ID A0A0R3S1M1_9BILA Unreviewed; 908 AA.
AC A0A0R3S1M1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000856901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000856901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) 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; A0A0R3S1M1; -.
DR STRING; 1147741.A0A0R3S1M1; -.
DR WBParaSite; EEL_0000856901-mRNA-1; EEL_0000856901-mRNA-1; EEL_0000856901.
DR Proteomes; UP000050640; Unplaced.
DR GO; GO:0140682; F:FAD-dependent H3K4me/H3K4me3 demethylase activity; IEA:UniProt.
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 Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR PANTHER; PTHR10742:SF413; LYSINE-SPECIFIC HISTONE DEMETHYLASE 1B; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF04433; SWIRM; 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 SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS50934; SWIRM; 1.
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 339..437
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 908 AA; 102319 MW; B86C91184072BC76 CRC64;
MHSPAYECGE NKNLTHYDFS NGARRGSTIS SFNGSSRDQQ DQKSGNVAEN GYDIESTNKS
ELAYLLYLNL KNNQEEMEME DEEGSNDSKR VRHHRESAEV AKKRLKLDLK SSVDRGSAEN
GSESNESREG SCERNDCGHL KKCALDVSSA CYGRENGGST HPADGNCNNK TFHHISKGEH
VCCACYDEIW KPGRTGNDRF NEWKGKWASE SRCTPCVRLY IQDQLLPFWL QCKLCNKRLP
TSVSSINRED VERFVCGSQT EADKDSTNDP CDVKEEECVQ EASERIWIKS VSIPPLLHNS
PAAPFLRHEY YYDEVGISPT NEILGHENVR SFMRPFNIPH EQSMAFCLRP DVMEYDELHS
FPEYATEPVA YLAMRNLVIA LWNLNPFQYL TVECCIPHVI CRGLARVWYI NELKRVINFL
SLKSLINYGV LNFPKTSIFT SKYNDMEVVI VGAGISGLTA ARQLRSFGAR VKVLEAKGKL
GGRLLDDWSL GVAVGSGAQL ITGIINNPIV LMCEQIGVVY RAVKDECPLL DAGTGKRASS
ICDRVVDEHF NCLLDCLADW KQKVKVGDES LYDRIMALHN AFLKTTGLKW TEEEERMLQW
QIGNVEFSCG SKLDGVSARN WDQNEAVAQF AGVHALLTDG TSELMRRLAE GTDIRCNHEV
SRIEWLGRKK ILVKCSNGKK YSCDKVLVTT PLAVLQKELI TFVPALPPTK TVALNNLGAG
LIEKVAVKFS RRFWLSILKS DGTLDYFGHV PKNADERGLF NMFYDFSTRG SKNHHYVLMS
YVCGDSVNLV NEKSDVEVVD IFVDTLRDMF PEENIPDPEG YVVTHWGRDR HIGMSYTYVR
VGGNGDDYDR LAEDIDEKLF FAGEGTNRFF PQTMTGACVS GLREAGKIAN SWLKQTSNYT
ENECCIYE
//