|
Name |
Accession |
Description |
Interval |
E-value |
| CheR |
COG1352 |
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms]; |
1-261 |
6.46e-93 |
|
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
Pssm-ID: 440963 [Multi-domain] Cd Length: 272 Bit Score: 274.73 E-value: 6.46e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 1 MIPDLEKDYLYFTRVVKRDLGLDLALYKETQMKRRILSFIVKKKYFTFGEFFKHLKKDAVLLDEFISLITINVSSFFRNR 80
Cdd:COG1352 1 MAELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 81 NRWDVLEKQVIPRLLEDSRGK--LRVWSAACSSGEEPYSLAIMME---RSVGTRHYDILATDLEPAILKRAVIGEYQSRQ 155
Cdd:COG1352 81 EHFEALREEVLPELLARRRAGrpLRIWSAGCSTGEEPYSLAMLLAeagGELAGWRVEILATDISEEALEKARAGIYPERS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 156 MEELNEEERNTAFVENGDTYQILPKYRKAIRFRRHDLLTDY-YEKGFDLIVCRNVLIYFTAEGKHQAYQKFADSLRRGGV 234
Cdd:COG1352 161 LRGLPPEYLSRYFTKEGGRYRIKPELREMVTFAQHNLLDDPpPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGY 240
|
250 260 270
....*....|....*....|....*....|
gi 500020776 235 LFIGGSEQILNPADyGLATLNN---FFYIK 261
Cdd:COG1352 241 LFLGHSESLGGLSD-LFEPVDKkgrFIYRK 269
|
|
| MeTrc |
smart00138 |
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ... |
6-248 |
2.04e-70 |
|
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: 217.15 E-value: 2.04e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 6 EKDYLYFTRVVKRDLGLDLALYKETQMKRRILSFIVKKKYFTFGEFFKHLKKD--AVLLDEFISLITINVSSFFRNRNRW 83
Cdd:smart00138 1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHrgEEELAELLDLMTTNETRFFRESKHF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 84 DVLEKQVIPRLLEDSR--GKLRVWSAACSSGEEPYSLAIMMERSVGTRH---YDILATDLEPAILKRAVIGEYQSRQMEE 158
Cdd:smart00138 81 EALEEKVLPLLIASRRhgRRVRIWSAGCSTGEEPYSLAMLLAETLPKGRepdVKILATDIDLKALEKARAGIYPERELED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 159 LNEEERNTAFVENGDTYQILPKYRKAIRFRRHDLLTDYYEKG-FDLIVCRNVLIYFTAEGKHQAYQKFADSLRRGGVLFI 237
Cdd:smart00138 161 LPKALLARYFKEVEDKYRVKPELKERVRFAKHNLLAESPPLGdFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLFL 240
|
250
....*....|.
gi 500020776 238 GGSEQILNPAD 248
Cdd:smart00138 241 GHSESLPGLTD 251
|
|
| CheR |
pfam01739 |
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ... |
72-243 |
4.63e-54 |
|
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: 172.85 E-value: 4.63e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 72 NVSSFFRNRNRWDVLEKQVIPRLLEDSRGK-LRVWSAACSSGEEPYSLAI---MMERSVGTRHYDILATDLEPAILKRAV 147
Cdd:pfam01739 1 NETRFFREPAHFEELKKYVLPLLAKAKNGKrVRIWSAGCSSGEEPYSLAMllkETFPNAARWDFKILATDIDLSVLEKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 148 IGEYQSRQMEELNEEERNTAFVEN-GDTYQILPKYRKAIRFRRHDLLTDY-YEKGFDLIVCRNVLIYFTAEGKHQAYQKF 225
Cdd:pfam01739 81 AGVYPERELEGLPEELLRRYFEKTaGGGYTVKPEIKSMVLFEYLNLLDEYpPLGDFDVIFCRNVLIYFDEETQRKILNRF 160
|
170
....*....|....*...
