PYR1_MICDP
ID PYR1_MICDP Reviewed; 286 AA.
AC P18542;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Phycobilisome 31.8 kDa linker polypeptide, phycoerythrin-associated, rod;
GN Name=cpeC;
OS Microchaete diplosiphon (Fremyella diplosiphon).
OC Bacteria; Cyanobacteria; Nostocales; Rivulariaceae; Microchaete.
OX NCBI_TaxID=1197;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1694529; DOI=10.1128/jb.172.7.4072-4081.1990;
RA Federspiel N.A., Grossman A.R.;
RT "Characterization of the light-regulated operon encoding the phycoerythrin-
RT associated linker proteins from the cyanobacterium Fremyella diplosiphon.";
RL J. Bacteriol. 172:4072-4081(1990).
RN [2]
RP PROTEIN SEQUENCE OF 2-5.
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 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 -!- SUBUNIT: The phycobilisome is a hemidiscoidal structure that is
CC composed of two distinct substructures: a core complex and six rods
CC radiating from the core.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane
CC protein; Cytoplasmic side. Note=Associated with phycoerythrin.
CC -!- INDUCTION: By green light.
CC -!- SIMILARITY: Belongs to the phycobilisome linker protein family.
CC {ECO:0000255|PROSITE-ProRule:PRU00775}.
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DR EMBL; M33832; AAA24882.1; -; Genomic_DNA.
DR PIR; S32608; S32608.
DR AlphaFoldDB; P18542; -.
DR SMR; P18542; -.
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..286
FT /note="Phycobilisome 31.8 kDa linker polypeptide,
FT phycoerythrin-associated, rod"
FT /id="PRO_0000199212"
FT DOMAIN 2..179
FT /note="PBS-linker"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT DOMAIN 231..286
FT /note="CpcD-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00771"
SQ SEQUENCE 286 AA; 31844 MW; F71A9AA40453E7B8 CRC64;
MPFGPASRLG VSLFDETPPV EWVPGRSQEE AETIIRAIYR QVLGNAYVME SERLAVPESQ
FKRGELSVRE FVRAVAKSEL YRSRFFTSCA RYRAIELNFR HLLGRPPLDL EEMRSHSTIL
DTQGFEAEID SYIDGDEYQS TFGENIVPYI RGYKTEALQS MVQFTHTFQL VRGASSSSLK
GDLSGKAPKL NALVIQSTPT AVISPASAGA TFSTPPTGAR TRLGVDASAG GKVYRIEVTG
YRAKTFNNIS KFRRSNQVFL VPYEKLSQEY QRIHQQGGVI ASITPV
