADHS--------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
170
....*....|....*..
gi 2681003857 183 TLRLMAEQGKAVIVISH 199
Cdd:cd03231 167 AMAGHCARGGMVVLTTH 183
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-218 |
3.71e-16 |
|
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: 74.79 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIyikgqqvemlspkaAVMQGIGMV 86
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--------------TWGSTVKIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 87 HqhfklvksftvaeniilgmkdmgllydqrkieaqieqfcnqygmcidpaakVWQLTLGEQQRVEIIKALFRGAEILILD 166
Cdd:cd03221 67 Y---------------------------------------------------FEQLSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2681003857 167 EPTAVLTPqEAKD-LYKTLRlmaEQGKAVIVISHK---LSEVlegTDKISVLRGGK 218
Cdd:cd03221 96 EPTNHLDL-ESIEaLEEALK---EYPGTVILVSHDryfLDQV---ATKIIELEDGK 144
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-199 |
8.57e-16 |
|
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: 78.82 E-value: 8.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIkGQQVEmlspkaavmqgIGMVHQ-H 89
Cdd:TIGR03719 327 NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK-----------LAYVDQsR 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 90 FKLVKSFTVAENIILGMKDMGLlydqRKIEAQIEQFCNQYG-MCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEP 168
Cdd:TIGR03719 395 DALDPNKTVWEEISGGLDIIKL----GKREIPSRAYVGRFNfKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
170 180 190
....*....|....*....|....*....|....*..
gi 2681003857 169 TavltpqeaKDL-YKTLR-----LMAEQGKAViVISH 199
Cdd:TIGR03719 471 T--------NDLdVETLRaleeaLLNFAGCAV-VISH 498
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
25-218 |
1.62e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.84 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQ------QVEMLSPKAavmQGIGMVHQHFKLVKSFTV 98
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaeKGICLPPEK---RRIGYVFQDARLFPHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 99 AENIILGMKdmgllydqRKIEAQIEQFCNQYGmcIDPAAKVWQLTL--GEQQRVEIIKALFRGAEILILDEPTAVLTPQE 176
Cdd:PRK11144 94 RGNLRYGMA--------KSMVAQFDKIVALLG--IEPLLDRYPGSLsgGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2681003857 177 AKDLYKTLRLMAEQGKAVIV-ISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK11144 164 KRELLPYLERLAREINIPILyVSHSLDEILRLADRVVVLEQGK 206
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
11-218 |
1.82e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.59 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQgIGMVHQHF 90
Cdd:PRK10575 16 NVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAYLPQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 91 KLVKSFTVAENIILGMKDM-GLL-----YDQRKIEAQIEQfcnqygMCIDPAAK--VWQLTLGEQQRVEIIKALFRGAEI 162
Cdd:PRK10575 95 PAAEGMTVRELVAIGRYPWhGALgrfgaADREKVEEAISL------VGLKPLAHrlVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2681003857 163 LILDEPTAVLTPQEAKDLYKTL-RLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVhRLSQERGLTVIAVLHDINMAARYCDYLVALRGGE 225
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
7-218 |
1.89e-15 |
|
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: 74.84 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFP--GVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAaVMQGIG 84
Cdd:cd03244 3 IEFKNVSLRYRpnLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHD-LRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 85 MVHQHfKLVKSFTVAENI-ILGMKDMGLLYDQRKiEAQIEQFCNQYGMCIDpaAKVW----QLTLGEQQRVEIIKALFRG 159
Cdd:cd03244 82 IIPQD-PVLFSGTIRSNLdPFGEYSDEELWQALE-RVGLKEFVESLPGGLD--TVVEeggeNLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2681003857 160 AEILILDEPTAVLTPQEAKDLYKTLRlMAEQGKAVIVISHKLSEVLEgTDKISVLRGGK 218
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIR-EAFKDCTVLTIAHRLDTIID-SDRILVLDKGR 214
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-235 |
2.23e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.81 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 21 ANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEI----YIKGQQVEMLSPKAAVMQGIGMVHQ--HFKLVK 94
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdYAIPANLKKIKEVKRLRKEIGLVFQfpEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 95 SfTVAENIILGMKDMGllYDQRKIEAQIEQFCNQYGMCIDPAAKV-WQLTLGEQQRVEIIKALFRGAEILILDEPTAVLT 173
Cdd:PRK13645 106 E-TIEKDIAFGPVNLG--ENKQEAYKKVPELLKLVQLPEDYVKRSpFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2681003857 174 PQEAKDLYKT-LRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK--PAGSTKTELASEEELTR 235
Cdd:PRK13645 183 PKGEEDFINLfERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKviSIGSPFEIFSNQELLTK 247
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
25-199 |
2.48e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 73.93 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAA-VMQGIGmvhqHFKLVKS-FTVAENI 102
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHeNILYLG----HLPGLKPeLSALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 103 ILGMKDMGllYDQRKIEAQIEQFcNQYGMCIDPAAkvwQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYK 182
Cdd:TIGR01189 95 HFWAAIHG--GAQRTIEDALAAV-GLTGFEDLPAA---QLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAG 168
|
170
....*....|....*..
gi 2681003857 183 TLRLMAEQGKAVIVISH 199
Cdd:TIGR01189 169 LLRAHLARGGIVLLTTH 185
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
25-217 |
2.49e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 75.93 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKA---AVMQGIGMVHQhFKLVKSF--TVA 99
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikPVRKKVGVVFQ-FPESQLFeeTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 100 ENIILGMKDMGLLYDQ-RKIEAQIEQFcnqygmcIDPAAKVWQ-----LTLGEQQRVEIIKALFRGAEILILDEPTAVLT 173
Cdd:PRK13643 104 KDVAFGPQNFGIPKEKaEKIAAEKLEM-------VGLADEFWEkspfeLSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2681003857 174 PQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGG 217
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKG 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
23-243 |
3.03e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.22 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGE---IYIKGQQvemLSPKAA--VMQGIGMVHQH--FKLVKS 95
Cdd:PRK13640 24 NDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGIT---LTAKTVwdIREKVGIVFQNpdNQFVGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 96 fTVAENIILGMKDMGLlyDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQ 175
Cdd:PRK13640 101 -TVGDDVAFGLENRAV--PRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 176 EAKDLYKTLR-LMAEQGKAVIVISHKLSEVlEGTDKISVLRGGKP-AGSTKTELASEEELTRwMVGRNVP 243
Cdd:PRK13640 178 GKEQILKLIRkLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLlAQGSPVEIFSKVEMLK-EIGLDIP 245
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
6-226 |
3.70e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 74.14 E-value: 3.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRF-PGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAA--VMQG 82
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 83 IGMVHQHFKLVKSFTVAENIILGMKDMGLLYD--QRKIEAQIEQFcnqyGMCIDPAAKVWQLTLGEQQRVEIIKALFRGA 160
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDdiRRRVSAALDKV----GLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2681003857 161 EILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGSTKTE 226
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-218 |
4.38e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 74.33 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIyIKGQqvemlSPKAAVMQGIGMVHQHF 90
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT-----APLAEAREDTRLMFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 91 KLVKSFTVAENIILGMKdmGLLYDQ--RKIEA-QIEQFCNQYgmcidPAAkvwqLTLGEQQRVEIIKALFRGAEILILDE 167
Cdd:PRK11247 91 RLLPWKKVIDNVGLGLK--GQWRDAalQALAAvGLADRANEW-----PAA----LSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2681003857 168 PTA---VLTPQEAKDLYKtlRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK11247 160 PLGaldALTRIEMQDLIE--SLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
25-199 |
4.82e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 73.66 E-value: 4.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVM---QGIGMVHQHFKLVKSFTVAEN 101
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKlraKHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 102 IIL-----GMKDmgllydqRKIEAQIEQFCNQYGMCID----PAakvwQLTLGEQQRVEIIKALFRGAEILILDEPTAVL 172
Cdd:PRK10584 109 VELpallrGESS-------RQSRNGAKALLEQLGLGKRldhlPA----QLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
|
170 180
....*....|....*....|....*...
gi 2681003857 173 TPQEAKDLYKTL-RLMAEQGKAVIVISH 199
Cdd:PRK10584 178 DRQTGDKIADLLfSLNREHGTTLILVTH 205
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-203 |
1.30e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 75.82 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFPGVV--ANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQqvemlspkaAVMQGI 83
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK---------SILTNI 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 84 GMVHQHFKLVKSFTVAENIILGMKDMGLLYDQRKIEA-QIEQFCN----QYGMCIDPAAKVWQLTLGEQQRVEIIKALFR 158
Cdd:TIGR01257 2008 SDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAeEIEKVANwsiqSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2681003857 159 GAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSE 203
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEE 2132
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
10-240 |
1.32e-14 |
|
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: 74.37 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 10 VNVTKRFPGVVANdhVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQqvemlspkaaVMQ-------- 81
Cdd:COG4148 5 VDFRLRRGGFTLD--VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE----------VLQdsargifl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 82 -----GIGMVHQHFKLVKSFTVAENIILGMKDMGLLYDQRKIEAQIEQFcnqyGmcIDP--AAKVWQLTLGEQQRVEIIK 154
Cdd:COG4148 73 pphrrRIGYVFQEARLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELL----G--IGHllDRRPATLSGGERQRVAIGR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 155 ALFRGAEILILDEPTAVLtPQEAK-DLYKTL-RLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGSTKT-ELASEE 231
Cdd:COG4148 147 ALLSSPRLLLMDEPLAAL-DLARKaEILPYLeRLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLaEVLSRP 225
|
....*....
