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Database: UniProt
Entry: A0A212EY39_DANPL
LinkDB: A0A212EY39_DANPL
Original site: A0A212EY39_DANPL 
ID   A0A212EY39_DANPL        Unreviewed;       562 AA.
AC   A0A212EY39;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Putative carotinoid oxygenase {ECO:0000313|EMBL:OWR46413.1};
GN   ORFNames=KGM_212590 {ECO:0000313|EMBL:OWR46413.1};
OS   Danaus plexippus plexippus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Nymphalidae; Danainae; Danaini; Danaina; Danaus; Danaus.
OX   NCBI_TaxID=278856 {ECO:0000313|EMBL:OWR46413.1, ECO:0000313|Proteomes:UP000007151};
RN   [1] {ECO:0000313|EMBL:OWR46413.1, ECO:0000313|Proteomes:UP000007151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F-2 {ECO:0000313|EMBL:OWR46413.1};
RX   PubMed=22118469; DOI=10.1016/j.cell.2011.09.052;
RA   Zhan S., Merlin C., Boore J.L., Reppert S.M.;
RT   "The monarch butterfly genome yields insights into long-distance
RT   migration.";
RL   Cell 147:1171-1185(2011).
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|PIRSR:PIRSR604294-1};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR604294-1};
CC   -!- SIMILARITY: Belongs to the carotenoid oxygenase family.
CC       {ECO:0000256|ARBA:ARBA00006787}.
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:OWR46413.1}.
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DR   EMBL; AGBW02011623; OWR46413.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A212EY39; -.
DR   SMR; A0A212EY39; -.
DR   STRING; 278856.A0A212EY39; -.
DR   KEGG; dpl:KGM_212590; -.
DR   eggNOG; KOG1285; Eukaryota.
DR   InParanoid; A0A212EY39; -.
DR   Proteomes; UP000007151; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro.
DR   InterPro; IPR004294; Carotenoid_Oase.
DR   PANTHER; PTHR10543; BETA-CAROTENE DIOXYGENASE; 1.
DR   PANTHER; PTHR10543:SF24; CAROTENOID ISOMEROOXYGENASE; 1.
DR   Pfam; PF03055; RPE65; 2.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR604294-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR604294-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007151}.
FT   BINDING         184
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         242
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         312
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         500
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ   SEQUENCE   562 AA;  63677 MW;  284719C625E7C33B CRC64;
     MEQCKEKLYP NCDNQVWLRS CEVEVNEPIT GEITGEFPRW VRGSLLRNGP GSLKVGSMRF
     KHLFDSSALL HRFNIQDGQV TYQCRFLRCN TYNRNMAAGR IVVTDFGTQS VPDPCHSIFD
     RFATLFSPGE ALSDNAMISV YPFGDEMYAF TEGPVIHRIN PVTLDTMERK NLMDSVALVN
     HTSHPHVMSN GDVYNVGMSL VKGRLRHVVV KFPFMEKGDM FQNATIVGSM KPRWTLHPAY
     MHTFGITANY FVIIEQPLSV SICRLVHNQL RNRPLASSLK WYPEHKTNIV LINRETGKEV
     KRYETETLFF LHIINCYEIA NKLIVDLCSY KDAKILDAMY IQAIETMQTN ANYADWFRGR
     PKRIEIDLNA PILTHFKPRL LADLGCETPR IHYDVYNGRP YRYFYAISSD VDAENPGLII
     KVDTVTGQTQ TWFNNNCYPS EPVFVPRCDG KSEDDGVLLT ALVKADDSHS VSLVCLCAVT
     LKELARCTFT TPSPTPKCLH GWFLPDSEDD GVLLTALVKA DDSHSVSLVC LCAVTLKELA
     RCTFTTPSPT PKCLHGWFLP DV
//
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