ID A0A164BQV3_9SYNE Unreviewed; 66 AA.
AC A0A164BQV3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Phycobilisome 7.8 kDa linker polypeptide, allophycocyanin-associated, core {ECO:0000256|ARBA:ARBA00019361, ECO:0000256|PIRNR:PIRNR000083};
GN Name=apcC {ECO:0000313|EMBL:KZR89123.1};
GN ORFNames=MITS9508_01634 {ECO:0000313|EMBL:KZR89123.1};
OS Synechococcus sp. MIT S9508.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1801629 {ECO:0000313|EMBL:KZR89123.1, ECO:0000313|Proteomes:UP000076799};
RN [1] {ECO:0000313|EMBL:KZR89123.1, ECO:0000313|Proteomes:UP000076799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT S9508 {ECO:0000313|EMBL:KZR89123.1,
RC ECO:0000313|Proteomes:UP000076799};
RA Cubillos-Ruiz A., Berta-Thompson J.W., Becker J.W., Chisholm S.W.;
RT "Evolutionary Radiation of Lanthipeptides in Marine Picocyanobacteria.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Rod linker protein, associated with allophycocyanin. 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. {ECO:0000256|ARBA:ARBA00025055,
CC ECO:0000256|PIRNR:PIRNR000083}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000256|PIRNR:PIRNR000083}; Peripheral membrane protein
CC {ECO:0000256|PIRNR:PIRNR000083}; Cytoplasmic side
CC {ECO:0000256|PIRNR:PIRNR000083}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}. Note=This protein occurs in the rod,
CC it is associated with allophycocyanin. {ECO:0000256|PIRNR:PIRNR000083}.
CC -!- SIMILARITY: Belongs to the phycobilisome linker protein family.
CC {ECO:0000256|ARBA:ARBA00005304, ECO:0000256|PIRNR:PIRNR000083}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZR89123.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LVHU01000007; KZR89123.1; -; Genomic_DNA.
DR RefSeq; WP_006851140.1; NZ_LVHU01000007.1.
DR AlphaFoldDB; A0A164BQV3; -.
DR STRING; 1801629.MITS9508_01634; -.
DR PATRIC; fig|1801629.3.peg.1731; -.
DR Proteomes; UP000076799; Unassembled WGS sequence.
DR GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-UniRule.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1490.170; Allophycocyanin linker chain (domain); 1.
DR InterPro; IPR011134; Allophyco_linker.
DR InterPro; IPR011064; Allophyco_linker_chain.
DR InterPro; IPR008213; CpcD-like_dom.
DR Pfam; PF01383; CpcD; 1.
DR PIRSF; PIRSF000083; Allophyco_linker; 1.
DR SMART; SM01094; CpcD; 1.
DR SUPFAM; SSF54580; Allophycocyanin linker chain (domain); 1.
DR PROSITE; PS51441; CPCD_LIKE; 1.
PE 3: Inferred from homology;
KW Antenna complex {ECO:0000256|ARBA:ARBA00022738,
KW ECO:0000256|PIRNR:PIRNR000083};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000083};
KW Photosynthesis {ECO:0000256|PIRNR:PIRNR000083};
KW Phycobilisome {ECO:0000256|ARBA:ARBA00022738,
KW ECO:0000256|PIRNR:PIRNR000083}; Thylakoid {ECO:0000256|PIRNR:PIRNR000083}.
FT DOMAIN 1..56
FT /note="CpcD-like"
FT /evidence="ECO:0000259|PROSITE:PS51441"
SQ SEQUENCE 66 AA; 7686 MW; FA5666F9089E504D CRC64;
MRLFKVTACI PSPEKVRTQR ELQNTFFTKW VPYDSWFAEQ QRIQKQGGRI IKVELCTGGQ
QVNVGN
//
