ID W7M1V9_GIBM7 Unreviewed; 674 AA.
AC W7M1V9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Peptidase M3A/M3B catalytic domain-containing protein {ECO:0000259|Pfam:PF01432};
GN ORFNames=FVEG_03590 {ECO:0000313|EMBL:EWG41479.1};
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:EWG41479.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG41479.1, 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|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; DS022245; EWG41479.1; -; Genomic_DNA.
DR RefSeq; XP_018747670.1; XM_018891198.1.
DR AlphaFoldDB; W7M1V9; -.
DR GeneID; 30061716; -.
DR KEGG; fvr:FVEG_03590; -.
DR VEuPathDB; FungiDB:FVEG_03590; -.
DR eggNOG; KOG2089; Eukaryota.
DR OrthoDB; 735202at2759; -.
DR Proteomes; UP000009096; Chromosome 2.
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 CDD; cd06455; M3A_TOP; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
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; 1.
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:UP000009096};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 221..668
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 674 AA; 76456 MW; 081C70F6F582F595 CRC64;
MTSEPKVPAP PSFASLTPDG VLAETENILT STSALHDDLA AKFTPSTATF NNIIRPIVDD
TNRAACRLRI LTTLLGQLSP DRELRDAARR AETRGAAAQV KILMRHDIAS LVGAIYEREK
TAPDGNLDGQ DRHLLARMHG EYLRSGSFLR SHKEREELQA TLDEIDRVRS AAQTAFTEDE
GGIWFDRADL AGVPETMLAS MPQEGTQVQV TFRNTHVTAV MRHAVSSDTR RRFAVADQNR
LPDNVTRLAS LVALRDEVAR LLRYEHHAAL KIVDKMAPSV DYVEAQLSDL HRRLKPLAKA
ETDRLIQLKQ RDCKEPVSEL YFWDRAYYLH KQTQRNFFVD HEPLAEYFEV NRTLQGMLDV
FKELFGIEFQ PIVTSVWHES VVAYEAWDTP SEGGEFLGHL YVDLFDREGK YRGAHHVLIQ
PGFAESTGEK HYPASALVCS FAHPSQSRPA LLQHSEVKTM FHELGHAIHN IVARTKYAIP
HSRDFIEIPS IMLENWIWLP DVLIRLGRHH KSQEALSREL TESVARTRNA NRANSILAQV
QPAVFDLAIH TPPSHKAALE MDTTEIWNRT KREILTHSFG PDPQHWGAGQ ARFAHMFRKN
DGSYFSYPLS MVIAADLFRS KFAVDPLNSE MGRNYRYQVL EPGSSRPEID ILKDFLGREP
CSKTILDELC HDTE
//
