ID A0A2R9ALG8_PANPA Unreviewed; 466 AA.
AC A0A2R9ALG8;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Protein arginine N-methyltransferase 5 {ECO:0000256|ARBA:ARBA00018777};
DE EC=2.1.1.320 {ECO:0000256|ARBA:ARBA00011935};
DE AltName: Full=Histone-arginine N-methyltransferase PRMT5 {ECO:0000256|ARBA:ARBA00031210};
DE AltName: Full=Shk1 kinase-binding protein 1 homolog {ECO:0000256|ARBA:ARBA00031000};
GN Name=PRMT5 {ECO:0000313|Ensembl:ENSPPAP00000017993.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000017993.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000017993.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000017993.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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};
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DR EMBL; AJFE02024238; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2R9ALG8; -.
DR SMR; A0A2R9ALG8; -.
DR Ensembl; ENSPPAT00000040715.1; ENSPPAP00000017993.1; ENSPPAG00000032055.1.
DR GeneTree; ENSGT00390000001141; -.
DR Proteomes; UP000240080; Chromosome 14.
DR Bgee; ENSPPAG00000032055; Expressed in testis and 6 other cell types or tissues.
DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 2.
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; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 4: Predicted;
KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01015}; Reference proteome {ECO:0000313|Proteomes:UP000240080};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR015894-2};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01015}.
FT DOMAIN 20..87
FT /note="PRMT5 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF17285"
FT DOMAIN 126..293
FT /note="PRMT5 arginine-N-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF05185"
FT DOMAIN 296..464
FT /note="PRMT5 oligomerisation"
FT /evidence="ECO:0000259|Pfam:PF17286"
FT ACT_SITE 264
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT ACT_SITE 273
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT BINDING 153
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 162..163
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 221
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 248..249
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT SITE 156
FT /note="Critical for specifying symmetric addition of methyl
FT groups"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-3"
SQ SEQUENCE 466 AA; 53580 MW; 62386C5B867CF619 CRC64;
MRGPNSGTEK GRLVIPEKQG FDFLCMPVFH PRFKREFIQE PAKNRPGPQT RSDLLLSGRD
WNTLIVGKLS PWIRPDSKVE KIRRNSEALE VQFIITGTNH HSEKEFCSYL QYLEYLSQNR
PPPNAYELFA KGYEDYLQSP LQPLMDNLES QTYEVFEKDP IKYSQYQQAI YKCLLDRVPE
EEKDTNVQVL MVLGAGRGPL VNASLRAAKQ ADRRIKLYAV EKNPNAVVTL ENWQFEEWGS
QVTVVSSDMR EWVAPEKADI IVSELLGSFA DNELSPECLD GAQHFLKDDG VSIPGEYTSF
LAPISSSKLY NEVRACREKD RDPEAQFEMP YVVRLHNFHQ LSAPQPCFTF SHPNRDPMID
NNRYCTLEFP VEVNTVLHGF AGYFETVLYQ DITLSIRPET HSPGMFSWFP ILFPIKQPIT
VREGQTICVR FWRCSNSKKV WYEWAVTAPV CSAIHNPTGR SYTIGL
//
