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PHCA1_MICDP
ID   PHCA1_MICDP             Reviewed;         162 AA.
AC   P07122;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=C-phycocyanin-1 alpha subunit;
GN   Name=cpcA1;
OS   Microchaete diplosiphon (Fremyella diplosiphon).
OC   Bacteria; Cyanobacteria; Nostocales; Rivulariaceae; Microchaete.
OX   NCBI_TaxID=1197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Mazel D., Houmard J., Tandeau de Marsac N.;
RT   "A multigene family in Calothrix sp. PCC 7601 encodes phycocyanin, the
RT   major component of the cyanobacterial light harvesting antenna.";
RL   Mol. Gen. Genet. 211:296-304(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3127591; DOI=10.1016/0022-2836(88)90617-1;
RA   Conley P.B., Lemaux P.G., Grossman A.;
RT   "Molecular characterization and evolution of sequences encoding light-
RT   harvesting components in the chromatically adapting cyanobacterium
RT   Fremyella diplosiphon.";
RL   J. Mol. Biol. 199:447-465(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
RX   PubMed=3086870; DOI=10.1073/pnas.83.11.3924;
RA   Conley P.B., Lemaux P.G., Lomax T.L., Grossman A.R.;
RT   "Genes encoding major light-harvesting polypeptides are clustered on the
RT   genome of the cyanobacterium Fremyella diplosiphon.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:3924-3928(1986).
RN   [4] {ECO:0007744|PDB:1CPC}
RP   X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) IN COMPLEX WITH PHYCOCYANOBILIN
RP   CHROMOPHORE, AND SUBUNIT.
RX   PubMed=1899708; DOI=10.1016/0022-2836(91)90759-y;
RA   Duerring M., Schmidt G.B., Huber R.;
RT   "Isolation, crystallization, crystal structure analysis and refinement of
RT   constitutive C-phycocyanin from the chromatically adapting cyanobacterium
RT   Fremyella diplosiphon at 1.66-A resolution.";
RL   J. Mol. Biol. 217:577-592(1991).
CC   -!- FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the
CC       phycobiliprotein complex (phycobilisome, PBS). Phycocyanin is the major
CC       phycobiliprotein in the PBS rod.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit, which further
CC       assembles into trimers and the trimers into hexamers.
CC       {ECO:0000269|PubMed:1899708}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane
CC       protein; Cytoplasmic side. Note=Part of the phycobilisome rod.
CC   -!- INDUCTION: Phycocyanin-1 is expressed at similar levels in green and
CC       red light (constitutive phycocyanin).
CC   -!- PTM: Contains one covalently linked bilin chromophore.
CC       {ECO:0000269|PubMed:1899708, ECO:0007744|PDB:1CPC}.
CC   -!- SIMILARITY: Belongs to the phycobiliprotein family. {ECO:0000305}.
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DR   EMBL; X06084; CAA29465.1; -; Genomic_DNA.
DR   EMBL; X07013; CAA30065.1; -; Genomic_DNA.
DR   EMBL; M13218; AAA24879.1; -; Genomic_DNA.
DR   PIR; S00714; S00714.
DR   PDB; 1CPC; X-ray; 1.66 A; A/K=1-162.
DR   PDBsum; 1CPC; -.
DR   AlphaFoldDB; P07122; -.
DR   SMR; P07122; -.
DR   EvolutionaryTrace; P07122; -.
DR   GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.490.20; -; 1.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012128; Phycobilisome_asu/bsu.
DR   InterPro; IPR038719; Phycobilisome_asu/bsu_sf.
DR   InterPro; IPR006246; Phycocyanin_a.
DR   Pfam; PF00502; Phycobilisome; 1.
DR   PIRSF; PIRSF000081; Phycocyanin; 1.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   TIGRFAMs; TIGR01338; phycocy_alpha; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antenna complex; Bile pigment; Chromophore;
KW   Electron transport; Membrane; Photosynthesis; Phycobilisome; Thylakoid;
KW   Transport.
FT   CHAIN           1..162
FT                   /note="C-phycocyanin-1 alpha subunit"
FT                   /id="PRO_0000199113"
FT   BINDING         84
FT                   /ligand="(2R,3E)-phycocyanobilin"
FT                   /ligand_id="ChEBI:CHEBI:85275"
FT                   /note="covalent, via 1 link"
FT                   /evidence="ECO:0000269|PubMed:1899708,
FT                   ECO:0007744|PDB:1CPC"
FT   CONFLICT        13
FT                   /note="D -> H (in Ref. 2; CAA30065)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        17
FT                   /note="R -> A (in Ref. 2; CAA30065)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        67
FT                   /note="Missing (in Ref. 2; CAA30065)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        101
FT                   /note="Missing (in Ref. 2; CAA30065)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..14
FT                   /evidence="ECO:0007829|PDB:1CPC"
FT   HELIX           21..46
FT                   /evidence="ECO:0007829|PDB:1CPC"
FT   HELIX           48..62
FT                   /evidence="ECO:0007829|PDB:1CPC"
FT   HELIX           65..68
FT                   /evidence="ECO:0007829|PDB:1CPC"
FT   STRAND          74..77
FT                   /evidence="ECO:0007829|PDB:1CPC"
FT   HELIX           78..101
FT                   /evidence="ECO:0007829|PDB:1CPC"
FT   HELIX           105..110
FT                   /evidence="ECO:0007829|PDB:1CPC"
FT   TURN            111..114
FT                   /evidence="ECO:0007829|PDB:1CPC"
FT   HELIX           115..122
FT                   /evidence="ECO:0007829|PDB:1CPC"
FT   HELIX           126..139
FT                   /evidence="ECO:0007829|PDB:1CPC"
FT   HELIX           144..160
FT                   /evidence="ECO:0007829|PDB:1CPC"
SQ   SEQUENCE   162 AA;  17228 MW;  35D2745AD38B4FFD CRC64;
     MKTPLTEAVA AADSQGRFLS STEIQTAFGR FRQASASLAA AKALTEKASS LASGAANAVY
     SKFPYTTSQN GPNFASTQTG KDKCVRDIGY YLRMVTYCLV VGGTGPLDDY LIGGIAEINR
     TFDLSPSWYV EALKYIKANH GLSGDPAVEA NSYIDYAINA LS
 
 
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