ID A0A118K579_CYNCS Unreviewed; 691 AA.
AC A0A118K579;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 08-NOV-2023, entry version 25.
DE SubName: Full=Non-heme dioxygenase N-terminal domain-containing protein {ECO:0000313|EMBL:KVI08700.1};
GN ORFNames=Ccrd_012926 {ECO:0000313|EMBL:KVI08700.1};
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:KVI08700.1, ECO:0000313|Proteomes:UP000243975};
RN [1] {ECO:0000313|EMBL:KVI08700.1, ECO:0000313|Proteomes:UP000243975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2C {ECO:0000313|EMBL:KVI08700.1};
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 iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00008056}.
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:KVI08700.1}.
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DR EMBL; LEKV01001097; KVI08700.1; -; Genomic_DNA.
DR STRING; 59895.A0A118K579; -.
DR EnsemblPlants; KVI08700; KVI08700; Ccrd_012926.
DR Gramene; KVI08700; KVI08700; Ccrd_012926.
DR OMA; IGFESWP; -.
DR Proteomes; UP000243975; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR47990:SF81; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1.
DR Pfam; PF03171; 2OG-FeII_Oxy; 2.
DR Pfam; PF14226; DIOX_N; 2.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 2.
DR PROSITE; PS51471; FE2OG_OXY; 2.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000313|EMBL:KVI08700.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:KVI08700.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000243975}.
FT DOMAIN 149..253
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT DOMAIN 535..639
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 691 AA; 77263 MW; 0F125B2CCC1EC8A9 CRC64;
MATKCNIPVI DLHDFPNQSS KLMAACEEWG CFRLLNHHEV LPSTLMSEMK LVVRSLFDLP
VEIKRQNLDV IAGSGYMAPT AKNPLYEALG LYDMASSRDV QTFCSQLDAS PHQRGILTKY
AGAVHELFMR IGEKLAEGLR IKSENIGFES WPCQFRINKY HFTPQSVGSS GVQIHTDSGF
LTILQDDEDV GGLEVMDKSS HFIPVDPWPD SLLVNLGDMA TMWSNGRFCN VKHRVQCKEA
TTRVSIASFL LGPTEAIEPP PELMNADHPR VYVPTTYEDY RKLRLSTNLH AGEALALLQT
QTCEEWGCFR LLNHHKVLPP TPVSKMKSVV KLPFDLPVKI SMSLPEVDIR LRRQKNPPYE
ALGLDDMASF CDVKIFCSQL DASPRLMATK CSIPVIDLHD FPNQSSKLIA ASEEWGCFRL
LNHQQVLPST XMSEMKSVVR SLFNLPVEIK RRNLDVIAGS GFVAPTAKNP LYEALGLYDM
ASRCDVETFC SQLDASLHQR EIITKYAGAV HKLFMRIGEK LAQGLGVESE NIGFESWPCQ
FRINKYHFTP QSVGSSGVQI HTDSGFLTIL QDDEDVGGLE VMHKSGHXVP VDPWPDTLLV
NLGDMAAVWS NGRFCNVKHR VQCKGPTIRV SVASFLLGPR ETIEPLPELV DADHPRVYMP
TTYEEYRKLR LSTKLQAGEA LALLHTSSSN N
//