ID   APCE_CYAPA              Reviewed;         883 AA.
AC   P48088;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 83.
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   Cyanophora paradoxa.
OG   Plastid; Cyanelle.
OC   Eukaryota; Glaucocystophyceae; Cyanophoraceae; Cyanophora.
OX   NCBI_TaxID=2762;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX LB 555 / Pringsheim;
RA   Stirewalt V.L., Michalowski C.B., Loeffelhardt W., Bohnert H.J.,
RA   Bryant D.A.;
RT   "Nucleotide sequence of the cyanelle DNA from Cyanophora paradoxa.";
RL   Plant Mol. Biol. Rep. 13:327-332(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX LB 555 / Pringsheim;
RA   Loeffelhardt W., Stirewalt V.L., Michalowski C.B., Annarella M.,
RA   Farley J.Y., Schluchter W.M., Chung S., Newmann-Spallart C., Steiner J.M.,
RA   Jakowitsch J., Bohnert H.J., Bryant D.A.;
RT   "The complete sequence of the cyanelle genome of Cyanophora paradoxa: the
RT   genetic complexity of a primitive plastid.";
RL   (In) Schenk H.E.A., Herrmann R., Jeon K.W., Mueller N.E., Schwemmler W.
RL   (eds.);
RL   Eukaryotism and symbiosis, pp.40-48, Springer-Verlag, Heidelberg (1997).
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, cyanelle 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; U30821; AAA81191.1; -; Genomic_DNA.
DR   PIR; T06848; T06848.
DR   RefSeq; NP_043160.1; NC_001675.1.
DR   AlphaFoldDB; P48088; -.
DR   SMR; P48088; -.
DR   PRIDE; P48088; -.
DR   GeneID; 801542; -.
DR   GO; GO:0033115; C:cyanelle 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; Chromophore; Cyanelle; Electron transport;
KW   Lyase; Membrane; Photosynthesis; Phycobilisome; Plastid; Repeat; Thylakoid;
KW   Transport.
FT   CHAIN           1..883
FT                   /note="Phycobiliprotein ApcE"
FT                   /id="PRO_0000199258"
FT   DOMAIN          238..418
FT                   /note="PBS-linker 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT   DOMAIN          488..669
FT                   /note="PBS-linker 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT   DOMAIN          684..861
FT                   /note="PBS-linker 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT   BINDING         181
FT                   /ligand="(2R,3E)-phycocyanobilin"
FT                   /ligand_id="ChEBI:CHEBI:85275"
FT                   /note="covalent, via 1 link"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   883 AA;  100484 MW;  B9D4914DC3723AEC CRC64;
     MTSVSGGSPL LRPQLYRTVT VSTILQADQQ DRFLESGELS QLATYLTSGN KRLDIIITLT
     NNSEAIVSRA ANRIFVGGSP ISYLERPQSG IDAKLGTNSY VESQSGFLEG FRSLFNTGGA
     DITPAGFKPI NVSRYGITRM QKSLRDLDWF LRYITYAIVA GDPNILVTNI RGLREIIENA
     CSSAVTLVAL QEMRRASLSY FTKDASAEAI VKQYFDVVIT EFLAPAPSDL VRKRTSTSLQ
     GLKLPQIYAN AVVQKPRFQM KSTLSTTEKE TVIKAVYRQI FERDVRRAYS LKNYDLESKV
     KNGQLSIKEF VRALGKSKLY AQQFYEPFIN SRALELAFRH FLGRGPGSRE EVQEYFALIS
     KGGLPLLVDA LVDSKEYEEY FGEEIVPYLR TLGEEAQECR NWGAQIKLLN YSARFQKTPQ
     FITLFAGYKN PLPDQHPYGQ GNDPLEIQFG AIFPKETLQT KAAFFGKDTR RILIRRGNGI
     DNQLSNPSAR QKSPGSFGPK VFKLSSVASL NKNTKNVSFG ETSTQAIIKA VYLQIIGRET
     YESQRLKVWE IKLENGEISI REFVKQVAKS NLFRSLYWTP YYVCKSIEYI NRRILGRPTY
     GRSEINKLFD IAAKKGFYAL IDTLMDSPEY DESFGENTVP YERYLTPGGL ALRIKRPNLS
     VSKEAKNELR FIELGAINES RGERSIQLRI QQGVSKRREQ TKIFKLNHHD DKVNLEKVIK
     AVYRQVFERD MDMYRIQNEF TVFESRLKNK EISVKEFVEA LGQSQLYQKE FYTPYPNTKV
     IELAMKHFLG RAPKNQIEIR KYNQLLASNG IAALIRSLVS SLEYAEVFGE DTVPYRRFPT
     FPATNFPNTE KLYNSLTKQT KTISNPSFAP EKTRRIDLLS PGA