ID A0A2K5CWW9_AOTNA Unreviewed; 531 AA.
AC A0A2K5CWW9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Protein arginine methyltransferase 3 {ECO:0000313|Ensembl:ENSANAP00000013183.1};
GN Name=PRMT3 {ECO:0000313|Ensembl:ENSANAP00000013183.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000013183.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000013183.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_012311911.1; XM_012456488.1.
DR AlphaFoldDB; A0A2K5CWW9; -.
DR STRING; 37293.ENSANAP00000013183; -.
DR Ensembl; ENSANAT00000031005.1; ENSANAP00000013183.1; ENSANAG00000024501.1.
DR GeneID; 105720177; -.
DR CTD; 10196; -.
DR GeneTree; ENSGT00940000156825; -.
DR OrthoDB; 197898at2759; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IEA:Ensembl.
DR GO; GO:0043022; F:ribosome binding; IEA:Ensembl.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:1900053; P:negative regulation of retinoic acid biosynthetic process; IEA:Ensembl.
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; IPR049482; ANM3-like_C2H2_Zf.
DR InterPro; IPR049009; ANM3_Znf-C2H2.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR11006; PROTEIN ARGININE N-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11006:SF114; PROTEIN ARGININE N-METHYLTRANSFERASE 3; 1.
DR Pfam; PF21137; ANM3_C2H2_Zf; 1.
DR Pfam; PF21336; ANM3_zf-C2H2; 1.
DR Pfam; PF06325; PrmA; 1.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01015}; Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01015}.
FT DOMAIN 50..71
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..37
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 531 AA; 59995 MW; 2566F8848CD32695 CRC64;
MCSLASGATG GRGAVEDEED LPELSDSGDE AAWEDEDDAD LPHDKQQTPC LFCNRLFTSA
EETFSHCKSE HQFNIDSMVH KHGLEFYGYI KLINFIRLKN PTVEYMNSIY NPVPWEKEEY
LKPVLEDDLL LQFDVEDLYE PVSVPFSYPN GLSENTSVVE KLKHMEARAL SAEAALARAR
EDLQKMKQFA QDFVMNADVR TCSSSTSAIA DLQEDEDCVY FSSYGHYGIH EEMLKDKIRT
ESYRDFIYQN PHIFKDKVVL DVGCGTGILS MFAAKAGAKK VLGVDQSEIL YQAMDIIRLN
KLEDTITLIK GKIEEVHLPV EKVDVIISEW MGYFLLFESM LDSVLYAKNK YLAKGGSVYP
DICTISLVAV SDVNKHAERI AFWDDVYGFK MSCMKKAVIP EAVVEVLDPK TLISEPCGIK
YIDCHTTSIS DLEFSSDFTL KITKTSMCTA LAGYFDIYFE KNCHNRVVFS TGPQSIKTHW
KQTVFLLEKP FAVKAGETLK GKVTVHKNKK DPRSLTVTLT LNNSTQTYSL Q
//
