PYR2_MASLA
ID PYR2_MASLA Reviewed; 279 AA.
AC P11399;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Phycobilisome 34.5 kDa linker polypeptide, phycoerythrocyanin-associated, rod;
GN Name=pecC;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
RX PubMed=2121619; DOI=10.1016/0378-1119(90)90480-f;
RA Eberlein M., Kufer W.;
RT "Genes encoding both subunits of phycoerythrocyanin, a light-harvesting
RT biliprotein from the cyanobacterium Mastigocladus laminosus.";
RL Gene 94:133-136(1990).
RN [3]
RP PROTEIN SEQUENCE OF 2-45; 158-220 AND 228-279.
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 phycoerythrocyanin.
CC Linker polypeptides determine the state of aggregation and the location
CC of the 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 phycoerythrocyanin.
CC -!- SIMILARITY: Belongs to the phycobilisome linker protein family.
CC {ECO:0000255|PROSITE-ProRule:PRU00775}.
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DR EMBL; M75599; AAC64646.1; -; Genomic_DNA.
DR EMBL; M34254; AAC64655.1; -; Genomic_DNA.
DR PIR; B24691; B24691.
DR PIR; PQ0129; PQ0129.
DR AlphaFoldDB; P11399; -.
DR SMR; P11399; -.
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..279
FT /note="Phycobilisome 34.5 kDa linker polypeptide,
FT phycoerythrocyanin-associated, rod"
FT /id="PRO_0000199226"
FT DOMAIN 2..178
FT /note="PBS-linker"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT DOMAIN 226..278
FT /note="CpcD-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00771"
FT CONFLICT 219..220
FT /note="TS -> VG (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 279 AA; 31492 MW; A140914A3981C175 CRC64;
MSTSVAERLA IKDEVDKKIE LRPNWSEDEL QIVFKTAYEQ VFGRQGLYAS QRFATAEALL
RNGKISVKQF IELLAKSEFY KECFFYNNSQ VRFIELNYKH LLGRAPYDQS EIAFHVDLYA
AAGYDAEIES YIYSPEYDNA FGNFVVPYYR GFQSIPGMKT VGFNRIFELY RGRANSDNAQ
FGGKSARLRS KISMNLANTI VPPTSPIAAS TSSARTLVTS PVMGDARMFI VEAIAGTLNT
NVAVRRSRQV YTVPYDRLSA TYQEIHKRGG KIVKITPAS