ID   PYC1_MASLA              Reviewed;          67 AA.
AC   P20116;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Phycobilisome 7.8 kDa linker polypeptide, allophycocyanin-associated, core;
DE   AltName: Full=LC 7.8;
GN   Name=apcC;
OS   Mastigocladus laminosus (Fischerella sp.).
OC   Bacteria; Cyanobacteria; Nostocales; Hapalosiphonaceae; Mastigocladus.
OX   NCBI_TaxID=83541;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Fueglistaller P., Ruembeli R., Suter F., Zuber H.;
RT   "Minor polypeptides from the phycobilisome of the cyanobacterium
RT   Mastigocladus laminosus. Isolation, characterization and amino-acid
RT   sequences of a colourless 8.9-kDa polypeptide and of a 16.2-kDa
RT   phycobiliprotein.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 365:1085-1096(1984).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RC   STRAIN=PCC 7603;
RX   PubMed=9990029; DOI=10.1073/pnas.96.4.1363;
RA   Reuter W., Wiegand G., Huber R., Than M.E.;
RT   "Structural analysis at 2.2 A of orthorhombic crystals presents the
RT   asymmetry of the allophycocyanin-linker complex, AP.LC7.8, from
RT   phycobilisomes of Mastigocladus laminosus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:1363-1368(1999).
CC   -!- FUNCTION: Rod linker protein, associated with allophycocyanin. 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 allophycocyanin.
CC   -!- SIMILARITY: Belongs to the phycobilisome linker protein family.
CC       {ECO:0000305}.
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DR   PIR; S00284; S00284.
DR   PDB; 1B33; X-ray; 2.30 A; N/O=1-67.
DR   PDBsum; 1B33; -.
DR   AlphaFoldDB; P20116; -.
DR   SMR; P20116; -.
DR   EvolutionaryTrace; P20116; -.
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; 3.30.1490.170; -; 1.
DR   InterPro; IPR011134; Allophyco_linker.
DR   InterPro; IPR011064; Allophyco_linker_chain.
DR   InterPro; IPR008213; CpcD-like_dom.
DR   Pfam; PF01383; CpcD; 1.
DR   PIRSF; PIRSF000083; Allophyco_linker; 1.
DR   SMART; SM01094; CpcD; 1.
DR   SUPFAM; SSF54580; SSF54580; 1.
DR   PROSITE; PS51441; CPCD_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antenna complex; Direct protein sequencing; Membrane;
KW   Photosynthesis; Phycobilisome; Thylakoid.
FT   CHAIN           1..67
FT                   /note="Phycobilisome 7.8 kDa linker polypeptide,
FT                   allophycocyanin-associated, core"
FT                   /id="PRO_0000199235"
FT   DOMAIN          1..56
FT                   /note="CpcD-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00771"
FT   VARIANT         9
FT                   /note="C -> S"
FT   STRAND          3..9
FT                   /evidence="ECO:0007829|PDB:1B33"
FT   HELIX           22..25
FT                   /evidence="ECO:0007829|PDB:1B33"
FT   STRAND          26..32
FT                   /evidence="ECO:0007829|PDB:1B33"
FT   HELIX           33..45
FT                   /evidence="ECO:0007829|PDB:1B33"
FT   STRAND          49..55
FT                   /evidence="ECO:0007829|PDB:1B33"
SQ   SEQUENCE   67 AA;  7741 MW;  BF92F96127EA7891 CRC64;
     GRLFKITACV PSQTRIRTQR ELQNTYFTKL VPYENWFREQ QRIQKMGGKI VKVELATGKQ
     GINTGLA