WSCD2_ARTBC
ID WSCD2_ARTBC Reviewed; 720 AA.
AC D4AUF4;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=WSC domain-containing protein ARB_07870 {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=ARB_07870;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21247460,
CC ECO:0000269|PubMed:21919205}.
CC -!- SIMILARITY: Belongs to the WSCD family. {ECO:0000305}.
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DR EMBL; ABSU01000011; EFE33119.1; -; Genomic_DNA.
DR RefSeq; XP_003013759.1; XM_003013713.1.
DR AlphaFoldDB; D4AUF4; -.
DR STRING; 663331.D4AUF4; -.
DR EnsemblFungi; EFE33119; EFE33119; ARB_07870.
DR GeneID; 9526949; -.
DR KEGG; abe:ARB_07870; -.
DR eggNOG; KOG4157; Eukaryota.
DR HOGENOM; CLU_004824_1_0_1; -.
DR OMA; RVGFHDM; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR002889; WSC_carb-bd.
DR Pfam; PF00141; peroxidase; 1.
DR Pfam; PF01822; WSC; 2.
DR PRINTS; PR00458; PEROXIDASE.
DR SMART; SM00321; WSC; 2.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
DR PROSITE; PS51212; WSC; 2.
PE 1: Evidence at protein level;
KW Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..720
FT /note="WSC domain-containing protein ARB_07870"
FT /id="PRO_5003053665"
FT DOMAIN 524..615
FT /note="WSC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00558"
FT DOMAIN 627..718
FT /note="WSC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00558"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 663
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 701
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 720 AA; 76986 MW; 7091FF4D460E4875 CRC64;
MLINLSAVWA AFALSGVLAP PTWPASIDEL EDLMFLNTGY HARGFSAGVT PCSFSQQGPS
RVASAEWVRT AFHDMATGNS FTGVGGLDAS IVFELGGKGG ENIGAGFNTT LETYTPFFST
RSSMADLIAL GVYTAVRSCG GPVVQVRTGR IDATARGPIG VPQPENSQGT FINQFTRMGF
NVSDMIAVTA CGHTMGGVHA SNFPQIVVPG SAPNDFQLFD STVSFDEKVA VDFVGGVAGN
PLTSTTAKRS QRDADMKVFT ADRNVTIKAL ADQVTFRSTC ARVLQKMIEV VPSGVNLTAP
IAPYEVKPGR LQLSLASNGS TIAFTGEIRV RTTSRPVTSI SKVELVYKDR TGGSSCGSCI
ITTEYKGTAE GFDDSFAFYG FEARFPVETA ISKFNVRVVL NTGETVVYNN NDEEDDNRLI
ISQKVRKNAN TGSVKLSVTT KTPRSCCVTP ALTTQSVPMS PQTTVGPYTL YAGNLTLAAA
YRSNAKFDVS LTSGGAVISD SFKNTADLSS TCAPFGSNDP TMPDYTFDGC YTDTPESRAL
TSAAFVKENM TIAACSSLCK GYQFFGLEYG TECYCGDTRS NSSMQAPKSE CNQPCGGDSS
ETCGAGYRIA IYKDDKWVPI TSPQIPGYNY TGCYSDSPSN RTLSGSFTYN EKMTVELCAS
FCNGTKYFGV EYFSECYCGA NMFPGSTIQP ESDCGFFFSA NKTQHCGGSN RINIYTKLDM