ID A0A183CIN9_GLOPA Unreviewed; 687 AA.
AC A0A183CIN9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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};
OS Globodera pallida (Potato cyst nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC Globodera.
OX NCBI_TaxID=36090 {ECO:0000313|Proteomes:UP000050741, ECO:0000313|WBParaSite:GPLIN_001274500};
RN [1] {ECO:0000313|Proteomes:UP000050741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA Aslett M.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000050741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA Cotton J.A., Lilley C.J., Jones L.M., Kikuchi T., Reid A.J., Thorpe P.,
RA Tsai I.J., Beasley H., Blok V., Cock P.J.A., Van den Akker S.E.,
RA Holroyd N., Hunt M., Mantelin S., Naghra H., Pain A., Palomares-Rius J.E.,
RA Zarowiecki M., Berriman M., Jones J.T., Urwin P.E.;
RT "The genome and life-stage specific transcriptomes of Globodera pallida
RT elucidate key aspects of plant parasitism by a cyst nematode.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:GPLIN_001274500}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
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 AlphaFoldDB; A0A183CIN9; -.
DR WBParaSite; GPLIN_001274500; GPLIN_001274500; GPLIN_001274500.
DR Proteomes; UP000050741; Unassembled WGS sequence.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-EC.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0005991; P:trehalose metabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR001661; Glyco_hydro_37.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR PANTHER; PTHR23403; TREHALASE; 1.
DR PANTHER; PTHR23403:SF1; TREHALASE; 1.
DR Pfam; PF00112; Peptidase_C1; 2.
DR Pfam; PF01204; Trehalase; 1.
DR PRINTS; PR00744; GLHYDRLASE37.
DR SUPFAM; SSF54001; Cysteine proteinases; 2.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361180};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..687
FT /note="Trehalase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008147667"
FT DOMAIN 392..472
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00112"
FT DOMAIN 611..658
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00112"
SQ SEQUENCE 687 AA; 77829 MW; F5DEA392F8CC4231 CRC64;
MPKNAFIFFL LLPFLPLLLP PAATAKTFYL KTQFEKNDGI VEKDVLNCSL NGIDLTELGL
ERNCDKAKSR AYHGKYQLFM EDFKSLFYKK EHGIWYDYNM DSGTLNEAFY GSAAMPLFVR
CYDTIDLGTA ERMFQRLELF DKQHKLLEHP FGVPVSITAN SSQQWDFPNI LPPSQHMLIE
GLRRSSNRRM EEKAKEMAQK WVFANYNRFQ NCLRQMWEKM TADTGTPGSG GEYNAQTGFG
WTNGAMLDLL VTYGDVLKLK GVPEIRCGLK DLVQEPEQYP NNVSEYRAQR FMEAQKKVDE
INRSQNDWTA VVYERFALMT EQQLRRLCGS KTENENDQPN LQFKQAVAPI DYGDMPKAFD
ARQKWPECAD FIGTTTDQSW NVPGRFDTSK RVGSSEDCGS CWAVSAASTF TDRICIARLK
KGIKTDSNDP RAYVSAQYTL ECSLKADGCK SGFADEAWKL YLKNGTVSGT DNAMLSGCKP
YIIPSMNVQC PVMGFGWTNG AMLDLLVTYG DVLKLEGVPE IRCGLKDLVQ EPEQYPNNVS
EYRAQRFMEA QKKVDELNRS KNDWTAVVYE RFALMTDEQL KQLTGSIIRN RPRKPKLQFK
QAVAPIDYGD LPETFDARQK WPECADLIGT TTDQDGCGSC WAVSAAATFT ARICVARLKK
GIITDSKDPR AYVSAQYTME CAPETNG
//
