ID A0A2H3HW08_FUSOX Unreviewed; 504 AA.
AC A0A2H3HW08;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Tripeptidyl aminopeptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AU210_005249 {ECO:0000313|EMBL:PCD42723.1};
OS Fusarium oxysporum f. sp. radicis-cucumerinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=327505 {ECO:0000313|EMBL:PCD42723.1, ECO:0000313|Proteomes:UP000219602};
RN [1] {ECO:0000313|EMBL:PCD42723.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD42723.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=27387256; DOI=10.1111/1462-2920.13445;
RA van Dam P., Fokkens L., Schmidt S.M., Linmans J.H., Kistler H.C., Ma L.J.,
RA Rep M.;
RT "Effector profiles distinguish formae speciales of Fusarium oxysporum.";
RL Environ. Microbiol. 18:4087-4102(2016).
RN [2] {ECO:0000313|EMBL:PCD42723.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD42723.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=28831051; DOI=10.1038/s41598-017-07995-y;
RA van Dam P., Fokkens L., Ayukawa Y., van der Gragt M., Ter Horst A.,
RA Brankovics B., Houterman P.M., Arie T., Rep M.;
RT "A mobile pathogenicity chromosome in Fusarium oxysporum for infection of
RT multiple cucurbit species.";
RL Sci. Rep. 7:9042-9042(2017).
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PCD42723.1}.
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DR EMBL; MABQ02000003; PCD42723.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3HW08; -.
DR STRING; 327505.A0A2H3HW08; -.
DR OrthoDB; 2407664at2759; -.
DR Proteomes; UP000219602; Chromosome 4.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR013595; Pept_S33_TAP-like_C.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000219602};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..504
FT /note="Tripeptidyl aminopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013931002"
FT DOMAIN 84..294
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 407..501
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
SQ SEQUENCE 504 AA; 53914 MW; B3D6155F8E67FF3A CRC64;
MAFLKSLVLF VLLQFVNAAA TKSSAPKISW GECPSLIPPG VDCGKINVPL AYQSGNSTSG
KGDDTVELVF TRLNHTGKGE KHGVLFFNTG GPGASGAITV AGSPYVSAIS FSDELRDVYD
IIGLDPRGVG VSSPVQCDPK VFNKRVKTFV TTDEEYDALF NYSRSVGESC AKLTGPLINH
LDSVHVAKDH EVVRKALGVE KFNYLGLSYG TLLGATYASL FPKSVGRMAL DANVDHSQSE
IATLLAEATA YETVLDQFFK WCDKNSTCAL HGKSASRIWD ETLARADSKA IPAPDCNGTC
RSDVTGEEIR YNAQEFLTFV DLDFGSGSTW AALGDAILQA SKGNATALST STPSGKVVND
PSGSPYSYLA IGCQDWLHKS KTSVDLRQKL INAVTFAPRT RGASQTYYYE STCIGWPAPL
TNPQGPLADG IKDAPTILIA ASVYDPETSL TGAEGVREQL THRVSITRNG AGHTSHYLGG
DTSKVMDRYL ATGKLPRDGT VYRT
//
