ID A0A087VES7_BALRE Unreviewed; 1351 AA.
AC A0A087VES7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Lysine-specific demethylase 5B {ECO:0000313|EMBL:KFO11119.1};
DE Flags: Fragment;
GN ORFNames=N312_04675 {ECO:0000313|EMBL:KFO11119.1};
OS Balearica regulorum gibbericeps (East African grey crowned-crane).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Gruidae; Balearica.
OX NCBI_TaxID=100784 {ECO:0000313|EMBL:KFO11119.1, ECO:0000313|Proteomes:UP000053309};
RN [1] {ECO:0000313|EMBL:KFO11119.1, ECO:0000313|Proteomes:UP000053309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N312 {ECO:0000313|EMBL:KFO11119.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KL490583; KFO11119.1; -; Genomic_DNA.
DR Proteomes; UP000053309; 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: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; cd15603; PHD1_KDM5B; 1.
DR CDD; cd15607; PHD2_KDM5B; 1.
DR CDD; cd15687; PHD3_KDM5B; 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; IPR003347; JmjC_dom.
DR InterPro; IPR048615; KDM5_C-hel.
DR InterPro; IPR047978; KDM5B_PHD1.
DR InterPro; IPR047979; KDM5B_PHD3.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
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; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF3; LYSINE-SPECIFIC DEMETHYLASE 5B; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF21323; KDM5_C-hel; 1.
DR Pfam; PF00628; PHD; 3.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 3.
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:KFO11119.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053309};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:KFO11119.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 114..164
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 258..424
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 981..1029
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1291..1345
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO11119.1"
FT NON_TER 1351
FT /evidence="ECO:0000313|EMBL:KFO11119.1"
SQ SEQUENCE 1351 AA; 154194 MW; E1DFE95207C32112 CRC64;
CLQKPDLTSD TKDKEYKPHD IPQRQSVQPS ETCPPARRAK RLRAEATNIK TESDPPEART
HNLRRRMGCA PPKCENEKEM HSTVKLPEKR EHAGEPEKDK SKVRSKKPTN AVDLYVCLLC
GSGNDEDRLL LCDGCDDSYH TFCLIPPLHD VPKGDWRCPQ CLAQECNKPQ EAFGFEQAAR
DYTLRTFGEM ADAFKSDYFN MPVHMVPTEL VEKEFWRLVS TIEEDVTVEY GADIASKEFG
SGFPVRGGKF KVRPEEEEYL DSGWNLNNMP VMEQSVLAHI TADICGMKLP WLYVGMCFSS
FCWHIEDHWS YSINYLHWGE PKTWYGAPGY AAEQLEDVMK KLAPELFESQ PDLLHQLVTI
MNPNTLMAHG VPVYRTNQCA GEFVITFPRA YHSGFNQGFN FAEAVNFCTV DWLPLGRQCV
EHYRLLNRYC VFSHDEMICK MASKADVLDV VVASTVQKDM AIMIEDEKRL REKVDKLGVT
DSERVAFELF PDDERQCLKC KTTCFMSAVY CPCKPGLLVC LYHVEDLCSC PTYKYKLGYR
YTLEELYPMM NALKMRAESY NEWASNVNEA LEAKINNKKS LISFKALIEE SEMKKFPDND
LLRHLRLVTQ DADKCASVAQ QLLNGKRQTR YRSGGGKCQN QLTVNELRLF VRQLYALPCV
LSQTPLLKDL LDRVESFQQQ SQKLLSEEMP SAAELQELLD VSFDFDVDLP QLAELRTRLE
QARWLEDVQL ASSDQNSLTL DDMRRLIDSG VGLVPYPAVE KAMAKLQELL TVSEHWDDKA
RNLIKARPRQ SLSSLVAAVK EIEEIPAYLP NGVALKDTVQ KAKDWLQEVE ALQVGGRVPV
LDTLAELVTR GRSIPVHLEY LPRLESLVSE VQAWKECAAS TFLCENSPYS LLEVLCPRCD
IGMLTLKRKQ KKLKEPVPSG KKKSTKLETL SDLERALSES KDTASAMATL GEARLKEMEA
LRSLRAANEV KVLSSEEDTE LKVCLCQKEP AAPMIQCELC RGFFHTGCVS VPNVLQGPRV
WLCPHCHRSE KPPLEKILPL LASLQRIRVR LPEGDALRYM IERTVNWQHR AQQMLYSGNL
KLVQDKVGSG LLYSRWQATA GQLPETNKVS QTIGAMSFSM PHDWDNRTIY LHSPFSTGQH
CIPLHVISTE LDELMMEAQL LQVSLPEIQE LYQILFTKQS PVLQTEQRSF VGPTNEKASC
CRGKKDGISY TERKLKRRFE RESFCDEKRA RVKKVRTPKK KKLKLNHSKD LCTNKLERER
ERLFEMQRSS ESHLLPSDMS FSEQEDSEDE DAICPAVNCL QPEGDEVDWV QCDGSCNQWF
HQVCVGISPE MAEKEDYICI SCTGKDSQYR K
//
