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CAZyme Information: MGYG000001693_00308
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Halorubrum lipolyticum | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Archaea; Halobacteriota; Halobacteria; Halobacteriales; Haloferacaceae; Halorubrum; Halorubrum lipolyticum | |||||||||||
| CAZyme ID | MGYG000001693_00308 | |||||||||||
| CAZy Family | GH15 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 250; End: 4998 Strand: - | |||||||||||
Full Sequence Download help
| MRLRTALTEH ERRRGERYPA ERPTTAGAFT GDDGRLVHVG PNGTVHDCSY SLSGVGGADR | 60 |
| LRMGITAGRG VRWFDDLTTT RQHYDGDTPL VETEYDAGRY TIHQFDLVVS DTHLTHVELR | 120 |
| GAPPADAELV AACAFSPDMV EGRVGNLVHE EAGPEAGSVV EVYHRTEHDF LTASTGLSAA | 180 |
| HGQRLRTVSE LLGEDGEGFP HRGEIDQRED SRLTPDVVVR APFERDGRTE RVTLASRAVL | 240 |
| DRRETRETGD DAMDAISDGP DRQRRIDELS RIATAYPDAD DLREAAEGRG PTVPGDVPRR | 300 |
| SVVASDLRAL DLLTAESGAR IAAPEFDPFY STSGGYGYTW FRDEAEASLA LLGASDELGL | 360 |
| DADEKLLATA SFFCRTQDAD GSWPHRVWAD SGKVAPGWAN ARIEGANGTA GPNDQLDQPA | 420 |
| SVVAFLARLR RTADLPAEWR DRVDDTITDA LAFLRETTED DGLPRRCQNC WENALGRFTH | 480 |
| TGATYLRAFA AAARAPLPED VRADAAAAAD AALAGLNDRW NPDTERFPQR ASAESRDDRP | 540 |
| DASTFALASA ATEYAALRDE RDEIGADGGS TPAAAPTAEV DFDAFLDRVT THVLTTIGEL | 600 |
| RRETADVEGL VRFTGDDWRT AEQGAAKVWS IATLWGSTAA AELGGLVGER GGDANELFGA | 660 |
| ARDLYALCEP DGPFVNDAGL IAEQAFDDGD LDGATPIAWS HALRIDATVT LARHGALPVP | 720 |
| HDEPRGPDEA PHWTTGRKFG VGTPADHEAA DPVPVWFTLT EGALTEARFP RIDVMNVRTF | 780 |
| DFLVADPETG YTVRTFDETS HVTATETVER TTEPTVDDAL AYTQTIRETG DEHGHRWTLT | 840 |
| VEYAVDTDGD AILADVTFEG SREYDVYALV DTTVTNVGTN DRGDRVSGSD GYHLLARNDD | 900 |
| AAERDPGKLV DDDGDSFEVA LALDSAGGFD WASALAAGGD EANALFADGD RDEGTETATG | 960 |
| NVVLAGLVGS GTEVSDAVAL GFAENADTAA ALGEARGAVS RGFADISESY VDTWRTWLAD | 1020 |
| REFPASVTGD ADLETQYRFA LMTLAAVEDK RHDGAGIASP SVPWGETEYA AEDRGYGYNF | 1080 |
| VWSRDLYQVF TALIEVGEVE RGADALAYLY NTQQDDDGFL PQNTYIDGRT RWGGEQMDNI | 1140 |
| AFPSVMAWQL YEHGVVPAEA DYTYEQVRRS LCYIAANGPE TAQERWEEEA GFSPSSIAAE | 1200 |
| IAGLVCGAAL AVAEADRIEA GDGSAGSGSA ADPDSLRADA LAWLALADDW TARVEEWCAT | 1260 |
| ATGTERHGET PYYVRVTADG DPESGRPRTI ANDGPTYDER EIVDGGFLEL VRLGVKPADD | 1320 |
| DAVRNSVSVV DDSIRVDTPY GPAWYRYVGD AYGELARGDP GGPWAGTGDG RGRLWPIFTG | 1380 |
| ERGEYELRAR AGGPDAFGGT DEDALEPDAL LETMAGFGNS GRMLPEQVWD REHPTDYGWE | 1440 |
| FGEGTGGATP LAWSMAGFIR LAHGVEAGEP VETPTVVRDR YVERGRAAAP DLDATAEYVD | 1500 |
| DALVVSGETT ADTVAVYSSE GSTLATPADG EYEVDLDPAL DAKTIVVAAA NTGGDADGEA | 1560 |
| TDADAVLDAF SGAGTAVERL RV | 1582 |
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH15 | 1042 | 1462 | 5.8e-93 | 0.9889196675900277 |
| GH15 | 302 | 707 | 1.8e-38 | 0.9806094182825484 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| TIGR01535 | glucan_glucosid | 2.16e-158 | 754 | 1481 | 2 | 648 | glucan 1,4-alpha-glucosidase. Glucan 1,4-alpha-glucosidase catalyzes the hydrolysis of terminal 1,4-linked alpha-D-glucose residues from non-reducing ends of polysaccharides, releasing a beta-D-glucose monomer. Some forms of this enzyme can hydrolyze terminal 1,6- and 1,3-alpha-D-glucosidic bonds in polysaccharides as well. [Energy metabolism, Biosynthesis and degradation of polysaccharides] |
