GenomeNet

Database: UniProt
Entry: Q6WP05_9EUKA
LinkDB: Q6WP05_9EUKA
Original site: Q6WP05_9EUKA 
ID   Q6WP05_9EUKA            Unreviewed;       384 AA.
AC   Q6WP05;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
DE   Flags: Fragment;
OS   Hypotrichomonas acosta.
OC   Eukaryota; Metamonada; Parabasalia; Hypotrichomonadida;
OC   Hypotrichomonadidae; Hypotrichomonas.
OX   NCBI_TaxID=5735 {ECO:0000313|EMBL:AAQ19197.1};
RN   [1] {ECO:0000313|EMBL:AAQ19197.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 30069 {ECO:0000313|EMBL:AAQ19197.1};
RA   Gerbod D., Sanders E., Moriya S., Noel C., Takasu H., Fast N.M.,
RA   Delgado-Viscogliosi P., Ohkuma M., Kudo T., Capron M., Palmer J.D.,
RA   Keeling P.J., Viscogliosi E.;
RT   "Molecular phylogenies of Parabasalia inferred from various protein coding
RT   gene sequences and comparison with small subunit rRNA-based trees.";
RL   Submitted (APR-2003) 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|RuleBase:RU000352}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
CC   -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a
CC       hollow water-filled tube with an outer diameter of 25 nm and an inner
CC       diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to
CC       form protofilaments running lengthwise along the microtubule wall with
CC       the beta-tubulin subunit facing the microtubule plus end conferring a
CC       structural polarity. Microtubules usually have 13 protofilaments but
CC       different protofilament numbers can be found in some organisms and
CC       specialized cells. {ECO:0000256|RuleBase:RU000352}.
CC   -!- SIMILARITY: Belongs to the tubulin family.
CC       {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY277776; AAQ19197.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6WP05; -.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   CDD; cd02186; alpha_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; IPR002452; Alpha_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:SF239; TUBULIN ALPHA CHAIN; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01162; ALPHATUBULIN.
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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000352};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000352}.
FT   DOMAIN          27..224
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          226..371
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAQ19197.1"
FT   NON_TER         384
FT                   /evidence="ECO:0000313|EMBL:AAQ19197.1"
SQ   SEQUENCE   384 AA;  42624 MW;  30EC9FFE5FB8A099 CRC64;
     LYCLEHGIQP DGQLPSDKTI GVEDDAFNTF FSETGAGKHV PRAVFVDLEP TVVDEVRTGT
     YRQLFHPEQL ISGKEDAANN YARGHYTVGK ELIDLTLDRI RKLADQCTGL QGFLIFHSFG
     GGTGAGFGSL LLERLSVDYG KKSKLEFTVY PSPQVSTAIV EPYNSILATH AMIDHSDCAF
     MVDNEALYDL CRRALDIERP TYTNLNRLIG QVVSSLTASL RFDGALNVDF TEFQTNLVPY
     ARIHFPICSY APVISAEKAY HEQLSVAEIT NSLFEPANMM VKCDPRHGKY MACTLLYRGD
     VVPKDVSAAV ATIKTKRTIQ FVDWCPTGFK MGINYQPPTV VPGGDLAKVQ RAVCMLANTT
     AIAEAWSRLD HKFDLMYAKR AFVH
//
DBGET integrated database retrieval system