GenomeNet

Database: UniProt
Entry: Q8MU31_HALGN
LinkDB: Q8MU31_HALGN
Original site: Q8MU31_HALGN 
ID   Q8MU31_HALGN            Unreviewed;       365 AA.
AC   Q8MU31;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
DE   Flags: Fragment;
OS   Halteria grandinella.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Halteriidae; Halteria.
OX   NCBI_TaxID=5974 {ECO:0000313|EMBL:AAL33694.1};
RN   [1] {ECO:0000313|EMBL:AAL33694.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Katz L.A., Israel R.L.;
RT   "The fate of duplicated alpha-tubulin genes in ciliates.";
RL   Submitted (JUN-2001) 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|ARBA:ARBA00011747,
CC       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; AY041114; AAL33694.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8MU31; -.
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          11..208
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          210..355
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAL33694.1"
FT   NON_TER         365
FT                   /evidence="ECO:0000313|EMBL:AAL33694.1"
SQ   SEQUENCE   365 AA;  40148 MW;  9CDE938DB12B1822 CRC64;
     DKTIGGGDDA FNTFFSETGA GKHVPRCVFL DLEPTVIDEV RTGTYRQLFH PEQLISGKED
     AANNFARGHY TIGKEIVDLC LDRIRKLADQ CTGLQGFLVF NAVGGGTGSG LGSLLLERLS
     VDYGKKSKLG FTVYPSPQVS TAVVEPYNSV LSTHSLLEHT DVAVMLDNEA VYDICRRNLD
     IERPTYTNLN RLIAQVISSL TASLRFDGAL NVDVTVFQTN LVPYPRIHFM LSSYAPVISA
     EKAYHEQLSV AEITNSAFEP ASMMAKCDPR HGKYMACCLM YRGDVVPKDV NAAVATIKTK
     RTIQFVDWCP TGFKCGINYQ PPTVVPGGDL AKVMRACCMI SNSTAIAEVF SRIDHKFDLM
     YAKRA
//
DBGET integrated database retrieval system