ANM10_ORYSJ
ID ANM10_ORYSJ Reviewed; 380 AA.
AC Q9SNQ2; B7ELX4;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Protein arginine N-methyltransferase PRMT10;
DE EC=2.1.1.319;
GN Name=PRMT10; Synonyms=PRMT4.2;
GN OrderedLocusNames=Os06g0142800, LOC_Os06g05090;
GN ORFNames=OsJ_019280, P0535G04.29;
OS Oryza sativa subsp. japonica (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=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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}.
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DR EMBL; AP000399; BAA83575.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF18686.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS96105.1; -; Genomic_DNA.
DR EMBL; CM000143; EAZ35797.1; -; Genomic_DNA.
DR EMBL; AK073269; BAG93371.1; -; mRNA.
DR EMBL; AK103971; BAG96350.1; -; mRNA.
DR RefSeq; XP_015642494.1; XM_015787008.1.
DR AlphaFoldDB; Q9SNQ2; -.
DR SMR; Q9SNQ2; -.
DR STRING; 4530.OS06T0142800-01; -.
DR PaxDb; Q9SNQ2; -.
DR PRIDE; Q9SNQ2; -.
DR EnsemblPlants; Os06t0142800-01; Os06t0142800-01; Os06g0142800.
DR GeneID; 4340089; -.
DR Gramene; Os06t0142800-01; Os06t0142800-01; Os06g0142800.
DR KEGG; osa:4340089; -.
DR eggNOG; KOG1499; Eukaryota.
DR HOGENOM; CLU_017375_1_2_1; -.
DR InParanoid; Q9SNQ2; -.
DR OMA; MWVAPIR; -.
DR OrthoDB; 840669at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q9SNQ2; OS.
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 2: Evidence at transcript level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..380
FT /note="Protein arginine N-methyltransferase PRMT10"
FT /id="PRO_0000294010"
FT DOMAIN 26..357
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 187..227
FT /note="Dimerization arm"
FT /evidence="ECO:0000250"
FT ACT_SITE 140
FT /evidence="ECO:0000250"
FT ACT_SITE 149
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 380 AA; 42718 MW; B857E3153279CA0F CRC64;
MASLPNGAAS ASASAAGGGP AVVDKEVDFA NYFCTYSYLY HQKEMLCDRV RMDAYHSAVF
RNAHHFRGKV VLDVGTGSGI LAIWSAQAGA RKVYAVEATN MAEHARELAR ANDVADIVEV
IQGSMEDVVL PEKVDVIISE WMGYFLLRES MFDSVICARD RWLKPDGVMY PSHARMWLAP
IRSDLAENKM EDLEIAMHDW NLFVEDTESY YGVNMNVLTK AYRAEHEKYY LKSAIWNNLH
PNQVIGQAAV IKEIDCLTAT VDEIREVRAQ VTMPIKLDMT RLAALAGWFD VHFRGSKQNP
ATQEVELSTA PDVNGGTHWG QQVFLLTPPL KVNEGDNVKV SFTMVRSKEN HRLMDMEFTY
ELHESSGKQL PAITTKIYLE
