|
Name |
Accession |
Description |
Interval |
E-value |
| Methyltransf_14 |
pfam08484 |
C-methyltransferase C-terminal domain; This domain is found in bacterial C-methyltransferase ... |
251-404 |
1.44e-65 |
|
C-methyltransferase C-terminal domain; This domain is found in bacterial C-methyltransferase proteins. This domain is found C-terminal to methyltransferase domains such as pfam08241 or pfam08242. But this domain is not a methyltransferase. :
Pssm-ID: 430022 Cd Length: 160 Bit Score: 206.15 E-value: 1.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503058085 251 KGGSVRLVAQLK-SARRSVDPSVGELIGEEHASGMRDAETYRKFAREIADAKHQLLSLLMGFKAAGKKIAGFGASHSTTT 329
Cdd:pfam08484 3 HGGSLRVYAARKeGGARPVSPAVAALLAEERAAGLDTLATYAGFAERVERVKDELLALLIDLKAEGKRVAGYGAAAKGNT 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503058085 330 LICHFGLAP-FIDYLVDDNPVKQGRYSPGFHLPVFSADKLIADQPDYVIMLGWQHRHSIMAKHP--LMNGTQWIIPLP 404
Cdd:pfam08484 83 LLNYCGIGPdLLDYVVDRNPAKQGRYTPGTHIPIVPPEKLREDRPDYVLILPWNLADEIMAQLAeyREWGGKFIVPVP 160
|
|
| Methyltransf_13 |
pfam08421 |
Putative zinc binding domain; This domain is found at the N-terminus of bacterial ... |
12-70 |
5.43e-16 |
|
Putative zinc binding domain; This domain is found at the N-terminus of bacterial methyltransferases and contains four conserved cysteines suggesting a potential zinc binding domain. :
Pssm-ID: 429987 Cd Length: 62 Bit Score: 71.84 E-value: 5.43e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503058085 12 CRLCGGNRIATVFKLADTPMEDQFVI-GPLEQP--FFPLELALCEDCGYLHLPHIVSPEASY 70
Cdd:pfam08421 1 CRLCGSPLLTPFLDLGRQPLANAFLTpEQLDQPepFYPLRLVVCEDCGLVQLEEVVPPEELF 62
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
106-244 |
2.41e-15 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain. :
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 73.23 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503058085 106 VVDLGSNDGSMLASFKRQGMQVVGVEPaasiaaRANQAGLETVNDFFTAEVAANITGKYGKASIVTANYMYANIDDVTEF 185
Cdd:pfam13489 26 VLDFGCGTGIFLRLLRAQGFSVTGVDP------SPIAIERALLNVRFDQFDEQEAAVPAGKFDVIVAREVLEHVPDPPAL 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503058085 186 TRSVARLLGPDGIFVVET--GYHPEQMKIRMFDY--IYHEHFSYFTVEVLQHLFAASGLELIH 244
Cdd:pfam13489 100 LRQIAALLKPGGLLLLSTplASDEADRLLLEWPYlrPRNGHISLFSARSLKRLLEEAGFEVVS 162
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Methyltransf_14 |
pfam08484 |
C-methyltransferase C-terminal domain; This domain is found in bacterial C-methyltransferase ... |
251-404 |
1.44e-65 |
|
C-methyltransferase C-terminal domain; This domain is found in bacterial C-methyltransferase proteins. This domain is found C-terminal to methyltransferase domains such as pfam08241 or pfam08242. But this domain is not a methyltransferase.
