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Database: UniProt
Entry: A0A0V1A0C5_9BILA
LinkDB: A0A0V1A0C5_9BILA
Original site: A0A0V1A0C5_9BILA 
ID   A0A0V1A0C5_9BILA        Unreviewed;      2157 AA.
AC   A0A0V1A0C5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   13-SEP-2023, 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=T12_13994 {ECO:0000313|EMBL:KRY18315.1};
OS   Trichinella patagoniensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY18315.1, ECO:0000313|Proteomes:UP000054783};
RN   [1] {ECO:0000313|EMBL:KRY18315.1, ECO:0000313|Proteomes:UP000054783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS2496 {ECO:0000313|EMBL:KRY18315.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) 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|RuleBase:RU361180};
CC   -!- SIMILARITY: Belongs to the CBF/MAK21 family.
CC       {ECO:0000256|ARBA:ARBA00007797}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family.
CC       {ECO:0000256|ARBA:ARBA00005615, ECO:0000256|RuleBase:RU361180}.
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:KRY18315.1}.
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DR   EMBL; JYDQ01000048; KRY18315.1; -; Genomic_DNA.
DR   STRING; 990121.A0A0V1A0C5; -.
DR   Proteomes; UP000054783; Unassembled WGS sequence.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0005991; P:trehalose metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.20.25.10; -; 2.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR005612; CCAAT-binding_factor.
DR   InterPro; IPR019761; DNA-dir_RNA_pol-M_15_CS.
DR   InterPro; IPR001529; DNA-dir_RNA_pol_M/15kDasu.
DR   InterPro; IPR001661; Glyco_hydro_37.
DR   PANTHER; PTHR23403; TREHALASE; 1.
DR   PANTHER; PTHR23403:SF12; TREHALASE; 1.
DR   Pfam; PF03914; CBF; 1.
DR   Pfam; PF02150; RNA_POL_M_15KD; 1.
DR   Pfam; PF01204; Trehalase; 1.
DR   PRINTS; PR00744; GLHYDRLASE37.
DR   SMART; SM00661; RPOL9; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 2.
DR   PROSITE; PS01030; RNA_POL_M_15KD; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361180};
KW   Hydrolase {ECO:0000256|RuleBase:RU361180};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        2059..2081
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          488..542
FT                   /note="DNA-directed RNA polymerase M/15kDa subunit"
FT                   /evidence="ECO:0000259|SMART:SM00661"
FT   REGION          1246..1303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1780..1817
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1246..1268
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1269..1303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1800..1817
