位置:首页 > 蛋白库 > PHE3_RHDS2
PHE3_RHDS2
ID   PHE3_RHDS2              Reviewed;         128 AA.
AC   Q00433; O82050;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Phycoerythrin alpha-3 chain, chloroplastic;
DE   Flags: Precursor;
GN   Name=cpeA3;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
RN   [2]
RP   ERRATUM OF PUBMED:2226853.
RX   PubMed=2004659; DOI=10.1016/0014-5793(91)80187-8;
RA   Jenkins J., Hiller R.G., Speirs J., Godovac-Zimmermann J.;
RL   FEBS Lett. 279:361-361(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION TO 62.
RA   Hiller R.G., Howe C.E.;
RT   "Nuclear-encoded genes of phycoerythrin alpha subunits.";
RL   Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 53-128 IN COMPLEX WITH CPEA2;
RP   CPEB AND 15,16-DIHYDROBILIVERDIN, SUBUNIT, AND HYDROXYLATION AT LYS-56.
RX   PubMed=10430868; DOI=10.1073/pnas.96.16.8901;
RA   Wilk K.E., Harrop S.J., Jankova L., Edler D., Keenan G., Sharples F.,
RA   Hiller R.G., Curmi P.M.;
RT   "Evolution of a light-harvesting protein by addition of new subunits and
RT   rearrangement of conserved elements: crystal structure of a cryptophyte
RT   phycoerythrin at 1.63-A resolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:8901-8906(1999).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (0.97 ANGSTROMS) OF 53-128 IN COMPLEX WITH CPEA2;
RP   CPEB AND 15,16-DIHYDROBILIVERDIN, SUBUNIT, AND HYDROXYLATION AT LYS-56.
RX   PubMed=15504407; DOI=10.1016/j.jmb.2004.09.044;
RA   Doust A.B., Marai C.N., Harrop S.J., Wilk K.E., Curmi P.M., Scholes G.D.;
RT   "Developing a structure-function model for the cryptophyte phycoerythrin
RT   545 using ultrahigh resolution crystallography and ultrafast laser
RT   spectroscopy.";
RL   J. Mol. Biol. 344:135-153(2004).
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.
CC       {ECO:0000269|PubMed:10430868, ECO:0000269|PubMed:15504407}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane;
CC       Peripheral membrane protein; Lumenal side.
CC   -!- PTM: Contains one covalently linked 15,16-dihydrobiliverdin
CC       chromophore.
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}.
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; AJ006994; CAA07415.2; -; Genomic_DNA.
DR   PIR; S12900; S12900.
DR   PDB; 1QGW; X-ray; 1.63 A; A=53-128.
DR   PDB; 1XF6; X-ray; 1.10 A; A=53-128.
DR   PDB; 1XG0; X-ray; 0.97 A; A=53-128.
DR   PDBsum; 1QGW; -.
DR   PDBsum; 1XF6; -.
DR   PDBsum; 1XG0; -.
DR   AlphaFoldDB; Q00433; -.
DR   SMR; Q00433; -.
DR   EvolutionaryTrace; Q00433; -.
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   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF02972; Phycoerythr_ab; 1.
DR   SUPFAM; SSF56568; SSF56568; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Bile pigment; Chloroplast; Chromophore; Electron transport;
KW   Hydroxylation; Membrane; Photosynthesis; Plastid; Thylakoid;
KW   Transit peptide; Transport.
FT   TRANSIT         1..52
FT                   /note="Chloroplast"
FT   CHAIN           53..128
FT                   /note="Phycoerythrin alpha-3 chain, chloroplastic"
FT                   /id="PRO_0000002828"
FT   REGION          70..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         71
FT                   /ligand="15,16-dihydrobiliverdin"
FT                   /ligand_id="ChEBI:CHEBI:57899"
FT                   /note="covalent, via 1 link"
FT                   /evidence="ECO:0000269|PubMed:10430868,
FT                   ECO:0000269|PubMed:15504407"
FT   BINDING         73
FT                   /ligand="15,16-dihydrobiliverdin"
FT                   /ligand_id="ChEBI:CHEBI:57899"
FT                   /evidence="ECO:0000269|PubMed:10430868,
FT                   ECO:0000269|PubMed:15504407"
FT   BINDING         77..78
FT                   /ligand="15,16-dihydrobiliverdin"
FT                   /ligand_id="ChEBI:CHEBI:57899"
FT   BINDING         93
FT                   /ligand="15,16-dihydrobiliverdin"
FT                   /ligand_id="ChEBI:CHEBI:57899"
FT                   /evidence="ECO:0000269|PubMed:10430868,
FT                   ECO:0000269|PubMed:15504407"
FT   MOD_RES         56
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:10430868,
FT                   ECO:0000269|PubMed:15504407"
FT   STRAND          59..67
FT                   /evidence="ECO:0007829|PDB:1XG0"
FT   HELIX           86..89
FT                   /evidence="ECO:0007829|PDB:1XG0"
FT   STRAND          90..98
FT                   /evidence="ECO:0007829|PDB:1XG0"
FT   HELIX           103..113
FT                   /evidence="ECO:0007829|PDB:1XG0"
FT   STRAND          120..122
FT                   /evidence="ECO:0007829|PDB:1XG0"
SQ   SEQUENCE   128 AA;  13175 MW;  44B1ECFD62C12732 CRC64;
     MFAKTLASLA VIGSAAAYVP MMSMDMGRRE VVQAGAAAAA VTPFLSGAPA GAAMDKSAKA
     PQITIFDHRG CSRAPKESTG GKAGGQDDEM MVKVASTKVT VSESDAAKKL QEFITFEKGI
     DGPFTSKN
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024