gi 2681003857 232 ELTRWMVGR 240
Cdd:COG4148 226 DLLPLAGGE 234
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
7-217 |
1.34e-14 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 72.71 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTL------MSILTGLYRPdEGEIYIKGQQVemLSPKAAVM 80
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLlrslnrMNDLVPGVRI-EGKVLFDGQDI--YDKKIDVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 81 Q---GIGMVHQHFKLVkSFTVAENIILGMKDMGLLyDQRKIEAQIEQFCNQygmcidpaAKVWQ------------LTLG 145
Cdd:TIGR00972 79 ElrrRVGMVFQKPNPF-PMSIYDNIAYGPRLHGIK-DKKELDEIVEESLKK--------AALWDevkdrlhdsalgLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2681003857 146 EQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIViSHKLSEVLEGTDKISVLRGG 217
Cdd:TIGR00972 149 QQQRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIV-THNMQQAARISDRTAFFYDG 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-240 |
1.83e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 72.77 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQ---------QVEMLSPKAAVmqgiGMVHQHFKLVKS 95
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkdifQIDAIKLRKEV----GMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 96 FTVAENIILGMKDMGLlYDQRKIEAQIEQFCNQYGMCID-------PAAkvwQLTLGEQQRVEIIKALFRGAEILILDEP 168
Cdd:PRK14246 105 LSIYDNIAYPLKSHGI-KEKREIKKIVEECLRKVGLWKEvydrlnsPAS---QLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2681003857 169 TAVLTPQEAKDLYKTLRLMAEQgKAVIVISHKLSEVLEGTDKISVLRGGK--PAGSTKTELAS-EEELT-RWMVGR 240
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGElvEWGSSNEIFTSpKNELTeKYVIGR 255
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
24-244 |
1.95e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 73.13 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 24 HVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIkGQQVEMLSPKA----AVMQGIGMV-----HQHFKLvk 94
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNkklkPLRKKVGIVfqfpeHQLFEE-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 95 sfTVAENIILGMKDMGLlyDQRKIEAQIEQFCNQYGMCIDPAAKV-WQLTLGEQQRVEIIKALFRGAEILILDEPTAVLT 173
Cdd:PRK13634 102 --TVEKDICFGPMNFGV--SEEDAKQKAREMIELVGLPEELLARSpFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2681003857 174 PQEAKDLYKTL-RLMAEQGKAVIVISHKLSEVLEGTDKISVLRGG--KPAGSTKTELASEEELTRWmvGRNVPK 244
Cdd:PRK13634 178 PKGRKEMMEMFyKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGtvFLQGTPREIFADPDELEAI--GLDLPE 249
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
8-199 |
2.24e-14 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 74.45 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 8 QMVNVTKRFPGVVANDH-----VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPkAAVMQG 82
Cdd:COG4615 329 ELRGVTYRYPGEDGDEGftlgpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNR-EAYRQL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 83 IGMVHQHFKLVKSFtvaeniiLGMKDMGLlydqrkiEAQIEQFCNQYGMcidpAAKV---------WQLTLGEQQRVEII 153
Cdd:COG4615 408 FSAVFSDFHLFDRL-------LGLDGEAD-------PARARELLERLEL----DHKVsvedgrfstTDLSQGQRKRLALL 469
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2681003857 154 KALFRGAEILILDEPTAVLTPQEAKDLYKTL--RLMAeQGKAVIVISH 199
Cdd:COG4615 470 VALLEDRPILVFDEWAADQDPEFRRVFYTELlpELKA-RGKTVIAISH 516
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-220 |
2.37e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 74.70 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPD---EGEIYIKGQQVEmlspkAAVMQGI-GMVHQHFKLVKSFTVAE 100
Cdd:TIGR00955 44 VSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPID-----AKEMRAIsAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 101 N-IILGMKDMGLLYDQRKIEAQIEQFCNQYGM--C----IDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLT 173
Cdd:TIGR00955 119 HlMFQAHLRMPRRVTKKEKRERVDEVLQALGLrkCantrIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2681003857 174 PQEAKDLYKTLRLMAEQGKAVIVISHK-LSEVLEGTDKISVLRGGKPA 220
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVA 246
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
23-218 |
2.38e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.41 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEML--SPKAAVMQGIGMVHQH-FKLVKS-FTV 98
Cdd:PRK10419 29 NNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnrAQRKAFRRDIQMVFQDsISAVNPrKTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 99 AENIILGMKDMGLLyDQRKIEAQIEQFCNQYGMCIDPAAKV-WQLTLGEQQRVEIIKALFRGAEILILDEptAV----LT 173
Cdd:PRK10419 109 REIIREPLRHLLSL-DKAERLARASEMLRAVDLDDSVLDKRpPQLSGGQLQRVCLARALAVEPKLLILDE--AVsnldLV 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2681003857 174 PQ-EAKDLYKTLRlmAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK10419 186 LQaGVIRLLKKLQ--QQFGTACLFITHDLRLVERFCQRVMVMDNGQ 229
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-212 |
2.48e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 71.67 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 1 MSAIPMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVM 80
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 81 QgigmVHQHFKLVKSF--TVAENIILGMKDMGLLYDQRKIEAQIEQFCNQYGMCIDPAAkvwQLTLGEQQRVEIIKALFR 158
Cdd:PRK10247 82 Q----VSYCAQTPTLFgdTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIA---ELSGGEKQRISLIRNLQF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2681003857 159 GAEILILDEPTAVLTPQEAKDLYKTL-RLMAEQGKAVIVISHKLSEVLEGTDKIS 212
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIhRYVREQNIAVLWVTHDKDEINHADKVIT 209
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
11-199 |
3.07e-14 |
|
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: 74.05 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPGVvandhvSLTIEAGQIH-----GLLGENGAGKSTLMSILTGLYRPDEGEI-----------YIKGQQvEMLs 74
Cdd:COG1245 346 DLTKSYGGF------SLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVdedlkisykpqYISPDY-DGT- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 75 pkaaVMQGIGMVHQHfKLVKSFTVAEnIIlgmKDMGL--LYDQRkieaqieqfcnqygmcidpaakVWQLTLGEQQRVEI 152
Cdd:COG1245 418 ----VEEFLRSANTD-DFGSSYYKTE-II---KPLGLekLLDKN----------------------VKDLSGGELQRVAI 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2681003857 153 IKALFRGAEILILDEPTAVLTPQEAKDLYKTL-RLMAEQGKAVIVISH 199
Cdd:COG1245 467 AACLSRDADLYLLDEPSAHLDVEQRLAVAKAIrRFAENRGKTAMVVDH 514
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
5-214 |
3.32e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.68 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIyikgQQVEMLSpkaavmqgIG 84
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----KRNGKLR--------IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 85 MVHQ--HFKLVKSFTVAENIIL--GMKDMGLLYDQRKIEAQ--IEQfcnqygmcidPAAKvwqLTLGEQQRVEIIKALFR 158
Cdd:PRK09544 71 YVPQklYLDTTLPLTVNRFLRLrpGTKKEDILPALKRVQAGhlIDA----------PMQK---LSGGETQRVLLARALLN 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2681003857 159 GAEILILDEPTAVLTPQEAKDLYKTL-RLMAEQGKAVIVISHKLSEVLEGTDKISVL 214
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNGQVALYDLIdQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
23-218 |
6.44e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.17 E-value: 6.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKaAVMQGIGMVHQHFKLVKSFTVAENI 102
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASK-EVARRIGLLAQNATTPGDITVQELV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 103 ILGMKDMGLLYD--QRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDL 180
Cdd:PRK10253 103 ARGRYPHQPLFTrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 2681003857 181 YKTL-RLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK10253 183 LELLsELNREKGYTLAAVLHDLNQACRYASHLIALREGK 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
7-230 |
6.80e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.07 E-value: 6.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRfPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEmlspKAAVMQGIGMV 86
Cdd:PRK15056 9 VNDVTVTWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 87 HQHFKLVKSFTV-AENIILGMK--DMGLL-----YDQRKIEAQIEQFcnqyGMCIDPAAKVWQLTLGEQQRVEIIKALFR 158
Cdd:PRK15056 84 PQSEEVDWSFPVlVEDVVMMGRygHMGWLrrakkRDRQIVTAALARV----DMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2681003857 159 GAEILILDEP-TAVLTPQEAKdLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPA-GSTKTELASE 230
Cdd:PRK15056 160 QGQVILLDEPfTGVDVKTEAR-IISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLAsGPTETTFTAE 232
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-218 |
7.13e-14 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 71.02 E-value: 7.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEI-YI--KGQQVEMLSPKAAVMQ 81
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtYImrSGAELELYQLSEAERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 82 GI-----GMVHQHFKLVKSFTVAENIILGMKDMGLlyDQR---KIEAQIEQFCNQygMCIDPAA---KVWQLTLGEQQRV 150
Cdd:TIGR02323 82 RLmrtewGFVHQNPRDGLRMRVSAGANIGERLMAI--GARhygNIRATAQDWLEE--VEIDPTRiddLPRAFSGGMQQRL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2681003857 151 EIIKALFRGAEILILDEPTAVL-TPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:TIGR02323 158 QIARNLVTRPRLVFMDEPTGGLdVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGR 226
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-168 |
7.99e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 71.80 E-value: 7.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFPGVV-ANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAavmQGIG 84
Cdd:PRK11650 3 GLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD---RDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 85 MVHQHFKLVKSFTVAENIILGMKDMGLlyDQRKIEAQIEQfcnqygmcidpAAKVW-----------QLTLGEQQRVEII 153
Cdd:PRK11650 80 MVFQNYALYPHMSVRENMAYGLKIRGM--PKAEIEERVAE-----------AARILeleplldrkprELSGGQRQRVAMG 146
|
170
....*....|....*
gi 2681003857 154 KALFRGAEILILDEP 168
Cdd:PRK11650 147 RAIVREPAVFLFDEP 161
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
23-200 |
1.05e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.21 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEmlSPKAAVMQGIGMVHQHFKLVKSFTVAENI 102
Cdd:PRK13540 18 QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK--KDLCTYQKQLCFVGHRSGINPYLTLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 103 ilgmkdmglLYD--QRKIEAQIEQFCNQY--GMCIDPAAKVwqLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAK 178
Cdd:PRK13540 96 ---------LYDihFSPGAVGITELCRLFslEHLIDYPCGL--LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|..
gi 2681003857 179 DLYKTLRLMAEQGKAVIVISHK 200
Cdd:PRK13540 165 TIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-235 |
1.72e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 71.68 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQGIGMVHQ-------HFKLVKSF- 96
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEerrstgiYAYLDIGFn 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 97 TVAENIILGMKDMGLLyDQRKIEAQIEQFCNqyGMCID-PAAK--VWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLT 173
Cdd:PRK10982 347 SLISNIRNYKNKVGLL-DNSRMKSDTQWVID--SMRVKtPGHRtqIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2681003857 174 PQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGSTKTELASEEELTR 235
Cdd:PRK10982 424 VGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQNEILR 485
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-199 |
2.54e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.29 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPK-AAVMQGIGmvhqHFKLVKS-FTVAE 100
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyHQDLLYLG----HQPGIKTeLTALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 101 NIILGMKDMGlLYDQRKIEAQIEQFcNQYGMCIDPAAkvwQLTLGEQQRVeiikALFR----GAEILILDEPTAVLTPQE 176
Cdd:PRK13538 94 NLRFYQRLHG-PGDDEALWEALAQV-GLAGFEDVPVR---QLSAGQQRRV----ALARlwltRAPLWILDEPFTAIDKQG 164
|
170 180
....*....|....*....|...
gi 2681003857 177 AKDLYKTLRLMAEQGKAVIVISH 199
Cdd:PRK13538 165 VARLEALLAQHAEQGGMVILTTH 187
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-199 |
3.10e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.99 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 26 SLTIEAGQIH-----GLLGENGAGKSTLMSILTGLYRPDEGEI-----------YIKGQQ---VEMLSPKAAVmqgigmv 86
Cdd:PRK13409 354 SLEVEGGEIYegeviGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpelkisykpqYIKPDYdgtVEDLLRSITD------- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 87 hqhfKLVKSFTVAEnIIlgmKDMGL--LYDQRkieaqieqfcnqygmcidpaakVWQLTLGEQQRVEIIKALFRGAEILI 164
Cdd:PRK13409 427 ----DLGSSYYKSE-II---KPLQLerLLDKN----------------------VKDLSGGELQRVAIAACLSRDADLYL 476
|
170 180 190
....*....|....*....|....*....|....*.
