ID N4TKX6_FUSC1 Unreviewed; 416 AA.
AC N4TKX6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=FOC1_g10009214 {ECO:0000313|EMBL:ENH63319.1};
OS Fusarium oxysporum f. sp. cubense (strain race 1) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1229664 {ECO:0000313|EMBL:ENH63319.1, ECO:0000313|Proteomes:UP000016928};
RN [1] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
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; KB731255; ENH63319.1; -; Genomic_DNA.
DR AlphaFoldDB; N4TKX6; -.
DR STRING; 1229664.N4TKX6; -.
DR VEuPathDB; FungiDB:FOC1_g10009214; -.
DR HOGENOM; CLU_021802_3_0_1; -.
DR OMA; NCDVDGF; -.
DR Proteomes; UP000016928; 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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000016928};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..416
FT /note="Peptidase M20 dimerisation domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004120095"
FT DOMAIN 228..317
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 416 AA; 45112 MW; 7E2AC58D693020FF CRC64;
MRVATVASFL ASASLATAFD WQQVLGDWDQ QPSSDAIASN DDAPSYRSEL LSLHKSLIET
SSVSGTEHDV GVWLEGYLEK KGYTTSRQEV EPFENTPEGK PRFNVLAWRQ DGKKTFDPKV
CVSSHIDVVP PHIPYGIDDG EVTKETMITG RGSVDAKGSV AAQITAVEDL IEHGKIDPHK
LVLLFVVGEE VKGDGMRRFS EAIETKELPY SLDAVIFGEP TELKLACGHK GMLGCDVTTK
GFPGHSGYPW LGKSANELMI RAFAKVLDTD LGSSELFGNT TVNIGRFHGG VASNVIPEEA
KVGLAVRVAS GKQADGHVVV HDKIQAIFDE VDKDAFIFDC THGYGPVEAN CDVDGFEKIT
VNYGTDIPNL KGDHTRYLYG PGNILVAHGA RENLTVADLE TAVEGYQKLI LHALKQ
//
