TBA_AJECA
ID TBA_AJECA Reviewed; 418 AA.
AC P53371;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Tubulin alpha chain;
DE Flags: Fragment;
GN Name=TUB1;
OS Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=5037;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26032 / G217B;
RX PubMed=2614394; DOI=10.1099/00221287-135-7-1817;
RA Harris G.S., Keath E.J., Medoff J.;
RT "Characterization of alpha and beta tubulin genes in the dimorphic fungus
RT Histoplasma capsulatum.";
RL J. Gen. Microbiol. 135:1817-1832(1989).
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; M28358; AAA61688.1; -; Genomic_DNA.
DR PIR; A45794; A45794.
DR AlphaFoldDB; P53371; -.
DR SMR; P53371; -.
DR PRIDE; P53371; -.
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; 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.
PE 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT CHAIN 1..>418
FT /note="Tubulin alpha chain"
FT /id="PRO_0000048132"
FT BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT NON_TER 418
SQ SEQUENCE 418 AA; 46608 MW; FEAE372D37222817 CRC64;
MREVVSLNVG QAGGQIANSC WELYCLEHGI QPDGYLTEER KAADPDQGFN TFFSETGQGK
YVPRTIYCDL EPNVVDEVRT GPYRALFHPE QMITGKEDAS NNYARGHYTV GKEMIDQCLD
KVRRVADNCS GLQGFLVFHS FGGGQGSGFG ALLMERLSVD YGKKTKLEFC VYPAPQNATS
VVEPYNSILT THTTLEHSDV QFMVDNEAIY DICRRNLGIE RPSYENSNRL MAQGQSPITA
IMLLFDCALN VDLNEFQTNL VPYPRIHFPL ASYSPVVSAG KASHESNSVM EVTIVCFEPN
NQMVKCDPRN GKYMATCLLY RGDVVPKDVH AVAATLKTKR TVQFVDLQPT GFKIGICYQP
PTMVPNGDLA KVNRACMLSN TTAISEAWTA LSHKFDLIYS KRAFVHWYVG EGMEEGEF
