TBB_PHANO
ID TBB_PHANO Reviewed; 447 AA.
AC P41799; Q0UN73; Q0UN74; Q5S3J6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Tubulin beta chain;
DE AltName: Full=Beta-tubulin;
GN Name=tubB; Synonyms=tubA; ORFNames=SNOG_06790, SNOG_06791;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF MUTANT TUBAR, AND VARIANT ARG-124.
RC STRAIN=BSm300;
RX PubMed=8455567; DOI=10.1007/bf00282784;
RA Cooley R.N., Caten C.E.;
RT "Molecular analysis of the Septoria nodorum beta-tubulin gene and
RT characterization of a benomyl-resistance mutation.";
RL Mol. Gen. Genet. 237:58-64(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=9074, 98-12981, ATCC 200805 / S-82-13, ATCC 200806 / S-74-20A,
RC S-80-301, Sn26-1, Sn27-1, Sn37-1, and Sn48-1;
RX PubMed=15972251; DOI=10.1016/j.femsle.2005.05.049;
RA Malkus A., Reszka E., Chang C.-J., Arseniuk E., Chang P.-F.L., Ueng P.P.;
RT "Sequence diversity of beta-tubulin (tubA) gene in Phaeosphaeria nodorum
RT and P. avenaria.";
RL FEMS Microbiol. Lett. 249:49-56(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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 -!- SEQUENCE CAUTION:
CC Sequence=EAT85442.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAT85442.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; S56922; AAB25800.1; -; Genomic_DNA.
DR EMBL; AY786331; AAV53378.1; -; Genomic_DNA.
DR EMBL; AY786332; AAV53379.1; -; Genomic_DNA.
DR EMBL; AY786334; AAV53381.1; -; Genomic_DNA.
DR EMBL; AY786335; AAV53382.1; -; Genomic_DNA.
DR EMBL; AY786336; AAV53383.1; -; Genomic_DNA.
DR EMBL; AY786337; AAV53384.1; -; Genomic_DNA.
DR EMBL; AY786338; AAV53385.1; -; Genomic_DNA.
DR EMBL; AY786339; AAV53386.1; -; Genomic_DNA.
DR EMBL; AY823526; AAV83496.1; -; Genomic_DNA.
DR EMBL; CH445334; EAT85442.2; ALT_SEQ; Genomic_DNA.
DR PIR; S30254; S30254.
DR RefSeq; XP_001797153.1; XM_001797101.1.
DR AlphaFoldDB; P41799; -.
DR SMR; P41799; -.
DR STRING; 321614.P41799; -.
DR PRIDE; P41799; -.
DR GeneID; 5974043; -.
DR KEGG; pno:SNOG_06791; -.
DR InParanoid; P41799; -.
DR OrthoDB; 962471at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..447
FT /note="Tubulin beta chain"
FT /id="PRO_0000048425"
FT REGION 425..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..447
FT /note="Acidic residues"
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 VARIANT 124
FT /note="A -> R (in strain: BSm300)"
FT /evidence="ECO:0000269|PubMed:8455567"
FT MUTAGEN 6
FT /note="H->Y: In tubAR; causes resistance to benomyl."
FT CONFLICT 230
FT /note="S -> Y (in Ref. 3; EAT85442)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="T -> P (in Ref. 3; EAT85442)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="P -> H (in Ref. 3; EAT85442)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 447 AA; 49827 MW; 7A2F557B40ECE319 CRC64;
MREIVHLQTG QCGNQIGAAF WQTISGEHGL DGSGVYNGTS DLQLERMNVY FNEASGNKFV
PRAVLVDLEP GTMDAVRAGP FGQLFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDQVLDVV
RREAEGCDCL QGFQITHSLG GGTGAGMGTL LISKIREEFP DRMMATFSVV PSPKVSDTVV
EPYNATLSIH QLVENSDETF CIDNEALYDI CMRTLKLNNP SYGDLNHLVS AVMSGVTTCL
RFPGQLNSDL RKLAVNMVPF PRLHFFMVGF APLTSRGAHS FRAVTVPELT QQMFDPKNMM
AASDFRNGRY LTCSAYFRGK VSMKEVEDQM RNVQNKNSSY FVEWIPNNVQ TALCSVPPRG
LKMSATFVGN STSIQELFKR IGDQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQEASI SEGEEEYDEE APLEAEE
