ID A0A0E9NGF1_SAICN Unreviewed; 1572 AA.
AC A0A0E9NGF1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Exocyst complex component Sec3 PIP2-binding N-terminal domain-containing protein {ECO:0000259|SMART:SM01313};
GN ORFNames=G7K_3042-t1 {ECO:0000313|EMBL:GAO48878.1};
OS Saitoella complicata (strain BCRC 22490 / CBS 7301 / JCM 7358 / NBRC 10748
OS / NRRL Y-17804).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Taphrinomycotina incertae sedis; Saitoella.
OX NCBI_TaxID=698492 {ECO:0000313|EMBL:GAO48878.1, ECO:0000313|Proteomes:UP000033140};
RN [1] {ECO:0000313|EMBL:GAO48878.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO48878.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=21914972; DOI=10.2323/jgam.57.243;
RA Nishida H., Hamamoto M., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic yeast Saitoella complicata.";
RL J. Gen. Appl. Microbiol. 57:243-246(2011).
RN [2] {ECO:0000313|EMBL:GAO48878.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO48878.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=24646756; DOI=10.2323/jgam.60.7;
RA Nishida H., Matsumoto T., Kondo S., Hamamoto M., Yoshikawa H.;
RT "The early diverging ascomycetous budding yeast Saitoella complicata has
RT three histone deacetylases belonging to the Clr6, Hos2, and Rpd3
RT lineages.";
RL J. Gen. Appl. Microbiol. 60:7-12(2014).
CC -!- SIMILARITY: Belongs to the SEC3 family.
CC {ECO:0000256|ARBA:ARBA00006518}.
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:GAO48878.1}.
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DR EMBL; BACD03000018; GAO48878.1; -; Genomic_DNA.
DR STRING; 698492.A0A0E9NGF1; -.
DR OMA; SFMRVFP; -.
DR Proteomes; UP000033140; 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:UP000033140};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 57..147
FT /note="Exocyst complex component Sec3 PIP2-binding N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01313"
FT REGION 160..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1489..1572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..416
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1540..1562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1572 AA; 174704 MW; AB6A75B80492FAB9 CRC64;
MSVASRSGDE AKERIKRSLF AARSEDGEAL ESYILHVKIT EDVYYPSTPA PPGSDPANRK
VRYIVVAVRR SGRVLMHKAR ENSNGTFSVG KTWNLDELKK IEDGPGPQAE MGPAFTITMQ
KPYYWVADSR REKMNFVHGL VKVFRKYTGG KSPDMVGFND DVGVSSATRQ PKQQTLPTSA
LPPQSQQAPV RTQATAPLQP TQPLQSSRPP RPQVQIPVTS SRFYEEPAQL SATSATSVQP
PPMSAKSELR AQFSPQPQQQ DFSRAPQSPS ASTIASVATS ITRPYEVPPP RQQPPRQELG
YVDSASTTSA TSSILTPLGY VDSARTPSSQ AAPARTPTSP NAPGPTTVRE VNTTHPDYFN
TRPLQPHAET QPLRPPAQSP EGRLQRLAQQ PMMTPPVEVA TPPAEQPEPP ARQPPATAAP
GRMLSETIRK ISDHQARPPI DTAELAPAAR PEAPWQLSAR ELRGFGPPTT APLQAMKPMI
DAAEPARETI PVVTQNDLPR QQSVPNIEED RARPQVAPRA QTVYRDYAEA DGQFGAYQLP
QSAAQPQQQH RPMTDVVDRD MGESPGASSS RLAGATGTPQ LPVTPRKLDD VREEEPEPEK
LASPIVMPSP VKPLQSDNTF MPPVLVAEQP PQEERPFTPP PRKSSPMRSR SPNKRRNRSS
VTSLASFQSR RRSYIQVSEN NATDGLNEVE KVLEDFDWTA LGNADRLEET LRDELAAIEA
ANNHAIVEGD ERMSDLLAKI DKSVLECENM DAMLTLYAFE LNTLADDIAY IESQSRGLQV
FTANQRALQS ELHNLLETIV IRPEQLESLQ SASLESPQGL ATVEKNLVPL YQALRTMSTQ
ADAVKAGMGG MGAVQERRQD YVAASEEFLR RLTQFMIMKF QAGVITYVRP KDKSSRQRKP
QLLSHDEAYT HLYRYAPLML YAKEINAQRF ADLQQHYVKP VKAAYSTDCA EFIDAYRTMT
RKATQDENEM TFTGAREAAM QSTVATMRSA TLKRSGTVAR NLRAPIEEAL GREKDRDQEG
KVYAHEVIAS MFDEIMPILI QEQNFLVKLF HLSSVSSDSY ADYVEHQAGR ELNLKDLNQL
KSKDTDRTIA RVLSDVMDQA FGFLRDDMRT FAEWCTNLDK IQCVGILKVL QLHLSRVMDT
DHEFAIVFLM KLCERIEGIL ARFIQEQIRA IEETKVKGTK RKGVVLFFKV FPDFANRIET
QLQGEGVHNL DIRLTVNDNY EKINKAMFES LKRIARELPT ATGGPVDPED KEQLNYAVTM
VENMHHYVQA VDTRGIDILE DYKFNAQSSY KENLSLYIRS VTRRPLGILL NFVEGAESLI
QANPAEDISA RVAYSKSAIR KLLATYDAKE IRKGVDALYK RVDKHFGEDE EGSTQLFTLV
WKAIQDEYFR ITDRTTTLVA RYRDPALQMG WGKASLRQAP RSRHERHKAG YLHRPPNLPH
TTHQLKTMTD LKQFAAEQAD AANAKGNYQA PKEMKANQKG TIIADESNVD ESGVANVPGA
DPADVKVGRS GLGAGGGDNQ KIPVEEGGGS WGPGAGRDVT ADDFEGHRGP EDKARAHAAM
HGGDNDVRSN LR
//
