ID A0A2K6FCI4_PROCO Unreviewed; 637 AA.
AC A0A2K6FCI4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Protein arginine N-methyltransferase 5 {ECO:0000256|ARBA:ARBA00018777, ECO:0000256|PIRNR:PIRNR015894};
DE EC=2.1.1.320 {ECO:0000256|ARBA:ARBA00011935, ECO:0000256|PIRNR:PIRNR015894};
GN Name=PRMT5 {ECO:0000313|Ensembl:ENSPCOP00000011702.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000011702.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000011702.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Arginine methyltransferase that can both catalyze the
CC formation of omega-N monomethylarginine (MMA) and symmetrical
CC dimethylarginine (sDMA). {ECO:0000256|PIRNR:PIRNR015894}.
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:0000256|ARBA:ARBA00000778,
CC ECO:0000256|PIRNR:PIRNR015894};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR015894}.
CC Nucleus {ECO:0000256|PIRNR:PIRNR015894}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. {ECO:0000256|PIRNR:PIRNR015894}.
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DR RefSeq; XP_012504777.1; XM_012649323.1.
DR AlphaFoldDB; A0A2K6FCI4; -.
DR STRING; 379532.ENSPCOP00000011702; -.
DR Ensembl; ENSPCOT00000022291.1; ENSPCOP00000011702.1; ENSPCOG00000017358.1.
DR GeneID; 105814387; -.
DR KEGG; pcoq:105814387; -.
DR CTD; 10419; -.
DR GeneTree; ENSGT00390000001141; -.
DR OrthoDB; 5489665at2759; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0035097; C:histone methyltransferase complex; IEA:Ensembl.
DR GO; GO:0034709; C:methylosome; IEA:Ensembl.
DR GO; GO:0044020; F:histone H4R3 methyltransferase activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008327; F:methyl-CpG binding; IEA:Ensembl.
DR GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:Ensembl.
DR GO; GO:0006353; P:DNA-templated transcription termination; IEA:Ensembl.
DR GO; GO:0042118; P:endothelial cell activation; IEA:Ensembl.
DR GO; GO:0090161; P:Golgi ribbon formation; IEA:Ensembl.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:1904992; P:positive regulation of adenylate cyclase-inhibiting dopamine receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IEA:Ensembl.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1.
DR Gene3D; 2.70.160.11; Hnrnp arginine n-methyltransferase1; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; PROTEIN ARGININE N-METHYLTRANSFERASE 5; 1.
DR PANTHER; PTHR10738:SF0; PROTEIN ARGININE N-METHYLTRANSFERASE 5; 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; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 3: Inferred from homology;
KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR015894};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|PIRNR:PIRNR015894}; Nucleus {ECO:0000256|PIRNR:PIRNR015894};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR015894};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR015894}.
FT DOMAIN 37..290
FT /note="PRMT5 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF17285"
FT DOMAIN 297..464
FT /note="PRMT5 arginine-N-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF05185"
FT DOMAIN 467..635
FT /note="PRMT5 oligomerisation"
FT /evidence="ECO:0000259|Pfam:PF17286"
FT ACT_SITE 435
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT ACT_SITE 444
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT BINDING 324
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 333..334
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 392
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 419..420
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT SITE 327
FT /note="Critical for specifying symmetric addition of methyl
FT groups"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-3"
SQ SEQUENCE 637 AA; 72621 MW; 60564C405FB71F16 CRC64;
MAAMAVGGAG GSRVSSGRDL NCVPEIADTL GAVAKQGFDF LCMPVFHPRF KREFTQEPAK
NRPGPQTRSD LLLSGRDWNT LIVGKLSPWI RPDSKVEKIR RNSEAAMLQE LNFGAYLGLP
AFLLPLNQED NTNLARVLTN HIHTGHHSSM FWMRVPLVAP EDLRDDIIDN APTTHTEEYS
GEEKTWMWWH NFRTLCDYSK RIAVALEIGA DLPSNHVIDR WLGEPIKAAI LPTSIFLTNK
KGFPVLSKMH QRLIFRLLKL EVQFIITGTN HHSEKEFCSY LQYLEYLSQN RPPPNAYELF
AKGYEDYLQS PLQPLMDNLE SQTYEVFEKD PIKYSQYQQA IYKCLLDRVS EEEKDTSVQV
LMVLGAGRGP LVNASLRAAK QADRRIKLYA VEKNPNAVVT LENWQFEEWG SQVTVVSSDM
REWVAPEKAD IIVSELLGSF ADNELSPECL DGAQHFLKDD GVSIPGEYTS FLAPISSSKL
YNEVRACREK DRDPEAQFEM PYVVRLHNFH QLSAPQPCFT FSHPNRDPMI DNNRYCTLEF
PVEVNTVLHG FAGYFETVLY QDITLSIRPE THSPGMFSWF PILFPIKQPI TVREGQTICV
RFWRCSNSKK VWYEWAVTAP VCSAIHNPTG RSYTIGL
//
