ID A0A428QD35_9HYPO Unreviewed; 494 AA.
AC A0A428QD35;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=CEP54_005350 {ECO:0000313|EMBL:RSL63189.1};
OS Fusarium duplospermum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=1325734 {ECO:0000313|EMBL:RSL63189.1, ECO:0000313|Proteomes:UP000288168};
RN [1] {ECO:0000313|EMBL:RSL63189.1, ECO:0000313|Proteomes:UP000288168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62584 {ECO:0000313|EMBL:RSL63189.1,
RC ECO:0000313|Proteomes:UP000288168};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M28 family.
CC {ECO:0000256|RuleBase:RU361240}.
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:RSL63189.1}.
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DR EMBL; NKCI01000040; RSL63189.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428QD35; -.
DR STRING; 1325734.A0A428QD35; -.
DR Proteomes; UP000288168; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
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; cd04816; PA_SaNapH_like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR PANTHER; PTHR12147:SF55; PEPTIDE HYDROLASE; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
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 Reference proteome {ECO:0000313|Proteomes:UP000288168};
KW Signal {ECO:0000256|RuleBase:RU361240};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT CHAIN 20..494
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5018812277"
FT DOMAIN 126..219
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 246..443
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 494 AA; 52658 MW; 5C3695A460A64096 CRC64;
MKLTTAATLL TLLPSLGAAG KDRRPQVKSN KLQKLITEKG LMRNLQKLND IAYDNGGNRA
FGLPGYAASV DFIYKELRKL KGFKAWKEDF PALFTETTAA EVTVDGETFR TVALTYTPST
PEEGITRELV HGPEGEAGCD ADNYEGLGAE DKIVLVERGR CPDQTTFAGK LKAAAKAGAV
AVVLYNSDPA KLTAGSLSNP NPDEYVPAGL IDQEPGQALK ARLDAGETVE AYVQIQQLIE
ERITQNVFAE TKGGDGTNVV MLGAHLDSVQ AGPGINDDGS GTSLILEIAK GLQHFSTNLK
VKFGWWGAEE NGLWGSKAYV NGLTPEEVNN LLVYLNFDMV SRGFYGVFDG TGDKAGPGGP
PGSDVIEDLF VEHFTSKGIE VTPVGLTGGT DYVPFLEVIK KPVGGLFTGT GAEQDACYHQ
ACDNITNPVP ETITINAKAA AHVLSILAVD GKKLIPKTAA NTTTASIKRV RDSASLHEHD
FTAVLGKFCD HDLI
//
