ID A0A087XTK1_POEFO Unreviewed; 1069 AA.
AC A0A087XTK1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=PHD finger protein 2 {ECO:0000313|Ensembl:ENSPFOP00000009104.2};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000009104.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000009104.2}
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 EMBL; AYCK01015299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01015300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01015301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01015302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01015303; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007573386.1; XM_007573324.2.
DR AlphaFoldDB; A0A087XTK1; -.
DR STRING; 48698.ENSPFOP00000009104; -.
DR Ensembl; ENSPFOT00000009116.2; ENSPFOP00000009104.2; ENSPFOG00000008892.2.
DR GeneID; 103152735; -.
DR CTD; 5253; -.
DR eggNOG; KOG1633; Eukaryota.
DR GeneTree; ENSGT00940000158148; -.
DR OMA; KDIVHTQ; -.
DR OrthoDB; 2784357at2759; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
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:UP000028760};
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 451..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1069 AA; 119635 MW; 0D64861B121FC9F5 CRC64;
MATVPVYCIC RLPYDVTQFM IECDACKDWF HGSCVGVDED DAPDIDIYHC PNCEKTHGKS
TLKKKKNWSK HDTGQSTDIR AVQNGSQVFI KELRSRTFPS ADDIVVKLSS SQLTLDYLEE
NGFNEPILVQ KKDGLGMSMP PPTFYISDVE KYVGPDVPVD VVDVTKQTDS QMKLKEFVDY
YYSTNRKKVL NVINLEFSDT RMSSVVESPQ IVRRLSWVEN YWPDDALLGK PKVTKYCLIC
VKDSYTDFHI ECGGASVWYH VLKGEKIFFL IKPTSANLSL YERWRSSSNH GEMFFADQVD
KCYKCTLKQG QTLFVPSGWI NAVLTPVDCL AFSGHFVHNL SVEMQMRAYE IEKRLKVKTL
TPFPNFETAC WYVGRHLLER FKGLHKANKQ PAPYLIHGAK IINGAFRAWT KKQALLEHED
ELPENMKPSQ LIKDLAKEIR LSENATKAIK SEPSIKAPVE EPAFTHSEPD EPVSPATIPS
PSREKPKKKA PKSQKPPKAP KAPKPPKVKD GEKKKVKKIK ELSPPPKPSS FAALESHAKE
ILSQMDQQKK PRFVKNVLSV SEKETSKQNN MDKFEIREQN KNKTEAKWKY KNSKPDSLLK
MEEECKFDRI PLSGNKDRFS FTMSHRKLAS SKTLKPQTNS SIFGSLQNLK EDKTKPVRDE
YEYVSDEGEL KIDEFPIRRK KNTVKRDLSF LSDIREPLQP AKKAKSQPLV TKSVDSSDEE
TLHIDTEAKP EVKSRNSKVK KKSGSAAGIL DLLQASKQVG GIDYNTNSQP PASPSTQEAI
QGMLSMANLS SSETLEQPWS NSQSKSNSHG SQAYKKSGAG AGGSSNSKRP TKRLPKKPRK
SSSIESLDYD DDEQDHMDAC FKDSDYVYPS LESEEDNPVF KSRSKKRKSS DDTPYSPTAR
VGPSVPRHER PAREGARVAS IETGLAAAAA KLSHQEEQQR TKKKKKSGKK KSAAVEEPPK
HSQDSSSPDH NADSQDGSLT DHEFTTGTAK SPGGPQPMAP GIFLSQRRPS VSSPNNSTNS
TSTNSSSAAR ADRLGPADAK AKRLKKGMAT AKQRLGKILK IHRNGKLLL
//
