|
Name |
Accession |
Description |
Interval |
E-value |
| CheR |
COG1352 |
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms]; |
10-271 |
5.51e-110 |
|
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
Pssm-ID: 440963 [Multi-domain] Cd Length: 272 Bit Score: 319.42 E-value: 5.51e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 10 PMTAADFGIIRELAYQHTGIVLPERKRHMVYSRLSRRLRLLRLTNFGDYCLKLQRDPLELAPFINALTTNLTAFFRERHH 89
Cdd:COG1352 3 ELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDPEH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 90 FNFLETELVPYWQQRKQ--RRLRVWSAACSSGEEPYSIAMTLAEHFPAASGWDLKILATDLDTNVLARAEAGVYPLTGLE 167
Cdd:COG1352 83 FEALREEVLPELLARRRagRPLRIWSAGCSTGEEPYSLAMLLAEAGGELAGWRVEILATDISEEALEKARAGIYPERSLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 168 AIPK-RQHHYLQSRAEEFSISSQIKKLIFFKQLNLLEPWPMQGPFDAIFCRNVLIYFDQSTKQKIVAGFRKLLADDGVLF 246
Cdd:COG1352 163 GLPPeYLSRYFTKEGGRYRIKPELREMVTFAQHNLLDDPPPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGYLF 242
|
250 260
....*....|....*....|....*...
gi 743517872 247 IGHSESLTNISREFETVAQ---TTYRLR 271
Cdd:COG1352 243 LGHSESLGGLSDLFEPVDKkgrFIYRKR 270
|
|
| MeTrc |
smart00138 |
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ... |
13-271 |
1.14e-96 |
|
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues.
Pssm-ID: 214534 [Multi-domain] Cd Length: 264 Bit Score: 285.33 E-value: 1.14e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 13 AADFGIIRELAYQHTGIVLPERKRHMVYSRLSRRLRLLRLTNFGDYCLKLQRDPL--ELAPFINALTTNLTAFFRERHHF 90
Cdd:smart00138 1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHRGeeELAELLDLMTTNETRFFRESKHF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 91 NFLETELVPYWQQRKQ--RRLRVWSAACSSGEEPYSIAMTLAEHFPAASGWDLKILATDLDTNVLARAEAGVYPLTGLEA 168
Cdd:smart00138 81 EALEEKVLPLLIASRRhgRRVRIWSAGCSTGEEPYSLAMLLAETLPKGREPDVKILATDIDLKALEKARAGIYPERELED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 169 IPK-RQHHYLQSRAEEFSISSQIKKLIFFKQLNLLEPWPMQGPFDAIFCRNVLIYFDQSTKQKIVAGFRKLLADDGVLFI 247
Cdd:smart00138 161 LPKaLLARYFKEVEDKYRVKPELKERVRFAKHNLLAESPPLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLFL 240
|
250 260
....*....|....*....|....
gi 743517872 248 GHSESLTNISREFETVAQTTYRLR 271
Cdd:smart00138 241 GHSESLPGLTDKFEPIEGTVYFYS 264
|
|
| PRK10611 |
PRK10611 |
protein-glutamate O-methyltransferase CheR; |
9-270 |
1.88e-82 |
|
protein-glutamate O-methyltransferase CheR;
Pssm-ID: 236725 [Multi-domain] Cd Length: 287 Bit Score: 250.04 E-value: 1.88e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 9 FPMTAADFGIIRELAYQHTGIVLPERKRHMVYSRLSRRLRLLRLTNFGDYCLKLQRDP--LELAPFINALTTNLTAFFRE 86
Cdd:PRK10611 20 LALSDAHFRRICQLIYQRAGIVLADHKREMVYNRLVRRLRSLGLNDFGQYLALLESNQnsAEWQAFINALTTNLTAFFRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 87 RHHFNFLETElvpywQQRKQRRLRVWSAACSSGEEPYSIAMTLAEHF-PAASGWdlKILATDLDTNVLARAEAGVYPLTG 165
Cdd:PRK10611 100 AHHFPILAEH-----ARRRSGEYRVWSAAASTGEEPYSIAMTLADTLgTAPGRW--KVFASDIDTEVLEKARSGIYRQEE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 166 LEAIP--KRQHHYLQ---SRAEEFSISSQIKKLIFFKQLNLLEP-WPMQGPFDAIFCRNVLIYFDQSTKQKIVAGFRKLL 239
Cdd:PRK10611 173 LKTLSpqQLQRYFMRgtgPHEGLVRVRQELANYVDFQQLNLLAKqWAVPGPFDAIFCRNVMIYFDKTTQERILRRFVPLL 252
|
250 260 270
....*....|....*....|....*....|.
