ID A0A2K6PQN4_RHIRO Unreviewed; 701 AA.
AC A0A2K6PQN4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Protein arginine N-methyltransferase {ECO:0000256|PIRNR:PIRNR036946};
DE EC=2.1.1.321 {ECO:0000256|PIRNR:PIRNR036946};
GN Name=PRMT7 {ECO:0000313|Ensembl:ENSRROP00000018836.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000018836.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000018836.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 ECO:0000256|PIRNR:PIRNR036946}.
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,
CC ECO:0000256|PIRNR:PIRNR036946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|PIRNR:PIRNR036946}. Nucleus
CC {ECO:0000256|PIRNR:PIRNR036946}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family. PRMT7
CC subfamily. {ECO:0000256|PIRNR:PIRNR036946}.
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DR RefSeq; XP_010353347.1; XM_010355045.1.
DR AlphaFoldDB; A0A2K6PQN4; -.
DR STRING; 61622.ENSRROP00000018836; -.
DR Ensembl; ENSRROT00000042998.1; ENSRROP00000018836.1; ENSRROG00000033451.1.
DR GeneID; 104655594; -.
DR KEGG; rro:104655594; -.
DR CTD; 54496; -.
DR GeneTree; ENSGT00940000156879; -.
DR OMA; CHHDEYS; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0042393; F:histone binding; IEA:Ensembl.
DR GO; GO:0044020; F:histone H4R3 methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IEA:Ensembl.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:Ensembl.
DR GO; GO:0071514; P:genomic imprinting; IEA:Ensembl.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|PIRNR:PIRNR036946};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR036946};
KW Differentiation {ECO:0000256|PIRNR:PIRNR036946};
KW Methyltransferase {ECO:0000256|PIRNR:PIRNR036946, ECO:0000256|PROSITE-
KW ProRule:PRU01015}; Nucleus {ECO:0000256|PIRNR:PIRNR036946};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR036946};
KW Transcription {ECO:0000256|PIRNR:PIRNR036946};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR036946};
KW Transferase {ECO:0000256|PIRNR:PIRNR036946, ECO:0000256|PROSITE-
KW ProRule:PRU01015}.
SQ SEQUENCE 701 AA; 79370 MW; B54CE7977F4F429E CRC64;
MKIFCSRANP TTGSVEWLEE DEHYDYHQEI ARSSYADMLH DKDRNVKYYQ GIRAAVSRVK
DRGQKALVLD IGTGTGLLSM MAVTAGADFC YAIEVFKPMA AAAAEIVEKN GFRDKIMVIN
KHSTEVTVGP EGDMPCRANI LVTELFDTEL IGEGALPSYE HAHRHLVEEN CEAVPHRATV
YAQLVESRRM WSWNKLFPIR VQTSLGEQVI VPPVDLENCP GAPSVCDIQL NQVSPADFTV
LSDVLPMFSI DFSKQVSSSA ACHSRQFEPL TSGRAQVVLS WWDIEMDPEG KIRCTTAPFW
AHSDPEEMQW RDHWMQCVYF LPQEEPVVQG SALCLVAHHD DYCVWYSLQR TSPEKNERVH
QMRPVCDCQA HLLWNRPRFG EINDQDRTDR YIQALSTVLK PDSVCLCVSD GSLLSVLAHH
LGVEQVFTVE SSAASHKLLR KIFKANHLED KINLIEKRPE LLTSEDLKDR KVSLLLGEPF
FTTSLLPWHN LYFWYVRTAV DRHLGPGAVV MPQAASLHAV VVEFRDLWRI RSPCGDCEGF
DVHVMDDMIK RALDFRESKE AEPHPLWEYP CRSLSEPRQI LAFDFRQLVP PRLLCAEGTM
ELRRPGRSHA AVLWMEYHLT PECTLSTGLL EPADPEGGCC WNPHCKQAVY FFSPVPDPRA
PLGGPQTVSY AVEFHPDTGD ITMEFRLADT PDSPLLSNKV A
//
