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Database: UniProt
Entry: A9LGN3_9STRA
LinkDB: A9LGN3_9STRA
Original site: A9LGN3_9STRA 
ID   A9LGN3_9STRA            Unreviewed;       404 AA.
AC   A9LGN3;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
DE   Flags: Fragment;
OS   Spumella-like flagellate JBNA45.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Chrysophyceae; Chromulinales;
OC   Chromulinaceae.
OX   NCBI_TaxID=373001 {ECO:0000313|EMBL:ABX55866.1};
RN   [1] {ECO:0000313|EMBL:ABX55866.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JBNA45 {ECO:0000313|EMBL:ABX55866.1};
RX   PubMed=18319484; DOI=10.1099/ijs.0.65310-0;
RA   Stoeck T., Jost S., Boenigk J.;
RT   "Multigene phylogenies of clonal Spumella-like strains, a cryptic
RT   heterotrophic nanoflagellate, isolated from different geographical
RT   regions.";
RL   Int. J. Syst. Evol. Microbiol. 58:716-724(2008).
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}.
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DR   EMBL; EF577226; ABX55866.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9LGN3; -.
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          38..235
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          237..382
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABX55866.1"
FT   NON_TER         404
FT                   /evidence="ECO:0000313|EMBL:ABX55866.1"
SQ   SEQUENCE   404 AA;  44827 MW;  87CDA7D14DF48FD4 CRC64;
     SRPQVGNACW ELFCLEHGIQ PDGRIPSDIS AQCDTDSFLS FFSETCAGKY VPRSIVFDSE
     PTVCDEVRTG VFRLLYHPEQ IISGKEDAGS NFARGHYTLG KEHIDQVLDR IRRLADDCAS
     LQGFMIYHAT GGGTGAGFGA LLMERLSVDY GKKSKLTLSV TPAPQVATAV VEPYNHVLAA
     HSLLNHADVT FNLDIEALYD ICRRSLDIER PTYTNLNRLV AQVVSTLTSS LRYDGCLNAD
     LAEFSTNLVP YPRVHFISTA YAPLVPWEKR GREVGMPVDV MRQAIDYSHH LVKIDPTHGK
     YMSLCMMFRG DVVPRDIGPA IRDVKVRRSV RFVDWCPTGF KCGINYQPPP ALPGGDYAQV
     SRAVCLLSNT TAIAEALAGL NHKFDVMYAK RAFVHWYVGE GMAR
//
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