ID A0A0A2KQ17_PENEN Unreviewed; 401 AA.
AC A0A0A2KQ17;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Peptidase M4, C-terminal {ECO:0000313|EMBL:KGO56940.1};
GN ORFNames=PEX2_002940 {ECO:0000313|EMBL:KGO56940.1};
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:KGO56940.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO56940.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO56940.1,
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 M4 family.
CC {ECO:0000256|ARBA:ARBA00009388}.
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:KGO56940.1}.
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DR EMBL; JQFZ01000155; KGO56940.1; -; Genomic_DNA.
DR RefSeq; XP_016598628.1; XM_016737572.1.
DR AlphaFoldDB; A0A0A2KQ17; -.
DR STRING; 27334.A0A0A2KQ17; -.
DR MEROPS; M04.025; -.
DR GeneID; 27672991; -.
DR HOGENOM; CLU_008590_0_1_1; -.
DR OrthoDB; 2679274at2759; -.
DR PhylomeDB; A0A0A2KQ17; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09597; M4_TLP; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR InterPro; IPR032475; Protealysin_N_PP.
DR PANTHER; PTHR43579; -; 1.
DR PANTHER; PTHR43579:SF1; NEUTRAL METALLOPROTEINASE; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR Pfam; PF16485; PLN_propep; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 61..89
FT /note="Protealysin N-terminal propeptide"
FT /evidence="ECO:0000259|Pfam:PF16485"
FT DOMAIN 108..223
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 228..391
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
SQ SEQUENCE 401 AA; 44504 MW; 85DD94F1E8C2E415 CRC64;
MAPLCGIIPE YVLEGIIEKG LAPQDTIRRC QSTLEKTKQL QDVRERHRQS IAAAQPQQTS
QGIIPPYILE TLARNAATEQ QREAARHTLA YSAKHRTVAG RVRQLNRTVY DAQNSRDDHP
PRDKILIPEG GELLSQETDP TNNANECYVG LGKTYDFYFN FFGRNSFDNN GIKLDGFVHA
GDLYNAFFNG EELVFGDGDG VLFDGFTDEL DVIGHEFSHG VVEFTSLLPY WYQSGALNES
IADAFGIMVK QWGEGNPQTV DHANWLIGEG IWAAGVNGRA LRDMANPGTA FDDDRVGKDP
QPAHWRDFKK LSNDNGGVHI NSGIPNRAFF LAATKIGGYA WEGAGPIWYR ALSSGKLPTD
GEATFKEFAD LTIESAGEHV DKVREAWTAV GYPFPEKRHE L
//
