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Database: UniProt
Entry: H2NKR0_PONAB
LinkDB: H2NKR0_PONAB
Original site: H2NKR0_PONAB 
ID   H2NKR0_PONAB            Unreviewed;       620 AA.
AC   H2NKR0; A0A2J8TRY8; A0A2J8TRZ2;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   24-JAN-2024, entry version 64.
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:ENSPPYP00000006422.2};
GN   ORFNames=CR201_G0032719 {ECO:0000313|EMBL:PNJ35794.1};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000006422.2, ECO:0000313|Proteomes:UP000001595};
RN   [1] {ECO:0000313|Ensembl:ENSPPYP00000006422.2, ECO:0000313|Proteomes:UP000001595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilson R.K., Mardis E.;
RT   "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PNJ35794.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Susie {ECO:0000313|EMBL:PNJ35794.1};
RA   Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA   Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA   Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA   Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA   Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT   "High-resolution comparative analysis of great ape genomes.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPPYP00000006422.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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   EMBL; NDHI03003485; PNJ35794.1; -; Genomic_DNA.
DR   Ensembl; ENSPPYT00000006677.2; ENSPPYP00000006422.2; ENSPPYG00000005650.3.
DR   GeneTree; ENSGT00390000001141; -.
DR   HOGENOM; CLU_010247_3_0_1; -.
DR   TreeFam; TF300626; -.
DR   Proteomes; UP000001595; Chromosome 14.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   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:UP000001595};
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          20..273
FT                   /note="PRMT5 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF17285"
FT   DOMAIN          280..447
FT                   /note="PRMT5 arginine-N-methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF05185"
FT   DOMAIN          450..618
FT                   /note="PRMT5 oligomerisation"
FT                   /evidence="ECO:0000259|Pfam:PF17286"
FT   ACT_SITE        418
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT   ACT_SITE        427
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT   BINDING         307
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   BINDING         316..317
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   BINDING         375
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   BINDING         402..403
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   SITE            310
FT                   /note="Critical for specifying symmetric addition of methyl
FT                   groups"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-3"
SQ   SEQUENCE   620 AA;  71319 MW;  07111D2B3A671037 CRC64;
     MRGPNSGTEK GRLVIPEKQG FDFLCMPVFH PRFKREFIQE PAKNRPGPQT RSDLLLSGRD
     WNTLIVGKLS PWIRPDSKVE KIRRNSEAAM LQELNFGAYL GLPAFLLPLN QEDNTNLARV
     LTNHIHTGHH SSMFWMRVPL VAPEDLRDDI IENAPTTHTQ EYSGEEKTWM WWHNFRTLCD
     YSKRIAVALE IGADLPSNHV IDRWLGEPIK AAILPTSIFL TNKKGFPVLS KMHQRLIFRL
     LKLEVQFIIT GTNHHSEKEF CSYLQYLEYL SQNRPPPNAY ELFAKGYEDY LQSPLQPLMD
     NLESQTYEVF EKDPIKYSQY QQAIYKCLLD RVPEEEKDTN VQVLMVLGAG RGPLVNASLR
     AAKQADRRIK LYAVEKNPNA VVTLENWQFE EWGSQVTVVS SDMREWVAPE KADIIVSELL
     GSFADNELSP ECLDGAQHFL KDDGVSIPGE YTSFLAPISS SKLYNEVRAC REKDRDPEAQ
     FEMPYVVRLH NFHQLSAPQP CFTFSHPNRD PMIDNNRYCT LEFPVEVNTV LHGFAGYFET
     VLYQDITLSI RPETHSPGMF SWFPILFPIK QPITVREGQT ICVRFWRCSN SKKVWYEWAV
     TAPVCSAIHN PTGRSYTIGL
//
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