ID A0A3Q3LF83_9TELE Unreviewed; 1013 AA.
AC A0A3Q3LF83;
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=PHD finger protein 8 {ECO:0000313|Ensembl:ENSMAMP00000008446.1};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000008446.1, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000008446.1}
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; A0A3Q3LF83; -.
DR STRING; 205130.ENSMAMP00000008446; -.
DR Ensembl; ENSMAMT00000008669.2; ENSMAMP00000008446.1; ENSMAMG00000005572.2.
DR GeneTree; ENSGT00940000157847; -.
DR InParanoid; A0A3Q3LF83; -.
DR Proteomes; UP000261640; 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:UP000261640};
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..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..629
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1013 AA; 111182 MW; 2B6DA4275C687963 CRC64;
MASVPVYCLC RLPYDVTRFM IECDICQDWF HGSCVGVEED KAAEIDLYHC PNCQVTHGPS
VMRKRRGGNK LTDVSATGAR DPSRPVKTGS PQFVRELRSR TFPSADEVLL KPSGAQLTVE
FLEEHSFSVP VMVLRRDGLG MTLPPSSFSV SDVEHYIGAD KEIDVIDVSR QCDLKMRLGD
FVEYYNSPNR DRVLNVISLE FSETRLSNLV ETPKIVRKLS WVENLWPEES VFERPNVQKY
CLMGVKDSYT DFHIDFGGTS VWYHVLRGEK IFYLISPTPA NLALFERWNS STNQNEMFFG
DQVDMCYKCS VKQGNTLFIP TGWIHAVLTP VDCLAFGGNF LHSLNIDMQL RAYEIEKRLS
TADMFKFPNF ETICWYVGKH LLDTFRGLRE NRRHPATYLV HGAKALNNAF RSWTRKEALA
EHEAEIPETI NTQTLVKDLA KEIRLVEDIF QQNIGRTGPQ FPGSPLSKAP LTTSQNSGRP
PGQKKGPKPK EVIGGHGPPG TKKKSQKGLL KAEAGELDLI EIHTKHTLKK FQPGKSKSKN
KLDLPLEEFE GKLNKSKLKL VLTNGKIQGK KDGSSNGAGS AGSYKHLATE GSSLSDLESE
DELQIDETPP PRRKPAGPSK KKKLSGLPRK LPRAKPCTDP NRIREPGEVD FDIEEDYTTD
EEALAAHGVK GGAGGILDLL KASKQVAGLD SATLSEEAPA SPSTRDAIQG MLSMANPPSS
SSSSSSSSPL SISGGLTEGL GVVKEKGGRA VWVTGGAKKT GSPEKKPVIQ RPGKRPIKRP
TRHISDEESA DEQETLGTCF KDSDYVYPSL ESDEEDHANK SKMKRKKNWD DTPWSPKARV
MPTLPKQDRP AREGARVASV ETGLAAAAAK LAQQEQQKPA KRKYTKKQRP PTEPAPPSPT
PASESAADFS PERRVDYYSA SLLDHEYTAG PGPFGPGGPR GSGAMAPGVF LTSRRPSLSP
QNSSSHSGTS PAGLASQGAM GVGQGKRPKK GLATAKQRLG KILKIHRNGK LLL
//
