ID A0A0A2VQ43_BEABA Unreviewed; 301 AA.
AC A0A0A2VQ43;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 03-MAY-2023, entry version 28.
DE SubName: Full=High osmolarity signaling protein SHO1 {ECO:0000313|EMBL:KGQ08482.1};
GN ORFNames=BBAD15_g6196 {ECO:0000313|EMBL:KGQ08482.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ08482.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ08482.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ08482.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Forms homooligomers. {ECO:0000256|ARBA:ARBA00011175}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the SHO1 family.
CC {ECO:0000256|ARBA:ARBA00009739}.
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:KGQ08482.1}.
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DR EMBL; ANFO01000575; KGQ08482.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VQ43; -.
DR STRING; 1245745.A0A0A2VQ43; -.
DR EnsemblFungi; BB8028_0006g07040.1; BB8028_0006g07040.1; BB8028_0006g07040.
DR eggNOG; ENOG502QW7A; Eukaryota.
DR HOGENOM; CLU_043316_1_0_1; -.
DR Proteomes; UP000030106; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR CDD; cd11855; SH3_Sho1p; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035522; Sho1_SH3.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000030106};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Stress response {ECO:0000256|ARBA:ARBA00023016};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 242..301
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 154..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 301 AA; 32498 MW; A2131666228CBE1A CRC64;
MEHSRHYGRR GLKMGNIIGD PFALATLSVG MLAWFICFVA CVVAQIQGGQ SFPKFSWWAV
VYALFLNIGV FVVVASDAIQ TYHVALSSYL AAGLVLSSSS VNNLVYSNIG ARQAAGAGFI
LLSMLNIVWI FYFGSAPSST PRAFLDSFAL SKESTSPMPR QPMTGYGASG RPETSNSVQP
PQMYTSAQLS GFENSTPLGN TMTGARASNF GTSSPQQALQ QPGPTPQVSK PAHDIEVVPP
TEYPYKAKAI YSYEANPDDA NEISFSKHEI LEVSDVSGRW WQARKESGET GIAPSNYLIL
L
//