ID K3X3Y3_GLOUD Unreviewed; 1050 AA.
AC K3X3Y3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Nardilysin {ECO:0008006|Google:ProtNLM};
OS Globisporangium ultimum (strain ATCC 200006 / CBS 805.95 / DAOM BR144)
OS (Pythium ultimum).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Pythiales; Pythiaceae;
OC Globisporangium.
OX NCBI_TaxID=431595 {ECO:0000313|EnsemblProtists:PYU1_T011932, ECO:0000313|Proteomes:UP000019132};
RN [1] {ECO:0000313|Proteomes:UP000019132}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DAOM:BR144 {ECO:0000313|Proteomes:UP000019132};
RX PubMed=20626842; DOI=10.1186/gb-2010-11-7-r73;
RA Levesque C.A., Brouwer H., Cano L., Hamilton J.P., Holt C., Huitema E.,
RA Raffaele S., Robideau G.P., Thines M., Win J., Zerillo M.M., Beakes G.W.,
RA Boore J.L., Busam D., Dumas B., Ferriera S., Fuerstenberg S.I.,
RA Gachon C.M., Gaulin E., Govers F., Grenville-Briggs L., Horner N.,
RA Hostetler J., Jiang R.H., Johnson J., Krajaejun T., Lin H., Meijer H.J.,
RA Moore B., Morris P., Phuntmart V., Puiu D., Shetty J., Stajich J.E.,
RA Tripathy S., Wawra S., van West P., Whitty B.R., Coutinho P.M.,
RA Henrissat B., Martin F., Thomas P.D., Tyler B.M., De Vries R.P., Kamoun S.,
RA Yandell M., Tisserat N., Buell C.R.;
RT "Genome sequence of the necrotrophic plant pathogen Pythium ultimum reveals
RT original pathogenicity mechanisms and effector repertoire.";
RL Genome Biol. 11:R73-R73(2010).
RN [2] {ECO:0000313|Proteomes:UP000019132}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM:BR144 {ECO:0000313|Proteomes:UP000019132};
RA Buell R., Hamilton J., Hostetler J.;
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblProtists:PYU1_T011932}
RP IDENTIFICATION.
RC STRAIN=DAOM BR144 {ECO:0000313|EnsemblProtists:PYU1_T011932};
RG EnsemblProtists;
RL Submitted (FEB-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; GL376621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K3X3Y3; -.
DR STRING; 431595.K3X3Y3; -.
DR EnsemblFungi; PYU1_T011932; PYU1_T011932-p1; PYU1_G011906.
DR EnsemblProtists; PYU1_T011932; PYU1_T011932; PYU1_G011906.
DR VEuPathDB; FungiDB:PYU1_G011906; -.
DR eggNOG; KOG0959; Eukaryota.
DR HOGENOM; CLU_004639_1_0_1; -.
DR InParanoid; K3X3Y3; -.
DR OMA; INQVMEH; -.
DR Proteomes; UP000019132; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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; IPR001431; Pept_M16_Zn_BS.
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.
DR PROSITE; PS00143; INSULINASE; 1.
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:UP000019132};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 103..223
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 258..444
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 450..734
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 754..922
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..74
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1050 AA; 119426 MW; 32BB737C607F87D2 CRC64;
MHLVGDVVER SKSPSDQKKY KLLTLPNALQ VVLISTKDVT RHGDDNDESD SDEDDEHDDD
KSGDDDDDES EGDERMSSES AGEHSDASEY EEDGEEDRGG HSRRAGACLT VGVGSYAEPE
SLPGLAHYLE HMVFMGSEKY PNENEFESFL SAHGGFSNGS TDNELTNYMF EVGPEHLETA
LDMFAQFFIA PLMKPETMDR ELSAIESEFS QATQNDRIRQ QQVLCAESKK AHPYAKFGWG
NRKSLKEQPE AEKIDVHKEI RAFYERYYSA NIMKLVVCGE DTLEDMEKWV TQSYSKIPNT
NVEVPSFASF GQPFGSQAHP SPVLCRIVPV RDIHTLQLDW MIPPIFGHYR QKPADYIASL
LGHESEGSVL SLLKERGWIS ALTAGVTETD GNDSGTYGAK FDVTMKLTLE GISHWEEITH
VVFEYLQMLE ASDFPEWVFE ELKALAEISF RFQEENSAVE KCEELAALMQ DMYQVPAHDL
LKVDLFQGAF DKQLVREILP HLSPENVFIS LTTKKHGDNP DFQTQALEEE WFGVKYTKED
INDAVVKKWK AVGLNEKLQL PKPNPFIPRD FTLVENGAVD EISCHRFAFG KMWYKPDTMF
ATPRAHIAFL FHLPSVMQSI TNVVSTELYV KLVRDALDEY AYHANVAEIM YSLRVKESGL
ELIVGGFNDK LGLLVKVVVE ALFHTQVKAA RFDIMKQEML REYRNSISKV AHKAKYLRLQ
LLERVAFPLN QSIAALEATT MESLNAFLAN ALWNANTHLS SFAHGNISVE AATELRKMVE
ADLERVSSVL PASGIPQRFI NQIPPTPSGL LIKARSEHKE EKNTQVEVYY QIGEHNLRTL
AYADLLEQLM EEPLFDTLRT KQELGYDVSC TVRVTHGIVG FGVMVQSSLF DAKYISYCID
RFMIDFEEAI AMMPDEHFHD HVQAQILKKL EPDHNLLETT HRLWYEIASG RLDFDIDDKL
AKEFETCTKP EMLELYHSWI LQNPKKLSLH VIGQSSRPAK SVNGKSKEQE MFPVPARIKD
LYAFKMELPF YPDNTRVRDE VESKEERTSL
//
