ID A0A084QLJ4_STAC4 Unreviewed; 302 AA.
AC A0A084QLJ4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=SH3 domain-containing protein {ECO:0000259|PROSITE:PS50002};
GN ORFNames=S40285_01362 {ECO:0000313|EMBL:KFA64829.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA64829.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA64829.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA64829.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
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}.
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DR EMBL; KL660654; KFA64829.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084QLJ4; -.
DR STRING; 1283841.A0A084QLJ4; -.
DR HOGENOM; CLU_043316_1_0_1; -.
DR InParanoid; A0A084QLJ4; -.
DR OMA; NIIGDPF; -.
DR OrthoDB; 1365981at2759; -.
DR Proteomes; UP000028524; 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 PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR PANTHER; PTHR15735:SF20; PROTEIN NERVOUS WRECK; 1.
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:UP000028524};
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..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 243..302
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 214..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 302 AA; 32425 MW; D61DE4824642CEE0 CRC64;
MDHSRHYGRK GIQMGNILGD PFALASLSVA MLAWIIAFIS CIVGQVTEPP PSARDDFPTF
PWFSVTYSLV LLIGVFVVIA SDSIQTYHVA VTGYLSAGLV LVTSSVNSLI YSAHGSRQAG
AAGFILLSMV MVIWIFYFGS TPSSTPRAFV DSFALTKESS TMHRSTMNGY GTGRPETSNS
VQPPQMYTSA QLNGFENPSP VGGISQINGS RGSAITPVYT GGTGQPPKSA SPGADTEVVP
PTEYPYRAKA IYSYEANPDD ANEISFTKHE VLEVSDVSGR WWQARKETGE TGIAPSNYLI
LL
//
