TBB_AJECA
ID TBB_AJECA Reviewed; 445 AA.
AC P41742;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Tubulin beta chain;
DE AltName: Full=Beta-tubulin;
GN Name=TUB2;
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; L39132; AAA61689.1; -; Genomic_DNA.
DR PIR; B45794; B45794.
DR AlphaFoldDB; P41742; -.
DR SMR; P41742; -.
DR PRIDE; P41742; -.
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; IPR013838; Beta-tubulin_BS.
DR InterPro; IPR002453; Beta_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; PR01163; BETATUBULIN.
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.
DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT CHAIN 1..445
FT /note="Tubulin beta chain"
FT /id="PRO_0000048392"
FT BINDING 140..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 445 AA; 50176 MW; 0D0575F7AE13DBE9 CRC64;
MREIVHLQTG QCGNQIGAAF WQTISGEHGV DGAGYYNGSL DIQLERMNVY FNEAAEKKYV
PRAVLVDLEP GTMDSVRAGP FGQLFRPDNF VFVQSGAGNT WAKGHYTEGS ELVDQVIDVV
RREAERCDCL QGFQIIHSLG GGTGAGMGTL LISKIREEFP DRMMATFSSV VPSPKVSDTV
VEPYNATLSN HQLVENSDET FCIDNEALYD ICMRTLKLSE PSYGDLNHLV SAVMSGVTTC
LRFPGQLNSD LRKLAVNMVP FPRLHFFMVG FAPLTSRGAY SFRVVTVPEL TQKMYDPKNM
MCLLDFRNGR YLTASAIFRG KVSMKEVEDQ MRNVQNKNHT YFVEWIPNNV QTALCSIPPR
GLKMSSTFVE NSTAIQELFK RVGDQFTAMF RRKAFLHWYT GEGMDEMEFT EAESNMNDLV
SEYQQYQDAS ISEGEDEYFD YAWAM
