ANM5_ORYSJ
ID ANM5_ORYSJ Reviewed; 649 AA.
AC Q6YXZ7; A3A2Z6; B7EM48;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Protein arginine N-methyltransferase 5;
DE EC=2.1.1.320;
DE AltName: Full=Shk1 kinase-binding protein 1 homolog;
GN Name=PRMT5; Synonyms=SKB1; OrderedLocusNames=Os02g0139200, LOC_Os02g04660;
GN ORFNames=OJ1679_B08.2, OsJ_005168, OSJNBa0026E05.36;
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 arginine residues in proteins such as histone H4.
CC {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:48108, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC COMP:11992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:88221; EC=2.1.1.320;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {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; AP005294; BAD10250.1; -; Genomic_DNA.
DR EMBL; AP005647; BAD10543.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF07757.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS76901.1; -; Genomic_DNA.
DR EMBL; CM000139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK073412; BAG93445.1; -; mRNA.
DR EMBL; AK103804; BAG96268.1; -; mRNA.
DR RefSeq; XP_015627032.1; XM_015771546.1.
DR AlphaFoldDB; Q6YXZ7; -.
DR SMR; Q6YXZ7; -.
DR STRING; 4530.OS02T0139200-01; -.
DR PaxDb; Q6YXZ7; -.
DR PRIDE; Q6YXZ7; -.
DR EnsemblPlants; Os02t0139200-01; Os02t0139200-01; Os02g0139200.
DR GeneID; 4328251; -.
DR Gramene; Os02t0139200-01; Os02t0139200-01; Os02g0139200.
DR KEGG; osa:4328251; -.
DR eggNOG; KOG0822; Eukaryota.
DR HOGENOM; CLU_010247_3_0_1; -.
DR InParanoid; Q6YXZ7; -.
DR OMA; IKYAWYE; -.
DR OrthoDB; 475852at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q6YXZ7; OS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0034969; P:histone arginine methylation; IBA:GO_Central.
DR GO; GO:0043985; P:histone H4-R3 methylation; IEA:EnsemblPlants.
DR GO; GO:0035246; P:peptidyl-arginine N-methylation; IEA:InterPro.
DR GO; GO:0010220; P:positive regulation of vernalization response; IEA:EnsemblPlants.
DR GO; GO:0009909; P:regulation of flower development; IEA:EnsemblPlants.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR007857; Arg_MeTrfase_PRMT5.
DR InterPro; IPR035075; PRMT5.
DR InterPro; IPR035248; PRMT5_C.
DR InterPro; IPR035247; PRMT5_TIM.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10738; PTHR10738; 1.
DR Pfam; PF05185; PRMT5; 1.
DR Pfam; PF17286; PRMT5_C; 1.
DR Pfam; PF17285; PRMT5_TIM; 1.
DR PIRSF; PIRSF015894; Skb1_MeTrfase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..649
FT /note="Protein arginine N-methyltransferase 5"
FT /id="PRO_0000293995"
FT DOMAIN 321..627
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 10..300
FT /note="TIM barrel"
FT /evidence="ECO:0000250"
FT REGION 479..649
FT /note="Beta barrel"
FT /evidence="ECO:0000250"
FT REGION 491..507
FT /note="Dimerization"
FT /evidence="ECO:0000250"
FT ACT_SITE 449
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 458
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_note="substrate"
FT /ligand_part="L-arginine residue"
FT /ligand_part_id="ChEBI:CHEBI:29965"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT BINDING 346..347
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 433..434
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 449
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_note="substrate"
FT /ligand_part="L-arginine residue"
FT /ligand_part_id="ChEBI:CHEBI:29965"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT BINDING 458
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_note="substrate"
FT /ligand_part="L-arginine residue"
FT /ligand_part_id="ChEBI:CHEBI:29965"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT SITE 340
FT /note="Critical for specifying symmetric addition of methyl
FT groups"
FT /evidence="ECO:0000250"
SQ SEQUENCE 649 AA; 72673 MW; 8341E95D15624F0E CRC64;
MPLGQRAGDK SESRYCGVEV LDFPAGEELP AVLSHSLSSS FDFLLAPLVD PDYRPTPGSV
LPVAASDLVL GPAQWSSHIV GKISEWIDLD AEDEQLRLDS EITLKQEIAW ASHLSLQACV
LPPPKRSSCA NYARVVNHIL QGLTNLQLWL RIPLEKSEPM DEDHDGAKDN SDMSDTVDSW
EWWNSFRLLC EHSSQLCVAL DVLSTLPSMN SLGRWFGEPV RAAILQTNAF LTNARGYPCL
SKRHQKLLTG FFNHSVQVII SGRSNHNVSQ GGVLSGDENH TEDTAVRHAL SPYLDYIAYI
YQRMDPLPEQ ERFEINYRDF LQSPLQPLMD NLEAQTYETF EKDTVKYTQY QRAIAKALVD
RVSDDDVSTT KTVLMVVGAG RGPLVRASLQ AAEETGRKLK VYAVEKNPNA VITLHSLIKL
EGWESLVTII SSDMRCWEAP EKADILVSEL LGSFGDNELS PECLDGAQRF LKPDGISIPS
SYTSFIEPIT ASKLHNDIKA HKDIAHFETA YVVKLHRIAR LAPTQSVFTF DHPNPSPNAS
NQRYTKLKFE IPQETGSCLV HGFAGYFDAV LYKDVHLGIE PNTATPNMFS WFPIFFPLRK
PIYVPSKTPI EVHFWRCCGA TKVWYEWAVT APSPSPIHNS NGRSYWVGL
