ID   A0A3A2ZJN6_9EURO        Unreviewed;      1005 AA.
AC   A0A3A2ZJN6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=alpha,alpha-trehalase {ECO:0000256|ARBA:ARBA00012757};
DE            EC=3.2.1.28 {ECO:0000256|ARBA:ARBA00012757};
GN   ORFNames=PHISCL_05156 {ECO:0000313|EMBL:RJE22513.1};
OS   Aspergillus sclerotialis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Polypaecilum.
OX   NCBI_TaxID=2070753 {ECO:0000313|EMBL:RJE22513.1, ECO:0000313|Proteomes:UP000266188};
RN   [1] {ECO:0000313|Proteomes:UP000266188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 366.77 {ECO:0000313|Proteomes:UP000266188};
RA   Tafer H., Lopandic K.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-
CC         glucose; Xref=Rhea:RHEA:32675, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903,
CC         ChEBI:CHEBI:16551, ChEBI:CHEBI:17925; EC=3.2.1.28;
CC         Evidence={ECO:0000256|ARBA:ARBA00001576};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family.
CC       {ECO:0000256|ARBA:ARBA00006768}.
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:RJE22513.1}.
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DR   EMBL; MVGC01000165; RJE22513.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A2ZJN6; -.
DR   STRING; 2070753.A0A3A2ZJN6; -.
DR   Proteomes; UP000266188; Unassembled WGS sequence.
DR   GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.70.98.40; Glycoside hydrolase, family 65, N-terminal domain; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR005195; Glyco_hydro_65_M.
DR   InterPro; IPR005196; Glyco_hydro_65_N.
DR   InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR   PANTHER; PTHR11051; GLYCOSYL HYDROLASE-RELATED; 1.
DR   PANTHER; PTHR11051:SF8; PROTEIN-GLUCOSYLGALACTOSYLHYDROXYLYSINE GLUCOSIDASE; 1.
DR   Pfam; PF03632; Glyco_hydro_65m; 1.
DR   Pfam; PF03636; Glyco_hydro_65N; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000266188};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1005
FT                   /note="alpha,alpha-trehalase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017201926"
FT   DOMAIN          67..316
FT                   /note="Glycoside hydrolase family 65 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03636"
FT   DOMAIN          410..623
FT                   /note="Glycoside hydrolase family 65 central catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03632"
SQ   SEQUENCE   1005 AA;  109211 MW;  2D6E00E645E7C259 CRC64;
     MKHTASTKVL AAAIAVLGAT LLEQVSANGP KDSKHHTRFA GVTWDNDAWT LTSSVVNNSD
     WHAQSFVSNG YIGSSFASSG PFPYIYSTDG GQWWLHQYGT FGTVAGFFDR EPITLGAVYP
     GFVQYGWDSV ISGLPCWGPL VLDLGNGVYL DGSVNSDELS NVALRQDFKK GSANYAYTWT
     PSSLDGFSVD VSFIAVADKL HPNRAYVQLN LTSSSPMDAT VVNILDGLSA RRTDFHAKGV
     EGDYLYSAVS PNGVGNITGW VYATLDGTGV DMSTLKPAAE RPYINNHSST IAQSVDVSLQ
     PHKTISLTKY VGIASNDAFD NPSHTAYSEM MEGKKSGFAT AFQQHVREWA AVLPEDSVTS
     FADPVTGETP EHLIDRQITS VVAAAMLLMN TVSENALEYV NNAPINVWGI PVCGLTADCY
     AGQIFWDMDI FMGPYIAATH PFEAKQIALP RTTLYEQAAA NIQAASRSPT QGNTDFSPQA
     VIYPWSTGRD GNCTATGPCW DFEYHINGDI VKGFTNYWAA TGDDDFFESS LLPITNSVAA
     LFSDLIQFDS STNKWVLMNM TDPDEYAMNV NNGAFTMALI QWTLRSANFF NGLYGKSENS
     TWDKQASALE IPFNEDQGIT LEYTGMNGSI SVKQADVILR TYPLDNHENY SIENQLADLD
     YYAAKQSQDG PGMTYAIFSI GASALKPPGC AAYTYDKYAW GPYVRAPWFQ FSEQIDDFGS
     DLLPAFPFLT GFGGFLQVDL MGYLGLRYGT SFHITISPNL PPQIPYMRLP IFYFHGWPIQ
     AEMNQTHTAL VRLGTPLSTA NMTFADSGIT VRVRGGQSDH KSFELSPNGI LVLENDDSSK
     NLAIDNNILQ CRPIIASNGT VLPGQFVEGA IDGSNSTSWQ AVSCQSINSI TADLSGDAFA
     PVKSIHINWA TAVASNFSVI FHNTSDHTAG VDSKTIDVPD VKISIPYNPS EQSIVRHYLG
     NTTTIDLTGK NVWTGRYATL LVTGNQGDMS RSAPGASVAE WAVLV
//