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Database: UniProt
Entry: A0A2U7U8N8_9VIRU
LinkDB: A0A2U7U8N8_9VIRU
Original site: A0A2U7U8N8_9VIRU 
ID   A0A2U7U8N8_9VIRU        Unreviewed;       206 AA.
AC   A0A2U7U8N8;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE            EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN   ORFNames=pqer_cds_375 {ECO:0000313|EMBL:AVK74797.1};
OS   Pandoravirus quercus.
OC   Viruses; Pandoravirus.
OX   NCBI_TaxID=2107709 {ECO:0000313|EMBL:AVK74797.1};
RN   [1] {ECO:0000313|EMBL:AVK74797.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Quercus {ECO:0000313|EMBL:AVK74797.1};
RX   PubMed=29891839; DOI=10.1038/s41467-018-04698-4;
RA   Legendre M., Fabre E., Poirot O., Jeudy S., Lartigue A., Alempic J.M.,
RA   Beucher L., Philippe N., Bertaux L., Christo-Foroux E., Labadie K.,
RA   Coute Y., Abergel C., Claverie J.M.;
RT   "Diversity and evolution of the emerging Pandoraviridae family.";
RL   Nat. Commun. 9:2285-2285(2018).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR';
CC         Xref=Rhea:RHEA:17357, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:16520, ChEBI:CHEBI:17412; EC=1.8.3.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000999,
CC         ECO:0000256|RuleBase:RU371123};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU371123};
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DR   EMBL; MG011689; AVK74797.1; -; Genomic_DNA.
DR   Proteomes; UP000248852; Genome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016971; F:flavin-dependent sulfhydryl oxidase activity; IEA:InterPro.
DR   Gene3D; 1.20.120.310; ERV/ALR sulfhydryl oxidase domain; 1.
DR   InterPro; IPR039799; ALR/ERV.
DR   InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR   InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR   PANTHER; PTHR12645; ALR/ERV; 1.
DR   PANTHER; PTHR12645:SF0; FAD-LINKED SULFHYDRYL OXIDASE ALR; 1.
DR   Pfam; PF04777; Evr1_Alr; 1.
DR   SUPFAM; SSF69000; FAD-dependent thiol oxidase; 1.
DR   PROSITE; PS51324; ERV_ALR; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU371123};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU371123}; Membrane {ECO:0000256|RuleBase:RU371123};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU371123};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248852};
KW   Transmembrane {ECO:0000256|RuleBase:RU371123};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU371123}.
FT   TRANSMEM        141..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU371123"
FT   DOMAIN          13..117
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000259|PROSITE:PS51324"
SQ   SEQUENCE   206 AA;  21893 MW;  9955271914CA3244 CRC64;
     MTPTLQPTTP SDGGSDVMHL VGPPMWETLH YAAFQCPEPF DERVSSALIG LVRGYVVLLP
     CAECRGHFAA LLDAHPPEVA ARSGRQAFAR WTVDAHNAVN ARLGKPLFTY DQATRRYARG
     NLHCRDPGGG PRAARRSSSP AVAFAVVLAA VALAAAVLAG VWFYLSARDG AGRLSPDPAV
     APAPSDTCAP APCMPKWPRW GPTDAR
//
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