ID   A0A3M2TDX8_9EURO        Unreviewed;       387 AA.
AC   A0A3M2TDX8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   ORFNames=PHISP_01550 {ECO:0000313|EMBL:RMJ27562.1};
OS   Aspergillus sp. HF37.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1960876 {ECO:0000313|EMBL:RMJ27562.1, ECO:0000313|Proteomes:UP000272442};
RN   [1] {ECO:0000313|EMBL:RMJ27562.1, ECO:0000313|Proteomes:UP000272442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HF37 {ECO:0000313|EMBL:RMJ27562.1,
RC   ECO:0000313|Proteomes:UP000272442};
RA   Tafer H., Lopandic K.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family.
CC       {ECO:0000256|RuleBase:RU361240}.
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:RMJ27562.1}.
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; RAQS01000040; RMJ27562.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M2TDX8; -.
DR   STRING; 1960876.A0A3M2TDX8; -.
DR   Proteomes; UP000272442; Unassembled WGS sequence.
DR   GO; GO:0016603; F:glutaminyl-peptide cyclotransferase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd03880; M28_QC_like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR037457; M28_QC.
DR   InterPro; IPR007484; Peptidase_M28.
DR   InterPro; IPR040234; QC/QCL.
DR   PANTHER; PTHR12283; GLUTAMINYL-PEPTIDE CYCLOTRANSFERASE; 1.
DR   PANTHER; PTHR12283:SF6; GLUTAMINYL-PEPTIDE CYCLOTRANSFERASE; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Hydrolase {ECO:0000256|RuleBase:RU361240};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361240}; Protease {ECO:0000256|RuleBase:RU361240};
KW   Reference proteome {ECO:0000313|Proteomes:UP000272442};
KW   Signal {ECO:0000256|RuleBase:RU361240};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|RuleBase:RU361240}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT   CHAIN           27..387
FT                   /note="Peptide hydrolase"
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT                   /id="PRO_5017855551"
FT   DOMAIN          125..360
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   387 AA;  43193 MW;  8140043947970441 CRC64;
     MSSAYTILRT LLSICLGLLL LPFASAYENV SDETLKALPR PKNDFDIHDG ALLSPILRTR
     VPGTPGSTAV LNHFADFFRT TLPDWNVQFQ NSTSKTPVSG NKEVPFVNFI ASRDPPWAPA
     GDVGRLTLVA HYDSKYEPEG FIGAIDSAAP CAIIMHAMRS IDAALTKKWD DMRKKGRRYE
     SLEGQKGIQV IFLDGEEAFK EWTEEDSLYG ARSLAEQWDD EVHPAMSVYK TPLTSISLFA
     LLDLLGAKNP TVQSYFETTH WAYQKLAALE GRLRQLNMFK SGDSNGKWFV DGSRDEHGLS
     GFGGVQDDHL PFLDRGVEIL HVIDAAPLKG FPSVWHTMDD NGENLDINTI EDWSLLITAF
     AAEWMGLEGY MLPSASQNEK RWDKTEL
//