ID   A0A0N5CMU4_THECL        Unreviewed;       678 AA.
AC   A0A0N5CMU4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Trehalase {ECO:0000256|ARBA:ARBA00019905, ECO:0000256|RuleBase:RU361180};
DE            EC=3.2.1.28 {ECO:0000256|ARBA:ARBA00012757, ECO:0000256|RuleBase:RU361180};
DE   AltName: Full=Alpha-trehalose glucohydrolase {ECO:0000256|RuleBase:RU361180};
GN   ORFNames=TCLT_LOCUS1484 {ECO:0000313|EMBL:VDM96954.1};
OS   Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX   NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000148301-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TCLT_0000148301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDM96954.1, ECO:0000313|Proteomes:UP000276776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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         ECO:0000256|RuleBase:RU361180};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family.
CC       {ECO:0000256|ARBA:ARBA00005615, ECO:0000256|RuleBase:RU361180}.
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DR   EMBL; UYYF01000195; VDM96954.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N5CMU4; -.
DR   STRING; 103827.A0A0N5CMU4; -.
DR   WBParaSite; TCLT_0000148301-mRNA-1; TCLT_0000148301-mRNA-1; TCLT_0000148301.
DR   OMA; GSEMEYW; -.
DR   Proteomes; UP000046394; Unplaced.
DR   Proteomes; UP000276776; Unassembled WGS sequence.
DR   GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005991; P:trehalose metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR001661; Glyco_hydro_37.
DR   InterPro; IPR018232; Glyco_hydro_37_CS.
DR   PANTHER; PTHR23403; TREHALASE; 1.
DR   PANTHER; PTHR23403:SF1; TREHALASE; 1.
DR   Pfam; PF01204; Trehalase; 1.
DR   PRINTS; PR00744; GLHYDRLASE37.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS00927; TREHALASE_1; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361180};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276776}.
SQ   SEQUENCE   678 AA;  78987 MW;  C718D12B704942A7 CRC64;
     MQFATITKIT ILSIHLFITD TENSDASSSS YGYRIEKRAR RRAYNHTKND TIISVADFFI
     DEGDMIELLY DNDDSNTHNA NISLLRYLSQ DDVLGSTFEA PEFACDQNDT EAVQIYCHGD
     ILHVVMMLGL YKDSKTFVDK PLKKNPQDVV ADFRKRFSAT ITEEDRERVK EFIADNFGVE
     GEELDECELS DWKEEPEALL TIEDSALRQF ALEINYLWRN LCRTVKKEVK NNQQRYSLIY
     IPNEFIVPGG RFREYYYWDG YWIIKGLLIS GMHTTTRRMI ENFAYLIDKF GFIPNGGRVY
     YARRSQPPLF IPMVYEYYAA TKDDEFLAKV IEAMEKELLF WKTKRTITIK KNGRNYTVFR
     YRADSNMPRP ESYREDYETA ENVLPSQKRS LWRDIASAAE SGWDFSSRWF ADRKSLETTE
     TSSIAPVDLN AFMCWNMAIL AHIHGHLGNV TRREQLNVER QAFVDTFTDI FYDNSEKAWF
     DVNLQTGTKN YEAYPSIAVP LFAECYRRMD RRMMTDVLNT LQRNGLLNYP GGIPVSLMKD
     TNQQWDFPNG WANVNHMIVE GLRRSYHYRM QQKAFDIAQK WVKLNYHGYL KDGKMWEKYD
     VSKLYTQKAT GGEYEIQDGF GWTNGVALDL LVTYGKILSF HDQMKDGADG STLPTQSNYL
     VCLLLLIVPH LLLTSAMI
//