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THSG_SACS2
ID   THSG_SACS2              Reviewed;         535 AA.
AC   Q9V2T7;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Thermosome subunit gamma;
DE   AltName: Full=Chaperonin subunit gamma;
DE   AltName: Full=Thermosome subunit 3;
GN   Name=thsC; Synonyms=thsG; OrderedLocusNames=SSO3000;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=10508614; DOI=10.1016/s0960-9822(99)80457-6;
RA   Archibald J.M., Logsdon J.M. Jr., Doolittle W.F.;
RT   "Recurrent paralogy in the evolution of archaeal chaperonins.";
RL   Curr. Biol. 9:1053-1056(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
CC   -!- FUNCTION: Molecular chaperone; binds unfolded polypeptides in vitro,
CC       and has a weak ATPase activity. {ECO:0000250}.
CC   -!- SUBUNIT: Forms a Heterooligomeric complex of two stacked eight-membered
CC       rings. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK43104.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF149921; AAF03362.1; -; Genomic_DNA.
DR   EMBL; AE006641; AAK43104.1; ALT_INIT; Genomic_DNA.
DR   PIR; A99481; A99481.
DR   RefSeq; WP_009992650.1; NC_002754.1.
DR   AlphaFoldDB; Q9V2T7; -.
DR   SMR; Q9V2T7; -.
DR   DIP; DIP-61908N; -.
DR   IntAct; Q9V2T7; 1.
DR   STRING; 273057.SSO3000; -.
DR   EnsemblBacteria; AAK43104; AAK43104; SSO3000.
DR   GeneID; 44128725; -.
DR   KEGG; sso:SSO3000; -.
DR   PATRIC; fig|273057.12.peg.3093; -.
DR   eggNOG; arCOG01257; Archaea.
DR   HOGENOM; CLU_008891_9_1_2; -.
DR   InParanoid; Q9V2T7; -.
DR   OMA; RYCRIEK; -.
DR   PhylomeDB; Q9V2T7; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   CDD; cd03343; cpn60; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR017998; Chaperone_TCP-1.
DR   InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR   InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR   InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR   InterPro; IPR027413; GROEL-like_equatorial_sf.
DR   InterPro; IPR027410; TCP-1-like_intermed_sf.
DR   InterPro; IPR012714; Thermosome_arc.
DR   PANTHER; PTHR11353; PTHR11353; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00304; TCOMPLEXTCP1.
DR   SUPFAM; SSF48592; SSF48592; 1.
DR   SUPFAM; SSF52029; SSF52029; 1.
DR   SUPFAM; SSF54849; SSF54849; 1.
DR   TIGRFAMs; TIGR02339; thermosome_arch; 1.
DR   PROSITE; PS00750; TCP1_1; 1.
DR   PROSITE; PS00751; TCP1_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..535
FT                   /note="Thermosome subunit gamma"
FT                   /id="PRO_0000128403"
SQ   SEQUENCE   535 AA;  58770 MW;  31AA897DBD19924F CRC64;
     MAYLLREGTQ RSTGNEVILN NIAVAKILLE MLKSSLGPKG LDKMLVEGQD VTITNDGATI
     VKNMEVQHPT AKLLIETAKT VDTEVGDGTT SVVVLAGLLL EKAEDLLNQK IHPTVIIEGY
     RKALNSSLEL LKNIADKISP EDRKIVHDLV YTTLSSKFFS TEHTLEKIIN LVIDASLAVL
     DKRDGSYDLD IKNIKIVKVN GGEFDDSELI NGIVVDKEPT NENMPKRVEN VKVMLADFPL
     KLEKTEISMK LGISDPTQIK GYLDEQTAYV KQMVDKIKAM GVKLFITQKD IDEIASYLMG
     KNGIMALKNV KRSDIELLSR ATGAKIASSM KDANESDLGE AKLVEVRNLG KNKYLFIQSD
     KAKAVTVIIK GSNNMITDEA ERSLNDAFNS IRNLLLEPYI VAGGGAVEEE LAKRLRDDAR
     KVIGKEQLAF NAFADALEEY VSILSETAGM DPISALTEIR HKHATGLKNA GIDVTKARIY
     DNMLELRVID SLKVKEQVLK SATEAATAIL KIDDMIAAAP AKQQPQPQQP NPYLG
 
 
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