ANM5_DICDI
ID ANM5_DICDI Reviewed; 642 AA.
AC Q54KI3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Protein arginine N-methyltransferase 5;
DE EC=2.1.1.320 {ECO:0000250|UniProtKB:O14744};
GN Name=prmt5; ORFNames=DDB_G0287327;
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: Methylates arginine residues in proteins such as small
CC nuclear ribonucleoproteins or histone H2A/H4. {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 Evidence={ECO:0000250|UniProtKB:O14744};
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; AAFI02000100; EAL63731.1; -; Genomic_DNA.
DR RefSeq; XP_637240.1; XM_632148.1.
DR AlphaFoldDB; Q54KI3; -.
DR SMR; Q54KI3; -.
DR STRING; 44689.DDB0235403; -.
DR PaxDb; Q54KI3; -.
DR EnsemblProtists; EAL63731; EAL63731; DDB_G0287327.
DR GeneID; 8626071; -.
DR KEGG; ddi:DDB_G0287327; -.
DR dictyBase; DDB_G0287327; prmt5.
DR eggNOG; KOG0822; Eukaryota.
DR HOGENOM; CLU_010247_3_0_1; -.
DR InParanoid; Q54KI3; -.
DR OMA; IKYAWYE; -.
DR PhylomeDB; Q54KI3; -.
DR Reactome; R-DDI-3214858; RMTs methylate histone arginines.
DR PRO; PR:Q54KI3; -.
DR Proteomes; UP000002195; Chromosome 5.
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:0016274; F:protein-arginine N-methyltransferase activity; ISS:dictyBase.
DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0034969; P:histone arginine methylation; IBA:GO_Central.
DR GO; GO:0035246; P:peptidyl-arginine N-methylation; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0030587; P:sorocarp development; HMP:dictyBase.
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 Chromatin regulator; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..642
FT /note="Protein arginine N-methyltransferase 5"
FT /id="PRO_0000330892"
FT DOMAIN 307..620
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 1..286
FT /note="TIM barrel"
FT /evidence="ECO:0000250"
FT REGION 465..642
FT /note="Beta barrel"
FT /evidence="ECO:0000250"
FT REGION 477..493
FT /note="Dimerization"
FT /evidence="ECO:0000250"
FT ACT_SITE 434
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 443
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 326
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 332..333
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 418..419
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 434
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 443
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 326
FT /note="Critical for specifying symmetric addition of methyl
FT groups"
FT /evidence="ECO:0000250"
SQ SEQUENCE 642 AA; 73499 MW; C616E64BF172BF10 CRC64;
MINSAQYEFS CGVELESVDI QLDIERAYDL EYQFIMTSIS HPRFNRDFTK ASIGNSFSNK
VAFTRSDTLL QSNYWRSSIV GKTSTNGIDL DSIDPTIRSN SVKTLKQEIS WAAHLSLPSI
LLPTPSFNST NYAQVVNQSL QSLSYMKVWI RIPLVSPKSQ LLNKFDYYQD HNTSGGSGNN
LVDNDNPWEW WNNFRLLCNQ HPNLSAVLEM TSDLPSKEQL QQWLGEPVKC VIIPTSVFLT
NKAGFPTLSK AHQQFLLQLF NYNIQFVVSG ASMDTLKDYK TYLKFLHTNQ NPLTQEEYFE
MPYLDFLQAP LQPLMDNLES QTYEVFEKDP IKYKQYQNAV RLALLDLDKK DSKDDPIIIM
VVGAGRGPLV NSSIQASIEA NKFVKVFAVE KNPNAIVTLR NRIIMEGWEE IVTVIDSDMR
DWNTEYRADI MVSELLGSFG DNELSPECLD GAQRYLKKDT GISIPTWYTS YIAPISSSKL
FNEVTAYGDL KHSETPYVVK PHNFHQLAES KPLFTFSHPN RDEIIDNSRY ESLEFELTIP
STTCHGFIGY FDCCLYKDVH ISINPSNFST GMFSWFPIYF PLKQPVYFSN GNLNNNNNNN
IKAKCAFWRN VSKSKVWYEW CLLSPTITPI QNVGGRSYYI GL
