ID A0A151GPB3_9HYPO Unreviewed; 463 AA.
AC A0A151GPB3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=DCS_05860 {ECO:0000313|EMBL:KYK58842.1};
OS Drechmeria coniospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Drechmeria.
OX NCBI_TaxID=98403 {ECO:0000313|EMBL:KYK58842.1, ECO:0000313|Proteomes:UP000076580};
RN [1] {ECO:0000313|EMBL:KYK58842.1, ECO:0000313|Proteomes:UP000076580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 6962 {ECO:0000313|EMBL:KYK58842.1,
RC ECO:0000313|Proteomes:UP000076580};
RX PubMed=26975455; DOI=10.1038/srep23122;
RA Zhang L., Zhou Z., Guo Q., Fokkens L., Miskei M., Pocsi I., Zhang W.,
RA Chen M., Wang L., Sun Y., Donzelli B.G., Gibson D.M., Nelson D.R.,
RA Luo J.G., Rep M., Liu H., Yang S., Wang J., Krasnoff S.B., Xu Y.,
RA Molnar I., Lin M.;
RT "Insights into Adaptations to a Near-Obligate Nematode Endoparasitic
RT Lifestyle from the Finished Genome of Drechmeria coniospora.";
RL Sci. Rep. 6:23122-23122(2016).
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:KYK58842.1}.
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DR EMBL; LAYC01000002; KYK58842.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151GPB3; -.
DR STRING; 98403.A0A151GPB3; -.
DR InParanoid; A0A151GPB3; -.
DR OrthoDB; 51543at2759; -.
DR Proteomes; UP000076580; Chromosome 02.
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; cd04816; PA_SaNapH_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; 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:UP000076580};
KW Signal {ECO:0000256|RuleBase:RU361240};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT CHAIN 19..463
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5007358738"
FT DOMAIN 139..217
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 246..441
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 463 AA; 49794 MW; 20D34D07D49B6909 CRC64;
MNLLLVVLYA SRLLVAAAAE APPALTPEAI EADIEWTGLI NVLENLSTIA NDHGGNRAFG
TSGYLASFNY VLQRVQDGIS KYFDTTVQEF THTYYQLKNI SLTGPTGDNT PVISPTHNMA
TPPEGLTALL MNIPVDDERG SGCFGDQWNG TDASGKFVLI KHGKCYIDEK VQLAKNNGAL
GVIVYSDKAG QMVGDYLDRD TVVKPLPVGV VGLDTGLRWS QQVTDGQQLN VSLFVDTLYE
PRKSWNIISE TKSGDSNNVV FLGAHLDSVP AGPGINDNGS GVAALLEMAK HFCKYTGFKN
KVRFAWWGAE EPAIVGSRHY ASKLNETEAD QIRLYINLDM IGSPRPNYTV EANNDADMAG
AAPLVEHLLK NGFPAKIVKY DANSSDYSGF VKLGIPAAGI YTGGLLPVDN PPDACYHKAC
DNITNVNQEA ILANTKAAAY VTAKFALSLD GVPARNKTNS TSP
//
