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Conserved domains on  [gi|117647226|ref|NP_060289|]
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tRNA methyltransferase 10 homolog C precursor [Homo sapiens]

Protein Classification

tRNA methyltransferase 10 homolog C( domain architecture ID 13031078)

tRNA methyltransferase 10 homolog C (TRMT10C) is a mitochondrial tRNA N(1)-methyltransferase involved in mitochondrial tRNA maturation

CATH:  3.40.1280.10
EC:  2.1.1.218|2.1.1.221
Gene Symbol:  TRMT10C
Gene Ontology:  GO:0097745|GO:0160106|GO:1904047|GO:0003723|GO:0032259|GO:0052905
PubMed:  17338813|11763972|30457841|18029778

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Trm10_MRRP1 cd18102
Mitochondrial ribonuclease P protein 1; Mitochondrial ribonuclease P protein 1 (or tRNA ...
 203-380 2.19e-95

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: 282.89  E-value: 2.19e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647226 203 QPLVFDMAYENYMKRKELQNTVSQLLESEGWNRRNVDPFHIYFCNLKIDGALH-RELVKRYQEKWDKLLLTSTEKSHVDL 281
Cdd:cd18102    1 QPLVIDMSYEDLMSPREIKNTARQLLEAYSANRRSTEPFHLHFCNLDPDGESIkRLLRLIPKLSLDKFPITVTEKSYLDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647226 282 FPKDSIIYLTADSPNVMTTFRHDKVYVIGSFVDKSMQPGTSLAKAKRLNLATECLPLDKYLQWEIGNKNLTLDQMIRILL 361
Cdd:cd18102   81 FPKEKLVYLSPDAPEVLKEFDPDKVYIIGGLVDKSTKKPLSLAKAKKEGIRMARLPLDRYLKWGGGSKSLTLNQVVSILL 160

                        170
                 ....*....|....*....
gi 117647226 362 CLKNNGNWQEALQFVPKRK 380
Cdd:cd18102  161 DLKDTGDWKEALKHVPPRK 179
 
Name Accession Description Interval E-value
Trm10_MRRP1 cd18102
Mitochondrial ribonuclease P protein 1; Mitochondrial ribonuclease P protein 1 (or tRNA ...
 203-380 2.19e-95

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: 282.89  E-value: 2.19e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647226 203 QPLVFDMAYENYMKRKELQNTVSQLLESEGWNRRNVDPFHIYFCNLKIDGALH-RELVKRYQEKWDKLLLTSTEKSHVDL 281
Cdd:cd18102    1 QPLVIDMSYEDLMSPREIKNTARQLLEAYSANRRSTEPFHLHFCNLDPDGESIkRLLRLIPKLSLDKFPITVTEKSYLDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647226 282 FPKDSIIYLTADSPNVMTTFRHDKVYVIGSFVDKSMQPGTSLAKAKRLNLATECLPLDKYLQWEIGNKNLTLDQMIRILL 361
Cdd:cd18102   81 FPKEKLVYLSPDAPEVLKEFDPDKVYIIGGLVDKSTKKPLSLAKAKKEGIRMARLPLDRYLKWGGGSKSLTLNQVVSILL 160

                        170
                 ....*....|....*....
gi 117647226 362 CLKNNGNWQEALQFVPKRK 380
Cdd:cd18102  161 DLKDTGDWKEALKHVPPRK 179
tRNA_m1G_MT pfam01746
tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC: ...
 213-380 6.66e-53

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: 174.46  E-value: 6.66e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647226  213 NYMKRKELQNTVSQLLESEGWNRRNVDPFHIYFCNLKIDGALHRELVKRYQ---EKWDKLLLTST-----EKSHVDLFPK 284
Cdd:pfam01746   1 GLAQEKGLVSLVVQNLRDYTANRRNTVDDEPYGGGFGMVLKPEPEFEALESvnyEKWKVILLTPTgkpffQEGAVDLSQK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647226  285 DSIIYLTADSPNVMTTFRHDKVYVIGSFVDKSMQPGT----SLAKAKRLNLATECLPLDKYLQWEIG-NKNLTLDQMIRI 359
Cdd:pfam01746  81 EHLVYLCGDYEGVDERVDDDKEYSIGDFVDKGGEKGAlvliDLVKRLLPGVLTASLPIDSFLLEKPHyTRPLTLNQVPEI 160

                         170       180
                  ....*....|....*....|..
gi 117647226  360 LLCLKNNGNWQEAL-QFVPKRK 380
Cdd:pfam01746 161 LLSGNHIRNWKEALlRTIPRRK 182
 
Name Accession Description Interval E-value
Trm10_MRRP1 cd18102
Mitochondrial ribonuclease P protein 1; Mitochondrial ribonuclease P protein 1 (or tRNA ...
 203-380 2.19e-95

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: 282.89  E-value: 2.19e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647226 203 QPLVFDMAYENYMKRKELQNTVSQLLESEGWNRRNVDPFHIYFCNLKIDGALH-RELVKRYQEKWDKLLLTSTEKSHVDL 281
Cdd:cd18102    1 QPLVIDMSYEDLMSPREIKNTARQLLEAYSANRRSTEPFHLHFCNLDPDGESIkRLLRLIPKLSLDKFPITVTEKSYLDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647226 282 FPKDSIIYLTADSPNVMTTFRHDKVYVIGSFVDKSMQPGTSLAKAKRLNLATECLPLDKYLQWEIGNKNLTLDQMIRILL 361
Cdd:cd18102   81 FPKEKLVYLSPDAPEVLKEFDPDKVYIIGGLVDKSTKKPLSLAKAKKEGIRMARLPLDRYLKWGGGSKSLTLNQVVSILL 160

