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Conserved domains on  [gi|22748659|ref|NP_689505|]
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tRNA methyltransferase 10 homolog A isoform 1 [Homo sapiens]

Protein Classification

tRNA methyltransferase 10 homolog A( domain architecture ID 13031076)

tRNA methyltransferase 10 homolog A (TRMT10A) is a S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in tRNAs

EC:  2.1.1.221
Gene Symbol:  TRMT10A
Gene Ontology:  GO:0008033|GO:0009019
PubMed:  17338813|30457841

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Trm10euk_A cd18101
eukaryotic tRNA m1G9 methyltransferase Trm10 homolog A; Eukaryotic tRNA m1G9 methyltransferase ...
 101-276 1.01e-112

eukaryotic tRNA m1G9 methyltransferase Trm10 homolog A; Eukaryotic tRNA m1G9 methyltransferase Trm10 homolog A (TM10A) catalyzes the N(1) methylation of guanine at Position 9 (m(1)G9) of tRNA, which might play a role in the stabilization of tRNA and in translation termination efficiency. Trm10 is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.


:

Pssm-ID: 349974  Cd Length: 174  Bit Score: 324.56  E-value: 1.01e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748659 101 LRLIIDCSFDHLMVLKDIKKLHKQIQRCYAENRRALHPVQFYLTSHGGQLKKNMdENDKGWVNWkDIHIKPEHYSELIKK 180
Cdd:cd18101   1 IRVAIDCSFDDLMTEKDIKKLVKQIQRCYAENRRADNPVQLYLTSLGGKTKENM-EKDKGYENW-DVNFKEEHYLEVFKK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748659 181 EDLIYLTSDSPNILKELDESKAYVIGGLVDHNHHKGLTYKQASDYGINHAQLPLGNFVKMNSRKVLAVNHVFEIILEYLE 260
Cdd:cd18101  79 EDIVYLTSDSPNVLEDLDEDKVYIIGGLVDHNHHKGLCYKRAVELGIQHARLPIDEYVKMKTRKVLTINHVFEILLRYTE 158

                       170
                ....*....|....*.
gi 22748659 261 TRDWQEAFFTILPQRK 276
Cdd:cd18101 159 GKDWKEAFFKVIPQRK 174
 
Name Accession Description Interval E-value
Trm10euk_A cd18101
eukaryotic tRNA m1G9 methyltransferase Trm10 homolog A; Eukaryotic tRNA m1G9 methyltransferase ...
 101-276 1.01e-112

eukaryotic tRNA m1G9 methyltransferase Trm10 homolog A; Eukaryotic tRNA m1G9 methyltransferase Trm10 homolog A (TM10A) catalyzes the N(1) methylation of guanine at Position 9 (m(1)G9) of tRNA, which might play a role in the stabilization of tRNA and in translation termination efficiency. Trm10 is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.


Pssm-ID: 349974  Cd Length: 174  Bit Score: 324.56  E-value: 1.01e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748659 101 LRLIIDCSFDHLMVLKDIKKLHKQIQRCYAENRRALHPVQFYLTSHGGQLKKNMdENDKGWVNWkDIHIKPEHYSELIKK 180
Cdd:cd18101   1 IRVAIDCSFDDLMTEKDIKKLVKQIQRCYAENRRADNPVQLYLTSLGGKTKENM-EKDKGYENW-DVNFKEEHYLEVFKK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748659 181 EDLIYLTSDSPNILKELDESKAYVIGGLVDHNHHKGLTYKQASDYGINHAQLPLGNFVKMNSRKVLAVNHVFEIILEYLE 260
Cdd:cd18101  79 EDIVYLTSDSPNVLEDLDEDKVYIIGGLVDHNHHKGLCYKRAVELGIQHARLPIDEYVKMKTRKVLTINHVFEILLRYTE 158

                       170
                ....*....|....*.
gi 22748659 261 TRDWQEAFFTILPQRK 276
Cdd:cd18101 159 GKDWKEAFFKVIPQRK 174
tRNA_m1G_MT pfam01746
tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC: ...
 112-276 9.58e-32

tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC:2.1.1.31. In E.coli K12 this enzyme catalyzes the conversion of a guanosine residue to N1-methylguanine in position 37, next to the anticodon, in tRNA.


