ID   GYP5_ASHGO              Reviewed;         829 AA.
AC   Q755I4;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=GTPase-activating protein GYP5;
GN   Name=GYP5; OrderedLocusNames=AFL161C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 301; 329 AND 332.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: GTPase-activating protein which accelerates the GTP
CC       hydrolysis rate of several GTPases. Involved in ER to Golgi trafficking
CC       and polarized exocytosis (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GYP5 family. {ECO:0000305}.
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DR   EMBL; AE016819; AAS53213.2; -; Genomic_DNA.
DR   RefSeq; NP_985389.2; NM_210743.2.
DR   AlphaFoldDB; Q755I4; -.
DR   SMR; Q755I4; -.
DR   STRING; 33169.AAS53213; -.
DR   EnsemblFungi; AAS53213; AAS53213; AGOS_AFL161C.
DR   GeneID; 4621615; -.
DR   KEGG; ago:AGOS_AFL161C; -.
DR   eggNOG; KOG1102; Eukaryota.
DR   HOGENOM; CLU_005350_11_3_1; -.
DR   InParanoid; Q755I4; -.
DR   OMA; LFVHDAM; -.
DR   Proteomes; UP000000591; Chromosome VI.
DR   GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR   GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005798; C:Golgi-associated vesicle; IEA:EnsemblFungi.
DR   GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
DR   GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
DR   GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:EnsemblFungi.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR   InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR   Pfam; PF00566; RabGAP-TBC; 1.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; SSF47923; 2.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; ER-Golgi transport; Exocytosis; GTPase activation;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..829
FT                   /note="GTPase-activating protein GYP5"
FT                   /id="PRO_0000240364"
FT   DOMAIN          371..550
FT                   /note="Rab-GAP TBC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT   REGION          1..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          600..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          790..812
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          279..341
FT                   /evidence="ECO:0000255"
FT   COILED          666..803
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        190..223
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..620
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        790..810
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   829 AA;  93774 MW;  CA117B4FA90FC9B7 CRC64;
     MVEAGAKISK GGTQQAAGHG LEGYASDGST DLRSAGAAEH ETQDSAKAQE NEASANSMDD
     GLELGRRGQG VSPVLTPPTE EEGDAPAQKN RRQRLKERKA TAAAAGALPG IGRARSGSVK
     EGGSPKAAGA ESPRRGAGAA AKDAKISERA EGAGSPQQRK QGTGAAAPGS PPRRRLEAAE
     PPATPPRRKQ AEGEQSRPEG EQGRPENKNK KAKDKHDDLP TRGPGTRRPQ VRAVPPPLSE
     ELKNEAFRKT LERVETVAPE VPLQAAEQRS EPSDFDLIIN RLRVNAQEYM SQDEQAQENL
     QEGVRQLKSS YTEFLQTIQP EEKKKGDVEE LDEEEEEMRK IDWQFWTSVV NNFATVAKND
     SAKLEEKVSD GIPKQIRGII WQLISNSKSK EIRQLYQDLL QIPSEHEKAI QRDISRTKFI
     PVDKTESLFN VLKAYSLFDP EVGYTQGMAF VTAPLLINVW EEADAFGLLI KLMKNYGLRE
     FFLPDMPGLQ LKLYEFDRLL EENSPQLYNH LIRLGIRSSM YATQWFLTLF AYKFPLGFVL
     RILDVIFVEG IESLLKFAVI LMLKNESVLV QLKFDKLLDF LKDGLFNYYL KENVRKRQEG
     KEDTNAIQNA EVSDSSSKSS TVGSEILGVE YNINVFIQDA IREVKITPIQ LRRYSSEYEE
     IHQLEFQREA QYEEMRIKNR QLQREVRKLE HDYTLLNREH IMLANELIQN RLKIETLNDE
     NKDLKLTVDV LKRHLSDEMR KQTLPNPDAQ IPTDLKEDLE KTMQRNLEVM NQNQELEDKV
     TALERQVKQL KKNRANTSVE HGEDSSSEPR VRSHIVTPSI SSWTFKKPW