Pssm-ID: 430022 Cd Length: 160 Bit Score: 206.15 E-value: 1.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503058085 251 KGGSVRLVAQLK-SARRSVDPSVGELIGEEHASGMRDAETYRKFAREIADAKHQLLSLLMGFKAAGKKIAGFGASHSTTT 329
Cdd:pfam08484 3 HGGSLRVYAARKeGGARPVSPAVAALLAEERAAGLDTLATYAGFAERVERVKDELLALLIDLKAEGKRVAGYGAAAKGNT 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503058085 330 LICHFGLAP-FIDYLVDDNPVKQGRYSPGFHLPVFSADKLIADQPDYVIMLGWQHRHSIMAKHP--LMNGTQWIIPLP 404
Cdd:pfam08484 83 LLNYCGIGPdLLDYVVDRNPAKQGRYTPGTHIPIVPPEKLREDRPDYVLILPWNLADEIMAQLAeyREWGGKFIVPVP 160
|
|
| Methyltransf_13 |
pfam08421 |
Putative zinc binding domain; This domain is found at the N-terminus of bacterial ... |
12-70 |
5.43e-16 |
|
Putative zinc binding domain; This domain is found at the N-terminus of bacterial methyltransferases and contains four conserved cysteines suggesting a potential zinc binding domain.
Pssm-ID: 429987 Cd Length: 62 Bit Score: 71.84 E-value: 5.43e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503058085 12 CRLCGGNRIATVFKLADTPMEDQFVI-GPLEQP--FFPLELALCEDCGYLHLPHIVSPEASY 70
Cdd:pfam08421 1 CRLCGSPLLTPFLDLGRQPLANAFLTpEQLDQPepFYPLRLVVCEDCGLVQLEEVVPPEELF 62
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
106-244 |
2.41e-15 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 73.23 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503058085 106 VVDLGSNDGSMLASFKRQGMQVVGVEPaasiaaRANQAGLETVNDFFTAEVAANITGKYGKASIVTANYMYANIDDVTEF 185
Cdd:pfam13489 26 VLDFGCGTGIFLRLLRAQGFSVTGVDP------SPIAIERALLNVRFDQFDEQEAAVPAGKFDVIVAREVLEHVPDPPAL 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503058085 186 TRSVARLLGPDGIFVVET--GYHPEQMKIRMFDY--IYHEHFSYFTVEVLQHLFAASGLELIH 244
Cdd:pfam13489 100 LRQIAALLKPGGLLLLSTplASDEADRLLLEWPYlrPRNGHISLFSARSLKRLLEEAGFEVVS 162
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
66-247 |
4.93e-13 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 66.95 E-value: 4.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503058085 66 PEASYTDY--VYVSSLTVGLthHYD---QYAQKIINDWAVPASALVVDLGSNDGSMLASFKRQGMQVVGVEPAASIAARA 140
Cdd:COG4976 7 VEALFDQYadSYDAALVEDL--GYEapaLLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503058085 141 NQAGLETvnDFFTAEVAAnITGKYGKASIVTANYMYANIDDVTEFTRSVARLLGPDGIFVVETGYHPEqmkirmfdyiyh 220
Cdd:COG4976 85 REKGVYD--RLLVADLAD-LAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSVEDADG------------ 149
|
170 180 190
....*....|....*....|....*....|.
gi 503058085 221 EHFSYFTVEVLQHLFAASGLE----LIHAEK 247
Cdd:COG4976 150 SGRYAHSLDYVRDLLAAAGFEvpglLVVARK 180
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
106-202 |
7.01e-04 |
|
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: 38.95 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503058085 106 VVDLGSNDG-SMLASFKRQGMQVVGVE---PAASIAARANQAGLETVNDFFTAEVAANITGKYGKASIVTANYMY-ANID 180
Cdd:cd02440 2 VLDLGCGTGaLALALASGPGARVTGVDispVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLhHLVE 81
|
90 100
....*....|....*....|..
gi 503058085 181 DVTEFTRSVARLLGPDGIFVVE 202
Cdd:cd02440 82 DLARFLEEARRLLKPGGVLVLT 103
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Methyltransf_14 |
pfam08484 |
C-methyltransferase C-terminal domain; This domain is found in bacterial C-methyltransferase ... |
251-404 |
1.44e-65 |
|
C-methyltransferase C-terminal domain; This domain is found in bacterial C-methyltransferase proteins. This domain is found C-terminal to methyltransferase domains such as pfam08241 or pfam08242. But this domain is not a methyltransferase.