gi 2681003857 165 LDEPTAVLTPQEAKDLYKTLRLMAE-QGKAVIVISH 199
Cdd:PRK13409 477 LDEPSAHLDVEQRLAVAKAIRRIAEeREATALVVDH 512
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-229 |
3.26e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 69.93 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 19 VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPD----EGEIYIKGQQVEMLSPKA--AVM-QGIGMVHQHFK 91
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRErrKIIgREIAMIFQEPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 92 --LVKSFTVAENIILGMKDMGL------LYDQRKIEAqIE----------QFC-NQYgmcidPaakvWQLTLGEQQRVEI 152
Cdd:COG4170 100 scLDPSAKIGDQLIEAIPSWTFkgkwwqRFKWRKKRA-IEllhrvgikdhKDImNSY-----P----HELTEGECQKVMI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 153 IKALFRGAEILILDEPTAVLtpqEAKDLYKTLRLMAE----QGKAVIVISHKLSEVLEGTDKISVLRGGK--PAGSTKTE 226
Cdd:COG4170 170 AMAIANQPRLLIADEPTNAM---ESTTQAQIFRLLARlnqlQGTSILLISHDLESISQWADTITVLYCGQtvESGPTEQI 246
|
...
gi 2681003857 227 LAS 229
Cdd:COG4170 247 LKS 249
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
24-217 |
3.45e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 70.90 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 24 HVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQ-----QVEMLSPKAAVmqgigmVHQHFKLVkSFTV 98
Cdd:PRK10789 333 NVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIpltklQLDSWRSRLAV------VSQTPFLF-SDTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 99 AENIILGMKDMgllyDQRKIEaQIEQFCNQY--------GMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTA 170
Cdd:PRK10789 406 ANNIALGRPDA----TQQEIE-HVARLASVHddilrlpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2681003857 171 VLTPQEAKDLYKTLRLMAeQGKAVIVISHKLSeVLEGTDKISVLRGG 217
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWG-EGRTVIISAHRLS-ALTEASEILVMQHG 525
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-298 |
5.90e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.12 E-value: 5.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKS-TLMSILTGLYRPD----EGEIYIKGQqvEMLSPKAAVMQG-----IGMVHQhfkl 92
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGE--SLLHASEQTLRGvrgnkIAMIFQ---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 93 vksftvaeniilgmKDMGLLYDQRKIEAQI-EQFCNQYGM-----------CID-----PAAKVW-----QLTLGEQQRV 150
Cdd:PRK15134 100 --------------EPMVSLNPLHTLEKQLyEVLSLHRGMrreaargeilnCLDrvgirQAAKRLtdyphQLSGGERQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 151 EIIKALFRGAEILILDEPTAVLTPQEAKDLYKTLR-LMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK----------- 218
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLReLQQELNMGLLFITHNLSIVRKLADRVAVMQNGRcveqnraatlf 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 219 --PAGS-TKTELASEEEltrwmvGRNVPkqldrtVTEPGAVVLELDN--ISCLNNRG--------QIAVRHASLCIRAGE 285
Cdd:PRK15134 246 saPTHPyTQKLLNSEPS------GDPVP------LPEPASPLLDVEQlqVAFPIRKGilkrtvdhNVVVKNISFTLRPGE 313
|
330
....*....|...
gi 2681003857 286 IVGIAGVAGNGQT 298
Cdd:PRK15134 314 TLGLVGESGSGKS 326
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
25-243 |
6.58e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 68.58 E-value: 6.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMlSPKAAVMQGIGMVHQH--FKLVKSfTVAENI 102
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA-ENVWNLRRKIGMVFQNpdNQFVGA-TVEDDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 103 ILGMKDMGLlyDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYK 182
Cdd:PRK13642 104 AFGMENQGI--PREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMR 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2681003857 183 TLRLMAEQGK-AVIVISHKLSEVlEGTDKISVLRGG---KPAGSTKTELASEEELTrwmVGRNVP 243
Cdd:PRK13642 182 VIHEIKEKYQlTVLSITHDLDEA-ASSDRILVMKAGeiiKEAAPSELFATSEDMVE---IGLDVP 242
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-199 |
6.98e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.21 E-value: 6.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPkAAVMQGIGmvHQHFklVK-SFTVAENI- 102
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV-AEACHYLG--HRNA--MKpALTVAENLe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 103 ----ILGMKDMGllydqrkIEAQIEQFcnQYGMCIDPAAKVwqLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPqEAK 178
Cdd:PRK13539 96 fwaaFLGGEELD-------IAAALEAV--GLAPLAHLPFGY--LSAGQKRRVALARLLVSNRPIWILDEPTAALDA-AAV 163
|
170 180
....*....|....*....|....
gi 2681003857 179 DLYktLRLMA---EQGKAVIVISH 199
Cdd:PRK13539 164 ALF--AELIRahlAQGGIVIAATH 185
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-169 |
7.13e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 69.76 E-value: 7.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 8 QMVNVTKRFPG--VVANDhVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEiyikgqqvemlspkAAVMQG--I 83
Cdd:PRK11819 8 TMNRVSKVVPPkkQILKD-ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE--------------ARPAPGikV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 84 GMVHQHFKLVKSFTVAENIILG----------------------------MKDMGLLydQRKIEA--------QIEQfcn 127
Cdd:PRK11819 73 GYLPQEPQLDPEKTVRENVEEGvaevkaaldrfneiyaayaepdadfdalAAEQGEL--QEIIDAadawdldsQLEI--- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2681003857 128 qyGM----CIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPT 169
Cdd:PRK11819 148 --AMdalrCPPWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPT 191
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-169 |
8.28e-13 |
|
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: 69.58 E-value: 8.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 8 QMVNVTKRFPG---VVANdhVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEiyikgqqvemlspkAAVMQGI- 83
Cdd:TIGR03719 6 TMNRVSKVVPPkkeILKD--ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE--------------ARPQPGIk 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 84 -GMVHQHFKLVKSFTVAENIILGMKDM----------------------GLLYDQRKIEAQIEQfCNQYGM--------- 131
Cdd:TIGR03719 70 vGYLPQEPQLDPTKTVRENVEEGVAEIkdaldrfneisakyaepdadfdKLAAEQAELQEIIDA-ADAWDLdsqleiamd 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2681003857 132 ---CIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPT 169
Cdd:TIGR03719 149 alrCPPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPT 189
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
23-218 |
9.78e-13 |
|
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: 66.50 E-value: 9.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGlyRPD----EGEIYIKGQQVEMLSPKaavmqGIGMVHQHFKLVKSFTV 98
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTagviTGEILINGRPLDKNFQR-----STGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 99 AENIILGMKDMGLLYDQRKIeaqieqfcnqygmcidpaakvwqLTLGeqqrVEiikaLFRGAEILILDEPTAVLTPQEAK 178
Cdd:cd03232 97 REALRFSALLRGLSVEQRKR-----------------------LTIG----VE----LAAKPSILFLDEPTSGLDSQAAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2681003857 179 DLYKTLRLMAEQGKAVIVISHKLSEVL-EGTDKISVL-RGGK 218
Cdd:cd03232 146 NIVRFLKKLADSGQAILCTIHQPSASIfEKFDRLLLLkRGGK 187
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-199 |
1.01e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 67.43 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 26 SLTIEAG-----QIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVemlSPKAavmqgigmvhQHFKLVKSFTVAE 100
Cdd:cd03237 14 TLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV---SYKP----------QYIKADYEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 101 NIILGMKDMGlLYDQRKIEA----QIEQFCNQygmcidpaaKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQE 176
Cdd:cd03237 81 LLSSITKDFY-THPYFKTEIakplQIEQILDR---------EVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQ 150
|
170 180
....*....|....*....|....
gi 2681003857 177 AKDLYKTLRLMAEQGKA-VIVISH 199
Cdd:cd03237 151 RLMASKVIRRFAENNEKtAFVVEH 174
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-239 |
1.80e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.04 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 2 SAIPMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGL------YRPdEGEIYIKGQQVEMLSP 75
Cdd:PRK14271 17 AAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkvsgYRY-SGDVLLGGRSIFNYRD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 76 KAAVMQGIGMVHQHFKLVkSFTVAENIILGMKDMGLLyDQRKIEAQIEQFCNQYGMCIDPAAKV----WQLTLGEQQRVE 151
Cdd:PRK14271 96 VLEFRRRVGMLFQRPNPF-PMSIMDNVLAGVRAHKLV-PRKEFRGVAQARLTEVGLWDAVKDRLsdspFRLSGGQQQLLC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 152 IIKALFRGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQgKAVIVISHKLSEVLEGTDKISVLRGGK--PAGSTKTELAS 229
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRlvEEGPTEQLFSS 252
|
250
....*....|..
gi 2681003857 230 EE--ELTRWMVG 239
Cdd:PRK14271 253 PKhaETARYVAG 264
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
11-199 |
2.70e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.22 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 11 NVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIkGQQVEM---------LSPKAAVMQ 81
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVKLayvdqsrdaLDPNKTVWE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 82 GI--GmvhqhfklvksftvAENIILGMKDM-GLLY---------DQRKieaqieqfcnqygmcidpaaKVWQLTLGEQQR 149
Cdd:PRK11819 408 EIsgG--------------LDIIKVGNREIpSRAYvgrfnfkggDQQK--------------------KVGVLSGGERNR 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2681003857 150 VEIIKALFRGAEILILDEPTavltpqeaKDL-YKTLR-----LMAEQGKAViVISH 199
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPT--------NDLdVETLRaleeaLLEFPGCAV-VISH 500
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-218 |
2.91e-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: 67.79 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 2 SAIPMVQMVNVTKRFPG-----------VVANDHVSLTIEAGQIHGLLGENGAGKSTL-MSILtGLYrPDEGEIYIKGQQ 69
Cdd:COG4172 271 DAPPLLEARDLKVWFPIkrglfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL-RLI-PSEGEIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 70 VEMLSPKA-----AVMQgigMVHQH-FklvKSF----TVAENIILGMK--DMGLLYDQRkiEAQIEQFCNQYGMciDPAA 137
Cdd:COG4172 349 LDGLSRRAlrplrRRMQ---VVFQDpF---GSLsprmTVGQIIAEGLRvhGPGLSAAER--RARVAEALEEVGL--DPAA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 138 KvW----QLTLGEQQRVEIIKALFRGAEILILDEPTAVL--TPQeaKDLYKTLR-LMAEQGKAVIVISHKLSEVLEGTDK 210
Cdd:COG4172 419 R-HryphEFSGGQRQRIAIARALILEPKLLVLDEPTSALdvSVQ--AQILDLLRdLQREHGLAYLFISHDLAVVRALAHR 495
|
....*...
