ID V5FYD3_BYSSN Unreviewed; 423 AA.
AC V5FYD3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Acetylornithine deacetylase, putative {ECO:0000313|EMBL:GAD93627.1};
GN ORFNames=PVAR5_2239 {ECO:0000313|EMBL:GAD93627.1};
OS Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD93627.1, ECO:0000313|Proteomes:UP000018001};
RN [1] {ECO:0000313|Proteomes:UP000018001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA Oka T., Ekino K., Fukuda K., Nomura Y.;
RT "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL Genome Announc. 2:E0116213-E0116213(2014).
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}.
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:GAD93627.1}.
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DR EMBL; BAUL01000062; GAD93627.1; -; Genomic_DNA.
DR AlphaFoldDB; V5FYD3; -.
DR eggNOG; KOG2275; Eukaryota.
DR HOGENOM; CLU_021802_2_3_1; -.
DR InParanoid; V5FYD3; -.
DR OrthoDB; 1771548at2759; -.
DR Proteomes; UP000018001; 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 Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
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:SF8; M20_DIMER DOMAIN-CONTAINING PROTEIN; 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; 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:UP000018001};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 192..319
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 423 AA; 45728 MW; D7EFFDD47FB2DC64 CRC64;
MDRSTLLSKI ESDRDLHISF LQSLAQAPSP NPPGDTRAAA SVITDYLQNH NVPFEIIAPK
ADMPNVVSEF AGASGKGGPR VAMNGHIDVF PAGDDSDWKH GGAWSGFNDG RHIYGRGTVD
MKAGTAASVI AFSYLYAYRE ALNGSVALSV VSDEETGGKW GSRWLLDQAR EKWGGDCMIN
AEPGGVQSVR FGEKGTLRMT FTIATKGAHG AYTFLTEGAT MMAVRLIQEL KTIENIRPTD
LPKSVEEHLQ KPEVRATIDE IMGKGAADVM LVPTLNIGTI HGGLKVNMIP EHCVFEADVR
LPIGLKAQTV LDHISNILGR YPDVQLTVQE AASNPASFCD PDHPMAKIMA DVAEATTGRK
PLAIPGLGAT DCKFWRYLDT PAYVYGVSPD TMGATDERVK IDEFLALIKV HSLSVWDYLN
GSN
//
