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Database: UniProt
Entry: T1KAT6_TETUR
LinkDB: T1KAT6_TETUR
Original site: T1KAT6_TETUR 
ID   T1KAT6_TETUR            Unreviewed;       629 AA.
AC   T1KAT6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE            EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN   Name=107362675 {ECO:0000313|EnsemblMetazoa:tetur08g01700.1};
OS   Tetranychus urticae (Two-spotted spider mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC   Tetranychoidea; Tetranychidae; Tetranychus.
OX   NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur08g01700.1, ECO:0000313|Proteomes:UP000015104};
RN   [1] {ECO:0000313|Proteomes:UP000015104}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA   Rombauts S.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:tetur08g01700.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
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; CAEY01001943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015785269.1; XM_015929783.1.
DR   AlphaFoldDB; T1KAT6; -.
DR   EnsemblMetazoa; tetur08g01700.1; tetur08g01700.1; tetur08g01700.
DR   eggNOG; KOG1731; Eukaryota.
DR   HOGENOM; CLU_020182_0_0_1; -.
DR   OMA; SDMDMRM; -.
DR   OrthoDB; 20090at2759; -.
DR   Proteomes; UP000015104; 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   Gene3D; 1.20.120.310; ERV/ALR sulfhydryl oxidase domain; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 2.
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; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
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   SUPFAM; SSF69000; FAD-dependent thiol oxidase; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51324; ERV_ALR; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW   Transmembrane {ECO:0000256|RuleBase:RU371123};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU371123}.
FT   TRANSMEM        594..613
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU371123"
FT   DOMAIN          4..184
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          405..508
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000259|PROSITE:PS51324"
SQ   SEQUENCE   629 AA;  72885 MW;  A5F6314E66730B29 CRC64;
     MKPVFIHQLI CSFIITTLLT LINGIPILYN GNEPGLIILG SSNFSQIIFH QNNTFIVEFY
     NSWCGHCVRF APTWKAFAKD IRHWSSVVRV AAIDCAEDSN VKLCSDYNIN LFPSVRYFWH
     NYDFKINGQP LTTNIGNVES LRHDYLNWLH GSWSHGVPQN WPNLNYFDPG NPEELTNITK
     AALDRDILIL VEGEKSHLGR EVILDLSPFL DSVIVRRIKT GHSWLNQLNE SPLLLPVILK
     ISKDGKPVIF KRPDELGPDH RKVTVETIMS EYNLTYKEIE SSSSSSKAFQ ERLKNQLVAP
     KLKPTDNIHL SDLYLSIRET LYKQIPLHKS LDSHKLQILK SFISILDDYF PFDSDSPKIF
     ITSLSKWLST QVHGLEMDDF TSVLDKLNQH NPFPKPQNWI TCQGSEPGFR GYPCSLWLLF
     HTLTVNEYIK TNGEPNDHRV LYTMRDYITN FFSCAECAKH FREMSSNMES SLINPNGSIL
     WLWRAHNIVN RRLAKDLTED PVHPKTQYPP TSVCNTCWTS DGLRFNETQT FNFLLTRYQS
     DNLIGLKSHL KPSKSDFINS NPAFESYDHD FQHVGNLWTW PNVILNRMDI SLCLLLYVIT
     SCMLLTFCFI LSIRKRRRKE HKFRYPMAL
//
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