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Conserved domains on  [gi|73535786|pdb|1Z0T|F]
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Chain F, Putative protease La homolog type

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Lon_C super family cl21678
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
9-185 1.78e-34

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.


The actual alignment was detected with superfamily member pfam05362:

Pssm-ID: 451353 [Multi-domain]  Cd Length: 205  Bit Score: 121.19  E-value: 1.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Z0T_F          9 EVGRVNGLAVIgESAGIVLPIIAEVTPSmsksEGRVIATGRLQEIAREAVMNVSAIIK---KYTGRD---ISNMDVHIQF 82
Cdd:pfam05362  26 QVGVVTGLAWT-EVGGDLLTIEAVIMPG----KGKLTLTGQLGDVMKESAQAALSYVRsraEELGIDpdfFEKKDIHIHV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Z0T_F         83 VgtyEGV---EGDSASISIATAVISAIEGIPVDQSVAMTGSLSVKGEVLPVGGVTQKIEAAIQAGLKKVIIPKDNIDDVL 159
Cdd:pfam05362 101 P---EGAtpkDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVIIPKENEKDLE 177
                         170       180
                  ....*....|....*....|....*..
1Z0T_F        160 -LDAEHEGKIEVIPVSRINEVLEHVLE 185
Cdd:pfam05362 178 dIPENVREGLEIIPVEHVDEVLKHALV 204
 
Name Accession Description Interval E-value
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
9-185 1.78e-34

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: 121.19  E-value: 1.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Z0T_F          9 EVGRVNGLAVIgESAGIVLPIIAEVTPSmsksEGRVIATGRLQEIAREAVMNVSAIIK---KYTGRD---ISNMDVHIQF 82
Cdd:pfam05362  26 QVGVVTGLAWT-EVGGDLLTIEAVIMPG----KGKLTLTGQLGDVMKESAQAALSYVRsraEELGIDpdfFEKKDIHIHV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Z0T_F         83 VgtyEGV---EGDSASISIATAVISAIEGIPVDQSVAMTGSLSVKGEVLPVGGVTQKIEAAIQAGLKKVIIPKDNIDDVL 159
Cdd:pfam05362 101 P---EGAtpkDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVIIPKENEKDLE 177
                         170       180
                  ....*....|....*....|....*..
1Z0T_F        160 -LDAEHEGKIEVIPVSRINEVLEHVLE 185
Cdd:pfam05362 178 dIPENVREGLEIIPVEHVDEVLKHALV 204
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
9-191 3.32e-33

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 125.13  E-value: 3.32e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Z0T_F        9 EVGRVNGLA---VIGEsagiVLPIiaEVTpsMSKSEGRVIATGRL----QEIAREAVMNVSAIIKKYtGRD---ISNMDV 78
Cdd:COG0466 597 QVGVVTGLAwteVGGD----ILFI--EAT--LMPGKGKLTLTGQLgdvmKESAQAALSYVRSRAEEL-GIDpdfFEKYDI 667
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Z0T_F       79 HIQFVgtyEGV---EGDSASISIATAVISAIEGIPVDQSVAMTGSLSVKGEVLPVGGVTQKIEAAIQAGLKKVIIPKDNI 155
Cdd:COG0466 668 HIHVP---EGAtpkDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVILPKENE 744
                       170       180       190
                ....*....|....*....|....*....|....*..
1Z0T_F      156 DDVL-LDAEHEGKIEVIPVSRINEVLEHVLEDGKKKN 191
Cdd:COG0466 745 KDLEeIPEEVKKGLEFHPVEHIDEVLKIALEKEPEPL 781
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
10-186 9.75e-21

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 89.23  E-value: 9.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Z0T_F        10 VGRVNGLAVIgESAGIVLPIIAEVTPSmsksEGRVIATGRLQEIAREAVMNVSAIIKK-----------YTGRDISnmdV 78
Cdd:PRK10787 595 VGQVTGLAWT-EVGGDLLTIETACVPG----KGKLTYTGSLGEVMQESIQAALTVVRAraeklginpdfYEKRDIH---V 666
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Z0T_F        79 HIQFVGTYEgvEGDSASISIATAVISAIEGIPVDQSVAMTGSLSVKGEVLPVGGVTQKIEAAIQAGLKKVIIPKDNIDDV 158
Cdd:PRK10787 667 HVPEGATPK--DGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDL 744
                        170       180
                 ....*....|....*....|....*....
1Z0T_F       159 L-LDAEHEGKIEVIPVSRINEVLEHVLED 186
Cdd:PRK10787 745 EeIPDNVIADLDIHPVKRIEEVLTLALQN 773
 
Name Accession Description Interval E-value
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
9-185 1.78e-34

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: 121.19  E-value: 1.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Z0T_F          9 EVGRVNGLAVIgESAGIVLPIIAEVTPSmsksEGRVIATGRLQEIAREAVMNVSAIIK---KYTGRD---ISNMDVHIQF 82
Cdd:pfam05362  26 QVGVVTGLAWT-EVGGDLLTIEAVIMPG----KGKLTLTGQLGDVMKESAQAALSYVRsraEELGIDpdfFEKKDIHIHV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Z0T_F         83 VgtyEGV---EGDSASISIATAVISAIEGIPVDQSVAMTGSLSVKGEVLPVGGVTQKIEAAIQAGLKKVIIPKDNIDDVL 159
Cdd:pfam05362 101 P---EGAtpkDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVIIPKENEKDLE 177
                         170       180
                  ....*....|....*....|....*..
1Z0T_F        160 -LDAEHEGKIEVIPVSRINEVLEHVLE 185
Cdd:pfam05362 178 dIPENVREGLEIIPVEHVDEVLKHALV 204
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
9-191 3.32e-33

