ID G5C017_HETGA Unreviewed; 373 AA.
AC G5C017;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=tRNA methyltransferase 10 homolog C {ECO:0000256|ARBA:ARBA00014681};
DE EC=2.1.1.218 {ECO:0000256|ARBA:ARBA00012794};
DE EC=2.1.1.221 {ECO:0000256|ARBA:ARBA00012797};
DE AltName: Full=Mitochondrial ribonuclease P protein 1 {ECO:0000256|ARBA:ARBA00030623};
DE AltName: Full=RNA (guanine-9-)-methyltransferase domain-containing protein 1 {ECO:0000256|ARBA:ARBA00029803};
DE AltName: Full=mRNA methyladenosine-N(1)-methyltransferase {ECO:0000256|ARBA:ARBA00031759};
DE AltName: Full=tRNA (adenine(9)-N(1))-methyltransferase {ECO:0000256|ARBA:ARBA00033019};
DE AltName: Full=tRNA (guanine(9)-N(1))-methyltransferase {ECO:0000256|ARBA:ARBA00029727};
GN ORFNames=GW7_00835 {ECO:0000313|EMBL:EHB14878.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB14878.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB14878.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methyladenosine(9) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43148, Rhea:RHEA-COMP:10363, Rhea:RHEA-COMP:10364,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.218;
CC Evidence={ECO:0000256|ARBA:ARBA00001023};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an adenosine in mRNA + S-adenosyl-L-methionine = an N(1)-
CC methyladenosine in mRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:55392, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12415,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491;
CC Evidence={ECO:0000256|ARBA:ARBA00033688};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43156, Rhea:RHEA-COMP:10367, Rhea:RHEA-COMP:10368,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.221;
CC Evidence={ECO:0000256|ARBA:ARBA00000855};
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DR EMBL; JH172624; EHB14878.1; -; Genomic_DNA.
DR AlphaFoldDB; G5C017; -.
DR STRING; 10181.G5C017; -.
DR eggNOG; KOG2967; Eukaryota.
DR InParanoid; G5C017; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0160106; F:tRNA (adenine(9)-N1)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0052905; F:tRNA (guanosine(9)-N1)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:InterPro.
DR CDD; cd18102; Trm10_MRRP1; 1.
DR Gene3D; 3.40.1280.30; -; 1.
DR InterPro; IPR028564; MT_TRM10-typ.
DR InterPro; IPR038459; MT_TRM10-typ_sf.
DR InterPro; IPR025812; Trm10_C_MTase_dom.
DR InterPro; IPR007356; tRNA_m1G_MeTrfase_euk.
DR InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR PANTHER; PTHR13563; TRNA (GUANINE-9-) METHYLTRANSFERASE; 1.
DR PANTHER; PTHR13563:SF5; TRNA METHYLTRANSFERASE 10 HOMOLOG C; 1.
DR Pfam; PF01746; tRNA_m1G_MT; 1.
DR PROSITE; PS51675; SAM_MT_TRM10; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 151..343
FT /note="SAM-dependent MTase TRM10-type"
FT /evidence="ECO:0000259|PROSITE:PS51675"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 99..135
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 373 AA; 43440 MW; FF0D7F9455B7D5C2 CRC64;
MSSKIPAVSY PDKDNASPPA QLELDGWKTT MKSSVQEEAV FTVPSNKDED TPAATRRLIE
MWRLLGRNVP EHITEEELKN IMECASKKSK QKYLKFLYIK ENLKKAKQNK KEMKAAKKEA
KKAQLLETTE EDEQQNVLFL RLWNIKETIA MGWKGAQAMQ FGQPLVFDMA YDNYMKPEEL
NNTIRQLLES EGCNRRDVDP FHIYFCNLKP DSAYHRELVK RYGKKWDKLF LTATEKSYVD
LFPKNNIIYL TADSPNVMTT YKHDKIYIVG SFVDKNMQPG ISLAKAKRLN LTTECLPLDK
YLQWSTGNKN LTLDQMMHIL LCLKNTGNWE EAMKFVPRRK HTGFLDISEH SRGFVNRLKK
AKTFNSFPKH TFK
//