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2157 AA;  248465 MW;  154DFE4D93CDF410 CRC64;
     MWTFSEHTYY EIKKHFKFAG YFTDFRFNVE PGLAWFARRN IRFASEIKKM PQHSILMFRL
     FCLFSLELLR SVMGDKPVTP QGSFFRVYSQ DRQYRDLAMT GDKASKLACG PTKRAFDHDV
     VWATDHPAAG PLLDELVDAM VYAKCDVNVP DDANMSVMMT LRAVNMEKPQ IKQDAASGMR
     SSALDPERMK SVLQAMQKSG AQGVSQDNID RALQLIELAL KEKRAISIHE MEEVLRLVEF
     NVFIGADGLK QMFERLVNDK TLTEGQANGI LQPLLAKAAS KADGKLPMQE IIFFTTLPTL
     GWCMSTPTNL HYLFKVMQRS GAQREAKDNI DRALRMIELV VKEKREISIQ EMEEILCMVE
     SNVFIGIDGL NQMFEYLVNK KTLTDAEAIG ILPSLLAKAA AKAQKKIPLQ NVREALKNFM
     TVKEYFFFIF IFYSIYQESS LSFQNYRTNI KSQCNYSTTV RLYSVEQLNK LKVEQKAHVD
     TLKHPGIIFC PECNNILYPK EDKSRRCLLY ACRNCSYVTD DIVSVCVYTN KLRREIDELA
     QVNVDVIYDP TLPKTDDHSC PLCNNSEAVF FQSQNTKAEL LLLTYCKVVR NLICQLFGHG
     AWLRGKIECV TIANALCRTS FSGTLKVERI VAAVHCCRWV SGAFGFEKNT KPNNKVSLDK
     MMYYVVSLLS QIYCQGPILD AVQTAHLFPD SKYFVDMALK KDPITTLQNF ISLGDRVKDK
     AVLRAFVDEH FDPPGTELET CFPEDWKPSP KSFNVIKDYE FRRWAVALNR IWKELCRRVK
     SKVFEHQELY SLLYVPNPFI IPGGRFREFY YWDTFWIAKG LIASEMFTTL KGMIRNLGYM
     VENHGFVPNG GRVYYLFRSQ PPLLIPMVYD YYLATGDIDF LQEMLPLLEQ EYGFWLLHRG
     MTFGDDSNNY MKLFQYKAEM KMPRPESYRE DLELVQNLTD DHAREFVWAQ IVSGAETGWD
     FSSRWFSHTG PEAFTLRSIR TWSIIPVDLN AFMCMNTKLL ANLYEMAGNV TKVLLYQARF
     EQAKAAMKQI HWNEQDGIWY DYDLETKRHV DVYYISNVLP LYAKCYDDED VPSRVYNYLK
     TVGALNSTRG VPTSFIQSDQ QWDSANAWPP MVHMLLEGLR TSGDPEIIEV AKELAIQWLR
     SSYDAFLKTN SMFEKYNVSS TAGEMPFGSG GEYEVQTGFG WTNGVILDLL VKYGDVITAQ
     DATTGTINYW KYAAYVVFVM KSELKQDEHA LKEEILGFMN KIGLKKDGKN KNSSRISTPV
     RRETKRTFNN NGKLIFSGDS AWNNNSSGSK NKQQQQQQQQ QRANKLLPTK IKTEDLNEHP
     VSESSVQRWF DAKFTDVVGS QPLSEHSLMK MEAYAKQLFQ NQAVNYEKET MNKKNNSNQL
     RWMNSVASGG TLSDRVAALG MLVQQSPLHN LKHLDTLLNK VTKKNRHEAL IAADVAKDLF
     IEELLPDRKL IPFKSRPYVE IENTKGQSKA AVDRKLLLWQ FESELKMKYQ QFVHALEQLC
     HDTVEAVRLK GCILLVDLLI AKAEQEQFIL SSLVNKLGDQ SVKVATQVVK LIGRLFLAHP
     NMKVVVVDEL EKLIYRKNIT PCAQFYAICA LLKVPLNRNN DEDLACKILN VYFDLFKIVI
     QSDVENQRLL RHLLLGTNVA FSYSKGKFDR ISEEVDTLYK IAATSSLYIN LQALALLFQV
     LDVKAEISDR FYRSLYRTML VPELLSSSRC HAMFFHLLFK SMSQDFSDQR IRAFVKRLLQ
     VCLMAPAPFI CAALLVISQA LHGRLKRFVA IADQWVEDDH EEQEKVDDEE EKEIGNGKKK
     QTSTESNNTN DNKQNANNIY GNVYGSREYN IAGREPLHAN ADRESLVELL LLRNHYHPTV
     AVFAENLLKG NHINYSGNPL DDFSLMHFLD RFVFKNPKKS ISENVEEKNT EKRGYKRKIY
     DPWSLRSLPV TSSAYALHHK SHVPPDEKYL HSFMTNANVK RAEEQLSEES DDESVNSEEF
     EILLDKMKPG SKNEEFLVDF SRQVRITVSK FVRRYNDVPV KLETNDDDGG RNVLKIRMIL
     IIHQILLEMN PILKRVDQSL MILQPLQVTM MIVLTAAYWM MMMMMQQLLR KSSVKFWKMT
     MKKMRRKSTT VNEKRTRNFK KFVNDDGVDV DEQADVFFSL SVFIKIYFGK IAGFWML
//
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