Y6955_ARTOC
ID Y6955_ARTOC Reviewed; 388 AA.
AC C5FW52;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Probable aspartic-type endopeptidase MCYG_06955;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN ORFNames=MCYG_06955;
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 -!- FUNCTION: Probable aspartic-type endopeptidase which contributes to
CC virulence. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; DS995706; EEQ34136.1; -; Genomic_DNA.
DR RefSeq; XP_002844991.1; XM_002844945.1.
DR AlphaFoldDB; C5FW52; -.
DR SMR; C5FW52; -.
DR STRING; 63405.XP_002844991.1; -.
DR EnsemblFungi; EEQ34136; EEQ34136; MCYG_06955.
DR GeneID; 9228217; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_0_1_1; -.
DR OMA; HRIYHPE; -.
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; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; PTHR47966; 2.
DR Pfam; PF00026; Asp; 2.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Secreted; Signal; Virulence.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..388
FT /note="Probable aspartic-type endopeptidase MCYG_06955"
FT /id="PRO_0000406415"
FT DOMAIN 96..384
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 388 AA; 43509 MW; 4C6418412969D42D CRC64;
MMGPFFYFTA YVSLLFAFTQ ALPTINGATA GLFSIEQKQY RSNRVNWPPY ELWRTLRKHH
RPPPRGMTAV SRIKAYGEHT INGTVEVTPS EYDTEFVNEI TVGNDTLYVD IDTGSSDFWV
FSSQLPEQSQ RNHRIYHPEE TGTKLPKHTW ESKYGDGTGA AGNVFLDKVN LAGLKVSSQA
VEAATWVSYE FVDQQTTDGV MGFGFDNFNL TCLKHQAPGF YDFGFIDGTK HVGKPTYLPI
DSLRGWWETT FNGFSAGDID NSTYRFKAVI GINFELPDTG TTFMLLPKQI TEQYYSTVPA
SMYDRNNGGW AFPCNTTLPN FTIHINDHKA IVPGEHIRWA QLPGTNTCFG GLQPVNNPPA
ILGGTFLKSQ FVIFDYDGPK IGFAAQRN