ID A0A3B3QIC6_9TELE Unreviewed; 450 AA.
AC A0A3B3QIC6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=type I protein arginine methyltransferase {ECO:0000256|ARBA:ARBA00011925};
DE EC=2.1.1.319 {ECO:0000256|ARBA:ARBA00011925};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000005574.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000005574.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3B3QIC6; -.
DR Ensembl; ENSPKIT00000029581.1; ENSPKIP00000005574.1; ENSPKIG00000022185.1.
DR GeneTree; ENSGT00940000164013; -.
DR Proteomes; UP000261540; 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: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; 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:SF49; HISTONE-ARGININE METHYLTRANSFERASE CARM1; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01015};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01015};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU01015}.
FT DOMAIN 19..118
FT /note="Histone-arginine methyltransferase CARM1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11531"
SQ SEQUENCE 450 AA; 50738 MW; 486D1B6710B97A08 CRC64;
MDTSNTQDSF AVSLHIFSED QAKGGIQLCK SSQHQDLTLQ VGGVEGEQEL TLKNGDGVCV
FKFSMGRETE CCRAGNQSFL VTLGCVSVLL HFRTGTEFHT FHKMVRRDSR LGKEPSAFDQ
RTDDSSARQY FQQNMLQDYL RTATYQKAIL LNEVDFKDKV VLDVGCGSGI LSFFAIQAGA
KKVYAVEASS VARYAEILVK SNNLSDRITV LAGKIEEVSC PEQVDVIVSE PIGYMLLNER
MLESYLYSKK WLKSKGMMFP TFSDLHLAPF SDEQLYIEHY TRSSFWHQTS FFGIDLSGLH
SAAVDEFFKQ PVVDTFDKQI LMAKSVKFSI NFLDAKEEDL HRIEIPFVFQ LHQSGLIHGL
AVWFDVAFVG SRTTVWLSTS PSEPLTHWYQ VRCLLQTPLF AKMGQTLSGT VLLVANKRQS
YDIHLSAVVD QSGFKSGNIL DLKNPFFRYA
//
