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TBG_EMENI
ID   TBG_EMENI               Reviewed;         454 AA.
AC   P18695; C8VRR9; Q5BFK4;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 3.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Tubulin gamma chain;
DE   AltName: Full=Gamma-tubulin;
GN   Name=mipA; ORFNames=AN0676;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2649796; DOI=10.1038/338662a0;
RA   Oakley C.E., Oakley B.R.;
RT   "Identification of gamma-tubulin, a new member of the tubulin superfamily
RT   encoded by mipA gene of Aspergillus nidulans.";
RL   Nature 338:662-664(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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 pole or the centrosome, suggesting that it is involved in the
CC       minus-end nucleation of microtubule assembly. Interacts physically with
CC       beta-tubulin and is involved in microtubule function.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, spindle pole body {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA65452.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; X15479; CAA33507.1; -; mRNA.
DR   EMBL; AACD01000010; EAA65452.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001308; CBF89007.1; -; Genomic_DNA.
DR   PIR; S03916; S03916.
DR   RefSeq; XP_658280.1; XM_653188.1.
DR   AlphaFoldDB; P18695; -.
DR   SMR; P18695; -.
DR   STRING; 162425.CADANIAP00001997; -.
DR   EnsemblFungi; CBF89007; CBF89007; ANIA_00676.
DR   EnsemblFungi; EAA65452; EAA65452; AN0676.2.
DR   GeneID; 2876456; -.
DR   KEGG; ani:AN0676.2; -.
DR   VEuPathDB; FungiDB:AN0676; -.
DR   eggNOG; KOG1374; Eukaryota.
DR   HOGENOM; CLU_015718_1_0_1; -.
DR   InParanoid; P18695; -.
DR   OMA; EHGINKE; -.
DR   OrthoDB; 514396at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000923; C:equatorial microtubule organizing center; IEA:EnsemblFungi.
DR   GO; GO:0000930; C:gamma-tubulin complex; IBA:GO_Central.
DR   GO; GO:0061496; C:half bridge of mitotic spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:0061497; C:inner plaque of mitotic spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:0031021; C:interphase microtubule organizing center; IEA:EnsemblFungi.
DR   GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005815; C:microtubule organizing center; IDA:AspGD.
DR   GO; GO:0005637; C:nuclear inner membrane; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0071957; C:old mitotic spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:0061499; C:outer plaque of mitotic spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:0005819; C:spindle; IBA:GO_Central.
DR   GO; GO:0005816; C:spindle pole body; IDA:AspGD.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IMP:AspGD.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:AspGD.
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; IMP:AspGD.
DR   GO; GO:0000278; P:mitotic cell cycle; IMP:AspGD.
DR   GO; GO:1902408; P:mitotic cytokinesis, site selection; IEA:EnsemblFungi.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR   GO; GO:0051256; P:mitotic spindle midzone assembly; IEA:EnsemblFungi.
DR   GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..454
FT                   /note="Tubulin gamma chain"
FT                   /id="PRO_0000048456"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   454 AA;  50770 MW;  2C82A2D60B943433 CRC64;
     MPREIITIQA GQCGNNVGSQ FWQQLCLEHG ISQDGNLEEF ATEGGDRKDV FFYQSDDTRY
     IPRAILLDLE PRVLNGIQSG PYKNIYNPEN FFIGQQGIGA GNNWGAGYAA GEVVQEEVFD
     MIDREADGSD SLEGFMFLHS IAGGTGSGLG SFLLERMNDR FPKKLIQTYS VFPDTQAADV
     VVNPYNSLLA MRRLTQNADS VVVLDNAALS RIVADRLHVQ EPSFQQTNRL VSTVMSASTT
     TLRYPGYMHN DLVGIIASLI PTPRSHFLLT SYTPFTGDNI DQAKTVRKTT VLDVMRRLLQ
     PKNRMVSINP SKSSCYISIL NIIQGEADPT DVHKSLLRIR ERRLASFIPW GPASIQVALT
     KKSPYIQNTH RVSGLMLANH TSVATLFKRI VQQYDRLRKR NAFLEQYKKE APFQDGLDEF
     DEARAVVMDL VGEYEAAERE NYLDPDAGKD EVGV
 
 
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