gi 2681003857 211 ISVLRGGK 218
Cdd:COG4172 496 VMVMKDGK 503
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
25-225 |
3.48e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 65.95 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILT--GLYRPD---EGEIYIKGQQVemLSPKAAVMQ---GIGMVHQH---Fklv 93
Cdd:PRK14239 24 VSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNI--YSPRTDTVDlrkEIGMVFQQpnpF--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 94 kSFTVAENIILGMKDMGLlYDQRKIEAQIEQFCNQygmcidpaAKVWQ------------LTLGEQQRVEIIKALFRGAE 161
Cdd:PRK14239 99 -PMSIYENVVYGLRLKGI-KDKQVLDEAVEKSLKG--------ASIWDevkdrlhdsalgLSGGQQQRVCIARVLATSPK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2681003857 162 ILILDEPTAVLTPQEAKDLYKTLRLMAEQgKAVIVISHKLSEVLEGTDKISVLRGGK--PAGSTKT 225
Cdd:PRK14239 169 IILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDliEYNDTKQ 233
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-311 |
6.84e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 66.73 E-value: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 28 TIEAGQIHGLLGENGAGKSTLMSILTGLYRPD------------------------------EGEI--YIKGQQVEMLsP 75
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNlgdydeepswdevlkrfrgtelqdyfkklaNGEIkvAHKPQYVDLI-P 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 76 KaaVMQGigmvhqhfklvksfTVAEniilgmkdmgLL--YDQRKIEAQIEQFCNqygmcIDPA--AKVWQLTLGEQQRVE 151
Cdd:COG1245 174 K--VFKG--------------TVRE----------LLekVDERGKLDELAEKLG-----LENIldRDISELSGGELQRVA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 152 IIKALFRGAEILILDEPTAVLtpqeakDLY------KTLRLMAEQGKAVIVISHKLSeVLEG-TDKISVLRgGKPAG--- 221
Cdd:COG1245 223 IAAALLRDADFYFFDEPSSYL------DIYqrlnvaRLIRELAEEGKYVLVVEHDLA-ILDYlADYVHILY-GEPGVygv 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 222 -----STKTE--------LASEeeltrwmvgrNV---PKQLDRTVTEP-----GAVVLELDNISCLNNRGQIAVRHASlc 280
Cdd:COG1245 295 vskpkSVRVGinqyldgyLPEE----------NVrirDEPIEFEVHAPrrekeEETLVEYPDLTKSYGGFSLEVEGGE-- 362
|
330 340 350
....*....|....*....|....*....|..
gi 2681003857 281 IRAGEIVGIAGVAGNGQTELAEVVAG-LRPVE 311
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGvLKPDE 394
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-199 |
1.02e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.82 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLY--RPDEGEIYIKGQQvemLSPKAAVMQGIGMvhqhfklVKSFTVAE 100
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQ---FGREASLIDAIGR-------KGDFKDAV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 101 NIIlgmKDMGLlydqrkieaqieqfcnqygmcIDPA---AKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEA 177
Cdd:COG2401 117 ELL---NAVGL---------------------SDAVlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180
....*....|....*....|...
gi 2681003857 178 KDLYKTLRLMA-EQGKAVIVISH 199
Cdd:COG2401 173 KRVARNLQKLArRAGITLVVATH 195
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
7-233 |
1.31e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.59 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRF---PGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYR-PDEGEIYIKGQQVEMLSPKAAVM-- 80
Cdd:PTZ00265 1166 IEIMDVNFRYisrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlKNDHHIVFKNEHTNDMTNEQDYQgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 81 --QGIGMVH-QHFKLVK----------------------------------------------SFTVAENIILGMKDMGL 111
Cdd:PTZ00265 1246 eeQNVGMKNvNEFSLTKeggsgedstvfknsgkilldgvdicdynlkdlrnlfsivsqepmlfNMSIYENIKFGKEDATR 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 112 LYDQR-----KIEAQIEQFCNQYGMCIDPAAKvwQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYKTLRL 186
Cdd:PTZ00265 1326 EDVKRackfaAIDEFIESLPNKYDTNVGPYGK--SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1403
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2681003857 187 MAEQG-KAVIVISHKLSEVlEGTDKISVLRGGKPAGSTKTELASEEEL 233
Cdd:PTZ00265 1404 IKDKAdKTIITIAHRIASI-KRSDKIVVFNNPDRTGSFVQAHGTHEEL 1450
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
7-218 |
1.80e-11 |
|
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: 62.87 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPGVVANDH-----VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGqqvemlspkaavmq 81
Cdd:cd03250 1 ISVEDASFTWDSGEQETSftlkdINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 82 GIGMVHQhFKLVKSFTVAENIILGMKdmgllYDQRKIEAQIEQfCnqygmCIDPAAKVWQ-----------LTL--GEQQ 148
Cdd:cd03250 67 SIAYVSQ-EPWIQNGTIRENILFGKP-----FDEERYEKVIKA-C-----ALEPDLEILPdgdlteigekgINLsgGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2681003857 149 RVEIIKALFRGAEILILDEPTAVLTPQEAKDLY-KTLRLMAEQGKAVIVISHKLsEVLEGTDKISVLRGGK 218
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-206 |
2.15e-11 |
|
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: 65.70 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPdEGEIYIKGqqvemLSPKAAVMQ----GIGMVHQH-FKLVKSFTVA 99
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDG-----VSWNSVTLQtwrkAFGVIPQKvFIFSGTFRKN 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 100 ENIILGMKDMGL--LYDQRKIEAQIEQFCNQYGMCIDPAAKVwqLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEA 177
Cdd:TIGR01271 1312 LDPYEQWSDEEIwkVAEEVGLKSVIEQFPDKLDFVLVDGGYV--LSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTL 1389
|
170 180
....*....|....*....|....*....
gi 2681003857 178 KDLYKTLRlMAEQGKAVIVISHKLSEVLE 206
Cdd:TIGR01271 1390 QIIRKTLK-QSFSNCTVILSEHRVEALLE 1417
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-169 |
3.36e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.97 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQV----EMLSPKAA-------VMQGIGMVHQHFK 91
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIvarlQQDPPRNVegtvydfVAEGIEEQAEYLK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 92 -------LVKSFTVAENIilgmKDMGLLYDQR------KIEAQIEQFCNQYGMciDPAAKVWQLTLGEQQRVEIIKALFR 158
Cdd:PRK11147 100 ryhdishLVETDPSEKNL----NELAKLQEQLdhhnlwQLENRINEVLAQLGL--DPDAALSSLSGGWLRKAALGRALVS 173
|
170
....*....|.
gi 2681003857 159 GAEILILDEPT 169
Cdd:PRK11147 174 NPDVLLLDEPT 184
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
23-199 |
4.35e-11 |
|
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: 61.02 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYI-KGQQVEMLSPKAAVMQGigmvhqhfklvksfTVAEN 101
Cdd:cd03223 18 KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDLLFLPQRPYLPLG--------------TLREQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 102 IILgmkdmgllydqrkieaqieqfcnqygmcidPAAKVwqLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLY 181
Cdd:cd03223 84 LIY------------------------------PWDDV--LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
170
....*....|....*...
gi 2681003857 182 KTLRlmaEQGKAVIVISH 199
Cdd:cd03223 132 QLLK---ELGITVISVGH 146
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-204 |
4.36e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 64.53 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 21 ANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGqqvemlspkAAVMQGIGMvhqhfKLVKSFTVAE 100
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG---------SAALIAISS-----GLNGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 101 NIILGMKDMGLLYDQRK------IE-AQIEQFCNQygmcidpaaKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLT 173
Cdd:PRK13545 105 NIELKGLMMGLTKEKIKeiipeiIEfADIGKFIYQ---------PVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
170 180 190
....*....|....*....|....*....|.
gi 2681003857 174 PQEAKDLYKTLRLMAEQGKAVIVISHKLSEV 204
Cdd:PRK13545 176 QTFTKKCLDKMNEFKEQGKTIFFISHSLSQV 206
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-240 |
4.52e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.55 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPD-----EGEIYIKGQQVemLSPKA---AVMQGIGMVHQHFKLVKSF 96
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNI--YSPDVdpiEVRREVGMVFQYPNPFPHL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 97 TVAENIILGMKDMGLLYDQRKIEAQIEQFCNQygmcidpaAKVW------------QLTLGEQQRVEIIKALFRGAEILI 164
Cdd:PRK14267 101 TIYDNVAIGVKLNGLVKSKKELDERVEWALKK--------AALWdevkdrlndypsNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 165 LDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIViSHKLSEVLEGTDKISVLRGGK--PAGSTKTELAS-EEELT-RWMVGR 240
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEYTIVLV-THSPAQAARVSDYVAFLYLGKliEVGPTRKVFENpEHELTeKYVTGA 251
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
5-225 |
4.96e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 63.45 E-value: 4.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFP---G-------VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVeMLS 74
Cdd:PRK11308 4 PLLQAIDLKKHYPvkrGlfkperlVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDL-LKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 75 PKAAVM---QGIGMVHQHfklvksftvaeniilgmkDMGLLYDQRKIEAQIEQ--FCNQYGMCIDPAAKVWQL------- 142
Cdd:PRK11308 83 DPEAQKllrQKIQIVFQN------------------PYGSLNPRKKVGQILEEplLINTSLSAAERREKALAMmakvglr 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 143 -----------TLGEQQRVEIIKALFRGAEILILDEPTAVLtpqeakDLY---KTLRLMA----EQGKAVIVISHKLSEV 204
Cdd:PRK11308 145 pehydryphmfSGGQRQRIAIARALMLDPDVVVADEPVSAL------DVSvqaQVLNLMMdlqqELGLSYVFISHDLSVV 218
|
250 260
....*....|....*....|...
gi 2681003857 205 LEGTDKISVLRGGKPA--GSTKT 225
Cdd:PRK11308 219 EHIADEVMVMYLGRCVekGTKEQ 241
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-218 |
5.26e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.64 E-value: 5.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 1 MSAIPMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIK---GQQVEMLSPKA 77
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRmrdGQLRDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 78 AVMQGI-----GMVHQHFK--LVKSFTVAENI-----ILGMKDMGLLYDQ-----RKIEAQIEQfcnqygmcID--PAAk 138
Cdd:PRK11701 81 AERRRLlrtewGFVHQHPRdgLRMQVSAGGNIgerlmAVGARHYGDIRATagdwlERVEIDAAR--------IDdlPTT- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 139 vwqLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYKTLR-LMAEQGKAVIVISHKLSEVLEGTDKISVLRGG 217
Cdd:PRK11701 152 ---FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRgLVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
.
gi 2681003857 218 K 218
Cdd:PRK11701 229 R 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-311 |
5.48e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 5.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 28 TIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEI-----------YIKGQQV----EMLSPKAA-VMQGIGMVHQHFK 91
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevlkRFRGTELqnyfKKLYNGEIkVVHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 92 LVKSfTVAEniilgmkdmgLL--YDQRKIeaqIEQFCNQYGMcidpaAKVW-----QLTLGEQQRVEIIKALFRGAEILI 164
Cdd:PRK13409 175 VFKG-KVRE----------LLkkVDERGK---LDEVVERLGL-----ENILdrdisELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 165 LDEPTAVLtpqeakDLY------KTLRLMAEqGKAVIVISHKLSeVLEG-TDKISVLRgGKPAG--------STKT---- 225
Cdd:PRK13409 236 FDEPTSYL------DIRqrlnvaRLIRELAE-GKYVLVVEHDLA-VLDYlADNVHIAY-GEPGAygvvskpkGVRVgine 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 226 ----ELASEeeltrwmvgrNV---PKQLDRTVTEP-----GAVVLELDNISCLNNRGQIAVRHASlcIRAGEIVGIAGVA 293
Cdd:PRK13409 307 ylkgYLPEE----------NMrirPEPIEFEERPPrdeseRETLVEYPDLTKKLGDFSLEVEGGE--IYEGEVIGIVGPN 374
|
330
....*....|....*....
