ANM1_ORYSI
ID ANM1_ORYSI Reviewed; 387 AA.
AC A2Z0C0;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Probable protein arginine N-methyltransferase 1;
DE EC=2.1.1.-;
GN Name=PRMT1; ORFNames=OsI_030013;
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 present in a glycine and arginine-rich
CC domain (can methylate histones). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {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; CM000134; EAZ08781.1; -; Genomic_DNA.
DR AlphaFoldDB; A2Z0C0; -.
DR SMR; A2Z0C0; -.
DR STRING; 39946.A2Z0C0; -.
DR iPTMnet; A2Z0C0; -.
DR EnsemblPlants; BGIOSGA029907-TA; BGIOSGA029907-PA; BGIOSGA029907.
DR Gramene; BGIOSGA029907-TA; BGIOSGA029907-PA; BGIOSGA029907.
DR HOGENOM; CLU_017375_1_2_1; -.
DR OMA; RNDFVHA; -.
DR Proteomes; UP000007015; Chromosome 9.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0018216; P:peptidyl-arginine methylation; IEA:InterPro.
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; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..387
FT /note="Probable protein arginine N-methyltransferase 1"
FT /id="PRO_0000293988"
FT DOMAIN 66..387
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /evidence="ECO:0000250"
FT ACT_SITE 187
FT /evidence="ECO:0000250"
SQ SEQUENCE 387 AA; 43014 MW; DB36D4628EF4BA63 CRC64;
MDQRKGSGSD ANGGLAEATA SRLRFEDPDE VMEENPAAAA ATVGAEEEGG EGGGGEEVIG
SDKTSADYYF DSYSHFGIHE EMLKDVVRTK SYQNVITQNS FLFKDKIVLD VGAGTGILSL
FCAKAGAKHV YAIECSQMAD MAKEIVKTNG YSNVITVIKG KVEEIELPVP KVDVIISEWM
GYFLLFENML NTVLYARDKW LADGGVVLPD KASLHLTAIE DAEYKEDKIE FWNNVYGFDM
RCIKKQAMME PLVDTVDANQ IVTNCQLLKT MDISKMTPGD ASFTVPFKLV AERNDYIHAL
VAYFNVSFTK CHKMMGFSTG PRSKATHWKQ TVLYLEDVLT ICEGETITGS MTVTPNKKNP
RDIDIKLCYA LSGHRCQVSR TQHYKMR