ID S4RFW7_PETMA Unreviewed; 612 AA.
AC S4RFW7;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=type I protein arginine methyltransferase {ECO:0000256|ARBA:ARBA00011925};
DE EC=2.1.1.319 {ECO:0000256|ARBA:ARBA00011925};
OS Petromyzon marinus (Sea lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000004099.1, ECO:0000313|Proteomes:UP000245300};
RN [1] {ECO:0000313|Ensembl:ENSPMAP00000004099.1}
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:ARBA00001817};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; S4RFW7; -.
DR STRING; 7757.ENSPMAP00000004099; -.
DR Ensembl; ENSPMAT00000004116.1; ENSPMAP00000004099.1; ENSPMAG00000003740.1.
DR GeneTree; ENSGT00940000160377; -.
DR HOGENOM; CLU_017375_0_1_1; -.
DR OMA; GDYATPG; -.
DR Proteomes; UP000245300; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0048742; P:regulation of skeletal muscle fiber development; IEA:Ensembl.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.70.160.11; Hnrnp arginine n-methyltransferase1; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR020989; Histone-Arg_MeTrfase_N.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006:SF10; HISTONE-ARGININE METHYLTRANSFERASE CARMER-RELATED; 1.
DR PANTHER; PTHR11006; PROTEIN ARGININE N-METHYLTRANSFERASE; 1.
DR Pfam; PF11531; CARM1; 1.
DR Pfam; PF06325; PrmA; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01015}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000245300};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01015};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU01015}.
FT DOMAIN 4..115
FT /note="Histone-arginine methyltransferase CARM1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11531"
SQ SEQUENCE 612 AA; 66626 MW; 7BC3C271511221C5 CRC64;
MAASFQGVRL TAVGEQNGGG VQRNPEANLR LEAKATGGGG DSLGVTLYNG GGVCVFKCMV
GRDTECCRVS KQAFLITLGQ NSVLVHFASQ PDFNSFMNLL KSCQGRSVER SVFSERTEES
SAVQYFQFYG YLSQQQNMMQ DYIRTGTYQR AILQNHADFR DKIVLDVGCG SGILSFFAVQ
AGARKVYAVE ASSMAQHAEV LVRSNNLQDR IVVIPGKVED VSIPDKVDVI ISEPMGYMLF
NERMLESYLH AKKWLKPNGN MFPTLGDVHL APFTDEQLYM EQFSKANFWY QQSFHGVDLS
SLRGAALEEY FRQPIVDTFD IRILMARSIK YTVNFQQARE EDLHRIEIPF KFQMLQSGLV
HGLAFWFDVA FVGSMLTVWL STAPTEPLTH WYQVRCLLQS PLFTKAGDTL SGTVVMIANK
RQSYDINLVA VVDQTGSKSS NLLDLKNPFF RYSGTTPSPP AGSHYTSPSE GMWGPSAYST
VGSTQLANHT AVPSAFDLSS VLNSVASPTP TNHIPMGLCG HPPVALIIAP TVQADLAIGR
RTNADTGPVN HSFSRLGSIM STGFVPGNAR SGNTGHSAVP GYPMSGQMAT AAAAAAMGGM
LGMTTSPVPL VN
//