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Database: UniProt
Entry: C1JZ18_9ASTR
LinkDB: C1JZ18_9ASTR
Original site: C1JZ18_9ASTR 
ID   C1JZ18_9ASTR            Unreviewed;       178 AA.
AC   C1JZ18;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 53.
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 {ECO:0000313|EMBL:ACO35888.1};
OS   Ageratina adenophora.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Eupatorieae; Ageratina.
OX   NCBI_TaxID=176616 {ECO:0000313|EMBL:ACO35888.1};
RN   [1] {ECO:0000313|EMBL:ACO35888.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:ACO35888.1};
RA   Pei X., Guo H., Cheng H.;
RT   "Construction of cDNA Library and Screening Gene in Eupatorium
RT   adenophorum.";
RL   Submitted (FEB-2009) 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|RuleBase:RU003627}.
CC   -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC       {ECO:0000256|RuleBase:RU003627}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, plasmodesma
CC       {ECO:0000256|ARBA:ARBA00024184}.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000256|RuleBase:RU003627}.
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DR   EMBL; FJ752421; ACO35888.1; -; mRNA.
DR   AlphaFoldDB; C1JZ18; -.
DR   GO; GO:0009506; C:plasmodesma; IEA:UniProtKB-SubCell.
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   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:SF27; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT, CHLOROPLASTIC; 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};
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};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          66..175
FT                   /note="Ribulose bisphosphate carboxylase small subunit"
FT                   /evidence="ECO:0000259|SMART:SM00961"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACO35888.1"
SQ   SEQUENCE   178 AA;  20029 MW;  F46CEC5A215A8B99 CRC64;
     IASISSSVAT VSRAAPAQAN MVAPFTGLKS NAAFPATKKA NDFSTLPNNG GRVQCMKVWP
     PLGLKKYETL SYLPTLTETQ LAKEVDYLLR NKWVPCLEFE LEHGFVYREH ARSPGYYDGR
     HWTMWKLPMF GCTDSAQVLK EVGECKKEYP QAWIRIIGFD NVRQVQCISF IASKPDGY
//
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