Analysis | Hit | start | end | length | Note | Hit coverage | Hit length | Hit pident | Hit pcons | eValue | Hit description |
blastp_kegg | bfu:BC1G_03627 | 1 | 124 | 124 | n/a | 100.00 | 124 | 100.00 | 0.00 | 5e-67 | ATP-dependent Clp protease proteolytic subunit K01358 ATP-dependent Clp protease protease subunit [EC:3.4.21.92] |
ssl:SS1G_12432 | 1 | 124 | 124 | n/a | 62.63 | 198 | 96.77 | 0.81 | 1e-64 | hypothetical protein K01358 ATP-dependent Clp protease protease subunit [EC:3.4.21.92] |
ure:UREG_07668 | 1 | 123 | 123 | n/a | 55.41 | 222 | 80.49 | 8.94 | 3e-53 | clp protease K01358 ATP-dependent Clp protease protease subunit [EC:3.4.21.92] |
cim:CIMG_07618 | 1 | 115 | 115 | n/a | 48.52 | 237 | 82.61 | 11.30 | 3e-53 | ATP-dependent Clp protease proteolytic subunit K01358 ATP-dependent Clp protease protease subunit [EC:3.4.21.92] |
aor:AO090005001444 | 1 | 115 | 115 | Gaps:2 | 43.82 | 267 | 84.62 | 6.84 | 4e-52 | ATP-dependent Clp protease proteolytic subunit K01358 ATP-dependent Clp protease protease subunit [EC:3.4.21.92] |
afv:AFLA_086760 | 1 | 115 | 115 | Gaps:2 | 45.70 | 256 | 84.62 | 6.84 | 9e-52 | ATP-dependent Clp protease proteolytic subunit ClpP K01358 ATP-dependent Clp protease protease subunit [EC:3.4.21.92] |
act:ACLA_036310 | 1 | 115 | 115 | Gaps:2 | 45.70 | 256 | 83.76 | 5.98 | 2e-51 | Clp protease putative K01358 ATP-dependent Clp protease protease subunit [EC:3.4.21.92] |
ang:An02g11960 | 1 | 119 | 119 | Gaps:2 | 48.21 | 251 | 79.34 | 9.09 | 6e-51 | hypothetical protein K01358 ATP-dependent Clp protease protease subunit [EC:3.4.21.92] |
afm:AFUA_3G08330 | 1 | 115 | 115 | Gaps:2 | 66.86 | 175 | 82.91 | 7.69 | 6e-51 | ATP-dependent Clp protease proteolytic subunit ClpP (EC:3.4.21.92) K01358 ATP-dependent Clp protease protease subunit [EC:3.4.21.92] |
nfi:NFIA_068790 | 1 | 115 | 115 | Gaps:2 | 66.86 | 175 | 82.91 | 6.84 | 1e-50 | Clp protease putative K01358 ATP-dependent Clp protease protease subunit [EC:3.4.21.92] |
blastp_uniprot_sprot | sp|Q5PBD0|CLPP_ANAMM | 1 | 115 | 115 | Gaps:2 | 52.56 | 215 | 64.60 | 16.81 | 5e-38 | ATP-dependent Clp protease proteolytic subunit OS Anaplasma marginale (strain St. Maries) GN clpP PE 3 SV 1 |
sp|B9KHZ4|CLPP_ANAMF | 1 | 115 | 115 | Gaps:2 | 52.56 | 215 | 64.60 | 16.81 | 5e-38 | ATP-dependent Clp protease proteolytic subunit OS Anaplasma marginale (strain Florida) GN clpP PE 3 SV 1 |
sp|B3CLB1|CLPP_WOLPP | 1 | 116 | 116 | Gaps:2 | 54.81 | 208 | 63.16 | 16.67 | 2e-37 | ATP-dependent Clp protease proteolytic subunit OS Wolbachia pipientis subsp. Culex pipiens (strain wPip) GN clpP PE 3 SV 1 |
sp|Q5GS83|CLPP_WOLTR | 1 | 116 | 116 | Gaps:2 | 54.81 | 208 | 63.16 | 16.67 | 3e-37 | ATP-dependent Clp protease proteolytic subunit OS Wolbachia sp. subsp. Brugia malayi (strain TRS) GN clpP PE 3 SV 1 |
sp|Q73I59|CLPP_WOLPM | 1 | 115 | 115 | Gaps:2 | 54.33 | 208 | 63.72 | 15.93 | 6e-37 | ATP-dependent Clp protease proteolytic subunit OS Wolbachia pipientis wMel GN clpP PE 3 SV 1 |
sp|C0R2W3|CLPP_WOLWR | 1 | 115 | 115 | Gaps:2 | 54.33 | 208 | 63.72 | 15.93 | 6e-37 | ATP-dependent Clp protease proteolytic subunit OS Wolbachia sp. subsp. Drosophila simulans (strain wRi) GN clpP PE 3 SV 1 |
sp|A8GSH5|CLPP_RICRS | 1 | 116 | 116 | Gaps:2 | 56.72 | 201 | 61.40 | 15.79 | 2e-36 | ATP-dependent Clp protease proteolytic subunit OS Rickettsia rickettsii (strain Sheila Smith) GN clpP PE 3 SV 1 |
sp|C4K1D4|CLPP_RICPU | 1 | 116 | 116 | Gaps:2 | 56.72 | 201 | 61.40 | 15.79 | 2e-36 | ATP-dependent Clp protease proteolytic subunit OS Rickettsia peacockii (strain Rustic) GN clpP PE 3 SV 1 |
sp|Q92HM5|CLPP_RICCN | 1 | 116 | 116 | Gaps:2 | 56.72 | 201 | 61.40 | 15.79 | 2e-36 | ATP-dependent Clp protease proteolytic subunit OS Rickettsia conorii GN clpP PE 3 SV 2 |
