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Database: UniProt
Entry: A0A1A6H477_NEOLE
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ID   A0A1A6H477_NEOLE        Unreviewed;       583 AA.
AC   A0A1A6H477;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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   ORFNames=A6R68_12326 {ECO:0000313|EMBL:OBS73124.1};
OS   Neotoma lepida (Desert woodrat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Neotominae; Neotoma.
OX   NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS73124.1, ECO:0000313|Proteomes:UP000092124};
RN   [1] {ECO:0000313|EMBL:OBS73124.1, ECO:0000313|Proteomes:UP000092124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=417 {ECO:0000313|EMBL:OBS73124.1};
RC   TISSUE=Liver {ECO:0000313|EMBL:OBS73124.1};
RA   Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT   "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT   lepida.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OBS73124.1}.
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DR   EMBL; LZPO01054712; OBS73124.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A6H477; -.
DR   STRING; 56216.A0A1A6H477; -.
DR   Proteomes; UP000092124; Unassembled WGS sequence.
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   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   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:UP000092124};
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..260
FT                   /note="PRMT5 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF17285"
FT   DOMAIN          252..410
FT                   /note="PRMT5 arginine-N-methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF05185"
FT   DOMAIN          413..581
FT                   /note="PRMT5 oligomerisation"
FT                   /evidence="ECO:0000259|Pfam:PF17286"
FT   ACT_SITE        381
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT   ACT_SITE        390
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT   BINDING         270
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   BINDING         279..280
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   BINDING         338
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   BINDING         365..366
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   SITE            273
FT                   /note="Critical for specifying symmetric addition of methyl
FT                   groups"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-3"
SQ   SEQUENCE   583 AA;  66334 MW;  663007ACA775FC0C CRC64;
     MAAMAVGGAG GSRVSSGRDL NCVPEIADTL GAVAKQGFDF LCMPVFHPRF KREFTQEPAK
     NRPGPQTRSD LLLSGRDWNT LIVGKLSPWI HPDSKVEKIR RNSEAAMLQE LNFGAYLGLP
     AFLLPLNQED NTNLARVLTN HIHTGHHSSM FWMRVPLVAP EDLRDDVIEN VPTTHTEEYS
     GEEKTWMWWH NFRTLCDYSK RIAVALEIGA DLPSNHVIDR WLGEPIKAAI LPTSIFLTNK
     KGFPVLSKMQ QRLIFRLLKP LMDNLESQTY EVFEKDPIKY SQYQQAIYKC LLDRVPEEEK
     ETNVQVLMVL GAGRGPLVNA SLRAAKQADR RIRLYAVEKN PNAVVTLENW QFEEWGSQVT
     VVSSDMREWV APEKADIIVS ELLGSFADNE LSPECLDGAQ HFLKDDGVSI PGEYTSFLAP
     ISSSKLYNEV RACREKDRDP EAQFEMPYVV RLHNFHQLSA PQPCFTFSHP NRDPMIDNNR
     YCTLEFPVEV NTVLHGFAGY FETVLYRDIT LSIRPETHSP GMFSWFPILF PIKQPITVRE
     GQSICVRFWR CSNSKKVWYE WAVTAPVCSS IHNPTGRSYT IGL
//
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