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Database: UniProt
Entry: L1IDY3_GUITC
LinkDB: L1IDY3_GUITC
Original site: L1IDY3_GUITC 
ID   L1IDY3_GUITC            Unreviewed;       454 AA.
AC   L1IDY3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Tubulin gamma chain {ECO:0000256|RuleBase:RU000352};
GN   ORFNames=GUITHDRAFT_158807 {ECO:0000313|EMBL:EKX34481.1};
OS   Guillardia theta (strain CCMP2712) (Cryptophyte).
OC   Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX   NCBI_TaxID=905079 {ECO:0000313|EMBL:EKX34481.1};
RN   [1] {ECO:0000313|EMBL:EKX34481.1, ECO:0000313|Proteomes:UP000011087}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP2712 {ECO:0000313|EMBL:EKX34481.1,
RC   ECO:0000313|Proteomes:UP000011087};
RX   PubMed=23201678; DOI=10.1038/nature11681;
RG   DOE Joint Genome Institute;
RA   Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M., Maruyama S.,
RA   Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F., Kuo A.,
RA   Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA   Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA   Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA   Durnford D.G., Fast N.M., Green B.R., Grisdale C.J., Hempel F.,
RA   Henrissat B., Hoppner M.P., Ishida K., Kim E., Koreny L., Kroth P.G.,
RA   Liu Y., Malik S.B., Maier U.G., McRose D., Mock T., Neilson J.A.,
RA   Onodera N.T., Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W.,
RA   Sarai C., Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA   Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA   Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA   Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RT   "Algal genomes reveal evolutionary mosaicism and the fate of
RT   nucleomorphs.";
RL   Nature 492:59-65(2012).
RN   [2] {ECO:0000313|Proteomes:UP000011087}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP2712 {ECO:0000313|Proteomes:UP000011087};
RA   Kuo A., Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M.,
RA   Maruyama S., Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F.,
RA   Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA   Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA   Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA   Durnford D.G., Fast N.M., Green B.R., Grisdale C., Hempe F., Henrissat B.,
RA   Hoppner M.P., Ishida K.-I., Kim E., Koreny L., Kroth P.G., Liu Y.,
RA   Malik S.-B., Maier U.G., McRose D., Mock T., Neilson J.A., Onodera N.T.,
RA   Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W., Sarai C.,
RA   Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA   Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA   Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA   Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblProtists:EKX34481}
RP   IDENTIFICATION.
RG   EnsemblProtists;
RL   Submitted (MAR-2016) to UniProtKB.
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. {ECO:0000256|RuleBase:RU000352}.
CC   -!- SIMILARITY: Belongs to the tubulin family.
CC       {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}.
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DR   EMBL; JH993108; EKX34481.1; -; Genomic_DNA.
DR   RefSeq; XP_005821461.1; XM_005821404.1.
DR   AlphaFoldDB; L1IDY3; -.
DR   STRING; 905079.L1IDY3; -.
DR   PaxDb; 55529-EKX34481; -.
DR   EnsemblProtists; EKX34481; EKX34481; GUITHDRAFT_158807.
DR   GeneID; 17291256; -.
DR   KEGG; gtt:GUITHDRAFT_158807; -.
DR   eggNOG; KOG1374; Eukaryota.
DR   HOGENOM; CLU_015718_1_0_1; -.
DR   OMA; FWKKLCA; -.
DR   OrthoDB; 5476567at2759; -.
DR   Proteomes; UP000011087; Unassembled WGS sequence.
DR   GO; GO:0000930; C:gamma-tubulin complex; IEA:InterPro.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR   GO; GO:0007020; P:microtubule nucleation; IEA:InterPro.
DR   CDD; cd02188; gamma_tubulin; 1.
DR   Gene3D; 1.10.287.600; Helix hairpin bin; 1.
DR   Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR   Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 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; TUBULIN; 1.
DR   PANTHER; PTHR11588:SF7; TUBULIN GAMMA CHAIN; 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; SSF55307; Tubulin C-terminal domain-like; 1.
DR   SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000352};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000352};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000352};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011087}.
FT   DOMAIN          49..249
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          251..399
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
SQ   SEQUENCE   454 AA;  50862 MW;  CB96265FA77A26E2 CRC64;
     MPREIITLQV GQCGNQIGYE FWKQLCLEHG ITQDGLIRDD MEVDAGDRKD VFFYQADDEH
     YIPRAILLDL EDRVINGIRT GEYRKLYNPE NFLVDTQGGG AGNNWASGYG QAKDKIEDIM
     DMIDREADGS DSLEGFVVCH SIAGGTGSGM GSYMLEALND RYSKKLVQTY SVFPNDGESN
     SDVVVQPYNS ILTLKRLTLE ADCVVVLDNN ALNRIATERL RIPKPDFTIV NGLVSTVMAA
     STATLRYPSY MNNDLVGLIA SLIPTPRCHF LMTGYTPMAY DLVERSVRKT TVLDVMRRLL
     QSKNMMVSTK MHSQQPGRNP CYISILNIIQ GEADPTQVHK SLQRIRERKL ANFIPWGPAS
     IQVALSRRSP YLPAGGPRVS GLLMANHTSI SSLFERILKQ FDLLIKKKAG SVDELKDEFD
     DSREIVQSLV QEYHACESPN YIEWGMQQRG GPSD
//
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