位置:首页 > 蛋白库 > TBA2_NEUCR
TBA2_NEUCR
ID   TBA2_NEUCR              Reviewed;         449 AA.
AC   P38669; Q7RVI2;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Tubulin alpha-B chain;
GN   Name=tba-2; ORFNames=B10K17.080, NCU09468;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=74-ORS-6a / FGSC 4200;
RX   PubMed=9163903; DOI=10.1111/j.1574-6968.1997.tb10346.x;
RA   Monnat J., Ortega Perez R., Turian G.;
RT   "Molecular cloning and expression studies of two divergent alpha-tubulin
RT   genes in Neurospora crassa.";
RL   FEMS Microbiol. Lett. 150:33-41(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; X79404; CAA55941.1; -; mRNA.
DR   EMBL; BX842596; CAE75716.1; -; Genomic_DNA.
DR   EMBL; CM002237; EAA33987.1; -; Genomic_DNA.
DR   PIR; S45051; S45051.
DR   RefSeq; XP_963223.1; XM_958130.3.
DR   AlphaFoldDB; P38669; -.
DR   SMR; P38669; -.
DR   STRING; 5141.EFNCRP00000009282; -.
DR   PRIDE; P38669; -.
DR   EnsemblFungi; EAA33987; EAA33987; NCU09468.
DR   GeneID; 3879371; -.
DR   KEGG; ncr:NCU09468; -.
DR   VEuPathDB; FungiDB:NCU09468; -.
DR   HOGENOM; CLU_015718_1_0_1; -.
DR   InParanoid; P38669; -.
DR   OMA; KVGICYQ; -.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005819; C:spindle; 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:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0000280; P:nuclear division; IBA:GO_Central.
DR   GO; GO:0098863; P:nuclear migration by microtubule mediated pushing forces; 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; 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   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..449
FT                   /note="Tubulin alpha-B chain"
FT                   /id="PRO_0000048200"
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        60..62
FT                   /note="KYV -> NTF (in Ref. 1; CAA55941)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        197..198
FT                   /note="HA -> QRR (in Ref. 1; CAA55941)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        367..373
FT                   /note="DLAKVNR -> RSGPRLTD (in Ref. 1; CAA55941)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        391..395
FT                   /note="LSSKF -> SFVQV (in Ref. 1; CAA55941)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   449 AA;  49966 MW;  9642CD388F1BAA10 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 EGEDVEAEY
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024