gi 2681003857 294 GNGQTELAEVVAG-LRPVE 311
Cdd:PRK13409 375 GIGKTTFAKLLAGvLKPDE 393
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-216 |
5.70e-11 |
|
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: 62.38 E-value: 5.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 32 GQIHGLLGENGAGKSTLMSILTGLYRPDEG---------EI--YIKGQQVE-----MLSPKAAVMQGIGMVHQHFKLVKS 95
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEIldEFRGSELQnyftkLLEGDVKVIVKPQYVDLIPKAVKG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 96 fTVAENII----LGMKDmgLLYDQRKIEAQIEQfcnqygmcidpaaKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAV 171
Cdd:cd03236 106 -KVGELLKkkdeRGKLD--ELVDQLELRHVLDR-------------NIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2681003857 172 LTPQEAKDLYKTLRLMAEQGKAVIVISHKLSeVLEG-TDKISVLRG 216
Cdd:cd03236 170 LDIKQRLNAARLIRELAEDDNYVLVVEHDLA-VLDYlSDYIHCLYG 214
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
23-206 |
5.78e-11 |
|
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: 62.56 E-value: 5.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPdEGEIYIKGQQVEMLsPKAAVMQGIGMVHQhfklvKSFTVAENI 102
Cdd:cd03289 21 ENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSV-PLQKWRKAFGVIPQ-----KVFIFSGTF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 103 ILGMKDMGLLYDQR--------KIEAQIEQFCNQ------YGMCIdpaakvwqLTLGEQQRVEIIKALFRGAEILILDEP 168
Cdd:cd03289 94 RKNLDPYGKWSDEEiwkvaeevGLKSVIEQFPGQldfvlvDGGCV--------LSHGHKQLMCLARSVLSKAKILLLDEP 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 2681003857 169 TAVLTPQEAKDLYKTLRlMAEQGKAVIVISHKLSEVLE 206
Cdd:cd03289 166 SAHLDPITYQVIRKTLK-QAFADCTVILSEHRIEAMLE 202
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-169 |
6.07e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 64.38 E-value: 6.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQV------EMLSPKAAVM 80
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMadarhrRAVCPRIAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 81 -QGIGmvhqhfK-LVKSFTVAENIilgmkD-MGLLYDQRKIE--AQIEQFCNQYGMC--ID-PAAKvwqLTLGEQQRVEI 152
Cdd:NF033858 82 pQGLG------KnLYPTLSVFENL-----DfFGRLFGQDAAErrRRIDELLRATGLApfADrPAGK---LSGGMKQKLGL 147
|
170
....*....|....*..
gi 2681003857 153 IKALFRGAEILILDEPT 169
Cdd:NF033858 148 CCALIHDPDLLILDEPT 164
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-218 |
6.36e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.96 E-value: 6.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 3 AIPMVQMVNVTKRFPG-------VVANDHV----SLTIEAGQIHGLLGENGAGKSTLMSILTGLYRpDEGEIYIKGQQVE 71
Cdd:PRK15134 272 ASPLLDVEQLQVAFPIrkgilkrTVDHNVVvkniSFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLH 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 72 MLSPKA--AVMQGIGMVHQ--HFKLVKSFTVAENIILGMK--DMGLLYDQRkiEAQIEQFCNQYGMciDPAAK---VWQL 142
Cdd:PRK15134 351 NLNRRQllPVRHRIQVVFQdpNSSLNPRLNVLQIIEEGLRvhQPTLSAAQR--EQQVIAVMEEVGL--DPETRhryPAEF 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2681003857 143 TLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYKTLR-LMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKsLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGE 503
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-238 |
7.89e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.11 E-value: 7.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 19 VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEmLSPKAAVMQGIGMVHQhfKLVKSFTV 98
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSQRIRMIFQ--DPSTSLNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 99 AENI--ILGMK---DMGLLYDQRkiEAQIEQFCNQYGMCIDPAAKV-WQLTLGEQQRVEIIKALFRGAEILILDEPTAVL 172
Cdd:PRK15112 103 RQRIsqILDFPlrlNTDLEPEQR--EKQIIETLRQVGLLPDHASYYpHMLAPGQKQRLGLARALILRPKVIIADEALASL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 173 TPQEAKDLYK-TLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK--PAGSTKTELASE-EELTRWMV 238
Cdd:PRK15112 181 DMSMRSQLINlMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEvvERGSTADVLASPlHELTKRLI 250
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
7-218 |
1.07e-10 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. 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: 213269 [Multi-domain] Cd Length: 207 Bit Score: 60.89 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRF----PGVVANdhVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLsPKAAVMQG 82
Cdd:cd03369 7 IEVENLSVRYapdlPPVLKN--VSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI-PLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 83 IGMVHQHFKLVkSFTVAENiiLGMKDMgllYDQRKIEAqieqfcnqygmcidpAAKVWQ----LTLGEQQRVEIIKALFR 158
Cdd:cd03369 84 LTIIPQDPTLF-SGTIRSN--LDPFDE---YSDEEIYG---------------ALRVSEgglnLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 159 GAEILILDEPTAVLTPQEAKDLYKTLRlMAEQGKAVIVISHKLSEVLEgTDKISVLRGGK 218
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIR-EEFTNSTILTIAHRLRTIID-YDKILVMDAGE 200
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-217 |
1.32e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.39 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGqQVEMLSPKAAVMQGigmvhqhfklvksfTVAENIIL 104
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-RISFSPQTSWIMPG--------------TIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 105 gmkdmGLLYDQRK---------IEAQIEQFCNQYGMCIDPAAKVwqLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQ 175
Cdd:TIGR01271 510 -----GLSYDEYRytsvikacqLEEDIALFPEKDKTVLGEGGIT--LSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2681003857 176 EAKDLYKT--LRLMAEqgKAVIVISHKLsEVLEGTDKISVLRGG 217
Cdd:TIGR01271 583 TEKEIFESclCKLMSN--KTRILVTSKL-EHLKKADKILLLHEG 623
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
25-232 |
3.11e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.04 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTG--LYRPDEGEIYIKGQQVEMLSPKAAVMQGIGMVHQhfklvksFTVAeni 102
Cdd:CHL00131 26 LNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGIFLAFQ-------YPIE--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 103 ILGMKDMGLL---YDQRKIEAQIEQfcnqygmcIDPAA----KVWQLTL------------------GEQQRVEIIKALF 157
Cdd:CHL00131 96 IPGVSNADFLrlaYNSKRKFQGLPE--------LDPLEfleiINEKLKLvgmdpsflsrnvnegfsgGEKKRNEILQMAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2681003857 158 RGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISH--KLSEVLEgTDKISVLRGGKPAGSTKTELASEEE 232
Cdd:CHL00131 168 LDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHyqRLLDYIK-PDYVHVMQNGKIIKTGDAELAKELE 243
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-233 |
3.32e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 60.88 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 21 ANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKA--AVMQGIGMVHQ---------- 88
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwrAVRSDIQMIFQdplaslnprm 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 89 -------------HFKLVKSfTVAENIILGMKDMGLLydqrkieaqiEQFCNQYgmcidPAakvwQLTLGEQQRVEIIKA 155
Cdd:PRK15079 116 tigeiiaeplrtyHPKLSRQ-EVKDRVKAMMLKVGLL----------PNLINRY-----PH----EFSGGQCQRIGIARA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2681003857 156 LFRGAEILILDEPTAVLTPQEAKDLYKTLR-LMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPagstkTELASEEEL 233
Cdd:PRK15079 176 LILEPKLIICDEPVSALDVSIQAQVVNLLQqLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHA-----VELGTYDEV 249
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-289 |
5.33e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 60.20 E-value: 5.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 4 IPMVQMVNVTKRFPG----VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGL-----------YRPDEGEIY---- 64
Cdd:PRK15093 1 MPLLDIRNLTIEFKTsdgwVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnwrvtadrMRFDDIDLLrlsp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 65 -----IKGQQVEM--------LSPKAAV----MQGI------GMVHQHFKLVKSFTVAENIILGMKDmgllydQRKIeaq 121
Cdd:PRK15093 81 rerrkLVGHNVSMifqepqscLDPSERVgrqlMQNIpgwtykGRWWQRFGWRKRRAIELLHRVGIKD------HKDA--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 122 ieqfcnqygMCIDPaakvWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYKTL-RLMAEQGKAVIVISHK 200
Cdd:PRK15093 152 ---------MRSFP----YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLtRLNQNNNTTILLISHD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 201 LSEVLEGTDKISVLRGGKPAGS-TKTELAS------EEELTRWM--VGRNVPKQlDRTVTEPGAV-VLELDNISC-LNNR 269
Cdd:PRK15093 219 LQMLSQWADKINVLYCGQTVETaPSKELVTtphhpyTQALIRAIpdFGSAMPHK-SRLNTLPGAIpLLEHLPIGCrLGPR 297
|
330 340
....*....|....*....|
gi 2681003857 270 GQIAVRHaslCIRAGEIVGI 289
Cdd:PRK15093 298 CPYAQRE---CIETPRLTGA 314
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-217 |
5.38e-10 |
|
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: 59.87 E-value: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGqQVEMLSPKAAVMQGigmvhqhfklvksfTVAENIIL 104
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-RISFSSQFSWIMPG--------------TIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 105 GMKdmgllYDQRK---------IEAQIEQFCNQYGMCIDPAAKVwqLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQ 175
Cdd:cd03291 121 GVS-----YDEYRyksvvkacqLEEDITKFPEKDNTVLGEGGIT--LSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2681003857 176 EAKDLYKT--LRLMAEqgKAVIVISHKLsEVLEGTDKISVLRGG 217
Cdd:cd03291 194 TEKEIFEScvCKLMAN--KTRILVTSKM-EHLKKADKILILHEG 234
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
23-209 |
1.30e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 58.62 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKA--AVMQGIGMVHQHFKLVKSFTVAE 100
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlyTVRKRMSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 101 NIILGMKDMGLLYDQ-------RKIEAqieqfcnqygMCIDPAAKVW--QLTLGEQQRVEIIKALFRGAEILILDEPTAV 171
Cdd:PRK11831 104 NVAYPLREHTQLPAPllhstvmMKLEA----------VGLRGAAKLMpsELSGGMARRAALARAIALEPDLIMFDEPFVG 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 2681003857 172 LTPQEAKDLYKTL-RLMAEQGKAVIVISHKLSEVLEGTD 209
Cdd:PRK11831 174 QDPITMGVLVKLIsELNSALGVTCVVVSHDVPEVLSIAD 212
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-218 |
2.04e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 57.74 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 4 IPMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPdEGEIYIKGQqVEMLSPKA------ 77
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGR-VEFFNQNIyerrvn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 78 --AVMQGIGMVHQHFKLVkSFTVAENIILGMKDMGLlYDQRKIEAQIEQFCNqygmcidpAAKVW------------QLT 143
Cdd:PRK14258 83 lnRLRRQVSMVHPKPNLF-PMSVYDNVAYGVKIVGW-RPKLEIDDIVESALK--------DADLWdeikhkihksalDLS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2681003857 144 LGEQQRVEIIKALFRGAEILILDEPTAVLTP---QEAKDLYKTLRLMAEQgkAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK14258 153 GGQQQRLCIARALAVKPKVLLMDEPCFGLDPiasMKVESLIQSLRLRSEL--TMVIVSHNLHQVSRLSDFTAFFKGNE 228
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
32-218 |
2.18e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.12 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 32 GQIHGLLGENGAGKSTLMSILTGLYRPD--EGEIYIKGQQvemlsPKAAVMQGIGMVHQHFKLVKSFTVAENIILG--MK 107
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRK-----PTKQILKRTGFVTQDDILYPHLTVRETLVFCslLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 108 DMGLLYDQRKIEAQiEQFCNQYGM--C---IDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYK 182
Cdd:PLN03211 169 LPKSLTKQEKILVA-ESVISELGLtkCentIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170 180 190
....*....|....*....|....*....|....*..
