ID   A0A135LBB3_PENPA        Unreviewed;       540 AA.
AC   A0A135LBB3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Peptidase S12, aminopeptidase DmpB, domain C {ECO:0000313|EMBL:KXG46268.1};
GN   ORFNames=PGRI_051240 {ECO:0000313|EMBL:KXG46268.1};
OS   Penicillium patulum (Penicillium griseofulvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG46268.1, ECO:0000313|Proteomes:UP000070168};
RN   [1] {ECO:0000313|EMBL:KXG46268.1, ECO:0000313|Proteomes:UP000070168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG3 {ECO:0000313|EMBL:KXG46268.1,
RC   ECO:0000313|Proteomes:UP000070168};
RX   PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA   Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA   Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT   "Genome sequencing and secondary metabolism of the postharvest pathogen
RT   Penicillium griseofulvum.";
RL   BMC Genomics 17:19-19(2016).
CC   -!- SIMILARITY: Belongs to the peptidase S12 family.
CC       {ECO:0000256|ARBA:ARBA00038215}.
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:KXG46268.1}.
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DR   EMBL; LHQR01000069; KXG46268.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135LBB3; -.
DR   OMA; QFVCALL; -.
DR   OrthoDB; 1931461at2759; -.
DR   Proteomes; UP000070168; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.128.50; -; 2.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR027279; D_amino_pept/lipop_sf.
DR   InterPro; IPR012856; DAP_B_dom.
DR   PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR   PANTHER; PTHR46825:SF9; PROTEIN FLP; 1.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   Pfam; PF07930; DAP_B; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF50886; D-aminopeptidase, middle and C-terminal domains; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:KXG46268.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022438, ECO:0000313|EMBL:KXG46268.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022438, ECO:0000313|EMBL:KXG46268.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070168}.
FT   DOMAIN          19..331
FT                   /note="Beta-lactamase-related"
FT                   /evidence="ECO:0000259|Pfam:PF00144"
FT   DOMAIN          358..536
FT                   /note="D-aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF07930"
SQ   SEQUENCE   540 AA;  59936 MW;  1A9F1BFC05BEBDC3 CRC64;
     MAITKETVQD VLIERALRCR GPGGAIAVVK DGELIGQHVW GLADLENRIP MTVETQMPIC
     SITKQFVCAL LLDLERNPTP ALAAKGSVRE QLTAHLTEIL SPELTRDGEL TIERLCDMQS
     GLRDYWAMTT LWGSKPDDEF LIARDSAPML AQTKSFQFQP GTEYSYCNVN FHILARVIER
     ATGESLDKLL EERILRPAGM STAFLCPNTA QHPPPCVGYE GDEEHGFTPA VNRMEWSGDA
     GLVASLTDMI AYEKYIDRCY ADPESWYNTA IADPKFSDGT TARYRYGLSH ADINEVHTIG
     HGGALRGYRL HRRHSPKDRL SVVVMLNSDA DAYGPTIKIF RDLLELPIRG LIPREVDMYW
     NGVYLDPDTQ LSIAVVPTNG AIDGELDIKY DGSATRFKLD EATWGKSDSM SGSIDTNTLT
     INRLADNRTL NARRILPKDS ALKDPSFLGV YQGVEIESTF HCIGGDGMLY GAFDGYLGKG
     NTTPMKHLGE DVWVLTCPRG LDAPAPGDWT MVFSRDENDQ IKGFTIGCWL ARKIEFVKKA
//