ID   CARP1_ARTBC             Reviewed;         417 AA.
AC   D4ATH2;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Probable secreted aspartic protease ARB_07536 {ECO:0000305};
DE            EC=3.4.23.- {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_07536;
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].
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   -!- FUNCTION: Probable secreted aspartic protease that supplies the fungus
CC       with nutrient amino acids (By similarity). May be able to degrade the
CC       selected host's proteins involved in the immune defense (By
CC       similarity). {ECO:0000250|UniProtKB:P0CY27}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; ABSU01000009; EFE33591.1; -; Genomic_DNA.
DR   RefSeq; XP_003014231.1; XM_003014185.1.
DR   AlphaFoldDB; D4ATH2; -.
DR   SMR; D4ATH2; -.
DR   EnsemblFungi; EFE33591; EFE33591; ARB_07536.
DR   GeneID; 9521649; -.
DR   KEGG; abe:ARB_07536; -.
DR   eggNOG; ENOG502SMFH; Eukaryota.
DR   HOGENOM; CLU_039077_0_0_1; -.
DR   OMA; FVDWTWI; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; PTHR47966; 1.
DR   Pfam; PF00026; Asp; 1.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   1: Evidence at protein level;
KW   Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..417
FT                   /note="Probable secreted aspartic protease ARB_07536"
FT                   /id="PRO_5003053641"
FT   DOMAIN          42..413
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        276
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        314
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        333..373
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ   SEQUENCE   417 AA;  47034 MW;  74672B015119BACF CRC64;
     MRGILILVAL GAATIPQASA APNDRQQSMI DLPLKLYQNG FNTDLVTIGT PAQATRLFVD
     WTWIGAYTVS TKCNHTNNAY GCLAPGQKLF NETQSTSLVN QTNLYPTRTW NPNHFFMDKD
     LTAVFASDIY RVGDRESRLT LQLSQLNWKA SFPYPFSGIF GMSPVFKSDN MSIQAPFHQM
     VQQKKFHSGL TSFIYCYSDE PGYKSPSKER CNGNDGIQTL GGYHHRDIGW RGIEWINTIV
     FPIVNDIDFI YNPAFYNYWS IPVTKHFIGN EEQALNTTTG SAVVFDHASY GRGAAMSVAS
     YRRLVSITNA QPVNLTMATL PNNGKQKFYS VDCDRVDSFP AVKYQFGKWR RVWSIEARHY
     ISKAKTMDGK DVCVLNVRVI GQGENFVIGN LGENFAKDKV ILFDFEKNRV GLADFRD