ID A0A3Q0HJR9_ALLSI Unreviewed; 1072 AA.
AC A0A3Q0HJR9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Lysine-specific demethylase 2A isoform X4 {ECO:0000313|RefSeq:XP_025071922.1};
GN Name=KDM2A {ECO:0000313|RefSeq:XP_025071922.1};
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_025071922.1};
RN [1] {ECO:0000313|RefSeq:XP_025071922.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_025071922.1; XM_025216137.1.
DR AlphaFoldDB; A0A3Q0HJR9; -.
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:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR CDD; cd21784; CTD_KDM2A; 1.
DR CDD; cd22181; F-box_FBXL11; 1.
DR CDD; cd15643; PHD_KDM2A; 1.
DR Gene3D; 1.20.58.1360; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR041070; JHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR002857; Znf_CXXC.
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:SF3; LYSINE-SPECIFIC DEMETHYLASE 2A; 1.
DR PANTHER; PTHR23123; PHD/F-BOX CONTAINING PROTEIN; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF17811; JHD; 1.
DR Pfam; PF16866; PHD_4; 1.
DR Pfam; PF02008; zf-CXXC; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00367; LRR_CC; 5.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51058; ZF_CXXC; 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 Repressor {ECO:0000256|ARBA:ARBA00022491};
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:PRU00509}.
FT DOMAIN 61..229
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 478..524
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 531..592
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 277..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..469
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..704
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..782
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1072 AA; 122298 MW; 18C68BC7850052F5 CRC64;
MPDPDFSVND VRLYVGSRRM VDVMDVNTQR DIEMSMAQWA RYYETPEEER EKLYNVISLE
FSHTRLENLV QRPATVDLID WVDNMWPRHL KESQTESTNA ILEMQYPKVQ KYCLMSVKGC
YTDFHVDFGG TSVWYHIHRG GKIFWLIPPT PQNLELYENW LLSGKQGDIF LGDRVSECQR
IELKQGYTFV IPSGWIHAVY TPTDTLVFGG NFLHSFNIPM QLRIYSIEDR TRVPNKFRYP
FYYEMCWYVL ERYVYCITNR SHLTKDFQKE SLSMDMELSS SESGNVDEEE DAADKEPRRP
VTRRSVLTSP VANGANLDYD ELSKGCRSLP GLKKTPSTDS SDSSRAPQNG QAWDPLASSP
HKSNKVHLTQ FELEGLRCLM DKLESLPLHK KCVPTGIEDE DALIADVKLL LEEYANSDPK
LALTGIPIVQ WPKRDKLKFQ ARPKLRLPTI PITKPHTMKP APRPAPVRPT VSPIVSGARR
RRVRCRKCKA CMQGECGMCH YCRDMKKFGG PGRMKQSCVL RQCLAPRLPH SVTCALCGEV
DQNEDSQDFE KKLMECCICN EIVHPGCLQM DGEGLLNDEL PNCWECPKCY QGDDSEKGQK
RKMEDSDEGT VQAKVLRPLR SCEEPLTPPP NSPTPMLQLI HDPASPRGMV TRSSPGAGPS
DHHSASRDER FKRRQLLRLQ ATERTMVREK ENNPSGKKEL SEVEKAKLHG SYLTVTLQRP
TKDMHGTSIV PKLQAITASS TNLRHSPRVV MRHSPARTPQ RGGDEEAEEE EEEEEEEDES
AEEGGAARLN GKGRLQDGEE SWMQREVWMS VFRYLTRREL CECMRVCKTW YKWCCDKRLW
TKIDLSRCKS ITPQALSGII KRQPVSLDLS WTNISKKQLT WLVNRLPGLK DLILAGCSWS
AVCALSTSSC PLLRTLDLRW AVGIKDPQIR DLLTPPTDKP SQDNRSKLRN MIDFRLAGLD
ITDATLRLII RHMPLLSRLD LSHCNHLTDQ SANLLTAVGS STRNSLTELN MAGCNKLTDQ
ALLYLRRISN VTLIDLRGCK QITRKACEHF ISDLSINSLY CLSDEKLIQK IS
//
