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PHE2_RHDS2
ID   PHE2_RHDS2              Reviewed;         104 AA.
AC   P30943; Q8VX02;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Phycoerythrin alpha-2 chain, chloroplastic;
DE   Flags: Precursor;
GN   Name=cpeA2;
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].
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   [2]
RP   PROTEIN SEQUENCE OF 38-82.
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   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 38-104 IN COMPLEX WITH CPEA2;
RP   CPEA3 AND 15,16-DIHYDROBILIVERDIN, SUBUNIT, AND HYDROXYLATION AT LYS-41.
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   [4]
RP   X-RAY CRYSTALLOGRAPHY (0.97 ANGSTROMS) OF 38-104 IN COMPLEX WITH CPEA2;
RP   CPEA3 AND 15,16-DIHYDROBILIVERDIN, AND SUBUNIT.
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}.
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DR   EMBL; AJ006994; CAD20039.1; -; Genomic_DNA.
DR   PIR; T10881; T10881.
DR   PDB; 1QGW; X-ray; 1.63 A; B=38-104.
DR   PDB; 1XF6; X-ray; 1.10 A; B=38-104.
DR   PDB; 1XG0; X-ray; 0.97 A; B=38-104.
DR   PDBsum; 1QGW; -.
DR   PDBsum; 1XF6; -.
DR   PDBsum; 1XG0; -.
DR   AlphaFoldDB; P30943; -.
DR   SMR; P30943; -.
DR   EvolutionaryTrace; P30943; -.
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   3D-structure; Bile pigment; Chloroplast; Chromophore;
KW   Direct protein sequencing; Electron transport; Hydroxylation; Membrane;
KW   Photosynthesis; Plastid; Thylakoid; Transit peptide; Transport.
FT   TRANSIT         1..37
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:2226853"
FT   CHAIN           38..104
FT                   /note="Phycoerythrin alpha-2 chain, chloroplastic"
FT                   /id="PRO_0000002827"
FT   REGION          61..63
FT                   /note="15,16-dihydrobiliverdin chromophore"
FT   BINDING         56
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         58
FT                   /ligand="15,16-dihydrobiliverdin"
FT                   /ligand_id="ChEBI:CHEBI:57899"
FT                   /evidence="ECO:0000269|PubMed:10430868,
FT                   ECO:0000269|PubMed:15504407"
FT   BINDING         78
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         41
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:10430868"
FT   CONFLICT        63..74
FT                   /note="YTGAKAGGKDDE -> TSKSGKSGQDDT (in Ref. 2; AA
FT                   sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          44..52
FT                   /evidence="ECO:0007829|PDB:1XG0"
FT   HELIX           71..74
FT                   /evidence="ECO:0007829|PDB:1XG0"
FT   STRAND          75..83
FT                   /evidence="ECO:0007829|PDB:1XG0"
FT   HELIX           88..101
FT                   /evidence="ECO:0007829|PDB:1XG0"
SQ   SEQUENCE   104 AA;  10696 MW;  1474D433E8CB4396 CRC64;
     MSAKIIAFSA VVATASAFAP TAGFVPRLRS GATSVNMAMD KSAKAPVITI FDHRGCSRAP
     KEYTGAKAGG KDDEMMVKAQ SVKIEVSTGT AEGVLATSLA KMTK
 
 
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