ID W7MLQ6_GIBM7 Unreviewed; 412 AA.
AC W7MLQ6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 28-JUN-2023, entry version 37.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=FVEG_08402 {ECO:0000313|EMBL:EWG48719.1};
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:EWG48719.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG48719.1, 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 -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; DS022252; EWG48719.1; -; Genomic_DNA.
DR RefSeq; XP_018754910.1; XM_018897296.1.
DR AlphaFoldDB; W7MLQ6; -.
DR EnsemblFungi; FVEG_08402T0; FVEG_08402T0; FVEG_08402.
DR GeneID; 30066140; -.
DR KEGG; fvr:FVEG_08402; -.
DR VEuPathDB; FungiDB:FVEG_08402; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_0_3_1; -.
DR OMA; KHWTIAV; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000009096; Chromosome 10.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd06097; Aspergillopepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF2; ASPERGILLOPEPSIN-1-RELATED; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000009096}.
FT DOMAIN 105..410
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 121
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 301
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 412 AA; 45143 MW; ED37CD76D82BDADF CRC64;
MGMKEGYLYD TFWSTYTDVL IMSLKLLQLI AALAASAHGL AVPDSQGAAF SLDALPSTAE
EFDPAAERQR LEAKFPTAHG SNIKARTTKQ SGSVKVKPIA GGQSFFTPTV IGNQTFKMLY
DTGSADLWVY SNDSSPFQRE DHPGYVPTSS ATLLKGYNFT LKYAFGDTIS GEVFTDTVKA
GPVVAKKQAV EAALIIQPEV AYDGIMGLAF STINQVTPKK QKTFFETLLP ILKKKIFAAN
LRVDGKPATW DFGYIDSTKF KGKVSYTPVV STKYWSMNVS SYAVGKSSFN SKKKVGEVIV
DSGTYLIYLP EAVVNDYYSH IKGYKLTEGG SRTYPCNATV PDFHLKTDST TLTIPGRDVN
YTVYDPTTRL CTGAITTQLN NKYSVLGNLF MKNYYVIHSQ EDATPKLGFA SL
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