ID A0A2S6CKM9_9PEZI Unreviewed; 573 AA.
AC A0A2S6CKM9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=BZIP domain-containing protein {ECO:0000259|PROSITE:PS50217};
GN ORFNames=CBER1_01268 {ECO:0000313|EMBL:PPJ60271.1};
OS Cercospora berteroae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ60271.1, ECO:0000313|Proteomes:UP000237631};
RN [1] {ECO:0000313|Proteomes:UP000237631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631};
RA de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A.,
RA Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT "Conservation of a gene cluster reveals novel cercosporin biosynthetic
RT mechanisms and extends production to the genus Colletotrichum.";
RL bioRxiv 0:0-0(2017).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PPJ60271.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PNEN01000293; PPJ60271.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6CKM9; -.
DR STRING; 357750.A0A2S6CKM9; -.
DR OrthoDB; 1330292at2759; -.
DR Proteomes; UP000237631; Unassembled WGS sequence.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR CDD; cd14686; bZIP; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 3.90.1200.10; -; 1.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR11012:SF30; PROTEIN KINASE-LIKE DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR11012; UNCHARACTERIZED; 1.
DR Pfam; PF01636; APH; 1.
DR Pfam; PF07716; bZIP_2; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000237631}.
FT DOMAIN 510..573
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 450..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 573 AA; 63373 MW; 84E5501C45A084F6 CRC64;
MSGPNDEIAT TANELLERLD LQLNKYDVRQ KLWQGYGYVC SVEGISDLGT SRSLILKYVR
PPPSRDAESE GHLRKVISYS VEQHFYTALA PLLPREIAIA QCHGSIHVEG KVALLLEDLR
NRFPVAGEKK ATLNEAQVHA AINWLARFHG FWLQNLAQAS KYRLRLPPLE DLRSRDAVGD
HREGGVWLNG GYTYLSTRRS EFEALSQNDS SEWSRALCVP RTNSGTCIAE QVARVLSPAT
VTSRSGLDQY QSLIHGDVKS ENLFTTVSGE AVAFFDFQYV GLGCGLSDLV KLFTCSVPED
SLHECNSADG LPNALTMGQG EKALLSSYRK TFEETSGKSY PWDLFVLHWQ VALIDWLRFQ
ASWGASDGVS WDAPQQAIDW SEDLYGLLDF NVNDISNFAL DTSLYGNAVD VPILPAIESM
QCASGHTTNG DAQYNQFGPG VEHDRAEPAA GLLNTGLPPD TQSSVTGIAS HSPATSSNSQ
TASSSPSSLL FDRRRTAPSS SFSDQSQSQP SYKVQKRKRN TEAARRYRQR KEDKVAQLKE
ALKAMTDERN ELSLKLARAE AETDVLRSMF KTS
//