ID A0A124SEE7_CYNCS Unreviewed; 432 AA.
AC A0A124SEE7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Oxoglutarate/iron-dependent dioxygenase {ECO:0000313|EMBL:KVH99880.1};
GN ORFNames=Ccrd_021882 {ECO:0000313|EMBL:KVH99880.1};
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:KVH99880.1, ECO:0000313|Proteomes:UP000243975};
RN [1] {ECO:0000313|EMBL:KVH99880.1, ECO:0000313|Proteomes:UP000243975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2C {ECO:0000313|EMBL:KVH99880.1};
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 -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|PIRSR:PIRSR604574-2};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR604574-2};
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:KVH99880.1}.
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DR EMBL; LEKV01003409; KVH99880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A124SEE7; -.
DR SMR; A0A124SEE7; -.
DR STRING; 59895.A0A124SEE7; -.
DR EnsemblPlants; KVH99880; KVH99880; Ccrd_021882.
DR Gramene; KVH99880; KVH99880; Ccrd_021882.
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:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 2.
DR InterPro; IPR004574; Alkb.
DR InterPro; IPR027450; AlkB-like.
DR InterPro; IPR037151; AlkB-like_sf.
DR PANTHER; PTHR16557; ALKYLATED DNA REPAIR PROTEIN ALKB-RELATED; 1.
DR PANTHER; PTHR16557:SF2; NUCLEIC ACID DIOXYGENASE ALKBH1; 1.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 2.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000313|EMBL:KVH99880.1};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Iron {ECO:0000256|PIRSR:PIRSR604574-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR604574-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000243975}.
FT DOMAIN 238..327
FT /note="Alpha-ketoglutarate-dependent dioxygenase AlkB-like"
FT /evidence="ECO:0000259|Pfam:PF13532"
FT DOMAIN 350..430
FT /note="Alpha-ketoglutarate-dependent dioxygenase AlkB-like"
FT /evidence="ECO:0000259|Pfam:PF13532"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 400
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
SQ SEQUENCE 432 AA; 47666 MW; 5BFC9C6D7523D2C3 CRC64;
MWSYSRQRNR FASGKSDSRR KNTTGGSRME WKPKAKVATD GSLGSASSSQ RDNSQSFNSE
PASDVNSPQE SLLPLIKDLA SGMENLNQMH ASNDSKHLAS VLTSDYSSKE SLTLSCQSES
SHMHPIREKT HSCPSKGRTG RGSEMYATPI KPSSVVCFPM EDRIPENGKQ IVVKFEEKAD
NSGKPEDTDC ASPIMRFDIC PRSSVIKIKP PLHVINKEKR NQLKRSVEGQ NFKILRPGMV
LMKGYISCDE QIGIVKTCRE LGLGDGGFYQ PGYRDGSKVH LKMMCLGKNW DPQTSEYSDT
RPIDNSKPPD IPDKFRDMVK KAIRDSNDHI QKSNSKADAG TIIPPISESI DQGLPVVSFS
IGDSADFLFG NVGDIDEATR VILESGDVLI FGGKSRSIFH GVASIRPDTA PLSLLEATNM
RPGRLNLTFR QF
//
