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Database: UniProt
Entry: A0A0J9V914_FUSO4
LinkDB: A0A0J9V914_FUSO4
Original site: A0A0J9V914_FUSO4 
ID   A0A0J9V914_FUSO4        Unreviewed;       581 AA.
AC   A0A0J9V914;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Peptidase M3A/M3B catalytic domain-containing protein {ECO:0000259|Pfam:PF01432};
GN   ORFNames=FOXG_08720 {ECO:0000313|EMBL:KNB07605.1};
OS   Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935
OS   / NRRL 34936) (Fusarium vascular wilt of tomato).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=426428 {ECO:0000313|EMBL:KNB07605.1, ECO:0000313|Proteomes:UP000009097};
RN   [1] {ECO:0000313|EMBL:KNB07605.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=4287 {ECO:0000313|EMBL:KNB07605.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Ma L.-J., Jaffe D.,
RA   Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
RA   Brockman W., MacCallum I.A., Young S., LaButti K., DeCaprio D.,
RA   Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C.,
RA   Larson L., White J., O'Leary S., Kodira C., Zeng Q., Yandava C.,
RA   Alvarado L., Kistler C., Shim W.-B., Kang S., Woloshuk C.;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KNB07605.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4287 {ECO:0000313|EMBL:KNB07605.1};
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|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; DS231705; KNB07605.1; -; Genomic_DNA.
DR   RefSeq; XP_018245650.1; XM_018387745.1.
DR   AlphaFoldDB; A0A0J9V914; -.
DR   GeneID; 28950342; -.
DR   KEGG; fox:FOXG_08720; -.
DR   VEuPathDB; FungiDB:FOXG_08720; -.
DR   OrthoDB; 735202at2759; -.
DR   Proteomes; UP000009097; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 2.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR024080; Neurolysin/TOP_N.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11804:SF84; SACCHAROLYSIN; 1.
DR   Pfam; PF01432; Peptidase_M3; 2.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009097};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          219..337
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
FT   DOMAIN          338..569
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   581 AA;  67753 MW;  143CD2A23A9CD325 CRC64;
     MDYSSLPPPL PRLIPADQIL PIMKRIVGQY QTVRENIIES VDVQKANFDN LIQPLVDIDN
     ETQGDIAIIA MLRYSPPDPA SCQGSEEACS LVNEDQAAFN ARPDFWPLLK AVKEACQEIS
     LHFEARKYLD KLFLEFKQFG YGTLRPVQIH EYLERRNYID GMRRKYNQRI RQDAGGLWFS
     LDELAGVKKH DLDRFVKDPE KHDRRFVRFS AADSLVVYRN ASESATRKRI YVGNVNNLSQ
     NAKLFEKIVV ERDLNARLVG YESHAAYRQE KRLMKTPAQV ESLLADLHDR LLARGQHDMN
     LLMDLKRKES RESAKITEYD VNAIFPWDYW YYAREASKGR FIGYLYMDLL SRDNKYKGNQ
     NVNLQCSSIS RNPSHVLLSA TCTFSLHIPK AQSDYLSIPR SELGHGIHDL LARTNYVAFH
     GHRSPPDFAE AFSVMLEKWC WMKPELKRLG LHYTSKDLHL KEKWLREHPG EDLPPERIPD
     DTIDRLIKGR QVTRSLWYLR QLVYAHFDMK VHHPRSHTEL RNMDSTKIFN DFLEKLWLVR
     APQPEDQGYP HADLGHLVSG YDAGYYSYLR RVDLNLTIKN D
//
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