ID A0A091NFB0_APAVI Unreviewed; 928 AA.
AC A0A091NFB0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Lysine-specific demethylase 4A {ECO:0000313|EMBL:KFP88438.1};
DE Flags: Fragment;
GN ORFNames=N311_12216 {ECO:0000313|EMBL:KFP88438.1};
OS Apaloderma vittatum (Bar-tailed trogon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Trogoniformes; Trogonidae; Apaloderma.
OX NCBI_TaxID=57397 {ECO:0000313|EMBL:KFP88438.1, ECO:0000313|Proteomes:UP000054244};
RN [1] {ECO:0000313|EMBL:KFP88438.1, ECO:0000313|Proteomes:UP000054244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N311 {ECO:0000313|EMBL:KFP88438.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KL382735; KFP88438.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091NFB0; -.
DR Proteomes; UP000054244; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd15713; ePHD_JMJD2A; 1.
DR CDD; cd20463; Tudor_JMJD2A_rpt1; 1.
DR CDD; cd20466; Tudor_JMJD2A_rpt2; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 3.10.330.70; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR047482; JMJD2A_ePHD.
DR InterPro; IPR040477; KDM4-like_Tudor.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR047479; Tudor_KDM4A_rpt1.
DR InterPro; IPR047481; Tudor_KDM4A_rpt2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF119; LYSINE-SPECIFIC DEMETHYLASE 4A; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF18104; Tudor_2; 2.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00333; TUDOR; 2.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51184; JMJC; 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 Methyltransferase {ECO:0000313|EMBL:KFP88438.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054244};
KW Transferase {ECO:0000313|EMBL:KFP88438.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 74..240
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 684..797
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 340..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP88438.1"
FT NON_TER 928
FT /evidence="ECO:0000313|EMBL:KFP88438.1"
SQ SEQUENCE 928 AA; 104419 MW; 2238E01DFE3453F9 CRC64;
APIQQVVTGQ SGLFTQYNIQ KKAMTVREFR RIANSDKYCT PRYTDFEDLE RKYWKNLTFN
APIYGADVNG TLYDKHVDAW NIGRLNTILD VVENESGITI EGVNTPYLYF GMWKTSFAWH
TEDMDLYSIN YLHFGEPKSW YSVPPEHGKR LERLAKGFFP GSAQSCEAFL RHKMTLISPS
ILKKYGIPFD KVTQEAGEFM ITFPYSYHAG FNHGFNCAES TNFATLRWIE YGKQSVLCSC
RKDMVKISMD VFVRKYQPDR YKLWKAGKDV TVIDHALPTP EAAEFLKGDL MQKVKNGKQC
AEEMETGEIC REEADRDETK SIPKHRIGTK RHRVCLEVPQ EVSESEAFPK EELGSAQYEA
DTAEPRERPT SELVQQGEQR LKLPVKLEEE EEEEQEAAAL DLSISHASNS SSALPASKQS
AASSVQSSSP TYSGSSDSES TDPLAKRTLP GPAGVLTVHS YARGDASGSD NEQTSGKKAS
ATASVNEQEL AEVAKEYLRS MKESKKSKGR RQPLSKLPRH HPLLVKDCIS DDEASEQLTP
EEEAEETEAW AKPLSQLWQN RPPNFEAEKE YNRTMAQQSP YCAVCMLFQT YQVRRPSLQN
AGVTSAGVDG KIRTKPLIPE MCFTTTGCST DLNLSTPYLE EDGTSILITC KNCHVCVHAS
CYGVSPDKAT EDWMCSRCAE NALEEDCCLC SLRGGALQRA NDDKWVHVMC AVAVLEAKFV
NIAERSPVDV GKIPLQRFRL KCIFCKKRRK RIAGCCVQCS HGRCPTSFHV SCAQAAGVMM
QPDDWPFVVF ITCFRHKIPS QAEAALQDLS PGQIVISKHK NGRFYQCEVV SLAKETFYEV
NFDDGSFSDN LYPEDIVSRD CLQLGPPDEG EVVQVRWTDG QVYGAKFVAS HVIQMYQVEF
EDGSQLMVKR DDVYTLDEEL PKRVKSRL
//
