ID   ANM2_DICDI              Reviewed;         512 AA.
AC   Q54HI0;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Protein arginine N-methyltransferase 2;
DE            EC=2.1.1.319 {ECO:0000250|UniProtKB:P55345};
DE   AltName: Full=Histone-arginine N-methyltransferase PRMT2;
GN   Name=prmt2; ORFNames=DDB_G0289445;
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 in some proteins such as histones.
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: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:P55345};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. 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; AAFI02000141; EAL62721.1; -; Genomic_DNA.
DR   RefSeq; XP_636224.1; XM_631132.1.
DR   AlphaFoldDB; Q54HI0; -.
DR   SMR; Q54HI0; -.
DR   STRING; 44689.DDB0235402; -.
DR   PaxDb; Q54HI0; -.
DR   PRIDE; Q54HI0; -.
DR   EnsemblProtists; EAL62721; EAL62721; DDB_G0289445.
DR   GeneID; 8627143; -.
DR   KEGG; ddi:DDB_G0289445; -.
DR   dictyBase; DDB_G0289445; prmt2.
DR   eggNOG; KOG1499; Eukaryota.
DR   HOGENOM; CLU_017375_1_2_1; -.
DR   InParanoid; Q54HI0; -.
DR   OMA; SEWMGAF; -.
DR   PhylomeDB; Q54HI0; -.
DR   PRO; PR:Q54HI0; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0042054; F:histone methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0008469; F:histone-arginine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0030331; F:nuclear estrogen receptor binding; ISS:UniProtKB.
DR   GO; GO:0016274; F:protein-arginine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR   GO; GO:0016571; P:histone methylation; ISS:UniProtKB.
DR   GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0018216; P:peptidyl-arginine methylation; IEA:InterPro.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0060765; P:regulation of androgen receptor signaling pathway; ISS:UniProtKB.
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   Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..512
FT                   /note="Protein arginine N-methyltransferase 2"
FT                   /id="PRO_0000330894"
FT   DOMAIN          120..508
FT                   /note="SAM-dependent MTase PRMT-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT   REGION          67..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        231
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        240
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   512 AA;  58871 MW;  CD083960519827C5 CRC64;
     MTDDYSKLKS EIMDLVSEEF LKTKDDIISV MIENNKLKRA ELVVGNDSLP PPPPTPSIVK
     IEHTTTTSNI DDLPLPPPIQ EVEEEEPTQQ NIEQQQQTQD ESDDYYKTVH PLGVQDTYED
     EEYFSSYSKI SLHHEMVFDK RRTAAYYHAI SKSKNIFKDK VVLDVGCGTG ILSCFVAKAG
     AKKVYAVDAS DMAHRAELIV QQNGLADIVT VFKGKLEHIA FPEYVDVIVS EWQGAFLIFE
     SMIESVIYAR DNLMRPGGII LPSKASIYLS PINVDSFYNQ YINQWSNVFN LDMSPLIPFA
     QEELLEEKTI RNYYVDNQDS VLDKPIILRT IDLSTITIED LSKTVKTFEF QVPNGSKYHG
     FGSWFSVWFE NLDDDDDDND NNNNNNDNSN DDENKQQFAY YTIDRDGELV KSTYQQYSID
     SKGLTPLFFK QSSNVLELST APGTGDQHWK QVLFLNSKEK ILQSSDKQLD TTSIKGTIRI
     LQNKDYRRHW WIEMYVSLKT NPFDYSYQKY LI