ID   HUNB_DROOR              Reviewed;         767 AA.
AC   O62537;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Protein hunchback;
GN   Name=hb;
OS   Drosophila orena (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12572604; DOI=10.1093/oxfordjournals.molbev.a025868;
RA   Tautz D., Nigro L.;
RT   "Microevolutionary divergence pattern of the segmentation gene hunchback in
RT   Drosophila.";
RL   Mol. Biol. Evol. 15:1403-1411(1998).
CC   -!- FUNCTION: Gap class segmentation protein that controls development of
CC       head structures. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the hunchback C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AJ005375; CAA06505.1; -; Genomic_DNA.
DR   AlphaFoldDB; O62537; -.
DR   SMR; O62537; -.
DR   FlyBase; FBgn0024421; Dore\hb.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0040034; P:regulation of development, heterochronic; IEA:InterPro.
DR   GO; GO:0035282; P:segmentation; IEA:UniProtKB-KW.
DR   InterPro; IPR027742; Hunchback.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24392:SF33; PTHR24392:SF33; 1.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 6.
DR   SUPFAM; SSF57667; SSF57667; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   3: Inferred from homology;
KW   Developmental protein; DNA-binding; Gap protein; Metal-binding; Nucleus;
KW   Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..767
FT                   /note="Protein hunchback"
FT                   /id="PRO_0000046959"
FT   ZN_FING         242..264
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         271..293
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         299..321
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         327..351
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         714..736
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         742..766
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          30..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          105..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          174..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          357..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          518..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          610..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..424
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..570
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..629
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   767 AA;  84207 MW;  9C7710B7AFD78814 CRC64;
     MQNWETTATT NYEQHNAWYN SMFAANIKQE PGHHLDGNSV ASSPRQSPIP STNHLEQFLK
     QQQQQHQHQQ QPMDTLCAMT PSPSQNDQNS LQHYDANLQQ QLLQQQQYQQ HFQAAQQQHH
     HHHHLMGGFN PLTPPGLPNP MQHFYGGNLR PSPQPTPISA STVASVAVAT GSSEKLQALT
     PPMDVTPPKS PAKSSQSNIE PEKEHDQMSN SSEDMKYMVE SEDDDTNIRM PIYNSHGKMK
     NYKCKTCGVV AITKVDFWAH TRTHMKPDKI LQCPKCPFVT EFKHHLEYHI RKHKNQKPFQ
     CDKCSYTCVN KSMLNSHRKS HSSVYQYRCA DCDYATKYCH SFKLHLRKYG HKPGMVLDED
     GTPNPSLVID VYGTRRGPKS KNGGPIASGG SGSGSGSGSR KSNVAAVAPQ QQQTQPTQPP
     TSQLSAALQG FPLVQSNSAP PAASPLLPLP VSPAKSVASV EQTPSLPSPA NLLPPLASLL
     QQNHNMAFFP YWNLNLQMLA AQQQAAVLAQ LSPRMREQLQ QQNQQQSDNE EEEQDDEYER
     KSVDSAMDLS QGTPVKEEEQ QQLHQQQPQQ PLVMNLKVEE EATPLVSSSN ASRRKGRVLK
     LDTLLQLRSG VMTSPEQLKV PSTPMPTASS PIAGRKPMPE DHCSGTSSAD ESMETAHVRQ
     ANTSASSTAS SSGNSSNASS NSNGNSSSNS SSSGTNSAAA APPSGTPAAA GAIYECKYCD
     IFFKDAVLYT IHMGYHSCDD VFKCNMCGEK CDGPVGLFVH MARNAHS