ID A0A094CN29_9PEZI Unreviewed; 514 AA.
AC A0A094CN29;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=V497_06866 {ECO:0000313|EMBL:KFY55586.1};
OS Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY55586.1, ECO:0000313|Proteomes:UP000029268};
RN [1] {ECO:0000313|EMBL:KFY55586.1, ECO:0000313|Proteomes:UP000029268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
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:KFY55586.1}.
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DR EMBL; JPJZ01001146; KFY55586.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094CN29; -.
DR STRING; 1420910.A0A094CN29; -.
DR HOGENOM; CLU_024336_0_0_1; -.
DR OrthoDB; 51543at2759; -.
DR Proteomes; UP000029268; 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; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR PANTHER; PTHR12147:SF55; PEPTIDE HYDROLASE; 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.
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:UP000029268};
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..514
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5005107419"
FT DOMAIN 149..230
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 256..470
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 21..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 514 AA; 53299 MW; DE771FF336750B41 CRC64;
MKVSLSLIAL FTALNTVSAA PPNSGGGGGG GHGNGNGHGN GNDHGHGRGP MVNSKALRGL
IKEKALMDKA QKLQDFAALS GTPITRVIGS PGHNATVNWY YDTIKKLDDY YSVYIQSFPV
VTADGNLTVN NALIESATMS FTGAGHPIAE LVPVANVACE AADFPTEVSG KIALLSRGTC
TFGAKAILAK AAGAIGVVVY NNEDGVVQGT LGEEGDYPPT IGISKAQGEA FLAAIAAGTV
QTADLFIEQK TVTTYNVIAE TLDGDHDNVI HLGGHSDSVA AGPGINDNGS GGIGILEVAL
HLTKFKINNA VRFSWWAAEE EGLLGALAYV KAQPQSELEK IRLYLNFDMI ASPNYVYAIY
DGDGSTFNVT GPAGSAQAEH LFIDYFRDIE KVDSVPSDFD GRSDYGPFLD AGIACGGLFT
GAEGLKTAEE AVMFGGEAAV AYDINYHAAG DTVANCNGTA FLVNTRAIAH SVAVLAKSTA
LLEEPLVRRG GYRDFTRAAG VGKKVAGGCG TKAL
//