ID A0A0G2FD24_9PEZI Unreviewed; 880 AA.
AC A0A0G2FD24;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Putative glycoside hydrolase family 2 protein {ECO:0000313|EMBL:KKY32074.1};
GN ORFNames=UCDDA912_g07977 {ECO:0000313|EMBL:KKY32074.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY32074.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY32074.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY32074.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY32074.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY32074.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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:KKY32074.1}.
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DR EMBL; LCUC01000345; KKY32074.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2FD24; -.
DR STRING; 1214573.A0A0G2FD24; -.
DR OrthoDB; 1847696at2759; -.
DR Proteomes; UP000034680; 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:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR032311; DUF4982.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR048229; GalB-like.
DR InterPro; IPR040605; Glyco_hydro2_dom5.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR NCBIfam; NF041463; GalB; 1.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF16355; DUF4982; 1.
DR Pfam; PF18565; Glyco_hydro2_C5; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KKY32074.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034680};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..880
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002544109"
FT DOMAIN 112..236
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 252..363
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 372..518
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 702..759
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 778..876
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
SQ SEQUENCE 880 AA; 95989 MW; B51747902C0AD874 CRC64;
MAFLTVPHKA LRLALIGLAA LGHSSANARS VTTRQQDAPP GLARERLNIN AGWRFARFES
NPDGLSYDQL KPWILPAANN FIKDTALHTE PPTGRPSNVS YAQASFDDGA WEALNLPHDW
AVKGPFYEGS DPPVGGNMGR LPIQGIGWYR RTIDIASADE DKTIYLEVDG AMSYATVWLN
GKLVGGWPYG YASFRLDLSP YIQSGENQLA IRLDQELDSS RWYPGAGIYR NVWLTKVNTV
HVGQWGTYIT AKDVSVEAAT LDLTIQVENA ATAGEASGIQ VVTDVHVLDT ATGQPGAKVG
QFPGTTVRVG AGSIESTNDS ITLDNPKLWG PRPSQEPNLH VAITRLYAEG QEIDTYQTRF
GVRSVSYAGD GLRINGERIY LQGVCQHHDL GSIGAAFNLV AAERQLQLLQ DMGSNAIRTS
HNPPAPEILD LADSLGIVVL DEIFDTWASH KTENDFAGLW EDWSEPDLRA FVRRDRNHPS
IWAWSYGNEI AEQEEGAAGA AAAQRLADIV REEDPTRQSS VGMNNAGPET PFVSVVDLIG
LNYQGEGKGN GGPTFENFRG EFPDKLIFST ESSSAVSSRG TYLFPVTPAN STTVLANGTG
ADPETRQVSA YELYAVPWGA SPDKVFDAQD RFPYVAGEFV WTGWDYIGEP TPYDGQSRSS
YFGIIDLAGF PKDRFYLYQS RWNPTIRNAH ILPHWNWPDR VGEVTPVHVF SSGDEAELFV
NGESQGRQAK AGYRFRWDDV IYQPGEVHVK TYKDGEEWAE ATVRTTGEAT QLRLSTYQNR
KTIAADGSDL SFVSVAVSDD NGDVVHTAEP AVTFSVTGGE IVSTDNGDPT DFTPFPSQER
NAFRGLALAI VRAPAGSSGP VTVTARADGL KTAEITLVVQ
//
