ID S8BJD5_DACHA Unreviewed; 502 AA.
AC S8BJD5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Glycoside hydrolase family 5 domain-containing protein {ECO:0000259|Pfam:PF00150};
GN ORFNames=H072_6818 {ECO:0000313|EMBL:EPS39403.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS39403.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS39403.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS39403.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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:EPS39403.1}.
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DR EMBL; AQGS01000472; EPS39403.1; -; Genomic_DNA.
DR RefSeq; XP_011112597.1; XM_011114295.1.
DR AlphaFoldDB; S8BJD5; -.
DR STRING; 1284197.S8BJD5; -.
DR eggNOG; ENOG502RDG8; Eukaryota.
DR HOGENOM; CLU_031875_1_1_1; -.
DR OMA; ECLVSEY; -.
DR OrthoDB; 1693706at2759; -.
DR Proteomes; UP000015100; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR PANTHER; PTHR31297:SF13; PUTATIVE-RELATED; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153};
KW Reference proteome {ECO:0000313|Proteomes:UP000015100}.
FT DOMAIN 100..365
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
SQ SEQUENCE 502 AA; 57628 MW; 9A4E715EBA5C0410 CRC64;
MTQVATELQQ QLLLKLSAPQ SNNVSGSKCK LLKVSGTSIV DPDGNVVVLK GAAIAGHLNM
ENFITGYSGH EHELRAAMIE VLGEEKATFF FDKLIENFFT ETDAQFYASL GLNCIRVPFN
YRHFIDDANP YTLKPEGFAQ LDRVVNICAK YDIYVILDLH AAPGGQNQDW HSDSGLNKAM
FWEYKVFQDQ AINLWTAIAK HYAGNPVVAG YNPLNEPADP KHTRLYEFYE RVEKAIRSVD
IDHMLFVDGN TYAMDFSHFP TDKVLPNTVY ACHDYAMMGF PIPGQPLYSG TQEQKERLRS
QFERKVEYMR NAGIPIWNGE FGPVYADPLR DPNADTVNNA RYEVLKEQLR IYQETGVSWS
IWLYKDIGYQ GMTYVHPESP YMKLIRGFVE KKGKLALDFW GFSEKEEVQG IYQPFIDGLK
ATVPEHIRKS KYPNIWQFDR QVERSVRECL MSEYLVKEFA ELFEGKTVEE LEELAASFKL
ENCVRREGLN DVLRKDAERR TA
//
