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Database: UniProt
Entry: A0A0K0EJV0_STRER
LinkDB: A0A0K0EJV0_STRER
Original site: A0A0K0EJV0_STRER 
ID   A0A0K0EJV0_STRER        Unreviewed;       512 AA.
AC   A0A0K0EJV0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   22-FEB-2023, entry version 23.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
OS   Strongyloides stercoralis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=6248 {ECO:0000313|Proteomes:UP000035681, ECO:0000313|WBParaSite:SSTP_0000974100.1};
RN   [1] {ECO:0000313|Proteomes:UP000035681}
RP   NUCLEOTIDE SEQUENCE.
RA   Martin A.A.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:SSTP_0000974100.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) 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; A0A0K0EJV0; -.
DR   STRING; 6248.A0A0K0EJV0; -.
DR   WBParaSite; SSTP_0000974100.1; SSTP_0000974100.1; SSTP_0000974100.
DR   Proteomes; UP000035681; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008131; F:primary amine oxidase activity; IEA:UniProt.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001613; Flavin_amine_oxidase.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR   PANTHER; PTHR10742:SF405; PEROXISOMAL N(1)-ACETYL-SPERMINE/SPERMIDINE OXIDASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   PRINTS; PR00757; AMINEOXDASEF.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|RuleBase:RU362067};
KW   Flavoprotein {ECO:0000256|RuleBase:RU362067};
KW   Membrane {ECO:0000256|RuleBase:RU362067};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362067};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035681};
KW   Transmembrane {ECO:0000256|RuleBase:RU362067};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362067}.
FT   TRANSMEM        25..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362067"
FT   DOMAIN          55..93
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   512 AA;  59835 MW;  C567E1E68C669242 CRC64;
     MQINFLACYS KYFFKMLNLI RYNHLKFSFF LLTFITFILL SLEKDNFEES IAIIGGGIAG
     ITAYNTLKNY GYKNVKIFEG SNRLGGRVYP LKYKNGYLQL GAQFINGQKN PIYKLAKKLN
     ILNGVENDDD FIYMGEYKLG SCNLSNNILE SFTKFSRNLE RYYEKLSRNS VMKEKSVGDM
     FYDDYKSFLF KETKFGDKIK IKKYYDALVK LYKSYYEIEW SSPIEKLSLI NLDLWDDKEN
     ELKSYTLNNI GYQAILDYLL QNITDSDIQL NSRIININYS NYKKILLTLN NGKIITNYTK
     IIVTVPLGHL KKYGYSLFTP TLNKKRMKAI NLLGFGNMQK IFFYYDKPFW DENTKWIHTL
     SIDGCTNTNI FSEIFQSFQP LEWMNKNILV GWLSGKGPHL IKDIPDNILS DIITNHFRNT
     FNNSLIPKPI EIKQKSWVSD ELFLGSYTYY TPESNLLNED PIKTISRPIF KNKKPIIMFA
     GEGTHPSIYQ TVIGAYLSGQ REAKRIFRHN HV
//
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