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
//