ID A0A2Y9KP17_ENHLU Unreviewed; 328 AA.
AC A0A2Y9KP17;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=tRNA N(3)-methylcytidine methyltransferase {ECO:0000256|PIRNR:PIRNR037755};
DE EC=2.1.1.- {ECO:0000256|PIRNR:PIRNR037755};
GN Name=LOC111158133 {ECO:0000313|RefSeq:XP_022375717.1,
GN ECO:0000313|RefSeq:XP_022375719.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022375717.1};
RN [1] {ECO:0000313|RefSeq:XP_022375717.1, ECO:0000313|RefSeq:XP_022375719.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022375717.1,
RC ECO:0000313|RefSeq:XP_022375719.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase.
CC {ECO:0000256|PIRNR:PIRNR037755}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(32) in tRNA(Arg)(CCU) + S-adenosyl-L-methionine =
CC H(+) + N(3)-methylcytidine(32) in tRNA(Arg)(CCU) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60912, Rhea:RHEA-COMP:15710, Rhea:RHEA-
CC COMP:15712, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74894, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000256|ARBA:ARBA00036328};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60913;
CC Evidence={ECO:0000256|ARBA:ARBA00036328};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(32) in tRNA(Thr) + S-adenosyl-L-methionine = H(+) +
CC N(3)-methylcytidine(32) in tRNA(Thr) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:50960, Rhea:RHEA-COMP:12850, Rhea:RHEA-COMP:12852,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74894, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000256|ARBA:ARBA00037010};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50961;
CC Evidence={ECO:0000256|ARBA:ARBA00037010};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METL family.
CC {ECO:0000256|ARBA:ARBA00009725, ECO:0000256|PIRNR:PIRNR037755}.
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DR RefSeq; XP_022375717.1; XM_022520009.1.
DR RefSeq; XP_022375719.1; XM_022520011.1.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:UniProt.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProt.
DR GO; GO:0001510; P:RNA methylation; IEA:UniProt.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR026113; METTL2/6/8-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22809; METHYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR22809:SF4; TRNA N(3)-METHYLCYTIDINE METHYLTRANSFERASE METTL2A; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR PIRSF; PIRSF037755; Mettl2_prd; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037755,
KW ECO:0000313|RefSeq:XP_022375717.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Transferase {ECO:0000256|PIRNR:PIRNR037755};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 186..288
FT /note="Methyltransferase type 12"
FT /evidence="ECO:0000259|Pfam:PF08242"
FT REGION 107..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 328 AA; 37373 MW; D9471379CDAC12D5 CRC64;
MADSYPECAL AAVGEKRQQF GSRFLSDPAR VFHHNAWDNV EWSEEQAAAA ERKVQENSTP
RVCQEKQVDY EVNAHKYWNE FYKIHENGFF KDRHWLFTEF PELAPNPNHN DLNDWLSENK
RSEVPEGRSK EEGPGLKTEE QHTCPSDSLG HKTQMPPLEE DVTRKLSHLE IRADEFPGSS
ATYRILEVGC GVGNTVFPIL QTNNDPGLFV YCCDFSSTAI ELVRTNSAYD PCRCFAFVHD
LCDEDATYPV PGGSLDVIIL IFVLSAVIPD KMQKAISRLS RLLKPGGMML LRDYGRYDMA
QLRFKKGPLG KLIRRRSASH PKQQEGKF
//
