ID   Y7979_ARTOC             Reviewed;         430 AA.
AC   C5FZ57;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Putative aspergillopepsin A-like aspartic endopeptidase MCYG_07979;
DE            EC=3.4.23.-;
DE   Flags: Precursor;
GN   ORFNames=MCYG_07979;
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS995708; EEQ35160.1; -; Genomic_DNA.
DR   RefSeq; XP_002842896.1; XM_002842850.1.
DR   AlphaFoldDB; C5FZ57; -.
DR   SMR; C5FZ57; -.
DR   STRING; 63405.XP_002842896.1; -.
DR   MEROPS; A01.079; -.
DR   EnsemblFungi; EEQ35160; EEQ35160; MCYG_07979.
DR   GeneID; 9227569; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_0_0_1; -.
DR   OMA; GGFIFPC; -.
DR   OrthoDB; 753343at2759; -.
DR   Proteomes; UP000002035; 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   CDD; cd06097; Aspergillopepsin_like; 1.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; PTHR47966; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Secreted; Signal; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..87
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000390770"
FT   CHAIN           88..430
FT                   /note="Putative aspergillopepsin A-like aspartic
FT                   endopeptidase MCYG_07979"
FT                   /id="PRO_0000390771"
FT   DOMAIN          109..427
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   REGION          59..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        314
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        306
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        352
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   430 AA;  46508 MW;  A0269BD128230680 CRC64;
     MHLSSLLVAV LLPLALSKPT PRKKPGSFTV HLARRSEAEY ARDGPTDLQR AYAKYGIPST
     QGMDGYRPEP ISRFQGNSKI AGGAPGAKDD GKDEKGEVEN NPTSHDIQFL SPVTIGGQPF
     IMNFDTGSSD TWVMNTDMDD EEAKKDHHLY DPRKSKTYSK LDGLTFSIKY GDKSHASGPV
     ITDVMDIGGA TVRKQAIGLP TKVAASLAND KSSDGLVGLA MNKLNTVRPD KQKTFFENLA
     EDLDEPVFTA QLRKGKMGSY EFGAIDKTKY AGDLVNVPVN NKNGFWEISS ALYSVGQLDK
     IQKVENGTGT AILDTGTTLL ILDEEVVKAY YAQVKGARYD ASRYAGWVYP CNASMPSLFL
     AVGHDHMAII PSSLLTFQNY GPGPDGTDVC YGGLQSNNAG GIQILGDVFF KALFVVFDYR
     GPSVSLAPHA