TBA_ENCHE
ID TBA_ENCHE Reviewed; 380 AA.
AC P92120;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Tubulin alpha chain;
DE Flags: Fragment;
GN Name=TUB1; Synonyms=ATUB;
OS Encephalitozoon hellem (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=27973;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CDC:0291:V213;
RX PubMed=8952074; DOI=10.1093/oxfordjournals.molbev.a025576;
RA Keeling P.J., Doolittle W.F.;
RT "Alpha-tubulin from early-diverging eukaryotic lineages and the evolution
RT of the tubulin family.";
RL Mol. Biol. Evol. 13:1297-1305(1996).
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; U66908; AAC47418.1; -; Genomic_DNA.
DR AlphaFoldDB; P92120; -.
DR SMR; P92120; -.
DR PRIDE; P92120; -.
DR VEuPathDB; MicrosporidiaDB:EHEL_071170; -.
DR VEuPathDB; MicrosporidiaDB:KMI_08g13440; -.
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; 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.
PE 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT CHAIN <1..>380
FT /note="Tubulin alpha chain"
FT /id="PRO_0000048168"
FT BINDING 117..123
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT NON_TER 1
FT NON_TER 380
SQ SEQUENCE 380 AA; 42480 MW; 1C453FC14491A60F CRC64;
LYCKEHGILP DGRLDQNRMD DESAESFFSQ TSVGTYVPRT LMVDLEPGVL ESIKTGKYRE
LYHPGQLISG KEDAANNYAR GHYTVGKEII EPVMEQIRRM ADNCDGLQGF LIYHSFGGGT
GSGFASLMMD RLAAEFGKKS KLEFSVYPAP KIATAVVEPY NSILTTHTTL DYSDCSFLVD
NEAIYDMCRN LGIQRPYYTD INRIIAQVVS SITASLRFPG SLNVDLTEFQ TNLVPYPRIH
FPLVAYSPML SKEKAAHEKL SVQEITNACF EPQSQMVRCD TRKGKYMACC LLFRGDVNPK
DANTATANVK AKRTNQFVEW CPTGFKVGIN SRKPTVLDGE AMAEVSRAVC ALSNTTAISE
AWKRLNNKFD LMFSKRAFVH
