ID D4DAH9_TRIVH Unreviewed; 264 AA.
AC D4DAH9;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 22-FEB-2023, entry version 37.
DE SubName: Full=Pyroglutamyl peptidase type I, putative {ECO:0000313|EMBL:EFE41177.1};
GN ORFNames=TRV_04126 {ECO:0000313|EMBL:EFE41177.1};
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE41177.1, ECO:0000313|Proteomes:UP000008383};
RN [1] {ECO:0000313|Proteomes:UP000008383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
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 -!- SIMILARITY: Belongs to the peptidase C15 family.
CC {ECO:0000256|ARBA:ARBA00006641}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFE41177.1}.
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DR EMBL; ACYE01000208; EFE41177.1; -; Genomic_DNA.
DR RefSeq; XP_003021795.1; XM_003021749.1.
DR AlphaFoldDB; D4DAH9; -.
DR GeneID; 9578675; -.
DR KEGG; tve:TRV_04126; -.
DR HOGENOM; CLU_043960_0_0_1; -.
DR OrthoDB; 5490159at2759; -.
DR Proteomes; UP000008383; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0016920; F:pyroglutamyl-peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00501; Peptidase_C15; 1.
DR Gene3D; 3.40.630.20; Peptidase C15, pyroglutamyl peptidase I-like; 1.
DR InterPro; IPR000816; Peptidase_C15.
DR InterPro; IPR016125; Peptidase_C15-like.
DR InterPro; IPR036440; Peptidase_C15-like_sf.
DR PANTHER; PTHR23402; PROTEASE FAMILY C15 PYROGLUTAMYL-PEPTIDASE I-RELATED; 1.
DR PANTHER; PTHR23402:SF1; RE07960P; 1.
DR Pfam; PF01470; Peptidase_C15; 1.
DR SUPFAM; SSF53182; Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase); 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 264 AA; 29443 MW; F1AC9104930E3628 CRC64;
MGDFGATSSL DEPVSLPGQP LPPQDDDIHV LVTGFGPFKT HPLNPSWLIN SLLPQYATTS
KNRRVHIHAH PRPIRVAYAA VREEIPRIIE EFRVAHDGRP PHLVIHIGMA ATRQYYAVET
VAHREGYKHT DVDGQFGIPF DPSLPERLQP GVPTPADYAS TSESTDKVRV IPSPLDTGFL
QTWRKSLPAG RSIDVRLSHD AGHYLCEYIY YTSLSMAWEE NRPRAALFLH VPGWTDKASV
EMGVEVVVGL VRAMVESWIV ETDA
//