gi 500020776 226 ADSLRRGGVLFIGGSEQI 243
Cdd:pfam01739 161 AEKLKPGGYLFLGHSEAL 178
|
|
| PRK10611 |
PRK10611 |
protein-glutamate O-methyltransferase CheR; |
48-241 |
4.53e-28 |
|
protein-glutamate O-methyltransferase CheR;
Pssm-ID: 236725 [Multi-domain] Cd Length: 287 Bit Score: 108.67 E-value: 4.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 48 FGEFFKHLKKDAVLLD--EFISLITINVSSFFRNRNRWDVLEKQVIPRlledsRGKLRVWSAACSSGEEPYSLAIMMERS 125
Cdd:PRK10611 66 FGQYLALLESNQNSAEwqAFINALTTNLTAFFREAHHFPILAEHARRR-----SGEYRVWSAAASTGEEPYSIAMTLADT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 126 VGTRHY--DILATDLEPAILKRAVIGEYQSRQMEELNEEERNTAFVENGDTYQILPKYRKA----IRFRRHDLLTDYY-- 197
Cdd:PRK10611 141 LGTAPGrwKVFASDIDTEVLEKARSGIYRQEELKTLSPQQLQRYFMRGTGPHEGLVRVRQElanyVDFQQLNLLAKQWav 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 500020776 198 EKGFDLIVCRNVLIYFTAEGKHQAYQKFADSLRRGGVLFIGGSE 241
Cdd:PRK10611 221 PGPFDAIFCRNVMIYFDKTTQERILRRFVPLLKPDGLLFAGHSE 264
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
103-237 |
6.77e-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: 35.48 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 103 RVWSAACSSGEepysLAIMMERSVGTRHYdilATDLEPAILKRAvigeyqsRQMEELNEEERNTAFVENGDTYQILPkyr 182
Cdd:cd02440 1 RVLDLGCGTGA----LALALASGPGARVT---GVDISPVALELA-------RKAAAALLADNVEVLKGDAEELPPEA--- 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 500020776 183 kairfrrhdlltdyyEKGFDLIVCRNVLIYFtAEGKHQAYQKFADSLRRGGVLFI 237
Cdd:cd02440 64 ---------------DESFDVIISDPPLHHL-VEDLARFLEEARRLLKPGGVLVL 102
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CheR |
COG1352 |
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms]; |
1-261 |
6.46e-93 |
|
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
Pssm-ID: 440963 [Multi-domain] Cd Length: 272 Bit Score: 274.73 E-value: 6.46e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 1 MIPDLEKDYLYFTRVVKRDLGLDLALYKETQMKRRILSFIVKKKYFTFGEFFKHLKKDAVLLDEFISLITINVSSFFRNR 80
Cdd:COG1352 1 MAELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 81 NRWDVLEKQVIPRLLEDSRGK--LRVWSAACSSGEEPYSLAIMME---RSVGTRHYDILATDLEPAILKRAVIGEYQSRQ 155
Cdd:COG1352 81 EHFEALREEVLPELLARRRAGrpLRIWSAGCSTGEEPYSLAMLLAeagGELAGWRVEILATDISEEALEKARAGIYPERS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 156 MEELNEEERNTAFVENGDTYQILPKYRKAIRFRRHDLLTDY-YEKGFDLIVCRNVLIYFTAEGKHQAYQKFADSLRRGGV 234
Cdd:COG1352 161 LRGLPPEYLSRYFTKEGGRYRIKPELREMVTFAQHNLLDDPpPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGY 240
|
250 260 270
....*....|....*....|....*....|
gi 500020776 235 LFIGGSEQILNPADyGLATLNN---FFYIK 261
Cdd:COG1352 241 LFLGHSESLGGLSD-LFEPVDKkgrFIYRK 269
|
|
| MeTrc |
smart00138 |
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ... |
6-248 |
2.04e-70 |
|
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: 217.15 E-value: 2.04e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 6 EKDYLYFTRVVKRDLGLDLALYKETQMKRRILSFIVKKKYFTFGEFFKHLKKD--AVLLDEFISLITINVSSFFRNRNRW 83
Cdd:smart00138 1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHrgEEELAELLDLMTTNETRFFRESKHF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 84 DVLEKQVIPRLLEDSR--GKLRVWSAACSSGEEPYSLAIMMERSVGTRH---YDILATDLEPAILKRAVIGEYQSRQMEE 158
Cdd:smart00138 81 EALEEKVLPLLIASRRhgRRVRIWSAGCSTGEEPYSLAMLLAETLPKGRepdVKILATDIDLKALEKARAGIYPERELED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 159 LNEEERNTAFVENGDTYQILPKYRKAIRFRRHDLLTDYYEKG-FDLIVCRNVLIYFTAEGKHQAYQKFADSLRRGGVLFI 237
Cdd:smart00138 161 LPKALLARYFKEVEDKYRVKPELKERVRFAKHNLLAESPPLGdFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLFL 240
|
250
....*....|.
