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Conserved domains on  [gi|17539998|ref|NP_501789|]
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tRNA methyltransferase 10 homolog A [Caenorhabditis elegans]

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
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 ...
 87-260 7.38e-95

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: 277.56  E-value: 7.38e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539998  87 QRIALDMSFDDLMIEKDQKRTVQQIGWCYTANRHSPDPFQFHVVGFDGPSRKIYDGNEHNLNQDIHLHQEKLENLFKPEE 166
Cdd:cd18101   1 IRVAIDCSFDDLMTEKDIKKLVKQIQRCYAENRRADNPVQLYLTSLGGKTKENMEKDKGYENWDVNFKEEHYLEVFKKED 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539998 167 IVYLTSESENVLSDLDDTKVYVIGGIVDHNSQKGLCYRIAQEKGFGHAKLPLDEHLLMKSRRVLTINQVYEILVHYSVHK 246
Cdd:cd18101  81 IVYLTSDSPNVLEDLDEDKVYIIGGLVDHNHHKGLCYKRAVELGIQHARLPIDEYVKMKTRKVLTINHVFEILLRYTEGK 160

                       170
                ....*....|....
gi 17539998 247 NWKDALLSIIPERK 260
Cdd:cd18101 161 DWKEAFFKVIPQRK 174
 
Name Accession Description Interval E-value
Trm10euk_A cd18101
eukaryotic tRNA m1G9 methyltransferase Trm10 homolog A; Eukaryotic tRNA m1G9 methyltransferase ...
 87-260 7.38e-95

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: 277.56  E-value: 7.38e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539998  87 QRIALDMSFDDLMIEKDQKRTVQQIGWCYTANRHSPDPFQFHVVGFDGPSRKIYDGNEHNLNQDIHLHQEKLENLFKPEE 166
Cdd:cd18101   1 IRVAIDCSFDDLMTEKDIKKLVKQIQRCYAENRRADNPVQLYLTSLGGKTKENMEKDKGYENWDVNFKEEHYLEVFKKED 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539998 167 IVYLTSESENVLSDLDDTKVYVIGGIVDHNSQKGLCYRIAQEKGFGHAKLPLDEHLLMKSRRVLTINQVYEILVHYSVHK 246
Cdd:cd18101  81 IVYLTSDSPNVLEDLDEDKVYIIGGLVDHNHHKGLCYKRAVELGIQHARLPIDEYVKMKTRKVLTINHVFEILLRYTEGK 160

                       170
                ....*....|....
gi 17539998 247 NWKDALLSIIPERK 260
Cdd:cd18101 161 DWKEAFFKVIPQRK 174
tRNA_m1G_MT pfam01746
tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC: ...
 97-260 5.19e-39

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: 135.17  E-value: 5.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539998    97 DLMIEKDQKRTVQQIGWCYTANRHSPDPFQFHVVGFD--GPSRKIYDGNE-------HNLN---QDIHLHQEKLENLFKP 164
Cdd:pfam01746   1 GLAQEKGLVSLVVQNLRDYTANRRNTVDDEPYGGGFGmvLKPEPEFEALEsvnyekwKVILltpTGKPFFQEGAVDLSQK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539998   165 EEIVYLTSESENVLSDLDDTKVYVIGGIVDHNSQKGL----CYRIAQEKGFGHAKLPLDEHLLMKS--RRVLTINQVYEI 238
Cdd:pfam01746  81 EHLVYLCGDYEGVDERVDDDKEYSIGDFVDKGGEKGAlvliDLVKRLLPGVLTASLPIDSFLLEKPhyTRPLTLNQVPEI 160

                         170       180
                  ....*....|....*....|..
gi 17539998   239 LVHYSVHKNWKDALLSIIPERK 260
Cdd:pfam01746 161 LLSGNHIRNWKEALLRTIPRRK 182
 
Name Accession Description Interval E-value
Trm10euk_A cd18101
eukaryotic tRNA m1G9 methyltransferase Trm10 homolog A; Eukaryotic tRNA m1G9 methyltransferase ...
 87-260 7.38e-95

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: 277.56  E-value: 7.38e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539998  87 QRIALDMSFDDLMIEKDQKRTVQQIGWCYTANRHSPDPFQFHVVGFDGPSRKIYDGNEHNLNQDIHLHQEKLENLFKPEE 166
Cdd:cd18101   1 IRVAIDCSFDDLMTEKDIKKLVKQIQRCYAENRRADNPVQLYLTSLGGKTKENMEKDKGYENWDVNFKEEHYLEVFKKED 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539998 167 IVYLTSESENVLSDLDDTKVYVIGGIVDHNSQKGLCYRIAQEKGFGHAKLPLDEHLLMKSRRVLTINQVYEILVHYSVHK 246
Cdd:cd18101  81 IVYLTSDSPNVLEDLDEDKVYIIGGLVDHNHHKGLCYKRAVELGIQHARLPIDEYVKMKTRKVLTINHVFEILLRYTEGK 160

                       170
                ....*....|....
gi 17539998 247 NWKDALLSIIPERK 260
Cdd:cd18101 161 DWKEAFFKVIPQRK 174
SPOUT_Trm10-like cd18089
tRNA methyltransferase Trm10-like; Family of tRNA methyltransferase Trm10-like proteins ...
 87-255 2.22e-70

