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Database: UniProt
Entry: E1EXM1_GIAIA
LinkDB: E1EXM1_GIAIA
Original site: E1EXM1_GIAIA 
ID   E1EXM1_GIAIA            Unreviewed;       472 AA.
AC   E1EXM1;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Tubulin gamma chain {ECO:0000256|RuleBase:RU000352};
GN   ORFNames=GLP15_2552 {ECO:0000313|EMBL:EFO65008.1};
OS   Giardia intestinalis (strain P15) (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=658858 {ECO:0000313|EMBL:EFO65008.1, ECO:0000313|Proteomes:UP000008974};
RN   [1] {ECO:0000313|EMBL:EFO65008.1, ECO:0000313|Proteomes:UP000008974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P15 {ECO:0000313|EMBL:EFO65008.1,
RC   ECO:0000313|Proteomes:UP000008974};
RX   PubMed=20929575; DOI=10.1186/1471-2164-11-543;
RA   Jerlstrom-Hultqvist J., Franzen O., Ankarklev J., Xu F., Nohynkova E.,
RA   Andersson J.O., Svard S.G., Andersson B.;
RT   "Genome analysis and comparative genomics of a Giardia intestinalis
RT   assemblage E isolate.";
RL   BMC Genomics 11:543-543(2010).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFO65008.1}.
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DR   EMBL; ACVC01000052; EFO65008.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1EXM1; -.
DR   STRING; 658858.E1EXM1; -.
DR   EnsemblProtists; EFO65008; EFO65008; GLP15_2552.
DR   VEuPathDB; GiardiaDB:GLP15_2552; -.
DR   OMA; HRYISIL; -.
DR   OrthoDB; 5476567at2759; -.
DR   Proteomes; UP000008974; 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}.
FT   DOMAIN          48..247
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          249..413
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
SQ   SEQUENCE   472 AA;  52022 MW;  07533CB1EFA4D9CA CRC64;
     MPREVITIQC GQCGNQIGEV FWNRLCTEHG IKPDGTLRPE AYTFNDRKDV FFYQSDDEHY
     VPRAILLDTE PGVISHIRNG PIKELINPEN VYIDSTGGGA GNIWTKGFQC GEAGFEKIVE
     IIDREADGAD SLAGFSLTHS IAGGTGSGMG SFLLDRLSDR YPKALLQTYS VFPNTTADII
     VQPYNSILTL QRLALCADAV VVLDNTALDR IITNHIPNEL LTNPFEHVNS LVSTVMAAST
     STLRLPGFMS NDLLSLVSSL VPTPRLHFLM SSYTPITSSS LNVKEHTKDQ ETGPGAVAGP
     AVGATRRQVH TDSIVQLVKR LLHPTNGMVS CGRDGKYISL LNIVQGEAES NQLYKSLQQI
     KEGRDVRFID WGPSNMQMAL SKRSPFTNEA HKVSGLMLAN HTSIRKIFDN INNTFTQLFS
     KRAYLQNYID SMVTGGEPEI LEQFTDAQAV CTSLSKEYEA AESKDYLEYI GM
//
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