ID   TBG_ASHGO               Reviewed;         470 AA.
AC   Q75A43;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Tubulin gamma chain;
DE   AltName: Full=Gamma-tubulin;
GN   Name=TUB4; OrderedLocusNames=ADR076C;
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.
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: Tubulin is the major constituent of microtubules. The gamma
CC       chain is found at microtubule organizing centers (MTOC) such as the
CC       spindle poles or the centrosome, suggesting that it is involved in the
CC       minus-end nucleation of microtubule assembly (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, spindle pole body {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; AE016817; AAS51996.1; -; Genomic_DNA.
DR   RefSeq; NP_984172.1; NM_209525.1.
DR   AlphaFoldDB; Q75A43; -.
DR   SMR; Q75A43; -.
DR   STRING; 33169.AAS51996; -.
DR   EnsemblFungi; AAS51996; AAS51996; AGOS_ADR076C.
DR   GeneID; 4620321; -.
DR   KEGG; ago:AGOS_ADR076C; -.
DR   eggNOG; KOG1374; Eukaryota.
DR   HOGENOM; CLU_015718_1_0_1; -.
DR   InParanoid; Q75A43; -.
DR   OMA; EHGINKE; -.
DR   Proteomes; UP000000591; Chromosome IV.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000930; C:gamma-tubulin complex; IBA:GO_Central.
DR   GO; GO:0008275; C:gamma-tubulin small complex; IEA:EnsemblFungi.
DR   GO; GO:0005822; C:inner plaque of spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005824; C:outer plaque of spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:0005819; C:spindle; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR   GO; GO:0000212; P:meiotic spindle organization; IBA:GO_Central.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central.
DR   GO; GO:0051417; P:microtubule nucleation by spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR   GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR   GO; GO:2000767; P:positive regulation of cytoplasmic translation; IEA:EnsemblFungi.
DR   CDD; cd02188; gamma_tubulin; 1.
DR   Gene3D; 1.10.287.600; -; 1.
DR   Gene3D; 3.30.1330.20; -; 1.
DR   Gene3D; 3.40.50.1440; -; 1.
DR   InterPro; IPR002454; Gamma_tubulin.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR   InterPro; IPR023123; Tubulin_C.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   PANTHER; PTHR11588; PTHR11588; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01164; GAMMATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF52490; SSF52490; 1.
DR   SUPFAM; SSF55307; SSF55307; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..470
FT                   /note="Tubulin gamma chain"
FT                   /id="PRO_0000048447"
FT   BINDING         144..150
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   470 AA;  52605 MW;  C7CB6658D10BF11A CRC64;
     MTGEIISIQV GQCGNQVGKQ FWGQLAREHG IGVDGQSLHP EDANVVREDD TNVFFRQNDH
     NRFTPRALLY DLEPSAIGDV QNCFPGFFNE RNVWISKEEL GAGNTWSIGY DYGLEKQDEF
     MNMIDKEIDA TGNFEGFQLI HSVAGGTGSG LGSNLLEALS DRYHKKIVST YSVFPSRESE
     VVVQPYNTIL TLRRLIDNSD ASVLFDNDAL LNLTARVLRD SNTSYQQTNQ LIASVMSSVT
     NSLRFPSYMY NSLPSIFSTL VPTPELHFLA PSFTPFTSDF VPGAKDFKRL SAYDVILDLF
     DKNNSMVTRD TDTPVYLAIY DALQGAVEQS DVTRAILKTQ QRIKFAPWSP TSLHVNLGRK
     SPYNSSANSD YVSGMMLANT SSIVSVFQKT VSSFDVIFKR GAFLHKFQNG KMFQHGWDEF
     LESREVIQGV IDEYIAAEQE NYLDDVLEED GNFVGGDAEM IDIESNDDII