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CAZyme Information: MGYG000004082_00101
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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 | AM51-8 sp900761925 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; AM51-8; AM51-8 sp900761925 | |||||||||||
| CAZyme ID | MGYG000004082_00101 | |||||||||||
| CAZy Family | GH106 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 283; End: 3099 Strand: - | |||||||||||
Full Sequence Download help
| MNETVQHLLN NQGENYILPF FWQHGETEEV LREYMAAIDA SNIKAVCVES RPHPDFCGEK | 60 |
| WWQDMDVILD EARKRHMKVW ILDDSHFPTG FANGALKDYP DCYCRQSICC RAYDLSAEDC | 120 |
| AGLTVSGGGQ RKLHIGAEQI AHPNPFEKNM IENFVLKEPG RVFDDDRLFS LWAIRRDENA | 180 |
| DGFSDPAWRI DLAPMIADGE LDWEVPEGNW KVYALHLTRN MGFHRTYINM MDASSCHVLI | 240 |
| DAVYEPHWEH YEADFGATIA GFFSDEPELG NGHLYDWNDP YGHISDYPWS EELETDLAEK | 300 |
| MHGDAGWMLS LLFENDADND LTAKVRYAFM DSVSSLVRKD FSYQLGDWCR QHGVQYIGHV | 360 |
| IEDNNHHSRT ASSLGHYFRG LQGQDMSGID DIGGQVYPQG EHDTYDQGMF QARNGEFYHF | 420 |
| VLGKLGASAA AIEPAKEGRA MCEIFGNYGW QEGVRLEKYL ADHFLVRGIN HYVPHAFTAK | 480 |
| DYPDPDCPPH FYAHGHNPQY RHFGWLMKYM NRVCNLISGG HHSAPVAVIY SGEGDWTGKY | 540 |
| MNIDAIGAAL TEHQIEYDIV PQDVFAIPEF YRTFIGNHVL KVNTQTYRAV VVPYMQYITK | 600 |
| ALAETITVLN SEGIPVLFAD KAPEGICDTP AVSADGVKDS RTVETDAALI AAVKKYAKVL | 660 |
| SVSDLAGAPE LAGIAEVNFA PADVFLRCYH YLHNDGSSVY MLVNEGTEVW RGTVTFAAEK | 720 |
| GNDAAVYGYD AWENICYPAD IDRTTGAWEI ALEPLQSRMV IFDATAKAAD IGTKLCLRAI | 780 |
| DRLASKSKEE IALAASSWKR STCAGIDYPA FGEAKEIVLP DPLAEEEPEF SGFVRYENTF | 840 |
| RADEALSAAG DKRLLLEITD AHEGVEVFVN DQSLGIQIVP TYCFDLTDAL VPGENRIRIE | 900 |
| AATTLERENY KIPHRMGLPK PEPKDPSGIN GEVHLYLI | 938 |
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH106 | 31 | 935 | 2.9e-64 | 0.9599514563106796 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam17132 | Glyco_hydro_106 | 0.003 | 140 | 213 | 297 | 378 | alpha-L-rhamnosidase. |
| cd00842 | MPP_ASMase | 0.006 | 53 | 103 | 192 | 237 | acid sphingomyelinase and related proteins, metallophosphatase domain. Acid sphingomyelinase (ASMase) is a ubiquitously expressed phosphodiesterase which hydrolyzes sphingomyelin in acid pH conditions to form ceramide, a bioactive second messenger, as part of the sphingomyelin signaling pathway. ASMase is localized at the noncytosolic leaflet of biomembranes (for example the luminal leaflet of endosomes, lysosomes and phagosomes, and the extracellular leaflet of plasma membranes). ASMase-deficient humans develop Niemann-Pick disease. This disease is characterized by lysosomal storage of sphingomyelin in all tissues. Although ASMase-deficient mice are resistant to stress-induced apoptosis, they have greater susceptibility to bacterial infection. The latter correlates with defective phagolysosomal fusion and antibacterial killing activity in ASMase-deficient macrophages. ASMase belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ANU53235.1 | 0.0 | 1 | 935 | 1 | 867 |
| QQR29381.1 | 0.0 | 1 | 935 | 1 | 867 |
| ASB40092.1 | 0.0 | 1 | 935 | 1 | 867 |
| QOV19610.1 | 1.66e-286 | 1 | 936 | 1 | 897 |
| ABX41053.1 | 3.10e-239 | 1 | 936 | 1 | 896 |
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 |
|---|---|---|---|---|---|
| 1.000060 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |