ID   PYR5_MICDP              Reviewed;         269 AA.
AC   P11401;
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 37.5 kDa linker polypeptide, phycocyanin-associated, rod;
DE            Short=L-37.5/R;
GN   Name=cpcH2;
OS   Microchaete diplosiphon (Fremyella diplosiphon).
OC   Bacteria; Cyanobacteria; Nostocales; Rivulariaceae; Microchaete.
OX   NCBI_TaxID=1197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3108238; DOI=10.1128/jb.169.6.2675-2684.1987;
RA   Lomax T.L., Conley P.B., Schilling J., Grossman A.R.;
RT   "Isolation and characterization of light-regulated phycobilisome linker
RT   polypeptide genes and their transcription as a polycistronic mRNA.";
RL   J. Bacteriol. 169:2675-2684(1987).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-8.
RX   PubMed=1551428; DOI=10.1016/0014-5793(92)80318-b;
RA   Glauser M., Sidler W.A., Graham K.W., Bryant D.A., Frank G., Wehrli E.,
RA   Zuber H.;
RT   "Three C-phycoerythrin-associated linker polypeptides in the phycobilisome
RT   of green-light-grown Calothrix sp. PCC 7601 (cyanobacteria).";
RL   FEBS Lett. 297:19-23(1992).
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=Associated with phycocyanin.
CC   -!- SIMILARITY: Belongs to the phycobilisome linker protein family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00775}.
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DR   EMBL; M16490; AAA24886.1; -; Genomic_DNA.
DR   PIR; A25974; A25974.
DR   AlphaFoldDB; P11401; -.
DR   SMR; P11401; -.
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:1551428"
FT   CHAIN           2..269
FT                   /note="Phycobilisome 37.5 kDa linker polypeptide,
FT                   phycocyanin-associated, rod"
FT                   /id="PRO_0000199216"
FT   DOMAIN          2..177
FT                   /note="PBS-linker"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT   DOMAIN          217..269
FT                   /note="CpcD-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00771"
SQ   SEQUENCE   269 AA;  30691 MW;  AC91D7F57C48D7F6 CRC64;
     MTSSTAARQL GFEPFASTAP TELRASSDVI HAAYRQVFQV FGNDHVMQSE RLTSAESLLQ
     QGNISVRDFV RLLAQSELYR QKFFYSTPQV RFIELNYKHL LGRAPYDESE ISYHVNLYTE
     KGYEAEINSY IDSAEYQESF GERIVPHYRG FETQPGQKTV GFNRMFQIYR GYANSDRSQG
     KNKSAWLTQD LALNLASNIQ TPNFGKGLTG VVAGDRGQLY RVRVIQADRG RTTQIRRSIQ
     EYLVSYDQLS PTLQRLNQRG SRVVNISPA