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Database: UniProt
Entry: A0A3Q3AE15_KRYMA
LinkDB: A0A3Q3AE15_KRYMA
Original site: A0A3Q3AE15_KRYMA 
ID   A0A3Q3AE15_KRYMA        Unreviewed;       847 AA.
AC   A0A3Q3AE15;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Lysine demethylase 7A {ECO:0000313|Ensembl:ENSKMAP00000014833.1};
GN   Name=KDM7A {ECO:0000313|Ensembl:ENSKMAP00000014833.1};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000014833.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000014833.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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_017267163.1; XM_017411674.1.
DR   AlphaFoldDB; A0A3Q3AE15; -.
DR   STRING; 37003.ENSKMAP00000014833; -.
DR   Ensembl; ENSKMAT00000015050.1; ENSKMAP00000014833.1; ENSKMAG00000011120.1.
DR   GeneID; 108233298; -.
DR   CTD; 321248; -.
DR   GeneTree; ENSGT00940000158039; -.
DR   OMA; PWEEDIT; -.
DR   OrthoDB; 2784357at2759; -.
DR   Proteomes; UP000264800; Unplaced.
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:UP000264800};
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          567..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          624..847
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        647..661
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..785
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   847 AA;  95045 MW;  2818EC225CE6C0BA CRC64;
     MAAAPLYCVC RQPYDVSRFM IECDICKDWF HGSCVQVEEH HAVDIDVYHC PNCDVKHGPS
     LMKKRNNWHR HDYTEPNDGL KPVQAGTSVF IKKLQNRTFP GAEEIMIRMR GEQVTTRFLE
     RHGFNYPIMI TEMEGLGLKL PPPTFSVKDV VQYVGGDKVI DVIDVARQAD SKMKLSEFIK
     YFTKPHRPKV LNLISLEFSD TKMSELVEVP DVAKKMSWVE NYWPDDSFFP KPFVQKYCLM
     GVKDSYTDFH IDFGGTSVWY HVLWGEKVFY LIKPTPANLA LYEAWSSSPN QSEVFFGDKV
     DKCYKCVVPQ GTTLLIPTGW IHGVLTSQDC MAFGGNFLHN LNIGMQLRCY EMERRLKTPD
     LFKFPYFEAI CWYVAKNLLE MLKELREDSC PPSTYLVDGV KALIGALRTW LKREVTEPSS
     EVPDNIRPNH LIKELTKEIR YLEEEPLSGG KPVKSQGCGA SSGMNGCLTT RSLERLCQAR
     QARRAARRLR EQQRQAPKVP SNLDILEQHT REVLKRLEVG PLEEDPGFCA KVHGKFNKVS
     TASAAAVAES LEDNHLRLMM VNGRIIRRPE SSPVKTEGEQ SSAGHSPTKS CVAVKLEKTP
     GGQEQRSAAE KATLLRGLET VKNELREDAS GHSSVSDVES DSDSPTERKA SSSSSSSSDD
     DSASSQEEEE ERGLSQQAGS GHTIELDPSG QALRHKHKPL KRERPTSPST EEAIQGMLSM
     AGLLCSSKPG EVTSPREPWW SSPSQRSLQE SHPHQHRLQG GNSPMDSQGN SSSEAWDNQG
     LPSPETDYQY CDPSMSPPLH PSKRHAPNPP PVSNQATKGK RPKKGMATAK QRLGKILKLN
     RHSHVFV
//
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