NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|98986333|ref|NP_001035752|]
View 

protein N-lysine methyltransferase METTL21D isoform b [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 22-191 1.23e-76

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: 227.22  E-value: 1.23e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986333    22 KRDGTVLRLQQYSSGGVGCVVWDAAIVLSKYLETPEFSGDGAHALSRRSVLELGSGTGAVGLMAATL--GADVVVTDLEE 99
Cdd:pfam10294   1 KLDNPGLRIEEDTGNGIGGHVWDAAVVLSKYLEMKIFKELGANNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986333   100 LQDLLKMNINMNkhLVTGSVQAKVLKWGEEIEGF---PSPPDFILMADCIYYEESLEPLLKTLKDISGFETCIICCYEQR 176
Cdd:pfam10294  81 ALELLKKNIELN--ALSSKVVVKVLDWGENLPPDlfdGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKESVILVAYKKR 158

                         170
                  ....*....|....*
gi 98986333   177 tmgknPEIEKKYFEK 191
Cdd:pfam10294 159 -----REAEKKFFKL 168
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 22-191 1.23e-76

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: 227.22  E-value: 1.23e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986333    22 KRDGTVLRLQQYSSGGVGCVVWDAAIVLSKYLETPEFSGDGAHALSRRSVLELGSGTGAVGLMAATL--GADVVVTDLEE 99
Cdd:pfam10294   1 KLDNPGLRIEEDTGNGIGGHVWDAAVVLSKYLEMKIFKELGANNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986333   100 LQDLLKMNINMNkhLVTGSVQAKVLKWGEEIEGF---PSPPDFILMADCIYYEESLEPLLKTLKDISGFETCIICCYEQR 176
Cdd:pfam10294  81 ALELLKKNIELN--ALSSKVVVKVLDWGENLPPDlfdGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKESVILVAYKKR 158

                         170
                  ....*....|....*
gi 98986333   177 tmgknPEIEKKYFEK 191
Cdd:pfam10294 159 -----REAEKKFFKL 168
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 43-162 3.11e-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: 3.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986333  43 WDAAivLSKYLEtpefsgdgAHALSRRSVLELGSGTGAVGLMAATLGADVVVTDL--EELQDLLKMNINMNKHLVTGSVq 120
Cdd:COG2227  10 WDRR--LAALLA--------RLLPAGGRVLDVGCGTGRLALALARRGADVTGVDIspEALEIARERAAELNVDFVQGDL- 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 98986333 121 akvlkwgEEIEGFPSPPDFILMADCIYYEESLEPLLKTLKDI 162
Cdd:COG2227  79 -------EDLPLEDGSFDLVICSEVLEHLPDPAALLRELARL 113
PRK14968 PRK14968
putative methyltransferase; Provisional
 70-97 2.95e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 36.80  E-value: 2.95e-03
                         10        20
                 ....*....|....*....|....*...
gi 98986333   70 SVLELGSGTGAVGLMAATLGADVVVTDL 97
Cdd:PRK14968  26 RVLEVGTGSGIVAIVAAKNGKKVVGVDI 53
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 71-161 4.56e-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: 35.48  E-value: 4.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986333  71 VLELGSGTGAVGL-MAATLGADVVVTDLEElqDLLKMNINMNKHLVTGSVQAKVLKWGEEIEGFPSPPDFILMAD-CIYY 148
Cdd:cd02440   2 VLDLGCGTGALALaLASGPGARVTGVDISP--VALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPpLHHL 79

                        90
                ....*....|...
gi 98986333 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 ...
 22-191 1.23e-76

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: 227.22  E-value: 1.23e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986333    22 KRDGTVLRLQQYSSGGVGCVVWDAAIVLSKYLETPEFSGDGAHALSRRSVLELGSGTGAVGLMAATL--GADVVVTDLEE 99
Cdd:pfam10294   1 KLDNPGLRIEEDTGNGIGGHVWDAAVVLSKYLEMKIFKELGANNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986333   100 LQDLLKMNINMNkhLVTGSVQAKVLKWGEEIEGF---PSPPDFILMADCIYYEESLEPLLKTLKDISGFETCIICCYEQR 176
Cdd:pfam10294  81 ALELLKKNIELN--ALSSKVVVKVLDWGENLPPDlfdGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKESVILVAYKKR 158