                        170
                 ....*....|....*....
gi 117647226 362 CLKNNGNWQEALQFVPKRK 380
Cdd:cd18102  161 DLKDTGDWKEALKHVPPRK 179
SPOUT_Trm10-like cd18089
tRNA methyltransferase Trm10-like; Family of tRNA methyltransferase Trm10-like proteins ...
 203-376 1.25e-53

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: 175.80  E-value: 1.25e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647226 203 QPLVFDMAYENYMKRKELQNTVSQLLESEGWNRRNVDPFHIYFCNLKIDGALHRELVKRYqEKWdKLLLTSTEKSHVDLF 282
Cdd:cd18089    1 PRIVIDLSFDDLMTEKEIRSLAKQLSRCYGANRRSEKPLRLHLTSFSGDLKQRLLKKSGA-ENW-KIITHEESLLEEEAF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647226 283 PKDSIIYLTADSPNVMTTFRHDKVYVIGSFVDKSMQPGTSLAKAKRLNLATECLPLDKYLQWEiGNKNLTLDQMIRILLC 362
Cdd:cd18089   79 PKEKLVYLTADAEEVLEELDPDKVYIIGGIVDRNRHKGLTLNKAEELGIRTARLPIREYIKLK-GRKVLTVNHVFEILLR 157

                        170
                 ....*....|....
gi 117647226 363 LKNNGNWQEALQFV 376
Cdd:cd18089  158 YLEGGDWKEALEEV 171
tRNA_m1G_MT pfam01746
tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC: ...
 213-380 6.66e-53

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: 174.46  E-value: 6.66e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647226  213 NYMKRKELQNTVSQLLESEGWNRRNVDPFHIYFCNLKIDGALHRELVKRYQ---EKWDKLLLTST-----EKSHVDLFPK 284
Cdd:pfam01746   1 GLAQEKGLVSLVVQNLRDYTANRRNTVDDEPYGGGFGMVLKPEPEFEALESvnyEKWKVILLTPTgkpffQEGAVDLSQK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647226  285 DSIIYLTADSPNVMTTFRHDKVYVIGSFVDKSMQPGT----SLAKAKRLNLATECLPLDKYLQWEIG-NKNLTLDQMIRI 359
Cdd:pfam01746  81 EHLVYLCGDYEGVDERVDDDKEYSIGDFVDKGGEKGAlvliDLVKRLLPGVLTASLPIDSFLLEKPHyTRPLTLNQVPEI 160

                         170       180
                  ....*....|....*....|..
gi 117647226  360 LLCLKNNGNWQEAL-QFVPKRK 380
Cdd:pfam01746 161 LLSGNHIRNWKEALlRTIPRRK 182
Trm10euk_B cd18100
eukaryotic tRNA m1G9 methyltransferase Trm10 homolog B; Eukaryotic tRNA m1G9 methyltransferase ...
 205-380 2.23e-42

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: 147.02  E-value: 2.23e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647226 205 LVFDMAYENYMKRKELQNTVSQLLESEGWNRRNVDPFHIYFCNLKIDGALHRELVkRYQEKWDKLLLTSTEKSHVDLFPK 284
Cdd:cd18100    3 VCIDLSLEHKMSEKEISKLAQQLRRLYGSNRKAEKPLHIYLTSFDKEGLLYKECV-RKNDGFENYLIDMTEESHSELFPK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647226 285 DSIIYLTADSPNVMTTFRHDKVYVIGSFVDKSMQPGTSLAKAKRLNLATECLPLDKYLQWEIGNKN----LTLDQMIRIL 360
Cdd:cd18100   82 EEIVYLSPDSENVLESIDPNKVYVIGGLVDESIQKKLTLQKAKEHGIQTARLPIDEYMVKADGKGNystvLAINQVFDIL 161

                        170       180
                 ....*....|....*....|.
gi 117647226 361 LCLKNNGNWQEALQF-VPKRK 380
Cdd:cd18100  162 LKYYETGDWREALSAgVPQRK 182
Trm10euk_A cd18101
eukaryotic tRNA m1G9 methyltransferase Trm10 homolog A; Eukaryotic tRNA m1G9 methyltransferase ...
 205-380 6.03e-35

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: 126.95  E-value: 6.03e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647226 205 LVFDMAYENYMKRKELQNTVSQLLESEGWNRRNVDPFHIYFCNLKIDGALHRELVKRYQeKWDKLLltsTEKSHVDLFPK 284
Cdd:cd18101    3 VAIDCSFDDLMTEKDIKKLVKQIQRCYAENRRADNPVQLYLTSLGGKTKENMEKDKGYE-NWDVNF---KEEHYLEVFKK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647226 285 DSIIYLTADSPNVMTTFRHDKVYVIGSFVDKSMQPGTSLAKAKRLNLATECLPLDKYLQWEIgNKNLTLDQMIRILLCLK 364
Cdd:cd18101   79 EDIVYLTSDSPNVLEDLDEDKVYIIGGLVDHNHHKGLCYKRAVELGIQHARLPIDEYVKMKT-RKVLTINHVFEILLRYT 157

                        170
                 ....*....|....*..
gi 117647226 365 NNGNWQEA-LQFVPKRK 380
Cdd:cd18101  158 EGKDWKEAfFKVIPQRK 174
 
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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