Pssm-ID: 430022 Cd Length: 160 Bit Score: 206.15 E-value: 1.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503058085 251 KGGSVRLVAQLK-SARRSVDPSVGELIGEEHASGMRDAETYRKFAREIADAKHQLLSLLMGFKAAGKKIAGFGASHSTTT 329
Cdd:pfam08484 3 HGGSLRVYAARKeGGARPVSPAVAALLAEERAAGLDTLATYAGFAERVERVKDELLALLIDLKAEGKRVAGYGAAAKGNT 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503058085 330 LICHFGLAP-FIDYLVDDNPVKQGRYSPGFHLPVFSADKLIADQPDYVIMLGWQHRHSIMAKHP--LMNGTQWIIPLP 404
Cdd:pfam08484 83 LLNYCGIGPdLLDYVVDRNPAKQGRYTPGTHIPIVPPEKLREDRPDYVLILPWNLADEIMAQLAeyREWGGKFIVPVP 160
|
|
| Methyltransf_13 |
pfam08421 |
Putative zinc binding domain; This domain is found at the N-terminus of bacterial ... |
12-70 |
5.43e-16 |
|
Putative zinc binding domain; This domain is found at the N-terminus of bacterial methyltransferases and contains four conserved cysteines suggesting a potential zinc binding domain.
Pssm-ID: 429987 Cd Length: 62 Bit Score: 71.84 E-value: 5.43e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503058085 12 CRLCGGNRIATVFKLADTPMEDQFVI-GPLEQP--FFPLELALCEDCGYLHLPHIVSPEASY 70
Cdd:pfam08421 1 CRLCGSPLLTPFLDLGRQPLANAFLTpEQLDQPepFYPLRLVVCEDCGLVQLEEVVPPEELF 62
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
106-244 |
2.41e-15 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 73.23 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503058085 106 VVDLGSNDGSMLASFKRQGMQVVGVEPaasiaaRANQAGLETVNDFFTAEVAANITGKYGKASIVTANYMYANIDDVTEF 185
Cdd:pfam13489 26 VLDFGCGTGIFLRLLRAQGFSVTGVDP------SPIAIERALLNVRFDQFDEQEAAVPAGKFDVIVAREVLEHVPDPPAL 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503058085 186 TRSVARLLGPDGIFVVET--GYHPEQMKIRMFDY--IYHEHFSYFTVEVLQHLFAASGLELIH 244
Cdd:pfam13489 100 LRQIAALLKPGGLLLLSTplASDEADRLLLEWPYlrPRNGHISLFSARSLKRLLEEAGFEVVS 162
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
66-247 |
4.93e-13 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 66.95 E-value: 4.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503058085 66 PEASYTDY--VYVSSLTVGLthHYD---QYAQKIINDWAVPASALVVDLGSNDGSMLASFKRQGMQVVGVEPAASIAARA 140
Cdd:COG4976 7 VEALFDQYadSYDAALVEDL--GYEapaLLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503058085 141 NQAGLETvnDFFTAEVAAnITGKYGKASIVTANYMYANIDDVTEFTRSVARLLGPDGIFVVETGYHPEqmkirmfdyiyh 220
Cdd:COG4976 85 REKGVYD--RLLVADLAD-LAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSVEDADG------------ 149
|
170 180 190
....*....|....*....|....*....|.
gi 503058085 221 EHFSYFTVEVLQHLFAASGLE----LIHAEK 247
Cdd:COG4976 150 SGRYAHSLDYVRDLLAAAGFEvpglLVVARK 180
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
87-203 |
5.44e-13 |
|
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: 65.42 E-value: 5.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503058085 87 YDQYAQKIINDWAvPASALVVDLGSNDGSMLASFKRQGMQVVGVEPAASIAARANQAGLETVNDFFTAEVaANITGKYGK 166
Cdd:COG2227 10 WDRRLAALLARLL-PAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNVDFVQGDL-EDLPLEDGS 87
|
90 100 110
....*....|....*....|....*....|....*..
