ID A0A3P8TG20_AMPPE Unreviewed; 1077 AA.
AC A0A3P8TG20;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=PHD finger protein 2 {ECO:0000313|Ensembl:ENSAPEP00000022638.1};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000022638.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000022638.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000022638.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3P8TG20; -.
DR STRING; 161767.ENSAPEP00000022638; -.
DR Ensembl; ENSAPET00000023237.1; ENSAPEP00000022638.1; ENSAPEG00000016046.1.
DR GeneTree; ENSGT00940000158148; -.
DR OMA; KDIVHTQ; -.
DR Proteomes; UP000265080; Chromosome 6.
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; cd15554; PHD_PHF2_like; 1.
DR Gene3D; 1.20.58.1360; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23123:SF14; LYSINE-SPECIFIC DEMETHYLASE PHF2; 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:UP000265080};
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 197..353
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 450..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..510
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..870
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..901
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1077 AA; 120531 MW; 462AFA3FE5E2A50B CRC64;
MATVPVYCIC RLPYDVTQFM IECDACKDWF HGSCVGVDED DAPDIDIYHC PNCEKTHGKS
TLKKKKNWSK HDTGQSTDIK AVQNGSQVFI KELRSRTFPS ADDVVVKLGG SQLTLDYLEE
NGFNEPILVQ KKDGLGVSMP APTFYISDVE NYVGPDIGVD VVDVTKQTDS KMKLKEFVDY
YYSTNRKKVL NVINLEFSDT RMNSIVESPQ IVRRLSWVEN YWPDDALLGK PKVTKYCLIC
VKDSYTDFHI ECGGASVWYH VLKGEKIFFL IKPTSANLSL YERWRSSSNH TEMFFADQVD
KCYKCTLKQG QTLFIPSGWI NAILTPVDCL AFSGHFVHNL SVEMQMRAYE IEKRLKVKTL
TPFPNFETAC WYVGRHLLER FKGLHKANKQ PAPYLIHGAK IINGAFRAWT KKQALLEHED
ELPENMKPSQ LIKDLAKEIR LSENATKAIK SEPSIKVPVE EPPSTHSEPE EDISPAHVPS
PSREKSRKKA SKPPKPPKPP KPPKMPKAPK PPKMPKVKEG GKKKAKKAKE LSPPPKPSSF
AALESHAKDI LSKMDQPKKT KAVKNVLSMS EKEISKQNNV EKFEIREQNK NKTEAKWKYK
NSKPDSLLKM EEECKFDRTP LSGNKDRFSF TMSHRKMPSS KTLKPQTNSS VFGSLQNLKE
DKTKPVRDEY EYVSDEGELK IDEFPIRRKK NTVKRDLSFL SDIREPIQPA KKPKFQPFVT
KTMDSSDEET LHIDTEAKPE VKSRNSKVKK KGGSAAGILD LLQASKQVGG IDYSANSQPP
ASPSTQEAIQ GMLSMANLSS SESLQQPWSN SQSKSNSHSS QASKKAGGGA GGGNNSKRPT
KRLPKKPRKS SSIESLDYDD DQDHMDACFK DSDYVYPSLE SEEDNPVFKS RSKKRKSSDD
TPYSPTARVG PSVPRQERPA REGARVASIE TGLAAAAAKL SHQEEQQKTK KKKKSTKKKT
IVIEEPPKIS QDSSSPEHNL DSQDGSLTDH EFNTGTVKSP GGPQPMAPGV FLSQRRPSMS
SPNNSTNSTS TNSSSMAKLD RVGSADAKAK RLKKGMATAK QRLGKILKIH RNGKLLL
//