ID   A0A1W2TTY7_ROSNE        Unreviewed;       425 AA.
AC   A0A1W2TTY7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Putative acetylornithine deacetylase {ECO:0000313|EMBL:GAP92064.2};
GN   ORFNames=SAMD00023353_3100560 {ECO:0000313|EMBL:GAP92064.2};
OS   Rosellinia necatrix (White root-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX   NCBI_TaxID=77044 {ECO:0000313|EMBL:GAP92064.2};
RN   [1] {ECO:0000313|EMBL:GAP92064.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W97 {ECO:0000313|EMBL:GAP92064.2};
RA   Kanematsu S.;
RT   "Draft genome sequence of Rosellinia necatrix.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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DR   EMBL; DF977476; GAP92064.2; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W2TTY7; -.
DR   STRING; 77044.A0A1W2TTY7; -.
DR   OMA; NCDVDGF; -.
DR   OrthoDB; 2875217at2759; -.
DR   Proteomes; UP000054516; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05652; M20_ArgE_DapE-like_fungal; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF30; ACETYLORNITHINE DEACETYLASE; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054516};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..425
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012777481"
FT   DOMAIN          231..311
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   425 AA;  44663 MW;  F1C7D7B06AD9A0D9 CRC64;
     MKLLGGAALL LSTAAVASRA ELRTPPGSGL PVPVASSDDA PPYRDELVSL HKSLVEIASV
     TYSENEVGNF LVDYLTKRDF TAKLEFLPPS STPDGAGDKK PRFNVVAWPG SERRRRPSPK
     VLVTSHIDTV PPHIPYSRSD GDEPPNGETV IRGRGSVDAK ASVAAQITAV SELLAAGRVD
     AGDVMLLFVV GEERTGDGMR HFSDAAAASP GPLGFRAAIF GEPTEGKLAC GHKGFFGCTI
     TARGKAGHSG YPWLGKSATE VLIRGLVKVL DADLGSSERF GNTTVNVGTI EGGVALNVIP
     EVAVARIAGR VAIGPELDGG RIVTGRVEDV LRSVDAEAFE TVCNNGYGVV ECACDVPDFE
     TITVNYGTDV ANLKGDHARY LYGPGSILVA HGANEAIKLK DLEAGVEGYK KLILHVVADE
     EVKEL
//