Pssm-ID: 396350  Cd Length: 182  Bit Score: 117.45  E-value: 9.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748659   112 LMVLKDIKKLHKQIQRCYAENRRALHPVQFYLTSHGGQLKKNMDE---NDKGWVNWKDIHIKPEHYS-------ELIKKE 181
Cdd:pfam01746   2 LAQEKGLVSLVVQNLRDYTANRRNTVDDEPYGGGFGMVLKPEPEFealESVNYEKWKVILLTPTGKPffqegavDLSQKE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748659   182 DLIYLTSDSPNILKELDESKAYVIGGLVDHNHHKGL----TYKQASDYGINHAQLPLGNFVKM--NSRKVLAVNHVFEII 255
Cdd:pfam01746  82 HLVYLCGDYEGVDERVDDDKEYSIGDFVDKGGEKGAlvliDLVKRLLPGVLTASLPIDSFLLEkpHYTRPLTLNQVPEIL 161

                         170       180
                  ....*....|....*....|.
gi 22748659   256 LEYLETRDWQEAFFTILPQRK 276
Cdd:pfam01746 162 LSGNHIRNWKEALLRTIPRRK 182
 
Name Accession Description Interval E-value
Trm10euk_A cd18101
eukaryotic tRNA m1G9 methyltransferase Trm10 homolog A; Eukaryotic tRNA m1G9 methyltransferase ...
 101-276 1.01e-112

eukaryotic tRNA m1G9 methyltransferase Trm10 homolog A; Eukaryotic tRNA m1G9 methyltransferase Trm10 homolog A (TM10A) catalyzes the N(1) methylation of guanine at Position 9 (m(1)G9) of tRNA, which might play a role in the stabilization of tRNA and in translation termination efficiency. Trm10 is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.


Pssm-ID: 349974  Cd Length: 174  Bit Score: 324.56  E-value: 1.01e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748659 101 LRLIIDCSFDHLMVLKDIKKLHKQIQRCYAENRRALHPVQFYLTSHGGQLKKNMdENDKGWVNWkDIHIKPEHYSELIKK 180
Cdd:cd18101   1 IRVAIDCSFDDLMTEKDIKKLVKQIQRCYAENRRADNPVQLYLTSLGGKTKENM-EKDKGYENW-DVNFKEEHYLEVFKK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748659 181 EDLIYLTSDSPNILKELDESKAYVIGGLVDHNHHKGLTYKQASDYGINHAQLPLGNFVKMNSRKVLAVNHVFEIILEYLE 260
Cdd:cd18101  79 EDIVYLTSDSPNVLEDLDEDKVYIIGGLVDHNHHKGLCYKRAVELGIQHARLPIDEYVKMKTRKVLTINHVFEILLRYTE 158

                       170
                ....*....|....*.
gi 22748659 261 TRDWQEAFFTILPQRK 276
Cdd:cd18101 159 GKDWKEAFFKVIPQRK 174
SPOUT_Trm10-like cd18089
tRNA methyltransferase Trm10-like; Family of tRNA methyltransferase Trm10-like proteins ...
 101-271 8.10e-79

tRNA methyltransferase Trm10-like; Family of tRNA methyltransferase Trm10-like proteins catalyzes the N(1) methylation of guanine at position 9 (m(1)G9) of tRNA (eukaryotes) or N(1) methylation of guanine or adenine at position 9 (m1G9/m1A9) of tRNA (archaea), which might play a role in the stabilization of tRNA and in translation termination efficiency. Trm10 is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.


