ID A0A2G5I8S1_CERBT Unreviewed; 422 AA.
AC A0A2G5I8S1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 22-FEB-2023, entry version 14.
DE SubName: Full=Protein hob1 {ECO:0000313|EMBL:PIB01191.1};
GN ORFNames=CB0940_00106 {ECO:0000313|EMBL:PIB01191.1};
OS Cercospora beticola (Sugarbeet leaf spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=122368 {ECO:0000313|EMBL:PIB01191.1, ECO:0000313|Proteomes:UP000230605};
RN [1] {ECO:0000313|EMBL:PIB01191.1, ECO:0000313|Proteomes:UP000230605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=09-40 {ECO:0000313|EMBL:PIB01191.1,
RC ECO:0000313|Proteomes:UP000230605};
RA De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA Thomma B.P., Van De Peer Y., Bolton M.D.;
RT "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT several fungal lineages and shown to be expanded in Cercospora beticola
RT based on microsynteny with recipient genomes.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:PIB01191.1}.
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DR EMBL; LKMD01000100; PIB01191.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5I8S1; -.
DR OrthoDB; 2972088at2759; -.
DR Proteomes; UP000230605; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0051666; P:actin cortical patch localization; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:InterPro.
DR CDD; cd07599; BAR_Rvs167p; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR046982; BIN3/RVS161-like.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR47174; BRIDGING INTEGRATOR 3; 1.
DR PANTHER; PTHR47174:SF1; REDUCED VIABILITY UPON STARVATION PROTEIN 167; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 17..265
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT DOMAIN 362..422
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 300..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 422 AA; 47875 MW; B31CE3A9E1AED77A CRC64;
MSWKGFTKGA VRAPQMVKQK FNMGEITKDA IYIDAERRFA DLERETKKLH DESKKYFDAI
NGMLDHQIEF SKACAEIYQP ISGRASDPDS YVIDGNPEGI RACEEYEQIV QELKASLAPE
LEMIETRIVK PADELMEIIK VVRKACVKRD HKQIDHDRHN ATLKALQDKK DKSLKDEKAL
YKAENNVEMA TQEYEFFNNL IKEELPQLFR LEKEFILPLF QSFYYMQLNV FYTLHEKMQS
IDIGYFDLTK GIEESFEEKR GDIQQQVEAL SMVKFKTTGG LRKPAALKYG NRLAITNGKA
EPENRRLTID GGHAPPAYDE KPSSTDLVQR ASSTGSNWAS AAKAKGAPPP PKPKPGRLSA
APAVETVTAL YDYDAQAEGD LSFRTGEVIE IVSRTDNQNE WWTGKIGVRQ GQFPGNYVQL
NS
//