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: 215.09  E-value: 2.22e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539998  87 QRIALDMSFDDLMIEKDQKRTVQQIGWCYTANRHSPDPFQFHVVGFDGP--SRKIYDGNEHNLNQDIHLHQEKLENLFKP 164
Cdd:cd18089   1 PRIVIDLSFDDLMTEKEIRSLAKQLSRCYGANRRSEKPLRLHLTSFSGDlkQRLLKKSGAENWKIITHEESLLEEEAFPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539998 165 EEIVYLTSESENVLSDLDDTKVYVIGGIVDHNSQKGLCYRIAQEKGFGHAKLPLDEHLLMKSRRVLTINQVYEILVHYSV 244
Cdd:cd18089  81 EKLVYLTADAEEVLEELDPDKVYIIGGIVDRNRHKGLTLNKAEELGIRTARLPIREYIKLKGRKVLTVNHVFEILLRYLE 160

                       170
                ....*....|.
gi 17539998 245 HKNWKDALLSI 255
Cdd:cd18089 161 GGDWKEALEEV 171
Trm10euk_B cd18100
eukaryotic tRNA m1G9 methyltransferase Trm10 homolog B; Eukaryotic tRNA m1G9 methyltransferase ...
 87-260 1.81e-51

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: 167.44  E-value: 1.81e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539998  87 QRIALDMSFDDLMIEKDQKRTVQQIGWCYTANRHSPDPFQFHVVGFDgPSRKIY-------DGNEHNLnqdIHLHQEKLE 159
Cdd:cd18100   1 LRVCIDLSLEHKMSEKEISKLAQQLRRLYGSNRKAEKPLHIYLTSFD-KEGLLYkecvrknDGFENYL---IDMTEESHS 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539998 160 NLFKPEEIVYLTSESENVLSDLDDTKVYVIGGIVDHNSQKGLCYRIAQEKGFGHAKLPLDEHLLMKSR-----RVLTINQ 234
Cdd:cd18100  77 ELFPKEEIVYLSPDSENVLESIDPNKVYVIGGLVDESIQKKLTLQKAKEHGIQTARLPIDEYMVKADGkgnysTVLAINQ 156

                       170       180
                ....*....|....*....|....*.
gi 17539998 235 VYEILVHYSVHKNWKDALLSIIPERK 260
Cdd:cd18100 157 VFDILLKYYETGDWREALSAGVPQRK 182
Trm10_MRRP1 cd18102
Mitochondrial ribonuclease P protein 1; Mitochondrial ribonuclease P protein 1 (or tRNA ...
 87-259 8.09e-48

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: 157.70  E-value: 8.09e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539998  87 QRIALDMSFDDLMIEKDQKRTVQQIGWCYTANRHSPDPFQFHVVGFDGPSRKIYDGNEHNLNQD-----IHLHQEKLENL 161
Cdd:cd18102   1 QPLVIDMSYEDLMSPREIKNTARQLLEAYSANRRSTEPFHLHFCNLDPDGESIKRLLRLIPKLSldkfpITVTEKSYLDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539998 162 FKPEEIVYLTSESENVLSDLDDTKVYVIGGIVDHNSQKGLCYRIAQEKGFGHAKLPLDEHLLMK-SRRVLTINQVYEILV 240
Cdd:cd18102  81 FPKEKLVYLSPDAPEVLKEFDPDKVYIIGGLVDKSTKKPLSLAKAKKEGIRMARLPLDRYLKWGgGSKSLTLNQVVSILL 160

                       170
                ....*....|....*....
gi 17539998 241 HYSVHKNWKDALLSIIPER 259
Cdd:cd18102 161 DLKDTGDWKEALKHVPPRK 179
tRNA_m1G_MT pfam01746
tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC: ...
 97-260 5.19e-39

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: 135.17  E-value: 5.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539998    97 DLMIEKDQKRTVQQIGWCYTANRHSPDPFQFHVVGFD--GPSRKIYDGNE-------HNLN---QDIHLHQEKLENLFKP 164
Cdd:pfam01746   1 GLAQEKGLVSLVVQNLRDYTANRRNTVDDEPYGGGFGmvLKPEPEFEALEsvnyekwKVILltpTGKPFFQEGAVDLSQK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539998   165 EEIVYLTSESENVLSDLDDTKVYVIGGIVDHNSQKGL----CYRIAQEKGFGHAKLPLDEHLLMKS--RRVLTINQVYEI 238
Cdd:pfam01746  81 EHLVYLCGDYEGVDERVDDDKEYSIGDFVDKGGEKGAlvliDLVKRLLPGVLTASLPIDSFLLEKPhyTRPLTLNQVPEI 160

                         170       180
                  ....*....|....*....|..
gi 17539998   239 LVHYSVHKNWKDALLSIIPERK 260
Cdd:pfam01746 161 LLSGNHIRNWKEALLRTIPRRK 182
Trm10arch cd18099
archaeal tRNA(m1G9/m1A9)-methyltransferase Trm10; Archaeal tRNA(m1G9/m1A9)-methyltransferase ...
 88-239 4.71e-06

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: 45.85  E-value: 4.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539998  88 RIALDMSFDDLMIEKDQKRTVQQIGWCYTANRHSPDPFQFHVVG----FDGPSRKIYDGNEHNlnqdiHLHQEKLENlfk 163
Cdd:cd18099   2 YFIIDLSLWDLHTEKEKKKLVLQVLLSIGVIRKYLWDGNLVLTWansmFLEMLNKVESLSLYT-----VGLKEKGED--- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539998 164 peEIVYLTSESENVLS--DLDDTKVYVIGGIVDHN-SQKGLCYRIAQEkgfghaklpLDEHLLMKSRRVL---------- 230
Cdd:cd18099  74 --NAVLLDPYAEEVATedIIRDTKAFIIGGIVDKGgNKKGATTELGEL---------LGGAIEVPRRKIVlrgsivgvpd 142


                ....*....
gi 17539998 231 TINQVYEIL 239
Cdd:cd18099 143 RINKILEII 151
 
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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