gi 743517872 240 ADDGVLFIGHSESLTNISREFETVAQTTYRL 270
Cdd:PRK10611 253 KPDGLLFAGHSENFSQLSREFYLRGQTVYGL 283
|
|
| CheR |
pfam01739 |
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ... |
79-263 |
4.50e-79 |
|
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase - the C-terminal domain (this one) binds SAM.
Pssm-ID: 426403 Cd Length: 190 Bit Score: 237.95 E-value: 4.50e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 79 NLTAFFRERHHFNFLETELVPYWQQRKQ-RRLRVWSAACSSGEEPYSIAMTLAEHFPAASGWDLKILATDLDTNVLARAE 157
Cdd:pfam01739 1 NETRFFREPAHFEELKKYVLPLLAKAKNgKRVRIWSAGCSSGEEPYSLAMLLKETFPNAARWDFKILATDIDLSVLEKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 158 AGVYPLTGLEAIPK--RQHHYLQSRAEEFSISSQIKKLIFFKQLNLLEPWPMQGPFDAIFCRNVLIYFDQSTKQKIVAGF 235
Cdd:pfam01739 81 AGVYPERELEGLPEelLRRYFEKTAGGGYTVKPEIKSMVLFEYLNLLDEYPPLGDFDVIFCRNVLIYFDEETQRKILNRF 160
|
170 180
....*....|....*....|....*...
gi 743517872 236 RKLLADDGVLFIGHSESLTNISREFETV 263
Cdd:pfam01739 161 AEKLKPGGYLFLGHSEALPGNPDKFKKV 188
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| CheR |
COG1352 |
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms]; |
10-271 |
5.51e-110 |
|
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
Pssm-ID: 440963 [Multi-domain] Cd Length: 272 Bit Score: 319.42 E-value: 5.51e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 10 PMTAADFGIIRELAYQHTGIVLPERKRHMVYSRLSRRLRLLRLTNFGDYCLKLQRDPLELAPFINALTTNLTAFFRERHH 89
Cdd:COG1352 3 ELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDPEH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 90 FNFLETELVPYWQQRKQ--RRLRVWSAACSSGEEPYSIAMTLAEHFPAASGWDLKILATDLDTNVLARAEAGVYPLTGLE 167
Cdd:COG1352 83 FEALREEVLPELLARRRagRPLRIWSAGCSTGEEPYSLAMLLAEAGGELAGWRVEILATDISEEALEKARAGIYPERSLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 168 AIPK-RQHHYLQSRAEEFSISSQIKKLIFFKQLNLLEPWPMQGPFDAIFCRNVLIYFDQSTKQKIVAGFRKLLADDGVLF 246
Cdd:COG1352 163 GLPPeYLSRYFTKEGGRYRIKPELREMVTFAQHNLLDDPPPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGYLF 242
|
250 260
....*....|....*....|....*...
gi 743517872 247 IGHSESLTNISREFETVAQ---TTYRLR 271
Cdd:COG1352 243 LGHSESLGGLSDLFEPVDKkgrFIYRKR 270
|
|
| MeTrc |
smart00138 |
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ... |
13-271 |
1.14e-96 |
|
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues.