gi 503058085 167 ASIVTANYMYANIDDVTEFTRSVARLLGPDGIFVVET 203
Cdd:COG2227 88 FDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLST 124
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
85-213 |
2.76e-08 |
|
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: 52.30 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503058085 85 HHYDQYaQKIINDWAVPASALVVDLGSNDGSMLASFKRQGMQVVGVEPAASIAARANQ-AGLETVNDFFTAEVAANITGK 163
Cdd:COG2226 6 ARYDGR-EALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARErAAEAGLNVEFVVGDAEDLPFP 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 503058085 164 YGKASIVTANYMYANIDDVTEFTRSVARLLGPDGIFVVETGYHPEQMKIR 213
Cdd:COG2226 85 DGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELE 134
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
101-202 |
5.84e-06 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 46.83 E-value: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503058085 101 PASALVVDLGSNDGSMLASF-KRQGMQVVGVEPAAS-IA---ARANQAGLETVnDFFTAEVAANITGKYGKASIVTANYM 175
Cdd:COG0500 25 PKGGRVLDLGCGTGRNLLALaARFGGRVIGIDLSPEaIAlarARAAKAGLGNV-EFLVADLAELDPLPAESFDLVVAFGV 103
|
90 100
....*....|....*....|....*....
gi 503058085 176 Y--ANIDDVTEFTRSVARLLGPDGIFVVE 202
Cdd:COG0500 104 LhhLPPEEREALLRELARALKPGGVLLLS 132
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
107-201 |
1.57e-05 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 43.04 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503058085 107 VDLGSNDGSMLASFKRQGMQVVGVEPAASIAARANQAGLETVNDFFTAEvAANITGKYGKASIVTANYMYANIDDVTEFT 186
Cdd:pfam08241 1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTFVVGD-AEDLPFPDNSFDLVLSSEVLHHVEDPERAL 79
|
90
....*....|....*
gi 503058085 187 RSVARLLGPDGIFVV 201
Cdd:pfam08241 80 REIARVLKPGGILII 94
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
106-204 |
2.51e-04 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 41.07 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503058085 106 VVDLGSNDGSMLASF-KRQGMQVVGV----EPAASIAARANQAGLETVNDFFTAEVAA-NITGKYGKASIVTAnYMYANI 179
Cdd:COG2230 55 VLDIGCGWGGLALYLaRRYGVRVTGVtlspEQLEYARERAAEAGLADRVEVRLADYRDlPADGQFDAIVSIGM-FEHVGP 133
|
90 100
....*....|....*....|....*
gi 503058085 180 DDVTEFTRSVARLLGPDGIFVVETG 204
Cdd:COG2230 134 ENYPAYFAKVARLLKPGGRLLLHTP 158
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
107-199 |
4.54e-04 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 39.27 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503058085 107 VDLGSNDGSMLASFKRQ--GMQVVGVE--PAASIAARANQAGLE-TVNDFFTAEVAANITGKYGKASIVTANYMYANIDD 181
Cdd:pfam08242 1 LEIGCGTGTLLRALLEAlpGLEYTGLDisPAALEAARERLAALGlLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80
|
90
....*....|....*...
gi 503058085 182 VTEFTRSVARLLGPDGIF 199
Cdd:pfam08242 81 PRAVLRNIRRLLKPGGVL 98
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
106-202 |
7.01e-04 |
|
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: 38.95 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503058085 106 VVDLGSNDG-SMLASFKRQGMQVVGVE---PAASIAARANQAGLETVNDFFTAEVAANITGKYGKASIVTANYMY-ANID 180
Cdd:cd02440 2 VLDLGCGTGaLALALASGPGARVTGVDispVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLhHLVE 81
|
90 100
....*....|....*....|..
gi 503058085 181 DVTEFTRSVARLLGPDGIFVVE 202
Cdd:cd02440 82 DLARFLEEARRLLKPGGVLVLT 103
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
106-197 |
1.27e-03 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 37.93 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503058085 106 VVDLGSNDGSMLASF-KRQGMQVVGVEPAASIAARANQ-AGLETVNDFFTAEVAANITGKYGKASIVTANYM--YANIDD 181
Cdd:pfam13649 1 VLDLGCGTGRLTLALaRRGGARVTGVDLSPEMLERARErAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVlhHLPDPD 80
|
90
....*....|....*.
gi 503058085 182 VTEFTRSVARLLGPDG 197
Cdd:pfam13649 81 LEAALREIARVLKPGG 96
|
|
|