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Conserved domains on  [gi|1915350477|dbj|BBW84051|]
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hypothetical protein THOESC015_P20210 (plasmid) [Escherichia coli]

Protein Classification

S24/S26 family peptidase( domain architecture ID 586)

S24/S26 family peptidase similar to human signal peptidase complex catalytic subunit SEC11C, a component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum

EC:  3.4.21.-
Gene Ontology:  GO:0017171

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_S24_S26 super family cl10465
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
1-177 4.99e-86

The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal peptidase families. The S24 LexA protein domains include: the lambda repressor CI/C2 family and related bacterial prophage repressor proteins; LexA (EC 3.4.21.88), the repressor of genes in the cellular SOS response to DNA damage; MucA and the related UmuD proteins, which are lesion-bypass DNA polymerases, induced in response to mitogenic DNA damage; RulA, a component of the rulAB locus that confers resistance to UV, and RuvA, which is a component of the RuvABC resolvasome that catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. The S26 type I signal peptidase (SPase) family also includes mitochondrial inner membrane protease (IMP)-like members. SPases are essential membrane-bound proteases which function to cleave away the amino-terminal signal peptide from the translocated pre-protein, thus playing a crucial role in the transport of proteins across membranes in all living organisms. All members in this superfamily are unique serine proteases that carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic acid triad found in most serine proteases.


The actual alignment was detected with superfamily member PRK13884:

Pssm-ID: 447902  Cd Length: 178  Bit Score: 250.33  E-value: 4.99e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915350477   1 MKKMTRYAAIGVISASLIGAVvcgfGYAAGLRINTSKSIPVGLYKISQKAPEKGDYVIFCPPEKAIFSLAQKRGYIGSGF 80
Cdd:PRK13884    5 LKRITAGVAVAGLAALLLAAL----GYAAGARVNTTKSIPVGLYWTSSAPVEKGAYVLFCPPQRGVFDDAKERGYIGAGF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915350477  81 CPGGYGEMMKRILAAKGDEVAFRDDGVYVNGQLLPYSKPLSVDPGGRKLPAIR-EVYTLGKSELLLMTDRSASSFDGRYF 159
Cdd:PRK13884   81 CPGGYGYMMKRVLAAKGDAVSVTDDGVRVNGELLPLSKPILADGAGRPLPRYQaNSYTLGESELLLMSDVSATSFDGRYF 160
                         170
                  ....*....|....*...
gi 1915350477 160 GAVTKSQIISTILPVMTW 177
Cdd:PRK13884  161 GPINRSQIKTVIRPVITW 178
 
Name Accession Description Interval E-value
PRK13884 PRK13884
conjugal transfer peptidase TraF; Provisional
1-177 4.99e-86

conjugal transfer peptidase TraF; Provisional


Pssm-ID: 184368  Cd Length: 178  Bit Score: 250.33  E-value: 4.99e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915350477   1 MKKMTRYAAIGVISASLIGAVvcgfGYAAGLRINTSKSIPVGLYKISQKAPEKGDYVIFCPPEKAIFSLAQKRGYIGSGF 80
Cdd:PRK13884    5 LKRITAGVAVAGLAALLLAAL----GYAAGARVNTTKSIPVGLYWTSSAPVEKGAYVLFCPPQRGVFDDAKERGYIGAGF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915350477  81 CPGGYGEMMKRILAAKGDEVAFRDDGVYVNGQLLPYSKPLSVDPGGRKLPAIR-EVYTLGKSELLLMTDRSASSFDGRYF 159
Cdd:PRK13884   81 CPGGYGYMMKRVLAAKGDAVSVTDDGVRVNGELLPLSKPILADGAGRPLPRYQaNSYTLGESELLLMSDVSATSFDGRYF 160
                         170
                  ....*....|....*...
gi 1915350477 160 GAVTKSQIISTILPVMTW 177
Cdd:PRK13884  161 GPINRSQIKTVIRPVITW 178
TraF_Ti TIGR02771
conjugative transfer signal peptidase TraF; This protein is found in apparent operons encoding ...
10-177 6.30e-64

conjugative transfer signal peptidase TraF; This protein is found in apparent operons encoding elements of conjugative transfer systems. This family is homologous to a broader family of signal (leader) peptidases such as lepB. This family is present in both Ti-type and I-type conjugative systems.


