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TBG_ENCCU
ID   TBG_ENCCU               Reviewed;         434 AA.
AC   Q8SRD2;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Tubulin gamma chain;
DE   AltName: Full=Gamma-tubulin;
GN   Name=TUB4; OrderedLocusNames=ECU08_0670;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. The gamma
CC       chain is found at microtubule organizing centers (MTOC) such as the
CC       spindle poles or the centrosome, suggesting that it is involved in the
CC       minus-end nucleation of microtubule assembly (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, spindle pole body {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; AL590448; CAD26372.1; -; Genomic_DNA.
DR   RefSeq; NP_597196.1; NM_001041805.1.
DR   AlphaFoldDB; Q8SRD2; -.
DR   SMR; Q8SRD2; -.
DR   STRING; 284813.Q8SRD2; -.
DR   GeneID; 859618; -.
DR   KEGG; ecu:ECU08_0670; -.
DR   VEuPathDB; MicrosporidiaDB:ECU08_0670; -.
DR   HOGENOM; CLU_015718_1_0_1; -.
DR   InParanoid; Q8SRD2; -.
DR   OMA; EHGINKE; -.
DR   OrthoDB; 687389at2759; -.
DR   Proteomes; UP000000819; Chromosome VIII.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0000930; C:gamma-tubulin complex; IEA:InterPro.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005816; C:spindle pole body; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR   GO; GO:0007020; P:microtubule nucleation; IEA:InterPro.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   CDD; cd02188; gamma_tubulin; 1.
DR   Gene3D; 1.10.287.600; -; 1.
DR   Gene3D; 3.30.1330.20; -; 1.
DR   Gene3D; 3.40.50.1440; -; 1.
DR   InterPro; IPR002454; Gamma_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; PR01164; GAMMATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 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..434
FT                   /note="Tubulin gamma chain"
FT                   /id="PRO_0000048457"
FT   BINDING         135..141
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   434 AA;  48240 MW;  E494B68A9AB8B2DA CRC64;
     MREVVTLQVG QCGNQMGAEF WKTLCKEHGI SMCGVLQDSR DLGDRKDVFF YQADDNVFVP
     RAILVDLEPR VISQAPSFFS QESIFLSNEG GGAGNNWGHG YCVGKAMGND VIDMIQREAE
     GCDALETFLL LHSIAGGTGS GFGSLLLERI KEEFPKKIVQ TYSIFPNNDE SSDVVVQPYN
     SVLTLHRLIE NSDCIVVMDN SSLGRYTLDS LRIGTPTFDH INLLISTVMA ASTSTIRFPG
     YMYCTHQSIN NCLVPLDPLK FVVPSYTPFV CDEMSRVVRK ATCSDVMRRL LLPKTRLAGY
     EQTKAQSVVS MLNILHGVED SGEVSRTVMR FLDKGMVNFV PWMPPSFNVA LGKCIANETR
     PSRVSGLSLT NSTGASLILS KISGQFDKLR KQRAFLDIYK RFGVEPEMFD EGKEIVQKAL
     EEYHSAEMAA YPNH
 
 
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