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Database: UniProt
Entry: Q4VHC1_NAEGR
LinkDB: Q4VHC1_NAEGR
Original site: Q4VHC1_NAEGR 
ID   Q4VHC1_NAEGR            Unreviewed;       442 AA.
AC   Q4VHC1;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Tubulin gamma chain {ECO:0000256|RuleBase:RU000352};
OS   Naegleria gruberi (Amoeba).
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=5762 {ECO:0000313|EMBL:AAY17321.1};
RN   [1] {ECO:0000313|EMBL:AAY17321.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15939759; DOI=10.1083/jcb.200410052;
RA   Kim H.K., Kang J.G., Yumura S., Walsh C.J., Cho J.W., Lee J.;
RT   "De novo formation of basal bodies in Naegleria gruberi: regulation by
RT   phosphorylation.";
RL   J. Cell Biol. 169:719-724(2005).
RN   [2] {ECO:0000313|EMBL:AAY17321.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Lee Y.K., Lee J.H.;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules, a cylinder
CC       consisting of laterally associated linear protofilaments composed of
CC       alpha- and beta-tubulin heterodimers. Microtubules grow by the addition
CC       of GTP-tubulin dimers to the microtubule end, where a stabilizing cap
CC       forms. Below the cap, tubulin dimers are in GDP-bound state, owing to
CC       GTPase activity of alpha-tubulin. {ECO:0000256|ARBA:ARBA00034296}.
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; AY919610; AAY17321.1; -; mRNA.
DR   AlphaFoldDB; Q4VHC1; -.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_56069; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000352};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000352};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000352}.
FT   DOMAIN          49..247
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          249..390
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
SQ   SEQUENCE   442 AA;  49423 MW;  9E1E6DFC8D6717A3 CRC64;
     MPREIITLQA GQCGNQIGTE FWKRLCLEHG IGTDGVLEDF AIQGAGDRKD VFFYQADDEH
     YIPRSVIVDL ETRVIEGIKK SHRNLFNPEN IYMPGDGGGA GNNWANGFQL AEKYHEKLMD
     IIDREADNSD SMEGFVLLHS IAGGTGSGLG SYLLEKLNDR YPKKLIQTYS VFPSYEAASD
     VVVQSYNSML ALKRLILNAD SVVVLDNTAL NQIATERLKI PNPSVDNINS LVSTIMAATT
     TTLRYPGYMN NDLVGLIASL VPTPRCHFLM TSYTPLSVVD NQAKIQKTSV LDVMRRLLNP
     KNIMVSSNIK KGCYVSILNI IQGEVDPTQV HKSLSLIRKK NLANFIPWGP SSIQVVLSKR
     SPYVQTQNRV SGLMMANHTS LGSLCQTILK NFLKQYKSKA FTQNYMESFE SKDEFEDSKE
     VVSSLIEEYK QSESENYLSM QQ
//
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