Pssm-ID: 349962  Cd Length: 171  Bit Score: 238.20  E-value: 8.10e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748659 101 LRLIIDCSFDHLMVLKDIKKLHKQIQRCYAENRRALHPVQFYLTSHGGQLKkNMDENDKGWVNWK-DIHIKPEHYSELIK 179
Cdd:cd18089   1 PRIVIDLSFDDLMTEKEIRSLAKQLSRCYGANRRSEKPLRLHLTSFSGDLK-QRLLKKSGAENWKiITHEESLLEEEAFP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748659 180 KEDLIYLTSDSPNILKELDESKAYVIGGLVDHNHHKGLTYKQASDYGINHAQLPLGNFVKMNSRKVLAVNHVFEIILEYL 259
Cdd:cd18089  80 KEKLVYLTADAEEVLEELDPDKVYIIGGIVDRNRHKGLTLNKAEELGIRTARLPIREYIKLKGRKVLTVNHVFEILLRYL 159

                       170
                ....*....|..
gi 22748659 260 ETRDWQEAFFTI 271
Cdd:cd18089 160 EGGDWKEALEEV 171
Trm10euk_B cd18100
eukaryotic tRNA m1G9 methyltransferase Trm10 homolog B; Eukaryotic tRNA m1G9 methyltransferase ...
 101-276 1.25e-55

eukaryotic tRNA m1G9 methyltransferase Trm10 homolog B; Eukaryotic tRNA m1G9 methyltransferase Trm10 homolog B (TM10B) catalyzes the N(1) methylation of guanine at Position 9 (m(1)G9) of tRNA, which might play a role in the stabilization of tRNA and in translation termination efficiency. Trm10 is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.


Pssm-ID: 349973  Cd Length: 182  Bit Score: 179.38  E-value: 1.25e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748659 101 LRLIIDCSFDHLMVLKDIKKLHKQIQRCYAENRRALHPVQFYLTS--HGGQLKKNMDENDKGWVNWKdIHIKPEHYSELI 178
Cdd:cd18100   1 LRVCIDLSLEHKMSEKEISKLAQQLRRLYGSNRKAEKPLHIYLTSfdKEGLLYKECVRKNDGFENYL-IDMTEESHSELF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748659 179 KKEDLIYLTSDSPNILKELDESKAYVIGGLVDHNHHKGLTYKQASDYGINHAQLPLGNFVKMNSRK-----VLAVNHVFE 253
Cdd:cd18100  80 PKEEIVYLSPDSENVLESIDPNKVYVIGGLVDESIQKKLTLQKAKEHGIQTARLPIDEYMVKADGKgnystVLAINQVFD 159

                       170       180
                ....*....|....*....|...
gi 22748659 254 IILEYLETRDWQEAFFTILPQRK 276
Cdd:cd18100 160 ILLKYYETGDWREALSAGVPQRK 182
Trm10_MRRP1 cd18102
Mitochondrial ribonuclease P protein 1; Mitochondrial ribonuclease P protein 1 (or tRNA ...
 103-275 1.61e-42

Mitochondrial ribonuclease P protein 1; Mitochondrial ribonuclease P protein 1 (or tRNA methyltransferase 10 homolog C) functions in mitochondrial tRNA maturation and is part of mitochondrial ribonuclease P, an enzyme composed of MRPP1/RG9MTD1, MRPP2/HSD17B10 and MRPP3/KIAA0391, which cleaves tRNA molecules in their 5'-ends. MRRP1 is related to Trm10, a tRNA m1G9 methyltransferase and is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.


