ID A0A061D4R7_BABBI Unreviewed; 383 AA.
AC A0A061D4R7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 08-NOV-2023, entry version 34.
DE RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN ORFNames=BBBOND_0102710 {ECO:0000313|EMBL:CDR93944.1};
OS Babesia bigemina.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=5866 {ECO:0000313|EMBL:CDR93944.1, ECO:0000313|Proteomes:UP000033188};
RN [1] {ECO:0000313|Proteomes:UP000033188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bond {ECO:0000313|Proteomes:UP000033188};
RX PubMed=24799432; DOI=10.1093/nar/gku322;
RA Jackson A.P., Otto T.D., Darby A., Ramaprasad A., Xia D., Echaide I.E.,
RA Farber M., Gahlot S., Gamble J., Gupta D., Gupta Y., Jackson L.,
RA Malandrin L., Malas T.B., Moussa E., Nair M., Reid AJ., Sanders M.,
RA Sharma J., Tracey A., Quail M.A., Weir W., Wastling J.M., Hall N.,
RA Willadsen P., Lingelbach K., Shiels B., Tait A., Berriman M., Allred D.R.,
RA Pain A.;
RT "The evolutionary dynamics of variant antigen genes in Babesia reveal a
RT history of genomic innovation underlying host-parasite interaction.";
RL Nucleic Acids Res. 42:7113-7131(2014).
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};
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DR EMBL; LK391707; CDR93944.1; -; Genomic_DNA.
DR RefSeq; XP_012766130.1; XM_012910676.1.
DR AlphaFoldDB; A0A061D4R7; -.
DR STRING; 5866.A0A061D4R7; -.
DR EnsemblProtists; CDR93944; CDR93944; BBBOND_0102710.
DR GeneID; 24562485; -.
DR KEGG; bbig:BBBOND_0102710; -.
DR VEuPathDB; PiroplasmaDB:BBBOND_0102710; -.
DR OrthoDB; 1265at2759; -.
DR Proteomes; UP000033188; Chromosome 1.
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 InterPro; IPR039799; ALR/ERV.
DR InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR PANTHER; PTHR12645; ALR/ERV; 1.
DR PANTHER; PTHR12645:SF0; FAD-LINKED SULFHYDRYL OXIDASE ALR; 1.
DR Pfam; PF04777; Evr1_Alr; 1.
DR SUPFAM; SSF69000; FAD-dependent thiol oxidase; 1.
DR PROSITE; PS51324; ERV_ALR; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
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};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU371123};
KW Reference proteome {ECO:0000313|Proteomes:UP000033188};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..383
FT /note="Sulfhydryl oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001600605"
FT DOMAIN 275..382
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000259|PROSITE:PS51324"
FT REGION 90..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 38..72
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 258..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 383 AA; 43749 MW; 3C275A5B77692923 CRC64;
MYLRLCLAFV FVLIAPPSFC RHASTDFSLS EQERESLLTR LSELVSQSTQ ALESLKEAAK
RSREEIDKYK YLIPNSKDSK PVEGVHLGEL KQGKTGGHPS HRGFTQVKSS EPASPEFIRN
ALYATQPVSG TPQATVSVDA LENPNDVVKN ATEVATFSDD GSRDFFEEEL YRMKREIHSV
NRLHSLKNNA NVLSTEIRRL MTYKPDSSTQ AHSKEAQRYE ICVNIQSCTE LLNTVNLWIF
LMAKTVEDAY KRCEDAACRD GSEGDSRNDR SNVKMPPNRK ELGRAGWMYL HSMAADFPDE
PSSLESLRVK AWCYSFAELY PCHICKEGLV EIYRRLPPVT DSRRDLLLWT HNLHNQVNAD
LSYPHYNGTY EELLQLDRHE KYS
//
