ID   S8BCP1_PENO1            Unreviewed;       537 AA.
AC   S8BCP1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Beta-lactamase-related domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PDE_07672 {ECO:0000313|EMBL:EPS32712.1};
OS   Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS32712.1, ECO:0000313|Proteomes:UP000019376};
RN   [1] {ECO:0000313|EMBL:EPS32712.1, ECO:0000313|Proteomes:UP000019376}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX   PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA   Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA   Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT   "Genomic and secretomic analyses reveal unique features of the
RT   lignocellulolytic enzyme system of Penicillium decumbens.";
RL   PLoS ONE 8:E55185-E55185(2013).
CC   -!- SIMILARITY: Belongs to the peptidase S12 family.
CC       {ECO:0000256|ARBA:ARBA00038215}.
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DR   EMBL; KB644414; EPS32712.1; -; Genomic_DNA.
DR   AlphaFoldDB; S8BCP1; -.
DR   MEROPS; S12.002; -.
DR   eggNOG; ENOG502QQBX; Eukaryota.
DR   HOGENOM; CLU_020027_0_4_1; -.
DR   OrthoDB; 1931461at2759; -.
DR   PhylomeDB; S8BCP1; -.
DR   Proteomes; UP000019376; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022438};
KW   Protease {ECO:0000256|ARBA:ARBA00022438};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019376}.
FT   DOMAIN          18..335
FT                   /note="Beta-lactamase-related"
FT                   /evidence="ECO:0000259|Pfam:PF00144"
FT   DOMAIN          351..533
FT                   /note="D-aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF07930"
SQ   SEQUENCE   537 AA;  58935 MW;  405DFB9CA991BB91 CRC64;
     MSGPTPAIQH AINAVPLRYR GPGGALAVVK DGQVIGKRVW GYADQSRRIP VDSSTRFPIC
     SITKQFVCGL LVDLQRHPTP AMAAKGDVQK QFADTLNEML PLAREGLTVQ NLCDMQSGIR
     DYWALTTLWG AKPDDEFLID RDCPPMLEKT KSFHFTPGTE YSYSNVNFYL LGRIIERVTG
     ESLGKLLEER ILKPAGMSTA FLCPNTAHHP PPCVGYEGNE DLGFSDAVNR MEWSGDAGLV
     ASLEDMIAYE KYLDQLYADP SSWYHKTAKL TTFSDGNTAR YHFGLGHVDV NGVESIGHGG
     ALRGYRLHRR HVPEQHLSVV VMFNHEADAA AAVDDILRTV LNRPTAESTP VEPAPAWYGA
     YLDEATQLAV TVAKSRRPGE VLITYGSHLE SAPLKMTDAT SGKSRSMTGS ISGDTLQIHR
     ISENRKLNAR RLVPLDSGLV DPKLAGAYYC DEIESTFYCT GEAGMFYGTF DGYLGNGIVT
     SMRYLGDDVW ALGCPRGLDA SAPGDWTMVF QRDESGTVSG FKIGCWLARG LDFVKLK
//