Y5382_TRIVH
ID Y5382_TRIVH Reviewed; 401 AA.
AC D4DE18;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Probable aspartic-type endopeptidase TRV_05382;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN ORFNames=TRV_05382;
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517;
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).
CC -!- FUNCTION: Probable aspartic-type endopeptidase which contributes to
CC virulence. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; ACYE01000282; EFE39910.1; -; Genomic_DNA.
DR RefSeq; XP_003020528.1; XM_003020482.1.
DR AlphaFoldDB; D4DE18; -.
DR SMR; D4DE18; -.
DR EnsemblFungi; EFE39910; EFE39910; TRV_05382.
DR GeneID; 9584268; -.
DR KEGG; tve:TRV_05382; -.
DR HOGENOM; CLU_013253_0_0_1; -.
DR Proteomes; UP000008383; 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; Secreted; Signal;
KW Virulence.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..401
FT /note="Probable aspartic-type endopeptidase TRV_05382"
FT /id="PRO_0000406416"
FT DOMAIN 94..398
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 401 AA; 44939 MW; E72365EC4680FF09 CRC64;
MWHSPFFTAF TLFLGFFTLT LALPTNSLAT TGRFTVEQRL IKTFESNWPP KELWRGLRKH
HRPLPPAVSR IATHRGPSAN GTVKVTPDEY NTEFVNEITI GNNTLFVDID TGSSDFWVFS
SQLPERSQLN HRIYHPEKTG TKLSKQIWEI GYGDGTGAAG NVFLDKASLA GLEVPSQAVQ
AATWVSYQFA DQTVTDGVIG FGFDHFNGVT PKKQKTWFGN IMERLEKPIF TACLKHKAPG
FYDFGFIDRT KHIGNPSYLP VDNSRGWWET TFNGFSTGRN DNSTYRFRAV VDTGTTFSLL
PREITEQYYS LITGSTFDRE NGGWTFPCNT TLPEFAIHIN DYKAIVPGEH INWAQIPGTN
TCFGGIQSVD RSPAVLGGSF LKSQFVIFDH DGPKMGFAAQ R
