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Database: UniProt
Entry: Q6RWD8_CAPAN
LinkDB: Q6RWD8_CAPAN
Original site: Q6RWD8_CAPAN 
ID   Q6RWD8_CAPAN            Unreviewed;       180 AA.
AC   Q6RWD8; A0A1U8FWC9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 86.
DE   RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic {ECO:0000256|HAMAP-Rule:MF_00860};
DE            Short=RuBisCO small subunit {ECO:0000256|HAMAP-Rule:MF_00860};
GN   Name=RBCS {ECO:0000256|HAMAP-Rule:MF_00860};
OS   Capsicum annuum (Capsicum pepper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX   NCBI_TaxID=4072 {ECO:0000313|EMBL:AAR83879.1};
RN   [1] {ECO:0000313|EMBL:AAR83879.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kim S., Lee K.-W.;
RT   "Monitoring expression patterns of 2500 hot pepper genes under cold stress
RT   by using full-length cDNA microarray.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC       ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC       fixation, as well as the oxidative fragmentation of the pentose
CC       substrate. Both reactions occur simultaneously and in competition at
CC       the same active site. Although the small subunit is not catalytic it is
CC       essential for maximal activity. {ECO:0000256|HAMAP-Rule:MF_00860,
CC       ECO:0000256|RuleBase:RU003627}.
CC   -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00860, ECO:0000256|RuleBase:RU003627}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, plasmodesma
CC       {ECO:0000256|ARBA:ARBA00024184}. Plastid, chloroplast
CC       {ECO:0000256|HAMAP-Rule:MF_00860}.
CC   -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC       chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO
CC       this homodimer is arranged in a barrel-like tetramer with the small
CC       subunits forming a tetrameric 'cap' on each end of the 'barrel'.
CC       {ECO:0000256|HAMAP-Rule:MF_00860}.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_00860, ECO:0000256|RuleBase:RU003627}.
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DR   EMBL; AY487801; AAR83879.1; -; mRNA.
DR   RefSeq; XP_016560735.1; XM_016705249.1.
DR   RefSeq; XP_016560738.1; XM_016705252.1.
DR   AlphaFoldDB; Q6RWD8; -.
DR   OrthoDB; 5482775at2759; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009506; C:plasmodesma; IEA:UniProtKB-SubCell.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009853; P:photorespiration; IEA:UniProtKB-UniRule.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd03527; RuBisCO_small; 1.
DR   Gene3D; 3.30.190.10; Ribulose bisphosphate carboxylase, small subunit; 1.
DR   HAMAP; MF_00859; RuBisCO_S_bact; 1.
DR   InterPro; IPR024681; RuBisCO_ssu.
DR   InterPro; IPR000894; RuBisCO_ssu_dom.
DR   InterPro; IPR024680; RuBisCO_ssu_N.
DR   InterPro; IPR036385; RuBisCO_ssu_sf.
DR   PANTHER; PTHR31262; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR31262:SF10; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT 1B, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF12338; RbcS; 1.
DR   Pfam; PF00101; RuBisCO_small; 1.
DR   PRINTS; PR00152; RUBISCOSMALL.
DR   SMART; SM00961; RuBisCO_small; 1.
DR   SUPFAM; SSF55239; RuBisCO, small subunit; 1.
PE   2: Evidence at transcript level;
KW   Calvin cycle {ECO:0000256|ARBA:ARBA00022567, ECO:0000256|HAMAP-
KW   Rule:MF_00860};
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_00860}; Chloroplast {ECO:0000256|HAMAP-Rule:MF_00860};
KW   Photorespiration {ECO:0000256|ARBA:ARBA00023238, ECO:0000256|HAMAP-
KW   Rule:MF_00860};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW   Rule:MF_00860};
KW   Plastid {ECO:0000256|HAMAP-Rule:MF_00860, ECO:0000256|RuleBase:RU003627};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          68..177
FT                   /note="Ribulose bisphosphate carboxylase small subunit"
FT                   /evidence="ECO:0000259|SMART:SM00961"
SQ   SEQUENCE   180 AA;  20392 MW;  F396755AB37E1D82 CRC64;
     MASSVMSTAT VATGANAAQA SMIASFNGLK SAASFPVTRK QDLDITSIAS NGGRVQCMLV
     WPPINKKKYE TLSYLPDLSD EQLLKEIEYL LQKGWVPCLE FETEHGFVYR EHHRSPGYYD
     GRYWTMWKLP MFGCTDATQV LNEVQEAKKA YPQAWIRIIG FDNVRQVQCI SFIAYKPEGY
//
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