ID A0A093UYV7_TALMA Unreviewed; 422 AA.
AC A0A093UYV7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=tRNA N(3)-methylcytidine methyltransferase {ECO:0000256|PIRNR:PIRNR037755};
DE EC=2.1.1.- {ECO:0000256|PIRNR:PIRNR037755};
GN ORFNames=GQ26_0251720 {ECO:0000313|EMBL:KFX45105.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX45105.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase.
CC {ECO:0000256|PIRNR:PIRNR037755}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METL family.
CC {ECO:0000256|ARBA:ARBA00009725, ECO:0000256|PIRNR:PIRNR037755}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFX45105.1}.
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DR EMBL; JPOX01000025; KFX45105.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093UYV7; -.
DR eggNOG; KOG2361; Eukaryota.
DR HOGENOM; CLU_029724_1_1_1; -.
DR Proteomes; UP000029285; Unassembled WGS sequence.
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 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:SF11; METHYLTRANSFERASE-LIKE PROTEIN; 1.
DR PANTHER; PTHR22809; METHYLTRANSFERASE-RELATED; 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 Methyltransferase {ECO:0000256|PIRNR:PIRNR037755,
KW ECO:0000313|EMBL:KFX45105.1};
KW Transferase {ECO:0000256|PIRNR:PIRNR037755, ECO:0000313|EMBL:KFX45105.1}.
FT DOMAIN 139..251
FT /note="Methyltransferase type 12"
FT /evidence="ECO:0000259|Pfam:PF08242"
FT REGION 306..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 422 AA; 48610 MW; CF0652F2A135E58A CRC64;
MPALPPDGDY ITISQLVEPP TVPSWRSHDP ARSAKRTDPF AFGQRYLEEG DDVFSYNAWD
HVETDEDYKA YAELQYAKQR ENPASDWHKS LYNSNPAKFW DRFYKNHNQN FFKDRKWLRQ
EFPVLAEVTK QGAGPKVVLE VGAGAGNTAF PLINNNENEE LKVFACDYSK NAVKVMRESE
HYNEKFMRAE VWDVTSEEEE IDGEIKSSMP PGVEEGSVDV VILIFIMSAL APDQWNAALR
NIHRVLKPGG LVLFRDYGRG DLAQVRFKKE RYLSENFYVR GDGTRVYFFD EEELRQMWST
WTPEKGLPMV NNDISTENTD SPELAENKEE QQTETSTEKT TEESIDKNQE EQEQTEDTEG
AFEVLNLGKD QRLLVNRQRK LKMYRCWIQA RFRKRVPGET SADQQPAPTA ESIAEGLAAT
TL
//
