ANM5_ORYSI
ID ANM5_ORYSI Reviewed; 649 AA.
AC A2X0Q3;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 61.
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; ORFNames=OsI_005646;
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 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; CM000127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A2X0Q3; -.
DR SMR; A2X0Q3; -.
DR STRING; 39946.A2X0Q3; -.
DR Proteomes; UP000007015; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0035246; P:peptidyl-arginine N-methylation; IEA:InterPro.
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 3: Inferred from homology;
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_0000293994"
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; 72700 MW; FBBFEFA015642816 CRC64;
MPLGQRAGDK SESRYCGVEV LDFPAGEELP AVLSHSLSSS FDFLLAPLVD PDYRPTPGSV
LPVAASDLVL GPAQWSSHIV GKINEWIDLD 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
