UniProt: A0A0V0S0Q4

Database: UniProt
Entry: A0A0V0S0Q4_9BILA

LinkDB:  A0A0V0S0Q4_9BILA 
Original site:  A0A0V0S0Q4_9BILA

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (18)   
   InterPro (10)   
   Pfam (4)   
   PROSITE (2)   
   SMART (2)   
All databases (28)   

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ID   A0A0V0S0Q4_9BILA        Unreviewed;      2692 AA.
AC   A0A0V0S0Q4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   08-NOV-2023, entry version 32.
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=T07_3637 {ECO:0000313|EMBL:KRX20349.1};
OS   Trichinella nelsoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX20349.1, ECO:0000313|Proteomes:UP000054630};
RN   [1] {ECO:0000313|EMBL:KRX20349.1, ECO:0000313|Proteomes:UP000054630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS37 {ECO:0000313|EMBL:KRX20349.1};
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the CBF/MAK21 family.
CC       {ECO:0000256|ARBA:ARBA00007797}.
CC   -!- SIMILARITY: Belongs to the NIP3 family.
CC       {ECO:0000256|ARBA:ARBA00007710}.
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:KRX20349.1}.
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DR   EMBL; JYDL01000050; KRX20349.1; -; Genomic_DNA.
DR   Proteomes; UP000054630; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005740; C:mitochondrial envelope; IEA:InterPro.
DR   GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042802; F:identical protein binding; IEA:UniProt.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:InterPro.
DR   GO; GO:0019222; P:regulation of metabolic process; IEA:UniProt.
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   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR010548; BNIP3.
DR   InterPro; IPR005612; CCAAT-binding_factor.
DR   InterPro; IPR001529; DNA-dir_RNA_pol_M/15kDasu.
DR   InterPro; IPR001661; Glyco_hydro_37.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR23403; TREHALASE; 1.
DR   PANTHER; PTHR23403:SF12; TREHALASE; 1.
DR   Pfam; PF06553; BNIP3; 1.
DR   Pfam; PF03914; CBF; 1.
DR   Pfam; PF01204; Trehalase; 1.
DR   Pfam; PF00400; WD40; 1.
DR   PRINTS; PR00744; GLHYDRLASE37.
DR   SMART; SM00661; RPOL9; 1.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361180};
KW   Hydrolase {ECO:0000256|RuleBase:RU361180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT   TRANSMEM        2657..2679
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REPEAT          125..160
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   DOMAIN          993..1041
FT                   /note="DNA-directed RNA polymerase M/15kDa subunit"
FT                   /evidence="ECO:0000259|SMART:SM00661"
FT   REGION          459..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1674..1719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2194..2231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..503
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1678..1695
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1696..1719
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2215..2231
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2692 AA;  307758 MW;  A794987E80CA3E2F CRC64;
     MMFYPKEDVR FVAVRKPSDK SILRRLSSAY YYHEPHSIYR CRFNPSIDLW NYLGFCDEAG
     FFYLYDTMFF EQKNDPKLLF KLQLHRNAVC DFAWHPCGRG EVLTGSADER IILTDCNIAK
     AVQCFHGHSY SIRSLSWCAE NTNLFASGGR DGSLRIWDVR LRAGCISTIA KAHYFGDFLT
     ASSSTLCNQK RTKTNLRKIL MSDVRRSGTS LNVPVTGVHF HNQHYVLSGA YTNTGIRIWD
     LRKLLQANKA VAAVDIWPYP SPRNSNYSRY GYTTFCVDSS RSLLFVPCTD NTVYQYSLSS
     FNPKPIARHT GVSINTYYVQ CAVCPYAPYL LCGSSNNKAM IWNINESGDP QFSLNDFEGR
     DANSVTWNHY GQLVTCCDPP SWRIWTVYSE KQQQQLDMER RNLVLRIQEN QRLESLQSER
     VQQQQQPLEE PIWFASQARS PPSRMQALAP VQSSPMRRYL HQRNKRPASS SPLSTAALDV
     NQPGPSRPVS SSRAPTTTPA RKRVRTTNTY YEIKKHFKFA ASASTLNLGL HGLHDGISDS
     LVKNGKNAAA QLFCLFPLEL FRSVMGDKPV TPPGSFFRVY SQDRQYRDLA MTGDKASKLA
     CGPTKRAFDH DVVWATDHPA AGPLLDELVD AMVYAKCDVN VPDDANMSVM MTLRSVNMEK
     PQIKQDAASG MRSSALDPER MKSVLQAMQK SGAQGVSQDN IDRALQLIEL ALKEKRAISI
     HEMEEVLRLV EFNVFIGADG LKQMFERLVN DKTLTEGQAN GILQPLLAKA ASKADGKLPM
     QEIIFFTTLP ALEWCMSTPT DLHYLFKVMR RSGAQRSRKE NIDRALRMID LVVKEKREIS
     IQEMEEILCI VESNVFIGID GLKRMFEHLV NKKTLTDAEA IGILPSLLAK AAAKAQKKIP
     LQNVREALKN FMTVIFTTLP ALERCMSTAT NLHYLFKITV QISNHSVIIR PQCGCILSNN
     STNLSDLLYY FNARSLCKKL KKCQIKLLSI APNNILYPKE DKSRRCLLYA CRNCSYVTDD
     IVSVCVYTNK LRREIDELAQ VNVDVIYDPT LPKTDDHSCP LCNNSEAVFF QSQNTKAEPN
     NKVSLDKMMY YVVSLLSQIY CQGPILDAVQ TAHLFPDSKY FVDMALKKDP ITTLQNFISL
     GDRVKDKAVL RAFVDEHFDP PGTELETCFP EDWKPSPKSF NVIKDYEFRR WAVALNRIWK
     ELCRRVKSKV FEHQELYSLL YVPNPFIIPG GRFREFYYWD TFWIAKGLIA SEMFTTLKGM
     IRNLGYMVEN HGFVPNGGRV YYLFRSQPPL LIPMVYDYYL ATGDIDFLQE MLPLLEQEYS
     FWLLHRGMTF GDDSNNYMKL FQYKAEMKMP RPESYREDLE LVQNLTDDHA REFVWAQIVS
     GAETGWDFSS RWFSHTGPEA FTLRSIRTWS IIPVDLNAFM CMNTKLLANL YEMAGNVTKV
     LLYQARFEQA KAAMKQIHWN EQDGIWYDYD LETKRHVDVY YISNVLPLYA KCYDDEDVPS
     RVYNYLKTVG ALNSTRGVPT SFIQSDQQWD SANAWPPMVH MLLEGLRTSG DPEIIEVAKD
     LAIQWLRSSY DAFLKTNSMF EKYNVSSTAG EMPFGSGGEY EVQTGFGWTN GVILDLLVKY
     GDVITAQDAT TGTINYWKYA TYVVFVMKSE LKQDEHALKE EILGFMNKIG LNRDGKNKNS
     SRISKPVRRE TKPDDSAWNN NSSGSKNKQH QQQQQSGNKL LPTKIKTEDL NEHPVSESSV
     QRWYDAKFTD VVGSQPLSEH SLMKMGTYAK QLFQNQAVNY EKETMNKKNN SNQLRWMNSV
     ASGGTLSDRV AALGMLVQQS PLHNLKHLDT LLNKVTKKNR HEALIAADVA KDLFIEELLP
     DRKLIPFKSR PYVEIENTKG QSKATVDRKL LLWQFESELK MKYQQFLHAL EQLCHDTVEA
     VRLKGCILLV DLLIAKAEQE QFILSSLVNK LGDQSVKVAT QVVKLIGRLF VAHPNMKVVV
     VDELEKLIYR KNITPCAQFY AICALLKVPL NRNNDEDLAC KILNVYFDLF KIVIQSDVEN
     QRLLRHLLLG TNVAFSYSKG KFDRISEEVD TLYKIAATSS LYINLQALAL LFQVLDVKAE
     ISDRFYRSLY RTMLVPELLS SSRCHAMFFH LLFKSMSQDF SDQRIRAFVK RLLQVCLMAP
     APFICAALLV ISQALHGRLK RFIAITDQWV EDDHEEQEKV DDEEEKEIEN GKKKQTSTES
     NNTNDNKQNA NNIYGNVYGS REYNIAGREP LHANADRESL VELLLLRNHY HPTVAVFAEN
     LLKGNHINYS GNPLDDFSLM HFLDRFVFKN PKKSISENVE EKNTEKRGYK RKIYDPWSLR
     SLPVTSSAYA LHHKSHVPPD EKYLHSFMTN ENVKRAEEQL SEESDDESVN SEEFEILLDK
     MKPGSKNEEF LILLEMNPIL KRVDQSLILQ PLQVTMMIVL TAAYWMMTMQ QLLRKSSVKF
     WKMTMKKMRR KSTTVNEKRT RNFKKFVNDD GVDVDEQADA FFSLSMSSPR GTIVVNEMDV
     ADADSWVELS HDSECGSSIT FLTDPSGAHG SPHKYTPPGG QTSPVLQFDG DLERVKFQLC
     RQFSNIQGGK SAWLSDWSSR PEVVPPLQYR RSGTIVRTPP NSPFGSSEEE TSDQSKPWFS
     LRHSRFVRHD WFSLEVLSVY ILGNVLSFLF GVCIGLAICR KGRSCCGTHF LP
//

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