gi 500020776 238 GGSEQILNPAD 248
Cdd:smart00138 241 GHSESLPGLTD 251
|
|
| CheR |
pfam01739 |
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ... |
72-243 |
4.63e-54 |
|
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: 172.85 E-value: 4.63e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 72 NVSSFFRNRNRWDVLEKQVIPRLLEDSRGK-LRVWSAACSSGEEPYSLAI---MMERSVGTRHYDILATDLEPAILKRAV 147
Cdd:pfam01739 1 NETRFFREPAHFEELKKYVLPLLAKAKNGKrVRIWSAGCSSGEEPYSLAMllkETFPNAARWDFKILATDIDLSVLEKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 148 IGEYQSRQMEELNEEERNTAFVEN-GDTYQILPKYRKAIRFRRHDLLTDY-YEKGFDLIVCRNVLIYFTAEGKHQAYQKF 225
Cdd:pfam01739 81 AGVYPERELEGLPEELLRRYFEKTaGGGYTVKPEIKSMVLFEYLNLLDEYpPLGDFDVIFCRNVLIYFDEETQRKILNRF 160
|
170
....*....|....*...
gi 500020776 226 ADSLRRGGVLFIGGSEQI 243
Cdd:pfam01739 161 AEKLKPGGYLFLGHSEAL 178
|
|
| PRK10611 |
PRK10611 |
protein-glutamate O-methyltransferase CheR; |
48-241 |
4.53e-28 |
|
protein-glutamate O-methyltransferase CheR;
Pssm-ID: 236725 [Multi-domain] Cd Length: 287 Bit Score: 108.67 E-value: 4.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 48 FGEFFKHLKKDAVLLD--EFISLITINVSSFFRNRNRWDVLEKQVIPRlledsRGKLRVWSAACSSGEEPYSLAIMMERS 125
Cdd:PRK10611 66 FGQYLALLESNQNSAEwqAFINALTTNLTAFFREAHHFPILAEHARRR-----SGEYRVWSAAASTGEEPYSIAMTLADT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 126 VGTRHY--DILATDLEPAILKRAVIGEYQSRQMEELNEEERNTAFVENGDTYQILPKYRKA----IRFRRHDLLTDYY-- 197
Cdd:PRK10611 141 LGTAPGrwKVFASDIDTEVLEKARSGIYRQEELKTLSPQQLQRYFMRGTGPHEGLVRVRQElanyVDFQQLNLLAKQWav 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 500020776 198 EKGFDLIVCRNVLIYFTAEGKHQAYQKFADSLRRGGVLFIGGSE 241
Cdd:PRK10611 221 PGPFDAIFCRNVMIYFDKTTQERILRRFVPLLKPDGLLFAGHSE 264
|
|
| CheR_N |
pfam03705 |
CheR methyltransferase, all-alpha domain; CheR proteins are part of the chemotaxis signaling ... |
7-58 |
4.04e-07 |
|
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: 45.89 E-value: 4.04e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 500020776 7 KDYLYFTRVVKRDLGLDLALYKETQMKRRILSFIVKKKYFTFGEFFKHLKKD 58
Cdd:pfam03705 1 AEFERLLELIYRRTGIDLSDYKRSLLERRLSRRMRALGLDSFSEYLDLLRSD 52
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
79-237 |
2.97e-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: 45.39 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 79 NRNRWDVLEKQVIPRLLEDSRgklRVWSAACSSGEepysLAIMMERsvgtRHYDILATDLEPAILKRAvigeyqSRQMEE 158
Cdd:COG2227 6 ARDFWDRRLAALLARLLPAGG---RVLDVGCGTGR----LALALAR----RGADVTGVDISPEALEIA------RERAAE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 159 LNeeerntafvengdtyqilpkyrkaIRFRRHDLLT-DYYEKGFDLIVCRNVLIYFTAEgkHQAYQKFADSLRRGGVLFI 237
