ID A0A179GG87_PURLI Unreviewed; 383 AA.
AC A0A179GG87;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=VFPBJ_08830 {ECO:0000313|EMBL:OAQ76470.1}, VFPFJ_10041
GN {ECO:0000313|EMBL:OAQ78009.1};
OS Purpureocillium lilacinum (Paecilomyces lilacinus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Purpureocillium.
OX NCBI_TaxID=33203 {ECO:0000313|EMBL:OAQ76470.1, ECO:0000313|Proteomes:UP000078240};
RN [1] {ECO:0000313|EMBL:OAQ76470.1, ECO:0000313|Proteomes:UP000078240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLBJ-1 {ECO:0000313|EMBL:OAQ76470.1}, and PLFJ-1
RC {ECO:0000313|EMBL:OAQ78009.1};
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 (JAN-2016) 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:OAQ76470.1}.
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DR EMBL; LSBH01000007; OAQ76470.1; -; Genomic_DNA.
DR EMBL; LSBI01000011; OAQ78009.1; -; Genomic_DNA.
DR RefSeq; XP_018174140.1; XM_018327109.1.
DR AlphaFoldDB; A0A179GG87; -.
DR STRING; 33203.A0A179GG87; -.
DR GeneID; 28892158; -.
DR KEGG; plj:VFPFJ_10041; -.
DR OMA; GIQDDHI; -.
DR OrthoDB; 3091175at2759; -.
DR Proteomes; UP000078240; Unassembled WGS sequence.
DR Proteomes; UP000078340; 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:SF2; PEPTIDE HYDROLASE; 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:UP000078340};
KW Signal {ECO:0000256|RuleBase:RU361240};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT CHAIN 25..383
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5010394691"
FT DOMAIN 122..349
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 359..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 383 AA; 42693 MW; 0AF1ADD38C6CBC3E CRC64;
MPSRSSAIVL LVTALLAFVW PACALTTLDD DDLRQIPSPG DDFDIHNGKL LAPILIPRVP
GTEGSEKTQR HFADFFKSNL PEWQLLWQNS TSRTPVTGDR DVPFANLIFR RDPPGAPTGE
VSRLTLVAHF DSKYEPTGFI GATDSAAPCA MLMHVARSIE SALKAKWSEE GEHDGLDVAH
GVQIVLLDGE EAFLHWTDDD SLYGARSLAA EWESHFHPSM STYRTPLDSI SLFVLLDLLG
SAGPKIPSYF LTTHWAYKNM ATIEKRMRDL GLLETKPTHA FLPEAEKHSG EFSAWMSISD
DHVPFMHRGV DILHVIPSPF PEVWHKMEDD GEHLDLPTTR DWAKIVTAFT AEWMDLKGHM
PKQSSTKQKR SVTTAATSSK TEL
//
