ID G0SXF2_RHOT2 Unreviewed; 1176 AA.
AC G0SXF2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Exocyst complex component EXO84 {ECO:0000256|ARBA:ARBA00021269};
GN ORFNames=RTG_01293 {ECO:0000313|EMBL:EGU12727.1};
OS Rhodosporidium toruloides (strain ATCC 204091 / IIP 30 / MTCC 1151) (Yeast)
OS (Rhodotorula glutinis (strain ATCC 204091)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1001064 {ECO:0000313|EMBL:EGU12727.1, ECO:0000313|Proteomes:UP000006141};
RN [1] {ECO:0000313|EMBL:EGU12727.1, ECO:0000313|Proteomes:UP000006141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204091 / IIP 30 / MTCC 1151
RC {ECO:0000313|Proteomes:UP000006141};
RX PubMed=24526636; DOI=10.1128/genomeA.00046-14;
RA Paul D., Magbanua Z., Arick M.II., French T., Bridges S.M., Burgess S.C.,
RA Lawrence M.L.;
RT "Genome sequence of the oleaginous yeast Rhodotorula glutinis ATCC
RT 204091.";
RL Genome Announc. 2:E0004614-E0004614(2014).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000256|ARBA:ARBA00004398}. Vesicle
CC {ECO:0000256|ARBA:ARBA00004373}.
CC -!- SIMILARITY: Belongs to the EXO84 family.
CC {ECO:0000256|ARBA:ARBA00007210}.
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:EGU12727.1}.
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DR EMBL; AEVR02000003; EGU12727.1; -; Genomic_DNA.
DR AlphaFoldDB; G0SXF2; -.
DR HOGENOM; CLU_273539_0_0_1; -.
DR InParanoid; G0SXF2; -.
DR Proteomes; UP000006141; Unassembled WGS sequence.
DR GO; GO:0000145; C:exocyst; IEA:InterPro.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.1220; Exo84p, C-terminal helical domain; 1.
DR Gene3D; 1.20.58.1210; Exo84p, N-terminal helical domain; 1.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR033961; Exo84.
DR InterPro; IPR032403; Exo84_C.
DR InterPro; IPR042561; Exo84_C_1.
DR InterPro; IPR042560; Exo84_C_2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR21426; EXOCYST COMPLEX COMPONENT 8; 1.
DR PANTHER; PTHR21426:SF12; EXOCYST COMPLEX COMPONENT 8; 1.
DR Pfam; PF16528; Exo84_C; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR Pfam; PF08700; VPS51_Exo84_N; 1.
DR SUPFAM; SSF74788; Cullin repeat-like; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000006141};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 38..180
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 190..357
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 871..1071
FT /note="Exocyst component Exo84 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16528"
FT REGION 1083..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 587..646
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1083..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1176 AA; 125611 MW; 439473235614C3FE CRC64;
MVLIQQALRT QSARKAAPAL ARGLATPAFT TQNAGGVKVA SSEDGSRTSS ISVVVKSGAR
YEPAPGVAHV LKNSVFKATN KRSQIRLVRE TEALGGVLST SLSREHLVLT AEFLKGDEAY
FAEALGDAVT QPKFPVYEYN EEVVPQVQAE YEQAIHDSRV YAFDLAHQLA FRKGLGNSLF
ASPHTAVDHS TLVSFAQASF APSNIAVFGQ NVDAGKLASL VSDFFASGSS SSSISTPQSQ
YYGGEVRIPA VGHSSTDELL IAFKGAARTE VDYAVLAVLL GGQASVKWGA GASPLAKLAT
STSSAKAFNL GYSDAGLFGI SVSAKTNDVA DVATKALSEL KNVAKGVSDE LVKQAVAKAK
FAAAAALETR EGKTLVLGEQ LASGGEAPAI DDIFAKLDKV TGESLAKAAK NALASKPTTV
AVGNTHALPC VRFNEPRPET GRPRAQSNVG AKLLKKRQSV AYSAHPAYEA GSVPAVPSLP
KLGPVAGSVE RVSTPTGTGG GASVLPGLAP FAARAPSPAT QIGAPVAKER QEQPQAQAQP
LSARNEAENQ LLATGLDVDQ LASEGFKPED FLKQNLPGGR SDAPAQMDDL RRLKGRLEGA
MKIAETELQK SVFNNYADFV LISKEIATLE NEMIELKGVL EEWRAVPELL EGGSGDDDLL
MGGAAGRRAQ RNSIADLATL YKSQLSALWE NVEGSQKFLP YTPGRHIITE APSFVELNPA
TYKPKQPVHL VLLNDAMLVS VKKRRGPGIG GPVRLVAERC FNLSEIVVVD LKDGGDLQNA
VKIKRGKETI IFRTDKPEEK KMLLLAFKKV AEELMNKKRK EMLNEAEARK GDPSSLRGYR
DYDGSFSSSN FNPAAALGLV SGDVPSRDLS WIGDFSDELA VDVSTREFED AVVLIEKGKS
ILPKISGDAH ASQLFRSKLD SRTSELVSAL LNDLSDHSIR KSGVVRTTSW LLRLGQGERA
RETFLSARGA LVRKRARQIK FEGDISMYIS ELAMVCFTLI KNTCEWYMAA FKDNSMASGF
VRWASEQVEI YAETFRRQVY GADQNGKVIE ESLEVTKAHG AMLRDVGLDF TFLLDGLLRP
QRPTTNTARS SSSSTRLRDD ALSGSHLRPP KSTASLAPTS AVAMARQSIF LQQGQAGVGN
GVARPREVLK AEGEEGRGRP ASGAGFARDD AVGQAQ
//