ID A0A094HRU8_9PEZI Unreviewed; 516 AA.
AC A0A094HRU8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=V501_04959 {ECO:0000313|EMBL:KFZ10976.1};
OS Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ10976.1, ECO:0000313|Proteomes:UP000029315};
RN [1] {ECO:0000313|EMBL:KFZ10976.1, ECO:0000313|Proteomes:UP000029315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC {ECO:0000256|ARBA:ARBA00005957}.
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:KFZ10976.1}.
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DR EMBL; JPKD01001591; KFZ10976.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094HRU8; -.
DR STRING; 1420914.A0A094HRU8; -.
DR HOGENOM; CLU_024336_0_1_1; -.
DR Proteomes; UP000029315; 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 CDD; cd03876; M28_SGAP_like; 1.
DR CDD; cd02130; PA_ScAPY_like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR041756; M28_SGAP-like.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147:SF17; AMINOPEPTIDASE Y; 1.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
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:UP000029315};
KW Signal {ECO:0000256|RuleBase:RU361240};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT CHAIN 21..516
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5005107551"
FT DOMAIN 160..239
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 268..477
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 516 AA; 55763 MW; 854FFC89E4CBA588 CRC64;
MRSLSLPLPV ALSLLGSACA FQIPFLSTPD NHPGKDNTIF STPTPATPVT SDELEQLINP
DNLFRRAEQL FEIAKLSIEE YGHPTRVIGS KGHLGTVDYI YSTIADLGDY YDLSNQTFAA
VTGNVFESRL VLGHEVPKSA APMGLTPPTK NRGPVYGQLR LVSHYGCDEH DFESDGKGPW
IALVSRGICP FGTKSANAGK AGAIAVIIYN NEKGGVSGTL GQPSKHHVAT FGISDTDAAP
YIEKLKGGHP VDSIAFIDAI VDTIRTTNII AQTRGGDPDN CVMLGGHSDS VAEGPGINDD
GSGSISLLEV ATQLTRFSVT NCVRFAWWAG EEEGLLGSDY YVAQLSAAEN QRIRLFMDYD
MMASPNFAFQ IYNATDAVNP AGSQQLRELY TDYYEAQSLN HTLIPFDGRS DYDAFLRSGV
PSGGIATGAE GIKTAAEAEM FGGSAGEWFD PCYHQLCDNL SNLDMVAWEV NTKLIAHSVA
TYARTLEDFP KREDNLAAKS MTAPRNEVYH GHKLIM
//