Pssm-ID: 214534 [Multi-domain] Cd Length: 264 Bit Score: 285.33 E-value: 1.14e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 13 AADFGIIRELAYQHTGIVLPERKRHMVYSRLSRRLRLLRLTNFGDYCLKLQRDPL--ELAPFINALTTNLTAFFRERHHF 90
Cdd:smart00138 1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHRGeeELAELLDLMTTNETRFFRESKHF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 91 NFLETELVPYWQQRKQ--RRLRVWSAACSSGEEPYSIAMTLAEHFPAASGWDLKILATDLDTNVLARAEAGVYPLTGLEA 168
Cdd:smart00138 81 EALEEKVLPLLIASRRhgRRVRIWSAGCSTGEEPYSLAMLLAETLPKGREPDVKILATDIDLKALEKARAGIYPERELED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 169 IPK-RQHHYLQSRAEEFSISSQIKKLIFFKQLNLLEPWPMQGPFDAIFCRNVLIYFDQSTKQKIVAGFRKLLADDGVLFI 247
Cdd:smart00138 161 LPKaLLARYFKEVEDKYRVKPELKERVRFAKHNLLAESPPLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLFL 240
|
250 260
....*....|....*....|....
gi 743517872 248 GHSESLTNISREFETVAQTTYRLR 271
Cdd:smart00138 241 GHSESLPGLTDKFEPIEGTVYFYS 264
|
|
| PRK10611 |
PRK10611 |
protein-glutamate O-methyltransferase CheR; |
9-270 |
1.88e-82 |
|
protein-glutamate O-methyltransferase CheR;
Pssm-ID: 236725 [Multi-domain] Cd Length: 287 Bit Score: 250.04 E-value: 1.88e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 9 FPMTAADFGIIRELAYQHTGIVLPERKRHMVYSRLSRRLRLLRLTNFGDYCLKLQRDP--LELAPFINALTTNLTAFFRE 86
Cdd:PRK10611 20 LALSDAHFRRICQLIYQRAGIVLADHKREMVYNRLVRRLRSLGLNDFGQYLALLESNQnsAEWQAFINALTTNLTAFFRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 87 RHHFNFLETElvpywQQRKQRRLRVWSAACSSGEEPYSIAMTLAEHF-PAASGWdlKILATDLDTNVLARAEAGVYPLTG 165
Cdd:PRK10611 100 AHHFPILAEH-----ARRRSGEYRVWSAAASTGEEPYSIAMTLADTLgTAPGRW--KVFASDIDTEVLEKARSGIYRQEE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 166 LEAIP--KRQHHYLQ---SRAEEFSISSQIKKLIFFKQLNLLEP-WPMQGPFDAIFCRNVLIYFDQSTKQKIVAGFRKLL 239
Cdd:PRK10611 173 LKTLSpqQLQRYFMRgtgPHEGLVRVRQELANYVDFQQLNLLAKqWAVPGPFDAIFCRNVMIYFDKTTQERILRRFVPLL 252
|
250 260 270
....*....|....*....|....*....|.
gi 743517872 240 ADDGVLFIGHSESLTNISREFETVAQTTYRL 270
Cdd:PRK10611 253 KPDGLLFAGHSENFSQLSREFYLRGQTVYGL 283
|
|
| CheR |
pfam01739 |
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ... |
79-263 |
4.50e-79 |
|
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase - the C-terminal domain (this one) binds SAM.
Pssm-ID: 426403 Cd Length: 190 Bit Score: 237.95 E-value: 4.50e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 79 NLTAFFRERHHFNFLETELVPYWQQRKQ-RRLRVWSAACSSGEEPYSIAMTLAEHFPAASGWDLKILATDLDTNVLARAE 157
Cdd:pfam01739 1 NETRFFREPAHFEELKKYVLPLLAKAKNgKRVRIWSAGCSSGEEPYSLAMLLKETFPNAARWDFKILATDIDLSVLEKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 158 AGVYPLTGLEAIPK--RQHHYLQSRAEEFSISSQIKKLIFFKQLNLLEPWPMQGPFDAIFCRNVLIYFDQSTKQKIVAGF 235
Cdd:pfam01739 81 AGVYPERELEGLPEelLRRYFEKTAGGGYTVKPEIKSMVLFEYLNLLDEYPPLGDFDVIFCRNVLIYFDEETQRKILNRF 160
|
170 180
....*....|....*....|....*...
