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Database: UniProt
Entry: A0A0V1P6A6_9BILA
LinkDB: A0A0V1P6A6_9BILA
Original site: A0A0V1P6A6_9BILA 
ID   A0A0V1P6A6_9BILA        Unreviewed;       921 AA.
AC   A0A0V1P6A6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE            EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
DE   Flags: Fragment;
GN   Name=QSOX1 {ECO:0000313|EMBL:KRZ91636.1};
GN   ORFNames=T08_15220 {ECO:0000313|EMBL:KRZ91636.1};
OS   Trichinella sp. T8.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ91636.1, ECO:0000313|Proteomes:UP000054924};
RN   [1] {ECO:0000313|EMBL:KRZ91636.1, ECO:0000313|Proteomes:UP000054924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS272 {ECO:0000313|EMBL:KRZ91636.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU371123};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU371123};
CC   -!- SIMILARITY: Belongs to the quiescin-sulfhydryl oxidase (QSOX) family.
CC       {ECO:0000256|ARBA:ARBA00006041}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRZ91636.1}.
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DR   EMBL; JYDM01000042; KRZ91636.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1P6A6; -.
DR   STRING; 92180.A0A0V1P6A6; -.
DR   Proteomes; UP000054924; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016971; F:flavin-dependent sulfhydryl oxidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.310; ERV/ALR sulfhydryl oxidase domain; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 1.20.120.1960; QSOX sulfhydryl oxidase domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR   InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR   InterPro; IPR040986; QSOX_FAD-bd_dom.
DR   InterPro; IPR042568; QSOX_FAD-bd_sf.
DR   InterPro; IPR039798; Sulfhydryl_oxidase.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR22897; QUIESCIN Q6-RELATED SULFHYDRYL OXIDASE; 1.
DR   PANTHER; PTHR22897:SF26; SULFHYDRYL OXIDASE; 1.
DR   Pfam; PF04777; Evr1_Alr; 1.
DR   Pfam; PF18371; FAD_SOX; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   Pfam; PF13771; zf-HC5HC2H; 1.
DR   SUPFAM; SSF69000; FAD-dependent thiol oxidase; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS51324; ERV_ALR; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU371123};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW   Transmembrane {ECO:0000256|RuleBase:RU371123};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU371123};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU371123"
FT   DOMAIN          69..209
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          453..558
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000259|PROSITE:PS51324"
FT   DOMAIN          744..875
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   REGION          895..921
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRZ91636.1"
SQ   SEQUENCE   921 AA;  103977 MW;  FAB2D02E46056AF1 CRC64;
     LPISAVIVLF AGSNNISTIG FDDLVFNQSI SSPSSTQKCC ILFLMWDKAT MTKFGGGHLT
     MLFSMLSLLL LLIPAATFAE VGVESLFSAT DQVHSLDKNS FDQFVYNQDY ATVVDFYSSW
     CGACINFAPT YSEMAISVKG WHRFVKVAAV NCASMVNREL CTANSVYFYP SLKYFKYHSK
     AASDGVPMTA GALHTADSIV LSLAKSVAGD WNEQKPVNWP NFAFIPPTQT VPEYHSPWAK
     YIAVVVQSRE DSMAAAITLD LTSQYLVECR PVEPSHPMAS SRGVRHTPGL MIFARGNDAP
     LFISTGSMSR AEILSTISRV TGIKNPAPAD PNYISPPASP NTDVVVADQN LDNFFVHIND
     LKSGISYMIL HEIPLRPVIE GEALNALQKF FALLAKYMPF EWKLKSLLSE LSAYANSQKS
     ITSQQWSHHF NALQWKYDRA LPTEPIWVAC NGSSPQYRGY PCSVWLIFHT LTVHAYMIDN
     NLPDFNPIEV PSAIYGYIKH FFGCRFCAEN FGRSAVKMSQ QIHNERDEIL WLWASHNRAN
     YHLKGDKTED PRFPKNPFPY PKLCPECRKM DGSFDEDKVL EFLIRFYTDI KSYDVATPAP
     LISHTTSPLT AGENVAFVIL DSKANRSSLT VTFEQTKQEK MPASNTKVSQ KRKKLYHMYE
     EADHERQVKE IMERFVKTTN GQPRKAAIRT TMFRKCTANF NQTSYLKMEI VLPQNYVSMQ
     NRMRQKKLKK ILLPIPYTTS LVGPPICALC QKVEKNTTLY GPYHVCINEA SFWPPFLSKP
     TNNRTITQRY STALFFHEIC FFYSPGLFIR GHLMSCEPET LIKYWKQKCA VCNVEGASIS
     CAHTNCNVTV HPMCAKKCGW ILDLVASVVR CRIHGSSEQL IFQEHYFRQI DLLSSTSSED
     SDSDTDGPDQ IKWLSDDSDE E
//
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