ID   PHE1_RHDS2              Reviewed;          44 AA.
AC   P30942;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   22-FEB-2023, entry version 82.
DE   RecName: Full=Phycoerythrin alpha-1 chain;
DE   Flags: Fragment;
GN   Name=cpeA1;
OS   Rhodomonas sp. (strain CS 24) (Chroomonas sp. (strain CS24)).
OC   Eukaryota; Cryptophyceae; Pyrenomonadales; Pyrenomonadaceae; Rhodomonas.
OX   NCBI_TaxID=79257;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=2226853; DOI=10.1016/0014-5793(90)81082-y;
RA   Jenkins J., Hiller R.G., Speirs J., Godovac-Zimmermann J.;
RT   "A genomic clone encoding a cryptophyte phycoerythrin alpha-subunit.
RT   Evidence for three alpha-subunits and an N-terminal membrane transit
RT   sequence.";
RL   FEBS Lett. 273:191-194(1990).
CC   -!- FUNCTION: Light-harvesting photosynthetic tetrapyrrole chromophore-
CC       protein from the phycobiliprotein complex.
CC   -!- SUBUNIT: Heterotetramer of 2 different alpha chains and 2 identical
CC       beta chains. The subunit composition could comprise of any combination
CC       of 2 out of 4 different alpha units with an invariant beta unit (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane;
CC       Peripheral membrane protein; Lumenal side.
CC   -!- PTM: Contains one covalently linked 15,16-dihydrobiliverdin
CC       chromophore. {ECO:0000250}.
CC   -!- MISCELLANEOUS: The light-harvesting system in Cryptophytes contains
CC       phycobiliprotein complexes. Unusually they are composed of either
CC       phycoerythrin (CPE) or phycocyanin (CPC) but never allophycocyanin
CC       (APC), with only one type of biliprotein being present in any one
CC       species. Unlike cyanobacteria or red algae these proteins are not
CC       arranged into higher-order phycobilisome complexes, and they are found
CC       in the thylakoid lumen.
CC   -!- SIMILARITY: Belongs to the phycoerythrin family. {ECO:0000305}.
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DR   AlphaFoldDB; P30942; -.
DR   SMR; P30942; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030089; C:phycobilisome; IEA:InterPro.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.510.10; Phycoerythrin alpha chain; 1.
DR   InterPro; IPR011070; Globular_prot_asu/bsu.
DR   InterPro; IPR037011; Phycoerythr-like_a_sf.
DR   InterPro; IPR004228; Phycoerythr_a.
DR   Pfam; PF02972; Phycoerythr_ab; 1.
DR   SUPFAM; SSF56568; Non-globular alpha+beta subunits of globular proteins; 1.
PE   1: Evidence at protein level;
KW   Bile pigment; Chloroplast; Chromophore; Direct protein sequencing;
KW   Electron transport; Hydroxylation; Membrane; Photosynthesis; Plastid;
KW   Thylakoid; Transport.
FT   CHAIN           1..>44
FT                   /note="Phycoerythrin alpha-1 chain"
FT                   /id="PRO_0000199209"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          24..26
FT                   /note="15,16-dihydrobiliverdin chromophore"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        25..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         19
FT                   /ligand="15,16-dihydrobiliverdin"
FT                   /ligand_id="ChEBI:CHEBI:57899"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         21
FT                   /ligand="15,16-dihydrobiliverdin"
FT                   /ligand_id="ChEBI:CHEBI:57899"
FT                   /evidence="ECO:0000250"
FT   BINDING         40
FT                   /ligand="15,16-dihydrobiliverdin"
FT                   /ligand_id="ChEBI:CHEBI:57899"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         4
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000250"
FT   NON_TER         44
SQ   SEQUENCE   44 AA;  4723 MW;  2EBE2D2EAF47AA7E CRC64;
     AMDKSAKAPQ ITIFDHRGCS RAPKSETGGT ATKDDQMMVK VSQV
//