PYR3_MICDP
ID PYR3_MICDP Reviewed; 289 AA.
AC P11400;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Phycobilisome 39 kDa linker polypeptide, phycocyanin-associated, rod;
DE Short=L-39/R;
GN Name=cpcI2;
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 2-22.
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; AAA24887.1; -; Genomic_DNA.
DR PIR; B25974; B25974.
DR AlphaFoldDB; P11400; -.
DR SMR; P11400; -.
DR PRIDE; P11400; -.
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..289
FT /note="Phycobilisome 39 kDa linker polypeptide,
FT phycocyanin-associated, rod"
FT /id="PRO_0000199214"
FT DOMAIN 2..180
FT /note="PBS-linker"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT DOMAIN 236..288
FT /note="CpcD-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00771"
FT REGION 213..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 289 AA; 32315 MW; CC679AB26CF687AF CRC64;
MPITSAASRL GTTAYQTNPI ELRPNWTAED AKIVIQAVYR QVLGNDYLMQ SERLTSLESL
LTNGKLSVRD FVRAVAKSEL YKTKFLYPHF QTRVIELNFK HLLGRAPYDE SEVIEHLDRD
QNQGFDADID SYIDSAEYDT YFGDSIVPYY RDLVTTGVGQ RTVGFTRSFR LYRGYANSDR
SQLAGSSSRL ASDLATNSAT AIIAPSGGTQ GWSYLPSKQG TAPSRTFGRS SQGSTPRLYR
IEVTGISLPR YPKVRRSNKE FIVPYEQLSS TLQQINKLGG KVASITFAQ
