ID U7PXZ9_SPOS1 Unreviewed; 812 AA.
AC U7PXZ9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Amine oxidase domain-containing protein {ECO:0000259|Pfam:PF01593};
GN ORFNames=HMPREF1624_03191 {ECO:0000313|EMBL:ERS99826.1};
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS99826.1, ECO:0000313|Proteomes:UP000018087};
RN [1] {ECO:0000313|Proteomes:UP000018087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183
RC {ECO:0000313|Proteomes:UP000018087};
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(2014).
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DR EMBL; KI440844; ERS99826.1; -; Genomic_DNA.
DR AlphaFoldDB; U7PXZ9; -.
DR STRING; 1391915.U7PXZ9; -.
DR eggNOG; KOG1276; Eukaryota.
DR HOGENOM; CLU_009629_1_0_1; -.
DR OrthoDB; 65450at2759; -.
DR Proteomes; UP000018087; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR42923; PROTOPORPHYRINOGEN OXIDASE; 1.
DR PANTHER; PTHR42923:SF3; PROTOPORPHYRINOGEN OXIDASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000018087};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..533
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT REGION 61..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 89112 MW; 481B107FF8FB3937 CRC64;
MSQRRRASFS PSPRLPVPKR VAVIGGGLTG LTTAYYLAML LPATSHITVY EGSGRLGGWI
DSESSSSSTT SDTANNEKKK DAGEHERTDV LEAGARMVAP QKGARYDDFL LLELIDQLGL
HEELRVSEWK AAQYIYYPDH LVNVSLGNLR PQRPQAEDNQ EGRSVTLAEQ LAYWKAFGRW
VVWCATRVLQ EPLFRSLLPG AFSYLLPSTA KAEKMQARMV AASKAPGRYP PASDDESAGA
FMTRMSGGNT ALTDNMLSAV MHGIYGGDVW KLSVASSILR PQWLKEAAGP LFRLYDRQAK
IAELRRQQAA RMGRAQPEDH DDFPGQNAGL GGGIAGFPPL TAETLRFAEE YSAAKGKVEL
MMESDLQLLH DIMLRLRDRY EPWLAAAQKK RGTPGYEGDA DDGLPREASP FDRLPMLMMR
STGWTQFGFA QGFGTLTDAL ARSLRSRPNV TIRSGEPVTG LRYEAQRVRV ATPKTSADGD
AYDRVVSTVA SPTLFRMAGG SDTSGDSGQL PSLRDAHAVT IMVVNLHYAE PNLHRPYGGF
GYLIPQSVPL EENPEGALGV IFDSDREMSM RELFDFERTL VMDDAHATDV YNKSQKGLDA
TRAARAAADS TRGSKYTVML GGHLWDGYQY PDDFPSADEA VRMAEAVLRR HLRDTPRFGG
GGGAPMPTPI ATRTKLCREC IPQHYVGHAR RMAALDAELK AAFGGRLAVA GGSFTATGPG
VLPSVRSAYD VALRVAGRGY QMVLEDKSRR ETTMAHVGDT GLGRFADPAT DSVGMRAREL
LPLRFNNKHV YARGYFGRNV HGDEYVRYPV RQ
//