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Database: UniProt
Entry: M2Y3E5_GALSU
LinkDB: M2Y3E5_GALSU
Original site: M2Y3E5_GALSU 
ID   M2Y3E5_GALSU            Unreviewed;       457 AA.
AC   M2Y3E5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Tubulin gamma chain {ECO:0000256|RuleBase:RU000352};
GN   ORFNames=Gasu_22430 {ECO:0000313|EMBL:EME30334.1};
OS   Galdieria sulphuraria (Red alga).
OC   Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC   Galdieria.
OX   NCBI_TaxID=130081 {ECO:0000313|EMBL:EME30334.1, ECO:0000313|Proteomes:UP000030680};
RN   [1] {ECO:0000313|Proteomes:UP000030680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX   PubMed=23471408; DOI=10.1126/science.1231707;
RA   Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA   Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA   Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA   Lercher M.J., Weber A.P.;
RT   "Gene transfer from bacteria and archaea facilitated evolution of an
RT   extremophilic eukaryote.";
RL   Science 339:1207-1210(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. {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; KB454500; EME30334.1; -; Genomic_DNA.
DR   RefSeq; XP_005706854.1; XM_005706797.1.
DR   AlphaFoldDB; M2Y3E5; -.
DR   STRING; 130081.M2Y3E5; -.
DR   EnsemblPlants; EME30334; EME30334; Gasu_22430.
DR   GeneID; 17089068; -.
DR   Gramene; EME30334; EME30334; Gasu_22430.
DR   KEGG; gsl:Gasu_22430; -.
DR   eggNOG; KOG1374; Eukaryota.
DR   OMA; HRYISIL; -.
DR   OrthoDB; 5476567at2759; -.
DR   Proteomes; UP000030680; 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:UP000030680}.
FT   DOMAIN          48..247
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          249..394
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
SQ   SEQUENCE   457 AA;  51241 MW;  8863E4EC70DCF504 CRC64;
     MPREIITLQI GQCGNQIGTE FWNQLCAEHG IRPDGVLEES VVDTGDRKDV FFYQADDDHY
     VPRALLIDLE PRVINGIRNS TFRNFYNPEN IFVSQVGGGA GNNWASGYRQ GEEKEEELMD
     MIEREADGSD SLEGFVLCHS IAGGTGSGLG SFVLEKLNER FPKKLVQTYS VFPNQQESSD
     VVVQPYNSIL TLKRLTQNAD CVVVLDNTAL NRIAVDRLHL ENPTFAQVNS LVSAVMAAST
     STLRYPGYMN NDLVGLLASL IPTPQCHYLV TGYTPLTLLE EERAGTSQVT KTTVLDVMRR
     LLQPKNIMVS CSTRKGCYIS ILNVIQGEAD PAQVHKSLQR IRERKLATFI PWGPTGIQVA
     LSKKSPYLKS HHRISGLMLA NHTSIQSLFS RSLAQYDKLR KRNAFLDNYK KEPMFQDGLE
     EFDNSRQVVE DLIAEYTAAE RPDYLSWSSS NVPEYSK
//
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