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Database: UniProt
Entry: A0A329SYZ2_9STRA
LinkDB: A0A329SYZ2_9STRA
Original site: A0A329SYZ2_9STRA 
ID   A0A329SYZ2_9STRA        Unreviewed;       490 AA.
AC   A0A329SYZ2;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE            EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN   ORFNames=PC110_g1464 {ECO:0000313|EMBL:RAW42353.1}, PC113_g4466
GN   {ECO:0000313|EMBL:KAG2864567.1}, PC115_g4122
GN   {ECO:0000313|EMBL:KAG2937603.1}, PC117_g4511
GN   {ECO:0000313|EMBL:KAG2950341.1}, PC118_g3886
GN   {ECO:0000313|EMBL:KAG2993670.1}, PC129_g3002
GN   {ECO:0000313|EMBL:KAG3226423.1};
OS   Phytophthora cactorum.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=29920 {ECO:0000313|EMBL:RAW42353.1, ECO:0000313|Proteomes:UP000251314};
RN   [1] {ECO:0000313|EMBL:RAW42353.1, ECO:0000313|Proteomes:UP000251314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10300 {ECO:0000313|EMBL:RAW42353.1,
RC   ECO:0000313|Proteomes:UP000251314};
RA   Armitage A.D., Lysoe E., Nellist C.F., Harrison R.J., Brurberg M.B.;
RT   "Draft genome of the strawberry crown rot pathogen Phytophthora cactorum.";
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAG2864567.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=15-7 {ECO:0000313|EMBL:KAG2864567.1}, 4032
RC   {ECO:0000313|EMBL:KAG2937603.1}, 4040 {ECO:0000313|EMBL:KAG2950341.1},
RC   P415 {ECO:0000313|EMBL:KAG2993670.1}, and P421
RC   {ECO:0000313|EMBL:KAG3226423.1};
RA   Armitage A.D., Nellist C.F., Bates H., Vickerstaff R.J., Harrison R.J.;
RT   "Effector identification in a new, highly contiguous assembly of the
RT   strawberry crown rot pathogen Phytophthora cactorum.";
RL   Submitted (OCT-2018) 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   -!- 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:RAW42353.1}.
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DR   EMBL; RCMG01000077; KAG2864567.1; -; Genomic_DNA.
DR   EMBL; RCMI01000075; KAG2937603.1; -; Genomic_DNA.
DR   EMBL; RCMK01000072; KAG2950341.1; -; Genomic_DNA.
DR   EMBL; RCML01000069; KAG2993670.1; -; Genomic_DNA.
DR   EMBL; RCMV01000058; KAG3226423.1; -; Genomic_DNA.
DR   EMBL; MJFZ01000017; RAW42353.1; -; Genomic_DNA.
DR   Proteomes; UP000251314; Unassembled WGS sequence.
DR   Proteomes; UP000697107; Unassembled WGS sequence.
DR   Proteomes; UP000735874; Unassembled WGS sequence.
DR   Proteomes; UP000736787; Unassembled WGS sequence.
DR   Proteomes; UP000760860; Unassembled WGS sequence.
DR   Proteomes; UP000774804; 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   CDD; cd02961; PDI_a_family; 1.
DR   Gene3D; 1.20.120.310; ERV/ALR sulfhydryl oxidase domain; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR   InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
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; 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   4: Predicted;
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:UP000251314};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|RuleBase:RU371123};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU371123}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..490
FT                   /note="Sulfhydryl oxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039986060"
FT   TRANSMEM        447..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU371123"
FT   DOMAIN          27..153
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          294..407
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000259|PROSITE:PS51324"
SQ   SEQUENCE   490 AA;  55188 MW;  B807D2B541246A0F CRC64;
     MPPALRLFGM AALVVSGWLP PISAIGPVRR DRGPLFTTSK AVRTLDIGSF DAMLNDTQTV
     WLVDFYSPWC PHCRQFGPQW EEVANVYADV DSIQFGAVDC TRQNEICDRE DVHSYPAVKM
     YHVPPEINEA IEMPHAGNVY ARHVAKWIEE TLKENGMGPL IDVDKVYPKN TLRNDLKKKE
     FKFGDPVEPL HDDRSAEIQL KRLRDAGTTA LFTLDDGFFM GTTVLAGERY DAAVTWVQTL
     AGAFPMKENR AAFALLVGMI RQQNRWKQAD WNTMLDKWKV TANAMSYPTN LFASKDDLIL
     CTTFTCGLWT LFHSLTVNGV GQLMPSEIMI AIRLVVKHFF GCEECKHHFL KANPESVIKK
     LALRDEDGPH AVTFWIWTMH NTVNKVLGKA RWPTNLSCPN CYFANDQPQS LDPAQLSEED
     IVAYIRGVYK IEGTLKLGQH ATTTTTWLTL GGFTSMAAVA LLIAIFATTF QQHKHRLIGV
     KALKTRDHIA
//
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