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Database: UniProt
Entry: A0A0D2LV19_9CHLO
LinkDB: A0A0D2LV19_9CHLO
Original site: A0A0D2LV19_9CHLO 
ID   A0A0D2LV19_9CHLO        Unreviewed;       193 AA.
AC   A0A0D2LV19;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
GN   ORFNames=MNEG_14495 {ECO:0000313|EMBL:KIY93466.1};
OS   Monoraphidium neglectum.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Selenastraceae; Monoraphidium.
OX   NCBI_TaxID=145388 {ECO:0000313|EMBL:KIY93466.1, ECO:0000313|Proteomes:UP000054498};
RN   [1] {ECO:0000313|EMBL:KIY93466.1, ECO:0000313|Proteomes:UP000054498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAG 48.87 {ECO:0000313|EMBL:KIY93466.1,
RC   ECO:0000313|Proteomes:UP000054498};
RX   PubMed=24373495; DOI=10.1186/1471-2164-14-926;
RA   Bogen C., Al-Dilaimi A., Albersmeier A., Wichmann J., Grundmann M.,
RA   Rupp O., Lauersen K.J., Blifernez-Klassen O., Kalinowski J., Goesmann A.,
RA   Mussgnug J.H., Kruse O.;
RT   "Reconstruction of the lipid metabolism for the microalga Monoraphidium
RT   neglectum from its genome sequence reveals characteristics suitable for
RT   biofuel production.";
RL   BMC Genomics 14:926-926(2013).
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}.
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DR   EMBL; KK104751; KIY93466.1; -; Genomic_DNA.
DR   RefSeq; XP_013892486.1; XM_014037032.1.
DR   AlphaFoldDB; A0A0D2LV19; -.
DR   STRING; 145388.A0A0D2LV19; -.
DR   GeneID; 25732063; -.
DR   KEGG; mng:MNEG_14495; -.
DR   OrthoDB; 980494at2759; -.
DR   Proteomes; UP000054498; Unassembled WGS sequence.
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   Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR   InterPro; IPR002452; Alpha_tubulin.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
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   PRINTS; PR01162; ALPHATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054498}.
FT   DOMAIN          49..193
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
SQ   SEQUENCE   193 AA;  20772 MW;  3B12C8790D537EE3 CRC64;
     MREVISIHIG QAGIQVGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDAFN TFFSETGAGK
     HVPRCIFLDL EPTVVDEVRT GTYRQLFHPE QLISGKEDAA NNFARGHYTI GKEIVDLALD
     RIRKLADNCT GLQGFLVFNA VGGGTGSGLG SLLLERLSVD YGKKSKLGFT IYPSPQYSGL
     GPRSLPARSA VLA
//
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