ID A0A094KS80_ANTCR Unreviewed; 903 AA.
AC A0A094KS80;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Lysine-specific demethylase 4B {ECO:0000313|EMBL:KFZ61495.1};
DE Flags: Fragment;
GN ORFNames=N321_02578 {ECO:0000313|EMBL:KFZ61495.1};
OS Antrostomus carolinensis (Chuck-will's-widow) (Caprimulgus carolinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Caprimulgiformes;
OC Caprimulgidae; Antrostomus.
OX NCBI_TaxID=279965 {ECO:0000313|EMBL:KFZ61495.1, ECO:0000313|Proteomes:UP000053620};
RN [1] {ECO:0000313|EMBL:KFZ61495.1, ECO:0000313|Proteomes:UP000053620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N321 {ECO:0000313|EMBL:KFZ61495.1};
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; KL354958; KFZ61495.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094KS80; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000053620; 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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR CDD; cd15714; ePHD_JMJD2B; 1.
DR CDD; cd15576; PHD_JMJD2B; 1.
DR CDD; cd20464; Tudor_JMJD2B_rpt1; 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; IPR040477; KDM4-like_Tudor.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR047483; Tudor_KDM4B_rpt1.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694:SF7; [HISTONE H3]-TRIMETHYL-L-LYSINE(9) DEMETHYLASE; 1.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053620};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1..100
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 598..711
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 162..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..257
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..283
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFZ61495.1"
FT NON_TER 903
FT /evidence="ECO:0000313|EMBL:KFZ61495.1"
SQ SEQUENCE 903 AA; 101862 MW; FFB64130647161F5 CRC64;
YAIPPEHGKR LERLAKGFFP GSSQGCDAFL RHKMTLISPS ILKKYGIPFD RITQEAGEFM
ITFPYGYHAG FNHGFNCAES TNFATLRWID YGKMATQCTC RKDMVKISMD VFVRVLQPER
YDLWKQGKDI AVLDHMKPTA LTSPELEAWN ETKAELKTKL LRRIGDEEED NKHRSHRKRS
QPRRHKTEDQ KSLGDVMAIE TALEDVKVKE ELKRGPDLEE EERSKGIEGG EGECKVKARP
PKVKGERKKK HLFHQHQHHL QAPQPPLQQQ QPPLPPPPVP QQQLAEDQAP AARPPVPTAA
PTSSTAEKTL PPAPLNVVQP SETPVEEDDF KPRPIIPMLY VVPRTKKVVF DKERMSCQQA
FEQFATQKSP SWREQTVPVE IPVKEEENAE AENMEVAAET ASAFSKMKME IKKSRRHPLG
KPPTRSPLSV VKQETSSDEE TFPFSGEEDM SDPEALKSLL SLQWKNKAYN FPAERKFNAA
AALSEPYCAV CTLFYPYNQS LQVDKEAVPV SAGETTSFVH LSKCGQKTKP LIPEMCFTSS
GENTEPLPSN SYIGEDGTSP LISCAKCCLQ VHASCYGIRP DLVNESWSCS RCSANAWAAE
CCLCNLRGGA LQMTTDGRWV HIICAIAVPE ARFLNVIERH PVDISAIPEQ RWKLKCVYCR
KRMKKVSGAC IQCSYEHCST SFHVTCAHAA GVPMEPDDWP YVVSITCFKH KAANQNIQFR
REVTLGQTVI TKNRNGLYYR CKVIGMTTQT FYEVNFDDGS YSDNVYPESI ISRDCIQMGP
PPEGEVVQLQ WTDGIVYKAK FIAAQISQIY QVEFEDGSQL MVKRGDIYTL EEELPKRVKS
RLSLSTGAPQ EDVFSGDEVR AAKRPRLGNS RNPEEYGQNP DYLAFMESLL QTQYQPGTQS
NMF
//