You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000004255_00012
You are here: Home > Sequence: MGYG000004255_00012
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 | Amulumruptor sp900547825 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Amulumruptor; Amulumruptor sp900547825 | |||||||||||
| CAZyme ID | MGYG000004255_00012 | |||||||||||
| CAZy Family | GT2 | |||||||||||
| CAZyme Description | Gramicidin S synthase 2 | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 11793; End: 19061 Strand: + | |||||||||||
Full Sequence Download help
| MTPLSQTQIG IYIESLRNEG QNIYHTPHLA LMHGVDDPER LVKAVQAVVA AFPSISARVK | 60 |
| VDDNGTPVLI DASSTGPVEV QLTRTTEEKL MLTRNELIKP FELDGGTLAH INVIATEKHV | 120 |
| YLFTDFHHSI FDGHSHKLFL KAVDAAYVGK DLEKENVTIY EVARREKEAR SSDALDRCRA | 180 |
| EYAEMLGGAD TELEIMPDTA GVEEGYATLS VPVGIAGKDY KEFCRRMEMP SSVPAVAAMG | 240 |
| LVLSSFCNKE DVVFSTIWHG RKGHEFDRTF GMMVKTIPAR VSVGAGESVS SLLRHTARRL | 300 |
| KIARDNGLYS FADVVSEFGI NSDFLFAYQG DFLDLPQVGG VPVDDIMLES IATGARITVN | 360 |
| LSIKQGEMSV EVQYRRDLYS SRLINAFVSS LGEILRGMIS GNRDTDVRTL RLVPAEDENE | 420 |
| IYTLGRGPEQ GGDPQATIPD LFVKAAERYP DNIAVVFRDR RMTYAELDKV TDALAAELKG | 480 |
| RYGVRKESIV GVLIERSELM AVLPLAIMKA GGAYIPLDPH FPEERLMFMA QDAGVKLIIG | 540 |
| DDGLVAEKMP AFSGAVINAS EIRDLPAPDF RPAIDTTPDS SMVVLYTSGS TGKPKGVTLE | 600 |
| QHNIVNFCHA YTELTGMSAT DIAGAYAAFG FDAHMMDLYP ALLSGATVHI FDSEIRLDLT | 660 |
| AMHGYMERER ITVMFMTTQI AWQMATLFEF STLRVLSGGG EKLPPLGPLP YVFFNVYGPT | 720 |
| ECSVLTTAFR LHDTTDGRLI GRPLAGYEVR ILDRNLRLLP AGVTGELVIM GAGVGRGYLN | 780 |
| RPELTSEKFI EIDGVKAYRT GDQARWTADG DIEFLGRMDG MVKLRGLRIE LGEIEAVAAS | 840 |
| HPDVASFTAA VKEIGGAGNL VGYFTVREGR ELTADDLREY MAGELTEFMV PAVIMKLDSM | 900 |
| PLTPNGKVDR RALPVPEMAV EEHVEPATDI EIKVTGIVAD ILGHADFGVT TGLISVGLTS | 960 |
| LMVMRLAAAI MKNLGVKLTA KQIMSAPTVR EIAVAIESAG TDTTARKESS RPRRRYYPLT | 1020 |
| ENQRGVYIDW EMNRDALQYN IPQAFRFGPG TDTEALRKAV LKVADAHPGL KTRLSIRGGD | 1080 |
| VVQERRDDDI VDVAVTDLAE RPTPEFFQSL VKPFDLLSDA LFRCGIFRYG SEVYMFMDTH | 1140 |
| HIIFDGVSAM VFQQELAKAY AGATLEAEEY TALDYALDQK ELVESEEMDK AAQWFDSLIG | 1200 |
| ESEPTRYPQN RKPDSDIAGE MGRLRLRIPS EDIKKFCAAG GVTPSNYLLS SFLQLLHRIV | 1260 |
| REETVQITTV TNGRSDLRLL NSTGMFVKTL PVVSRCKNPG VSPLEFVRDI QQQFITSTDY | 1320 |
| DFYPFTSLVE RNGVRPEIMY VFEGGINLGG DDAMKAEKIP LRLDTAKVPL TLLVFEPSEG | 1380 |
| EYELVAEYDT SVYNKADMEL LLRMMASLNL SLPEVAAVGH AKMVDDDQEH ELSALRNGRR | 1440 |
| CEVEYESFHG AMEMRADATP DAPALVACDR RMTYREFDEE CNRVANALIS RGVQRGDRIV | 1500 |
| ILLPRRSYLI TAIYGTMKAG AAYIPCDPDY PADRIRLITE DSGARYIVTT SDRLGIDPGR | 1560 |
| TIDINDLLSG TDTARPAVSI DPEDVAYMIY TSGSTGRPKG VMIPHRAITN YLYGYRKLFF | 1620 |
| EDNPDIRTQM LIVTISFDAS LVNLGTALTS GHCLVLADEE ECKDVVLLSK LMLENQVDSF | 1680 |
| DITPSRLDAM LDLPEFRQAV SIAKHINIGG EGFQSSLVTK LYEAGFRGMT VNEYGPTETT | 1740 |
| VGSNHAVLQP GGPIVAGRPF MNMSQRIVDA WGSELPVGAV GELYIFGRGV GLGYNKLPEK | 1800 |
| TAEAYVTFHG ERAYRTGDLA RWTPDGEVVI LGRIDHQVKI RGLRIELGEI ENVARTFPGI | 1860 |
| LAAAADVREI NKIQHLCLYY TAAAAVDKEA LREHLAASLT EYMVPDAYTQ IEQMPLTPNG | 1920 |
| KTNRKALPEP ELAPLNPYVE PEGDLEKEIA RVFGDILQRE LIGANDDFFA IGGTSISAIK | 1980 |
| VVAALVSAGH AITYKNVFAC RTPRAIAAML EGGDRAVSAV PEPASSSVVG ESEFAAILNR | 2040 |
| NTIDAFRGGE RQPIGNVLLT GATGFMGIHM LHELLGNTDS NICCLLRSRQ GLSAESRLRT | 2100 |
| LLFYYFNDTF DDEFASGRLR VVEGDVTAAV PDAIAECGID TVINCAANVK HFSAGDDIET | 2160 |
| VNVESVRNLA AFCLGTGARL VHVSTVSIAG ESVNGVPDPS ILLTEKMFDF GQSLSNQYVH | 2220 |
