ID A0A2V1E8T0_9PLEO Unreviewed; 495 AA.
AC A0A2V1E8T0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=DM02DRAFT_609754 {ECO:0000313|EMBL:PVI06572.1};
OS Periconia macrospinosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Periconiaceae; Periconia.
OX NCBI_TaxID=97972 {ECO:0000313|EMBL:PVI06572.1, ECO:0000313|Proteomes:UP000244855};
RN [1] {ECO:0000313|EMBL:PVI06572.1, ECO:0000313|Proteomes:UP000244855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE2036 {ECO:0000313|EMBL:PVI06572.1,
RC ECO:0000313|Proteomes:UP000244855};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
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}.
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DR EMBL; KZ805308; PVI06572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1E8T0; -.
DR STRING; 97972.A0A2V1E8T0; -.
DR Proteomes; UP000244855; 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; 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:UP000244855};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT DOMAIN 130..224
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 251..447
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 495 AA; 51967 MW; FECDE7759785BE66 CRC64;
MRLQDTLFLV GAAKAVASSL PRPSYEPYKP LVNSKGLQDG ITTENLMGNL QQLDTIAKAN
GGNRAFGWPG YAASVDYILS RTQNSSNFVT WVQDFPTLYQ YVESISFQAG NQTIRAIGLT
YSPSTSAEGV TAPLVLGPSG DAGCTNEAYA DLDVEGKIVL AERGLCPDGT TFAGRMKPAA
AAGAAAVVIY NNVATPATGG TLSNPNPEEY VSSGLINQAE GQALVARLTA GETISAHFQQ
TQIIETRITQ NVFTETVGGD PNNVIMLGAH LDSVVAGAGI NDDGSGTSLI LEVKTALEKF
NVKNKVRFAW WGAEENGLKG SLYYVANLNT TALDNILVYL NFDMVSKGYF GVFDGDGSTH
GLAGPPGSDV VEKLFVDDHV SKGVNVTAAV FTGGSDYRSF MDAGKPVGGL HTGTGVAQDP
CYHQSCDTIE NPEPATLTVN AKAAAHVLSV LATTGHELIP KSPQNATLSA RGLMGRDIEY
TLVEGERHVG CGTEA
//
