ID   PYG1_MASLA              Reviewed;         279 AA.
AC   P29731;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Phycobilisome rod-core linker polypeptide CpcG1;
DE   AltName: Full=L-RC 31.7;
GN   Name=cpcG1;
OS   Mastigocladus laminosus (Fischerella sp.).
OC   Bacteria; Cyanobacteria; Nostocales; Hapalosiphonaceae; Mastigocladus.
OX   NCBI_TaxID=83541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PCC 7603;
RX   PubMed=1577010; DOI=10.1111/j.1432-1033.1992.tb16859.x;
RA   Glauser M., Stirewalt V.L., Bryant D.A., Sidler W., Zuber H.;
RT   "Structure of the genes encoding the rod-core linker polypeptides of
RT   Mastigocladus laminosus phycobilisomes and functional aspects of the
RT   phycobiliprotein/linker-polypeptide interactions.";
RL   Eur. J. Biochem. 205:927-937(1992).
CC   -!- FUNCTION: Rod-core linker protein required for attachment of
CC       phycocyanin to allophycocyanin in cores of phycobilisomes.
CC       {ECO:0000250}.
CC   -!- FUNCTION: Linker polypeptides determine the state of aggregation and
CC       the location of the disk-shaped phycobiliprotein units within the
CC       phycobilisome and modulate their spectroscopic properties in order to
CC       mediate a directed and optimal energy transfer. {ECO:0000250}.
CC   -!- SUBUNIT: The phycobilisome is a hemidiscoidal structure that is
CC       composed of two distinct substructures: a core complex and a number of
CC       rods radiating from the core. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phycobilisome linker protein family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00775}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X59763; CAA42433.1; -; Genomic_DNA.
DR   AlphaFoldDB; P29731; -.
DR   SMR; P29731; -.
DR   PRIDE; P29731; -.
DR   GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3130.20; -; 1.
DR   InterPro; IPR001297; PBS_linker_dom.
DR   InterPro; IPR038255; PBS_linker_sf.
DR   InterPro; IPR016470; Phycobilisome.
DR   Pfam; PF00427; PBS_linker_poly; 1.
DR   PIRSF; PIRSF005898; Phycobilisome_CpeC/CpcI; 1.
DR   PROSITE; PS51445; PBS_LINKER; 1.
PE   3: Inferred from homology;
KW   Antenna complex; Membrane; Photosynthesis; Phycobilisome; Thylakoid.
FT   CHAIN           1..279
FT                   /note="Phycobilisome rod-core linker polypeptide CpcG1"
FT                   /id="PRO_0000199250"
FT   DOMAIN          11..189
FT                   /note="PBS-linker"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
SQ   SEQUENCE   279 AA;  31782 MW;  4F57045224A20CC1 CRC64;
     MPIPLLSFPL TTQNQRVEGY EVPNEDTPTI YRLTDTSSDT EIDAIIWAAY RQIFSEHLIL
     ETYRQPYLES QLRNRAINVR DFIRGLGKSE VYRQEVAQTN SNYRLVDISF KRFLGRATYG
     KSEQIAWSIV IATQGLHGFI DALVDSEEYR QNFGDDIVPF QRRRFKDRPF NLVNPRYADY
     WRNRLLEQFL GGQSFYRVVR AGESGKRGVA GAIPSTFLSM AASIAPSGIS YQRTADSART
     FISTVKLPET TSESKTPPPT VKPATVALPY RYIPGNKTT