sp|Q4ULF0|CLPP_RICFE | 1 | 116 | 116 | Gaps:2 | 56.72 | 201 | 61.40 | 16.67 | 2e-36 | ATP-dependent Clp protease proteolytic subunit OS Rickettsia felis GN clpP PE 3 SV 1 |
blastp_pdb | 1yg8_B | 1 | 115 | 115 | Gaps:2 | 58.55 | 193 | 62.83 | 13.27 | 2e-35 | mol:protein length:193 ATP-dependent Clp protease proteolytic subuni |
1yg8_A | 1 | 115 | 115 | Gaps:2 | 58.55 | 193 | 62.83 | 13.27 | 2e-35 | mol:protein length:193 ATP-dependent Clp protease proteolytic subuni |
1yg8_b | 1 | 115 | 115 | Gaps:2 | 58.55 | 193 | 62.83 | 13.27 | 2e-35 | mol:protein length:193 ATP-dependent Clp protease proteolytic subuni |
1yg8_a | 1 | 115 | 115 | Gaps:2 | 58.55 | 193 | 62.83 | 13.27 | 2e-35 | mol:protein length:193 ATP-dependent Clp protease proteolytic subuni |
1yg8_Z | 1 | 115 | 115 | Gaps:2 | 58.55 | 193 | 62.83 | 13.27 | 2e-35 | mol:protein length:193 ATP-dependent Clp protease proteolytic subuni |
1yg8_Y | 1 | 115 | 115 | Gaps:2 | 58.55 | 193 | 62.83 | 13.27 | 2e-35 | mol:protein length:193 ATP-dependent Clp protease proteolytic subuni |
1yg8_X | 1 | 115 | 115 | Gaps:2 | 58.55 | 193 | 62.83 | 13.27 | 2e-35 | mol:protein length:193 ATP-dependent Clp protease proteolytic subuni |
1yg8_W | 1 | 115 | 115 | Gaps:2 | 58.55 | 193 | 62.83 | 13.27 | 2e-35 | mol:protein length:193 ATP-dependent Clp protease proteolytic subuni |
1yg8_V | 1 | 115 | 115 | Gaps:2 | 58.55 | 193 | 62.83 | 13.27 | 2e-35 | mol:protein length:193 ATP-dependent Clp protease proteolytic subuni |
1yg8_U | 1 | 115 | 115 | Gaps:2 | 58.55 | 193 | 62.83 | 13.27 | 2e-35 | mol:protein length:193 ATP-dependent Clp protease proteolytic subuni |
rpsblast_cdd | gnl|CDD|166883 | 1 | 116 | 116 | Gaps:2 | 57.00 | 200 | 56.14 | 20.18 | 1e-53 | PRK00277 clpP ATP-dependent Clp protease proteolytic subunit Reviewed. |
gnl|CDD|132928 | 1 | 111 | 111 | Gaps:2 | 63.74 | 171 | 59.63 | 17.43 | 9e-48 | cd07017 S14_ClpP_2 Caseinolytic protease (ClpP) is an ATP-dependent highly conserved serine protease. Clp protease (caseinolytic protease ClpP Peptidase S14) is a highly conserved serine protease present throughout in bacteria and eukaryota but seems to be absent in archaea mollicutes and some fungi. Clp proteases are involved in a number of cellular processes such as degradation of misfolded proteins regulation of short-lived proteins and housekeeping removal of dysfunctional proteins. They are also implicated in the control of cell growth targeting DNA-binding protein from starved cells. ClpP has also been linked to the tight regulation of virulence genes in the pathogens Listeria monocytogenes and Salmonella typhimurium. This enzyme belong to the family of ATP-dependent proteases the functional Clp protease is comprised of two components: a proteolytic component and one of several regulatory ATPase components both of which are required for effective levels of protease activity in the presence of ATP although the proteolytic subunit alone does possess some catalytic activity. Active site consists of the triad Ser His and Asp some members have lost all of these active site residues and are therefore inactive while others may have one or two large insertions. ClpP seems to prefer hydrophobic or non-polar residues at P1 or P1' positions in its substrate. The protease exists as a tetradecamer made up of two heptameric rings stacked back-to-back such that the catalytic triad of each subunit is located at the interface between three monomers thus making oligomerization essential for function. |
gnl|CDD|144241 | 1 | 115 | 115 | Gaps:2 | 62.09 | 182 | 56.64 | 18.58 | 2e-47 | pfam00574 CLP_protease Clp protease. The Clp protease has an active site catalytic triad. In E. coli Clp protease ser-111 his-136 and asp-185 form the catalytic triad. A putative Clp protease from Cyanophora paradoxa has lost all of these active site residues and is therefore inactive. A member from Chlamydomonas eugametos contains two large insertions a member from Chlamydomonas reinhardtii contains one large insertion. |
