ID   TBA1_PNECA              Reviewed;         449 AA.
AC   P53372;
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;
GN   Name=TUB1;
OS   Pneumocystis carinii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Pneumocystidomycetes; Pneumocystidaceae; Pneumocystis.
OX   NCBI_TaxID=4754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8422998; DOI=10.1016/0378-1119(93)90553-f;
RA   Zhang J., Stringer J.R.;
RT   "Cloning and characterization of an alpha-tubulin-encoding gene from rat-
RT   derived Pneumocystis carinii.";
RL   Gene 123:137-141(1993).
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; M95294; AAA33783.1; -; Genomic_DNA.
DR   PIR; JU0154; JU0154.
DR   AlphaFoldDB; P53372; -.
DR   SMR; P53372; -.
DR   PRIDE; P53372; -.
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; 2.
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..449
FT                   /note="Tubulin alpha chain"
FT                   /id="PRO_0000048219"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   SITE            449
FT                   /note="Involved in polymerization"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   449 AA;  50383 MW;  B566CF525E5B413E CRC64;
     MREVISIHVG QAGTQIGNAC WELYCLEHGI EPDGRLSPEK TTKPLDDGFS TFFSETGSGK
     YVPRSIYVDL EPNVIDQVRT GTYRHLFHPE QLITGKEDAA NNYARGHYTV GKELIDHVLD
     RIRRVADNCT GLQGFLVFHS FGGGTGSGFG ALLLERLSVD YGKKSKLEFS VYPAPQVSTS
     VVEPYNSILT THTTLEHSDC SFMVDNEAIY DICRRNLDIE RPGYENLNRL IAQVVSSITA
     SLRFDGSLNV DLNEFQTNLV PYPRIHFPLV TYAPLISAAK AHHEANSVAE ITNACFEPNN
     QMVKCDPRNG KYMATCLLYR GDIVTKDVNC AVSSIRTKRT IQFVDWCPTG FKLGVCYQPP
     QYVPNGDLAK VNRAVCMLSN TTSIAEAWSR LDHKFDLMYS KRAFVHWYVG EGMEEGEFSE
     AREDLAALEK DYEEVGQDSI EGEIMEEEY