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Database: UniProt
Entry: A0A397HU58_9EURO
LinkDB: A0A397HU58_9EURO
Original site: A0A397HU58_9EURO 
ID   A0A397HU58_9EURO        Unreviewed;       486 AA.
AC   A0A397HU58;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=Glycoside hydrolase family 5 domain-containing protein {ECO:0000259|Pfam:PF00150};
GN   ORFNames=CDV56_106810 {ECO:0000313|EMBL:RHZ66735.1};
OS   Aspergillus thermomutatus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ66735.1, ECO:0000313|Proteomes:UP000215305};
RN   [1] {ECO:0000313|EMBL:RHZ66735.1, ECO:0000313|Proteomes:UP000215305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ66735.1,
RC   ECO:0000313|Proteomes:UP000215305};
RA   Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA   Perkins V., De Repentigny L., Dufresne S.F.;
RT   "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT   (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT   aspirate.";
RL   Submitted (AUG-2018) 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:RHZ66735.1}.
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DR   EMBL; NKHU02000010; RHZ66735.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397HU58; -.
DR   STRING; 41047.A0A397HU58; -.
DR   VEuPathDB; FungiDB:CDV56_106810; -.
DR   OrthoDB; 1693706at2759; -.
DR   Proteomes; UP000215305; 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:UP000215305}.
FT   DOMAIN          89..349
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
SQ   SEQUENCE   486 AA;  55625 MW;  5EE0204B876D765C CRC64;
     MSPHANDSTT HTNPVFKGSL LHVSGTSIVD ACGNPVVLKG AALGGYLNME NFITGYSGHE
     HEHRAQMSAV LGPKKAQFFF DRLIHYSFTE SDAAFYASLG LNCLRLPFNY RHFIDDTNPT
     VLKKSGFALL DRIVGICRQF NLYVILDLHA VPGGQNQDWH SDSGLARALF WDFKVFQDQM
     VELWVEIAKH YAGDPVIAGY NPLNEPADPE HTRLIAWYER VERAIRAVDP DHILFVDGNT
     YAMDFSLFAA VLPNTVYACH DYAKMGFPGQ EVYAGTDEQK AKLRRQFERK VRFMRERGVP
     IWNGEFGPVY PDAREDGAEA TNKARLGVLR EQLRIYGESR ISWSIWLYKD IGYQGMVYVD
     PESPYRKLIA PFVAKKQRLG LDFWGCTDKD GVKDVYEPFL RGLREMVGAE LLQKKYPPVW
     TFDRQVERVV RECLLSEYLG WEFAELFRGK TEEELEELAR SFSFEKCVKR DGLNRVLQED
     AGLLKR
//
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