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Database: UniProt
Entry: A0A182JL50_9DIPT
LinkDB: A0A182JL50_9DIPT
Original site: A0A182JL50_9DIPT 
ID   A0A182JL50_9DIPT        Unreviewed;       574 AA.
AC   A0A182JL50;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   03-JUL-2019, entry version 14.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|VectorBase:AATE020101-PA};
OS   Anopheles atroparvus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Nematocera; Culicoidea;
OC   Culicidae; Anophelinae; Anopheles.
OX   NCBI_TaxID=41427 {ECO:0000313|Proteomes:UP000075880, ECO:0000313|VectorBase:AATE020101-PA};
RN   [1] {ECO:0000313|VectorBase:AATE020101-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EBRO {ECO:0000313|VectorBase:AATE020101-PA};
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S.,
RA   Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Anopheles atroparvus EBRO.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000075880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EBRO {ECO:0000313|Proteomes:UP000075880};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S.,
RA   Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Anopheles atroparvus EBRO.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|VectorBase:AATE020101-PA}
RP   IDENTIFICATION.
RC   STRAIN=EBRO {ECO:0000313|VectorBase:AATE020101-PA};
RG   VectorBase;
RL   Submitted (JUN-2016) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|RuleBase:RU003968}.
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DR   VectorBase; AATE020101-RA; AATE020101-PA; AATE020101.
DR   Proteomes; UP000075880; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000075880};
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075880}.
FT   DOMAIN       45     68       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00623}.
FT   DOMAIN      222    236       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00624}.
FT   REGION      554    574       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A182JL50}.
FT   BINDING      47     47       FAD; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000137-2}.
FT   BINDING     185    185       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000137-
FT                                2}.
SQ   SEQUENCE   574 AA;  64359 MW;  B8CA1C51CE42C3C0 CRC64;
     MSDSVDAYAS TTRDYWTRFR IQGWTQPQKT ACQAMKDNRC CWTRGKVLGG SSVLNTMLYI
     RGNKRDFDLW RALGNPGWGY EDVLPYFRKS EDQRNPYLAR NKRQHGTGGL LQVQDAPYLT
     PLGVSFLQAG EEMGYDIVDV NGEQQTGFAF FQFTMRRGTR CSTSKAFLRP VRNRKNLHVA
     LFAHVTRVIL DPVTRRALGV EFIRHGKTQQ VFATREVILS AGAIGTPHLL MLSGIGSREN
     LERVGIPVVH ELPGVGQNLQ DHIAVGGLVF RIDQPISTIM NRLVNLNSAL RYAITEDGPL
     TSSIGLEAVG FISTKYANQT DDWPDIEFML TSASTPSDGG DQVKKAHGLK DEFYEDMFSA
     INNQDVFGVF PMMLRPKSRG FIRLQSRNPL RYPLLYHNYL THPDDVGVLR EGVKAAIAFG
     ETQAMKRFGA RFHSKQVPNC RHLPEFTDEY WDCAIRQYTM TIYHMSGTAK MGPPDDPWAV
     VDPKLRVYGI KGLRVIDASI MPRITSGNIN APVIMIGEKG ADLIKELWLQ GKTRRGKRQE
     LFANETITVV PVANQTEPFP EASTTNCPNG TTAS
//
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