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Database: UniProt
Entry: A0A1V6TLT2_9EURO
LinkDB: A0A1V6TLT2_9EURO
Original site: A0A1V6TLT2_9EURO 
ID   A0A1V6TLT2_9EURO        Unreviewed;       444 AA.
AC   A0A1V6TLT2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   ORFNames=PENSTE_c005G07289 {ECO:0000313|EMBL:OQE26799.1};
OS   Penicillium steckii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE26799.1, ECO:0000313|Proteomes:UP000191285};
RN   [1] {ECO:0000313|Proteomes:UP000191285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 24891 {ECO:0000313|Proteomes:UP000191285};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:OQE26799.1}.
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DR   EMBL; MLKD01000005; OQE26799.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6TLT2; -.
DR   STRING; 303698.A0A1V6TLT2; -.
DR   OrthoDB; 1384212at2759; -.
DR   Proteomes; UP000191285; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147:SF26; ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1; 1.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361240};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191285};
KW   Signal {ECO:0000256|RuleBase:RU361240};
KW   Zinc {ECO:0000256|RuleBase:RU361240}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT   CHAIN           20..444
FT                   /note="Peptide hydrolase"
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT                   /id="PRO_5011830271"
FT   DOMAIN          214..412
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   444 AA;  49559 MW;  CDE960939690FDDA CRC64;
     MMQKSIIVCL IGAAHLATAL PDVQRVLAPI HPPSGAARQH GDHSIHESIL SAIESHTDPV
     TAFISLQDQD DRAETKAALA EPRLLRKLGS NKADWMTEGD KMRLRREGIR FMDITEHEDF
     YAQQVDTQVA AKPNLPDLIH ERLIRPLFSF VDTGRMSDVL QHMTGYYNRY FDDIHGELSA
     EWLHDHISQI ISNSPLHTHI SLEYFTHPFR QSSIIARFEP KIRNFSHPLT ILGAHQDSAN
     YLFPLLPAPG ADDDCSGTVS ILEAFRVLAE AGFVPKNGPV EFHWYAAEEG GLLGSQAIAR
     YKKEQGAHIG AMMEFDMTAF IAANATETIG FIATEADEVL TNWTVNLSRK YISIPTEIYE
     LSGGAGSDYM SYTQLNYPAS FASEGNPIAG GDFPGEYDPY VHGINDTMWV NDETGYFSLD
     HMARFSELAI AFAVEQAGWD NKWR
//
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