GenomeNet

Database: UniProt
Entry: A0A2K0W8H5_GIBNY
LinkDB: A0A2K0W8H5_GIBNY
Original site: A0A2K0W8H5_GIBNY 
ID   A0A2K0W8H5_GIBNY        Unreviewed;       341 AA.
AC   A0A2K0W8H5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN   ORFNames=FNYG_08061 {ECO:0000313|EMBL:PNP78582.1};
OS   Gibberella nygamai (Bean root rot disease fungus) (Fusarium nygamai).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=42673 {ECO:0000313|EMBL:PNP78582.1, ECO:0000313|Proteomes:UP000236664};
RN   [1] {ECO:0000313|EMBL:PNP78582.1, ECO:0000313|Proteomes:UP000236664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS10214 {ECO:0000313|EMBL:PNP78582.1,
RC   ECO:0000313|Proteomes:UP000236664};
RA   Gardiner D.M., Obanor F., Kazan K.;
RT   "Genome of Fusarium nygamai isolate CS10214.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:PNP78582.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MTQA01000101; PNP78582.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K0W8H5; -.
DR   OrthoDB; 1074531at2759; -.
DR   Proteomes; UP000236664; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:InterPro.
DR   CDD; cd05672; M20_ACY1L2-like; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   InterPro; IPR017144; Xaa-Arg_dipeptidase.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR30575; PEPTIDASE M20; 1.
DR   PANTHER; PTHR30575:SF0; XAA-ARG DIPEPTIDASE; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF037226; Amidohydrolase_ACY1L2_prd; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000236664};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          183..275
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   REGION          321..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   341 AA;  36918 MW;  2FC39759A3C92E51 CRC64;
     MSSNEQVYEN ISKSVAHHEQ DLADICKKIH ENPELNYKEF KAHDNICDLM HRLGYNLKRS
     AYGIQTSFEV ESGQNGKLIV FNAEYDALPG LGHACGHNLI ATSSIAAFIA TAETIRSLNI
     PGRVRLLGTP AEEGGGGKVH LIKAGAYEGV DACLMAHPTG RLSPQGEKNV DGVSAARSSA
     RRQMKVAFTG QNAHAGNTPW HGKNALDAVV SSYVNISLLR QQIQPTERIH GVIRNGGAEP
     NIIPDSTNLE YYLRAAGADQ IKELTGRVEA CFKAGAIATG CQVQCSCESD QDYMELRPNM
     SMSNEFTKHM QAFGRDYIGD ANQPPMGAST DMGKSMPLPQ S
//
DBGET integrated database retrieval system