gi 2681003857 183 TLRLMAEQGKAVIVISHK-LSEVLEGTDKISVLRGGK 218
Cdd:PLN03211 248 TLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-220 |
2.46e-09 |
|
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: 59.19 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 24 HVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVemlspkaavmQGIGMVHQHFKLVksfTVAENII 103
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI----------AKIGLHDLRFKIT---IIPQDPV 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 104 L--GMKDMGL----LYDQRKIE-----AQIEQFCNQY--GMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTA 170
Cdd:TIGR00957 1371 LfsGSLRMNLdpfsQYSDEEVWwalelAHLKTFVSALpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2681003857 171 VLTPQEAKDLYKTLRLMAEQGkAVIVISHKLSEVLEGT-----DKISVLRGGKPA 220
Cdd:TIGR00957 1451 AVDLETDNLIQSTIRTQFEDC-TVLTIAHRLNTIMDYTrvivlDKGEVAEFGAPS 1504
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-218 |
3.61e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.13 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 21 ANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGqQVEMLSPKAAvmqgigmvhqhfkLVKSFTVAE 100
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAISAG-------------LSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 101 NIILGMKDMGllYDQRKIEA---QIEQFCNQYGMCIDPAAKvwqLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEA 177
Cdd:PRK13546 105 NIEFKMLCMG--FKRKEIKAmtpKIIEFSELGEFIYQPVKK---YSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2681003857 178 KDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK13546 180 QKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGK 220
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
21-218 |
6.88e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 56.67 E-value: 6.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 21 ANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLY----RPDEGEIYIKGQQVEMLSPKAA---VMQGIGMVHQH--FK 91
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKERrnlVGAEVAMIFQDpmTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 92 LVKSFTVAENIILGMK-DMGLLYDQRKIEAqIEqFCNQYGMcIDPAAKV----WQLTLGEQQRVEIIKALFRGAEILILD 166
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKvHQGGNKKTRRQRA-ID-LLNQVGI-PDPASRLdvypHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2681003857 167 EPTAVL--TPQeAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK11022 179 EPTTALdvTIQ-AQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQ 231
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-217 |
8.89e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 55.41 E-value: 8.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 17 PGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAAVMQGIGMV---HQHFKLV 93
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVayaAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 94 KSfTVAENIILGMKdmgllYDQRKIEAQIEQFCNQYGMCIDPAAKVWQ-------LTLGEQQRVEIIKALFRGAEILILD 166
Cdd:cd03290 92 NA-TVEENITFGSP-----FNKQRYKAVTDACSLQPDIDLLPFGDQTEigerginLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2681003857 167 EPTAVLTPQEAKDLYKT--LRLMAEQGKAVIVISHKLsEVLEGTDKISVLRGG 217
Cdd:cd03290 166 DPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
23-199 |
9.15e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 57.12 E-value: 9.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQihGLL--GENGAGKSTLMSILTGLYRPDEGEIYI-KGQQVEMLSPKAAVMQGigmvhqhfklvksfTVA 99
Cdd:COG4178 380 EDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLPQRPYLPLG--------------TLR 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 100 ENiilgmkdmgLLY--DQRKI-EAQIEQFCNQYGM-----CIDpAAKVWQ--LTLGEQQRVEIIKALFRGAEILILDEPT 169
Cdd:COG4178 444 EA---------LLYpaTAEAFsDAELREALEAVGLghlaeRLD-EEADWDqvLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190
....*....|....*....|....*....|
gi 2681003857 170 AVLTPQEAKDLYKTLRLMAEQGkAVIVISH 199
Cdd:COG4178 514 SALDEENEAALYQLLREELPGT-TVISVGH 542
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
25-204 |
1.18e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.35 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYI------KGQQVEMLSPKaavmqgIGMVHQHfKLVKSFTV 98
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIndshnlKDINLKWWRSK------IGVVSQD-PLLFSNSI 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 99 AENI---ILGMKDMGLLYDQRK------------------------------------IEAQIEQFCNQYGMCIDPAAKV 139
Cdd:PTZ00265 477 KNNIkysLYSLKDLEALSNYYNedgndsqenknkrnscrakcagdlndmsnttdsnelIEMRKNYQTIKDSEVVDVSKKV 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 140 W---------------------QLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYKTL-RLMAEQGKAVIVI 197
Cdd:PTZ00265 557 LihdfvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInNLKGNENRITIII 636
|
....*..
gi 2681003857 198 SHKLSEV 204
Cdd:PTZ00265 637 AHRLSTI 643
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-233 |
2.33e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 56.11 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMlsPKAAVMQgigmvhqhfklvkSFTVAENIIL 104
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYV--PQQAWIQ-------------NDSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 105 GmKDMGLLYDQRKIEA-----QIEQFCNqyGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKD 179
Cdd:TIGR00957 722 G-KALNEKYYQQVLEAcallpDLEILPS--GDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2681003857 180 LYKTL----RLMAeqGKAVIVISHKLSeVLEGTDKISVLRGGKpagstKTELASEEEL 233
Cdd:TIGR00957 799 IFEHVigpeGVLK--NKTRILVTHGIS-YLPQVDVIIVMSGGK-----ISEMGSYQEL 848
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-218 |
5.28e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.86 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFP-----------GVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEML 73
Cdd:PRK10261 312 PILQVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 74 SPKA--AVMQGIGMVHQ--HFKLVKSFTVAENIILGMKDMGLLyDQRKIEAQIEQFCNQYGMCIDPAAKV-WQLTLGEQQ 148
Cdd:PRK10261 392 SPGKlqALRRDIQFIFQdpYASLDPRQTVGDSIMEPLRVHGLL-PGKAAAARVAWLLERVGLLPEHAWRYpHEFSGGQRQ 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2681003857 149 RVEIIKALFRGAEILILDEPTAVLTPQ-EAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK10261 471 RICIARALALNPKVIIADEAVSALDVSiRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQ 541
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
15-217 |
5.95e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.68 E-value: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 15 RFPGVVANDhVSLTIEAGQIHGLLGENGAGKSTLMSI----LTGLYRPD----EGEIYIKGQQVEML-SPKAAVMQGIgm 85
Cdd:PRK13547 11 RRHRAILRD-LSLRIEPGRVTALLGRNGAGKSTLLKAlagdLTGGGAPRgarvTGDVTLNGEPLAAIdAPRLARLRAV-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 86 VHQHFKLVKSFTVAENIILG-----MKDMGLLYDQRKIeaqIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKAL---- 156
Cdd:PRK13547 88 LPQAAQPAFAFSAREIVLLGryphaRRAGALTHRDGEI---AWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlw 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2681003857 157 -----FRGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGK-AVIVISHKLSEVLEGTDKISVLRGG 217
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlGVLAIVHDPNLAARHADRIAMLADG 231
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
25-89 |
1.25e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.10 E-value: 1.25e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGL--YRPDEGEIYIKGQQVEMLSPKAAVMQGIGMVHQH 89
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQY 86
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
273-366 |
1.87e-07 |
|
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: 51.28 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 273 AVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGENHTISSARDMIRAGVSYVPEDRlgtGLVPGLN 352
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVPEGR---RIFPELT 91
|
90
....*....|....
gi 2681003857 353 AIDNYILKGYDQKG 366
Cdd:cd03224 92 VEENLLLGAYARRR 105
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-214 |
2.26e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 26 SLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSpkaaVMQGIGMVHQHFKLVKS---------- 95
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLS----FEQLQKLVSDEWQRNNTdmlspgeddt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 96 -FTVAENIILGMKDmgllydqrkiEAQIEQFCNQYGmcIDP--AAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVL 172
Cdd:PRK10938 99 gRTTAEIIQDEVKD----------PARCEQLAQQFG--ITAllDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2681003857 173 TPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVL 214
Cdd:PRK10938 167 DVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVL 208
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
258-341 |
2.70e-07 |
|
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: 51.05 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 258 LELDNIS-CLNNRGQIAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGENHTISSARDmIRAGVS 336
Cdd:cd03245 3 IEFRNVSfSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD-LRRNIG 81
|
....*
gi 2681003857 337 YVPED 341
Cdd:cd03245 82 YVPQD 86
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-174 |
3.27e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTG-----------LY--RPDEGE-IY-IKgqq 69
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLFgrRRGSGEtIWdIK--- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 70 vemlspkaavmQGIGMV----HQHFKLvkSFTVAENIILGMKDMGLLY----DQRKIEAQieQFCNQYGMCIDPAAKVWQ 141
Cdd:PRK10938 336 -----------KHIGYVssslHLDYRV--STSVRNVILSGFFDSIGIYqavsDRQQKLAQ--QWLDILGIDKRTADAPFH 400
|
170 180 190
....*....|....*....|....*....|....
