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CAZyme Information: MGYG000001950_01491
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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 | Gastranaerophilus phascolarctosicola | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Cyanobacteria; Vampirovibrionia; Gastranaerophilales; Gastranaerophilaceae; Gastranaerophilus; Gastranaerophilus phascolarctosicola | |||||||||||
| CAZyme ID | MGYG000001950_01491 | |||||||||||
| CAZy Family | CBM5 | |||||||||||
| CAZyme Description | Negative regulator of genetic competence ClpC/MecB | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 1236; End: 3737 Strand: + | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| NF033606 | heat_AAA_ClpK | 0.0 | 4 | 833 | 111 | 924 | heat shock survival AAA family ATPase ClpK. ClpK, a Clp family AAA ATPase, was discovered as a plasmid-encoded determinant for survival of heat shock along with other putative heat shock proteins. ClpK requires the presence of ClpP to confer heat resistance. ClpK is about 65% identical to ClpG. Note that PMID:26974352 and PMID:29263094 discuss both ClpG itself and a member of this family (ClpK) that they call ClpG-GI. |
| TIGR03346 | chaperone_ClpB | 0.0 | 5 | 814 | 1 | 849 | ATP-dependent chaperone ClpB. Members of this protein family are the bacterial ATP-dependent chaperone ClpB. This protein belongs to the AAA family, ATPases associated with various cellular activities (pfam00004). This molecular chaperone does not act as a protease, but rather serves to disaggregate misfolded and aggregated proteins. [Protein fate, Protein folding and stabilization] |
| NF033607 | disagg_AAA_ClpG | 0.0 | 3 | 830 | 87 | 898 | AAA family protein disaggregase ClpG. ClpG, as characterized in Pseudomonas aeruginosa, is a Clp family member of the AAA+ family of ATPases. ClpG has stand-alone ability to disaggregate proteins from aggregates that result from heat stess. Both ClpG and its mobilized homolog ClpK provide increased survival of exposure to heat. |
| COG0542 | ClpA | 0.0 | 4 | 821 | 1 | 786 | ATP-dependent Clp protease ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones]. |
| PRK11034 | clpA | 0.0 | 20 | 831 | 17 | 757 | ATP-dependent Clp protease ATP-binding subunit; Provisional |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AGL63717.2 | 1.20e-190 | 174 | 792 | 107 | 710 |
| AXG45674.1 | 7.39e-130 | 174 | 806 | 180 | 862 |
| AXG41146.1 | 7.39e-130 | 174 | 806 | 180 | 862 |
| AWK40335.1 | 2.85e-129 | 174 | 806 | 180 | 862 |
| QIE96744.1 | 2.57e-11 | 361 | 434 | 1 | 74 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 7ABR_A | 0.0 | 1 | 821 | 2 | 808 | ChainA, Negative regulator of genetic competence ClpC/MecB [Bacillus subtilis subsp. subtilis str. 168],7ABR_B Chain B, Negative regulator of genetic competence ClpC/MecB [Bacillus subtilis subsp. subtilis str. 168],7ABR_C Chain C, Negative regulator of genetic competence ClpC/MecB [Bacillus subtilis subsp. subtilis str. 168],7ABR_D Chain D, Negative regulator of genetic competence ClpC/MecB [Bacillus subtilis subsp. subtilis str. 168],7ABR_E Chain E, Negative regulator of genetic competence ClpC/MecB [Bacillus subtilis subsp. subtilis str. 168],7ABR_F Chain F, Negative regulator of genetic competence ClpC/MecB [Bacillus subtilis subsp. subtilis str. 168] |
| 3J3T_A | 0.0 | 1 | 821 | 2 | 808 | Structuraldynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3T_B Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3T_C Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3T_D Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3T_E Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3T_F Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168] |
| 3J3S_A | 0.0 | 1 | 821 | 2 | 808 | Structuraldynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3S_B Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3S_C Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3S_D Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3S_E Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3S_F Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168] |
| 3J3R_A | 0.0 | 1 | 821 | 2 | 808 | Structuraldynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3R_B Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3R_C Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3R_D Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3R_E Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3R_F Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3U_A Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3U_B Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3U_C Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3U_D Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3U_E Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3U_F Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168] |
| 6EM9_A | 1.13e-318 | 1 | 805 | 2 | 792 | S.aureusClpC resting state, asymmetric map [Staphylococcus aureus RF122],6EM9_B S.aureus ClpC resting state, asymmetric map [Staphylococcus aureus RF122],6EM9_C S.aureus ClpC resting state, asymmetric map [Staphylococcus aureus RF122],6EM9_D S.aureus ClpC resting state, asymmetric map [Staphylococcus aureus RF122],6EM9_E S.aureus ClpC resting state, asymmetric map [Staphylococcus aureus RF122],6EM9_F S.aureus ClpC resting state, asymmetric map [Staphylococcus aureus RF122],6EM9_G S.aureus ClpC resting state, asymmetric map [Staphylococcus aureus RF122],6EM9_H S.aureus ClpC resting state, asymmetric map [Staphylococcus aureus RF122],6EM9_I S.aureus ClpC resting state, asymmetric map [Staphylococcus aureus RF122],6EM9_L S.aureus ClpC resting state, asymmetric map [Staphylococcus aureus RF122] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q2QVG9 | 0.0 | 1 | 804 | 88 | 889 | Chaperone protein ClpC2, chloroplastic OS=Oryza sativa subsp. japonica OX=39947 GN=CLPC2 PE=2 SV=2 |
| Q1XDF4 | 0.0 | 1 | 804 | 1 | 798 | ATP-dependent Clp protease ATP-binding subunit ClpA homolog OS=Neopyropia yezoensis OX=2788 GN=clpC PE=3 SV=1 |
| Q9SXJ7 | 0.0 | 1 | 805 | 114 | 916 | Chaperone protein ClpC2, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=CLPC2 PE=1 SV=1 |
| Q9FI56 | 0.0 | 1 | 805 | 94 | 895 | Chaperone protein ClpC1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=CLPC1 PE=1 SV=1 |
| Q8EU05 | 0.0 | 1 | 809 | 2 | 799 | Chaperone protein ClpB OS=Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831) OX=221109 GN=clpB PE=3 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 |
|---|---|---|---|---|---|
| 1.000046 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |