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Database: UniProt
Entry: A0A0V1A1Y6_9BILA
LinkDB: A0A0V1A1Y6_9BILA
Original site: A0A0V1A1Y6_9BILA 
ID   A0A0V1A1Y6_9BILA        Unreviewed;      2041 AA.
AC   A0A0V1A1Y6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   13-SEP-2023, entry version 27.
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:KRY18313.1};
OS   Trichinella patagoniensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY18313.1, ECO:0000313|Proteomes:UP000054783};
RN   [1] {ECO:0000313|EMBL:KRY18313.1, ECO:0000313|Proteomes:UP000054783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS2496 {ECO:0000313|EMBL:KRY18313.1};
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:KRY18313.1}.
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DR   EMBL; JYDQ01000048; KRY18313.1; -; Genomic_DNA.
DR   Proteomes; UP000054783; Unassembled WGS sequence.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
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   Reference proteome {ECO:0000313|Proteomes:UP000054783}.
FT   DOMAIN          488..542
FT                   /note="DNA-directed RNA polymerase M/15kDa subunit"
FT                   /evidence="ECO:0000259|SMART:SM00661"
FT   REGION          1174..1231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1708..1745
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1938..2041
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1174..1196
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1197..1231
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1728..1745
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1985..2011
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2022..2041
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2041 AA;  234921 MW;  FD947D562C300656 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 FQSQNTKAEP NNKVSLDKMM YYVVSLLSQI
     YCQGPILDAV QTAHLFPDSK YFVDMALKKD PITTLQNFIS LGDRVKDKAV LRAFVDEHFD
     PPGTELETCF PEDWKPSPKS FNVIKDYEFR RWAVALNRIW KELCRRVKSK VFEHQELYSL
     LYVPNPFIIP GGRFREFYYW DTFWIAKGLI ASEMFTTLKG MIRNLGYMVE NHGFVPNGGR
     VYYLFRSQPP LLIPMVYDYY LATGDIDFLQ EMLPLLEQEY GFWLLHRGMT FGDDSNNYMK
     LFQYKAEMKM PRPESYREDL ELVQNLTDDH AREFVWAQIV SGAETGWDFS SRWFSHTGPE
     AFTLRSIRTW SIIPVDLNAF MCMNTKLLAN LYEMAGNVTK VLLYQARFEQ AKAAMKQIHW
     NEQDGIWYDY DLETKRHVDV YYISNVLPLY AKCYDDEDVP SRVYNYLKTV GALNSTRGVP
     TSFIQSDQQW DSANAWPPMV HMLLEGLRTS GDPEIIEVAK ELAIQWLRSS YDAFLKTNSM
     FEKYNVSSTA GEMPFGSGGE YEVQTGFGWT NGVILDLLVK YGDVITAQDA TTGTINYWKY
     AAYVVFVMKS ELKQDEHALK EEILGFMNKI GLKKDGKNKN SSRISTPVRR ETKRTFNNNG
     KLIFSGDSAW NNNSSGSKNK QQQQQQQQQR ANKLLPTKIK TEDLNEHPVS ESSVQRWFDA
     KFTDVVGSQP LSEHSLMKME AYAKQLFQNQ AVNYEKETMN KKNNSNQLRW MNSVASGGTL
     SDRVAALGML VQQSPLHNLK HLDTLLNKVT KKNRHEALIA ADVAKDLFIE ELLPDRKLIP
     FKSRPYVEIE NTKGQSKAAV DRKLLLWQFE SELKMKYQQF VHALEQLCHD TVEAVRLKGC
     ILLVDLLIAK AEQEQFILSS LVNKLGDQSV KVATQVVKLI GRLFLAHPNM KVVVVDELEK
     LIYRKNITPC AQFYAICALL KVPLNRNNDE DLACKILNVY FDLFKIVIQS DVENQRLLRH
     LLLGTNVAFS YSKGKFDRIS EEVDTLYKIA ATSSLYINLQ ALALLFQVLD VKAEISDRFY
     RSLYRTMLVP ELLSSSRCHA MFFHLLFKSM SQDFSDQRIR AFVKRLLQVC LMAPAPFICA
     ALLVISQALH GRLKRFVAIA DQWVEDDHEE QEKVDDEEEK EIGNGKKKQT STESNNTNDN
     KQNANNIYGN VYGSREYNIA GREPLHANAD RESLVELLLL RNHYHPTVAV FAENLLKGNH
     INYSGNPLDD FSLMHFLDRF VFKNPKKSIS ENVEEKNTEK RGYKRKIYDP WSLRSLPVTS
     SAYALHHKSH VPPDEKYLHS FMTNANVKRA EEQLSEESDD ESVNSEEFEI LLGKKLDFKK
     QNFWSTFLGK FEIGNKRRRR RSKRSEDSDD SDNPSDSSGD ESDFEAGRSK LDDTAALTGD
     NDDSTDGGVL DDDDDDATTA AEEFGEILEN DDEEDEKKKH DRKRKAYKKF QKVRQRRRRR
     R
//
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