ID   A0A423XAR1_9PEZI        Unreviewed;      1081 AA.
AC   A0A423XAR1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Peptidase M16 N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=VPNG_05948 {ECO:0000313|EMBL:ROW13013.1};
OS   Cytospora leucostoma.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Cytospora.
OX   NCBI_TaxID=1230097 {ECO:0000313|EMBL:ROW13013.1, ECO:0000313|Proteomes:UP000285146};
RN   [1] {ECO:0000313|EMBL:ROW13013.1, ECO:0000313|Proteomes:UP000285146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SXYLt {ECO:0000313|EMBL:ROW13013.1,
RC   ECO:0000313|Proteomes:UP000285146};
RA   Yin Z., Huang L.;
RT   "Host preference determinants of Valsa canker pathogens revealed by
RT   comparative genomics.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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:ROW13013.1}.
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DR   EMBL; LKEB01000022; ROW13013.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A423XAR1; -.
DR   STRING; 1230097.A0A423XAR1; -.
DR   InParanoid; A0A423XAR1; -.
DR   Proteomes; UP000285146; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR032632; Peptidase_M16_M.
DR   PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   Pfam; PF16187; Peptidase_M16_M; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000285146};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          39..188
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          215..394
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          401..690
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          694..875
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1081 AA;  123465 MW;  6F86527772303899 CRC64;
     MPLAEHEARP AELLTDHLET PSLDDRTYRV VRLPNQLEVL LVHDAETDKA SAAMDVNVGN
     FSDETDMPGM AHAVEHLLFM GTKKYPEENA YNQYLSAHSG TSNAYTASTS TNYYFEIAGR
     PSDDSEPSAT NPSPLKGALD RFAQFFVEPL FLESTLDREL RAVDSENKKN LQSDTWRLHQ
     LEKSLSNPAH PYCHFSTGNL EVLKIQPEAR GINVRQKFID FYEKHYSANR MKLVVLGREP
     LDVLESWAVE YFTGIRNKNL EPNRWPDAAP LGPEQLGAQV FAKPVMDSRE LGLSFPFLDE
     DELYESLPSR YISHLIGHEG PGSIMSYIKS KGWANGLSAG AYPVCPGSPG IFDCQVRLTE
     EGLKNYKEIV KIIFQYVALL RETPPQEWIF EEQKGMADVD FKFKQKTPAS RFTSKTSSVM
     QRPLPREWLL SGLSRLRKFD PELIRKSIEC LRPENLRLTI VSRDFPGKWE KKEKWYGTEY
     TSEKIPDDLL EELRKAASST PAQRIPSLHL PHKNQFIPTK LEVEKKEVKE PAVAPRLIRN
     DGLSRTWYKK DDRFWVPKAS LLVSCRSPIT FASAENAVKA RFFTDLVRDA LEEYSYDADL
     AGLQYSVSLD ARGLVIEVSG YNDKLPVLLE QVLKTMRELD IQEERFTIIK ERLSRAYRNW
     AYQQPFHQVG EYTSWLNTEQ DFLVEQYAEE LPHITCEATR AFQKELLAQM HMEVVVHGNL
     YKEDALKLTD MLEKTLKTRV LPSSQWPIWR SLLFPPGSNY VYKKTLGDPA NVNHCIEYWL
     YIGPRHERVT RAKALLLDQI LHEPAFDQLR TKEQLGYVVF SGAKNSSTTT GFRFLIQSEK
     TAQYLETRVE SFLSNYAATL ENMSDSDFES HKRSLCIRLL EKMKNLDQET SRIWNQISTE
     YYDFESATKT SECVKGLSKK DMVEFFNKYI NPSSPDRAKV SVWMIAQATS DVSTKQISEL
     VKSLELSSTE KEAEAATDLQ ARLSAAGHDE AKEIEGLREY LLHDLKVVET KIDAAAESWK
     KLHTAKTNGV VGRQEENPPS LNGTEIVFVN DIRDFKARLP VSAGARPVVD LTGYEELEPK
     L
//