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Database: UniProt
Entry: A0A1B8AGC3_FUSPO
LinkDB: A0A1B8AGC3_FUSPO
Original site: A0A1B8AGC3_FUSPO 
ID   A0A1B8AGC3_FUSPO        Unreviewed;      1178 AA.
AC   A0A1B8AGC3;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=VASt domain-containing protein {ECO:0000259|PROSITE:PS51778};
GN   ORFNames=FPOA_11181 {ECO:0000313|EMBL:OBS19456.1};
OS   Fusarium poae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=36050 {ECO:0000313|EMBL:OBS19456.1, ECO:0000313|Proteomes:UP000091967};
RN   [1] {ECO:0000313|EMBL:OBS19456.1, ECO:0000313|Proteomes:UP000091967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2516 {ECO:0000313|EMBL:OBS19456.1,
RC   ECO:0000313|Proteomes:UP000091967};
RA   Vanheule A., Audenaert K., Warris S., Van De Geest H., Schijlen E.,
RA   Hofte M., De Saeger S., Haesaert G., Waalwijk C., Van Der Lee T.;
RT   "Living apart together: crosstalk between the core and supernumerary
RT   genomes in a fungal plant pathogen.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the YSP2 family.
CC       {ECO:0000256|ARBA:ARBA00006582}.
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:OBS19456.1}.
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DR   EMBL; LYXU01000004; OBS19456.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B8AGC3; -.
DR   STRING; 36050.A0A1B8AGC3; -.
DR   OMA; PSGNMIS; -.
DR   OrthoDB; 45896at2759; -.
DR   Proteomes; UP000091967; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043226; C:organelle; IEA:UniProt.
DR   CDD; cd13220; PH-GRAM_GRAMDC; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR004182; GRAM.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR031968; VASt.
DR   PANTHER; PTHR23319:SF4; AT22714P-RELATED; 1.
DR   PANTHER; PTHR23319; UNCHARACTERIZED; 1.
DR   Pfam; PF02893; GRAM; 1.
DR   Pfam; PF16016; VASt; 1.
DR   SMART; SM00568; GRAM; 1.
DR   PROSITE; PS51778; VAST; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000091967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1044..1062
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          804..975
FT                   /note="VASt"
FT                   /evidence="ECO:0000259|PROSITE:PS51778"
FT   REGION          1..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          376..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          462..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          687..732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          746..798
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          972..1010
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1158..1178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..77
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..144
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..270
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..354
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..394
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..422
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..520
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        695..709
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        711..732
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1178 AA;  126984 MW;  3EBDF1899FAEFBD7 CRC64;
     MTTTLDNSSN SGLNKLLPKS ISSKRLRRKQ DREAAGLSLD DSSVFAHSQS SRETLESDGT
     RSGHIGGDED EGTSQGHRSY ESDGNDSSNS RHPPPFSTHP SQIGHLTTNS AVIQTNYLPE
     SQLSASDHDS NSSTSKSSTF PPTALDSVDF KDPRIGRSKT GLLPPQSSTR RSPSPGGRLK
     DIFKPKKSSG NSSSPERRPV SEPLETHDEQ HPIISVDPEF TQRFPVLEPP AAAKVASPER
     RARVQPKVDT NIPPRTPPSG DKPAPVIVNT PPTPTEFANR SGQSSPERKS FWGSPTSSSG
     ANGRPSSQSM SANRRSRSNS QNIGPSKLSH IVSAPLTPTP ESGEATPNAN SNPSGGFFSS
     MISAAQNAAN TLSNTSLNIG GNKGRSVSQN IQEQSEPDDA KDDAEPTPTT AEMADKKESN
     RKSAVSTIGA GELSLSQLGL AEAPSLVASP VNARFPDVDT RARSESAPVD SPISPVDFAP
     DESSSRPRSL YEPVSRERTP PPSDYTNKEN GVQRTSSIRS ALRQNHRKRG SSVTTGTTIG
     AAIAAANNSL AHPNLSAPKL TGFAIASKKR NRDFHDLFKS VPDDDYLIED YSCALQREIL
     AHGRLYVSEG HLCFSSNIFG WTTTLVMSFD EIVSVEKRST ALLFKNGLMI STLHAKHIFA
     SFTSRDATYD LIVNIWKLGH PTLKSTLNGV RLEGTGGDKT EKVDAEPAAE DEVQGGSETD
     DDSDEEEEYY DEDVHEEMHN ASVAAEANGA DADVEKTASR KASGAALPSG PVPEEASAGS
     GGATDFPGPA THAPTDCGDS ASHYDRIVGD DIIPAPLGKV YNLMFGPASV TFMSNWLSGE
     QKCLDLQMED KKGLTLDNRT RTFSYIKPLY GSIGPKQTKT ITSETIETLD LEKSVNLTCS
     TQTPDVPSGN VFAVKTRYCL SWAENNATRV QMNCTIEWSG KSWLKGPIEK GATDGQTTYG
     KDLFAAIKAA VSSKPQGTTP QGPGSKGGKK KGKKAKQSQS NTGVVETNAA PKRPVQADWG
     VLEPVRGILE PIGDIIQPLL TGNVMYGLLV GLLVATWFGF GFSPSRNASY GHELGGIYRP
     DRIAAYEEMW RREDSELWDW LEERVGMDRL HNDNAGVRKR AMEPKTVEEN LRATRMGERE
     VKEAIRVTEE KLRVLKGVME KKSKPNRSAT DEAGSQEL
//
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