ID A0A395MBF9_9HYPO Unreviewed; 451 AA.
AC A0A395MBF9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN ORFNames=FIE12Z_10572 {ECO:0000313|EMBL:RFN45188.1};
OS Fusarium flagelliforme.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN45188.1, ECO:0000313|Proteomes:UP000265631};
RN [1] {ECO:0000313|EMBL:RFN45188.1, ECO:0000313|Proteomes:UP000265631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN45188.1,
RC ECO:0000313|Proteomes:UP000265631};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247, ECO:0000256|PIRNR:PIRNR037226}.
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:RFN45188.1}.
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DR EMBL; PXXK01000365; RFN45188.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395MBF9; -.
DR OrthoDB; 1074531at2759; -.
DR Proteomes; UP000265631; 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:SF4; PEPTIDASE M20 DOMAIN-CONTAINING PROTEIN 2; 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:UP000265631};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 216..306
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 451 AA; 48518 MW; C59F016D898B3100 CRC64;
MVYLSQAKGL AAVVYGLALL AAPVSSSQTL LSPRAKKNAT SPYTETVSKY VDSLDKELWS
INKNIHDNPE LGYKEFKAHK LLTSYMKKQK GWKVTDTVGG IDTAFKAVFE GSGDGPVVSF
NAEYDALEGL GHACGHNLIA TASLGGALAA AEIMREEKLG GKVILFGTPA EESLGGKVKM
LEAGVFKDAK IDISLISHPS NSPDTPYMLA QSTDRFDVEY TGREAHAAAG PWDGINAQDA
LLLANSALSY MRQQMRTTDR VHGIIHSAGS RINVIPADAS GSYQLRSANE EQLEELSDKV
YNCFKAGAIG TGAKMNFTMR PYGYANMNSN DGLAASYTRW FEELGGDLPD ADVDKMRSPG
GSTDQGNISQ DFPTISPMFQ ITFQNGTVPK EGPHTAPFEE AAGSKAAFEK SLMVAKSLAG
VAVDMLTVDG LLDEIKDEFK KSKKSSGRRR R
//
