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Database: UniProt
Entry: A0A150VC87_9PEZI
LinkDB: A0A150VC87_9PEZI
Original site: A0A150VC87_9PEZI 
ID   A0A150VC87_9PEZI        Unreviewed;       261 AA.
AC   A0A150VC87;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=BAR domain-containing protein {ECO:0000259|PROSITE:PS51021};
GN   ORFNames=M433DRAFT_84464 {ECO:0000313|EMBL:KYG48095.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG48095.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG48095.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG48095.1,
RC   ECO:0000313|Proteomes:UP000075602};
RX   PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA   Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA   Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA   Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT   "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT   Carbon Cycling in Acid Mine Drainage.";
RL   Front. Microbiol. 7:238-238(2016).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
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:KYG48095.1}.
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DR   EMBL; JPDO01000057; KYG48095.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150VC87; -.
DR   STRING; 766039.A0A150VC87; -.
DR   Proteomes; UP000075602; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0051666; P:actin cortical patch localization; IEA:InterPro.
DR   GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:InterPro.
DR   CDD; cd07591; BAR_Rvs161p; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR004148; BAR_dom.
DR   InterPro; IPR046982; BIN3/RVS161-like.
DR   InterPro; IPR037429; Rvs161/Hob3_BAR.
DR   PANTHER; PTHR47174; BRIDGING INTEGRATOR 3; 1.
DR   PANTHER; PTHR47174:SF3; BRIDGING INTEGRATOR 3; 1.
DR   Pfam; PF03114; BAR; 1.
DR   PRINTS; PR01251; AMPHIPHYSIN.
DR   SMART; SM00721; BAR; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   PROSITE; PS51021; BAR; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075602}.
FT   DOMAIN          17..237
FT                   /note="BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51021"
FT   COILED          163..194
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   261 AA;  29861 MW;  DAF32BC56BF65272 CRC64;
     MSWSGFKKAT SRAGTQLMMK TGHVEKTTDR EYEVEERRYR TLEAASLRLQ KEAKGYLDSL
     RAMTASQMRI AETIDAFYGE SGARDGVSRS YKQAVEDLDA ETVKALDGPY RQTVLEPINR
     FCAYFPDINE CIKKRNHKML DYDAMRSKVK KLVEKPDKDP GKLPRTEKEC EMAKAAYEQL
     NEQLTNELPQ LIDLRVPYLD PTFEALVKIQ LRFCAEAYSR MAQVQQYLDA STRDQYANGD
     LDARVEDVLG QIRELSIAGT V
//
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