ID A0A1V6SKF7_9EURO Unreviewed; 405 AA.
AC A0A1V6SKF7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Peptidase M4 C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENFLA_c040G02283 {ECO:0000313|EMBL:OQE14174.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE14174.1, ECO:0000313|Proteomes:UP000191342};
RN [1] {ECO:0000313|Proteomes:UP000191342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE14174.1}.
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DR EMBL; MLQL01000040; OQE14174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6SKF7; -.
DR STRING; 254877.A0A1V6SKF7; -.
DR OrthoDB; 2679274at2759; -.
DR Proteomes; UP000191342; 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:UP000191342};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 61..91
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 226..395
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
SQ SEQUENCE 405 AA; 45307 MW; 75B4A09CEE4534EC CRC64;
MAPLCAILPQ YVLEGIIEKG VAPQDIINRC QSTIEKTKHL RDVREHHGQT IVAPPQQQTF
QGIIPPYILE SIARNAGTEQ QREAARHTLE HRTKYRIAVG RVRQLHRTVY DAYHQGQHPF
RRDKVLIREG GDLLSQNADL TQNANECYVG LGKAYDFYFN FFQRNSINDA GFNLDGFVHA
GDLYNAYWDG EELVFGDGDD IVFHGFTDEL DVIGHEFSHG VVEYTSSLPY HDQSGALNES
LADAFGVMIK QWGEGSPQTV DQANWLIGEG IWGPSVKGRA LRDMANPGTA YDDDQVGEDR
QPAHWKDFKK LPDTPSGDWG GVHINSGIPN RAFFLAATKI GGYAWEGAGP IWYRALSSGK
LPTNGKATFK EFADLTIESA GEYVDKVREA WTAVGYPFPE KRHEL
//
