ID A0A093IBP0_EURHL Unreviewed; 2029 AA.
AC A0A093IBP0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Zinc finger homeobox protein 3 {ECO:0000313|EMBL:KFV96981.1};
DE Flags: Fragment;
GN ORFNames=N326_00763 {ECO:0000313|EMBL:KFV96981.1};
OS Eurypyga helias (Sunbittern) (Ardea helias).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Eurypygimorphae; Eurypygiformes;
OC Eurypygidae; Eurypyga.
OX NCBI_TaxID=54383 {ECO:0000313|EMBL:KFV96981.1, ECO:0000313|Proteomes:UP000054232};
RN [1] {ECO:0000313|EMBL:KFV96981.1, ECO:0000313|Proteomes:UP000054232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N326 {ECO:0000313|EMBL:KFV96981.1};
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,
CC ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
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DR EMBL; KK554068; KFV96981.1; -; Genomic_DNA.
DR Proteomes; UP000054232; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00086; homeodomain; 4.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
DR Gene3D; 1.10.10.60; Homeodomain-like; 4.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR45891; ZINC FINGER HOMEOBOX PROTEIN; 1.
DR PANTHER; PTHR45891:SF4; ZINC FINGER HOMEOBOX PROTEIN 3; 1.
DR Pfam; PF00046; Homeodomain; 4.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00389; HOX; 4.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SMART; SM00451; ZnF_U1; 3.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 5.
DR SUPFAM; SSF46689; Homeodomain-like; 4.
DR PROSITE; PS00027; HOMEOBOX_1; 2.
DR PROSITE; PS50071; HOMEOBOX_2; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00108};
KW Homeobox {ECO:0000256|ARBA:ARBA00023155, ECO:0000256|PROSITE-
KW ProRule:PRU00108}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00108}; Reference proteome {ECO:0000313|Proteomes:UP000054232};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 219..249
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 260..282
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 404..435
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 455..484
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 840..868
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1000..1060
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DOMAIN 1097..1157
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DOMAIN 1185..1214
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1387..1409
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1496..1556
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DOMAIN 1568..1598
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1801..1861
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DNA_BIND 1002..1061
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT DNA_BIND 1099..1158
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT DNA_BIND 1498..1557
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT DNA_BIND 1803..1862
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1233..1254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1268..1364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1476..1504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1628..1653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1698..1730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1769..1805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1994..2029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 578..610
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 16..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..933
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1336..1351
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1698..1729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1769..1791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV96981.1"
FT NON_TER 2029
FT /evidence="ECO:0000313|EMBL:KFV96981.1"
SQ SEQUENCE 2029 AA; 224957 MW; 336973494426ACD2 CRC64;
SEESIEDVEG PNETAGDAEE PAKEQESGGD KDQSKWTASQ AEKELTEPPA SSKRVSFPSS
SESPLSFKWS KTSEETKSEQ MYQCPYCKYS NTDVNRLRVH AMTQHSVQPM LRCPLCQDML
NNKIHLQLHL THLHSVSPDC VEKLIMTVTT PEVMMPSSMF LPAAAPEKDG NSTTEELGKQ
PEISEDSGKG LLPSESAEHS GDPKPVPADQ SSAREDSGFL CWKKGCNQVF KSSAALQTHF
NEVHAKRPQL PVSDRHVYKY RCNQCSLAFK TIEKLQLHSQ YHVIRAATMC CLCQRSFRTF
QALKKHLETS HLELSEADIQ QLYGGLLVNG DLLAMGDPSL AEDHTIIVEE DKEEESDLED
KQSPTGSDSG SVQEDSGSEP KRALPFRKGP NFTMEKFLDP SRPYKCTVCK ESFTQKNILL
VHYNSVSHLH KLKRALQESA TGQPEPTSSP DNKPFKCNTC NVAYSQSSTL EIHMRSVLHQ
TKARAAKLEA AGGSGSSNGA GNSSNSSLSL GSSTPSPVSA SNSNTFTTAN TSNSGTTPIP
SLLNQVSSDS VGIPPLGNPV STNISSPSEP KEVNRKKLAD MIASRQQQQQ QQQQQQQQQQ
AQTLAQAQAQ VQAHLQQELQ QQAALLQSQL FNPALLPHFP MTTETLLQLQ QQQHLLFPFY
IPSAEFQLNP EVSLPVTSGA LTLTGTGPSL LEDLKAQVQL PQQSHPQLLQ QQQGQLSLSQ
PHSVLIQQSQ QHPEKKNKSV VKEKEKETPR ESAERGDNNV ASKESLPDNL KPKEKKDFVP
GSTSEPSLLP PRIASDARGN ATKALLENFG FELVIQYNEN KQKVQKKNGK TEQGENLEKL
ECDTCGKFFS NILILKSHQE HVHQHYFPFK QLERFAKQYR EHYDKLYPLR PQTPEPPPPP
PPPPPPLPPA PPQPASTPTI PTSAPPITSP TIAPAQPSVP LTQLSMPMEL PIFSPLMMQT
MPLQTLPAQL PPQLGPVDPL PADLAQLYQH QLNPSLLQQQ QNKRPRTRIT DDQLRVLRQY
FDINNSPSEE QIKEMADKSG LPQKVIKHWF RNTLFKERQR NKDSPYNFSN PPITSLEELK
IDSRPPSPEP QKQEYWGSKR SSRTRFTDYQ LRVLQDFFDA NAYPKDDEFE QLSNLLNLPT
RVIVVWFQNA RQKARKNYEN QGEGKDGERR ELTNDRYIRT SNLNYQCKKC SLVFQRIFDL
IKHQKKLCYK DEDEDGQDDS QNEDSMDAME LLTPTSSSCS TPMPSQAYST PTSSANATSS
AFLQLTAEAD DSSTYSSKVE ATDEKPKQSE PPSTQQNQTQ DKQVQPKQES QQQQDQGEQK
TSSAHQKISQ LSSPSSLQQP PPPPQPPQCS LSQSSPSPSQ LSHLSLKPIH TSTPQQLANL
PPQLIPYQCD QCKLAFPSFE HWQEHQQLHF LSAQNQFIHP PFLDRTLDMP FMLFDPSNPL
LASQLLSGTL PQIPASSATS PSTPTSTMNT LKRKLEEKAS ASPGENDSGT GGEEPQRDKR
LRTTITPEQL EILYQKYLLD SNPTRKMLDH IAHEVGLKKR VVQVWFQNTR ARERKGQFRA
VGPAQAHRRC PFCRALFKAK TALEAHIRSR HWHEAKRAGY NLTLSAMLLD CDGGLQMKGD
IFDGASFSHM PPTSSDGQSV PLSPVNKSME LSPRTLLSPS SIKVEGIEDF ESPSMSSVNL
SFDQTKLDND DCSSVNTAIT DTTTGDEGNA DNDSATGIAT ETKSASGPSE GLTKAAMIAM
SEYEDRLSSG LVSPAPSFYS KEYDNEGTVD YSETSSLADP CSPSPGARGS ASKSGESGDR
PGQKRFRTQM TNLQLKVLKS CFNDYRTPTM LECEVLGNDI GLPKRVVQVW FQNARAKEKK
SKLSMAKHFG INQTSYEGPK TECTLCGIKY SARLSVRDHI FSQQHISKVK ETIGSQLDKE
KEYFDPATVR QLMAQQELDR IKKANEVLGL AAQQQGMFDN TPLQALNLPA AYPALQGIPP
VLLPGLNSPS LPGFTPSNTA LTSPKPNLMG LPSTSVPSPG LPTSGLPNK
//
