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Conserved domains on  [gi|98986329|ref|NP_001028408|]
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protein N-lysine methyltransferase METTL21D isoform 2 [Mus musculus]

Protein Classification

protein N-lysine methyltransferase family protein( domain architecture ID 10563300)

protein N-lysine methyltransferase family protein is a class I SAM-dependent methyltransferase that catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to human METTL21D that specifically trimethylates 'Lys-315' of VCP/p97

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 22-194 1.35e-77

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: 231.07  E-value: 1.35e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986329    22 KRDGTVLRLQQYGSGGVGCVVWDAAIVLSKYLETPGFSGDGAHALSRRSVLELGSGTGAVGLMAATL--GADVIVTDLEE 99
Cdd:pfam10294   1 KLDNPGLRIEEDTGNGIGGHVWDAAVVLSKYLEMKIFKELGANNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986329   100 LQDLLKMNIDMNkhLVTGSVQAKVLKWGEDIEDLMSP----DYILMADCIYYEESLEPLLKTLKDLSGSETCIICCYEQR 175
Cdd:pfam10294  81 ALELLKKNIELN--ALSSKVVVKVLDWGENLPPDLFDghpvDLILAADCVYNEDSFPLLEKTLKDLLGKESVILVAYKKR 158

                         170
                  ....*....|....*....
gi 98986329   176 tmgknPEIEKKYFELLQLD 194
Cdd:pfam10294 159 -----REAEKKFFKLLERF 172
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 22-194 1.35e-77

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: 231.07  E-value: 1.35e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986329    22 KRDGTVLRLQQYGSGGVGCVVWDAAIVLSKYLETPGFSGDGAHALSRRSVLELGSGTGAVGLMAATL--GADVIVTDLEE 99
Cdd:pfam10294   1 KLDNPGLRIEEDTGNGIGGHVWDAAVVLSKYLEMKIFKELGANNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986329   100 LQDLLKMNIDMNkhLVTGSVQAKVLKWGEDIEDLMSP----DYILMADCIYYEESLEPLLKTLKDLSGSETCIICCYEQR 175
Cdd:pfam10294  81 ALELLKKNIELN--ALSSKVVVKVLDWGENLPPDLFDghpvDLILAADCVYNEDSFPLLEKTLKDLLGKESVILVAYKKR 158

                         170
                  ....*....|....*....
gi 98986329   176 tmgknPEIEKKYFELLQLD 194
Cdd:pfam10294 159 -----REAEKKFFKLLERF 172
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 43-161 1.54e-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: 45.78  E-value: 1.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986329  43 WDAAivLSKYLEtpgfsgdgAHALSRRSVLELGSGTGAVGLMAATLGADVIVTDL--EELQDLLKMNIDMNKHLVTGsvq 120
Cdd:COG2227  10 WDRR--LAALLA--------RLLPAGGRVLDVGCGTGRLALALARRGADVTGVDIspEALEIARERAAELNVDFVQG--- 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 98986329 121 akvlkwgeDIEDLMSP----DYILMADCIYYEESLEPLLKTLKDL 161
Cdd:COG2227  77 --------DLEDLPLEdgsfDLVICSEVLEHLPDPAALLRELARL 113
PRK14968 PRK14968
putative methyltransferase; Provisional
 70-97 6.49e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 36.42  E-value: 6.49e-03
                         10        20
                 ....*....|....*....|....*...
gi 98986329   70 SVLELGSGTGAVGLMAATLGADVIVTDL 97
Cdd:PRK14968  26 RVLEVGTGSGIVAIVAAKNGKKVVGVDI 53
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 71-161 9.00e-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: 34.71  E-value: 9.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986329  71 VLELGSGTGAVGL-MAATLGADVIVTDL-EELQDLLKMNIDMNKHlvtgsVQAKVLKwgEDIEDLM-----SPDYILMAD 143
Cdd:cd02440   2 VLDLGCGTGALALaLASGPGARVTGVDIsPVALELARKAAAALLA-----DNVEVLK--GDAEELPpeadeSFDVIISDP 74

                        90
                ....*....|....*....
gi 98986329 144 -CIYYEESLEPLLKTLKDL 161
Cdd:cd02440  75 pLHHLVEDLARFLEEARRL 93
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 22-194 1.35e-77

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: 231.07  E-value: 1.35e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986329    22 KRDGTVLRLQQYGSGGVGCVVWDAAIVLSKYLETPGFSGDGAHALSRRSVLELGSGTGAVGLMAATL--GADVIVTDLEE 99
Cdd:pfam10294   1 KLDNPGLRIEEDTGNGIGGHVWDAAVVLSKYLEMKIFKELGANNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986329   100 LQDLLKMNIDMNkhLVTGSVQAKVLKWGEDIEDLMSP----DYILMADCIYYEESLEPLLKTLKDLSGSETCIICCYEQR 175
Cdd:pfam10294  81 ALELLKKNIELN--ALSSKVVVKVLDWGENLPPDLFDghpvDLILAADCVYNEDSFPLLEKTLKDLLGKESVILVAYKKR 158

