ID A0A671URG8_SPAAU Unreviewed; 624 AA.
AC A0A671URG8;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=tRNA (guanine(26)-N(2))-dimethyltransferase {ECO:0000256|PROSITE-ProRule:PRU00958};
DE EC=2.1.1.216 {ECO:0000256|PROSITE-ProRule:PRU00958};
GN Name=TRMT1L {ECO:0000313|Ensembl:ENSSAUP00010017052.1};
OS Sparus aurata (Gilthead sea bream).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Spariformes; Sparidae; Sparus.
OX NCBI_TaxID=8175 {ECO:0000313|Ensembl:ENSSAUP00010017052.1, ECO:0000313|Proteomes:UP000472265};
RN [1] {ECO:0000313|Ensembl:ENSSAUP00010017052.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: May play a role in motor coordination and exploratory
CC behavior. {ECO:0000256|ARBA:ARBA00003652}.
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; A0A671URG8; -.
DR Ensembl; ENSSAUT00010018034.1; ENSSAUP00010017052.1; ENSSAUG00010007735.1.
DR GeneTree; ENSGT00530000063646; -.
DR Proteomes; UP000472265; Unplaced.
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:0007610; P:behavior; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
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 InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002905; Trm1.
DR InterPro; IPR042296; tRNA_met_Trm1_C.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR10631; N 2 ,N 2 -DIMETHYLGUANOSINE TRNA METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10631:SF1; TRMT1-LIKE PROTEIN; 1.
DR Pfam; PF02005; TRM; 2.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51626; SAM_MT_TRM1; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 3: Inferred from homology;
KW Behavior {ECO:0000256|ARBA:ARBA00022610};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU00958}; Reference proteome {ECO:0000313|Proteomes:UP000472265};
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}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 98..125
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 510..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 624 AA; 69718 MW; E98366DBF1AC3E50 CRC64;
EKKIDLHPRL VTLPPSIQFH SFEFLIFQPS CPLCPEEKFK ACYSHKLRRH LQNLHWKVYV
EFEGQRMCIC HLPCRNLKPS LSGDQVRNET HKLHVAHYHC VVCSVTIARK TDMISHLKRH
VNKGETEASY SGNSDAYEIM KELGTNVQLL PNHTTPQKSD TYFNRKMKTN RQLVFCSLAV
LAEERNPLEC LDAFGATGIM GLQWAKHLRN AVKVTITDIS DTCVKMIKEN CELNHIRAEG
GSRVPRGPDG TSSEAKGVSI ATVEVAKMDA NVIMHLRPFD YIHLDPYGTA VNYLDAAFRN
IRNLGIISVT STDTGSLYSK SPNVTLRHYG CHIVRTEYYK ELAARMVVAT VARAAARCNK
GIEVLLAVAL EHFVLVVVRV LRGPTQADES AKKLRKLVHC QWCEERVFLK QGNMVDVSPP
DTLPCNCHGS LPGKTAVQLG PLWCGPLFNT GFLRRMLSAA VQHSMDDIQP LVKTLICESE
CTTLKSLVHG PSALTNQVEC GVVIKTLQSG EESGPADQSG KRKTGEESGN VVKKLKSDAS
LEHPSFYYSI HRHSIKGMNM PKLNKFLQYL TEAGFRVSRT HFDPTGVRTD ATLEQFKSVL
TKYSVPTYTN ATATQTSVSM QKTV
//
