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Database: UniProt
Entry: A0A2U4BMA2_TURTR
LinkDB: A0A2U4BMA2_TURTR
Original site: A0A2U4BMA2_TURTR 
ID   A0A2U4BMA2_TURTR        Unreviewed;       352 AA.
AC   A0A2U4BMA2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 {ECO:0000256|ARBA:ARBA00039354};
DE   AltName: Full=Histone arginine demethylase JMJD6 {ECO:0000256|ARBA:ARBA00041379};
DE   AltName: Full=JmjC domain-containing protein 6 {ECO:0000256|ARBA:ARBA00042860};
DE   AltName: Full=Jumonji domain-containing protein 6 {ECO:0000256|ARBA:ARBA00042719};
DE   AltName: Full=Lysyl-hydroxylase JMJD6 {ECO:0000256|ARBA:ARBA00041767};
DE   AltName: Full=Peptide-lysine 5-dioxygenase JMJD6 {ECO:0000256|ARBA:ARBA00042996};
DE   AltName: Full=Phosphatidylserine receptor {ECO:0000256|ARBA:ARBA00042876};
GN   Name=JMJD6 {ECO:0000313|RefSeq:XP_019794345.1};
OS   Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Delphinidae; Tursiops.
OX   NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019794345.1};
RN   [1] {ECO:0000313|RefSeq:XP_019794345.1}
RP   IDENTIFICATION.
RC   TISSUE=Spleen {ECO:0000313|RefSeq:XP_019794345.1};
RG   RefSeq;
RL   Submitted (NOV-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   RefSeq; XP_019794345.1; XM_019938786.2.
DR   AlphaFoldDB; A0A2U4BMA2; -.
DR   GeneID; 101334570; -.
DR   OrthoDB; 120564at2759; -.
DR   Proteomes; UP000245320; Chromosome 20.
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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000245320}.
FT   DOMAIN          141..305
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   REGION          324..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   352 AA;  40845 MW;  5AEE410A17099BE6 CRC64;
     MNHKSKKRIR EAKRSARPEL KDSLDWIRHN YYESFSLNPA AVADNVERAD ALQLSVGEFV
     ERYERPYKPV VLLNAQEGWS AQEKWTLERL KRKYRNQKFK CGEDNDGYSV KMKMKYYIEY
     MESTRDDSPL YIFDSSYGEH PKRRKLLEDY KVPKFFTDDL FQYAGEKRRP PYRWFVMGPP
     RSGTGIHIDP LGTSAWNALV QGHKRWCLFP TSTPRELIKV TREEGGNQQD EAITWFNIIY
     PRTQLPTWPP EFKPLEILQK PGETVFVPGG WWHVVLNLDT TIAITQNFAS STNFPVVWHK
     TVRGRPKLSR KWYRTDTARA AAVQATPSHP VPLCPNPDLE GPALGDLEAG AP
//
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