ID   A0A177CPF0_9PLEO        Unreviewed;       493 AA.
AC   A0A177CPF0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   ORFNames=CC84DRAFT_1137037 {ECO:0000313|EMBL:OAG09403.1};
OS   Paraphaeosphaeria sporulosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC   Paraphaeosphaeria.
OX   NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG09403.1, ECO:0000313|Proteomes:UP000077069};
RN   [1] {ECO:0000313|EMBL:OAG09403.1, ECO:0000313|Proteomes:UP000077069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG09403.1,
RC   ECO:0000313|Proteomes:UP000077069};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) 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}.
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DR   EMBL; KV441549; OAG09403.1; -; Genomic_DNA.
DR   RefSeq; XP_018039768.1; XM_018176125.1.
DR   AlphaFoldDB; A0A177CPF0; -.
DR   STRING; 1460663.A0A177CPF0; -.
DR   GeneID; 28759611; -.
DR   InParanoid; A0A177CPF0; -.
DR   OrthoDB; 51543at2759; -.
DR   Proteomes; UP000077069; 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:UP000077069};
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..493
FT                   /note="Peptide hydrolase"
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT                   /id="PRO_5007948970"
FT   DOMAIN          125..211
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          238..452
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   493 AA;  52396 MW;  8841BC23412B7C8F CRC64;
     MKVAVATLAA VGATVVNCAA IEPRGNKLVT SEGLRKLIKL KALQEKAHLF ERFAYDSPDK
     NRVIGSEGHQ ATIDYITKTI KKYSKYYDVY QQPMPLSIGL SANLTVNEKE VTVDAVGLAP
     GGSASGPVVA IPNLGCEEAD FPADLSGSIA LISRGTCVSG EKVAFAASKG AIGVLIYNNV
     DGNLAGYSLQ RFPESDGEYV PTGGITQAAG EGFVSLLASG GSVTAELTTS SKDVITYNII
     AQTKGGDQDN VIHVSGHSDS VAQGPGINDN GSGSISILET AIQLTQFSVK NAVRFSWWTA
     EEAGLLGAEF YVKSLNQTEK DKIRLLLDFD MMASPNYAYQ IYDGDGSAFN LTGPAGSAEA
     EAEFAYYFDK IAKVNHTEIE FDGRSDYGPF LDAGIAAGGI ACGAEGIKTQ EEFEMFGGAA
     GVPYDVNYHE DGDTYNNLNF DAFIVMAKAI AHSTATYARS FDSLPPKNTT AIKARSDANQ
     FKYKKSARYL SMI
//