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 125.13  E-value: 3.32e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Z0T_F        9 EVGRVNGLA---VIGEsagiVLPIiaEVTpsMSKSEGRVIATGRL----QEIAREAVMNVSAIIKKYtGRD---ISNMDV 78
Cdd:COG0466 597 QVGVVTGLAwteVGGD----ILFI--EAT--LMPGKGKLTLTGQLgdvmKESAQAALSYVRSRAEEL-GIDpdfFEKYDI 667
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Z0T_F       79 HIQFVgtyEGV---EGDSASISIATAVISAIEGIPVDQSVAMTGSLSVKGEVLPVGGVTQKIEAAIQAGLKKVIIPKDNI 155
Cdd:COG0466 668 HIHVP---EGAtpkDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVILPKENE 744
                       170       180       190
                ....*....|....*....|....*....|....*..
1Z0T_F      156 DDVL-LDAEHEGKIEVIPVSRINEVLEHVLEDGKKKN 191
Cdd:COG0466 745 KDLEeIPEEVKKGLEFHPVEHIDEVLKIALEKEPEPL 781
COG1750 COG1750
Predicted archaeal serine protease, S18 family [General function prediction only];
16-182 6.39e-29

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


Pssm-ID: 441356 [Multi-domain]  Cd Length: 213  Bit Score: 106.99  E-value: 6.39e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Z0T_F       16 LAVIGESAGIVLPIIAEVTPSmskSEGRV-IATGRLQEIAREAVMNVSAII-KKYTGRDISNMDVHIQFVGTYEGVEGDS 93
Cdd:COG1750  35 PAVSGTGEGVVINITVTVTYP---GSGRVyVSTSPLTGPDTQASARIAALVaSLLAGVDLSSYDVYISIESDSPIVGGPS 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Z0T_F       94 ASISIATAVISAIEGIPVDQSVAMTGSLSVKGEVLPVGGVTQKIEAAIQAGLKKVIIPKDN------------IDDVLLD 161
Cdd:COG1750 112 AGGAMTVATYAALLGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYFLIPKGQailtgyntqvgeTVDLVEY 191
                       170       180
                ....*....|....*....|.
1Z0T_F      162 AEHEGkIEVIPVSRINEVLEH 182
Cdd:COG1750 192 GKELG-VKVIEVSTIADALQY 211
LonB COG1067
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ...
5-181 7.23e-29

Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440686 [Multi-domain]  Cd Length: 742  Bit Score: 112.73  E-value: 7.23e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Z0T_F        5 TEGYEVGRVNGLAVI--GESA-GIVLPIIAEVtpsmSKSEGRVIatgrlqEIAREA----------VMNVSAIIK-KYtG 70
Cdd:COG1067 503 TEGEKVGQINGLSVLdlGDYSfGRPSRITATV----YLGKGGVI------DIEREVelsgpihskgVLILSGYLGaRY-A 571
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Z0T_F       71 RDI-SNMDVHIQFVGTYEGVEGDSASISIATAVISAIEGIPVDQSVAMTGSLSVKGEVLPVGGVTQKIE---AAIQA-GL 145
Cdd:COG1067 572 QDKpLSLSASLVFEQSYGGVDGDSASSAELYALLSALSGVPIRQDIAVTGSVNQHGEVQPIGGVNEKIEgffDVCKArGL 651
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
1Z0T_F      146 KK---VIIPKDNIDDVLLDAE-----HEGKIEVIPVSRINEVLE 181
Cdd:COG1067 652 TGkqgVIIPAANVKNLMLRDEvveavKAGQFHIYAVEHVDEAIE 695
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
10-186 9.75e-21

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 89.23  E-value: 9.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Z0T_F        10 VGRVNGLAVIgESAGIVLPIIAEVTPSmsksEGRVIATGRLQEIAREAVMNVSAIIKK-----------YTGRDISnmdV 78
Cdd:PRK10787 595 VGQVTGLAWT-EVGGDLLTIETACVPG----KGKLTYTGSLGEVMQESIQAALTVVRAraeklginpdfYEKRDIH---V 666
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Z0T_F        79 HIQFVGTYEgvEGDSASISIATAVISAIEGIPVDQSVAMTGSLSVKGEVLPVGGVTQKIEAAIQAGLKKVIIPKDNIDDV 158
Cdd:PRK10787 667 HVPEGATPK--DGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDL 744
                        170       180
                 ....*....|....*....|....*....
1Z0T_F       159 L-LDAEHEGKIEVIPVSRINEVLEHVLED 186
Cdd:PRK10787 745 EeIPDNVIADLDIHPVKRIEEVLTLALQN 773
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
115-193 3.33e-05

Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 43.65  E-value: 3.33e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1Z0T_F      115 VAMTGSLSVKGEVLPVGGVTQKIEAAIQAGLKKVIIPKDNIDDVlLDAEHEGkIEVIPVSRINEVLeHVLEDGKKKNRL 193
Cdd:COG3480 266 IAGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASNCAEA-VGTIPTG-LKVVPVDTLDDAL-DALEALRAGGDL 341
 
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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