TBA_SORMK
ID TBA_SORMK Reviewed; 449 AA.
AC Q92335; D1Z927; F7W9K4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Tubulin alpha chain;
GN Name=TUBA; ORFNames=SMAC_08161;
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RA Poeggeler S., Nowrousian M., Jacobsen S., Kueck U.;
RT "An efficient procedure to isolate fungal genes from an indexed cosmid
RT library.";
RL J. Microbiol. Methods 29:49-61(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S.,
RA Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
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; Z70290; CAA94304.1; -; Genomic_DNA.
DR EMBL; CABT02000053; CCC13995.1; -; Genomic_DNA.
DR RefSeq; XP_003351146.1; XM_003351098.1.
DR AlphaFoldDB; Q92335; -.
DR SMR; Q92335; -.
DR STRING; 771870.Q92335; -.
DR EnsemblFungi; CCC13995; CCC13995; SMAC_08161.
DR GeneID; 10808725; -.
DR KEGG; smp:SMAC_08161; -.
DR VEuPathDB; FungiDB:SMAC_08161; -.
DR eggNOG; KOG1376; Eukaryota.
DR HOGENOM; CLU_015718_1_0_1; -.
DR InParanoid; Q92335; -.
DR OMA; KVGICYQ; -.
DR OrthoDB; 514396at2759; -.
DR Proteomes; UP000001881; 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; IPR013838; Beta-tubulin_BS.
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..449
FT /note="Tubulin alpha chain"
FT /id="PRO_0000048227"
FT BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 449
FT /note="Involved in polymerization"
FT /evidence="ECO:0000250"
FT CONFLICT 186..188
FT /note="NSI -> HNF (in Ref. 1; CAA94304)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="H -> N (in Ref. 1; CAA94304)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="H -> Q (in Ref. 1; CAA94304)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="R -> G (in Ref. 1; CAA94304)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="T -> S (in Ref. 1; CAA94304)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="D -> V (in Ref. 1; CAA94304)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="R -> A (in Ref. 1; CAA94304)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 449 AA; 49980 MW; 9642CD388F1A1A10 CRC64;
MREIISLNVG QAGCQIANSC WELYCLEHGI QPDGYLTEER KAADPDHGFS TFFSETGNGK
YVPRTIYADL EPNVIDEVRT GAYRGLFHPE HMISGKEDAS NNYARGHYTV GKELIDQVLD
KVRRVADNCS GLQGFLVFHS FGGGTGSGFG ALLMERLSVD YGKKSKLEFC VYPAPQTATS
VVEPYNSILT THTTLEHADC SFMVDNEAIY DICRRNLGLE RPNYENLNRL IAQVVSSITA
SLRFDGSLNV DLNEFQTNLV PYPRIHFPLV AYAPVISAAK AAHEANSVQE MTMSCFEPNN
QMVKCDPRHG KYMATCLLYR GDVVPNDAHA AVATLKTKRT IQFVDWCPTG FKLGICYQPP
HQVPNGDLAK VNRAVCMLSN TTAIAEAWSA LSSKFDLMYS KRAFVHWYVG EGMEEGEFSE
AREDLAALER DYEEVAADSM EGEEVEAEY