| cd07430 | GH15_N | 1.22e-65 | 724 | 1017 | 1 | 260 | Glycoside hydrolase family 15, N-terminal domain. Members of this family are N-terminal domains uniquely found in bacterial and archaeal glucoamylases and glucodextranases. Glucoamylase (glucan 1,4-alpha-glucosidase; 4-alpha-D-glucan glucohydrolase; amyloglucosidase; exo-1,4-alpha-glucosidase; gamma-amylase; lysosomal alpha-glucosidase; EC 3.2.1.3) hydrolyzes beta-1,4-glucosidic linkages of starch, glycogen and malto-oligosaccharides, releasing beta-D-glucose from the non-reducing end. Glucodextranase (glucan 1,6-alpha-glucosidase; exo-1,6-alpha-glucosidase; EC 3.2.1.70) uses an inverting reaction mechanism to hydrolyze alpha-1,6-glucosidic linkages of dextran and related oligosaccharides, releasing beta-D-glucose from the non-reducing end. These N-terminal domains adopt a structure consisting of antiparallel beta-strands, divided into two beta-sheets, with one sheet wrapped by an extended polypeptide, which appears to stabilize the domain. The function of these domains in the enzymes is as yet unknown. However, it is suggested that domain N of bacterial GA is involved in folding and/or the thermostability of the A domain that forms an (alpha/alpha)6-barrel structure. |
| pfam09137 | Glucodextran_N | 2.35e-54 | 724 | 1019 | 2 | 263 | Glucodextranase, domain N. Members of this family, which are uniquely found in bacterial and archaeal glucoamylases and glucodextranases, adopt a structure consisting of 17 antiparallel beta-strands. These beta-strands are divided into two beta-sheets, and one of the beta-sheets is wrapped by an extended polypeptide, which appears to stabilize the domain. Members of this family are mainly concerned with catalytic activity, hydrolysing alpha-1,6-glucosidic linkages of dextran to release beta-D-glucose from the non-reducing end via an inverting reaction mechanism. |
| COG3387 | SGA1 | 1.68e-47 | 754 | 1468 | 8 | 607 | Glucoamylase (glucan-1,4-alpha-glucosidase), GH15 family [Carbohydrate transport and metabolism]. |
| pfam00723 | Glyco_hydro_15 | 5.84e-32 | 1041 | 1463 | 11 | 417 | Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ACM57091.1 | 0.0 | 1 | 1582 | 1 | 1592 |
| AZQ14640.1 | 0.0 | 1 | 1582 | 1 | 1580 |
| QKY17980.1 | 0.0 | 1 | 1582 | 1 | 1574 |
| QWC20589.1 | 0.0 | 1 | 1582 | 1 | 1582 |
| QKG93726.1 | 0.0 | 1 | 1582 | 1 | 1571 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1UG9_A | 4.63e-131 | 722 | 1553 | 4 | 762 | CrystalStructure of Glucodextranase from Arthrobacter globiformis I42 [Arthrobacter globiformis],1ULV_A Crystal Structure of Glucodextranase Complexed with Acarbose [Arthrobacter globiformis] |
| 1LF6_A | 4.07e-92 | 726 | 1482 | 25 | 683 | CRYSTALSTRUCTURE OF BACTERIAL GLUCOAMYLASE [Thermoanaerobacterium thermosaccharolyticum],1LF6_B CRYSTAL STRUCTURE OF BACTERIAL GLUCOAMYLASE [Thermoanaerobacterium thermosaccharolyticum],1LF9_A Crystal Structure Of Bacterial Glucoamylase Complexed With Acarbose [Thermoanaerobacterium thermosaccharolyticum],1LF9_B Crystal Structure Of Bacterial Glucoamylase Complexed With Acarbose [Thermoanaerobacterium thermosaccharolyticum] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P29761 | 2.15e-92 | 726 | 1484 | 42 | 702 | Glucoamylase OS=Clostridium sp. (strain G0005) OX=72582 GN=cga PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.998857 | 0.001169 | 0.000020 | 0.000002 | 0.000001 | 0.000002 |