PHCB_AGLNE
ID PHCB_AGLNE Reviewed; 172 AA.
AC P28558;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=C-phycocyanin beta chain;
GN Name=cpcB;
OS Aglaothamnion neglectum (Red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Ceramiales;
OC Callithamniaceae; Aglaothamnion.
OX NCBI_TaxID=2765;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7678762; DOI=10.1007/bf00039615;
RA Apt K.E., Grossman A.R.;
RT "Characterization and transcript analysis of the major phycobiliprotein
RT subunit genes from Aglaothamnion neglectum (Rhodophyta).";
RL Plant Mol. Biol. 21:27-38(1993).
CC -!- FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the
CC phycobiliprotein complex (phycobilisome, PBS). Phycocyanin is the major
CC phycobiliprotein in the PBS rod.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit, which further
CC assembles into trimers and the trimers into hexamers. The basic
CC functional unit of phycobiliproteins is a ring-shaped hexamer formed
CC from two back-to-back trimers contacting via the alpha chain subunits.
CC The trimers are composed of alpha/beta subunit heterodimers arranged
CC around a three-fold axis of symmetry. The phycoerythrins also contain a
CC gamma subunit which is located in the center of the hexamer.
CC {ECO:0000250|UniProtKB:P00311}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Stromal side
CC {ECO:0000250}. Note=Part of the phycobilisome rod. {ECO:0000250}.
CC -!- PTM: Contains two covalently linked bilin chromophores.
CC {ECO:0000250|UniProtKB:P00311}.
CC -!- SIMILARITY: Belongs to the phycobiliprotein family. {ECO:0000305}.
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DR EMBL; Z11906; CAA77960.1; -; Genomic_DNA.
DR PIR; S30939; S30939.
DR AlphaFoldDB; P28558; -.
DR SMR; P28558; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.490.20; -; 1.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012128; Phycobilisome_asu/bsu.
DR InterPro; IPR038719; Phycobilisome_asu/bsu_sf.
DR InterPro; IPR006247; Phycocyanin_b.
DR Pfam; PF00502; Phycobilisome; 1.
DR PIRSF; PIRSF000081; Phycocyanin; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR TIGRFAMs; TIGR01339; phycocy_beta; 1.
PE 3: Inferred from homology;
KW Antenna complex; Bile pigment; Chloroplast; Chromophore;
KW Electron transport; Membrane; Methylation; Photosynthesis; Phycobilisome;
KW Plastid; Thylakoid; Transport.
FT CHAIN 1..172
FT /note="C-phycocyanin beta chain"
FT /id="PRO_0000199141"
FT BINDING 82
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="1"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000250|UniProtKB:P00311"
FT BINDING 153
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="2"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000250|UniProtKB:P00311"
FT MOD_RES 72
FT /note="N4-methylasparagine"
FT /evidence="ECO:0000250|UniProtKB:P00311"
SQ SEQUENCE 172 AA; 18130 MW; 23B9AE73918CA3C4 CRC64;
MLDAFAKVVA QADARGEFLS SQQIDALSDI IAEGNKRLDT VNKINSNASA IVTNSARALF
AEQPQLAQPG GNAYPSRRMA ACLRDMEIVL RYVSYAIAAG DSSVLDDRCL NGLRETYQAL
GTPGSSVAVA IQKMKEASIS LANDVNGVPL GDCSSLVAEL SVYFDRAAAS VV