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Conserved domains on  [gi|98986323|ref|NP_078834|]
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protein N-lysine methyltransferase METTL21D isoform a [Homo sapiens]

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 ...
 22-195 4.73e-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: 229.53  E-value: 4.73e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986323    22 KRDGTVLRLQQYSSGGVGCVVWDAAIVLSKYLETPEFSGDGAHALSRRSVLELGSGTGAVGLMAATL--GADVVVTDLEE 99
Cdd:pfam10294   1 KLDNPGLRIEEDTGNGIGGHVWDAAVVLSKYLEMKIFKELGANNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986323   100 LQDLLKMNINMNkhLVTGSVQAKVLKWGEEIEGF---PSPPDFILMADCIYYEESLEPLLKTLKDISGFETCIICCYEQR 176
Cdd:pfam10294  81 ALELLKKNIELN--ALSSKVVVKVLDWGENLPPDlfdGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKESVILVAYKKR 158

                         170
                  ....*....|....*....
gi 98986323   177 tmgknPEIEKKYFELLQLD 195
Cdd:pfam10294 159 -----REAEKKFFKLLERF 172
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 22-195 4.73e-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: 229.53  E-value: 4.73e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986323    22 KRDGTVLRLQQYSSGGVGCVVWDAAIVLSKYLETPEFSGDGAHALSRRSVLELGSGTGAVGLMAATL--GADVVVTDLEE 99
Cdd:pfam10294   1 KLDNPGLRIEEDTGNGIGGHVWDAAVVLSKYLEMKIFKELGANNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986323   100 LQDLLKMNINMNkhLVTGSVQAKVLKWGEEIEGF---PSPPDFILMADCIYYEESLEPLLKTLKDISGFETCIICCYEQR 176
Cdd:pfam10294  81 ALELLKKNIELN--ALSSKVVVKVLDWGENLPPDlfdGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKESVILVAYKKR 158

                         170
                  ....*....|....*....
gi 98986323   177 tmgknPEIEKKYFELLQLD 195
Cdd:pfam10294 159 -----REAEKKFFKLLERF 172
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 43-162 4.38e-07

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: 47.32  E-value: 4.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986323  43 WDAAivLSKYLEtpefsgdgAHALSRRSVLELGSGTGAVGLMAATLGADVVVTDL--EELQDLLKMNINMNKHLVTGSVq 120
Cdd:COG2227  10 WDRR--LAALLA--------RLLPAGGRVLDVGCGTGRLALALARRGADVTGVDIspEALEIARERAAELNVDFVQGDL- 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 98986323 121 akvlkwgEEIEGFPSPPDFILMADCIYYEESLEPLLKTLKDI 162
Cdd:COG2227  79 -------EDLPLEDGSFDLVICSEVLEHLPDPAALLRELARL 113
PRK14968 PRK14968
putative methyltransferase; Provisional
 70-97 4.76e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 36.80  E-value: 4.76e-03
                         10        20
                 ....*....|....*....|....*...
gi 98986323   70 SVLELGSGTGAVGLMAATLGADVVVTDL 97
Cdd:PRK14968  26 RVLEVGTGSGIVAIVAAKNGKKVVGVDI 53
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 71-161 7.24e-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: 35.10  E-value: 7.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986323  71 VLELGSGTGAVGL-MAATLGADVVVTDLEElqDLLKMNINMNKHLVTGSVQAKVLKWGEEIEGFPSPPDFILMAD-CIYY 148
Cdd:cd02440   2 VLDLGCGTGALALaLASGPGARVTGVDISP--VALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPpLHHL 79

                        90
                ....*....|...
gi 98986323 149 EESLEPLLKTLKD 161
Cdd:cd02440  80 VEDLARFLEEARR 92
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 22-195 4.73e-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: 229.53  E-value: 4.73e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986323    22 KRDGTVLRLQQYSSGGVGCVVWDAAIVLSKYLETPEFSGDGAHALSRRSVLELGSGTGAVGLMAATL--GADVVVTDLEE 99
Cdd:pfam10294   1 KLDNPGLRIEEDTGNGIGGHVWDAAVVLSKYLEMKIFKELGANNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986323   100 LQDLLKMNINMNkhLVTGSVQAKVLKWGEEIEGF---PSPPDFILMADCIYYEESLEPLLKTLKDISGFETCIICCYEQR 176
Cdd:pfam10294  81 ALELLKKNIELN--ALSSKVVVKVLDWGENLPPDlfdGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKESVILVAYKKR 158

                         170
                  ....*....|....*....
gi 98986323   177 tmgknPEIEKKYFELLQLD 195
Cdd:pfam10294 159 -----REAEKKFFKLLERF 172
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 43-162 4.38e-07

