ID A0A0V0ZN27_9BILA Unreviewed; 1025 AA.
AC A0A0V0ZN27;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN Name=QSOX1 {ECO:0000313|EMBL:KRY13887.1};
GN ORFNames=T12_9811 {ECO:0000313|EMBL:KRY13887.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY13887.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY13887.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY13887.1};
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU371123}.
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:KRY13887.1}.
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DR EMBL; JYDQ01000129; KRY13887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0ZN27; -.
DR Proteomes; UP000054783; 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:SF8; 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:UP000054783};
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 63..83
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU371123"
FT TRANSMEM 710..736
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU371123"
FT DOMAIN 73..210
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 457..556
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000259|PROSITE:PS51324"
FT DOMAIN 848..979
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1000..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1025 AA; 116574 MW; 1B6429CA7E5DF481 CRC64;
MTYIANLCGH CTLFAGSNNI STIGFDDLVF NQSISSPSST QKCCILFYMW DKATMTKFGG
GHLTMLFSML SLLLLLIPAA TFAEVGVESL FSATDQVHSL DKNSFDQFVY NQDYATVVDF
YSSWCGACIN FAPTYSEMAI SVKGWHRYVK VAAVNCASMV NRELCTANSV YFYPSLKYHS
KAASDGVPMT AGALHTADSI VLSLAKSVAG DWNEQKPVNW PNFAFIPPTQ TVPEYHSPWA
KYIAVVVQSR EDSMAAAITL DLTSQYLVEC RPVEPSHPMA SSRGVRHTPG LMIFARGNDG
PLFISTGSMS RAEILSTISR VTGIKNPAPA DPNYISPPAS PNTDVVVYRI ADQNLDNFFV
HINDLKSGIS YMILHEIPLR PVIEGEPLNA LQKFFALLAK YMPFEWRLKS LLSELSAYAN
SQKSITSQQW SHHFNALQWK YDRALPTEPI WVACNGSSPQ YRGYPCSLTF MNCMDLYILV
PDFNPIEVPS AIYGYIKHFF GCRFCAENFG RSAVKMSQQI HNEQDEILWL WASHNRANYH
LKGDKTEDPR FPKNPFPYPK LCPECRKMDG SFDEDKVLEF LIRFYTDIKS YDVATPAPLI
SHTTSPLTAG ENVACMCSRP TFLTFILTIL LTWDCEDGFS SKHTHTTSPH KSFIISDFPF
NFIIISYHYH YHYYYAWLVK IINRSSAFSL QYCYVLGGYV HEFQCIYLQY ALQMLVCLMY
HILCNLFCIL IFSMLFSQLF NVAQMPASNT KVSQKRKKLY HMYEEADHER QVKEIMKRFV
KTTNGQPRKA AIRATMFRKC TANFNQTSYL KMEIVLPQNY VSMQNRMRQK KLKKILLPIP
YTTSLVGPPI CALCQKVEQN ITLYGPYHVC INEASFWPPF LSKPTNNRTI TQRYSTALFF
HEICFFYSPG LFIRGHLMSC EPEILIKYWK QKCALCNVEG ASISCAHTNC NATVHPMCAK
KCGWILDLVA SVVRCRIHGS SEQLIFQEHY FRQIDLLSST SSEDSDTDTD GPDQIKWLSD
DSDEE
//
