ID A0A232ENF0_9HYME Unreviewed; 508 AA.
AC A0A232ENF0;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Beta-glucosidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=TSAR_002989 {ECO:0000313|EMBL:OXU19852.1};
OS Trichomalopsis sarcophagae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU19852.1, ECO:0000313|Proteomes:UP000215335};
RN [1] {ECO:0000313|EMBL:OXU19852.1, ECO:0000313|Proteomes:UP000215335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alberta {ECO:0000313|EMBL:OXU19852.1,
RC ECO:0000313|Proteomes:UP000215335};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXU19852.1};
RX PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL Curr. Biol. 27:2007-2013(2017).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|RuleBase:RU003690}.
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:OXU19852.1}.
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DR EMBL; NNAY01003182; OXU19852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A232ENF0; -.
DR STRING; 543379.A0A232ENF0; -.
DR Proteomes; UP000215335; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000215335};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 406
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 508 AA; 58979 MW; 16284BDDFBAB8800 CRC64;
MCRKSLIKIY VFIFILIIIT LLVFNSSDKS ADIDYSFPDG FLIGAASSSY QVEGAWNTSG
KSESVWDNFV HTRPEKIADR STGDIACDSY HKYKEDIQLM KDIGINHYRF SLSWARILPT
GYSKDVNKEG LLYYHNILDE LEKHEIEPMV TIYHWDHPQI LERLGGWMNE LMADFFADYA
TVVFREFGHR VKIFSTINEP YIYCIVGYKT LRFAPGLNLS GWGEYQCVHN MLKAHAIAYH
IYDRDFRSQQ NGKIGIVMPC FQHYSKDKND LVSTNIAFEF QCGWTAHPIF SKDGDYPKIM
KQMIAKNSKL EGRKRSKLPT FSKEWIEYIK GTSDYFGLNH YTADLVEPSP KAAAFDSLND
DGLLYTVDEK WLSSQSKWLK VVPDGLGEIL RQIKNRYNNP PVYIMENGVS DPNIVNDTIR
IQYLYAYMKE MLVAMKRDNC NIKAYTIWSF LDSFEWDMGY VLVSLKDHFG LVSVDFNDPN
RKRTPKKSVS WLKSVLKSRK LQPIIDYT
//
