RUB2_BRANA
ID RUB2_BRANA Reviewed; 583 AA.
AC P34794;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 97.
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;
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 TISSUE=Seed;
RX PubMed=7913240; DOI=10.1104/pp.105.1.453;
RA Cole K.P., Blakeley S.D., Dennis D.T.;
RT "Isolation of a full-length cDNA encoding Brassica napus plastid
RT chaperonin-60 alpha subunit.";
RL Plant Physiol. 105:453-453(1994).
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; Z27222; CAA81736.1; -; mRNA.
DR PIR; S38642; S38642.
DR RefSeq; NP_001303090.1; NM_001316161.1.
DR AlphaFoldDB; P34794; -.
DR SMR; P34794; -.
DR PRIDE; P34794; -.
DR GeneID; 106352579; -.
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; 1.
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..45
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 46..583
FT /note="RuBisCO large subunit-binding protein subunit alpha,
FT chloroplastic"
FT /id="PRO_0000005018"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21238"
SQ SEQUENCE 583 AA; 61606 MW; 9EF92FF521FDB7E9 CRC64;
MATANALSSP SVLCSSRQGK LSGGSQQKGQ RVSYRKANRR FSLRANVKEI AFDQSSRAAL
QAGIDKLADA VGLTLGPRGR NVVLDEFGSP KVVNDGVTIA RAIELPDAME NAGAALIREV
ASKTNDSAGD GTTTASVLAR EIIKHGLLSV TSGANPVSLK RGIDKTVQAL IEELEKRSRP
VKGGRDIKAV ATISAGNDEL IGAMIADAID KVGPDGVSPI ESSSSFETTV EVEEGMEIDR
GYISPQFVTN PEKLLVEFEN ARVLITDQKI TAIKDIIPIL EKTTQLRAPL LIIAEDVTGE
ALATLVVNKL RGVLNVVAVK APGFGERRKA MLQDIAILTE PSTALDMGLL VENTTIDQLG
IARKVTISKD STTLIADAAS KAELQARISQ LKKESFETDS VYDSEKLAER IAKLSGGVAV
IKVGAATETE LEDRKLRIED AKNATFAAIE EGIVPGGGAT LVHLSTVIPA IKETFEDADV
RLGADIVQKA LVAQSLIAQN AGIEGEVVVE KIMFSEWELG YNAMTDTYEN LLEAGVIDPA
KVTRCALQNA ASVAGMVLTT QAIVVDKPKP KAPAAAAPEG LMV