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: 47.32  E-value: 4.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986323  43 WDAAivLSKYLEtpefsgdgAHALSRRSVLELGSGTGAVGLMAATLGADVVVTDL--EELQDLLKMNINMNKHLVTGSVq 120
Cdd:COG2227  10 WDRR--LAALLA--------RLLPAGGRVLDVGCGTGRLALALARRGADVTGVDIspEALEIARERAAELNVDFVQGDL- 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 98986323 121 akvlkwgEEIEGFPSPPDFILMADCIYYEESLEPLLKTLKDI 162
Cdd:COG2227  79 -------EDLPLEDGSFDLVICSEVLEHLPDPAALLRELARL 113
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 63-121 1.82e-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: 44.37  E-value: 1.82e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 98986323  63 AHALSRRSVLELGSGTGAVGLMAATLGADVVVTDLE---ELQDLLKMNINMNK-----HLVTGSVQA 121
Cdd:COG4123  33 APVKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEiqpEAAELARRNVALNGledriTVIHGDLKE 99
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 69-162 1.35e-03

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 38.36  E-value: 1.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986323  69 RSVLELGSGTG-AVGLMAATLGADVVVTD-----LEELQDLLKMNINMNKHLVTGSVqakvlkwgEEIEGFPSPP-DFIL 141
Cdd:COG0500  28 GRVLDLGCGTGrNLLALAARFGGRVIGIDlspeaIALARARAAKAGLGNVEFLVADL--------AELDPLPAESfDLVV 99

                        90       100
                ....*....|....*....|.
gi 98986323 142 MADCIYYeESLEPLLKTLKDI 162
Cdd:COG0500 100 AFGVLHH-LPPEEREALLREL 119
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 71-162 1.49e-03

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 36.77  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986323    71 VLELGSGTGAVGL-MAATLGADVVVTDL-EELQDLLKMNINMNKHLVTGsVQAKVLKWGEEIEGFpsppDFILMADCIYY 148
Cdd:pfam13649   1 VLDLGCGTGRLTLaLARRGGARVTGVDLsPEMLERARERAAEAGLNVEF-VQGDAEDLPFPDGSF----DLVVSSGVLHH 75

                          90
                  ....*....|....*.
gi 98986323   149 --EESLEPLLKTLKDI 162
Cdd:pfam13649  76 lpDPDLEAALREIARV 91
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
42-162 3.47e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 37.29  E-value: 3.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986323  42 VWDAAIVLSKYLETPEFSGDGA----HALSRRSVLELGSGTGAVGLMAATLGADVVVTDLEElqdllkmniNMNKHLVTG 117
Cdd:COG4976  17 SYDAALVEDLGYEAPALLAEELlarlPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSE---------EMLAKAREK 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 98986323 118 SVQAKVLKwgEEIEGFPSPP---DFILMADCIYYEESLEPLLKTLKDI 162
Cdd:COG4976  88 GVYDRLLV--ADLADLAEPDgrfDLIVAADVLTYLGDLAAVFAGVARA 133
PRK14968 PRK14968
putative methyltransferase; Provisional
 70-97 4.76e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 36.80  E-value: 4.76e-03
                         10        20
                 ....*....|....*....|....*...
gi 98986323   70 SVLELGSGTGAVGLMAATLGADVVVTDL 97
Cdd:PRK14968  26 RVLEVGTGSGIVAIVAAKNGKKVVGVDI 53
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 71-161 7.24e-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: 35.10  E-value: 7.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986323  71 VLELGSGTGAVGL-MAATLGADVVVTDLEElqDLLKMNINMNKHLVTGSVQAKVLKWGEEIEGFPSPPDFILMAD-CIYY 148
Cdd:cd02440   2 VLDLGCGTGALALaLASGPGARVTGVDISP--VALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPpLHHL 79

                        90
                ....*....|...
gi 98986323 149 EESLEPLLKTLKD 161
Cdd:cd02440  80 VEDLARFLEEARR 92
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 62-96 9.72e-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: 36.15  E-value: 9.72e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 98986323  62 GAHALSRRSVLELGS-----GTGAVGLMAA----TLGADVVVTD 96
Cdd:cd05188 122 AYHALRRAGVLKPGDtvlvlGAGGVGLLAAqlakAAGARVIVTD 165
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 63-105 9.74e-03

Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (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 an 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. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. 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.


Pssm-ID: 176219 [Multi-domain]  Cd Length: 306  Bit Score: 36.52  E-value: 9.74e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 98986323  63 AHALSRRSVLELG-----SGTGAVGLMAA----TLGADVVVTDLEELQDLLK 105
Cdd:cd08258 153 VHAVAERSGIRPGdtvvvFGPGPIGLLAAqvakLQGATVVVVGTEKDEVRLD 204
 
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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