ANM1_DICDI
ID ANM1_DICDI Reviewed; 341 AA.
AC Q54EF2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Protein arginine N-methyltransferase 1;
DE EC=2.1.1.319 {ECO:0000250|UniProtKB:Q99873};
DE AltName: Full=Histone-arginine N-methyltransferase PRMT1;
GN Name=prmt1; ORFNames=DDB_G0291556;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Arginine methyltransferase that methylates the guanidino
CC nitrogens of arginyl residues present in proteins such as
CC ribonucleoproteins and histones. {ECO:0000250|UniProtKB:Q99873}.
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 Evidence={ECO:0000250|UniProtKB:Q99873};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytosol
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; AAFI02000177; EAL61762.1; -; Genomic_DNA.
DR RefSeq; XP_635288.1; XM_630196.1.
DR AlphaFoldDB; Q54EF2; -.
DR SMR; Q54EF2; -.
DR STRING; 44689.DDB0235399; -.
DR PaxDb; Q54EF2; -.
DR EnsemblProtists; EAL61762; EAL61762; DDB_G0291556.
DR GeneID; 8628232; -.
DR KEGG; ddi:DDB_G0291556; -.
DR dictyBase; DDB_G0291556; prmt1.
DR eggNOG; KOG1499; Eukaryota.
DR HOGENOM; CLU_017375_1_2_1; -.
DR InParanoid; Q54EF2; -.
DR OMA; RNDFVHA; -.
DR PhylomeDB; Q54EF2; -.
DR Reactome; R-DDI-3214858; RMTs methylate histone arginines.
DR Reactome; R-DDI-8876725; Protein methylation.
DR PRO; PR:Q54EF2; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042054; F:histone methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0008170; F:N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; ISS:dictyBase.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; ISS:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; ISS:dictyBase.
DR GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; ISS:UniProtKB.
DR GO; GO:0018216; P:peptidyl-arginine methylation; IEA:InterPro.
DR GO; GO:0018195; P:peptidyl-arginine modification; ISS:dictyBase.
DR GO; GO:0006479; P:protein methylation; ISS:UniProtKB.
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 PANTHER; PTHR11006; PTHR11006; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..341
FT /note="Protein arginine N-methyltransferase 1"
FT /id="PRO_0000328417"
FT DOMAIN 20..315
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT ACT_SITE 132
FT /evidence="ECO:0000250"
FT ACT_SITE 141
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
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 66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 341 AA; 39121 MW; E920FB50A8479EB4 CRC64;
MTETNKNVDA LEKINQMSSA DYYFDSYSHF GIHEEMLKDE VRTLAYRRAI INNRKLFEGK
VVLDVGCGTG ILCMFAAQAG AKMVIGVDNS EMLPIAQKII TANNFDKTIT LIKGKMEEVV
LPVDKVDIII SEWMGYFMLY EGMLDTVLYA RDKYLVPGGV ILPDKASLYI TAIEDQDYKE
EKINYWNNVY GFDMSCIREI ALKEPLVDVV QPNMIVTNDC CILTVDIMTI TKDELKFRSD
FKLKALRDDL IHAFVVYFDI EFSKGDKPVC FSTGPKAKYT HWKQSIMYFE DHIKIQQGEI
ITGTMDCAPF DKNQRDLKIK LDFNFAGELM KSSSSLEYHM R
