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Database: UniProt
Entry: F9G870_FUSOF
LinkDB: F9G870_FUSOF
Original site: F9G870_FUSOF 
ID   F9G870_FUSOF            Unreviewed;       569 AA.
AC   F9G870;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=AB hydrolase-1 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FOXB_14852 {ECO:0000313|EMBL:EGU74624.1};
OS   Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU74624.1};
RN   [1] {ECO:0000313|EMBL:EGU74624.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU74624.1};
RX   PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA   Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT   "A highly conserved effector in Fusarium oxysporum is required for full
RT   virulence on Arabidopsis.";
RL   Mol. Plant Microbe Interact. 25:180-190(2012).
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:EGU74624.1}.
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DR   EMBL; AFQF01003655; EGU74624.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9G870; -.
DR   STRING; 660025.F9G870; -.
DR   PaxDb; 5507-FOXG_12189P0; -.
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}.
FT   DOMAIN          113..279
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          439..526
FT                   /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08386"
SQ   SEQUENCE   569 AA;  63805 MW;  CECB1C2AF0933F0B CRC64;
     MDKHSLNPPE WAEPRRKSRV NKWKVFGAGI LTVAAFHWLA PHCSHRHQHP HHHGPTTYPG
     EHIEWKPCGE ISNRSVECSK IDVPIDQFHP DVSNKTFNVP IIRMRGKDGS KNILLNPGGP
     GGSGFEFLHR RGEQLSTIVG DGFHLVSFDP RGINSSSPRA SCYPSKQARQ QLGSVHDIDI
     VKDGAEIYAW THNYVRACED TMGEHGKYIN TPQTAADMNS ILDALGQKDM YYWGFSYGTL
     LGQTYATLFP ERSHRVIIDG VVNQFLWYQA RFDMEDLNDT ENVMDGLLKE CIKSGDACPL
     SSMADSWEGL KDKFLSFVGE LKEQPMNVYV NNSVYGLLDY QKIWYGALFP VLYKPQFWGT
     FAERMAQLMG GNATEALMAY GLDDGEDSDA LYTVSMNDGL SGPLHWPQDL DSLLDIVMPT
     FNRSVFAPDD LVYLFAKQQW RIPKTHNYVP RNGVETAHPL LILTTTYDPV CPLISARSAE
     AAFKDSKIVE VKGYGHCSVA VPSLCLAKHV RAFLYNGTMP ANDTQCEVDG PYFKPNGTAG
     VMSFEDPEDQ AIHLAQMALA RDPEWPRHV
//
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