ID A0A2G5CW52_AQUCA Unreviewed; 166 AA.
AC A0A2G5CW52;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Plastocyanin {ECO:0000256|RuleBase:RU363020};
GN ORFNames=AQUCO_03500105v1 {ECO:0000313|EMBL:PIA35509.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA35509.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA35509.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Participates in electron transfer between P700 and the
CC cytochrome b6-f complex in photosystem I.
CC {ECO:0000256|RuleBase:RU363020}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|PIRSR:PIRSR602387-1};
CC Note=The crystal structure with reduced Cu(1+) has also been
CC determined. {ECO:0000256|PIRSR:PIRSR602387-1};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000256|ARBA:ARBA00004622, ECO:0000256|RuleBase:RU363020};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004622,
CC ECO:0000256|RuleBase:RU363020}; Lumenal side
CC {ECO:0000256|ARBA:ARBA00004622, ECO:0000256|RuleBase:RU363020}.
CC -!- SIMILARITY: Belongs to the plastocyanin family.
CC {ECO:0000256|ARBA:ARBA00005338, ECO:0000256|RuleBase:RU363020}.
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DR EMBL; KZ305052; PIA35509.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5CW52; -.
DR STRING; 218851.A0A2G5CW52; -.
DR InParanoid; A0A2G5CW52; -.
DR OrthoDB; 471748at2759; -.
DR Proteomes; UP000230069; Unassembled WGS sequence.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR CDD; cd04219; Plastocyanin; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR InterPro; IPR000923; BlueCu_1.
DR InterPro; IPR028871; BlueCu_1_BS.
DR InterPro; IPR001235; Copper_blue_Plastocyanin.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR002387; Plastocyanin.
DR NCBIfam; TIGR02656; cyanin_plasto; 1.
DR PANTHER; PTHR34192; PLASTOCYANIN MAJOR ISOFORM, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR34192:SF10; PLASTOCYANIN MAJOR ISOFORM, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00127; Copper-bind; 1.
DR PRINTS; PR00156; COPPERBLUE.
DR PRINTS; PR00157; PLASTOCYANIN.
DR SUPFAM; SSF49503; Cupredoxins; 1.
DR PROSITE; PS00196; COPPER_BLUE; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRSR:PIRSR602387-1};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|RuleBase:RU363020};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363020};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602387-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000230069};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|RuleBase:RU363020};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU363020}.
FT DOMAIN 69..166
FT /note="Blue (type 1) copper"
FT /evidence="ECO:0000259|Pfam:PF00127"
FT BINDING 104
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR602387-1"
FT BINDING 151
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR602387-1"
FT BINDING 154
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR602387-1"
FT BINDING 159
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR602387-1"
SQ SEQUENCE 166 AA; 16966 MW; 2501F2BC9095CFDF CRC64;
MATVTSASVA IPSFTGLKAG ATTRVANFSK VSASSTPMVS VKASLKDVGV AVAVTAATVM
FASNAMAVEV LLGSDDGGLA FVPSDFSVSA GEKIVFKNNA GFPHNVVFDE DEIPSGVEVS
KISMGEEDYL NAPGESYAVT LDAKGTYKFY CAPHQGAGMI GKVTVN
//
