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Database: UniProt
Entry: A0A674MRQ3_TAKRU
LinkDB: A0A674MRQ3_TAKRU
Original site: A0A674MRQ3_TAKRU 
ID   A0A674MRQ3_TAKRU        Unreviewed;       598 AA.
AC   A0A674MRQ3;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=tRNA (guanine(26)-N(2))-dimethyltransferase {ECO:0000256|ARBA:ARBA00039099, ECO:0000256|PROSITE-ProRule:PRU00958};
DE            EC=2.1.1.216 {ECO:0000256|ARBA:ARBA00039099, ECO:0000256|PROSITE-ProRule:PRU00958};
GN   Name=TRMT1 {ECO:0000313|Ensembl:ENSTRUP00000063670.1};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000063670.1, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000063670.1, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000063670.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) +
CC         N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43140, Rhea:RHEA-COMP:10359, Rhea:RHEA-COMP:10360,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74513; EC=2.1.1.216;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU00958};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Trm1 family. {ECO:0000256|PROSITE-ProRule:PRU00958}.
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DR   AlphaFoldDB; A0A674MRQ3; -.
DR   Ensembl; ENSTRUT00000062036.1; ENSTRUP00000063670.1; ENSTRUG00000010700.3.
DR   GeneTree; ENSGT00530000063646; -.
DR   Proteomes; UP000005226; Chromosome 17.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0160102; F:tRNA (guanine(10)-N2)-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0160104; F:tRNA (guanine(26)-N2)-dimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProt.
DR   Gene3D; 3.30.56.70; N2,N2-dimethylguanosine tRNA methyltransferase, C-terminal domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002905; Trm1.
DR   InterPro; IPR042296; tRNA_met_Trm1_C.
DR   InterPro; IPR041367; Znf-CCCH_4.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   NCBIfam; TIGR00308; TRM1; 1.
DR   PANTHER; PTHR10631; N 2 ,N 2 -DIMETHYLGUANOSINE TRNA METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10631:SF3; TRNA (GUANINE(26)-N(2))-DIMETHYLTRANSFERASE; 1.
DR   Pfam; PF02005; TRM; 1.
DR   Pfam; PF18044; zf-CCCH_4; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   SUPFAM; SSF90229; CCCH zinc finger; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51626; SAM_MT_TRM1; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00723};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU00958}; Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00958};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU00958};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00958}; tRNA processing {ECO:0000256|PROSITE-ProRule:PRU00958};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE-
KW   ProRule:PRU00958};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}.
FT   DOMAIN          561..588
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         561..588
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          78..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..101
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   598 AA;  66190 MW;  8BF0BF9EF7819B1F CRC64;
     KVSVDRYSAT ELLPGETVVK EGKAAILFPS ANEVFYNPVQ EFNRDLTCAV ITEFARELLV
     QRGVKLVVPG EEDRVVVSLG EEEVEEEKKE EEEEEEEEKN GADEPALTAT VGEKCEGLRV
     LEGLAASGLR SVRFALEVPG LQSITANDFS AKAAALIARN AMYNGVSHLI QASCKDASML
     MYEMRGKKQR YDVIDLDPYG SPATFLDAAV QAVSDGGLLC VTCTDMAVMA GNSGETCYSK
     YGSVSIKSKY CHEMALRIIL HSLDQRAGVY QRYIQPLLSI SADFYIRVFV RVFTGQATVK
     NSASKQALVY NCTGCGSFYL QRMGRRTSNG RHGTRSTSCK AQVFVKVDVI KTASLLLQLG
     GPLWAEAIHD LTFVQKVLSA LSANPGRFGT SKRIEGVLSM VTEELEDVPF YYTLDSLSSS
     IRCNTPPMLQ FRSALLHAGY KVSLSHACKN AIKTDAPPAT MWDIMRCWEK IHPVKREKLS
     NTSPSFRILS KEPSLEACFT VREDANPQSR RRHLTRFQEN PQAFWGPKAR AKAGGGISDN
     LQDKRKKFQN KRKNQITESS ELKKFPCKKF RKGTCTYGDQ CSYSHDSGLG LSSRCPPV
//
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