ID A0A179GZD5_PURLI Unreviewed; 374 AA.
AC A0A179GZD5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=VFPFJ_08423 {ECO:0000313|EMBL:OAQ82620.1};
OS Purpureocillium lilacinum (Paecilomyces lilacinus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Purpureocillium.
OX NCBI_TaxID=33203 {ECO:0000313|EMBL:OAQ82620.1, ECO:0000313|Proteomes:UP000078340};
RN [1] {ECO:0000313|EMBL:OAQ82620.1, ECO:0000313|Proteomes:UP000078340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLFJ-1 {ECO:0000313|EMBL:OAQ82620.1};
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yin W., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins and their inhibition on
RT Phytophthora in bio-control Purpureocillium lilacinum.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Extracellular aminopeptidase that allows assimilation of
CC proteinaceous substrates. {ECO:0000256|ARBA:ARBA00043843}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28E subfamily.
CC {ECO:0000256|ARBA:ARBA00043962}.
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:OAQ82620.1}.
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DR EMBL; LSBI01000008; OAQ82620.1; -; Genomic_DNA.
DR RefSeq; XP_018175248.1; XM_018325496.1.
DR AlphaFoldDB; A0A179GZD5; -.
DR STRING; 33203.A0A179GZD5; -.
DR GeneID; 28890545; -.
DR KEGG; plj:VFPFJ_08423; -.
DR OMA; FTHSWNQ; -.
DR OrthoDB; 1384212at2759; -.
DR Proteomes; UP000078340; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
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 Aminopeptidase {ECO:0000313|EMBL:OAQ82620.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {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:UP000078340};
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..374
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5007950242"
FT DOMAIN 171..364
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 374 AA; 40327 MW; 46FAFF9F0642F527 CRC64;
MHVNAALAIL AASCPLALAA PAESVPAGRT SLRLVKTSEK DPGQWVDEKD FWNKFISKNI
NFVDITDIED KEVLAILSGQ TASTSVANIA ATYPDGPQHV DEANKLISQS NTNGPQSWLK
ILTEFHTRHY QSQTGLQASN WLFEQVKKTA AANSAITVKQ FKHTRFNQPS VIAQLPGESS
NLVIVGAHMD STGGSSSARS PGADDNGSGS VTVLEALRVV ASSGLKPKNT LEFHWYAGEE
GGLLGSKEVY ANYKQTGKKV TAFLNQDMTG YSPNKKPAVF TDNVDASLTA YVRKIVKQYT
GVEPSTSQCG YGCSDHASGR SNGFPSAFVG EDTFDAMNPN IHSSRDSLEK IDWSAVHRHV
KLTIGFLVEA SYVQ
//