gnl|CDD|31083 | 1 | 120 | 120 | Gaps:2 | 59.00 | 200 | 55.93 | 22.03 | 7e-41 | COG0740 ClpP Protease subunit of ATP-dependent Clp proteases [Posttranslational modification protein turnover chaperones / Intracellular trafficking and secretion]. |
gnl|CDD|171575 | 1 | 115 | 115 | Gaps:4 | 59.90 | 192 | 50.43 | 20.87 | 7e-41 | PRK12553 PRK12553 ATP-dependent Clp protease proteolytic subunit Reviewed. |
gnl|CDD|129584 | 1 | 114 | 114 | Gaps:2 | 58.64 | 191 | 58.04 | 15.18 | 6e-39 | TIGR00493 clpP ATP-dependent Clp protease proteolytic subunit ClpP. This model for the proteolytic subunit ClpP has been rebuilt to a higher stringency. In every bacterial genome with the ClpXP machine a ClpP protein will be found that scores with this model. In general this ClpP member will be encoded adjacent to the clpX gene as were all examples used in the seed alignment. A large fraction of genomes have one or more additional ClpP paralogs sometimes encoded nearby and sometimes elsewhere. The stringency of the trusted cutoff used here excludes the more divergent ClpP paralogs from being called authentic ClpP by this model. |
gnl|CDD|164436 | 1 | 112 | 112 | Gaps:3 | 55.50 | 200 | 43.24 | 18.02 | 6e-37 | CHL00028 clpP ATP-dependent Clp protease proteolytic subunit. |
gnl|CDD|132924 | 1 | 111 | 111 | Gaps:2 | 67.28 | 162 | 45.87 | 18.35 | 8e-32 | cd07013 S14_ClpP Caseinolytic protease (ClpP) is an ATP-dependent highly conserved serine protease. Clp protease (caseinolytic protease ClpP Peptidase S14) is a highly conserved serine protease present throughout in bacteria and eukaryota but seems to be absent in archaea mollicutes and some fungi. Clp proteases are involved in a number of cellular processes such as degradation of misfolded proteins regulation of short-lived proteins and housekeeping removal of dysfunctional proteins. Additionally they are implicated in the control of cell growth targeting DNA-binding protein from starved cells. ClpP has also been linked to the tight regulation of virulence genes in the pathogens Listeria monocytogenes and Salmonella typhimurium. This enzyme belong to the family of ATP-dependent proteases the functional Clp protease is comprised of two components: a proteolytic component and one of several regulatory ATPase components both of which are required for effective levels of protease activity in the presence of ATP although the proteolytic subunit alone does possess some catalytic activity. Active site consists of the triad Ser His and Asp some members have lost all of these active site residues and are therefore inactive while others may have one or two large insertions. ClpP seems to prefer hydrophobic or non-polar residues at P1 or P1' positions in its substrate. The protease exists as a tetradecamer made up of two heptameric rings stacked back-to-back such that the catalytic triad of each subunit is located at the interface between three monomers thus making oligomerization essential for function. |
gnl|CDD|139060 | 1 | 115 | 115 | Gaps:2 | 57.65 | 196 | 50.44 | 15.04 | 4e-30 | PRK12551 PRK12551 ATP-dependent Clp protease proteolytic subunit Reviewed. |
gnl|CDD|172984 | 1 | 116 | 116 | Gaps:2 | 51.58 | 221 | 47.37 | 18.42 | 4e-30 | PRK14514 PRK14514 ATP-dependent Clp protease proteolytic subunit Provisional. |
rpsblast_kog | gnl|CDD|36058 | 1 | 122 | 122 | Gaps:2 | 43.64 | 275 | 54.17 | 18.33 | 5e-42 | KOG0840 KOG0840 KOG0840 ATP-dependent Clp protease proteolytic subunit [Posttranslational modification protein turnover chaperones]. |