ID I3N4M3_ICTTR Unreviewed; 318 AA.
AC I3N4M3;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=type I protein arginine methyltransferase {ECO:0000256|ARBA:ARBA00011925};
DE EC=2.1.1.319 {ECO:0000256|ARBA:ARBA00011925};
GN Name=PRMT1 {ECO:0000313|Ensembl:ENSSTOP00000019319.2};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000019319.2, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000019319.2}
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:48096, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61897; EC=2.1.1.319;
CC Evidence={ECO:0000256|ARBA:ARBA00036963};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48097;
CC Evidence={ECO:0000256|ARBA:ARBA00036963};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + S-adenosyl-L-methionine = H(+) +
CC N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:48100, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11990,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:65280;
CC Evidence={ECO:0000256|ARBA:ARBA00036919};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48101;
CC Evidence={ECO:0000256|ARBA:ARBA00036919};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-methionine
CC = H(+) + N(omega),N(omega)-dimethyl-L-arginyl-[protein] + S-adenosyl-
CC L-homocysteine; Xref=Rhea:RHEA:48104, Rhea:RHEA-COMP:11990,
CC Rhea:RHEA-COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61897, ChEBI:CHEBI:65280;
CC Evidence={ECO:0000256|ARBA:ARBA00035899};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48105;
CC Evidence={ECO:0000256|ARBA:ARBA00035899};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Nucleus, nucleoplasm
CC {ECO:0000256|ARBA:ARBA00004642}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGTP01089717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3N4M3; -.
DR Ensembl; ENSSTOT00000023436.2; ENSSTOP00000019319.2; ENSSTOG00000025543.2.
DR GeneTree; ENSGT00940000154700; -.
DR HOGENOM; CLU_017375_1_1_1; -.
DR TreeFam; TF300608; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042054; F:histone methyltransferase activity; IEA:UniProt.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 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; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PROTEIN ARGININE N-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11006:SF54; PROTEIN ARGININE N-METHYLTRANSFERASE 1; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01015};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01015};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU01015}.
FT DOMAIN 39..136
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
SQ SEQUENCE 318 AA; 36593 MW; 3A687C597559A6AF CRC64;
MAAAEAANCI MEMLKDEVRT LTYRNSMFHN RHLFKDKVVL DVGSGTGILC MFAAKAGARK
VIGIECSSIS DYAVKIVKAN KLDHVVTIIK GKVEEVELPV EKVDIIISEW MGYCLFYESM
LNTVLYARDK WLAPDGLIFP DRATLYVTAI EDRQYKDYKI HWWENVYGFD MSCIKDVAIK
EPLVDVVDPK QLVTNACLIK EVDIYTVKVE DLTFTSPFCL QVKRNDYVHA LVAYFNIEFT
RCHKRTGFST SPESPYTHWK QTVFYMEDYL TVKTGEEIFG TIGMRPNAKN NRDLDFTIDL
DFKGQLCELS CSTDYRMR
//
