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Conserved domains on  [gi|588256394|ref|XP_006957373|]
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hypothetical protein WALSEDRAFT_68147 [Wallemia mellicola CBS 633.66]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 1904217)

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

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:1904047
PubMed:  12504684|12826405

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Nnt1 super family cl43977
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
31-230 1.17e-18

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG3897:

Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 81.08  E-value: 1.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588256394  31 GRELSIRLESFhPLWAhYLWNASRVFCDYLINNKLCKGKTVCELGAGAGLPSLVASLEGAKRAVVTDYPDEPL------- 103
Cdd:COG3897   36 EEALGESGAPP-PFWA-FLWPSGQALARYLLDHPEVAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALaalrlna 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588256394 104 -LNNLRINIKECGIEKTAIVEGfvwgsnidhlieanggdeFDILILSDLVFNHSQHNALLRSCKNLMKKGGKCLVffSH- 181
Cdd:COG3897  114 aLNGVAITTRLGDWRDPPAAGG------------------FDLILGGDVLYERDLAEPLLPFLDRLAAPGGEVLI--GDp 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 588256394 182 HRPHKAKedmeFFEKATED-GWNVkkvveelvgVMFEEDGGDETVRATVH 230
Cdd:COG3897  174 GRGYLPA----FRERLEALaGYEV---------VTRELEDTEKVKRGRVL 210
 
Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
31-230 1.17e-18

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 81.08  E-value: 1.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588256394  31 GRELSIRLESFhPLWAhYLWNASRVFCDYLINNKLCKGKTVCELGAGAGLPSLVASLEGAKRAVVTDYPDEPL------- 103
Cdd:COG3897   36 EEALGESGAPP-PFWA-FLWPSGQALARYLLDHPEVAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALaalrlna 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588256394 104 -LNNLRINIKECGIEKTAIVEGfvwgsnidhlieanggdeFDILILSDLVFNHSQHNALLRSCKNLMKKGGKCLVffSH- 181
Cdd:COG3897  114 aLNGVAITTRLGDWRDPPAAGG------------------FDLILGGDVLYERDLAEPLLPFLDRLAAPGGEVLI--GDp 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 588256394 182 HRPHKAKedmeFFEKATED-GWNVkkvveelvgVMFEEDGGDETVRATVH 230
Cdd:COG3897  174 GRGYLPA----FRERLEALaGYEV---------VTRELEDTEKVKRGRVL 210
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
49-200 3.11e-12

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 62.73  E-value: 3.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588256394   49 LWNASRVFCDYLI--------NNKLcKGKTVCELGAGAGLPSL-VASLEGAKRAVVTDYPDepLLNNLRINIKECGIEKT 119
Cdd:pfam10294  21 VWDAAVVLSKYLEmkifkelgANNL-SGLNVLELGSGTGLVGIaVALLLPGASVTITDLEE--ALELLKKNIELNALSSK 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588256394  120 AIVEGFVWGSNIDHLIEANGgdEFDILILSDLVFNHSQHNALLRSCKNLMKKGGKCLVffSHHRPHKAkeDMEFFEKATE 199
Cdd:pfam10294  98 VVVKVLDWGENLPPDLFDGH--PVDLILAADCVYNEDSFPLLEKTLKDLLGKESVILV--AYKKRREA--EKKFFKLLER 171

                  .
gi 588256394  200 D 200
Cdd:pfam10294 172 F 172
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
70-174 5.32e-07

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: 46.65  E-value: 5.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588256394  70 TVCELGAGAGLPSLVASLEGAKRAVVTDYpDEPLLNNLRINIKECGIEKTAIVEGfvwgsNIDHLIEANGGdEFDIlILS 149
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDI-SPVALELARKAAAALLADNVEVLKG-----DAEELPPEADE-SFDV-IIS 72
                         90       100
                 ....*....|....*....|....*..
gi 588256394 150 DLVFNHSQHN--ALLRSCKNLMKKGGK 174
Cdd:cd02440   73 DPPLHHLVEDlaRFLEEARRLLKPGGV 99
 
Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
31-230 1.17e-18

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 81.08  E-value: 1.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588256394  31 GRELSIRLESFhPLWAhYLWNASRVFCDYLINNKLCKGKTVCELGAGAGLPSLVASLEGAKRAVVTDYPDEPL------- 103
Cdd:COG3897   36 EEALGESGAPP-PFWA-FLWPSGQALARYLLDHPEVAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALaalrlna 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588256394 104 -LNNLRINIKECGIEKTAIVEGfvwgsnidhlieanggdeFDILILSDLVFNHSQHNALLRSCKNLMKKGGKCLVffSH- 181
Cdd:COG3897  114 aLNGVAITTRLGDWRDPPAAGG------------------FDLILGGDVLYERDLAEPLLPFLDRLAAPGGEVLI--GDp 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 588256394 182 HRPHKAKedmeFFEKATED-GWNVkkvveelvgVMFEEDGGDETVRATVH 230
Cdd:COG3897  174 GRGYLPA----FRERLEALaGYEV---------VTRELEDTEKVKRGRVL 210
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
49-200 3.11e-12

