|
Name |
Accession |
Description |
Interval |
E-value |
| CheR |
COG1352 |
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms]; |
1-260 |
7.38e-91 |
|
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
Pssm-ID: 440963 [Multi-domain] Cd Length: 272 Bit Score: 269.34 E-value: 7.38e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005591306 1 MIIEQDYDHFIASFKQQFNMDIASYKQDRMRRRIDAFISRKGFENYTNFLSNLRTDQNLFLSFIDYITINVSEFFRNKER 80
Cdd:COG1352 3 ELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDPEH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005591306 81 WQTLETKALPKLLEQN--NGKLKVWSAACAAGEEPYTLSLILSKH---LAPFRFEIQATDLDFHILETAKRGQYTERSLK 155
Cdd:COG1352 83 FEALREEVLPELLARRraGRPLRIWSAGCSTGEEPYSLAMLLAEAggeLAGWRVEILATDISEEALEKARAGIYPERSLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005591306 156 ELPTDLKERHFTKENDIYSLHQNIKQNVTFKQHDLLM-QSFDTNYDLIICRNVMIYFTEEARVKLYEKFSRALRKGGVLF 234
Cdd:COG1352 163 GLPPEYLSRYFTKEGGRYRIKPELREMVTFAQHNLLDdPPPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGYLF 242
|
250 260
....*....|....*....|....*...
gi 1005591306 235 VGSTEQILTPERY--NLQRFDTFFYEKI 260
Cdd:COG1352 243 LGHSESLGGLSDLfePVDKKGRFIYRKR 270
|
|
| MeTrc |
smart00138 |
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ... |
4-241 |
1.99e-74 |
|
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: 227.55 E-value: 1.99e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005591306 4 EQDYDHFIASFKQQFNMDIASYKQDRMRRRIDAFISRKGFENYTNFLSNLRTDQNLFL--SFIDYITINVSEFFRNKERW 81
Cdd:smart00138 1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHRGEEElaELLDLMTTNETRFFRESKHF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005591306 82 QTLETKALPKLLE--QNNGKLKVWSAACAAGEEPYTLSLILSKHL---APFRFEIQATDLDFHILETAKRGQYTERSLKE 156
Cdd:smart00138 81 EALEEKVLPLLIAsrRHGRRVRIWSAGCSTGEEPYSLAMLLAETLpkgREPDVKILATDIDLKALEKARAGIYPERELED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005591306 157 LPTDLKERHFTKENDIYSLHQNIKQNVTFKQHDLLMQSF-DTNYDLIICRNVMIYFTEEARVKLYEKFSRALRKGGVLFV 235
Cdd:smart00138 161 LPKALLARYFKEVEDKYRVKPELKERVRFAKHNLLAESPpLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLFL 240
|
....*.
gi 1005591306 236 GSTEQI 241
Cdd:smart00138 241 GHSESL 246
|
|
| CheR |
pfam01739 |
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ... |
70-241 |
1.72e-61 |
|
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: 191.73 E-value: 1.72e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005591306 70 NVSEFFRNKERWQTLETKALPKLLEQNNGK-LKVWSAACAAGEEPYTLSLILSKHL---APFRFEIQATDLDFHILETAK 145
Cdd:pfam01739 1 NETRFFREPAHFEELKKYVLPLLAKAKNGKrVRIWSAGCSSGEEPYSLAMLLKETFpnaARWDFKILATDIDLSVLEKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005591306 146 RGQYTERSLKELPTDLKERHFTK-ENDIYSLHQNIKQNVTFKQHDLL-MQSFDTNYDLIICRNVMIYFTEEARVKLYEKF 223
Cdd:pfam01739 81 AGVYPERELEGLPEELLRRYFEKtAGGGYTVKPEIKSMVLFEYLNLLdEYPPLGDFDVIFCRNVLIYFDEETQRKILNRF 160
|
170
....*....|....*...
gi 1005591306 224 SRALRKGGVLFVGSTEQI 241
Cdd:pfam01739 161 AEKLKPGGYLFLGHSEAL 178
|
|
| PRK10611 |
PRK10611 |
protein-glutamate O-methyltransferase CheR; |
22-239 |
1.14e-32 |
|
protein-glutamate O-methyltransferase CheR;
Pssm-ID: 236725 [Multi-domain] Cd Length: 287 Bit Score: 120.61 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005591306 22 IASYKQD----RMRRRIDAFisrkGFENYTNFLSNLRTDQNL--FLSFIDYITINVSEFFRNKERWQTLETKAlpkllEQ 95
Cdd:PRK10611 42 LADHKREmvynRLVRRLRSL----GLNDFGQYLALLESNQNSaeWQAFINALTTNLTAFFREAHHFPILAEHA-----RR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005591306 96 NNGKLKVWSAACAAGEEPYTLSLILSKHL--APFRFEIQATDLDFHILETAKRGQYTERSLKELPTDLKERHFTKENDIY 173
Cdd:PRK10611 113 RSGEYRVWSAAASTGEEPYSIAMTLADTLgtAPGRWKVFASDIDTEVLEKARSGIYRQEELKTLSPQQLQRYFMRGTGPH 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005591306 174 S----LHQNIKQNVTFKQHDLLMQ--SFDTNYDLIICRNVMIYFTEEARVKLYEKFSRALRKGGVLFVGSTE 239
Cdd:PRK10611 193 EglvrVRQELANYVDFQQLNLLAKqwAVPGPFDAIFCRNVMIYFDKTTQERILRRFVPLLKPDGLLFAGHSE 264
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
181-235 |
2.93e-03 |
|
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).
Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 36.64 E-value: 2.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1005591306 181 QNVTFKQHDLLMQSF--DTNYDLIICRNVMIYFtEEARVKLYEKFSRALRKGGVLFV 235
Cdd:cd02440 47 DNVEVLKGDAEELPPeaDESFDVIISDPPLHHL-VEDLARFLEEARRLLKPGGVLVL 102
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CheR |
COG1352 |
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms]; |
1-260 |
7.38e-91 |
|
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
Pssm-ID: 440963 [Multi-domain] Cd Length: 272 Bit Score: 269.34 E-value: 7.38e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005591306 1 MIIEQDYDHFIASFKQQFNMDIASYKQDRMRRRIDAFISRKGFENYTNFLSNLRTDQNLFLSFIDYITINVSEFFRNKER 80
Cdd:COG1352 3 ELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDPEH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005591306 81 WQTLETKALPKLLEQN--NGKLKVWSAACAAGEEPYTLSLILSKH---LAPFRFEIQATDLDFHILETAKRGQYTERSLK 155
Cdd:COG1352 83 FEALREEVLPELLARRraGRPLRIWSAGCSTGEEPYSLAMLLAEAggeLAGWRVEILATDISEEALEKARAGIYPERSLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005591306 156 ELPTDLKERHFTKENDIYSLHQNIKQNVTFKQHDLLM-QSFDTNYDLIICRNVMIYFTEEARVKLYEKFSRALRKGGVLF 234
Cdd:COG1352 163 GLPPEYLSRYFTKEGGRYRIKPELREMVTFAQHNLLDdPPPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGYLF 242
|
250 260
....*....|....*....|....*...
gi 1005591306 235 VGSTEQILTPERY--NLQRFDTFFYEKI 260
Cdd:COG1352 243 LGHSESLGGLSDLfePVDKKGRFIYRKR 270
|
|
| MeTrc |
smart00138 |
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ... |
4-241 |
1.99e-74 |
|
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: 227.55 E-value: 1.99e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005591306 4 EQDYDHFIASFKQQFNMDIASYKQDRMRRRIDAFISRKGFENYTNFLSNLRTDQNLFL--SFIDYITINVSEFFRNKERW 81
Cdd:smart00138 1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHRGEEElaELLDLMTTNETRFFRESKHF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005591306 82 QTLETKALPKLLE--QNNGKLKVWSAACAAGEEPYTLSLILSKHL---APFRFEIQATDLDFHILETAKRGQYTERSLKE 156
Cdd:smart00138 81 EALEEKVLPLLIAsrRHGRRVRIWSAGCSTGEEPYSLAMLLAETLpkgREPDVKILATDIDLKALEKARAGIYPERELED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005591306 157 LPTDLKERHFTKENDIYSLHQNIKQNVTFKQHDLLMQSF-DTNYDLIICRNVMIYFTEEARVKLYEKFSRALRKGGVLFV 235
Cdd:smart00138 161 LPKALLARYFKEVEDKYRVKPELKERVRFAKHNLLAESPpLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLFL 240
|
....*.
gi 1005591306 236 GSTEQI 241
Cdd:smart00138 241 GHSESL 246
|
|
| CheR |
pfam01739 |
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ... |
70-241 |
1.72e-61 |
|
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: 191.73 E-value: 1.72e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005591306 70 NVSEFFRNKERWQTLETKALPKLLEQNNGK-LKVWSAACAAGEEPYTLSLILSKHL---APFRFEIQATDLDFHILETAK 145
Cdd:pfam01739 1 NETRFFREPAHFEELKKYVLPLLAKAKNGKrVRIWSAGCSSGEEPYSLAMLLKETFpnaARWDFKILATDIDLSVLEKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005591306 146 RGQYTERSLKELPTDLKERHFTK-ENDIYSLHQNIKQNVTFKQHDLL-MQSFDTNYDLIICRNVMIYFTEEARVKLYEKF 223
Cdd:pfam01739 81 AGVYPERELEGLPEELLRRYFEKtAGGGYTVKPEIKSMVLFEYLNLLdEYPPLGDFDVIFCRNVLIYFDEETQRKILNRF 160
|
170
....*....|....*...
gi 1005591306 224 SRALRKGGVLFVGSTEQI 241
Cdd:pfam01739 161 AEKLKPGGYLFLGHSEAL 178
|
|
| PRK10611 |
PRK10611 |
protein-glutamate O-methyltransferase CheR; |
22-239 |
1.14e-32 |
|
protein-glutamate O-methyltransferase CheR;
Pssm-ID: 236725 [Multi-domain] Cd Length: 287 Bit Score: 120.61 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005591306 22 IASYKQD----RMRRRIDAFisrkGFENYTNFLSNLRTDQNL--FLSFIDYITINVSEFFRNKERWQTLETKAlpkllEQ 95
Cdd:PRK10611 42 LADHKREmvynRLVRRLRSL----GLNDFGQYLALLESNQNSaeWQAFINALTTNLTAFFREAHHFPILAEHA-----RR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005591306 96 NNGKLKVWSAACAAGEEPYTLSLILSKHL--APFRFEIQATDLDFHILETAKRGQYTERSLKELPTDLKERHFTKENDIY 173
Cdd:PRK10611 113 RSGEYRVWSAAASTGEEPYSIAMTLADTLgtAPGRWKVFASDIDTEVLEKARSGIYRQEELKTLSPQQLQRYFMRGTGPH 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005591306 174 S----LHQNIKQNVTFKQHDLLMQ--SFDTNYDLIICRNVMIYFTEEARVKLYEKFSRALRKGGVLFVGSTE 239
Cdd:PRK10611 193 EglvrVRQELANYVDFQQLNLLAKqwAVPGPFDAIFCRNVMIYFDKTTQERILRRFVPLLKPDGLLFAGHSE 264
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
182-231 |
9.18e-08 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 48.71 E-value: 9.18e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1005591306 182 NVTFKQHDLLMQSFDTN-YDLIICRNVMIYFTEEARVKLYEKFSRALRKGG 231
Cdd:pfam13649 46 NVEFVQGDAEDLPFPDGsFDLVVSSGVLHHLPDPDLEAALREIARVLKPGG 96
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
182-235 |
6.86e-06 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 43.66 E-value: 6.86e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1005591306 182 NVTFKQHDLLMQSFDTNYDLIICRNVMIYFTEeaRVKLYEKFSRALRKGGVLFV 235
Cdd:COG4106 47 NVRFVVADLRDLDPPEPFDLVVSNAALHWLPD--HAALLARLAAALAPGGVLAV 98
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
182-235 |
8.26e-06 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 45.29 E-value: 8.26e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1005591306 182 NVTFKQHDLLM--QSFDTNYDLIICRNVMIYFTEEARVKLYEKFSRALRKGGVLFV 235
Cdd:COG0500 76 NVEFLVADLAEldPLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLL 131
|
|
| CheR_N |
pfam03705 |
