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Conserved domains on  [gi|165932358|ref|NP_859076|]
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tRNA N(3)-methylcytidine methyltransferase METTL2A [Homo sapiens]

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

EC:  2.1.-.-
Gene Ontology:  GO:1904047|GO:0008168
PubMed:  12504684|12826405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 184-286 8.95e-18

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


:

Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 77.60  E-value: 8.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932358  184 ILEVGCGVGNTVFPILQTnndPGLFVYCCDFSSTAIELVQTNSEYDPSRCFAFVHDLCDeeksYPVPKGSLDIIILIFVL 263
Cdd:pfam13649   1 VLDLGCGTGRLTLALARR---GGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAED----LPFPDGSFDLVVSSGVL 73

                          90       100
                  ....*....|....*....|...
gi 165932358  264 SAIVPDKMQKAINRLSRLLKPGG 286
Cdd:pfam13649  74 HHLPDPDLEAALREIARVLKPGG 96
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 184-286 8.95e-18

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 77.60  E-value: 8.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932358  184 ILEVGCGVGNTVFPILQTnndPGLFVYCCDFSSTAIELVQTNSEYDPSRCFAFVHDLCDeeksYPVPKGSLDIIILIFVL 263
Cdd:pfam13649   1 VLDLGCGTGRLTLALARR---GGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAED----LPFPDGSFDLVVSSGVL 73

                          90       100
                  ....*....|....*....|...
gi 165932358  264 SAIVPDKMQKAINRLSRLLKPGG 286
Cdd:pfam13649  74 HHLPDPDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 183-302 2.42e-15

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: 72.33  E-value: 2.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932358 183 RILEVGCGVGNTVFPILQTnndpGLFVYCCDFSSTAIELVQTNSEYDPSRCFAFVHDLCDeeksYPVPKGSLDIIILIFV 262
Cdd:COG2226   25 RVLDLGCGTGRLALALAER----GARVTGVDISPEMLELARERAAEAGLNVEFVVGDAED----LPFPDGSFDLVISSFV 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 165932358 263 LSAiVPDKmQKAINRLSRLLKPGGMMLLRDYGRYDMAQLR 302
Cdd:COG2226   97 LHH-LPDP-ERALAEIARVLKPGGRLVVVDFSPPDLAELE 134
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 183-290 4.13e-13

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: 65.14  E-value: 4.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932358 183 RILEVGCGVGNTVFPILQtnnDPGLFVYCCDFSSTAIELVQTNSEYDPSRCFAFVHdlCDEEKSYPVPKGSLDIIILIFV 262
Cdd:cd02440    1 RVLDLGCGTGALALALAS---GPGARVTGVDISPVALELARKAAAALLADNVEVLK--GDAEELPPEADESFDVIISDPP 75

                         90       100
                 ....*....|....*....|....*...
gi 165932358 263 LSAIVPDkMQKAINRLSRLLKPGGMMLL 290
Cdd:cd02440   76 LHHLVED-LARFLEEARRLLKPGGVLVL 102
PRK08317 PRK08317
hypothetical protein; Provisional
 183-286 1.53e-05

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 45.70  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932358 183 RILEVGCGVGNTVFPILQTNNDPGLfVYCCDFSSTAIELVQTNSEYDPSRCFaFVHDlcDEEKSyPVPKGSLDIIILIFV 262
Cdd:PRK08317  22 RVLDVGCGPGNDARELARRVGPEGR-VVGIDRSEAMLALAKERAAGLGPNVE-FVRG--DADGL-PFPDGSFDAVRSDRV 96

                         90       100
                 ....*....|....*....|....
gi 165932358 263 LSAIvPDKmQKAINRLSRLLKPGG 286
Cdd:PRK08317  97 LQHL-EDP-ARALAEIARVLRPGG 118
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 184-286 8.95e-18

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 77.60  E-value: 8.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932358  184 ILEVGCGVGNTVFPILQTnndPGLFVYCCDFSSTAIELVQTNSEYDPSRCFAFVHDLCDeeksYPVPKGSLDIIILIFVL 263
Cdd:pfam13649   1 VLDLGCGTGRLTLALARR---GGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAED----LPFPDGSFDLVVSSGVL 73

                          90       100
                  ....*....|....*....|...
gi 165932358  264 SAIVPDKMQKAINRLSRLLKPGG 286
Cdd:pfam13649  74 HHLPDPDLEAALREIARVLKPGG 96
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 185-287 4.11e-16

