(data stored in ACNUC9399 zone)

HOGENOM: GUITH_1_PE11

ID   GUITH_1_PE11                         STANDARD;      PRT;   529 AA.
AC   GUITH_1_PE11; O78419;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=60 kDa chaperonin, chloroplastic;AltName: Full=Protein
DE   Cpn60;AltName: Full=groEL protein; (GUITH_1.PE11).
GN   Name=groL; Synonyms=groEL;
OS   GUILLARDIA THETA.
OG   Plastid:Chloroplast.
OC   Eukaryota; Cryptophyta; Pyrenomonadales; Geminigeraceae; Guillardia.
OX   NCBI_TaxID=55529;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS GUITH_1.PE11.
CC       Guillardia theta chloroplast, complete sequence.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:CH60_GUITH
CC   -!- FUNCTION: Prevents misfolding and promotes the refolding and
CC       proper assembly of unfolded polypeptides generated under stress
CC       conditions (By similarity).
CC   -!- SUBUNIT: Oligomer of 14 subunits composed of two stacked rings of
CC       7 subunits (By similarity).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC   -!- GENE_FAMILY: HOG000076290 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; O78419; -.
DR   EMBL; AF041468; AAC35604.1; -; Genomic_DNA.
DR   RefSeq; NP_050670.1; NC_000926.1.
DR   ProteinModelPortal; O78419; -.
DR   SMR; O78419; 2-529.
DR   GeneID; 856959; -.
DR   GenomeReviews; AF041468_GR; groL.
DR   OMA; KLEMLGT; -.
DR   ProtClustDB; CHL00093; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR   HAMAP; MF_00600; CH60; 1; -.
DR   InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR   InterPro; IPR001844; Chaprnin_Cpn60.
DR   InterPro; IPR002423; Cpn60/TCP-1.
DR   PANTHER; PTHR11353; Cpn60/TCP-1; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00298; CHAPERONIN60.
DR   SUPFAM; SSF48592; GroEL-ATPase; 1.
DR   TIGRFAMs; TIGR02348; GroEL; 1.
DR   PROSITE; PS00296; CHAPERONINS_CPN60; 1.
DR   HOGENOMDNA; GUITH_1.PE11; -.
KW   AAC35604.1000028595old_1320000031;
KW   60 kDa chaperonin, chloroplastic ;
KW   ATP-binding; Chaperone; Chloroplast; Nucleotide-binding; Plastid.
SQ   SEQUENCE   529 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSKIILYQED ARRALERGMD ILAEAVSVTL GPKGRNVVLE RKYGAPQIVN DGVTIAKEIE
     LEDHIENTGV ALIRQAASKT NDVAGDGTTT ATVLAHAMVK QGMKNVAAGA NAIALKRGIE
     KATQFIVTQI AEYARPVEDT RAISQVASIS AGNDIETGKM IADAIDKVGR EGVISLEEGK
     STITELEMTE GMCFEKGFIS PYFVTDTERM EVIQDNPYIL LTDKKITLVQ QELLPTLELI
     SKTSRPLVII AEDVEKEALA TLVVNKLRGI VNVVAVRAPG FGDRRKAMLE DIAILTGGQV
     ISEDAGFSLE TLTLDMLGQA RRITITKENT TIIAEGNEKD VKSRCEQIRR QIEASDSSYE
     REKLQERLAK LAGGVAVIKV GAATETEMKD KKLRLEDAIN ATKAAVEEGI VPGGGSTLTH
     LANDLKDWAE DNLIEDELIG ALIVERSLTS PLRRIIENTG QNSAIIIEQI KESEFNIGYD
     AAKGEIVDMY DVGIIDPAKV TRSGLQNAAS IASMILTTEC IVVDKQDEK
//

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