ID A0A3P9B1P0_9CICH Unreviewed; 841 AA.
AC A0A3P9B1P0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Lysine demethylase 7A {ECO:0000313|Ensembl:ENSMZEP00005003789.1};
GN Name=KDM7A {ECO:0000313|Ensembl:ENSMZEP00005003789.1};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005003789.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005003789.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005003789.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family. JHDM1D
CC subfamily. {ECO:0000256|ARBA:ARBA00006942}.
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DR RefSeq; XP_004548436.1; XM_004548379.1.
DR AlphaFoldDB; A0A3P9B1P0; -.
DR STRING; 106582.ENSMZEP00005003789; -.
DR Ensembl; ENSMZET00005003942.1; ENSMZEP00005003789.1; ENSMZEG00005002933.1.
DR GeneID; 101484672; -.
DR KEGG; mze:101484672; -.
DR CTD; 321248; -.
DR GeneTree; ENSGT00940000158039; -.
DR OrthoDB; 2784357at2759; -.
DR Proteomes; UP000265160; LG17.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; 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 CDD; cd15640; PHD_KDM7; 1.
DR Gene3D; 1.20.58.1360; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR InterPro; IPR041070; JHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR PANTHER; PTHR23123:SF15; LYSINE-SPECIFIC DEMETHYLASE 7A; 1.
DR PANTHER; PTHR23123; PHD/F-BOX CONTAINING PROTEIN; 1.
DR Pfam; PF17811; JHD; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000265160};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 5..56
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 198..354
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 570..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 841 AA; 94920 MW; 3F548D85FDE4622A CRC64;
MAAAPLYCVC RQPYDVSRFM IECDICKDWF HGSCVQVEEH HAVDIDVYHC PNCDVVHGPS
LMKKRNNWHR HDYTEPDDGS KPVQAGTSVF IKELQNRTFP SAEEILIRMK GELVTTRYLE
RQGFNYPIAV TEMEGLGLKL PPSTFSVKDV EQYVGGNKVI DVIDVARQAD SKMKLSEFIK
YFTNPHRPKV LNLISLEFSD TKMAKLVEVP DVAQTLSWVE NYWPDDSFFP KPFVQKYCLM
GVKDSYTDFH IDFGGTSVWY HVLWGEKVFY LIKPTLTNLA LYEAWSSSPN QSEVFFGDKV
DKCYKCIVPQ GTTLLIPTGW IHAVLTSQDC MAFGGNFLHN LNIGMQLRCY EMERRLKTPD
LFKFPYFEAI CWYVAKNLLE MLKELREDNC PPPTYLVDGV KALISALKTW LKREVNEPTS
EVPDNIRPNH LIKELTKEIR YLEEEPVGGS KLVKSQGSGV PSGSNGCLST RATVERLCQA
RRARRAARQL REQERHAPKL PTNLDILEQH TRDVLKRLEV GPLEEDPAFG AKVHAKFNKV
STASAAAAAE SLEDNHIRLM LVNGRIIRDL RRPGSSSPVK SEDEGLSVGP PKGCMDVKFE
RMYDSQERHS TAEKSALLRD LERMKTELGE EVSGHSSVSD VESDSDFPTE HKESSSSSSS
DEDSESSQDE EDEDEQQTGS GHIKLDQSGE KLRHKHKPLK RECPTSPSTA EAIQGMLSMA
GLLCSSKSET ADSLQESWWP SPLEQAQHQR RLQGDKSPID SQGNSSSEAW DNQGLPSPEM
DYQYCDPSMS PPLHPSKRHA PNPPPISNQA TKGKRPKKGM ATAKQRLGKI LKLSRHNRVF
V
//