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 73.17  E-value: 4.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932358  185 LEVGCGVGNTVFPILQTNndPGLFVYCCDFSSTAIELV-QTNSEYDPSRCFAFVHDLCDEEKSYPvpkGSLDIIILIFVL 263
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAL--PGLEYTGLDISPAALEAArERLAALGLLNAVRVELFQLDLGELDP---GSFDVVVASNVL 75

                          90       100
                  ....*....|....*....|....
gi 165932358  264 SAIvpDKMQKAINRLSRLLKPGGM 287
Cdd:pfam08242  76 HHL--ADPRAVLRNIRRLLKPGGV 97
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 183-302 2.42e-15

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: 72.33  E-value: 2.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932358 183 RILEVGCGVGNTVFPILQTnndpGLFVYCCDFSSTAIELVQTNSEYDPSRCFAFVHDLCDeeksYPVPKGSLDIIILIFV 262
Cdd:COG2226   25 RVLDLGCGTGRLALALAER----GARVTGVDISPEMLELARERAAEAGLNVEFVVGDAED----LPFPDGSFDLVISSFV 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 165932358 263 LSAiVPDKmQKAINRLSRLLKPGGMMLLRDYGRYDMAQLR 302
Cdd:COG2226   97 LHH-LPDP-ERALAEIARVLKPGGRLVVVDFSPPDLAELE 134
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 183-302 8.86e-15

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 72.26  E-value: 8.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932358 183 RILEVGCGVGNTVFPILQTNNDPglfVYCCDFSSTAIELVQTN-SEYDPSRCFAFVHDLCDEEksyPVPKGSLDIIILIF 261
Cdd:COG0500   29 RVLDLGCGTGRNLLALAARFGGR---VIGIDLSPEAIALARARaAKAGLGNVEFLVADLAELD---PLPAESFDLVVAFG 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 165932358 262 VLSAIVPDKMQKAINRLSRLLKPGG--MMLLRDYGRYDMAQLR 302
Cdd:COG0500  103 VLHHLPPEEREALLRELARALKPGGvlLLSASDAAAALSLARL 145
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 183-290 4.13e-13

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: 65.14  E-value: 4.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932358 183 RILEVGCGVGNTVFPILQtnnDPGLFVYCCDFSSTAIELVQTNSEYDPSRCFAFVHdlCDEEKSYPVPKGSLDIIILIFV 262
Cdd:cd02440    1 RVLDLGCGTGALALALAS---GPGARVTGVDISPVALELARKAAAALLADNVEVLK--GDAEELPPEADESFDVIISDPP 75

                         90       100
                 ....*....|....*....|....*...
gi 165932358 263 LSAIVPDkMQKAINRLSRLLKPGGMMLL 290
Cdd:cd02440   76 LHHLVED-LARFLEEARRLLKPGGVLVL 102
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 183-293 1.63e-11

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: 61.19  E-value: 1.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932358 183 RILEVGCGVGNTVFPILQTnndpGLFVYCCDFSSTAIELVQTNseYDPSRCFAFVHDLCDeeksYPVPKGSLDIIILIFV 262
Cdd:COG2227   27 RVLDVGCGTGRLALALARR----GADVTGVDISPEALEIARER--AAELNVDFVQGDLED----LPLEDGSFDLVICSEV 96

                         90       100       110
                 ....*....|....*....|....*....|.
gi 165932358 263 LSAiVPDkMQKAINRLSRLLKPGGMMLLRDY 293
Cdd:COG2227   97 LEH-LPD-PAALLRELARLLKPGGLLLLSTP 125
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 183-343 5.45e-11

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 60.52  E-value: 5.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932358  183 RILEVGCGVGNtVFPILQTNNdpglfvyccdFSSTAIELvqtnSEYDPSRCFAFVHDLCDEEKSYPVPKGSLDIIILIFV 262
Cdd:pfam13489  25 RVLDFGCGTGI-FLRLLRAQG----------FSVTGVDP----SPIAIERALLNVRFDQFDEQEAAVPAGKFDVIVAREV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932358  263 LSAiVPDkMQKAINRLSRLLKPGGMMLLRDYGRYDMAQLRFKKgqclsgNFYVRGDGTRVYFFTQEELDTLFTTAGLEKV 342
Cdd:pfam13489  90 LEH-VPD-PPALLRQIAALLKPGGLLLLSTPLASDEADRLLLE------WPYLRPRNGHISLFSARSLKRLLEEAGFEVV 161


                  .
gi 165932358  343 Q 343
Cdd:pfam13489 162 S 162
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 185-290 6.15e-11

