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Database: UniProt
Entry: A0A182MXI2_9DIPT
LinkDB: A0A182MXI2_9DIPT
Original site: A0A182MXI2_9DIPT 
ID   A0A182MXI2_9DIPT        Unreviewed;      1081 AA.
AC   A0A182MXI2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
OS   Anopheles dirus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7168 {ECO:0000313|EnsemblMetazoa:ADIR000085-PA, ECO:0000313|Proteomes:UP000075884};
RN   [1] {ECO:0000313|Proteomes:UP000075884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WRAIR2 {ECO:0000313|Proteomes:UP000075884};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles dirus WRAIR2.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:ADIR000085-PA}
RP   IDENTIFICATION.
RC   STRAIN=WRAIR2 {ECO:0000313|EnsemblMetazoa:ADIR000085-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362067};
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000256|RuleBase:RU362067}.
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DR   AlphaFoldDB; A0A182MXI2; -.
DR   STRING; 7168.A0A182MXI2; -.
DR   EnsemblMetazoa; ADIR000085-RA; ADIR000085-PA; ADIR000085.
DR   VEuPathDB; VectorBase:ADIR000085; -.
DR   OrthoDB; 2642916at2759; -.
DR   Proteomes; UP000075884; Unassembled WGS sequence.
DR   GO; GO:0008131; F:primary amine oxidase activity; IEA:UniProt.
DR   Gene3D; 3.90.660.10; -; 2.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001613; Flavin_amine_oxidase.
DR   PANTHER; PTHR10742:SF398; AMINO_OXIDASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 3.
DR   PRINTS; PR00757; AMINEOXDASEF.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 2.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|RuleBase:RU362067};
KW   Flavoprotein {ECO:0000256|RuleBase:RU362067};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362067}.
FT   DOMAIN          13..469
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
FT   DOMAIN          496..897
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
FT   DOMAIN          1043..1075
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
FT   REGION          956..987
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1006..1040
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1081 AA;  120443 MW;  BEAD397DCD498AA0 CRC64;
     MNPRIVIIGA GAAGVAAATR LIERGYRNVK ILEAENRIGG RIHTVPFGAN VVDLGAQWCH
     GEKGNVCYEL GSRYNVFDSN SARYERFVLT RSNGEQIPKE QSEKLLGLIW SILETHKHEL
     TGFRGSLGAF IMGKFRALLE TPEYADVSGE TAYQVLEFFQ KFENSIEASD SWYDTSGPGY
     LHYWECDGDL LLNWRDKGYR TVLEILMKRH PLPIAADAIN LEDYTHFNKT VANINWTAGP
     DSLVSIRCTD NSVYDADHVI CTISLGVLKE RYQTLFTPDL PPIKRNAIQG LTIGTVNKLF
     LEFDKPFWAK GWQGLSLIWN QADLDEVRKL PDSWMEDVFG FYIVDYQPNV LCGWISGKNA
     RRMERASDED VRRSCMFLLR KFMKGCTIPE PVRFQRTTWY SNPNFRGSYT FRSLTTDLLN
     TSASHLAIPL TNSCGMPVVQ FAGEATHDHY YSTVHGAVET GWREASRLID LYDRLIPPFN
     HGPKAYVDVL ILGAGIAGLG AAKQLRNSGK SFAILEAQSG PGGRVSTKAL KKPHAGAKGQ
     SQLVEAGAQW LHGRQNELHE VAKRNGLLRE ETSEEGLGEF LRDDGFRIDD HLAKKVDFIV
     GQILEQCEEF AARAVHDRDA TYPASLEAFL REQFRKRTEK EFTAEQKVLA QQLLDWHCRF
     QIIDNSCLHV SDISAKLWGS YSFNGESCQA HINMRYGFQA LVSCLIEEIG LEKIVYNKAI
     CEIRWLDARG KVIVKCTDGT VYCCQHLVVT FSLGVLKDTM DQLFQPNLPA SFSRSIRSIG
     YGTIDKIFLQ FEDAWWGKAE GIQLVWRDEL RKDSHWTRFI SGFDVLSPGP ANTLLGWIGS
     YGALEMEALN DEQIVSDCVF ILEKFTKKKV PKPVNYYCTR WNSNRYIRGS YSYTSVNCDR
     EQNFMSNLTE TLVCNQYDKS GEESRKKDTL PSLAACSAVA SSASLDASNV RGAAGMSACT
     TSGHSTSSSN SSNTLTTVPT HGGSTTPSKV LASSVHKITT DPVTITDTSK SANTTPPLST
     AAKAATKGTS SSKSNVSGST QTSATIHFAG EACHERYFST VHGAYLSGME QAKKIMLLDK
     Q
//
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