APCE_CYACA
ID APCE_CYACA Reviewed; 870 AA.
AC Q9TLS6;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Phycobiliprotein ApcE;
DE EC=4.-.-.-;
DE AltName: Full=Anchor polypeptide;
DE AltName: Full=PBS-anchor protein;
DE AltName: Full=Phycobilisome linker polypeptide;
GN Name=apcE;
OS Cyanidium caldarium (Red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX NCBI_TaxID=2771;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RK-1;
RX PubMed=11040290; DOI=10.1007/s002390010101;
RA Gloeckner G., Rosenthal A., Valentin K.-U.;
RT "The structure and gene repertoire of an ancient red algal plastid
RT genome.";
RL J. Mol. Evol. 51:382-390(2000).
CC -!- FUNCTION: This protein is postulated to act both as terminal energy
CC acceptor and as a linker polypeptide that stabilizes the phycobilisome
CC architecture. May have intrinsic bilin lyase activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Stromal side
CC {ECO:0000250}.
CC -!- PTM: Contains one covalently linked bilin chromophore. This protein
CC autochromophorylates (Potential). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phycobilisome linker protein family.
CC {ECO:0000255|PROSITE-ProRule:PRU00775}.
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DR EMBL; AF022186; AAF12901.1; -; Genomic_DNA.
DR RefSeq; NP_045193.1; NC_001840.1.
DR AlphaFoldDB; Q9TLS6; -.
DR SMR; Q9TLS6; -.
DR GeneID; 800215; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3130.20; -; 3.
DR Gene3D; 1.10.490.20; -; 1.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR001297; PBS_linker_dom.
DR InterPro; IPR038255; PBS_linker_sf.
DR InterPro; IPR012128; Phycobilisome_asu/bsu.
DR InterPro; IPR038719; Phycobilisome_asu/bsu_sf.
DR Pfam; PF00427; PBS_linker_poly; 3.
DR Pfam; PF00502; Phycobilisome; 2.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS51445; PBS_LINKER; 3.
PE 3: Inferred from homology;
KW Antenna complex; Bile pigment; Chloroplast; Chromophore;
KW Electron transport; Lyase; Membrane; Photosynthesis; Phycobilisome;
KW Plastid; Repeat; Thylakoid; Transport.
FT CHAIN 1..870
FT /note="Phycobiliprotein ApcE"
FT /id="PRO_0000199260"
FT DOMAIN 241..421
FT /note="PBS-linker 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT DOMAIN 482..665
FT /note="PBS-linker 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT DOMAIN 679..856
FT /note="PBS-linker 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT BINDING 184
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000255"
SQ SEQUENCE 870 AA; 99077 MW; 7FC11E1AEC6EA2BA CRC64;
MGLRTSSGSP LVKPKLYKTS ASNVISLAEK QDRFLNLGEL TDLNTYFSSG NRRLDIAKVI
SLNANLIISR AADRIFVGGS PLSFLERPQA AVTLTSDQAS STSIQSTKGL GNGNIFQNFF
KSTSEAPTGF KPINVVRYGS SNMKKSIRDL DWFLRYVTYA IVAGDTSILI VNTKGLRELI
DKACSSSAAI VALKEMKNVS LSLFNYDIES QNIVRLYFNT LVSEFESPAS SSKVRKRNSL
DLQGLAIPDI YLVAADKSLR YVMKPNLSNT EKAQVIKACY RQVFERDIAK AYGLSLLELE
SKLKNLQISV KEFIRALGKS TLYRKNFYEG FTNSRVVELA FRHFMGRGLS SLQEFRKYFA
ILSSNGLDAL IDSIINNSEY AEYFGEETVP YIRGYGQEAQ ECRNWGSQFA LFKYSAPFRT
IPQFITLFAD YTQLPPSQHC YGKLNDPLNI QFGAIFKNSY VNEQSRPVLF PRGSRRILVY
KGAGIFNQLG SPNALEKPPS NVSIAKWSKE TDLNFILNAA YLRVFGRYVY EEEKIALRPL
ENEFKRRSIS VRDFVGQLAK SDVFRSLYWS RLYICKSIEY IHIRLLGRPT YGRTEINNYF
DIVYKSGFYA FVDSLVNSRE YIKCFGNDTV PYDRYSTPEA VSSSIFRLSF INSVSYKSLK
PKIEKFIQLG VARDAKSLSS LNSKVFQGVS QARSQKRVFK VSDYSNVMNL RIVFYAALRQ
VFERNIEPYI KGGEFKDIES LFLSGKISVR ELIKEIGSSS LYRKEFYIPF PNTQVIEFCT
KHFLGRAPKN QSEIRYYNQV LAVQGLREMI NYMINSKEYL SVFGDDIVPY RRFPTLPAAN
FPNTQRLYSR QTKQNRNIVV PSFSGLLNTV