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 58.45  E-value: 6.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932358  185 LEVGCGVGNTVFPILQTnndpGLFVYCCDFSSTAIELVQTNSEYDPsrcFAFVHdlCDEEKSyPVPKGSLDIIILIFVLS 264
Cdd:pfam08241   1 LDVGCGTGLLTELLARL----GARVTGVDISPEMLELAREKAPREG---LTFVV--GDAEDL-PFPDNSFDLVLSSEVLH 70

                          90       100
                  ....*....|....*....|....*.
gi 165932358  265 AiVPDkMQKAINRLSRLLKPGGMMLL 290
Cdd:pfam08241  71 H-VED-PERALREIARVLKPGGILII 94
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
183-290 5.22e-08

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 50.21  E-value: 5.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932358 183 RILEVGCGVGNTVFPILQTNndPGLFVYCCDFSSTAIELVQTNSeydpSRCFAFVHDLCDEEksypvPKGSLDIIILIFV 262
Cdd:COG4106    4 RVLDLGCGTGRLTALLAERF--PGARVTGVDLSPEMLARARARL----PNVRFVVADLRDLD-----PPEPFDLVVSNAA 72

                         90       100
                 ....*....|....*....|....*...
gi 165932358 263 LSAiVPDkMQKAINRLSRLLKPGGMMLL 290
Cdd:COG4106   73 LHW-LPD-HAALLARLAAALAPGGVLAV 98
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
183-340 7.94e-08

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 51.92  E-value: 7.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932358 183 RILEVGCGVGNTVFPILQTnndpGLFVYCCDFSSTAIELVQTNSEYDPsrcfAFVHDLCDeeksYPVPKGSLDIIILIFV 262
Cdd:COG4976   49 RVLDLGCGTGLLGEALRPR----GYRLTGVDLSEEMLAKAREKGVYDR----LLVADLAD----LAEPDGRFDLIVAADV 116

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 165932358 263 LSAIvpDKMQKAINRLSRLLKPGGMMLlrdygrydmaqlrfkkgqclsgnFYV-RGDGTRVYFFTQEELDTLFTTAGLE 340
Cdd:COG4976  117 LTYL--GDLAAVFAGVARALKPGGLFI-----------------------FSVeDADGSGRYAHSLDYVRDLLAAAGFE 170
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 182-293 4.96e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 48.95  E-value: 4.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932358  182 YRILEVGCGVGNTVFPILQTNNDPGlFVYCCDFSSTAIELVQTNSEydpSRCFAFVH-DLCD-EEKSYPVPKGSLDIIIL 259
Cdd:pfam13847   5 MRVLDLGCGTGHLSFELAEELGPNA-EVVGIDISEEAIEKARENAQ---KLGFDNVEfEQGDiEELPELLEDDKFDVVIS 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 165932358  260 IFVLSAIvPDKmQKAINRLSRLLKPGGMMLLRDY 293
Cdd:pfam13847  81 NCVLNHI-PDP-DKVLQEILRVLKPGGRLIISDP 112
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 183-292 1.21e-06

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 48.00  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932358 183 RILEVGCGVGNTVFPILQTNndpGLFVYCCDFSSTAIELVQTNSEYDPSRCFAFVH--DLCDEEksypvPKGSLDIIILI 260
Cdd:COG2230   54 RVLDIGCGWGGLALYLARRY---GVRVTGVTLSPEQLEYARERAAEAGLADRVEVRlaDYRDLP-----ADGQFDAIVSI 125

                         90       100       110
                 ....*....|....*....|....*....|..
gi 165932358 261 FVLSAIVPDKMQKAINRLSRLLKPGGMMLLRD 292
Cdd:COG2230  126 GMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
PRK08317 PRK08317
hypothetical protein; Provisional
 183-286 1.53e-05

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 45.70  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932358 183 RILEVGCGVGNTVFPILQTNNDPGLfVYCCDFSSTAIELVQTNSEYDPSRCFaFVHDlcDEEKSyPVPKGSLDIIILIFV 262
Cdd:PRK08317  22 RVLDVGCGPGNDARELARRVGPEGR-VVGIDRSEAMLALAKERAAGLGPNVE-FVRG--DADGL-PFPDGSFDAVRSDRV 96

                         90       100
                 ....*....|....*....|....
gi 165932358 263 LSAIvPDKmQKAINRLSRLLKPGG 286
Cdd:PRK08317  97 LQHL-EDP-ARALAEIARVLRPGG 118
 
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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