ID A0A0A2KR89_PENEN Unreviewed; 540 AA.
AC A0A0A2KR89;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Peptidase S12, Pab87-related, C-terminal {ECO:0000313|EMBL:KGO51548.1};
GN ORFNames=PEX2_007530 {ECO:0000313|EMBL:KGO51548.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO51548.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO51548.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO51548.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO51548.1}.
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DR EMBL; JQFZ01000284; KGO51548.1; -; Genomic_DNA.
DR RefSeq; XP_016594475.1; XM_016738030.1.
DR AlphaFoldDB; A0A0A2KR89; -.
DR STRING; 27334.A0A0A2KR89; -.
DR GeneID; 27673449; -.
DR HOGENOM; CLU_020027_14_1_1; -.
DR OrthoDB; 1699300at2759; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR Gene3D; 2.40.128.600; -; 1.
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; IPR021860; Peptidase_S12_Pab87-rel_C.
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; PF11954; DUF3471; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT DOMAIN 10..345
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
FT DOMAIN 433..534
FT /note="Peptidase S12 Pab87-related C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11954"
FT REGION 360..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 60051 MW; 2AC714724878B496 CRC64;
MDLFHSAGFA SDVTELMKQQ HVPGLAIAII HNDQIVSAGY GHASLDPEIP CTADTLFDIA
SSAKSITAAA VGLLVDDNDM FPDIQYDAVM STLLPEDFVM SGEGYTEGVT VEDILSHRSG
MPSHNDSYMS VRAAKPDNAR SITRNLRNLP IAAPIRSRYI YCNMMYTVAT HLVEVKSGQD
FGTFLEERFF KPLDMASTTL QPSSARSKGF ESRMATGYTW KRADSTYRGL ENPDCPEGQG
AGSIISSVND FIKFVKAFIN REDPINKNVY EGLTRLRTFV NPNPGRRKRY TSPIAYAAGL
DIYFYKGHMV VGHNGVFSGF GSRFFFLPDF SFGAVIMGNS DGANGVATTL VQKLIDNLHG
VTDERPHDSK SKATRPVEIR GPKPQAEAKD ANPMSQNQEK KEKKKHEKKA QAKKSQDIQK
GQVNEQRPKG NNTPQPPTMP LSAYAGNYWN PGYHNLLVQI GDDALFIDAT DRSMGFTLKF
EHVSDDRKFD AHLTDWLDGS DDIVKAEFVI KDAQVTRLGL QLEEMLKEMI WFERKDEVIS
//
