ID F9F1Z4_FUSOF Unreviewed; 481 AA.
AC F9F1Z4;
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:0000259|Pfam:PF00561};
GN ORFNames=FOXB_00418 {ECO:0000313|EMBL:EGU89069.1};
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:EGU89069.1};
RN [1] {ECO:0000313|EMBL:EGU89069.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU89069.1};
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:EGU89069.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFQF01000129; EGU89069.1; -; Genomic_DNA.
DR AlphaFoldDB; F9F1Z4; -.
DR STRING; 660025.F9F1Z4; -.
DR PaxDb; 5507-FOXG_01990P0; -.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR002410; Peptidase_S33.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF2; PROLYL AMINOPEPTIDASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 85..245
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT REGION 61..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 481 AA; 54065 MW; 49677266BDDF1864 CRC64;
MSTPDNLSIP QADLVSRKSH VLPGQLCVTE LFFKVPLDYT DIQGPSITLF ARAVKKHDVP
IFPPDDEESE NSPKDEFGEP PKPYMVYLEG GPGFGNREPQ DHPLTRHALA KGYQLLLLDH
RGVGLSTPVG ADMLSLVSED VEGRTRYLGL MRQDNTVRDC EAVRKYLTAS WPATKQPWSI
FGQSYGGFIA LSYLSMHPEG LREVFLTGGL APVGKKPDQV YEATFQRVIE RNEQYYEKFP
EDVENVRQVA KFIESKGGSI PLPSGGVLTV PRLLTIGISF GSHGGFDQVH STILTLKTSL
DQFGFFNRAS LVPLEGWNPF DTNIIYAILH EAIYCDGPGL ASAWSANRIG KELKPFSWLN
DNYSTESTSG CLYFSGEMIF PFHFETYPEL QILRQEAKLL ASRDNWPALY DQEKLRKNKV
PVYAASFVED MYVDYNFARD TAKLVKGTKT FETNVMYHSA LRAKSDEVLQ QLFSLRDDVI
D
//
