PHE1_RHDS2
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 03-AUG-2022, entry version 79.
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;
OC unclassified 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; -; 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; SSF56568; 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, via 1 link"
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
