ID A0A2B7ZFW6_9EURO Unreviewed; 1488 AA.
AC A0A2B7ZFW6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Exocyst complex component Sec3 PIP2-binding N-terminal domain-containing protein {ECO:0000259|SMART:SM01313};
GN ORFNames=GX50_05183 {ECO:0000313|EMBL:PGH32058.1};
OS Emmonsia crescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=73230 {ECO:0000313|EMBL:PGH32058.1, ECO:0000313|Proteomes:UP000226031};
RN [1] {ECO:0000313|EMBL:PGH32058.1, ECO:0000313|Proteomes:UP000226031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH4076 {ECO:0000313|EMBL:PGH32058.1,
RC ECO:0000313|Proteomes:UP000226031};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:PGH32058.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PDND01000106; PGH32058.1; -; Genomic_DNA.
DR STRING; 73230.A0A2B7ZFW6; -.
DR VEuPathDB; FungiDB:EMCG_02108; -.
DR OrthoDB; 1547052at2759; -.
DR Proteomes; UP000226031; 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:UP000226031};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 93..194
FT /note="Exocyst complex component Sec3 PIP2-binding N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01313"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..239
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..348
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..693
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1488 AA; 165865 MW; C5C3C596670E7550 CRC64;
MNGRDRPRGL PSNVSPLKER RPMADVRNGS GTNPAVGMSR AEKFEDEKRR LVQSCFGKQD
VDGSVLESYI THIRITEDAA YPSSPPPPNS PPENKKARLI IVSVRKSGRV RMHKARENND
GTFSIGKTWM LDDLSRIQIY EHMSASNPTE QQQKIWASNV GFVVTVSKPY YWQAATPKEK
DFFIGSLVKI YKKYTGGKVP ELLGFDPRDR DAIAGTVSGP QSAPPAGSRG PPPGRPDGSG
PQSRSPQNQS NIRQPPYVTN RLPSRDGARE PRMQSSREQF LRTPPGQDEG QRPRPQFTPS
KSSQQQGFRS ELSSKPTESS TPNDSPTPIP FQAGPAPRTR PPGISPAPNP LSSSTGNQPR
TQFNNENGIR PARDPASDDN VRPIEYSKRP TPEASAKLDS EAPNSKPVPL DSAQQSAPAT
LRRPPASTKG SSEEQSIKSE AEDRFVTPFT SPEPRNLDVR ALSRGSEKSA GALDPPRAQH
QVPMSLRPGS GDFNTNAKSD TRPVNEPEEA VRKPSPDEPE SPIVREIADI PSMLSSGVNP
ITPTESPGMA PTEEGEGEMH RPGLGPMVKK KPTEIAFTLR KAATAYGAFK PRAGGAADRL
LSTKEKNGDE PDGITGVIPA PLSRTMTDDS VKTTALTGTE PSTKDTQEIV PAKEVPKVQE
VPKVQVTEPA PQPQPSKEIP APIDSPPETV PSKVPPSQAE RRRQRREDNK AKYCTALAID
PSLLEGRGGY FDDILSDLGW DGKLSEDKRI EDLEADVRRE IGRVQASSWL GHLEQQEGKV
DQLAKLFDKT IAECDELDGL LMLYAHELNT LVDDVAYIEA QSQGLQVQTA NQKLLQNELQ
NLLKTISISS ADLRPLREAS LSSADGVEET ESSLAILYKA MVTIDPDIRI NKKRLADAAG
DRGGIGVYAD TEVGQMRAVK EKKGDYRDEA QLFLQRLKQF MGLAFKIAEQ KTMDSIASSK
SAKIVLGAHD TARQELWMYN ALMLFAREVS TDDWTAITTQ YEQQMKKSYQ NEFRDNTMAW
KREARKPTGD EQELLFTHQE KEREGEGITT AARKLTVRRG KTIRVAGTSR MPVADKSDGK
IEAYEVFGGS LEDTTKLIAE EQTFIVKFFH LTSLSSVEFQ DLISAARPED RRTPNLSGKE
SYDPDREMAK KVEQIMEEVF SSWVADMQNL AEWAIRADPL QGVGVLFTLE RKMSAFDETS
QEFIVRSLQK IHSRFMGLFN RFVDEQIRAI EETKVKVKKR KGVISFMKIF PNFSASIENM
ISLPSQETFD IRFCVNDAYE KINRAMWDSL KFIAKEAPGQ QPVASGGGQD PEDKEALNYH
ILLIENMNHY IEEVDCRDNI ILVEWKDRAT HDLHEHLRLY IDAVIRRPLG KLLDFIESTE
SLLQTAATPT DIALRTSHSR VLAKKLLTSY DAKELRRGID ALKKRIEKHF GDADDPGVSR
SLVVKVLKEC ETRYSDLHDR MRRIIDLVYE GQMELEWRKE EATAMFKR
//