                         170
                  ....*....|....*
gi 98986333   177 tmgknPEIEKKYFEK 191
Cdd:pfam10294 159 -----REAEKKFFKL 168
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 43-162 3.11e-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: 3.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986333  43 WDAAivLSKYLEtpefsgdgAHALSRRSVLELGSGTGAVGLMAATLGADVVVTDL--EELQDLLKMNINMNKHLVTGSVq 120
Cdd:COG2227  10 WDRR--LAALLA--------RLLPAGGRVLDVGCGTGRLALALARRGADVTGVDIspEALEIARERAAELNVDFVQGDL- 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 98986333 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 1.08e-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: 1.08e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 98986333  63 AHALSRRSVLELGSGTGAVGLMAATLGADVVVTDLE---ELQDLLKMNINMNK-----HLVTGSVQA 121
Cdd:COG4123  33 APVKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEiqpEAAELARRNVALNGledriTVIHGDLKE 99
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 69-162 8.03e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 38.74  E-value: 8.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986333  69 RSVLELGSGTG-AVGLMAATLGADVVVTD-----LEELQDLLKMNINMNKHLVTGSVqakvlkwgEEIEGFPSPP-DFIL 141
Cdd:COG0500  28 GRVLDLGCGTGrNLLALAARFGGRVIGIDlspeaIALARARAAKAGLGNVEFLVADL--------AELDPLPAESfDLVV 99

                        90       100
                ....*....|....*....|.
gi 98986333 142 MADCIYYeESLEPLLKTLKDI 162
Cdd:COG0500 100 AFGVLHH-LPPEEREALLREL 119
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 71-162 1.47e-03

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 36.39  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986333    71 VLELGSGTGAVGL-MAATLGADVVVTDL-EELQDLLKMNINMNKHLVTGsVQAKVLKWGEEIEGFpsppDFILMADCIYY 148
Cdd:pfam13649   1 VLDLGCGTGRLTLaLARRGGARVTGVDLsPEMLERARERAAEAGLNVEF-VQGDAEDLPFPDGSF----DLVVSSGVLHH 75

                          90
                  ....*....|....*.
gi 98986333   149 --EESLEPLLKTLKDI 162
Cdd:pfam13649  76 lpDPDLEAALREIARV 91
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
42-162 2.33e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 37.29  E-value: 2.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986333  42 VWDAAIVLSKYLETPEFSGDGA----HALSRRSVLELGSGTGAVGLMAATLGADVVVTDLEElqdllkmniNMNKHLVTG 117
Cdd:COG4976  17 SYDAALVEDLGYEAPALLAEELlarlPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSE---------EMLAKAREK 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 98986333 118 SVQAKVLKwgEEIEGFPSPP---DFILMADCIYYEESLEPLLKTLKDI 162
Cdd:COG4976  88 GVYDRLLV--ADLADLAEPDgrfDLIVAADVLTYLGDLAAVFAGVARA 133
PRK14968 PRK14968
putative methyltransferase; Provisional
 70-97 2.95e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 36.80  E-value: 2.95e-03
                         10        20
                 ....*....|....*....|....*...
gi 98986333   70 SVLELGSGTGAVGLMAATLGADVVVTDL 97
Cdd:PRK14968  26 RVLEVGTGSGIVAIVAAKNGKKVVGVDI 53
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 71-161 4.56e-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: 35.48  E-value: 4.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986333  71 VLELGSGTGAVGL-MAATLGADVVVTDLEElqDLLKMNINMNKHLVTGSVQAKVLKWGEEIEGFPSPPDFILMAD-CIYY 148
Cdd:cd02440   2 VLDLGCGTGALALaLASGPGARVTGVDISP--VALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPpLHHL 79

                        90
                ....*....|...
gi 98986333 149 EESLEPLLKTLKD 161
Cdd:cd02440  80 VEDLARFLEEARR 92
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 63-105 8.92e-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: 36.14  E-value: 8.92e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 98986333  63 AHALSRRSVLELG-----SGTGAVGLMAA----TLGADVVVTDLEELQDLLK 105
Cdd:cd08258 153 VHAVAERSGIRPGdtvvvFGPGPIGLLAAqvakLQGATVVVVGTEKDEVRLD 204
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
63-111 9.36e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 35.78  E-value: 9.36e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 98986333  63 AHALSRRSVLELGSGTGAVGLMAATLGADVVVTdLEELQDLLKM---NINMN 111
Cdd:COG4076  31 RVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYA-VEVNPDIAAVarrIIAAN 81
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 69-97 9.40e-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: 34.97  E-value: 9.40e-03
                        10        20
                ....*....|....*....|....*....
gi 98986333  69 RSVLELGSGTGAVGLMAATLGADVVVTDL 97
Cdd:COG2226  24 ARVLDLGCGTGRLALALAERGARVTGVDI 52
 
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