| SKYEAERVIL ENIRDHGLNA KIMRVGNLSA RGSDGEFQIN SRSNAFMGKL RAYAMLGCAP | 2280 |
| YSDLDAPCEF SPIDEVCHAI VLLSTTPVDM TVFQPCNNHR FPLGDVLHIL SETGIPVEPV | 2340 |
| EAETFEAAKN EAMTETDTDR ISALQPLLAY DSGTAGRTAF IRYDSSFTNQ ILYRLGFRWN | 2400 |
| YTSSEYVRQF VKAISSLDYF SI | 2422 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK05691 | PRK05691 | 0.0 | 100 | 2008 | 780 | 2773 | peptide synthase; Validated |
| PRK12467 | PRK12467 | 0.0 | 54 | 2019 | 102 | 2172 | peptide synthase; Provisional |
| PRK12316 | PRK12316 | 0.0 | 99 | 2013 | 1659 | 3625 | peptide synthase; Provisional |
| cd05930 | A_NRPS | 3.80e-162 | 450 | 913 | 1 | 444 | The adenylation domain of nonribosomal peptide synthetases (NRPS). The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. |
| cd05930 | A_NRPS | 5.94e-157 | 1460 | 1927 | 1 | 444 | The adenylation domain of nonribosomal peptide synthetases (NRPS). The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QND46664.1 | 3.89e-213 | 225 | 1997 | 792 | 2649 |
| ACX49739.1 | 2.72e-146 | 3 | 1711 | 11 | 1837 |
| BAZ00088.1 | 2.49e-95 | 4 | 1000 | 2247 | 3296 |
| BAZ75991.1 | 2.49e-95 | 4 | 1000 | 2247 | 3296 |
| BAY30132.1 | 4.27e-95 | 24 | 1000 | 2269 | 3298 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6MFZ_A | 8.20e-243 | 344 | 2022 | 113 | 1809 | Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis] |
| 6MFY_A | 8.25e-232 | 344 | 1931 | 113 | 1716 | Crystalstructure of a 5-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis],6MG0_A Crystal structure of a 5-domain construct of LgrA in the thiolation state [Brevibacillus parabrevis],6MG0_B Crystal structure of a 5-domain construct of LgrA in the thiolation state [Brevibacillus parabrevis] |
| 6MFX_A | 1.30e-142 | 344 | 1406 | 113 | 1178 | Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis] |
| 6MFW_A | 1.09e-141 | 344 | 1406 | 113 | 1178 | Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis] |
| 5ES5_A | 5.68e-113 | 344 | 992 | 111 | 760 | Crystalstructure of the initiation module of LgrA in the 'open' and 'closed ' adenylation states [Brevibacillus parabrevis],5ES5_B Crystal structure of the initiation module of LgrA in the 'open' and 'closed ' adenylation states [Brevibacillus parabrevis],5ES8_A Crystal structure of the initiation module of LgrA in the thiolation state [Brevibacillus parabrevis],5ES8_B Crystal structure of the initiation module of LgrA in the thiolation state [Brevibacillus parabrevis],5ES9_A Crystal structure of the LgrA initiation module in the formylation state [Brevibacillus parabrevis],5ES9_B Crystal structure of the LgrA initiation module in the formylation state [Brevibacillus parabrevis] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| O68006 | 1.44e-253 | 3 | 1999 | 1673 | 3718 | Bacitracin synthase 1 OS=Bacillus licheniformis OX=1402 GN=bacA PE=3 SV=1 |
| P0C064 | 2.65e-245 | 3 | 1982 | 1063 | 3093 | Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2 |
| P0C063 | 2.25e-243 | 3 | 1982 | 1063 | 3094 | Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2 |
| Q70LM7 | 1.13e-237 | 344 | 2007 | 110 | 1791 | Linear gramicidin synthase subunit A OS=Brevibacillus parabrevis OX=54914 GN=lgrA PE=1 SV=1 |
| P39847 | 2.25e-228 | 237 | 1998 | 257 | 2061 | Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2 |
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 |
|---|---|---|---|---|---|
| 1.000031 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |