ID   A0A151WNP9_9HYME        Unreviewed;       384 AA.
AC   A0A151WNP9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Bifunctional arginine demethylase and lysyl-hydroxylase PSR {ECO:0000313|EMBL:KYQ49494.1};
GN   ORFNames=ALC60_11423 {ECO:0000313|EMBL:KYQ49494.1};
OS   Trachymyrmex zeteki.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ49494.1, ECO:0000313|Proteomes:UP000075809};
RN   [1] {ECO:0000313|EMBL:KYQ49494.1, ECO:0000313|Proteomes:UP000075809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ49494.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYQ49494.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex zeteki WGS genome.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
CC   -!- SIMILARITY: Belongs to the JMJD6 family.
CC       {ECO:0000256|ARBA:ARBA00038068}.
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DR   EMBL; KQ982905; KYQ49494.1; -; Genomic_DNA.
DR   RefSeq; XP_018311884.1; XM_018456382.1.
DR   AlphaFoldDB; A0A151WNP9; -.
DR   STRING; 64791.A0A151WNP9; -.
DR   GeneID; 108728036; -.
DR   OrthoDB; 120564at2759; -.
DR   Proteomes; UP000075809; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1280.270; -; 1.
DR   Gene3D; 2.60.120.650; Cupin; 1.
DR   InterPro; IPR003347; JmjC_dom.
DR   PANTHER; PTHR12480; ARGININE DEMETHYLASE AND LYSYL-HYDROXYLASE JMJD; 1.
DR   PANTHER; PTHR12480:SF32; BIFUNCTIONAL ARGININE DEMETHYLASE AND LYSYL-HYDROXYLASE JMJD6; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51184; JMJC; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000313|EMBL:KYQ49494.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075809};
KW   Transferase {ECO:0000313|EMBL:KYQ49494.1}.
FT   DOMAIN          146..310
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   REGION          335..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..366
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   384 AA;  44684 MW;  A5A61BB0A1E7AD4A CRC64;
     MTEAWRLDHR ARKRIKEVKK KARPELADKA AWIQHGYCKI FQKFWEFQDN AERIDESSVA
     TEEFVEKYEK PYKPVIIRGV QNGWRAQHKW TIERLAKKYR NQKFKCGEDN EGYSVKMKMK
     YYVRYIFNNE DDSPLYIFDS SFGEHPRRKK LLEDYVIPKY FRDDLFHHAG EHRRPPYRWF
     VMGPARSGTG IHIDPLGTSA WNALISGHKR WCLFPTHTPR ELLKVTAAEG GKQRDEAITW
     FSIVYPRTKL PTWPKDCRPI EILQTPGETV FIPGGWWHIV LNLDETIAVT QNFCSRTNFP
     VVWHKTVRGR PKLSRKWLKV LNDKEPELAT LAETIDVKED TGVASDSSSG SSSSSSSSTS
     SSQSEDSEDD SGQESLTAHK KKKR
//