ID A0A1V6TL39_9EURO Unreviewed; 360 AA.
AC A0A1V6TL39;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Peptidase M12B domain-containing protein {ECO:0000259|PROSITE:PS50215};
GN ORFNames=PENFLA_c006G02487 {ECO:0000313|EMBL:OQE27105.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE27105.1, 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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:OQE27105.1}.
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DR EMBL; MLQL01000006; OQE27105.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6TL39; -.
DR STRING; 254877.A0A1V6TL39; -.
DR OrthoDB; 2961161at2759; -.
DR Proteomes; UP000191342; Unassembled WGS sequence.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF222; ADAM FAMILY OF METALLOPROTEASE ADM-A (AFU_ORTHOLOGUE AFUA_6G14420); 1.
DR Pfam; PF13688; Reprolysin_5; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000191342};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..360
FT /note="Peptidase M12B domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012799752"
FT DOMAIN 217..360
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
SQ SEQUENCE 360 AA; 39135 MW; D7E13E7CFB939E48 CRC64;
MKKSTLFTIF TVLIIPLIPA LAIPFEASIF RLVNSSIPPR LDGGLRPSTF DITTDIDKSE
LALRFVLETN DDLISEHAYI HNLDVNGQSA GEGAISSGLY LTKGSVWIQE APGRQWENVG
WARLAVTQEK EALSLDGTFT VLSSQYGIRQ EPQENGPAEI IARKRESDFP TGNWMASNST
CATAPEDVLN KRQLEWNAWG DNLADNIGIT YGCPQTRRIA YIGIATDCTY TASFNSSDSA
QRYILNMVNT ASVVFENSFN ISLSIQNLTM SNAECPTSVS ASTDWNTPCS VGDLNTRLET
FSSWRSSIGD NNAYWTLLTG CSVGAGQVGV SWIGALCNSG SSYSASSANV VARTQSEWQS
//
