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Database: UniProt
Entry: A0A164XAD8_9AGAM
LinkDB: A0A164XAD8_9AGAM
Original site: A0A164XAD8_9AGAM 
ID   A0A164XAD8_9AGAM        Unreviewed;      1150 AA.
AC   A0A164XAD8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Exocyst complex component Sec3 PIP2-binding N-terminal domain-containing protein {ECO:0000259|SMART:SM01313};
GN   ORFNames=SISNIDRAFT_451394 {ECO:0000313|EMBL:KZS95779.1};
OS   Sistotremastrum niveocremeum HHB9708.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX   NCBI_TaxID=1314777 {ECO:0000313|EMBL:KZS95779.1, ECO:0000313|Proteomes:UP000076722};
RN   [1] {ECO:0000313|EMBL:KZS95779.1, ECO:0000313|Proteomes:UP000076722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB9708 {ECO:0000313|EMBL:KZS95779.1,
RC   ECO:0000313|Proteomes:UP000076722};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the SEC3 family.
CC       {ECO:0000256|ARBA:ARBA00006518}.
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DR   EMBL; KV419400; KZS95779.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A164XAD8; -.
DR   STRING; 1314777.A0A164XAD8; -.
DR   OrthoDB; 1547052at2759; -.
DR   Proteomes; UP000076722; Unassembled WGS sequence.
DR   GO; GO:0000145; C:exocyst; IEA:InterPro.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   CDD; cd13315; PH_Sec3; 1.
DR   Gene3D; 2.30.29.90; -; 1.
DR   InterPro; IPR028258; Sec3-PIP2_bind.
DR   InterPro; IPR048628; Sec3_C.
DR   InterPro; IPR019160; Sec3_CC.
DR   PANTHER; PTHR16092:SF14; EXOCYST COMPLEX COMPONENT 1 ISOFORM X1; 1.
DR   PANTHER; PTHR16092; SEC3/SYNTAXIN-RELATED; 1.
DR   Pfam; PF15277; Sec3-PIP2_bind; 1.
DR   Pfam; PF20654; Sec3_C-term; 1.
DR   Pfam; PF09763; Sec3_CC; 1.
DR   SMART; SM01313; Sec3-PIP2_bind; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076722};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          42..126
FT                   /note="Exocyst complex component Sec3 PIP2-binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01313"
FT   REGION          143..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..187
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..209
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..250
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..313
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..361
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1150 AA;  127834 MW;  06C29BB220FCA7ED CRC64;
     MTELMDIRQR INASLFSREA SRGVPNGTYL SHVKIWEDDE QGGRKPRFIV LAQDGEGRGK
     IYKTKINTGG SFSIGKSWDL DGLRGVEVLS PAAFNITLNR TYRWDTENSK EQVHFVNTLI
     RTFRDLTRGA PLNVVGNIVE EPRLPAASPR SPAQNGSTIP GRGIGHSRTS SQASSTGTAM
     PSSPSTPSRR PLISPAPVPA QPSPRAPPTP STAQSSYRPT SPAEFGPIGA RMNMASPSPT
     PTSATGSPTL RARAANRPPP SSGLRNSESS STLPSVVTSA SSPRSAAPSS RFEDAYDTRS
     PQDTIRDEPQ GRPSLDVPRS GSPAPRNGRK SPRTRTPSPS ASGPSSQPSS VKRSSPLQTP
     RAQTRPPSPE YIPKPAEPIK KDANARVSFF DPANSASADR LLTRNESFPD NEFGFDGDGT
     AATLADVEDM LDGYEWTEMN YTRGRSAADQ IEAMLHDELM ALEKANIHSF IESDDRILHV
     LKYVDDALKD LDSMDQMVQS YKIHLNAVGD DISHIQSQNR GLQVQTQNQR ALLGELNRLL
     ETVDVDRNAL MALKMEKLDI PEGIARLESA AAELYKALQA SRDTDMAATM ERLQEYRTHN
     TQFCQRLFDF LKIMFSVQAD RVLNEKIGSK STISLAQSLT LARHEIMEAY LGQYSGLMLY
     LKDMDEERYG KVCAVYFSTI SELHSKQIKA MLMAYVSLIK KASDDEVSQN FSVATSSGIK
     PSAIRRAGTI VRSPLESRKD RDKDKVGDGE LRGYEALGKV LEQIAPQIYH EEEFIADFLQ
     INDAGLTFAD YANLENYYRR QAARAAGLSA TTSKLIRGAM DLIFGFLPNE LKQWIDGALR
     RDSIQIVGML ACIERFVIDA EERGNNFLLR VLEKQHTRLK SLYDRHVDEQ IKAVEDTKLT
     TKKRKGVAHF IKYFPIYVHR VEDQLIGSNS LEVRTSVDAA YEKIIHAMFE ALQQMAKMDG
     EGEDKGQLNF HVILIENMHF FLTESDVQEL VSMVPFNKRA ERTYEENLDA YIKLVLRRPF
     AKLFDYFEGV ERLLQTTAPS EVANSGSYNR SALKKVVKEF SSKDVKRHVD SLYKRIDKHF
     SETSSSTPGE EGGSIIPGST FVGVWKACEE ELLKNTSRFS SLISQCYPDS GVGLDYTSQD
     VEAAFKKHRV
//
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