gi 2681003857 142 -LTLGEQQRVEIIKALFRGAEILILDEPTAVLTP 174
Cdd:PRK10938 401 sLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP 434
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
118-300 |
3.56e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.52 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 118 IEAQIEQFCNQYGMCID-------PAAKVWQLTLGEQQRVEIIKALfrGAEIL----ILDEPTAVLTPQEAKDLYKTLRL 186
Cdd:PRK00635 446 IEEVLQGLKSRLSILIDlglpyltPERALATLSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKK 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 187 MAEQGKAVIVISHKlSEVLEGTDKI------------SVLRGGKPagstKTELASEEELT----RWMVGRNVPkqlDRTV 250
Cdd:PRK00635 524 LRDQGNTVLLVEHD-EQMISLADRIidigpgagifggEVLFNGSP----REFLAKSDSLTakylRQELTIPIP---EKRT 595
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2681003857 251 TEPGAVVLELDNIsclNNRGQIAVRhaslcIRAGEIVGIAGVAGNGQTEL 300
Cdd:PRK00635 596 NSLGTLTLSKATK---HNLKDLTIS-----LPLGRLTVVTGVSGSGKSSL 637
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
25-210 |
4.92e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.55 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTL------MSILTGLYRPdEGEIYIKGQQV--EMLSPkAAVMQGIGMVHQH-FKLVKS 95
Cdd:PRK14243 29 VWLDIPKNQITAFIGPSGCGKSTIlrcfnrLNDLIPGFRV-EGKVTFHGKNLyaPDVDP-VEVRRRIGMVFQKpNPFPKS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 96 ftVAENIILGMKDMGLlydQRKIEAQIEQFCNQYGMCIDPAAKVWQ----LTLGEQQRVEIIKALFRGAEILILDEPTAV 171
Cdd:PRK14243 107 --IYDNIAYGARINGY---KGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 2681003857 172 LTPQEAKDLYKTLRLMAEQGKAVIViSHKLSEVLEGTDK 210
Cdd:PRK14243 182 LDPISTLRIEELMHELKEQYTIIIV-THNMQQAARVSDM 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
6-231 |
5.34e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRF-PGVVANDH-VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSpKAAVMQGI 83
Cdd:PLN03232 1234 SIKFEDVHLRYrPGLPPVLHgLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG-LTDLRRVL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 84 GMVHQHFKLVkSFTVAENI--ILGMKDMGL--LYDQRKIEAQIEQfcNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRG 159
Cdd:PLN03232 1313 SIIPQSPVLF-SGTVRFNIdpFSEHNDADLweALERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARALLRR 1389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2681003857 160 AEILILDEPTAVLTPQEAKDLYKTLRlmaEQGKA--VIVISHKLSEVLEgTDKISVLRGGKP-AGSTKTELASEE 231
Cdd:PLN03232 1390 SKILVLDEATASVDVRTDSLIQRTIR---EEFKSctMLVIAHRLNTIID-CDKILVLSSGQVlEYDSPQELLSRD 1460
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-218 |
6.40e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGlyRPDEGeiYIKGQqvEMLS---PKAAVMQ-GIGMVHQHFKLVKSFTV 98
Cdd:TIGR00956 780 NNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTG--VITGG--DRLVngrPLDSSFQrSIGYVQQQDLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 99 AENIILGMkdmgllYDQRKIEAQIEQfCNQYgmcIDPAAKVWQLT---------LGEQQRVEIIKALFRGAE-------I 162
Cdd:TIGR00956 854 RESLRFSA------YLRQPKSVSKSE-KMEY---VEEVIKLLEMEsyadavvgvPGEGLNVEQRKRLTIGVElvakpklL 923
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2681003857 163 LILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVL-EGTDKISVL-RGGK 218
Cdd:TIGR00956 924 LFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILfEEFDRLLLLqKGGQ 981
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
7-250 |
6.43e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.89 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAG--KSTLMSILTGlyrPDEGEIyiKGQQVEMLSPKAAVMQGIG 84
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRR--PWRF*TWCANRRALRRTIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 85 MvHQHFKLVK--SFTVAENIILGMKDMGLlyDQRKIEAQIEQFCNQYGMCIDPAAKVWQLTLGEQQRVEIIKALFRGAEI 162
Cdd:NF000106 89 *-HRPVR*GRreSFSGRENLYMIGR*LDL--SRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 163 LILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGKPAGSTKTelaseEELTRWMVGRNV 242
Cdd:NF000106 166 LYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV-----DELKTKVGGRTL 240
|
250
....*....|....
gi 2681003857 243 ------PKQLDRTV 250
Cdd:NF000106 241 qirpahAAELDRMV 254
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
23-218 |
8.75e-07 |
|
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: 49.18 E-value: 8.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGL---YRPDEGEIYIKGQQV-EMLS--PKAAVMQGIGMVHQHfklvkSF 96
Cdd:cd03233 24 KDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPYkEFAEkyPGEIIYVSEEDVHFP-----TL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 97 TVAENIILGMKDMGllydqrkieaqieqfcNQYgmcidpaakVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQE 176
Cdd:cd03233 99 TVRETLDFALRCKG----------------NEF---------VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2681003857 177 AKDLYKTLRLMAEQGKAVIVIShkLSEVLEGT----DKISVLRGGK 218
Cdd:cd03233 154 ALEILKCIRTMADVLKTTTFVS--LYQASDEIydlfDKVLVLYEGR 197
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
11-63 |
1.02e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.66 E-value: 1.02e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2681003857 11 NVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEI 63
Cdd:PRK15064 324 NLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
25-199 |
1.03e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.71 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLSPKAavmqgIGMVHQHFKLVKSFTVAENIIL 104
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY-----CTYIGHNLGLKLEMTVFENLKF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 105 GMKdmglLYDQRK-IEAQIEQFCNQYGMcidpAAKVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYKT 183
Cdd:PRK13541 94 WSE----IYNSAEtLYAAIHYFKLHDLL----DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNL 165
|
170
....*....|....*.
gi 2681003857 184 LRLMAEQGKAVIVISH 199
Cdd:PRK13541 166 IVMKANSGGIVLLSSH 181
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
29-216 |
1.07e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 48.34 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 29 IEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVemlspkaavmqgigmvhqhfklvksftvaeniilgmkd 108
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP-------------------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 109 mglLYDQRKIEaqieqfcnqygmcidpaakvwqLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYKTLRLMA 188
Cdd:cd03222 64 ---VYKPQYID----------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170 180
....*....|....*....|....*....
gi 2681003857 189 EQG-KAVIVISHKLSEVLEGTDKISVLRG 216
Cdd:cd03222 119 EEGkKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-300 |
1.35e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 50.40 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 142 LTLGEQQRVEIIKALfrGAE----ILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKlSEVLEGTDKISVL--- 214
Cdd:TIGR00630 489 LSGGEAQRIRLATQI--GSGltgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD-EDTIRAADYVIDIgpg 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 215 ---RGGK--PAGSTKTELASEEELT-RWMVGR---NVPKQldRTVTEPGAVVLELDNIsclNNrgqiaVRHASLCIRAGE 285
Cdd:TIGR00630 566 ageHGGEvvASGTPEEILANPDSLTgQYLSGRkkiEVPAE--RRPGNGKFLTLKGARE---NN-----LKNITVSIPLGL 635
|
170
....*....|....*
gi 2681003857 286 IVGIAGVAGNGQTEL 300
Cdd:TIGR00630 636 FTCITGVSGSGKSTL 650
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
258-356 |
2.09e-06 |
|
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: 47.57 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 258 LELDNISCLNNrGQIAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGENHTISSARDM-IRAGVS 336
Cdd:cd03229 1 LELKNVSKRYG-QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPpLRRRIG 79
|
90 100
....*....|....*....|
gi 2681003857 337 YVPEDrlgTGLVPGLNAIDN 356
Cdd:cd03229 80 MVFQD---FALFPHLTVLEN 96
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-211 |
2.51e-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: 47.32 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLmsILTGLYRpdegeiyiKGQQVEMLSPKAAVMQGIGMVHQHFKLVksftvaeniil 104
Cdd:cd03238 14 LDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYA--------SGKARLISFLPKFSRNKLIFIDQLQFLI----------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 105 gmkDMGLLYdqrkieaqieqfcnqygmcIDPAAKVWQLTLGEQQRVEIIKALFRGAE--ILILDEPTAVLTPQEAKDLYK 182
Cdd:cd03238 73 ---DVGLGY-------------------LTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLE 130
|
170 180
....*....|....*....|....*....
gi 2681003857 183 TLRLMAEQGKAVIVISHKLsEVLEGTDKI 211
Cdd:cd03238 131 VIKGLIDLGNTVILIEHNL-DVLSSADWI 158
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
273-387 |
2.72e-06 |
|
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: 47.75 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 273 AVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGenHTISSARDMIRAGVSYVPEDRlgtGLVPGLN 352
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVREPREVRRRIGIVFQDL---SVDDELT 89
|
90 100 110
....*....|....*....|....*....|....*
gi 2681003857 353 AIDNYILKGydqKGWLINWQQALQKTQAAIDAFDI 387
Cdd:cd03265 90 GWENLYIHA---RLYGVPGAERRERIDELLDFVGL 121
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-218 |
6.45e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.00 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPD----EGEIYIKGQQVEMLSPK----AAVMQGigmVHQHFKLVK 94
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVAPCALRgrkiATIMQN---PRSAFNPLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 95 sfTVAENIILGMKDMGLLYDQRKIEAQIEqfcnqyGMCIDPAAKV-----WQLTLGEQQRVEIIKALFRGAEILILDEPT 169
Cdd:PRK10418 97 --TMHTHARETCLALGKPADDATLTAALE------AVGLENAARVlklypFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2681003857 170 AVLTP-QEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK10418 169 TDLDVvAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGR 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
267-362 |
6.91e-06 |
|
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: 46.73 E-value: 6.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 267 NNRGQIAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGenHTISSARDMIRAGVSYVPEDRLgtg 346
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING--YSIRTDRKAARQSLGYCPQFDA--- 85
|
90 100
....*....|....*....|
gi 2681003857 347 LVPGLNAIDN-YI---LKGY 362
Cdd:cd03263 86 LFDELTVREHlRFyarLKGL 105
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
7-233 |
2.57e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRF----PGVVanDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQVEMLS-------- 74
Cdd:PLN03130 1238 IKFEDVVLRYrpelPPVL--HGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGlmdlrkvl 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 75 ---PKAAVMQGiGMV---------HQHFKLVKSFTVAEniilgMKDMgllydQRKieaqieqfcNQYGMCIDPAAKVWQL 142
Cdd:PLN03130 1316 giiPQAPVLFS-GTVrfnldpfneHNDADLWESLERAH-----LKDV-----IRR---------NSLGLDAEVSEAGENF 1375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 143 TLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYKTLRlmaEQGKA--VIVISHKLSEVLEgTDKISVLRGGKpa 220
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIR---EEFKSctMLIIAHRLNTIID-CDRILVLDAGR-- 1449
|
250
....*....|...
gi 2681003857 221 gstKTELASEEEL 233
Cdd:PLN03130 1450 ---VVEFDTPENL 1459
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-218 |
3.79e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 45.62 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 19 VVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKG--------QQVEMLSPKAAVMQG-----IGM 85
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrQVIELSEQSAAQMRHvrgadMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 86 VHQH--FKLVKSFTVAENIILGMK-DMGLLYDQRKIEAQieQFCNQYGMcidPAAKVW------QLTLGEQQRVEIIKAL 156
Cdd:PRK10261 109 IFQEpmTSLNPVFTVGEQIAESIRlHQGASREEAMVEAK--RMLDQVRI---PEAQTIlsryphQLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2681003857 157 FRGAEILILDEPTAVL-TPQEAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKISVLRGGK 218
Cdd:PRK10261 184 SCRPAVLIADEPTTALdVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-81 |
3.84e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 5 PMVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEI---------YIKGQQVEMLSP 75
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgYFAQHQLEFLRA 390
|
....*.
