ID   TBAA_SCHCO              Reviewed;         448 AA.
AC   P49741;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Tubulin alpha-1A chain;
GN   Name=TUB-1A;
OS   Schizophyllum commune (Split gill fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX   NCBI_TaxID=5334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 44201 / CBS 340.81 / UVM 4-40 / 4-40;
RA   Pukki H.K., Juuti J.T., Raudaskoski M.;
RL   Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
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; X86079; CAA60034.1; -; Genomic_DNA.
DR   AlphaFoldDB; P49741; -.
DR   SMR; P49741; -.
DR   PRIDE; P49741; -.
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..448
FT                   /note="Tubulin alpha-1A chain"
FT                   /id="PRO_0000048223"
FT   BINDING         141..147
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   SITE            448
FT                   /note="Involved in polymerization"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   448 AA;  49445 MW;  919CDA74C903C1C9 CRC64;
     MREVVSIHVG QAGVQIGNAC WELYTIEHGL SPDGRLSDDS PSKHDDGFST FFSETSSGKY
     VPRSLYVDLE PNVIDEVRNG PYRSLFHPET MITGKEDAAS NYARGHYTIG KEQIDVVMDK
     VRRLVDNCNG LQGFFVFHSF GGGTGSGFGA LILERLSTDY GKKSKLEFSV YPAPTLASSV
     VEPYNSVLTT HTTLEHSDCS FMVDNEAIYD ICKKNLNIAQ PGLTNLNRLI AQVVSSITAS
     LRFDGSLNVD LNEFQTNLVP FPRIHFPLAT LAPIVSVDKA GHESNSVAEM TYSCFEPGNQ
     MVKCDPRDGK YMACALLYRG DVVPKDTNAA VALIKTKRTI QFVDWCPTGF KLGICNEPPA
     HVPGGDLAKV KRSMCMLSNT TAISSAWSRL DHKFDLLYSK RAFVHWYVGE GMEEGEFSEA
     RQDLAALEKD YEEVGMDSAD AEEEAAEY