ID A0A2H3TTG8_FUSOX Unreviewed; 496 AA.
AC A0A2H3TTG8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=BFJ69_g12528 {ECO:0000313|EMBL:RKK69674.1}, FRV6_16040
GN {ECO:0000313|EMBL:SCO91912.1};
OS Fusarium oxysporum (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=5507 {ECO:0000313|EMBL:SCO91912.1, ECO:0000313|Proteomes:UP000219369};
RN [1] {ECO:0000313|EMBL:SCO91912.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V64-1 {ECO:0000313|EMBL:SCO91912.1};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000219369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA Guldener U.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RKK69674.1, ECO:0000313|Proteomes:UP000285084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo_A13 {ECO:0000313|EMBL:RKK69674.1,
RC ECO:0000313|Proteomes:UP000285084};
RX PubMed=30202022; DOI=10.1038/s41598-018-30335-7;
RA Armitage A.D., Taylor A., Sobczyk M.K., Baxter L., Greenfield B.P.,
RA Bates H.J., Wilson F., Jackson A.C., Ott S., Harrison R.J., Clarkson J.P.;
RT "Characterisation of pathogen-specific regions and novel effector
RT candidates in Fusarium oxysporum f. sp. cepae.";
RL Sci. Rep. 8:13530-13530(2018).
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; MRCX01000151; RKK69674.1; -; Genomic_DNA.
DR EMBL; FMJY01000010; SCO91912.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3TTG8; -.
DR VEuPathDB; FungiDB:FOC1_g10003554; -.
DR VEuPathDB; FungiDB:FOC4_g10005334; -.
DR VEuPathDB; FungiDB:FOIG_11715; -.
DR VEuPathDB; FungiDB:FOMG_09278; -.
DR VEuPathDB; FungiDB:FOXG_13549; -.
DR VEuPathDB; FungiDB:FOZG_15151; -.
DR VEuPathDB; FungiDB:HZS61_004631; -.
DR OrthoDB; 51543at2759; -.
DR Proteomes; UP000219369; Unassembled WGS sequence.
DR Proteomes; UP000285084; 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 ECO:0000313|EMBL:SCO91912.1}; 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 Zinc {ECO:0000256|RuleBase:RU361240}.
FT DOMAIN 124..217
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 244..440
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 496 AA; 53238 MW; 3B84F9F1C8E0A6AA CRC64;
MKFSTGVATL LALAPSHGLA KTHKLESKKI QADMKTKNLM SNLEAFNDIA FANGGNRAFG
LPGYDASVDY IFKRISKVKN AKVWKQNFPA LFAFVDSIEL KVDDTPVYVY GLTYSPSTSE
EGITAEIALG PEGAAGCDAS SYDDLDVKGK IVLVQRFRCP TGGTLAGRVI PAAAAGASAV
IIYHDLTTNV TAGSLSQPDP EKHVPAGFIN LVDGEKIKER IEAGETVTAH FQQTQTIEER
ITQNVIAETK GGDPRNVIML GAHLDSVQAG PGINDDGSGS SLILELFLAL SKYKTKNRIR
FAWWGAEENG LLGSKHYTST LPAKDVNDLL VYLNFDMVSK GFFGVADTDG SSHGSKAPKG
SEVTEKIFTE YFESKGIEVT PAVLTNGSDY APFWQNLNKP FGFLHTGTAV AQDPCYHQAC
DTIDNPDSKT LTINAKAAAH ILAVLDDRGT KLIPKTKTTA ASLQGLQERS VGPDLAQIDE
LEAMGIRHLG CGIHEI
//