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Database: UniProt
Entry: A0A3Q0FZW5_ALLSI
LinkDB: A0A3Q0FZW5_ALLSI
Original site: A0A3Q0FZW5_ALLSI 
ID   A0A3Q0FZW5_ALLSI        Unreviewed;      1044 AA.
AC   A0A3Q0FZW5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Lysine-specific demethylase PHF2 isoform X6 {ECO:0000313|RefSeq:XP_025052909.1};
GN   Name=PHF2 {ECO:0000313|RefSeq:XP_025052909.1};
OS   Alligator sinensis (Chinese alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025052909.1};
RN   [1] {ECO:0000313|RefSeq:XP_025052909.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_025052909.1; XM_025197124.1.
DR   AlphaFoldDB; A0A3Q0FZW5; -.
DR   Proteomes; UP000189705; 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; 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   4: Predicted;
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:UP000189705};
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          462..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          645..722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          761..817
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          831..987
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..513
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..531
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..572
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..709
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        761..798
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        803..817
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..856
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        914..957
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1044 AA;  116395 MW;  FEAB75D8E9EF3CA9 CRC64;
     MATVPVYCIC RLPYDVTRFM IECDACKDWF HGSCVGVEED EAPDIDIYHC PNCEKTHGKS
     TLKKKRNWHK HDTGQTTEVK PVQNGSQVFI KELRSRTFPS AEDIVVKVTG SQLTTEYLEE
     NGFTEPILVP KKDGLGLAVP APTFYVSDVE NYVGPERSVD VTDVTKQKDC KMKLKEFVDY
     YYSTNRKRVL NVTNLEFSDT RMSSFVEPPD IVKKLSWVEN YWPDDALLGK PKVTKYCLIC
     VKDSYTDFHI DSGGASAWYH VLKGEKIFYL IKPASANISL YERWQSAANH SEMFFADQVD
     KCYKCTVKQG QTLFIPSGWI YATLTPVDCL AFAGHFLHSL SVEMQMRAYE VERRLKIVSL
     TQFPNYETAC WYMGKHLLET FKGLHKAGQQ PPPHLLQGAK ILNGAFRSWT KKQALVDHED
     ELPENFKPAQ LIKDLAKEIR LSENASKANK TEASANVNVE EVCPVEKEET PSPIQVATPP
     PPTEKVPKKK TPKNVKTPKP PKVPKPPKHP KPPKTPKVKG EGKKKGKKAK ESPPPAIPNL
     DLLEAHTKEA LTKIETPKKG KNSKPDSLLK MEEEHKLEKT PLSGNKDNKF TFSFANKKLL
     GSKGVKTQLN TTVFGSLQNF KEDKTKPVRD EYEYVSDDGE LKIDEFPIRR KKNTTKRDLP
     FLSDKKETLQ HTPIKKPKVE SVSYKSDDSS DEDSLHIDTE AKPGRNSKVK KESGSSAGIL
     DLLQASKEVG GLEYNTNSQP PASPSTQEAI QGMLSMANLQ SSDSCLQTSW NTNQAKNNSI
     STQNSKKTGS SNNKNAGKRL LKKSTKNSID IEDYDDQDHL DACFKDSDYV YPSLESDEDN
     PVFKSRSKKR KSSDDAPYSP TARVGPSVPR QDRPVREGTR VASIETGLAA AAAKLSQQEE
     QKGKKKKNTK KKLSPNNTNK LSQEGSSPEP KLESHSSTLT DHEYTAGAST FGVAQVNRGS
     QPMAPGVFLT QKRPSSSPNN AAAKGPCVNH HSTKEARMTA FSTPPLEAVP LCSQSGKRTK
     KGMATAKQRL GKILKIHRNG KLLL
//
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