ID H3BD96_LATCH Unreviewed; 320 AA.
AC H3BD96;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Protein arginine methyltransferase 1 {ECO:0000313|Ensembl:ENSLACP00000019867.1};
GN Name=PRMT1 {ECO:0000313|Ensembl:ENSLACP00000019867.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000019867.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000019867.1}
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: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: Nucleus, nucleoplasm
CC {ECO:0000256|ARBA:ARBA00004642}.
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DR EMBL; AFYH01030527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01030528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01030529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01030530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3BD96; -.
DR STRING; 7897.ENSLACP00000019867; -.
DR Ensembl; ENSLACT00000020005.1; ENSLACP00000019867.1; ENSLACG00000017467.1.
DR eggNOG; KOG1499; Eukaryota.
DR GeneTree; ENSGT00940000154700; -.
DR HOGENOM; CLU_017375_1_1_1; -.
DR InParanoid; H3BD96; -.
DR OMA; DTGMMFP; -.
DR TreeFam; TF300608; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000017467; Expressed in muscle tissue and 6 other cell types or tissues.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044020; F:histone H4R3 methyltransferase activity; IEA:Ensembl.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; IEA:Ensembl.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; IPR013216; Methyltransf_11.
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; PF08241; Methyltransf_11; 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 Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01015};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU01015}.
FT DOMAIN 65..164
FT /note="Methyltransferase type 11"
FT /evidence="ECO:0000259|Pfam:PF08241"
SQ SEQUENCE 320 AA; 36734 MW; 915AC6D3DC687A63 CRC64;
KVTCVQTGEG SIKPPAEEMT SKDYYFDSYA HFGIHEEMLK DEVRTMTYRN SMFHNRHLFK
DKVVLDVGSG TGILCMFAAK AGAKKVIGVC MWGCLEMSAF LNTALFDPCA VVTIVKGKVE
DVELPVEKVD IIISEWMGYC LFYESMLNTV IYARDKWLNP DGLIFPDRAT LYITAIEDRQ
YKDYKIHWWE NVYGFDMSCI KEVAIKEPLV DVVDPKQLVT NACLIKEVDI YTVKVEDLSF
TSPFCLQVKR NDYIHALVAY FNIEFTRCHK RTGFSTGPES PYTHWKQTVF YMEDYLTVKT
GEEIFGTISM KPNAKNNVSL
//