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 62.73  E-value: 3.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588256394   49 LWNASRVFCDYLI--------NNKLcKGKTVCELGAGAGLPSL-VASLEGAKRAVVTDYPDepLLNNLRINIKECGIEKT 119
Cdd:pfam10294  21 VWDAAVVLSKYLEmkifkelgANNL-SGLNVLELGSGTGLVGIaVALLLPGASVTITDLEE--ALELLKKNIELNALSSK 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588256394  120 AIVEGFVWGSNIDHLIEANGgdEFDILILSDLVFNHSQHNALLRSCKNLMKKGGKCLVffSHHRPHKAkeDMEFFEKATE 199
Cdd:pfam10294  98 VVVKVLDWGENLPPDLFDGH--PVDLILAADCVYNEDSFPLLEKTLKDLLGKESVILV--AYKKRREA--EKKFFKLLER 171

                  .
gi 588256394  200 D 200
Cdd:pfam10294 172 F 172
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
70-174 5.32e-07

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: 46.65  E-value: 5.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588256394  70 TVCELGAGAGLPSLVASLEGAKRAVVTDYpDEPLLNNLRINIKECGIEKTAIVEGfvwgsNIDHLIEANGGdEFDIlILS 149
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDI-SPVALELARKAAAALLADNVEVLKG-----DAEELPPEADE-SFDV-IIS 72
                         90       100
                 ....*....|....*....|....*..
gi 588256394 150 DLVFNHSQHN--ALLRSCKNLMKKGGK 174
Cdd:cd02440   73 DPPLHHLVEDlaRFLEEARRLLKPGGV 99
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
60-180 6.33e-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: 44.24  E-value: 6.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588256394  60 LINNKLCKGKTVCELGAGAGLPSLVASLEGAkRAVVTDyPDEPLLNNLRINIKECGIEktaivegFVWGSnIDHLIEANG 139
Cdd:COG2227   17 LLARLLPAGGRVLDVGCGTGRLALALARRGA-DVTGVD-ISPEALEIARERAAELNVD-------FVQGD-LEDLPLEDG 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 588256394 140 GdeFDILILSDlVFNH-SQHNALLRSCKNLMKKGGkcLVFFS 180
Cdd:COG2227   87 S--FDLVICSE-VLEHlPDPAALLRELARLLKPGG--LLLLS 123
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
67-197 6.30e-05

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: 41.90  E-value: 6.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588256394  67 KGKTVCELGAGAGLPSLVASLEGAkRAVVTDyPDEPLLNNLRINIKECGIEKTAIVegfvwgSNIDHLIEANGgdEFDiL 146
Cdd:COG2226   22 PGARVLDLGCGTGRLALALAERGA-RVTGVD-ISPEMLELARERAAEAGLNVEFVV------GDAEDLPFPDG--SFD-L 90
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 588256394 147 ILSDLVFNHSQH-NALLRSCKNLMKKGGKcLVFFSHHRPHKAkEDMEFFEKA 197
Cdd:COG2226   91 VISSFVLHHLPDpERALAEIARVLKPGGR-LVVVDFSPPDLA-ELEELLAEA 140
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
32-115 3.71e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 40.27  E-value: 3.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588256394  32 RELSIRLES---FH-------------PLWAHYLWNAsrvfcdYLINNKlcKGKTVCELGAGAGLPSLVASLEGAKRAVV 95
Cdd:COG2263    2 RELEIILEKlpgFSnpkveleqyptpaELAAELLHLA------YLRGDI--EGKTVLDLGCGTGMLAIGAALLGAKKVVG 73
                         90       100
                 ....*....|....*....|
gi 588256394  96 TDYpDEPLLNNLRINIKECG 115
Cdd:COG2263   74 VDI-DPEALEIARENAERLG 92
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
71-173 1.03e-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: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588256394   71 VCELGAGAGLPSLVASLEGAKRAVVTDyPDEPLLNNLRINIKECGIEKTAIVegfvwgSNIDHLIEANGgdEFDiLILSD 150
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVD-LSPEMLERARERAAEAGLNVEFVQ------GDAEDLPFPDG--SFD-LVVSS 70
                          90       100
                  ....*....|....*....|....*.
gi 588256394  151 LVFNH---SQHNALLRSCKNLMKKGG 173
Cdd:pfam13649  71 GVLHHlpdPDLEAALREIARVLKPGG 96
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
67-194 7.00e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 35.86  E-value: 7.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588256394   67 KGKTVCELGAGAGLPSLVASLEGAKRAVVT--DYpDEPLLNNLRINIKECGIEKTAIVEGfvwgsNIDHLIEANGGDEFD 144
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGPNAEVVgiDI-SEEAIEKARENAQKLGFDNVEFEQG-----DIEELPELLEDDKFD 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 588256394  145 IlILSDLVFNHSQHNAL-LRSCKNLMKKGGKCLVF---FSHHRPHKAKEDMEFF 194
Cdd:pfam13847  77 V-VISNCVLNHIPDPDKvLQEILRVLKPGGRLIISdpdSLAELPAHVKEDSTYY 129
 
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.
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