Cdd:COG2227 69 LN------------------------VDFVQGDLEDlPLEDGSFDLVICSEVLEHLPDP--AALLRELARLLKPGGLLLL 122
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
185-233 |
1.35e-05 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 42.94 E-value: 1.35e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 500020776 185 IRFRRHDLLT-DYYEKGFDLIVCRNVLIYFTAEGKHQAYQKFADSLRRGG 233
Cdd:pfam13649 47 VEFVQGDAEDlPFPDGSFDLVVSSGVLHHLPDPDLEAALREIARVLKPGG 96
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
185-237 |
3.40e-05 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 41.73 E-value: 3.40e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 500020776 185 IRFRRHDLLTDYYEKGFDLIVCRNVLIYFtaEGKHQAYQKFADSLRRGGVLFI 237
Cdd:COG4106 48 VRFVVADLRDLDPPEPFDLVVSNAALHWL--PDHAALLARLAAALAPGGVLAV 98
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
185-237 |
1.53e-03 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 37.99 E-value: 1.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 500020776 185 IRFRRHDLLTDYYEKGFDLIVCRNVLIYFTAEGKHQAYQKFADSLRRGGVLFI 237
Cdd:COG2230 103 VEVRLADYRDLPADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
76-237 |
5.26e-03 |
|
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: 36.51 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 76 FFRNRNRWDVLEKQVipRLLEDSRGKlRVWSAACSSGEepysLAIMMERsvgtRHYDILATDLEPAILKRAvigeyqsrq 155
Cdd:COG2226 1 FDRVAARYDGREALL--AALGLRPGA-RVLDLGCGTGR----LALALAE----RGARVTGVDISPEMLELA--------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 156 meelneEERNTAFVENgdtyqilpkyrkaIRFRRHDLL-TDYYEKGFDLIVCRNVLIYFtaEGKHQAYQKFADSLRRGGV 234
Cdd:COG2226 61 ------RERAAEAGLN-------------VEFVVGDAEdLPFPDGSFDLVISSFVLHHL--PDPERALAEIARVLKPGGR 119
|
...
gi 500020776 235 LFI 237
Cdd:COG2226 120 LVV 122
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
185-240 |
5.33e-03 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 37.20 E-value: 5.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 500020776 185 IRFRRHDL--LTDYYEKGFDLIVCRNVLIYFTAEGKHQAYQKFADSLRRGGVLFIGGS 240
Cdd:COG0500 77 VEFLVADLaeLDPLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLSAS 134
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
103-237 |
6.77e-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: 35.48 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500020776 103 RVWSAACSSGEepysLAIMMERSVGTRHYdilATDLEPAILKRAvigeyqsRQMEELNEEERNTAFVENGDTYQILPkyr 182
Cdd:cd02440 1 RVLDLGCGTGA----LALALASGPGARVT---GVDISPVALELA-------RKAAAALLADNVEVLKGDAEELPPEA--- 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 500020776 183 kairfrrhdlltdyyEKGFDLIVCRNVLIYFtAEGKHQAYQKFADSLRRGGVLFI 237
Cdd:cd02440 64 ---------------DESFDVIISDPPLHHL-VEDLARFLEEARRLLKPGGVLVL 102
|
|
| |
