ID V8NJF8_OPHHA Unreviewed; 323 AA.
AC V8NJF8;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=type I protein arginine methyltransferase {ECO:0000256|ARBA:ARBA00011925};
DE EC=2.1.1.319 {ECO:0000256|ARBA:ARBA00011925};
DE Flags: Fragment;
GN Name=prmt1 {ECO:0000313|EMBL:ETE61672.1};
GN ORFNames=L345_12575 {ECO:0000313|EMBL:ETE61672.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE61672.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE61672.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE61672.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
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 -!- 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:ETE61672.1}.
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DR EMBL; AZIM01003726; ETE61672.1; -; Genomic_DNA.
DR AlphaFoldDB; V8NJF8; -.
DR Proteomes; UP000018936; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
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 ECO:0000313|EMBL:ETE61672.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01015};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU01015,
KW ECO:0000313|EMBL:ETE61672.1}.
FT DOMAIN 71..165
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE61672.1"
FT NON_TER 323
FT /evidence="ECO:0000313|EMBL:ETE61672.1"
SQ SEQUENCE 323 AA; 37414 MW; 869CE0F99FF79AF0 CRC64;
MTWAFLYFHQ VSCTQPESSK PTAEEMTSKD YYFDSYAHFG IHEEMLKDEV RTLTYRNSMF
HNRHLFKDKV VLDVGSGTGI LCMFAAKAGA KRVIGIECSS ISDYAVKIVK ANKLDHVVSI
IKGKVEEVEL PVEKVDIIIS EWMGYCLFYE SMLNTVIYAR DKWLIPDGLI FPDRATLYIT
AIEDRQYKDY KIHWWENVYG FDMSCIKDVA IKEPLVDVVD PKQLVTNACL IKEVDIYTVK
VEDLTFTSPF CLQVKRNDYI HALVAYFNIE FTRCHKRTGF STSPESPYTH WKQTVFYMED
YLTVKTGEEI FGTIGMKPNA KNN
//
