ID   V9DUR4_PHYPR            Unreviewed;      1113 AA.
AC   V9DUR4;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Nardilysin {ECO:0008006|Google:ProtNLM};
GN   ORFNames=F443_22276 {ECO:0000313|EMBL:ETI30604.1};
OS   Phytophthora parasitica P1569.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI30604.1, ECO:0000313|Proteomes:UP000018721};
RN   [1] {ECO:0000313|EMBL:ETI30604.1, ECO:0000313|Proteomes:UP000018721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1569 {ECO:0000313|EMBL:ETI30604.1,
RC   ECO:0000313|Proteomes:UP000018721};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica P1569.";
RL   Submitted (NOV-2013) 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:ETI30604.1}.
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DR   EMBL; ANIZ01003888; ETI30604.1; -; Genomic_DNA.
DR   AlphaFoldDB; V9DUR4; -.
DR   EnsemblProtists; ETI30604; ETI30604; F443_22276.
DR   eggNOG; KOG0959; Eukaryota.
DR   HOGENOM; CLU_004639_1_0_1; -.
DR   OrthoDB; 129328at2759; -.
DR   Proteomes; UP000018721; 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:UP000018721};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          113..233
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          267..438
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          466..764
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          798..944
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          76..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1113 AA;  124115 MW;  F378D79BF76D3DFA CRC64;
     MLGAFVESCS SPPAYSHRNR TGGRVEEVAE MTSPLSSRMS LDSFRSPADK KSYRLITLSN
     GLEVLLVQSD ASPVNRSTFD CNDDGNDLDS LSSTDDTGFD EEGDEINDRA PTLAAACLTV
     DVGSLADPEG LPGLAHYFEH MIFMGSEKYP AEDAFESFLS AHGGSSNGAT ECESTRFVFD
     VDAAYLAPAL DIFANLFVAP ILRREAMERE LKAVESEFQR MRNNNSVRLQ QVMCETSVPE
     HPYSRCFTWG NVESLKHNPE RDGINVRGQM LQLFNKFYVA PAMKLCVYGC ESLDVLEQYV
     TQSFSDIPAY RGSYDKPRSE TLTVPYGGGA GQKPTVLHVI PVGEKCSIRL YWMLPPMMKN
     YRQKPWLYVG HLLGHESPES IASLLKQRQW ATDIIAGTSD RDGYEFGSFG TVFEVRISLT
     EQGLACWEQV VQVIFDALHI FSSLAAAGDL PACVFEELHS SSEMDFRFQE DDIAPVTLCR
     ELSERMLPRH NIQQHCEGDL LRYDLIQGGF DISSVYSLLS GLSANNVRAV LVASSFADTL
     NPNDLQTERW FGTKYTVNSI PESVIAAWSQ LSNESIELSV LPTPNPFMPR NFSVLPLEPV
     IQVDNDTPPD LILTTSTTQL WYKRDRKFLV PKASVSFLVT LPEPTAAIHM LAELHVELVR
     RRLQHTLEQA ETASFTTELD VRDEAIEVVI SGFSDMLPSL VLVIMREVLR PSTTFDIESE
     LTLARGELER EYRNATLSPR AKAYELRLQM LESRAVTTDD KLEALQSKYG HESDLAADLA
     HLTVSVLGCS KDTPVIRCMV IGNMSREAAV SLVLDVEAVK TGDSSLLPCE PEPELEPEPP
     ILAPRCHTIA LPPTTNGLLV RRDSERIGER NSVVEVYFQI GKVGPTDRAY AILLRSLLAQ
     PLFHELRTKQ QLGYTVTCSI RDTHGVLGLN LSVQSASHAA GAVAKKLDVF LHEEFPHDYL
     LSDERLSPKR FAAYVQTLQR AYARPDATLT EQSERYWEEI VSGRLEFDLD ARVATALGDC
     TRQGLLERYQ CWIQGSTSCC NTCTQSRDGN RQAQHRSSKS HGTRKLRVHV VGQCSPLKPL
     EQLVPPGKTP FIITGDLHDF KRELRCYCHL TSD
//