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Database: UniProt
Entry: A0A3B4D1J0_PYGNA
LinkDB: A0A3B4D1J0_PYGNA
Original site: A0A3B4D1J0_PYGNA 
ID   A0A3B4D1J0_PYGNA        Unreviewed;       367 AA.
AC   A0A3B4D1J0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Jumonji domain containing 6, arginine demethylase and lysine hydroxylase {ECO:0000313|Ensembl:ENSPNAP00000017435.1};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000017435.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000017435.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 2-oxoglutarate + N(omega),N(omega)'-dimethyl-L-arginyl-
CC         [protein] + 2 O2 = 2 CO2 + 2 formaldehyde + L-arginyl-[protein] + 2
CC         succinate; Xref=Rhea:RHEA:58348, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC         COMP:11992, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:16842, ChEBI:CHEBI:29965, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:88221; Evidence={ECO:0000256|ARBA:ARBA00036511};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-lysyl-[protein] + O2 = (5S)-5-hydroxy-L-
CC         lysyl-[protein] + CO2 + succinate; Xref=Rhea:RHEA:58360, Rhea:RHEA-
CC         COMP:9752, Rhea:RHEA-COMP:15144, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:141843;
CC         Evidence={ECO:0000256|ARBA:ARBA00035940};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + N(omega),N(omega)'-dimethyl-L-arginyl-
CC         [protein] + O2 = CO2 + formaldehyde + N(omega)-methyl-L-arginyl-
CC         [protein] + succinate; Xref=Rhea:RHEA:58472, Rhea:RHEA-COMP:11990,
CC         Rhea:RHEA-COMP:11992, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:65280, ChEBI:CHEBI:88221;
CC         Evidence={ECO:0000256|ARBA:ARBA00036252};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + a 5'-end methyltriphosphate-guanosine-
CC         ribonucleotide-snRNA + O2 = a 5'-end triphospho-guanosine-
CC         ribonucleotide-snRNA + CO2 + formaldehyde + H(+) + succinate;
CC         Xref=Rhea:RHEA:58784, Rhea:RHEA-COMP:15220, Rhea:RHEA-COMP:15221,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:138278, ChEBI:CHEBI:142789;
CC         Evidence={ECO:0000256|ARBA:ARBA00036280};
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   AlphaFoldDB; A0A3B4D1J0; -.
DR   Ensembl; ENSPNAT00000038531.1; ENSPNAP00000017435.1; ENSPNAG00000005464.1.
DR   GeneTree; ENSGT00940000156867; -.
DR   OMA; NAWVAMR; -.
DR   Proteomes; UP000261440; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; 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;
FT   DOMAIN          105..269
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   REGION          299..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   367 AA;  42473 MW;  F83D5D448E87C7AE CRC64;
     MFFLLPKDNV ERVDVLRLSP EEFIQRFEKP YKPVVLLNCQ ESWPAREKWT LERLKRKYRN
     QKFKCGEDND GYSVKMKMKY YVEYMESTRD DSPLYIFDSS YGEHAKRRKL LEDYQVPVFF
     RDDLFQFAGE KRRPPYRWFV MGPARSGTGI HIDPLGTSAW NALVQGHKRW CLFPTHTPRE
     LIKVTRDEGG NQQDEAITWF SVIYPRTQQP TWPAEFRPLE ILQRPGETVF VPGGWWHVVL
     NLDTTIAVTQ NFASTTNFPI VWHKTVRGRP KLSRKWYRIL KQERPDLAAL ADKVDLQEST
     GIASDSSSDS SSSSSSSSSD SDSEAESGSE GDPMAHRRKK RRTCGMMGNG DITSQDDCAS
     KERSSSR
//
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