gi 2681003857 76 KAAVMQ 81
Cdd:PRK10636 391 DESPLQ 396
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-233 |
4.50e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.74 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 25 VSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEgeiyikgqqvemlsPKAAVMQGIGMVHQHFKLVKSFTVAENIIL 104
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE--------------TSSVVIRGSVAYVPQVSWIFNATVRENILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 105 GMKdmgllYDQRKIEAQIEQFCNQYGMCIDPAAKVWQL-------TLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEA 177
Cdd:PLN03232 702 GSD-----FESERYWRAIDVTALQHDLDLLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVA 776
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2681003857 178 KDLYKTLRLMAEQGKAVIVISHKLsEVLEGTDKISVLRGG--KPAGsTKTELASEEEL 233
Cdd:PLN03232 777 HQVFDSCMKDELKGKTRVLVTNQL-HFLPLMDRIILVSEGmiKEEG-TFAELSKSGSL 832
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
259-339 |
5.00e-05 |
|
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: 44.06 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 259 ELDNIScLNNRGQIAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGENHTISSARdmiragVSYV 338
Cdd:cd03235 1 EVEDLT-VSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR------IGYV 73
|
.
gi 2681003857 339 P 339
Cdd:cd03235 74 P 74
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
37-218 |
5.80e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 37 LLGENGAGKSTLMSILTGLYRPDEGEIYikgqqvemLSPKAAvmqgIGMVHQHFklVKSFTVAENIILGMKDMGLLYDQR 116
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVF--------RSAKVR----MAVFSQHH--VDGLDLSSNPLLYMMRCFPGVPEQ 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 117 KIEAQIEQFCNQYGMCIDPaakVWQLTLGEQQRVEIIKALFRGAEILILDEPTAVLTPQEAKDLYKTLRLMaeQGkAVIV 196
Cdd:PLN03073 606 KLRAHLGSFGVTGNLALQP---MYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLF--QG-GVLM 679
|
170 180
....*....|....*....|..
gi 2681003857 197 ISHKLSEVLEGTDKISVLRGGK 218
Cdd:PLN03073 680 VSHDEHLISGSVDELWVVSEGK 701
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
29-70 |
6.56e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 43.68 E-value: 6.56e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2681003857 29 IEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIKGQQV 70
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA 75
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
142-201 |
6.61e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.14 E-value: 6.61e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2681003857 142 LTLGEQQRVEIIKALFR---GAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKL 201
Cdd:cd03271 170 LSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL 232
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-199 |
7.74e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.94 E-value: 7.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 8 QMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIYIkGQQVEmlspkaavmqgIGMVH 87
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLE-----------VAYFD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 88 QH-FKLVKSFTVAENIILGMKDMGLLYDQRKIEAQIEQFCNQYGMCIDPaakVWQLTLGEQQRVEIIKALFRGAEILILD 166
Cdd:PRK11147 389 QHrAELDPEKTVMDNLAEGKQEVMVNGRPRHVLGYLQDFLFHPKRAMTP---VKALSGGERNRLLLARLFLKPSNLLILD 465
|
170 180 190
....*....|....*....|....*....|....*....
gi 2681003857 167 EPTavltpqeaKDL-YKTLRLMAE-----QGkAVIVISH 199
Cdd:PRK11147 466 EPT--------NDLdVETLELLEElldsyQG-TVLLVSH 495
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
7-218 |
8.63e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 43.94 E-value: 8.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 7 VQMVNVTKRFPG--VVANDHVSLTIEAGQIHGLLGENGAGKS----TLMSIL------TGLYRPDEGEIY---------I 65
Cdd:PRK09473 15 VKDLRVTFSTPDgdVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLaangriGGSATFNGREILnlpekelnkL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 66 KGQQVEM--------LSPKAAV-MQGIGMVHQHFKLVKSFTVAENIilGMKDMGLLYDQRKieaQIEQFCNQY--GMcid 134
Cdd:PRK09473 95 RAEQISMifqdpmtsLNPYMRVgEQLMEVLMLHKGMSKAEAFEESV--RMLDAVKMPEARK---RMKMYPHEFsgGM--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 135 paakvwqltlgeQQRVEIIKALFRGAEILILDEPTAVL--TPQeAKDLYKTLRLMAEQGKAVIVISHKLSEVLEGTDKIS 212
Cdd:PRK09473 167 ------------RQRVMIAMALLCRPKLLIADEPTTALdvTVQ-AQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVL 233
|
....*.
gi 2681003857 213 VLRGGK 218
Cdd:PRK09473 234 VMYAGR 239
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
270-343 |
9.74e-05 |
|
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: 43.24 E-value: 9.74e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2681003857 270 GQIAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGENHTIsSARDMIRAGVSYVPEDRL 343
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAL-ADPAWLRRQVGVVLQENV 86
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
258-341 |
1.74e-04 |
|
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: 43.67 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 258 LELDNISC-LNNRGQIAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGEN-HTISsaRDMIRAGV 335
Cdd:COG2274 474 IELENVSFrYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDlRQID--PASLRRQI 551
|
....*.
gi 2681003857 336 SYVPED 341
Cdd:COG2274 552 GVVLQD 557
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
258-388 |
2.44e-04 |
|
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: 42.07 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 258 LELDNIS---CLNNRGQIAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGENHTISSARdmirag 334
Cdd:cd03293 1 LEVRNVSktyGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2681003857 335 VSYVPEDrlgTGLVPGLNAIDNyILKGYDQKGWliNWQQALQKTQAAIDAFDIK 388
Cdd:cd03293 75 RGYVFQQ---DALLPWLTVLDN-VALGLELQGV--PKAEARERAEELLELVGLS 122
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
269-341 |
2.83e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 42.19 E-value: 2.83e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2681003857 269 RGQIAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGENHTISSARDMIRAGVSYVPED 341
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQE 86
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
257-329 |
3.33e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 41.33 E-value: 3.33e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2681003857 257 VLELDNISCLnnRGQ-IAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGENhtISSARD 329
Cdd:PRK13538 1 MLEARNLACE--RDErILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP--IRRQRD 70
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
273-362 |
5.52e-04 |
|
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: 40.73 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 273 AVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGENHTISSARDMiragvSYVPEDRlgtGLVPGLN 352
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRI-----GYLPEER---GLYPKMK 86
|
90
....*....|....
gi 2681003857 353 AIDNYI----LKGY 362
Cdd:cd03269 87 VIDQLVylaqLKGL 100
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
23-63 |
6.30e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.69 E-value: 6.30e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2681003857 23 DHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEI 63
Cdd:PRK10636 18 DNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSY 58
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-201 |
7.74e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 7.74e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2681003857 142 LTLGEQQRVEIIKALFR---GAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKL 201
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
270-340 |
8.61e-04 |
|
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: 39.54 E-value: 8.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2681003857 270 GQIAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGENHTISSARDmIRAGVSYVPE 340
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE-LRRRIGYVPQ 80
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
257-319 |
9.33e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 40.74 E-value: 9.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2681003857 257 VLELDNISCLNNRGQIAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAG 319
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG 63
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
142-199 |
9.94e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 40.32 E-value: 9.94e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2681003857 142 LTLGEQQRVEIIKALfrGAE----ILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISH 199
Cdd:cd03270 138 LSGGEAQRIRLATQI--GSGltgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEH 197
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
258-329 |
1.04e-03 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 40.84 E-value: 1.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2681003857 258 LELDNISCLNNRGQIaVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGENHTISSARD 329
Cdd:PRK10851 3 IEIANIKKSFGRTQV-LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD 73
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-199 |
1.06e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.03 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 6 MVQMVNVTKRFPGVVANDHVSLTIEAGQIHGLLGENGAGKSTLMSILTGLYRPDEGEIyikgqqveMLSPKaavmQGIGM 85
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV--------SLDPN----ERLGK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 86 VHQHFKLVKSFTVAENIILGMKDMGLLYDQR-KIEAQIE--------------QFCNQYGMCIDpaAKVWQLTLG----- 145
Cdd:PRK15064 69 LRQDQFAFEEFTVLDTVIMGHTELWEVKQERdRIYALPEmseedgmkvadlevKFAEMDGYTAE--ARAGELLLGvgipe 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2681003857 146 EQQ-------------RVEIIKALFRGAEILILDEPTAVLtpqeakDLYkTLRLMA----EQGKAVIVISH 199
Cdd:PRK15064 147 EQHyglmsevapgwklRVLLAQALFSNPDILLLDEPTNNL------DIN-TIRWLEdvlnERNSTMIIISH 210
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
273-366 |
1.29e-03 |
|
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: 39.66 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 273 AVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGENhTISSARDmIRAGVSYVPEdrlGTGLVPGLN 352
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD-VVKEPAE-ARRRLGFVSD---STGLYDRLT 94
|
90 100
....*....|....*....|.
gi 2681003857 353 AIDN-------YILKGYDQKG 366
Cdd:cd03266 95 ARENleyfaglYGLKGDELTA 115
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
240-361 |
1.34e-03 |
|
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: 39.82 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 240 RNVPKQLDRTVTEPGAVVLELDNISCLNNRGQIAVRHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAG 319
Cdd:cd03220 4 ENVSKSYPTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG 83
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2681003857 320 enhtissardmiraGVSYVPEdrLGTGLVPGLNAIDNYILKG 361
Cdd:cd03220 84 --------------RVSSLLG--LGGGFNPELTGRENIYLNG 109
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
141-211 |
2.18e-03 |
|
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: 38.49 E-value: 2.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2681003857 141 QLTLGEQQRVEIIKAL----FRGAEILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKLsEVLEGTDKI 211
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLP-ELAELADKL 150
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
278-326 |
2.70e-03 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 38.79 E-value: 2.70e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2681003857 278 SLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGENHTISS 326
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP 67
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
143-201 |
5.16e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 5.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2681003857 143 TL--GEQQRVEIIKALFRGAE---ILILDEPTAVLTPQEAKDLYKTLRLMAEQGKAVIVISHKL 201
Cdd:COG0178 826 TLsgGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNL 889
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
256-342 |
7.58e-03 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 37.55 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 256 VVLELDNISClnNRGQIAVRH-ASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGENHTISSARDMIRAG 334
Cdd:PRK11614 4 VMLSFDKVSA--HYGKIQALHeVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREA 81
|
....*...
gi 2681003857 335 VSYVPEDR 342
Cdd:PRK11614 82 VAIVPEGR 89
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
255-321 |
9.27e-03 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 38.17 E-value: 9.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2681003857 255 AVVLELDNI--SCLNNRGQIAV-RHASLCIRAGEIVGIAGVAGNGQTELAEVVAGLRPVEDGQKYVAGEN 321
Cdd:PRK10535 2 TALLELKDIrrSYPSGEEQVEVlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQD 71
|
|
| |
