ID A0A060XLV8_ONCMY Unreviewed; 403 AA.
AC A0A060XLV8; A0A8C7S9B4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Jumonji domain containing 6, arginine demethylase and lysine hydroxylase {ECO:0000313|Ensembl:ENSOMYP00000063071.2};
GN ORFNames=GSONMT00034781001 {ECO:0000313|EMBL:CDQ80603.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ80603.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ80603.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ80603.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSOMYP00000063071.2}
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 EMBL; FR905628; CDQ80603.1; -; Genomic_DNA.
DR STRING; 8022.A0A060XLV8; -.
DR PaxDb; 8022-A0A060XLV8; -.
DR Ensembl; ENSOMYT00000068676.2; ENSOMYP00000063071.2; ENSOMYG00000029172.2.
DR GeneTree; ENSGT00940000156867; -.
DR OrthoDB; 120564at2759; -.
DR Proteomes; UP000193380; Unassembled WGS sequence.
DR Proteomes; UP000694395; Chromosome 13.
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:UP000193380}.
FT DOMAIN 141..305
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 403 AA; 46686 MW; 9BECA5409DC601B6 CRC64;
MNHKSKKRIK EAKRSARPEL KDSSDWTKHD YCETFDVSHR SVKDNVERVD TLRLSAEEFI
QRFERPYKPV VLLNCQDTWP AREKWTMERL KRKYRNQKFK CGEDNDGYSV KMKMKYYVEY
LESTQDDSPL YIFDSSYGEH AKRRKLLEDY QVPVYFRDDL FQFAGEKRRP PYRWFVMGPA
RSGTGIHIDP LGTSAWNALV QGHKRWCLFP THTPRELIKV TRDDGGNQQD EAITWFNVVY
PRTQQPTWPA EFRPLEILQG PGETVFVPGG WWHVVLNMDT TIAITQNFAS TTNFPIVWHK
TVRGRPKLSR KWYRILKQER PDMATLADKV DLQESTGIAS DSSSDSSSSS SSSSSDSDSE
AESGSEGDAM SHRRKKRKTC GMISNGDSST KDDCVSKERS SSR
//
