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Database: UniProt
Entry: W5J3D8_ANODA
LinkDB: W5J3D8_ANODA
Original site: W5J3D8_ANODA 
ID   W5J3D8_ANODA            Unreviewed;       785 AA.
AC   W5J3D8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Beta,beta-carotene 15,15'-monooxygenase {ECO:0000313|EMBL:ETN58862.1};
GN   ORFNames=AND_009524 {ECO:0000313|EMBL:ETN58862.1};
OS   Anopheles darlingi (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=43151 {ECO:0000313|EMBL:ETN58862.1};
RN   [1] {ECO:0000313|EMBL:ETN58862.1, ECO:0000313|Proteomes:UP000000673}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20920257; DOI=10.1186/1471-2164-11-529;
RA   Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.;
RT   "Combination of measures distinguishes pre-miRNAs from other stem-loops in
RT   the genome of the newly sequenced Anopheles darlingi.";
RL   BMC Genomics 11:529-529(2010).
RN   [2] {ECO:0000313|EMBL:ETN58862.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Almeida L.G., Nicolas M.F., Souza R.C., Vasconcelos A.T.R.;
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ETN58862.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23761445;
RA   Marinotti O., Cerqueira G.C., de Almeida L.G., Ferro M.I., Loreto E.L.,
RA   Zaha A., Teixeira S.M., Wespiser A.R., Almeida E Silva A.,
RA   Schlindwein A.D., Pacheco A.C., Silva A.L., Graveley B.R., Walenz B.P.,
RA   Lima Bde A., Ribeiro C.A., Nunes-Silva C.G., de Carvalho C.R., Soares C.M.,
RA   de Menezes C.B., Matiolli C., Caffrey D., Araujo D.A., de Oliveira D.M.,
RA   Golenbock D., Grisard E.C., Fantinatti-Garboggini F., de Carvalho F.M.,
RA   Barcellos F.G., Prosdocimi F., May G., Azevedo Junior G.M., Guimaraes G.M.,
RA   Goldman G.H., Padilha I.Q., Batista Jda S., Ferro J.A., Ribeiro J.M.,
RA   Fietto J.L., Dabbas K.M., Cerdeira L., Agnez-Lima L.F., Brocchi M.,
RA   de Carvalho M.O., Teixeira Mde M., Diniz Maia Mde M., Goldman M.H.,
RA   Cruz Schneider M.P., Felipe M.S., Hungria M., Nicolas M.F., Pereira M.,
RA   Montes M.A., Cantao M.E., Vincentz M., Rafael M.S., Silverman N.,
RA   Stoco P.H., Souza R.C., Vicentini R., Gazzinelli R.T., Neves Rde O.,
RA   Silva R., Astolfi-Filho S., Maciel T.E., Urmenyi T.P., Tadei W.P.,
RA   Camargo E.P., de Vasconcelos A.T.;
RT   "The genome of Anopheles darlingi, the main neotropical malaria vector.";
RL   Nucleic Acids Res. 41:7387-7400(2013).
RN   [4] {ECO:0000313|EnsemblMetazoa:ADAC009524-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
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}.
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DR   EMBL; ADMH02002111; ETN58862.1; -; Genomic_DNA.
DR   AlphaFoldDB; W5J3D8; -.
DR   STRING; 43151.W5J3D8; -.
DR   EnsemblMetazoa; ADAC009524-RA; ADAC009524-PA; ADAC009524.
DR   VEuPathDB; VectorBase:ADAC009524; -.
DR   VEuPathDB; VectorBase:ADAR2_004906; -.
DR   eggNOG; KOG1285; Eukaryota.
DR   HOGENOM; CLU_016472_1_1_1; -.
DR   OMA; RDFFAVK; -.
DR   OrthoDB; 294919at2759; -.
DR   Proteomes; UP000000673; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004497; F:monooxygenase activity; 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   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   PANTHER; PTHR10543; BETA-CAROTENE DIOXYGENASE; 1.
DR   PANTHER; PTHR10543:SF24; CAROTENOID ISOMEROOXYGENASE; 1.
DR   Pfam; PF03055; RPE65; 1.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
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   Monooxygenase {ECO:0000313|EMBL:ETN58862.1};
KW   Oxidoreductase {ECO:0000313|EMBL:ETN58862.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000673}.
FT   REGION          56..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          574..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..189
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..592
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         389
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         445
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         515
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         775
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ   SEQUENCE   785 AA;  86852 MW;  54EF480B7B9F40FA CRC64;
     MDVTVEDFCE ETNFSESPCP SPFDANILLN MGFLQINGRF TPHSAHSSAC STRSCSLAAT
     PVPPETASSE TGPGPQLTVP DDRDGSSGPG PRARKCSLVT VPTEATKFEI SGRATPVFTW
     NPIPTSTNVI YALSETSQQI VFSQLEQEAE TETEGSISGV SSDAESECGE LEHDDATNTV
     PRARQSEHKD PAAAAAAAAD RKQQEAPNNN NMYPNCDVNV WLRSCEQEIV QPIEGTVKGT
     VPEWLNGSLL RNGPGSLKVG DMMFNHLFDS SALLHRFNIN EGKVTYQCRF LKSDAYKKNT
     AARRIVVTEF GTSAVPDPCQ TIFQKVAAIF NKPGANNSDN AMISIYPFGD EFFAFTESPI
     IHRIDPETLD TEAKLNVSDY VGIVNHTSHP HVMSDGTVYN LGCSVTKTGP AYTIICFPHG
     EGMFENARIV ASVPARWKFH PGYMHTFGIT ENFYVIVEQP LSVSVPTMVV SQIRNKPMAA
     ALKWFESQQT YIYLLDRDTG ELRHTYHTDP FFYLHIINQY EQDGHVVLDI CCYKDPAMLN
     CMYVETMRDM QNNPDYAKMF RGRPLRFVLP LQKQKSAGGS SSTSSSSKLP RGVSVDDASW
     TDMWQHLANG AEKECPADDR QTAGLVLQNL VRLAGTKATA YVMPNRTIFC KPELLCDLGC
     ETPRIYYECH LGRPYRYFYA ISSDVDASNP GTLIKVDVVS KSRLTWCEEN VYPSEPIFVP
     GPDPQSEDDG VVLAAMVWGR EEENRAGLLV LDAKTFTELG RCEFTTPGPV PKCLHGWFQP
     SQPKQ
//
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