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Conserved domains on  [gi|1125341796|gb|OLC82155|]
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hypothetical protein AUI96_00010 [Nitrospirae bacterium 13_1_40CM_3_62_11]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG1750 super family cl34354
Predicted archaeal serine protease, S18 family [General function prediction only];
143-261 1.60e-24

Predicted archaeal serine protease, S18 family [General function prediction only];


The actual alignment was detected with superfamily member COG1750:

Pssm-ID: 441356 [Multi-domain]  Cd Length: 213  Bit Score: 97.36  E-value: 1.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125341796 143 LGEDSRNWTITIKNRSYSNLTQGPSASSAVAIGIMAAARGETLRPGVALTGAITADGGIDEVGGLPGKLEGAAMANMHTL 222
Cdd:COG1750    87 AGVDLSSYDVYISIESDSPIVGGPSAGGAMTVATYAALLGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYF 166

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1125341796 223 LVPKGQA--------RTEEWDLPQLGRLRNITVIEVGSLREAYELMT 261
Cdd:COG1750   167 LIPKGQAiltgyntqVGETVDLVEYGKELGVKVIEVSTIADALQYFT 213
 
Name Accession Description Interval E-value
COG1750 COG1750
Predicted archaeal serine protease, S18 family [General function prediction only];
143-261 1.60e-24

Predicted archaeal serine protease, S18 family [General function prediction only];


Pssm-ID: 441356 [Multi-domain]  Cd Length: 213  Bit Score: 97.36  E-value: 1.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125341796 143 LGEDSRNWTITIKNRSYSNLTQGPSASSAVAIGIMAAARGETLRPGVALTGAITADGGIDEVGGLPGKLEGAAMANMHTL 222
Cdd:COG1750    87 AGVDLSSYDVYISIESDSPIVGGPSAGGAMTVATYAALLGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYF 166

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1125341796 223 LVPKGQA--------RTEEWDLPQLGRLRNITVIEVGSLREAYELMT 261
Cdd:COG1750   167 LIPKGQAiltgyntqVGETVDLVEYGKELGVKVIEVSTIADALQYFT 213
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
 165-238 3.81e-07

Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activity resides in a C-terminal domain. The Lon proteases are classified as family S16 in Merops.


Pssm-ID: 428442 [Multi-domain]  Cd Length: 205  Bit Score: 49.54  E-value: 3.81e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1125341796 165 GPSASSAVAIGIMAAARGETLRPGVALTGAITADGGIDEVGGLPGKLEGAAMANMHTLLVPKGQARTEEwDLPQ 238
Cdd:pfam05362 109 GPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVIIPKENEKDLE-DIPE 181
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
 165-238 7.71e-06

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 46.86  E-value: 7.71e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1125341796 165 GPSASSAVAIGIMAAARGETLRPGVALTGAITADGGIDEVGGLPGKLEGAAMANMHTLLVPKGQARTEEwDLPQ 238
Cdd:PRK10787  677 GPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLE-EIPD 749
 
Name Accession Description Interval E-value
COG1750 COG1750
Predicted archaeal serine protease, S18 family [General function prediction only];
143-261 1.60e-24

Predicted archaeal serine protease, S18 family [General function prediction only];


Pssm-ID: 441356 [Multi-domain]  Cd Length: 213  Bit Score: 97.36  E-value: 1.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125341796 143 LGEDSRNWTITIKNRSYSNLTQGPSASSAVAIGIMAAARGETLRPGVALTGAITADGGIDEVGGLPGKLEGAAMANMHTL 222
Cdd:COG1750    87 AGVDLSSYDVYISIESDSPIVGGPSAGGAMTVATYAALLGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYF 166

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1125341796 223 LVPKGQA--------RTEEWDLPQLGRLRNITVIEVGSLREAYELMT 261
Cdd:COG1750   167 LIPKGQAiltgyntqVGETVDLVEYGKELGVKVIEVSTIADALQYFT 213
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
 165-238 3.81e-07

Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activity resides in a C-terminal domain. The Lon proteases are classified as family S16 in Merops.


Pssm-ID: 428442 [Multi-domain]  Cd Length: 205  Bit Score: 49.54  E-value: 3.81e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1125341796 165 GPSASSAVAIGIMAAARGETLRPGVALTGAITADGGIDEVGGLPGKLEGAAMANMHTLLVPKGQARTEEwDLPQ 238
Cdd:pfam05362 109 GPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVIIPKENEKDLE-DIPE 181
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
 165-238 7.71e-06

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 46.86  E-value: 7.71e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1125341796 165 GPSASSAVAIGIMAAARGETLRPGVALTGAITADGGIDEVGGLPGKLEGAAMANMHTLLVPKGQARTEEwDLPQ 238
Cdd:PRK10787  677 GPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLE-EIPD 749
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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