ID A0A103YH68_CYNCS Unreviewed; 554 AA.
AC A0A103YH68;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Cupredoxin {ECO:0000313|EMBL:KVI09024.1};
GN ORFNames=Ccrd_012608 {ECO:0000313|EMBL:KVI09024.1};
OS Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC Carduinae; Cynara.
OX NCBI_TaxID=59895 {ECO:0000313|EMBL:KVI09024.1, ECO:0000313|Proteomes:UP000243975};
RN [1] {ECO:0000313|EMBL:KVI09024.1, ECO:0000313|Proteomes:UP000243975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2C {ECO:0000313|EMBL:KVI09024.1};
RX PubMed=26786968; DOI=10.1038/srep19427;
RA Scaglione D., Reyes-Chin-Wo S., Acquadro A., Froenicke L., Portis E.,
RA Beitel C., Tirone M., Mauro R., Lo Monaco A., Mauromicale G., Faccioli P.,
RA Cattivelli L., Rieseberg L., Michelmore R., Lanteri S.;
RT "The genome sequence of the outbreeding globe artichoke constructed de novo
RT incorporating a phase-aware low-pass sequencing strategy of F1 progeny.";
RL Sci. Rep. 6:19427-19427(2016).
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KVI09024.1}.
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DR EMBL; LEKV01001074; KVI09024.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A103YH68; -.
DR STRING; 59895.A0A103YH68; -.
DR EnsemblPlants; KVI09024; KVI09024; Ccrd_012608.
DR Gramene; KVI09024; KVI09024; Ccrd_012608.
DR OMA; NSNWTYK; -.
DR Proteomes; UP000243975; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR001117; Cu-oxidase_2nd.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709:SF530; LACCASE-RELATED; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 2.
DR SUPFAM; SSF49503; Cupredoxins; 3.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000243975};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..554
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007119714"
FT TRANSMEM 81..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..84
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 102..164
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 177..313
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 394..533
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 554 AA; 62807 MW; 3625D8971BE7BFDB CRC64;
MNHPIFLPFY LGFLAWLCLF SVKAEDPYKF FTMEVTYGQI NPLGVPQRGI LINGRFPGPT
IDCVTNDNVI VNVINKLDEP FLITCYTFVF LFFFVSWDQD SNGIKQRKTS WQDGVLGTNC
PIPPNSNWTY QMQMKDQIGS FSYFPSTLMH RAAGGYGGIN IYARAVIFVP YLKPVEQFTL
LVSDWWKSDH KVLQQTLDSG KPLPMADALL INGHPSLKSF TVLGGQLYMF RVSNVALTTS
INFRIQGHTM TLVETEGSHT LQETYESLDL HVGQSASFLV RMSASPKDYF IVASTRFTKP
ILTATSILHY DGSNTKASLP LPTAPTYHIH WSMKQARTIR WNLTANAARP NPQGSYHYGT
IPVTRTIVLA NSEENINGKL RYAVNQVSYV NPETPLKIAD FYNISGVFKL NSTKDTPHSI
PATLGTSVLG FTLHDYVEII FQNNENTTQS WHLDGSDFWP VGFGSGQWDT TKRRRFYNLN
DATTRHTVQV YPKSWSAILV SLDNKGMWNL RSAIWPRQYL GQQLYIKVWN DEQSYRTEYG
IPDNALRCGQ APLK
//
