ID F9FHI1_FUSOF Unreviewed; 574 AA.
AC F9FHI1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Beta-xylosidase C-terminal Concanavalin A-like domain-containing protein {ECO:0000259|Pfam:PF17851};
GN ORFNames=FOXB_05860 {ECO:0000313|EMBL:EGU83612.1};
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:EGU83612.1};
RN [1] {ECO:0000313|EMBL:EGU83612.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU83612.1};
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 glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:EGU83612.1}.
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DR EMBL; AFQF01001829; EGU83612.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FHI1; -.
DR STRING; 660025.F9FHI1; -.
DR PaxDb; 5507-FOXG_09888P0; -.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd18833; GH43_PcXyl-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF12; BETA-XYLOSIDASE-RELATED; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..574
FT /note="Beta-xylosidase C-terminal Concanavalin A-like
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003383331"
FT DOMAIN 343..541
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 38
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 151
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 574 AA; 63295 MW; 34FF28FEE3447678 CRC64;
MRFSWLWCPL LALGSALPEK KTDVSTYTNP VLPGWHSDPS CIQKDGLFLC VTSTFISFPG
LPVYASRDLV NWRLISHVWN REKQLPGISW KTVGQQQGMY APTIRYHKGT YYVICEYLGV
GDIIGVIFKT TNPWDESSWS DLVTFKPTHI DPDLFWDDDG KVYCATHGIT LQELDLETGK
LSPELNIWNG TGGVWPEGPH IYKRDGYYYL MIAEGGTAED HAITIARARK ITGPYEAYKN
NPILTNRGTS EYFQTVGHGD LFQDTKGNWW GLCLATRITA PGVSPMGREA VLFNGTWNKG
EWPKLQPVRG RMPGNLLPKP TRNVPGDGPF NADPDNYNLK KAKNIPPHFV HHRVPREGAF
SLSAKGLHIV PSRNNVTGSL LAGDEIELSG QRGLAFIGRR QTHTLFKYSV DIDFKPKSDD
QEAGITVFRT QLDHIDLGIV RLPTKQGSNK KSKLAFRFRA TGAQNVPAPK VVPVPDGWEK
GVITLHIEAA NATHYNLGAS SRGGRTLNIA TASASLVSGG MGQFVGSLLG PYATCNGKGS
GVDCPKGGDV YVSQWTYKPV AQEIDHGVFV KSEL
//
