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Database: UniProt/TrEMBL
Entry: Q5EUC0_MAIZE
LinkDB: Q5EUC0_MAIZE
Original site: Q5EUC0_MAIZE 
ID   Q5EUC0_MAIZE            Unreviewed;       511 AA.
AC   Q5EUC0;
DT   15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2005, sequence version 1.
DT   26-NOV-2014, entry version 66.
DE   RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE            EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN   Name=TEL1 {ECO:0000313|EMBL:AAW66880.1};
GN   Synonyms=Zm.18471 {ECO:0000313|EnsemblPlants:GRMZM2G113216_P02};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae;
OC   PACMAD clade; Panicoideae; Andropogoneae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:AAW66880.1};
RN   [1] {ECO:0000313|EMBL:AAW66880.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15684019; DOI=10.1104/pp.104.056507;
RA   Houston N.L., Fan C., Xiang Q.Y., Schulze J.M., Jung R., Boston R.S.;
RT   "Phylogenetic analyses identify 10 classes of the protein disulfide
RT   isomerase family in plants, including single-domain protein disulfide
RT   isomerase-related proteins.";
RL   Plant Physiol. 137:762-778(2005).
RN   [2] {ECO:0000313|EMBL:ACN27863.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B73 {ECO:0000313|EMBL:ACN27863.1};
RX   PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA   Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA   Angelova A., Collura K., Wissotski M., Ashley E., Morrow D.,
RA   Fernandes J., Walbot V., Yu Y.;
RT   "Sequencing, mapping, and analysis of 27,455 maize full-length
RT   cDNAs.";
RL   PLoS Genet. 5:E1000740-E1000740(2009).
RN   [3] {ECO:0000313|EnsemblPlants:GRMZM2G113216_P02, ECO:0000313|Proteomes:UP000007305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:GRMZM2G113216_P02,
RC   ECO:0000313|Proteomes:UP000007305};
RX   PubMed=19965430; DOI=10.1126/science.1178534;
RA   Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA   Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA   Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA   Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K.,
RA   Abbott R.M., Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M.,
RA   Gillam B., Chen W., Yan L., Higginbotham J., Cardenas M.,
RA   Waligorski J., Applebaum E., Phelps L., Falcone J., Kanchi K.,
RA   Thane T., Scimone A., Thane N., Henke J., Wang T., Ruppert J.,
RA   Shah N., Rotter K., Hodges J., Ingenthron E., Cordes M., Kohlberg S.,
RA   Sgro J., Delgado B., Mead K., Chinwalla A., Leonard S., Crouse K.,
RA   Collura K., Kudrna D., Currie J., He R., Angelova A., Rajasekar S.,
RA   Mueller T., Lomeli R., Scara G., Ko A., Delaney K., Wissotski M.,
RA   Lopez G., Campos D., Braidotti M., Ashley E., Golser W., Kim H.,
RA   Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A., Fan C.,
RA   Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA   Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA   Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA   Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA   Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA   Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y.,
RA   Jeddeloh J.A., Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z.,
RA   Nagel D.H., McCann M.C., SanMiguel P., Myers A.M., Nettleton D.,
RA   Nguyen J., Penning B.W., Ponnala L., Schneider K.L., Schwartz D.C.,
RA   Sharma A., Soderlund C., Springer N.M., Sun Q., Wang H., Waterman M.,
RA   Westerman R., Wolfgruber T.K., Yang L., Yu Y., Zhang L., Zhou S.,
RA   Zhu Q., Bennetzen J.L., Dawe R.K., Jiang J., Jiang N., Presting G.G.,
RA   Wessler S.R., Aluru S., Martienssen R.A., Clifton S.W., McCombie W.R.,
RA   Wing R.A., Wilson R.K.;
RT   "The B73 maize genome: complexity, diversity, and dynamics.";
RL   Science 326:1112-1115(2009).
RN   [4] {ECO:0000313|EnsemblPlants:GRMZM2G113216_P02}
RP   IDENTIFICATION.
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:GRMZM2G113216_P02};
RG   EnsemblPlants;
RL   Submitted (OCT-2014) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY: 2 R'C(R)SH + O(2) = R'C(R)S-S(R)CR' +
CC       H(2)O(2). {ECO:0000256|RuleBase:RU371123}.
CC   -!- COFACTOR:
CC       Note=FAD. {ECO:0000256|RuleBase:RU371123};
CC   -!- SIMILARITY: Contains 1 ERV/ALR sulfhydryl oxidase domain.
CC       {ECO:0000256|RuleBase:RU371123}.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
CC       {ECO:0000256|RuleBase:RU004207}.
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DR   EMBL; CM000782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY739305; AAW66880.1; -; mRNA.
DR   EMBL; BT063166; ACN27863.1; -; mRNA.
DR   RefSeq; NP_001105769.1; NM_001112299.1.
DR   UniGene; Zm.18471; -.
DR   EnsemblPlants; GRMZM2G113216_T02; GRMZM2G113216_P02; GRMZM2G113216.
DR   GeneID; 606424; -.
DR   KEGG; zma:606424; -.
DR   HOGENOM; HOG000029909; -.
DR   GO; GO:0016972; F:thiol oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 1.20.120.310; -; 1.
DR   Gene3D; 3.40.30.10; -; 1.
DR   InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF04777; Evr1_Alr; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF69000; SSF69000; 1.
DR   PROSITE; PS51324; ERV_ALR; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007305};
KW   FAD {ECO:0000256|RuleBase:RU371123};
KW   Flavoprotein {ECO:0000256|RuleBase:RU371123};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU371123};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007305}.
SQ   SEQUENCE   511 AA;  57059 MW;  96E16E6FE2B8E074 CRC64;
     MAASTAAARR LLLALAVLAA CLGSAPHGAV ALRSLGVGGA KAADGDAAVD LDASNFTAFL
     QTSPESFAVV EFFAHWCPAC RNYKPHYERV AKLFNGPDAA HPGTVVMARV DCASKVNVDL
     CNKFSVDHYP YLVWGPPTKF NLAQWKPKQE NSELELIDDG RTADRLLKWI NKKMGSSFNL
     DDKKYENESM HPKNTSDPEQ IVRAIYDVEE ATSHALQIIL EHKMIKPDTR DSLISFLQIL
     VAHHPSKRCR RGSAELLIDF DDHWHTNLSL SLEDSTTLLK GAGEKVCGNG VPRGYWIFCR
     GSKKETRGFS CGLWVLLHSL TVRIGDGESQ TTFTSICDFI HNFFICEECR THFYEMCSSV
     SVPFKSARDL ALWLWTAHNK VNERLMKEEK ELDNADPSFP KIIWPPKQLC PLCYRSSSRT
     ADGAMQVEWN EDEVFNFLVN YYGKMLVSSY RETSMQSFQV ASISDDSSAS SAATVPIGAA
     LGIALASCTF GALACFWRTQ QKNRKQRKNW N
//
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