ID A0A3Q1H5G7_9TELE Unreviewed; 963 AA.
AC A0A3Q1H5G7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=PHD finger protein 8 {ECO:0000313|Ensembl:ENSAPOP00000024215.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000024215.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000024215.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family. JHDM1D
CC subfamily. {ECO:0000256|ARBA:ARBA00006942}.
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DR AlphaFoldDB; A0A3Q1H5G7; -.
DR Ensembl; ENSAPOT00000009310.1; ENSAPOP00000024215.1; ENSAPOG00000006591.1.
DR GeneTree; ENSGT00940000157847; -.
DR Proteomes; UP000257200; 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; cd15642; PHD_PHF8; 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:SF11; HISTONE LYSINE DEMETHYLASE PHF8; 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:UP000257200};
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 201..357
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 61..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..790
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..871
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..937
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 963 AA; 106443 MW; 0C02B75371876CE5 CRC64;
MASVPVYCLC RLPYDVTRFM IECDICQDWF HGSCVGVEED KAAEIDLYHC PNCQVTHGPS
VMRKRRGGNK QIDAGTAGGR DPSRPVKTGS PQFVRELRSR TFPNADEVLL KPSGAQLTVE
FLEEHSFSVP VMVLRRDGLG MTLPPSSFSV TDVEHYIGSD KEIDVIDVSR QCDLKMRLGD
FVEYYNSPNR DRVLNVISLE FSETRLSNLV ETPKIVRKLS WVENLWPEES VFERPNVQKY
CLMGVKDSYT DFHIDFGGTS VWYHVLRGEK IFYLISPTPA NLALFERWNS SSNQNEMFFG
DQADMCYKCS VKQGNTLFIP TGWIHAVLTP VDCLAFGGNF LHSLNIDMQL RAYEIEKRLS
TADLFKFPNF ETVCWYVGKH LLDTFRGLRE NRRHPATYLV HGAKALNNAF RTWTRKEALA
EHEVEIPETI NTQTLVKDLA KEIRLVEDIF QQNIGRTGPQ FPGSPLSKAP LTTSQNSGRP
PGKKKGPKPK EVMGGLGPPG TKKKNQKGLL KAEAGELDLI EIHTKHTLKK FQPGKSKHKN
KPTTCWDFTC YYSVFSKKDG SNGAGRAGNY KHLAAEGSSL SDLESEDELQ IDETPPPRRK
PAGPGLPRKL PRAKPCSDPN RIREPGEVDF DIEEDYTTDE EALAAHGVKG GAGGILDLLK
ASKQVAGLDS SALSEEAPAS PSTRDAIQGM LSMANPPSSS SSSSSSSPLS ISGGLTEGLG
VKKPVIERPG KRPIKRPARH LSDEESPDEQ ETLGTCFKDS DYVYPSLESD EEDHVNKTKM
KRKKNWDDTP WSPKARVMPT LPKQDRPARE GARVASVETG LAAAAAKLAQ QEQQKPAKRK
YTKKQRPPPP VVTPPPVQTE PAPPSPTPAP ESVADVSPDR RMDYYSASLL DHEYTAGPGP
FGPGGPRGSG AMAPGVFLTS RRPSLSPQNS SSHSGKRPKK GLATAKQRLG KILKIHRNGK
LLL
//
