TBB_PHYCI
ID TBB_PHYCI Reviewed; 444 AA.
AC O59837;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Tubulin beta chain;
DE AltName: Full=Beta-tubulin;
OS Phytophthora cinnamomi (Cinnamon fungus).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4785;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 200982 / H1000 / 6Br / DAR 52646;
RX AGRICOLA=IND20633136;
RA Weerakoon N.D., Roberts J.K., Lehnen L.P. Jr., Wilkinson J.M.,
RA Marshall J.S., Hardham A.R.;
RT "Isolation and characterization of the single beta-tubulin gene in
RT Phytophthora cinnamomi.";
RL Mycologia 90:85-95(1998).
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; U22050; AAC05441.1; -; Genomic_DNA.
DR AlphaFoldDB; O59837; -.
DR SMR; O59837; -.
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..444
FT /note="Tubulin beta chain"
FT /id="PRO_0000048308"
FT BINDING 140..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 444 AA; 49922 MW; 8392C8C288378929 CRC64;
MRELVHIQGG QCGNQIGAKF WEVISDEHGV DPTGSYHGDS DLQLERINVY YNEATGGRYV
PRAILMDLEP GTMDSVRAGP YGQLFRPDNF VFGQTGAGNN WAKGHYTEGA ELIDSVLDVV
RKEAESCDCL QGFQITHSLG GGTGSGMGTL LISKIREEYP DRIMCTYSVC PSPKVSDTVV
EPYNATLSVH QLVENADEVM CLDNEALYDI CFRTLKLTNP TYGDLNHLVC AAMSGITTCL
RFPGQLNSVL KLFAVNLIPF PRLHFFMIGF APLTSRGSQQ YRALTVPELT QQQFDAKNMM
CAADPRHGRY LTAACMFRGR MSTKEVDEQM LNVQNKNSSY FVEWIPNNIK ASVCDIPPQG
LKMSTTFIGN STAIQEMFKR VSEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDGTA EEEGEFDEDE EWMR
