ID A0A087VHY0_BALRE Unreviewed; 689 AA.
AC A0A087VHY0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Protein arginine N-methyltransferase 7 {ECO:0000256|ARBA:ARBA00018773};
DE EC=2.1.1.321 {ECO:0000256|ARBA:ARBA00011954};
DE AltName: Full=Histone-arginine N-methyltransferase PRMT7 {ECO:0000256|ARBA:ARBA00031211};
DE AltName: Full=[Myelin basic protein]-arginine N-methyltransferase PRMT7 {ECO:0000256|ARBA:ARBA00033232};
DE Flags: Fragment;
GN ORFNames=N312_06029 {ECO:0000313|EMBL:KFO12222.1};
OS Balearica regulorum gibbericeps (East African grey crowned-crane).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Gruidae; Balearica.
OX NCBI_TaxID=100784 {ECO:0000313|EMBL:KFO12222.1, ECO:0000313|Proteomes:UP000053309};
RN [1] {ECO:0000313|EMBL:KFO12222.1, ECO:0000313|Proteomes:UP000053309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N312 {ECO:0000313|EMBL:KFO12222.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Arginine methyltransferase that can both catalyze the
CC formation of omega-N monomethylarginine (MMA) and symmetrical
CC dimethylarginine (sDMA), with a preference for the formation of MMA.
CC Specifically mediates the symmetrical dimethylation of arginine
CC residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm
CC D3 (SNRPD3); such methylation being required for the assembly and
CC biogenesis of snRNP core particles. Specifically mediates the symmetric
CC dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in
CC gene imprinting by being recruited by CTCFL at the H19 imprinted
CC control region (ICR) and methylating histone H4 to form H4R3me2s,
CC possibly leading to recruit DNA methyltransferases at these sites. May
CC also play a role in embryonic stem cell (ESC) pluripotency. Also able
CC to mediate the arginine methylation of histone H2A and myelin basic
CC protein (MBP) in vitro; the relevance of such results is however
CC unclear in vivo. {ECO:0000256|ARBA:ARBA00025570}.
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; EC=2.1.1.321;
CC Evidence={ECO:0000256|ARBA:ARBA00000482};
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DR EMBL; KL494046; KFO12222.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087VHY0; -.
DR Proteomes; UP000053309; Unassembled WGS sequence.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase 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; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR014644; MeTrfase_PRMT7.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PROTEIN ARGININE N-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11006:SF4; PROTEIN ARGININE N-METHYLTRANSFERASE 7; 1.
DR Pfam; PF06325; PrmA; 1.
DR PIRSF; PIRSF036946; Arg_N-mtase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
DR PROSITE; PS51678; SAM_MT_PRMT; 2.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01015,
KW ECO:0000313|EMBL:KFO12222.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053309};
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:KFO12222.1}.
FT NON_TER 689
FT /evidence="ECO:0000313|EMBL:KFO12222.1"
SQ SEQUENCE 689 AA; 78546 MW; 4A880B9E332F54C0 CRC64;
MKTFCGRANP TTGAMEWLEE DENYDYHQEI ARSRYADMLH DKDRNTKYYQ GIRAAVSRVK
ERGEKAIVLD IGTGTGLLSM MAASAGADFC YAIEVFKPMA NAAVKIVEKN GFRDKIKVIN
KHSTEVTVGP DGDMQCRANI LVTELFDTEL IGEGALPTYE HAHKYLVQEG CEAVPHRATV
YVQLVESKRM WSWNKLFPVH VEAEDGEKII VSPSEMENCP GVPSVCDIQL NQMPSSDFTI
LSDVVTMFSV DFSKPVRSAS TYYRVQLEPV KSGKAQIVLS WWDIDMDPSG MISCTMAPYW
VKSTSAFQWR DHWMQCVYFL PNEEPVLQGE KVYLTACRDQ YSVWYKLEKA RGDEENKADV
RVESPVCRCQ AHLLWNRPRF GELNDQNRTQ QYVKSLMKVL KTDSVCLCIS DGSLLPVLAH
YLGAKQVQYF FLVFRSLRFT LGFLFFKANH LEDKIKIIEA RPELLTSSHL EDKKISVLVG
EPFFTTSLLP WHNLYFWYAR TAVTSHLTSN VTVLPQSASL HMMIVEFQDL WRIRSPCGTC
EGFDVQTMDD MINNSLNFRE SKEAEPHPLW EYPCKSLSDP QKVLTFDFRK TVPQHCLSTE
GSVNLLRKGK SHGAVLWMEY HLAADISVNT GLMQISNEKV FLQPNLLCQS VYFFSSVIES
ETLSDLPSTV TYAINFDTKT GEIAMDFKL
//
