ID A0A1Q5SY60_9EURO Unreviewed; 371 AA.
AC A0A1Q5SY60;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Zinc metalloproteinase nas-5 {ECO:0000313|EMBL:OKO92961.1};
GN ORFNames=PENSUB_12556 {ECO:0000313|EMBL:OKO92961.1};
OS Penicillium subrubescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKO92961.1, ECO:0000313|Proteomes:UP000186955};
RN [1] {ECO:0000313|EMBL:OKO92961.1, ECO:0000313|Proteomes:UP000186955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 132785 {ECO:0000313|EMBL:OKO92961.1,
RC ECO:0000313|Proteomes:UP000186955};
RA De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA Grigoriev I., Riley R., Granchi Z.;
RT "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OKO92961.1}.
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DR EMBL; MNBE01000735; OKO92961.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5SY60; -.
DR STRING; 1316194.A0A1Q5SY60; -.
DR OrthoDB; 2876847at2759; -.
DR Proteomes; UP000186955; Unassembled WGS sequence.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; 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; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR PANTHER; PTHR10127:SF850; METALLOENDOPEPTIDASE; 1.
DR Pfam; PF01400; Astacin; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000186955};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..371
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012004801"
FT DOMAIN 88..224
FT /note="Peptidase metallopeptidase"
FT /evidence="ECO:0000259|SMART:SM00235"
SQ SEQUENCE 371 AA; 39595 MW; D9E32E66707D49EA CRC64;
MSLLVTICIA LLIFSFSSAI VAAQTPSGSD PLYPLDKNVS VATIFDNSFG ERNVSYFTTV
ERLAIIDGDV IYGTEAQLLS SEFRSFAVKQ PWPGATVVYK YDTAGTAARV AAIVNTAIVR
WQLVSPYLTF QQLSNNVTPM NGVLTISSND CGGCNANVGF GALLPLQMNL QQPSTACNGS
CGPNEATHEL GHVLGLLHEH QRPDRERTVN YHCENLSPNC TGGATMPAGS DCCSGAPPGC
CGNAHNFDII SGLGKSYEYQ YDVNSVMHYV SQAFALPGTF TLTPVNTTVT LPTVNPSNPD
VPDFERVCKI YEAQCPQAQS CLALGCPYKE KACTDFGSGY CSFHPYADGC GGSKAAKCVE
KNEMCKENGC S
//