ID   ANM3_ORYSI              Reviewed;         620 AA.
AC   A2YP56;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Probable protein arginine N-methyltransferase 3;
DE            EC=2.1.1.-;
GN   Name=PRMT3; ORFNames=OsI_026099;
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: The zinc-finger is responsible for substrate specificity.
CC       {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}.
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DR   EMBL; CM000132; EAZ04867.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2YP56; -.
DR   SMR; A2YP56; -.
DR   STRING; 39946.A2YP56; -.
DR   EnsemblPlants; BGIOSGA026235-TA; BGIOSGA026235-PA; BGIOSGA026235.
DR   Gramene; BGIOSGA026235-TA; BGIOSGA026235-PA; BGIOSGA026235.
DR   HOGENOM; CLU_017375_6_1_1; -.
DR   OMA; ETHWQQG; -.
DR   Proteomes; UP000007015; Chromosome 7.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:EnsemblPlants.
DR   GO; GO:0018216; P:peptidyl-arginine methylation; IEA:InterPro.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR025799; Arg_MeTrfase.
DR   InterPro; IPR041698; Methyltransf_25.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR041661; ZN622/Rei1/Reh1_Znf-C2H2.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR11006; PTHR11006; 1.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   Pfam; PF12756; zf-C2H2_2; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS51678; SAM_MT_PRMT; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Metal-binding; Methyltransferase; Reference proteome; Repeat;
KW   S-adenosyl-L-methionine; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..620
FT                   /note="Probable protein arginine N-methyltransferase 3"
FT                   /id="PRO_0000293991"
FT   DOMAIN          253..582
FT                   /note="SAM-dependent MTase PRMT-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT   ZN_FING         55..78
FT                   /note="C2H2-type 1"
FT   ZN_FING         110..137
FT                   /note="C2H2-type 2; degenerate"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..45
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        383
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        392
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   620 AA;  68144 MW;  481B85CBD9BDCC53 CRC64;
     MATREHELRP EQERLGEDRE EYEDGEEEEE EEEEEEGWDD WESDGDDAGG GGGGLLCLFC
     SARFDSESSL FSHCASEHRF DFYRVVKETG MDFYGCIKLI NFVRSKVAEN KCWSCGQVFS
     SNSELCGHLH ALEIPQLEGK VPWGDDVYLK PFLEDDSLLH SLSVFDDDDE DDCGMPMEKG
     GCSAGNGSLA ETCESNLKSI INDGSDVIDR FERTCTIEST DGECSGSLAQ EPSDKQLKIA
     RASAAARGIN SVDESYFGSY SSFGIHREML GDKVRTEAYR DALLGNPSLM NGATVLDVGC
     GTGILSLFAA KAGASRVIAV DGSAKMVSVA TEVTKSNGFL YDENMEMQQK RDTQVITVVH
     TKAEELNHKI QVPSNKFDVL VSEWMGYCLL YESMLSSVLY ARDHFLKPGG AILPDTATIF
     GAGFGKGGTS LPFWENVYGF DMSCIGKEVT GNSARFPVVD ILASEDIVTE TAVLNSFDLA
     TMKENEMDFT SSFELRLSES GVSPSGVTWC YGIILWFDTG FTNRFCKEKP VNLSTSPFST
     PTHWSQTIFT FEEPIAMAKE ESAVVSSASV GTDECPAVMI RSRISIVRAS EHRSIDISIE
     TTGISSDGRK RSWPVQIFNL