TBB_PNECA
ID TBB_PNECA Reviewed; 442 AA.
AC P24637;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Tubulin beta chain;
DE AltName: Full=Beta-tubulin;
GN Name=TUB-B;
OS Pneumocystis carinii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Pneumocystidomycetes; Pneumocystidaceae; Pneumocystis.
OX NCBI_TaxID=4754;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1584027; DOI=10.1111/j.1365-2958.1992.tb02165.x;
RA Dyer M., Volpe F., Delves C.J., Somia N., Burns S., Scaife J.G.;
RT "Cloning and sequence of a beta-tubulin cDNA from Pneumocystis carinii:
RT possible implications for drug therapy.";
RL Mol. Microbiol. 6:991-1001(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=1484490; DOI=10.1111/j.1365-2958.1992.tb02204.x;
RA Edlind T.D., Bartlett M.S., Weinberg G.A., Prah G.N., Smith J.W.;
RT "The beta-tubulin gene from rat and human isolates of Pneumocystis
RT carinii.";
RL Mol. Microbiol. 6:3365-3373(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 96-208.
RX PubMed=8325503; DOI=10.1016/0378-1119(93)90265-5;
RA Fletcher L.D., Berger L.C., Peel S.A., Baric R.S., Tidwell R.R.,
RA Dykstra C.C.;
RT "Isolation and identification of six Pneumocystis carinii genes utilizing
RT codon bias.";
RL Gene 129:167-174(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X62113; CAA44023.1; -; mRNA.
DR EMBL; L05466; AAA33786.1; -; Genomic_DNA.
DR EMBL; M96932; AAA02566.1; -; Unassigned_DNA.
DR PIR; S20908; S20908.
DR AlphaFoldDB; P24637; -.
DR SMR; P24637; -.
DR IntAct; P24637; 1.
DR MINT; P24637; -.
DR PRIDE; P24637; -.
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 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT CHAIN 1..442
FT /note="Tubulin beta chain"
FT /id="PRO_0000048427"
FT BINDING 140..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 442 AA; 49118 MW; 9A26706E1B6487F7 CRC64;
MREIVHLQTG QCGNQIGASF WSTISGEHGL DSTGVYQGTS DLQLERMNVY FNEASGGKYV
PRSILIDLEP GTMDAVRSGP FGNLFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
RREAEACDCL QGFQITHSLG GGTGAGMGTL LISKIREEYP DRMMATFSVV PSPKVSDTVV
EPYNATLSVH QLVENSDETF CIDNEALYDI CMRTLKLPDP GYGDLNHLVS AVMSGITTCL
RFPGQLNSDL RKLAVNMVPF PRLHFFIVGF APLTSKGSHS FRSLTVPELT QQMFDAKNMM
AASDPRHGRY LTVAAIFRGR VSMKEVEDQM HSVQQKNSSY FVEWIPNNVQ TALCSIPPRG
LKMSSTFIGN STSIQELFKR VGDQFSAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYEIAGV DEEVELDDEI ET