ID A0A0M4ERR7_DROBS Unreviewed; 941 AA.
AC A0A0M4ERR7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=BicC {ECO:0000313|EMBL:ALC39912.1};
GN ORFNames=Dbus_chr2Lg1997 {ECO:0000313|EMBL:ALC39912.1};
OS Drosophila busckii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC39912.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC39912.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC39912.1};
RA Zhou Q., Bachtrog D.;
RT "Ancestral chromatin configuration constrains chromatin evolution on
RT differentiating sex chromosomes in Drosophila.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the BicC family.
CC {ECO:0000256|ARBA:ARBA00007662}.
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DR EMBL; CP012523; ALC39912.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M4ERR7; -.
DR SMR; A0A0M4ERR7; -.
DR STRING; 30019.A0A0M4ERR7; -.
DR OMA; MIKVEAY; -.
DR Proteomes; UP000494163; Chromosome 2l sequence.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR CDD; cd22420; KH-I_BICC1_rpt1; 1.
DR CDD; cd22421; KH-I_BICC1_rpt2; 1.
DR CDD; cd22422; KH-I_BICC1_rpt3; 1.
DR Gene3D; 3.30.310.270; -; 2.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR047549; BICC1_KH-I_rpt1.
DR InterPro; IPR047554; BICC1_KH-I_rpt2.
DR InterPro; IPR047553; BICC1_KH-I_rpt3.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR10627:SF69; PROTEIN BICAUDAL C; 1.
DR PANTHER; PTHR10627; SCP160; 1.
DR Pfam; PF00013; KH_1; 2.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00322; KH; 2.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 2.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50084; KH_TYPE_1; 2.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000494163};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117}.
FT DOMAIN 842..905
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 500..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 721..750
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 941 AA; 103615 MW; E8E01E747AF96817 CRC64;
MLSCAPFNKL IYDVTAMASG KSSVVGSLDA LTVGSGAPSE THSEISSVDS DWSDIRAIAL
KLGVQNPDDL HTERFKVDRQ KLEQLIKADS SVEGMNGAEH FFQDIMNTTE TYVSWPCRLK
IGAKSKKDPH VRIVGKVDQV QRAKDRILSS LDSRGTRVIM KMDVSYTDHS YIIGRGGNNI
KRIMDDTHTH IHFPDSNRSN PTEKSNQVSL CGTLEGVEHA RALVRLSTPL LISFEMPVMG
PGKPQPDHET PYIKTIESKY NVQVIFSTRP KLHTSLVLVK GSEKESIKVR NATQLLINYA
YECIASQITV NVQMEITPQH HEIVKGKNNV NLLSIMERTQ TKIIFPDLTD MNVKPLKKSQ
VTITGRIDDV YRARQQLLGN LPVALIFDFP DNQNDASQIM GLNNKYGVYI TLRQKQRQST
LAIVIKGIEK FIDKIYEARQ EILRLATPAI RAEIPDYYYM PKDKDVNLAY RTQLTALLAG
YPDSPKTPSL MPPNMANHLA QFANNNNSNN NNSNSNNNNN NNNHLLPNAN PVSSMATPTG
ICVPTQKYLQ LHDSSYQPRQ LLNLPNNNNS NGNNNNYLLP GAILKPPPPP QQQQQHSVVP
VVAISAPLNT SPRNSCSQNT SGYQSFSSST TSLEQSYPPY AQLQAAVSST SSSSGSFANR
AHYSPDSTHS SETGSIVGNM RLGRRLSDGV LLGLGNGTGG THLLPGSAES YRHLHYDLAT
AAGKQQQQKQ QQQKKQQQQQ QQQQQQATQR AFNFDMKRAL GFKAMERTPV PGELRTPTPA
WLGMGLSRTS PAPIETGDDG ECASANGWRI PPPPPGISSP YGLSATTGLL DATPVNRRMQ
LSQHKDIQTL LTSLGLEHYI KIFVLNEIDL EMYTTLTEEN LMELGITAFG ARKKLLAAIH
TLLANEAACS SMPSSSSSQS SSPRFSGSAA PGAERRPSNQ W
//
