RUB1_BRANA
ID RUB1_BRANA Reviewed; 546 AA.
AC P21239;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=RuBisCO large subunit-binding protein subunit alpha, chloroplastic;
DE AltName: Full=60 kDa chaperonin subunit alpha;
DE AltName: Full=CPN-60 alpha;
DE Flags: Precursor; Fragment;
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Westar;
RX PubMed=1979547; DOI=10.1016/0378-1119(90)90385-5;
RA Martel R., Cloney L.P., Pelcher L.E., Hemmingsen S.M.;
RT "Unique composition of plastid chaperonin-60: alpha and beta polypeptide-
RT encoding genes are highly divergent.";
RL Gene 94:181-187(1990).
CC -!- FUNCTION: This protein binds RuBisCO small and large subunits and is
CC implicated in the assembly of the enzyme oligomer.
CC -!- SUBUNIT: Oligomer of probably six alpha and six beta subunits.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- MISCELLANEOUS: This protein shows ATPase activity.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR EMBL; M35599; AAA32979.1; -; mRNA.
DR PIR; PW0005; PW0005.
DR AlphaFoldDB; P21239; -.
DR SMR; P21239; -.
DR PRIDE; P21239; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR CDD; cd03344; GroEL; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR HAMAP; MF_00600; CH60; 1.
DR InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR InterPro; IPR001844; Cpn60/GroEL.
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 Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00298; CHAPERONIN60.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 2.
DR TIGRFAMs; TIGR02348; GroEL; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Chloroplast; Nucleotide-binding; Phosphoprotein;
KW Plastid; Transit peptide.
FT TRANSIT <1..6
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 7..546
FT /note="RuBisCO large subunit-binding protein subunit alpha,
FT chloroplastic"
FT /id="PRO_0000005017"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21238"
FT NON_TER 1
SQ SEQUENCE 546 AA; 57692 MW; 20AFD8EE4FD602AF CRC64;
RFSVRANVKE ISFDQSSRAA LQAGIDKLAD AVGLTLGPRG RNVVLDEFGS PKVVNDGVTI
ARAIELPDAM ENAGAALIRE VASKTNDSAG DGTTTASVLA REIIKHGLLS VTSGANPVSL
KRGIDKTVQA LIEELEKRAR PVKGGSDIKA VATISAGNDE LVGTMIADAI DKVGPDGVLS
IESSSSFETT VEVEEGMEID RGYISPQFVT NPEKLLVEFE NARVLITDQK ITAIKDIIPI
LEKTTQLRAP LLIIAEDVTG EALATLVVNK LRGVLNVVAV KAPGFGERRK AMLQDIAILT
GAEYQALDMG LLVENTTIDQ LGIARKVTIS KDSTTLIADA ASKDELQARI SQLKKELSET
DSVYDSEKLA ERIAKLAGGV AVIKVGAATE TELEDRKLRI EDAKNATFAA IEEGIVPGGG
ATLVHLSTVI PAIKEKLEDA DERLGADIVQ KALVAPAALI AQNAGIEGEV VVEKIMFSEW
EIGYNAMTDT YENLLEAGVI DPAKVTRCAL QNAASVAGMV LTTQAIVVDK PKPKAPTAAP
PQGLMV
