ID T0L8L5_9MICR Unreviewed; 441 AA.
AC T0L8L5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
GN ORFNames=NAPIS_ORF01579 {ECO:0000313|EMBL:EQB60848.1};
OS Vairimorpha apis BRL 01.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae;
OC Vairimorpha.
OX NCBI_TaxID=1037528 {ECO:0000313|EMBL:EQB60848.1, ECO:0000313|Proteomes:UP000053780};
RN [1] {ECO:0000313|EMBL:EQB60848.1, ECO:0000313|Proteomes:UP000053780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRL 01 {ECO:0000313|EMBL:EQB60848.1,
RC ECO:0000313|Proteomes:UP000053780};
RX PubMed=23829473; DOI=10.1186/1471-2164-14-451;
RA Chen Yp., Pettis J.S., Zhao Y., Liu X., Tallon L.J., Sadzewicz L.D., Li R.,
RA Zheng H., Huang S., Zhang X., Hamilton M.C., Pernal S.F.,
RA Melathopoulos A.P., Yan X., Evans J.D.;
RT "Genome sequencing and comparative genomics of honey bee microsporidia,
RT Nosema apis reveal novel insights into host-parasite interactions.";
RL BMC Genomics 14:451-451(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|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; KE647224; EQB60848.1; -; Genomic_DNA.
DR AlphaFoldDB; T0L8L5; -.
DR VEuPathDB; MicrosporidiaDB:NAPIS_ORF01579; -.
DR HOGENOM; CLU_015718_0_0_1; -.
DR Proteomes; UP000053780; 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 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; IPR013838; Beta-tubulin_BS.
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.
DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 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:UP000053780}.
FT DOMAIN 46..242
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 244..389
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
SQ SEQUENCE 441 AA; 48961 MW; E38B452DA89A3779 CRC64;
MREIISVHVG QAGVQIGNSC WELYCKEHGI LPDGTLSPDA MEDEGSQSFF SHTSAGTFVP
RTVMVDLEPS VIGSIKSSKY RNLFHPDQLI HGKEDAANNY ARGHYTVGKD VIETVLEQIR
RIADNCEGLQ GFLIFHSFGG GTGSGLGSLL MERLDAEFGK KSKLEISVYP APRIATAVVE
PYNSVLTTHA TLDHSDCSFL VDNEAIYDMC KNLGVSRPHY NDINRIIAQV VSSITASLRF
TGTLNVDLTE FQTNLVPYPR IHFPLVAYAP MLSKEKASHE KMSVQEITNA CFEPQNQMVK
CDTTKGKYMA CCLLFRGDVN PKEANSATAN IKAKKNNQFV EWCPTGFKIG INNRVPTVLD
GQDMAPTKRA VCVLSNTTAI GEAWKRLDDK YDLMYAKRAF VHWYVGEGME EGEFSEAREN
LAMLEDDYKQ IMGCGEPSES Y
//
