NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|754494997|ref|WP_041911892|]
View 

MULTISPECIES: class I SAM-dependent methyltransferase [Enterobacter]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10614797)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
183-277 4.50e-10

Methyltransferase domain; This family appears to be a methyltransferase domain.


:

Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 56.03  E-value: 4.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754494997  183 DVGGNTGKWSLRCCRYDdNVAVTILDL-PQQIALAQENIEKAGFshRIGFHAVDMLSPSALPGDADVWWMSQFLDCFSPD 261
Cdd:pfam13649   3 DLGCGTGRLTLALARRG-GARVTGVDLsPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDP 79
                          90
                  ....*....|....*.
gi 754494997  262 QIVAMLTRVAEVMKPG 277
Cdd:pfam13649  80 DLEAALREIARVLKPG 95
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
183-277 4.50e-10

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 56.03  E-value: 4.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754494997  183 DVGGNTGKWSLRCCRYDdNVAVTILDL-PQQIALAQENIEKAGFshRIGFHAVDMLSPSALPGDADVWWMSQFLDCFSPD 261
Cdd:pfam13649   3 DLGCGTGRLTLALARRG-GARVTGVDLsPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDP 79
                          90
                  ....*....|....*.
gi 754494997  262 QIVAMLTRVAEVMKPG 277
Cdd:pfam13649  80 DLEAALREIARVLKPG 95
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
154-342 5.25e-07

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 49.53  E-value: 5.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754494997 154 WFAFDHYYSDAAFDAALPYIFA-SSPTKLYDVGGNTGKWSLRCCRYDdNVAVTILDL-PQQIALAQENIEKAGFSHrIGF 231
Cdd:COG0500    2 WDSYYSDELLPGLAALLALLERlPKGGRVLDLGCGTGRNLLALAARF-GGRVIGIDLsPEAIALARARAAKAGLGN-VEF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754494997 232 HAVDMLSPSALP-GDADVWWMSQFLDCFSPDQIVAMLTRVAEVMKPGARLcIMELFWDAQKYEAAAFSLNATSLyfTCMA 310
Cdd:COG0500   80 LVADLAELDPLPaESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVL-LLSASDAAAALSLARLLLLATAS--LLEL 156
                        170       180       190
                 ....*....|....*....|....*....|..
gi 754494997 311 NGNSRFYSVEKFYHYLERAGFSIAQRLDNLGV 342
Cdd:COG0500  157 LLLLRLLALELYLRALLAAAATEDLRSDALLE 188
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
183-277 4.50e-10

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 56.03  E-value: 4.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754494997  183 DVGGNTGKWSLRCCRYDdNVAVTILDL-PQQIALAQENIEKAGFshRIGFHAVDMLSPSALPGDADVWWMSQFLDCFSPD 261
Cdd:pfam13649   3 DLGCGTGRLTLALARRG-GARVTGVDLsPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDP 79
                          90
                  ....*....|....*.
gi 754494997  262 QIVAMLTRVAEVMKPG 277
Cdd:pfam13649  80 DLEAALREIARVLKPG 95
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
179-332 4.60e-09

O-methyltransferase domain; This family includes a range of O-methyltransferases. These enzymes utilize S-adenosyl methionine.


Pssm-ID: 395719 [Multi-domain]  Cd Length: 208  Bit Score: 55.87  E-value: 4.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754494997  179 TKLYDVGGNTGKWSLRCCRYDDNVAVTILDLPQQIALAQENIEkAGFSHRIGFHAVDMLSpSALPGdADVWWMSQFLDCF 258
Cdd:pfam00891  62 RSLVDVGGGTGALAQAIVSLYPGCKGIVFDLPHVVEAAPTHFS-AGEEPRVTFHGGDFFK-DSLPE-ADAYILKRVLHDW 138
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754494997  259 SPDQIVAMLTRVAEVMKPGARLCIMELFWDAQKYEAAAFSLnaTSLYFTCMANGNSRfySVEKFYHYLERAGFS 332
Cdd:pfam00891 139 SDEKCVKLLKRCYKACPAGGKVILVESLLGADPSGPLHTQL--YSLNMLAQTEGRER--TEAEYSELLTGAGFS 208
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
154-342 5.25e-07

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 49.53  E-value: 5.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754494997 154 WFAFDHYYSDAAFDAALPYIFA-SSPTKLYDVGGNTGKWSLRCCRYDdNVAVTILDL-PQQIALAQENIEKAGFSHrIGF 231
Cdd:COG0500    2 WDSYYSDELLPGLAALLALLERlPKGGRVLDLGCGTGRNLLALAARF-GGRVIGIDLsPEAIALARARAAKAGLGN-VEF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754494997 232 HAVDMLSPSALP-GDADVWWMSQFLDCFSPDQIVAMLTRVAEVMKPGARLcIMELFWDAQKYEAAAFSLNATSLyfTCMA 310
Cdd:COG0500   80 LVADLAELDPLPaESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVL-LLSASDAAAALSLARLLLLATAS--LLEL 156
                        170       180       190
                 ....*....|....*....|....*....|..
gi 754494997 311 NGNSRFYSVEKFYHYLERAGFSIAQRLDNLGV 342
Cdd:COG0500  157 LLLLRLLALELYLRALLAAAATEDLRSDALLE 188
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
157-287 4.32e-06

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: 45.76  E-value: 4.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754494997 157 FDHYYSD-AAFDAALPYIFASSPTKLYDVGGNTGKWSLRCCRYDDNVavTILDL-PQQIALAQENIEKAGFshRIGFHAV 234
Cdd:COG2226    1 FDRVAARyDGREALLAALGLRPGARVLDLGCGTGRLALALAERGARV--TGVDIsPEMLELARERAAEAGL--NVEFVVG 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 754494997 235 DMLSPSALPGDADVWWMSQFLdCFSPDqIVAMLTRVAEVMKPGARLCIMELFW 287
Cdd:COG2226   77 DAEDLPFPDGSFDLVISSFVL-HHLPD-PERALAEIARVLKPGGRLVVVDFSP 127
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
180-282 1.18e-05

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 44.92  E-value: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754494997 180 KLYDVGGNTGKWSLRCCRYDDnVAVTILDL-PQQIALAQENIEKAGFSHRIGFHAVDMLSPsALPGDADVWWMSQFLDCF 258
Cdd:COG2230   54 RVLDIGCGWGGLALYLARRYG-VRVTGVTLsPEQLEYARERAAEAGLADRVEVRLADYRDL-PADGQFDAIVSIGMFEHV 131
                         90       100
                 ....*....|....*....|....
gi 754494997 259 SPDQIVAMLTRVAEVMKPGARLCI 282
Cdd:COG2230  132 GPENYPAYFAKVARLLKPGGRLLL 155
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
164-280 3.28e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 38.48  E-value: 3.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754494997 164 AAFDAALPYifASSPTKL-YDVGGNTGKWSLRCCRYDDNVAVTILDLPQQIALAQENIEKAGFSHRIGF---HAVDMLsp 239
Cdd:COG4076   23 DAFKAAIER--VVKPGDVvLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVinaDATDLD-- 98
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 754494997 240 saLPGDADVwWMSQFLDC--FSPDQIVAMLTRVAEVMKPGARL 280
Cdd:COG4076   99 --LPEKADV-IISEMLDTalLDEGQVPILNHARKRLLKPGGRI 138
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH