TBAB_SCHCO
ID TBAB_SCHCO Reviewed; 446 AA.
AC P49742;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Tubulin alpha-1B chain;
GN Name=TUB-1B;
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; X86080; CAA60035.1; -; Genomic_DNA.
DR AlphaFoldDB; P49742; -.
DR SMR; P49742; -.
DR PRIDE; P49742; -.
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..446
FT /note="Tubulin alpha-1B chain"
FT /id="PRO_0000048224"
FT REGION 34..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 446
FT /note="Involved in polymerization"
FT /evidence="ECO:0000250"
SQ SEQUENCE 446 AA; 49363 MW; 9339F965ABEE5A41 CRC64;
MREVISVHVG QAGVQIGNAC WELYTLEHGL SPDGRLMDDS PSKHDSGSTF FSETGQGKHV
PRRLYVDLEP GVIDDVKNGP YRSLFHPETM ITGKEDAANN YARGHYTVGK ELIDPVMDKL
RRLADNCSGR QGLFVFHSFG GGTGSGFGAL LLERLSTDYG KKAKLEFCVY PAPQLSSSVV
EPYNSLLTTH TTLEHSDCSF MVDNEAIYDI CKKNLGVAQP GFTNLNRLIA QVVSSITASL
RFDGSLNVDL NEFQTNLVPF PRIHFPLASY APLLSAPRRQ HEQNSVEEMT FSCFESGNQM
VKCDAKDGKY MACCLLYRGD VVPKDTQAAV ASIKTKRTIQ FVDWCPTGFK LGVCNEAPAT
VPGGDLAKVP RSLCMLSNTT AIAAAWNRLD YKFDLMYRKR AFVHWYVGEA MEEGEFSEAR
EDLAALEKDY EEVGTDSADA EEEGEY
