METL2_CHICK
ID METL2_CHICK Reviewed; 370 AA.
AC Q5ZHP8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=tRNA N(3)-methylcytidine methyltransferase METTL2 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q8BMK1};
DE AltName: Full=Methyltransferase-like protein 2;
GN Name=METTL2; ORFNames=RCJMB04_34l11 {ECO:0000303|PubMed:15642098};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC mediates N(3)-methylcytidine modification of residue 32 of the tRNA
CC anticodon loop of tRNA(Thr)(UGU) and tRNA(Arg)(CCU). N(3)-
CC methylcytidine methylation by METTL2 requires the N6-
CC threonylcarbamoylation of tRNA (t6A37) by the EKC/KEOPS complex as
CC prerequisite. {ECO:0000250|UniProtKB:Q96IZ6}.
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:0000250|UniProtKB:Q8BMK1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50961;
CC Evidence={ECO:0000250|UniProtKB:Q8BMK1};
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:0000250|UniProtKB:Q8BMK1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60913;
CC Evidence={ECO:0000250|UniProtKB:Q8BMK1};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q96IZ6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96IZ6}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METL family.
CC {ECO:0000305}.
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DR EMBL; AJ721086; CAG32745.1; -; mRNA.
DR RefSeq; NP_001006329.1; NM_001006329.1.
DR AlphaFoldDB; Q5ZHP8; -.
DR SMR; Q5ZHP8; -.
DR STRING; 9031.ENSGALP00000000540; -.
DR PaxDb; Q5ZHP8; -.
DR Ensembl; ENSGALT00000076563; ENSGALP00000055408; ENSGALG00000000396.
DR GeneID; 419948; -.
DR KEGG; gga:419948; -.
DR CTD; 55798; -.
DR VEuPathDB; HostDB:geneid_419948; -.
DR eggNOG; KOG2361; Eukaryota.
DR GeneTree; ENSGT00940000156059; -.
DR HOGENOM; CLU_029724_0_2_1; -.
DR InParanoid; Q5ZHP8; -.
DR OMA; PAKWWNL; -.
DR OrthoDB; 987359at2759; -.
DR PhylomeDB; Q5ZHP8; -.
DR PRO; PR:Q5ZHP8; -.
DR Proteomes; UP000000539; Chromosome 27.
DR Bgee; ENSGALG00000000396; Expressed in testis and 14 other tissues.
DR ExpressionAtlas; Q5ZHP8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016427; F:tRNA (cytosine) methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0052735; F:tRNA (cytosine-3-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR026113; MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22809; PTHR22809; 1.
DR PIRSF; PIRSF037755; Mettl2_prd; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..370
FT /note="tRNA N(3)-methylcytidine methyltransferase METTL2"
FT /id="PRO_0000328848"
FT BINDING 72
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 181
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 206
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 232
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 233
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 253
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
SQ SEQUENCE 370 AA; 42729 MW; 0038DE1C459E2649 CRC64;
MAAPSEAPER RRPFGRRFLT DPTRLFQHNA WDNVEWSEEQ EATAKSKVQE NSSQLLPQDK
QEEYEVNAKR YWDDFYKIHE NGFFKDRHWL FTEFPELAPN RNPSQNEDSL CEFSCKEVSK
NEGLGSCENG HCTLENRAEN QLNLLKSSPR FCTEELAPQK LKQSYEDYPG SSASYRILEV
GCGAGNTVFP ILQTNNDPGL FVYCCDFSTT AVDLVQSNVE YDSSRCFAFV HDLCNDQSPF
PMPDESLDIV ILIFVLSAIL PEKMQCVINK LSRLLKPGGM ILLRDYGRYD LAQLRFKKGQ
CLSANFYVRG DGTRVYFFTQ DELDDLFTRA GLQKIQNLVD RRLQVNRGKQ MTMYRVWIQC
KYQKPAGPQL
