TBA_COLOR
ID TBA_COLOR Reviewed; 454 AA.
AC Q9C413; A0A484FW37; N4VQM2;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Tubulin alpha chain;
DE AltName: Full=Alpha-tubulin;
GN Name=TUB1; ORFNames=Cob_05533, Cob_v004984;
OS Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS lagenarium).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum orbiculare species complex.
OX NCBI_TaxID=1213857;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422;
RX PubMed=11686676; DOI=10.1006/fgbi.2001.1293;
RA Takano Y., Oshiro E., Okuno T.;
RT "Microtubule dynamics during infection-related morphogenesis of
RT Colletotrichum lagenarium.";
RL Fungal Genet. Biol. 34:107-121(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422;
RX PubMed=23252678; DOI=10.1111/nph.12085;
RA Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT stage shift of Colletotrichum fungi.";
RL New Phytol. 197:1236-1249(2013).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422;
RX PubMed=30893003; DOI=10.1094/mpmi-12-18-0352-a;
RA Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA Shirasu K.;
RT "Genome sequence resources for four phytopathogenic fungi from the
RT Colletotrichum orbiculare species complex.";
RL Mol. Plant Microbe Interact. 32:1088-1090(2019).
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 (By similarity).
CC {ECO:0000250}.
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; AF321052; AAK11178.1; -; Genomic_DNA.
DR EMBL; KB725738; ENH86182.1; -; Genomic_DNA.
DR EMBL; AMCV02000011; TDZ21951.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9C413; -.
DR SMR; Q9C413; -.
DR STRING; 1213857.Q9C413; -.
DR PRIDE; Q9C413; -.
DR EnsemblFungi; ENH86182; ENH86182; Cob_05533.
DR eggNOG; KOG1376; Eukaryota.
DR HOGENOM; CLU_015718_0_0_1; -.
DR OrthoDB; 514396at2759; -.
DR Proteomes; UP000014480; Unassembled WGS sequence.
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;
KW Reference proteome.
FT CHAIN 1..454
FT /note="Tubulin alpha chain"
FT /id="PRO_0000048174"
FT BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 454
FT /note="Involved in polymerization"
FT /evidence="ECO:0000250"
FT CONFLICT 279..280
FT /note="AS -> GF (in Ref. 1; AAK11178)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="Missing (in Ref. 1; AAK11178)"
FT /evidence="ECO:0000305"
FT CONFLICT 389..390
FT /note="IA -> MP (in Ref. 1; AAK11178)"
FT /evidence="ECO:0000305"
FT CONFLICT 395..398
FT /note="RLDH -> KTGIT (in Ref. 1; AAK11178)"
FT /evidence="ECO:0000305"
FT CONFLICT 404..405
FT /note="YS -> SA (in Ref. 1; AAK11178)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 454 AA; 50266 MW; 6A685BFC14642AC0 CRC64;
MKGEILHLHL GQAGTQLGNS AWELYLLEHG LGHDGRPDPS AKDVVDGGSY ETFFTETSNG
KYVPRSLFVD LDPSPIDEIR TGGYRQLFHP ELLISGKEDA ANNYARGHYT IGKEMVDNVI
DRIRRVADNC HSLQGFLIFH SFGGGTGSGF GALLLERLST EYGKKSKLEF AVYPAPRVST
AVVEPYNAVL STHSTIENSD CTFLVDNEAV YDICRRNLDI PRPSYDHLNR LIAQVVSSIT
SSLRFDGALN VDLNEFQTNL VPYPRIHYPL ISYAPVISAS KSAHESFKVQ ELTFQCFEPN
NQMVVCDPRN GKYMAVALLY RGDAVPRDCN AAIAALKAKS SFNLVEWCPT GFKLGINYQK
PMAVPAAPGD GGLAPVDRSV SMLSNTTAIA EAWSRLDHKF DLMYSKRAFV HWYVGEGMEE
GEFSEAREDL AALEKDYEEV AADSYEGDEG EAEY
