GenomeNet

Database: UniProt
Entry: E2CWH5_9EUKA
LinkDB: E2CWH5_9EUKA
Original site: E2CWH5_9EUKA 
ID   E2CWH5_9EUKA            Unreviewed;       373 AA.
AC   E2CWH5;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
DE   Flags: Fragment;
GN   Name=Atub {ECO:0000313|EMBL:ADK26606.1};
OS   Eukaryota sp. ATCC 50646.
OC   Eukaryota.
OX   NCBI_TaxID=862250 {ECO:0000313|EMBL:ADK26606.1};
RN   [1] {ECO:0000313|EMBL:ADK26606.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wegener Parfrey L., Grant J.R., Tekle Y.I., Lasek-Nesselquist E.,
RA   Morrison H.G., Sogin M.L., Patterson D.J., Katz L.A.;
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADK26606.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20656852; DOI=10.1093/sysbio/syq037;
RA   Parfrey L.W., Grant J., Tekle Y.I., Lasek-Nesselquist E., Morrison H.G.,
RA   Sogin M.L., Patterson D.J., Katz L.A.;
RT   "Broadly sampled multigene analyses yield a well-resolved eukaryotic tree
RT   of life.";
RL   Syst. Biol. 59:518-533(2010).
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; GQ377661; ADK26606.1; -; Genomic_DNA.
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          20..217
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          219..364
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADK26606.1"
FT   NON_TER         373
FT                   /evidence="ECO:0000313|EMBL:ADK26606.1"
SQ   SEQUENCE   373 AA;  41136 MW;  FA47D500EB9685BB CRC64;
     IQPDGQMPSD KTIGVEDDAF NTFFSETGAG KHVPRAVFLD LEPTVIDEVR TGTYRQLFHP
     EQLISGKEDS ANNYARGHYT IGKEIVDLCL DRIRKLADNC TGLQGFLVFN AVGGGTGSGL
     GALLLERLSV DYGKKSKLGF TVYPSPQVST AVVEPYNSVL STHALLEHTD VAVMLDNEAI
     YDICRRSLDI ERPTYTNLNR LIAQVISSLT ASLRFDGALN VDITEFQTNL VPYPRIHFML
     SSYAPVISAE KAYHEQLSVA EITNSAFEPA SMMAKCDPRH GKYMACCLMY RGDVVPKDVX
     ASVATIKTKR TIQFVDWCPT GFKCGINYQP PTVVPGGDLA KVQRAVCMIS NSTAIAEVFS
     RIDHKFDLMY AKR
//
DBGET integrated database retrieval system