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Database: UniProt
Entry: A0A226MG47_CALSU
LinkDB: A0A226MG47_CALSU
Original site: A0A226MG47_CALSU 
ID   A0A226MG47_CALSU        Unreviewed;       184 AA.
AC   A0A226MG47;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Lysine-specific demethylase {ECO:0000256|RuleBase:RU369087};
DE            EC=1.14.11.65 {ECO:0000256|RuleBase:RU369087};
GN   ORFNames=ASZ78_012704 {ECO:0000313|EMBL:OXB54267.1};
OS   Callipepla squamata (Scaled quail).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC   Callipepla.
OX   NCBI_TaxID=9009 {ECO:0000313|EMBL:OXB54267.1, ECO:0000313|Proteomes:UP000198323};
RN   [1] {ECO:0000313|EMBL:OXB54267.1, ECO:0000313|Proteomes:UP000198323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texas {ECO:0000313|EMBL:OXB54267.1,
RC   ECO:0000313|Proteomes:UP000198323};
RC   TISSUE=Leg muscle {ECO:0000313|EMBL:OXB54267.1};
RA   Oldeschulte D.L., Halley Y.A., Bhattarai E.K., Brashear W.A., Hill J.,
RA   Metz R.P., Johnson C.D., Rollins D., Peterson M.J., Bickhart D.M.,
RA   Decker J.E., Seabury C.M.;
RT   "Disparate Historic Effective Population Sizes Predicted by Modern Levels
RT   of Genome Diversity for the Scaled Quail (Callipepla squamata) and the
RT   Northern Bobwhite (Colinus virginianus): Inferences from First and Second
RT   Generation Draft Genome Assemblies for Sympatric New World Quail.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' of
CC       histone H3, thereby playing a central role in histone code.
CC       {ECO:0000256|RuleBase:RU369087}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3]
CC         + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(9)-[histone H3] + 2
CC         succinate; Xref=Rhea:RHEA:60188, Rhea:RHEA-COMP:15541, Rhea:RHEA-
CC         COMP:15546, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:61976; EC=1.14.11.65;
CC         Evidence={ECO:0000256|ARBA:ARBA00036306,
CC         ECO:0000256|RuleBase:RU369087};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|RuleBase:RU369087};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|RuleBase:RU369087};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU369087}.
CC   -!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to mediate the
CC       association with nuclear receptors. {ECO:0000256|RuleBase:RU369087}.
CC   -!- DOMAIN: The JmjC domain and the C6-type zinc-finger are required for
CC       the demethylation activity. {ECO:0000256|RuleBase:RU369087}.
CC   -!- SIMILARITY: Belongs to the JHDM2 histone demethylase family.
CC       {ECO:0000256|ARBA:ARBA00037987, ECO:0000256|RuleBase:RU369087}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OXB54267.1}.
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DR   EMBL; MCFN01000952; OXB54267.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A226MG47; -.
DR   STRING; 9009.A0A226MG47; -.
DR   Proteomes; UP000198323; Unassembled WGS sequence.
DR   GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0032454; F:histone H3K9 demethylase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.120.650; Cupin; 2.
DR   InterPro; IPR045109; JHDM2-like.
DR   InterPro; IPR003347; JmjC_dom.
DR   PANTHER; PTHR12549; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN; 1.
DR   PANTHER; PTHR12549:SF7; LYSINE-SPECIFIC DEMETHYLASE 3A; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51184; JMJC; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Iron {ECO:0000256|RuleBase:RU369087};
KW   Metal-binding {ECO:0000256|RuleBase:RU369087};
KW   Nucleus {ECO:0000256|RuleBase:RU369087};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198323};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..184
FT                   /note="Lysine-specific demethylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012736905"
FT   DOMAIN          1..144
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
SQ   SEQUENCE   184 AA;  20716 MW;  F74D1D120608A7D2 CRC64;
     MGAHPPHVYV SVILRGCCVV TRLSLALQVA EEQGQENPVD HDPIHDQSWY LDRSLRKRLH
     QEYGVQGWAI VQFLGDVVFI PAGAPHQARR SATVCSLTPG QLCSTLTLVC SPQVHNLYSC
     IKVAEDFVSP EHVKHCFWLT QEFRYLSHTH TNHEDKLQVK NVIYHAVKDA VGILRANESS
     LSRS
//
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