CheR methyltransferase, all-alpha domain; CheR proteins are part of the chemotaxis signaling ... |
5-57 |
1.42e-05 |
|
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: 41.65 E-value: 1.42e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1005591306 5 QDYDHFIASFKQQFNMDIASYKQDRMRRRIDAFISRKGFENYTNFLSNLRTDQ 57
Cdd:pfam03705 1 AEFERLLELIYRRTGIDLSDYKRSLLERRLSRRMRALGLDSFSEYLDLLRSDP 53
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
77-235 |
1.54e-04 |
|
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: 40.39 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005591306 77 NKERWQtletKALPKLLEQNNGK-LKVWSAACAAGeepytlslILSKHLAPFRFEIQATDLDFHILETAKRgqyterslk 155
Cdd:COG2227 6 ARDFWD----RRLAALLARLLPAgGRVLDVGCGTG--------RLALALARRGADVTGVDISPEALEIARE--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005591306 156 elptdlkerhftkendiyslhQNIKQNVTFKQHDLL-MQSFDTNYDLIICRNVMIYFTEEARVklYEKFSRALRKGGVLF 234
Cdd:COG2227 65 ---------------------RAAELNVDFVQGDLEdLPLEDGSFDLVICSEVLEHLPDPAAL--LRELARLLKPGGLLL 121
|
.
gi 1005591306 235 V 235
Cdd:COG2227 122 L 122
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
182-235 |
2.68e-04 |
|
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 441828 [Multi-domain] Cd Length: 143 Bit Score: 39.98 E-value: 2.68e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1005591306 182 NVTFKQHDLLMQSFDTN-YDLIICRNVMIYFTEEARVklYEKFSRALRKGGVLFV 235
Cdd:COG2226 70 NVEFVVGDAEDLPFPDGsFDLVISSFVLHHLPDPERA--LAEIARVLKPGGRLVV 122
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
182-235 |
1.31e-03 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 38.37 E-value: 1.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1005591306 182 NVTFKQHDLLMQSFDTNYDLIICRNVMIYFTEEARVKLYEKFSRALRKGGVLFV 235
Cdd:COG2230 102 RVEVRLADYRDLPADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
181-237 |
1.80e-03 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 37.78 E-value: 1.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005591306 181 QNVTFKQ---HDLLMQSFDTNYDLIICRNVMIYFTEEARVklYEKFSRALRKGGVLFVGS 237
Cdd:pfam13847 54 DNVEFEQgdiEELPELLEDDKFDVVISNCVLNHIPDPDKV--LQEILRVLKPGGRLIISD 111
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
181-235 |
2.93e-03 |
|
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).
Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 36.64 E-value: 2.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1005591306 181 QNVTFKQHDLLMQSF--DTNYDLIICRNVMIYFtEEARVKLYEKFSRALRKGGVLFV 235
Cdd:cd02440 47 DNVEVLKGDAEELPPeaDESFDVIISDPPLHHL-VEDLARFLEEARRLLKPGGVLVL 102
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
183-247 |
7.16e-03 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 36.51 E-value: 7.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005591306 183 VTFKQHDLL-MQSFDTNYDLIICRNVMIYFteEARVKLYEKFSRALRKGGvLFVGSTEQILTPERY 247
Cdd:COG4976 91 DRLLVADLAdLAEPDGRFDLIVAADVLTYL--GDLAAVFAGVARALKPGG-LFIFSVEDADGSGRY 153
|
|
| |
