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
//