ID   ANM10_ORYSI             Reviewed;         382 AA.
AC   A2Y953;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Protein arginine N-methyltransferase PRMT10;
DE            EC=2.1.1.319;
GN   Name=PRMT10; Synonyms=PRMT4.2; ORFNames=OsI_020846;
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
CC   -!- FUNCTION: Methylates (mono and asymmetric dimethylation) the guanidino
CC       nitrogens of arginyl residues in some proteins. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) +
CC         N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:48096, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC         COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61897; EC=2.1.1.319;
CC   -!- SUBUNIT: Ring-like homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Protein arginine N-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01015}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM000131; EAY99613.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2Y953; -.
DR   SMR; A2Y953; -.
DR   STRING; 39946.A2Y953; -.
DR   PRIDE; A2Y953; -.
DR   EnsemblPlants; BGIOSGA022276-TA; BGIOSGA022276-PA; BGIOSGA022276.
DR   Gramene; BGIOSGA022276-TA; BGIOSGA022276-PA; BGIOSGA022276.
DR   HOGENOM; CLU_017375_1_2_1; -.
DR   OMA; MWVAPIR; -.
DR   Proteomes; UP000007015; Chromosome 6.
DR   GO; GO:0016277; F:[myelin basic protein]-arginine N-methyltransferase activity; IEA:EnsemblPlants.
DR   GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IEA:EnsemblPlants.
DR   GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IEA:EnsemblPlants.
DR   GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; IEA:EnsemblPlants.
DR   GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IEA:EnsemblPlants.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR025799; Arg_MeTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR11006; PTHR11006; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51678; SAM_MT_PRMT; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..382
FT                   /note="Protein arginine N-methyltransferase PRMT10"
FT                   /id="PRO_0000294009"
FT   DOMAIN          28..359
FT                   /note="SAM-dependent MTase PRMT-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..229
FT                   /note="Dimerization arm"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        142
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        151
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   382 AA;  42876 MW;  702A77F97C67AD15 CRC64;
     MASLPNGAAS ASAASSAAGG GPAVVDKEVD FANYFCTYSY LYHQKEMLCD RVRMDAYHSA
     VFRNAHHFRG KVVLDVGTGS GILAIWSAQA GARKVYAVEA TNMAEHAREL ARANDVADIV
     EVIQGSMEDV VLPEKVDVII SEWMGYFLLR ESMFDSVICA RDRWLKPDGV MYPSHARMWL
     APIRSDLAEN KMEDLEIAMH DWNLFVEDTE SYYGVNMNVL TKAYRAEHEK YYLKSAIWNN
     LHPNQVIGQA AVIKEIDCLT ATVDEIREVR AQVTMPIKLD MTRLAALAGW FDVHFRGSKQ
     NPATQEVELS TAPDVNGGTH WGQQVFLLTP PLKVNEGDNV KVSFTMVRSK ENHRLMDMEF
     TYELHESSGK QLPAITTKIY LE