UniProt: A0A095C2P2

Database: UniProt
Entry: A0A095C2P2_SCHHA

LinkDB:  A0A095C2P2_SCHHA 
Original site:  A0A095C2P2_SCHHA

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (11)   
   InterPro (7)   
   Pfam (2)   
   PROSITE (2)   
Literature (1)   
   PubMed (1)   
All databases (19)   

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ID   A0A095C2P2_SCHHA        Unreviewed;       594 AA.
AC   A0A095C2P2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE            EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN   ORFNames=MS3_04220 {ECO:0000313|EMBL:KGB35943.1};
OS   Schistosoma haematobium (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6185 {ECO:0000313|EMBL:KGB35943.1};
RN   [1] {ECO:0000313|EMBL:KGB35943.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22246508; DOI=10.1038/ng.1065;
RA   Young N.D., Jex A.R., Li B., Liu S., Yang L., Xiong Z., Li Y.,
RA   Cantacessi C., Hall R.S., Xu X., Chen F., Wu X., Zerlotini A., Oliveira G.,
RA   Hofmann A., Zhang G., Fang X., Kang Y., Campbell B.E., Loukas A.,
RA   Ranganathan S., Rollinson D., Rinaldi G., Brindley P.J., Yang H., Wang J.,
RA   Wang J., Gasser R.B.;
RT   "Whole-genome sequence of Schistosoma haematobium.";
RL   Nat. Genet. 44:221-225(2012).
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}.
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DR   EMBL; KL250730; KGB35943.1; -; Genomic_DNA.
DR   RefSeq; XP_012795708.1; XM_012940254.1.
DR   AlphaFoldDB; A0A095C2P2; -.
DR   STRING; 6185.A0A095C2P2; -.
DR   EnsemblMetazoa; XM_012940254.2; XP_012795708.2; MS3_0014082.
DR   GeneID; 24591773; -.
DR   KEGG; shx:MS3_00001410; -.
DR   CTD; 24591773; -.
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   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 1.20.120.1960; QSOX sulfhydryl oxidase domain; 1.
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   PANTHER; PTHR22897; QUIESCIN Q6-RELATED SULFHYDRYL OXIDASE; 1.
DR   PANTHER; PTHR22897:SF8; SULFHYDRYL OXIDASE; 1.
DR   Pfam; PF18371; FAD_SOX; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF69000; FAD-dependent thiol oxidase; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU371123}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|RuleBase:RU371123};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU371123}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..594
FT                   /note="Sulfhydryl oxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001907126"
FT   TRANSMEM        549..575
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU371123"
FT   DOMAIN          9..146
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          346..480
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000259|PROSITE:PS51324"
SQ   SEQUENCE   594 AA;  67102 MW;  9847F8ABDDD8C09A CRC64;
     MLVTVFVLNI LLRTVHSFAY SQIEGVTVLH PEDFDNKTSE GIWLVIFYRK TCGHCISYSK
     PFSQFCRSVK NWNWALHLGS VDCEDETNMD LCYRFKVQGV PTLRVKYCFI IISQFLSTKN
     SKQTSEEIPA EWNMTLLRKS IASKLVNVSA LQLPRDLAVN DPIIVTGSDI EVNALLLLDY
     SLLLKREIQS VVKPGLKEID VTNRLSGEVI VKGPEEQVRM VLERIAGSEP RLEENSQPEI
     DVKTTPIQVK YPPVYAVDIY RSLSMLLQSD VGARDKIEGP ALEALKEFLD MLYEILPASQ
     EYKAHLSEIS VWLNSKTSIT GQEWIAYLEG IQFPTYKGPF IACNGSKPHF RGYPCGLWTL
     FHALTVEQYL LSSSGPDHQV DSVAHALNRF VPQFFSCSYC AFHFALNTAN VVRPGESVLP
     ENRVTPNPHE LVLNESVIPT LPKAPETPRD TVLWLNILHN RVNKHLAGQP SEDPSAPKIQ
     FPPSYLCPAC WSQSSTGELE LGKTPETEES LFQFLVERYR ASSWKYVDLP TVFITNAVEL
     KTEQPVPDLL IISIISVVLT ILAAVILLAG LRFLCRRRRL FRRRRGQYTG GQSV
//

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