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Database: UniProt
Entry: R1GB50_BOTPV
LinkDB: R1GB50_BOTPV
Original site: R1GB50_BOTPV 
ID   R1GB50_BOTPV            Unreviewed;       509 AA.
AC   R1GB50;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Putative glycosyl hydrolase family 43 protein {ECO:0000313|EMBL:EOD43079.1};
GN   ORFNames=UCRNP2_10225 {ECO:0000313|EMBL:EOD43079.1};
OS   Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS   (Neofusicoccum parvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Neofusicoccum.
OX   NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD43079.1, ECO:0000313|Proteomes:UP000013521};
RN   [1] {ECO:0000313|Proteomes:UP000013521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX   PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT   vascular pathogen associated with grapevine cankers.";
RL   Genome Announc. 1:E0033913-E0033913(2013).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR   EMBL; KB916912; EOD43079.1; -; Genomic_DNA.
DR   RefSeq; XP_007589455.1; XM_007589393.1.
DR   AlphaFoldDB; R1GB50; -.
DR   KEGG; npa:UCRNP2_10225; -.
DR   eggNOG; ENOG502SI39; Eukaryota.
DR   HOGENOM; CLU_009397_6_0_1; -.
DR   OMA; FEAPWLM; -.
DR   OrthoDB; 5470935at2759; -.
DR   Proteomes; UP000013521; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd08990; GH43_AXH_like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR   PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013521};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..509
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004351201"
FT   SITE            179
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   509 AA;  54235 MW;  DA34E7057181E1F0 CRC64;
     MVTQTHLSLL FLHGALALAQ NSPVTVQSTG NPILADGSYY SADPAPLVVN NTLYIIAGHD
     EAPVDQNAFV INEWEMFVAT SPKPSGGEWT FHPGIAKPHE IFTWAAEGTA YASQIVQGPD
     GKFYLYAPVT EANSANADPF AIGVAVADSP LGPFTDAHPS GPILSQSVPA PGNDIQNIDP
     TVLVDDDGKV YVYYGTFGAL RGYELDEDMA TTVGDVTEVS GLTGFFEAPW IMKRNDTYYM
     LYAANNAGPD SPCTPTSYHA CIAYGTASSP LGPWTFQDVI LGIVSSTTSH SGAVELDGQW
     YLVYHTADAE GGGHFRRSVA FDLLTWDDSQ SPPAINRVVQ THRPQAAAEP TRNIAPKAKA
     SSVNETPIQY WVESLHDGKI PSNPLPPDYW ASYAGDTSPE TSTLVYTWNS TVALNGARMA
     FFADQDAGAS VGVPPPASWH IEYLNAAGTW EKVANSSAYP VTVTDDPEEV SFTEIRTTSI
     RAVLIASGSG GTFGGVGVKE WEALAPTAQ
//
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