TBA_ENCCU
ID TBA_ENCCU Reviewed; 441 AA.
AC Q8SRI6;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Tubulin alpha chain;
GN Name=TUB1; OrderedLocusNames=ECU07_1190;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It binds
CC two moles of GTP, one at an exchangeable site on the beta chain and one
CC at a non-exchangeable site on the alpha chain.
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; AL590447; CAD25652.1; -; Genomic_DNA.
DR RefSeq; NP_586048.1; NM_001041670.1.
DR AlphaFoldDB; Q8SRI6; -.
DR SMR; Q8SRI6; -.
DR STRING; 284813.Q8SRI6; -.
DR PRIDE; Q8SRI6; -.
DR GeneID; 859478; -.
DR KEGG; ecu:ECU07_1190; -.
DR VEuPathDB; MicrosporidiaDB:ECU07_1190; -.
DR HOGENOM; CLU_015718_0_0_1; -.
DR InParanoid; Q8SRI6; -.
DR OMA; KVGICYQ; -.
DR OrthoDB; 514396at2759; -.
DR Proteomes; UP000000819; Chromosome VII.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; 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; 1.10.287.600; -; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 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; PTHR11588; 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; SSF52490; SSF52490; 1.
DR SUPFAM; SSF55307; SSF55307; 1.
DR PROSITE; PS00227; TUBULIN; 1.
DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..441
FT /note="Tubulin alpha chain"
FT /id="PRO_0000048167"
FT BINDING 139..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 441
FT /note="Involved in polymerization"
FT /evidence="ECO:0000250"
SQ SEQUENCE 441 AA; 49315 MW; 1195C73B376A6856 CRC64;
MREIISLHIG QAGVQIGNAC WELYCKEHGI LPNGQLDQNK MDDESAESFF SPTSVGTYVP
RTLMVDLEPG VLDSIKTGKY RELYHPGQLI SGKEDAANNY ARGHYTVGKE IIEPAMEQIR
RMADSCDGLQ GFLIYHSFGG GTGSGFASLM MDRLAAEFGK KSKLEFSVYP APKIATAVVE
PYNSILTTHT TLDYSDCSFL VDNEAIYDMC RNLGIQRPYY TDINRVIAQV VSSITASLRF
PGSLNVDLTE FQTNLVPYPR IHFPLVAYSP MLSKEKAAHE KLSVQEITNA CFEPQNQMVR
CDTRKGKYMA CCLLFRGDVN PKEANNATAN VKAKRTNQFV EWCPTGFKVG INSRKPTVLD
GEAMAEVSRA VCALSNTTAI SEAWKRLNNK FDLMFSKRAF VHWYVGEGME EGEFSEARED
LAMLEDDYER ISSNAEPVDE Y