Pssm-ID: 349975  Cd Length: 179  Bit Score: 145.37  E-value: 1.61e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748659 103 LIIDCSFDHLMVLKDIKKLHKQIQRCYAENRRALHPVQFYLTSHG------GQLKKNMDENDkgWVNWkDIHIKPEHYSE 176
Cdd:cd18102   3 LVIDMSYEDLMSPREIKNTARQLLEAYSANRRSTEPFHLHFCNLDpdgesiKRLLRLIPKLS--LDKF-PITVTEKSYLD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748659 177 LIKKEDLIYLTSDSPNILKELDESKAYVIGGLVDHNHHKGLTYKQASDYGINHAQLPLGNFVKMN-SRKVLAVNHVFEII 255
Cdd:cd18102  80 LFPKEKLVYLSPDAPEVLKEFDPDKVYIIGGLVDKSTKKPLSLAKAKKEGIRMARLPLDRYLKWGgGSKSLTLNQVVSIL 159

                       170       180
                ....*....|....*....|
gi 22748659 256 LEYLETRDWQEAFFTILPQR 275
Cdd:cd18102 160 LDLKDTGDWKEALKHVPPRK 179
tRNA_m1G_MT pfam01746
tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC: ...
 112-276 9.58e-32

tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC:2.1.1.31. In E.coli K12 this enzyme catalyzes the conversion of a guanosine residue to N1-methylguanine in position 37, next to the anticodon, in tRNA.


Pssm-ID: 396350  Cd Length: 182  Bit Score: 117.45  E-value: 9.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748659   112 LMVLKDIKKLHKQIQRCYAENRRALHPVQFYLTSHGGQLKKNMDE---NDKGWVNWKDIHIKPEHYS-------ELIKKE 181
Cdd:pfam01746   2 LAQEKGLVSLVVQNLRDYTANRRNTVDDEPYGGGFGMVLKPEPEFealESVNYEKWKVILLTPTGKPffqegavDLSQKE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748659   182 DLIYLTSDSPNILKELDESKAYVIGGLVDHNHHKGL----TYKQASDYGINHAQLPLGNFVKM--NSRKVLAVNHVFEII 255
Cdd:pfam01746  82 HLVYLCGDYEGVDERVDDDKEYSIGDFVDKGGEKGAlvliDLVKRLLPGVLTASLPIDSFLLEkpHYTRPLTLNQVPEIL 161

                         170       180
                  ....*....|....*....|.
gi 22748659   256 LEYLETRDWQEAFFTILPQRK 276
Cdd:pfam01746 162 LSGNHIRNWKEALLRTIPRRK 182
Trm10arch cd18099
archaeal tRNA(m1G9/m1A9)-methyltransferase Trm10; Archaeal tRNA(m1G9/m1A9)-methyltransferase ...
 102-260 1.32e-03

archaeal tRNA(m1G9/m1A9)-methyltransferase Trm10; Archaeal tRNA(m1G9/m1A9)-methyltransferase Trm10 catalyzes the N(1) methylation of guanine or adenine at position 9 (m1G9/m1A9) of tRNA, which might play a role in the stabilization of tRNA and in translation termination efficiency. Trm10 is a member of the SPOUT (SpoU-TrmD) methyltransferase (MTase) superfamily, a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.


Pssm-ID: 349972  Cd Length: 170  Bit Score: 38.92  E-value: 1.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748659 102 RLIIDCSFDHLMVLKDIKKLHKQIQRCYAENRRALHPVQFYLTshggqlkkNMDENDKGWVNWKDIHIKPEHYSELIKKE 181
Cdd:cd18099   2 YFIIDLSLWDLHTEKEKKKLVLQVLLSIGVIRKYLWDGNLVLT--------WANSMFLEMLNKVESLSLYTVGLKEKGED 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748659 182 DLIYLTSDSPNILKELD--ESKAYVIGGLVDHN-HHKGLTYKQASDYGINhaqlplgnfVKMNSRKVL----------AV 248
Cdd:cd18099  74 NAVLLDPYAEEVATEDIirDTKAFIIGGIVDKGgNKKGATTELGELLGGA---------IEVPRRKIVlrgsivgvpdRI 144

                       170
                ....*....|..
gi 22748659 249 NHVFEIILEYLE 260
Cdd:cd18099 145 NKILEIILRVIE 156
 
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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