ID W7MAH9_GIBM7 Unreviewed; 491 AA.
AC W7MAH9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=FVEG_05601 {ECO:0000313|EMBL:EWG44580.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG44580.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG44580.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
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}.
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DR EMBL; DS022247; EWG44580.1; -; Genomic_DNA.
DR RefSeq; XP_018750771.1; XM_018893846.1.
DR AlphaFoldDB; W7MAH9; -.
DR STRING; 334819.W7MAH9; -.
DR EnsemblFungi; FVEG_05601T0; FVEG_05601T0; FVEG_05601.
DR GeneID; 30063584; -.
DR KEGG; fvr:FVEG_05601; -.
DR VEuPathDB; FungiDB:FVEG_05601; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_024336_1_1_1; -.
DR OMA; YWVQASK; -.
DR OrthoDB; 51543at2759; -.
DR Proteomes; UP000009096; Chromosome 3.
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:UP000009096};
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..491
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5005151260"
FT DOMAIN 125..218
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 246..431
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 491 AA; 53782 MW; 0002792E39CB48A6 CRC64;
MKFLNTLLYG ALLFSEVSAT KKLTPSQVEG DIKKSNLRKT LEDLNTIAKK NGGNRAFGFP
GYKASVDYIS KQLKGQYGKH LNTYIQPFNY TFEQTKDIWV RGPDGEDVYV ITLIYNVGTP
TPDGVTAPLV LVPIDDERGS GCFADQWEDV DAKDKLALVK RGSCAISDKL KLAKQAGALG
VLLVNNQPGE GITSATLSAE NLELIVPVGV IPLEVGTAWR TRIEDGETLE VTLLVDSFYE
TRETWNIIAE TKQGDPNNVV MMGAHLDSVQ AGPGINDDGS GTAGILEIAK SFTKYTGYKN
KVRFAWWGAE ESGLAGSYYY GEQLTEEEAD SIRFYFNYDM IGSPKPKYWV QASKPADRVG
GDILAAWLRK KGKTVEWEEF GESSDYAAFI ELGIPSSGIF TGADAETDPC YHLECDTINN
IHWGALTLNT KAAGRAAAQF ALSLKGVPAR DKTSANPKSK RAVAARFEQW QKKKTLASNA
HKCNHKTKVV V
//
