You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000002490_04047
You are here: Home > Sequence: MGYG000002490_04047
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 | Paenibacillus_B thiaminolyticus | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_B; Paenibacillus_B thiaminolyticus | |||||||||||
| CAZyme ID | MGYG000002490_04047 | |||||||||||
| CAZy Family | CBM13 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 417828; End: 419630 Strand: - | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG5555 | COG5555 | 4.31e-08 | 157 | 427 | 43 | 282 | Cytolysin, a secreted calcineurin-like phosphatase [Intracellular trafficking, secretion, and vesicular transport]. |
| cd00839 | MPP_PAPs | 1.13e-07 | 202 | 390 | 29 | 203 | purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain. Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs belong 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: 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. |
| pfam14200 | RicinB_lectin_2 | 1.17e-06 | 492 | 577 | 2 | 86 | Ricin-type beta-trefoil lectin domain-like. |
| cd07396 | MPP_Nbla03831 | 1.08e-05 | 160 | 401 | 5 | 212 | Homo sapiens Nbla03831 and related proteins, metallophosphatase domain. Nbla03831 (also known as LOC56985) is an uncharacterized Homo sapiens protein with a domain that 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: 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. |
| cd07395 | MPP_CSTP1 | 6.50e-05 | 159 | 394 | 8 | 221 | Homo sapiens CSTP1 and related proteins, metallophosphatase domain. CSTP1 (complete S-transactivated protein 1) is an uncharacterized Homo sapiens protein with a metallophosphatase domain, that is transactivated by the complete S protein of hepatitis B virus. CSTP1 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: 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 |
|---|---|---|---|---|---|
| QDM42212.1 | 0.0 | 1 | 600 | 1 | 600 |
| AQT83473.1 | 1.57e-208 | 4 | 598 | 1 | 594 |
| ARF70105.1 | 8.65e-208 | 4 | 598 | 1 | 593 |
| QDX94829.1 | 1.31e-144 | 157 | 597 | 9 | 469 |
| AUM94646.1 | 4.48e-135 | 157 | 580 | 17 | 451 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1QXM_A | 1.34e-12 | 445 | 591 | 13 | 152 | Crystalstructure of a hemagglutinin component (HA1) from type C Clostridium botulinum [Clostridium botulinum D phage],1QXM_B Crystal structure of a hemagglutinin component (HA1) from type C Clostridium botulinum [Clostridium botulinum D phage] |
| 4OUJ_A | 2.60e-12 | 453 | 591 | 10 | 142 | Crystalstructure of HA33B-Lac [Clostridium botulinum B1 str. Okra],4OUJ_B Crystal structure of HA33B-Lac [Clostridium botulinum B1 str. Okra] |
| 3WIN_A | 2.84e-12 | 453 | 591 | 31 | 163 | Clostridiumbotulinum Hemagglutinin [Clostridium botulinum B],3WIN_B Clostridium botulinum Hemagglutinin [Clostridium botulinum B] |
| 5B2H_A | 3.62e-12 | 451 | 591 | 3 | 136 | Crystalstructure of HA33 from Clostridium botulinum serotype C strain Yoichi [Clostridium botulinum],5B2H_B Crystal structure of HA33 from Clostridium botulinum serotype C strain Yoichi [Clostridium botulinum] |
| 3AJ5_A | 3.75e-12 | 451 | 591 | 5 | 138 | HA1(HA33) subcomponent of botulinum type C progenitor toxin complexed with N-acetylgalactosamine, bound at site II [Clostridium botulinum],3AJ5_B HA1 (HA33) subcomponent of botulinum type C progenitor toxin complexed with N-acetylgalactosamine, bound at site II [Clostridium botulinum] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P0DPR0 | 2.05e-11 | 451 | 591 | 5 | 138 | Main hemagglutinin component type C OS=Clostridium botulinum C phage OX=12336 GN=HA-33 PE=1 SV=1 |
| P0DPR1 | 2.05e-11 | 451 | 591 | 5 | 138 | Main hemagglutinin component type D OS=Clostridium botulinum D phage OX=29342 GN=ha-33 PE=1 SV=1 |
| Q9GV36 | 1.89e-08 | 472 | 574 | 584 | 688 | Pierisin OS=Pieris brassicae OX=7116 PE=1 SV=1 |
| Q9U8Q4 | 2.25e-07 | 472 | 574 | 584 | 688 | Pierisin OS=Pieris rapae OX=64459 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 |
|---|---|---|---|---|---|
| 1.000091 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |