ID   PYR1_MASLA              Reviewed;         286 AA.
AC   P11398;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Phycobilisome 32.1 kDa linker polypeptide, phycocyanin-associated, rod;
GN   Name=cpcC;
OS   Mastigocladus laminosus (Fischerella sp.).
OC   Bacteria; Cyanobacteria; Nostocales; Hapalosiphonaceae; Mastigocladus.
OX   NCBI_TaxID=83541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kufer W., Hoegner A., Eberlein M., Mayer K., Buchner A., Gottschalk L.;
RT   "Structure and molecular evolution of the gene cluster encoding proteins of
RT   the rod substructure of the phycobilisome from the cyanobacterium
RT   Mastigocadus laminosus.";
RL   Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 2-45.
RX   PubMed=3933528; DOI=10.1515/bchm3.1985.366.2.993;
RA   Fueglistaller P., Suter F., Zuber H.;
RT   "Linker polypeptides of the phycobilisome from the cyanobacterium
RT   Mastigocladus laminosus: amino-acid sequences and relationships.";
RL   Biol. Chem. Hoppe-Seyler 366:993-1001(1985).
CC   -!- FUNCTION: Rod linker protein, associated with phycocyanin. Linker
CC       polypeptides determine the state of aggregation and the location of the
CC       disk-shaped phycobiliprotein units within the phycobilisome and
CC       modulate their spectroscopic properties in order to mediate a directed
CC       and optimal energy transfer.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane
CC       protein; Cytoplasmic side. Note=This protein occurs in the rod, it is
CC       associated with phycocyanin.
CC   -!- SIMILARITY: Belongs to the phycobilisome linker protein family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00775}.
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DR   EMBL; M75599; AAC64651.1; -; Genomic_DNA.
DR   PIR; C24691; C24691.
DR   AlphaFoldDB; P11398; -.
DR   SMR; P11398; -.
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; IPR008213; CpcD-like_dom.
DR   InterPro; IPR001297; PBS_linker_dom.
DR   InterPro; IPR038255; PBS_linker_sf.
DR   InterPro; IPR016470; Phycobilisome.
DR   Pfam; PF01383; CpcD; 1.
DR   Pfam; PF00427; PBS_linker_poly; 1.
DR   PIRSF; PIRSF005898; Phycobilisome_CpeC/CpcI; 1.
DR   SMART; SM01094; CpcD; 1.
DR   PROSITE; PS51441; CPCD_LIKE; 1.
DR   PROSITE; PS51445; PBS_LINKER; 1.
PE   1: Evidence at protein level;
KW   Antenna complex; Direct protein sequencing; Membrane; Photosynthesis;
KW   Phycobilisome; Thylakoid.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3933528"
FT   CHAIN           2..286
FT                   /note="Phycobilisome 32.1 kDa linker polypeptide,
FT                   phycocyanin-associated, rod"
FT                   /id="PRO_0000199220"
FT   DOMAIN          2..180
FT                   /note="PBS-linker"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT   DOMAIN          234..286
FT                   /note="CpcD-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00771"
FT   CONFLICT        42
FT                   /note="H -> E (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   286 AA;  32308 MW;  614BEEB5BD376598 CRC64;
     MAITAAASRL GTEPFSNAAK IELRSDASRE EVEAVINAVY RHVLGNDYIM ASERLVSAES
     LLRDGNLTVR EFVRSVAKSE LYKKKFFYNS FQTRFIELNY KHLLGRAPYD ESEIVFHLDL
     YQNKGYDAEI DSYIDSVEYQ NNFGDNIVPY YRGFETQPGQ KTVGFNRMFR LYRGYANSDR
     AQIEGTKPRL ARELATNKAS SIVGPSGSNP AWGYRPSVDI TPRKTLGNAV GENDRVYRIE
     VTGVRSPGYP SVRRSSYAII VPYERLSEKI QQIHKLGGKI VSITSA