                         170
                  ....*....|....*....
gi 98986329   176 tmgknPEIEKKYFELLQLD 194
Cdd:pfam10294 159 -----REAEKKFFKLLERF 172
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 43-161 1.54e-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: 45.78  E-value: 1.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986329  43 WDAAivLSKYLEtpgfsgdgAHALSRRSVLELGSGTGAVGLMAATLGADVIVTDL--EELQDLLKMNIDMNKHLVTGsvq 120
Cdd:COG2227  10 WDRR--LAALLA--------RLLPAGGRVLDVGCGTGRLALALARRGADVTGVDIspEALEIARERAAELNVDFVQG--- 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 98986329 121 akvlkwgeDIEDLMSP----DYILMADCIYYEESLEPLLKTLKDL 161
Cdd:COG2227  77 --------DLEDLPLEdgsfDLVICSEVLEHLPDPAALLRELARL 113
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 63-121 1.35e-05

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 44.75  E-value: 1.35e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 98986329  63 AHALSRRSVLELGSGTGAVGLMAATLGADVIVTDLE---ELQDLLKMNIDMNK-----HLVTGSVQA 121
Cdd:COG4123  33 APVKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEiqpEAAELARRNVALNGledriTVIHGDLKE 99
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 71-161 4.50e-03

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 35.62  E-value: 4.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986329    71 VLELGSGTGAVGL-MAATLGADVIVTDL-EELQDLLKMNIDMNKHLVTGsVQAkvlkwgeDIEDLMSP----DYILMADC 144
Cdd:pfam13649   1 VLDLGCGTGRLTLaLARRGGARVTGVDLsPEMLERARERAAEAGLNVEF-VQG-------DAEDLPFPdgsfDLVVSSGV 72

                          90
                  ....*....|....*....
gi 98986329   145 IYY--EESLEPLLKTLKDL 161
Cdd:pfam13649  73 LHHlpDPDLEAALREIARV 91
PRK14968 PRK14968
putative methyltransferase; Provisional
 70-97 6.49e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 36.42  E-value: 6.49e-03
                         10        20
                 ....*....|....*....|....*...
gi 98986329   70 SVLELGSGTGAVGLMAATLGADVIVTDL 97
Cdd:PRK14968  26 RVLEVGTGSGIVAIVAAKNGKKVVGVDI 53
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
42-161 7.65e-03

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 36.13  E-value: 7.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986329  42 VWDAAIVLSKYLETPGFSGDGA----HALSRRSVLELGSGTGAVGLMAATLGADVIVTDLEElqdllkmniDMNKHLVTG 117
Cdd:COG4976  17 SYDAALVEDLGYEAPALLAEELlarlPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSE---------EMLAKAREK 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 98986329 118 SVQAKVLKwgEDIEDLMSP----DYILMADCIYYEESLEPLLKTLKDL 161
Cdd:COG4976  88 GVYDRLLV--ADLADLAEPdgrfDLIVAADVLTYLGDLAAVFAGVARA 133
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 71-161 9.00e-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: 34.71  E-value: 9.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986329  71 VLELGSGTGAVGL-MAATLGADVIVTDL-EELQDLLKMNIDMNKHlvtgsVQAKVLKwgEDIEDLM-----SPDYILMAD 143
Cdd:cd02440   2 VLDLGCGTGALALaLASGPGARVTGVDIsPVALELARKAAAALLA-----DNVEVLK--GDAEELPpeadeSFDVIISDP 74

                        90
                ....*....|....*....
gi 98986329 144 -CIYYEESLEPLLKTLKDL 161
Cdd:cd02440  75 pLHHLVEDLARFLEEARRL 93
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 62-96 9.29e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 36.53  E-value: 9.29e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 98986329  62 GAHALSRRSVLELGS-----GTGAVGLMAA----TLGADVIVTD 96
Cdd:cd05188 122 AYHALRRAGVLKPGDtvlvlGAGGVGLLAAqlakAAGARVIVTD 165
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 69-156 9.65e-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: 35.35  E-value: 9.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986329  69 RSVLELGSGTGAVGLMAATLGADVIVTD-----LEELQDLLKmNIDMNKHLVTGSVQAkvLKWGEDiedlmSPDYILMAD 143
Cdd:COG2226  24 ARVLDLGCGTGRLALALAERGARVTGVDispemLELARERAA-EAGLNVEFVVGDAED--LPFPDG-----SFDLVISSF 95

                        90
                ....*....|...
gi 98986329 144 CIYYEESLEPLLK 156
Cdd:COG2226  96 VLHHLPDPERALA 108
 
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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