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Database: UniProt
Entry: Q106X7_MUSPR
LinkDB: Q106X7_MUSPR
Original site: Q106X7_MUSPR 
ID   Q106X7_MUSPR            Unreviewed;       115 AA.
AC   Q106X7;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Ribulose bisphosphate carboxylase small subunit {ECO:0000256|RuleBase:RU003627};
DE            Short=RuBisCO small subunit {ECO:0000256|RuleBase:RU003627};
DE   Flags: Fragment;
GN   Name=rbcS-Ma5 {ECO:0000313|EMBL:ABA46917.1};
OS   Musa AAB Group.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Musaceae; Musa.
OX   NCBI_TaxID=485264 {ECO:0000313|EMBL:ABA46917.1};
RN   [1] {ECO:0000313|EMBL:ABA46917.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Thomas-Hall S.R., Schenk P.M.;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABA46917.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17584952; DOI=10.1093/jxb/erm129;
RA   Thomas-Hall S., Campbell P.R., Carlens K., Kawanishi E., Swennen R.,
RA   Sagi L., Schenk P.M.;
RT   "Phylogenetic and molecular analysis of the ribulose-1,5-bisphosphate
RT   carboxylase small subunit gene family in banana.";
RL   J. Exp. Bot. 58:2685-2697(2007).
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|RuleBase:RU003627}.
CC   -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC       {ECO:0000256|RuleBase:RU003627}.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000256|RuleBase:RU003627}.
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DR   EMBL; DQ088117; ABA46917.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q106X7; -.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR   GO; GO:0009853; P:photorespiration; IEA:UniProtKB-UniRule.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR   CDD; cd03527; RuBisCO_small; 1.
DR   Gene3D; 3.30.190.10; Ribulose bisphosphate carboxylase, small subunit; 1.
DR   InterPro; IPR024681; RuBisCO_ssu.
DR   InterPro; IPR000894; RuBisCO_ssu_dom.
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, CHLOROPLASTIC 2; 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   3: Inferred from homology;
KW   Calvin cycle {ECO:0000256|ARBA:ARBA00022567};
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300,
KW   ECO:0000256|RuleBase:RU003627};
KW   Photorespiration {ECO:0000256|ARBA:ARBA00023238,
KW   ECO:0000256|RuleBase:RU003627};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531,
KW   ECO:0000256|RuleBase:RU003627}; Plastid {ECO:0000256|RuleBase:RU003627}.
FT   DOMAIN          21..115
FT                   /note="Ribulose bisphosphate carboxylase small subunit"
FT                   /evidence="ECO:0000259|SMART:SM00961"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABA46917.1"
FT   NON_TER         115
FT                   /evidence="ECO:0000313|EMBL:ABA46917.1"
SQ   SEQUENCE   115 AA;  13510 MW;  F189C7355BA9D61E CRC64;
     LPSNGGRVQC MKVWPIEGKK KFETLSYLPT LVDEALLKQI EYLLRSKWIP CLEFSHEGFV
     GRENHRSPGY YDGRYWTMWK LPMFGCTDAV QVVKEVEECK KEYPKAFIRI IGFDN
//
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