ID   A0A366S371_9HYPO        Unreviewed;       374 AA.
AC   A0A366S371;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   ORFNames=FIESC28_03380 {ECO:0000313|EMBL:RBR23764.1};
OS   Fusarium coffeatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium incarnatum-equiseti species complex.
OX   NCBI_TaxID=231269 {ECO:0000313|EMBL:RBR23764.1, ECO:0000313|Proteomes:UP000253153};
RN   [1] {ECO:0000313|EMBL:RBR23764.1, ECO:0000313|Proteomes:UP000253153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FIESC_28 {ECO:0000313|EMBL:RBR23764.1,
RC   ECO:0000313|Proteomes:UP000253153};
RA   Gardiner D.M.;
RT   "Fusarium incarnatum-equiseti species complex species 28.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Extracellular aminopeptidase that allows assimilation of
CC       proteinaceous substrates. {ECO:0000256|ARBA:ARBA00043843}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28E subfamily.
CC       {ECO:0000256|ARBA:ARBA00043962}.
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:RBR23764.1}.
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DR   EMBL; QKXC01000069; RBR23764.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A366S371; -.
DR   OrthoDB; 1384212at2759; -.
DR   Proteomes; UP000253153; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd03879; M28_AAP; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147:SF26; ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1; 1.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|RuleBase:RU361240};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW   Zinc {ECO:0000256|RuleBase:RU361240}.
FT   DOMAIN          158..363
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   374 AA;  41794 MW;  E861CCF5DF4FE642 CRC64;
     MRYSVPLMAA LAASATATAP PQKRAEKLFT LETAAGETVE VTEDEKFQMI DDHIHFFDIT
     EWKDHSPASS LMALTPSYPT KLSHQSNVAK MVSKVKTKTM EKQLKKFSSF HNRYFNSRYG
     VEAAQWLHKE VEKVIKKSKH PLASVRLIQH QAWSQPSIVV SIPGKVRLKT VVTGSHLDSV
     ISNDRGAGRA PGADDNGSAS IMLLNLLGAF LEDERIAKGD HLNTVEFHWY SAEETGLLGS
     QDIFNSYSRL GIQVEAMLNQ DMVGYKGRDG IERFGLVTDF TNAAQNDFLK LLIDEYADIS
     YEESTCGYAC SDHASAHRNG YPSSFLFETP FGNHNPHIHT PNDTMEYVDF DHVMQHAKVT
     AGFVYELAHK DFTA
//