gi 743517872 236 RKLLADDGVLFIGHSESLTNISREFETV 263
Cdd:pfam01739 161 AEKLKPGGYLFLGHSEALPGNPDKFKKV 188
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
86-247 |
1.17e-06 |
|
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 441829 [Multi-domain] Cd Length: 126 Bit Score: 46.93 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 86 ERHHFNFLETELVPYWQQRKQRRLRVWSAACSSGEepysiamtLAEHFpAASGWDlkILATDLDTNVLARAEagvypltg 165
Cdd:COG2227 3 DPDARDFWDRRLAALLARLLPAGGRVLDVGCGTGR--------LALAL-ARRGAD--VTGVDISPEALEIAR-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 166 lEAIPKRQHHYLQSRAEEFSISSqikkliffkqlnllepwpmqGPFDAIFCRNVLIYFDQStkQKIVAGFRKLLADDGVL 245
Cdd:COG2227 64 -ERAAELNVDFVQGDLEDLPLED--------------------GSFDLVICSEVLEHLPDP--AALLRELARLLKPGGLL 120
|
..
gi 743517872 246 FI 247
Cdd:COG2227 121 LL 122
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
124-245 |
2.56e-05 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 42.35 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 124 SIAMTLAEHFPaasgwDLKILATDLDTNVLARAEAgvypltglEAIPKRQHHYLQSRaeefsissqikklifFKQLNLLE 203
Cdd:pfam08242 9 TLLRALLEALP-----GLEYTGLDISPAALEAARE--------RLAALGLLNAVRVE---------------LFQLDLGE 60
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 743517872 204 PWPmqGPFDAIFCRNVLIYFDQstKQKIVAGFRKLLADDGVL 245
Cdd:pfam08242 61 LDP--GSFDVVVASNVLHHLAD--PRAVLRNIRRLLKPGGVL 98
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
164-247 |
4.46e-05 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 42.99 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 164 TGLEaIPKRQHHYLQSRAEEFSISSQIKklifFKQLNLLEpWPMQGPFDAIFCRNVLIYFDQSTKQKIVAGFRKLLADDG 243
Cdd:COG2230 78 TGVT-LSPEQLEYARERAAEAGLADRVE----VRLADYRD-LPADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGG 151
|
....
gi 743517872 244 VLFI 247
Cdd:COG2230 152 RLLL 155
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
194-247 |
7.82e-05 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 42.60 E-value: 7.82e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 743517872 194 IFFKQLNLLEPWPM-QGPFDAIFCRNVLIYFDQSTKQKIVAGFRKLLADDGVLFI 247
Cdd:COG0500 77 VEFLVADLAELDPLpAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLL 131
|
|
| CheR_N |
pfam03705 |
CheR methyltransferase, all-alpha domain; CheR proteins are part of the chemotaxis signaling ... |
14-66 |
2.98e-04 |
|
CheR methyltransferase, all-alpha domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase.
Pssm-ID: 461017 [Multi-domain] Cd Length: 53 Bit Score: 37.80 E-value: 2.98e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 743517872 14 ADFGIIRELAYQHTGIVLPERKRHMVYSRLSRRLRLLRLTNFGDYCLKLQRDP 66
Cdd:pfam03705 1 AEFERLLELIYRRTGIDLSDYKRSLLERRLSRRMRALGLDSFSEYLDLLRSDP 53
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
114-243 |
1.30e-03 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 37.16 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 114 AACSSGeepySIAMTLAEHFPAasgwdlKILATDLDTNVLARAeagvypltgleaipkrqhhylQSRAEEFSISsqikkl 193
Cdd:pfam13649 4 LGCGTG----RLTLALARRGGA------RVTGVDLSPEMLERA---------------------RERAAEAGLN------ 46
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 743517872 194 IFFKQLNLLEPWPMQGPFDAIFCRNVLIYFDQSTKQKIVAGFRKLLADDG 243
Cdd:pfam13649 47 VEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPDLEAALREIARVLKPGG 96
|
|
|