Pssm-ID: 131818 [Multi-domain]  Cd Length: 171  Bit Score: 194.24  E-value: 6.30e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915350477  10 IGVISASLIGAVVCGFgYAAGLRINTSKSIPVGLYKISQKAP-EKGDYVIFCPPEKAIFSLAQKRGYIGSGFCPGGYGEM 88
Cdd:TIGR02771   6 LGIAGLALSGLTILGL-YCVGARINTTKSLPLGLYWTTSSKPvERGDYVVFCPPDNPQFEEARERGYLREGLCPGGFGPL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915350477  89 MKRILAAKGDEVAFRDDGVYVNGQLLPYSKPLSVDPGGRKLPAIRE-VYTLGkseLLLMTDRSASSFDGRYFGAVTKSQI 167
Cdd:TIGR02771  85 LKRVLGLPGDRVTVRADVVAINGQLLPYSKPLATDSSGRPLPPFPEgVIPPG---FFVVHDTSPTSFDSRYFGPISREQV 161
                         170
                  ....*....|
gi 1915350477 168 ISTILPVMTW 177
Cdd:TIGR02771 162 IGRVKPLFTW 171
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
53-177 9.66e-35

Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, chaperones, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443985 [Multi-domain]  Cd Length: 114  Bit Score: 118.09  E-value: 9.66e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915350477  53 KGDYVIFCPPEKaifsLAQKRGYIGSGFcpggygEMMKRILAAKGDEVAFRDDGVYVNGQLLPYSKPlsVDPGGRKLPAI 132
Cdd:COG4959     1 RGDLVAFRPPEP----LAAERGYLPRGV------PLIKRVAALPGDTVCIKGGQVYINGKPVAEALE--RDRAGRPLPVW 68
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1915350477 133 REVYTLGKSELLLMTDRSASSFDGRYFGAVTKSQIISTILPVMTW 177
Cdd:COG4959    69 QGCGVVPEGEYFLLGDNRPNSFDSRYFGPVPRSQIIGRAVPLWTP 113
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
4-168 9.21e-30

Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases which function in the processing of newly-synthesized secreted proteins. Peptidase S26 removes the hydrophobic, N-terminal, signal peptides as proteins are translocated across membranes. The active site residues take the form of a catalytic dyad that is Ser, Lys in subfamily S26A; the Ser is the nucleophile in catalysis, and the Lys is the general base.


Pssm-ID: 431321 [Multi-domain]  Cd Length: 162  Bit Score: 106.91  E-value: 9.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915350477   4 MTRYAAIGVIsASLIGAVVCGFgYAAGLRI---NTSKSIPVGLYKISQKA------PEKGDYVIFCPPEkaifslaqkrg 74
Cdd:pfam10502   1 LLEWVKAIVI-ALLLALLIRTF-LFEPYVVpggSMSPTLPIGDYLIVNKFsyglgePKRGDIVVFRPPE----------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915350477  75 yiGSGFcpggygEMMKRILAAKGDEVAFRDDGVYVNGQllPYSKPLSVDPGGRK---LPAIREVYTLGKSELLLMTDRSA 151
Cdd:pfam10502  68 --GPGV------PLIKRVIGLPGDRVEYKDDQLYINGK--PVGEPYLADRKGRPtfdLPPWQGCRVVPEGEYFVMGDNRD 137
                         170
                  ....*....|....*..
gi 1915350477 152 SSFDGRYFGAVTKSQII 168
Cdd:pfam10502 138 NSLDSRYFGFVPASNIV 154
 
Name Accession Description Interval E-value
PRK13884 PRK13884
conjugal transfer peptidase TraF; Provisional
1-177 4.99e-86

conjugal transfer peptidase TraF; Provisional


Pssm-ID: 184368  Cd Length: 178  Bit Score: 250.33  E-value: 4.99e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915350477   1 MKKMTRYAAIGVISASLIGAVvcgfGYAAGLRINTSKSIPVGLYKISQKAPEKGDYVIFCPPEKAIFSLAQKRGYIGSGF 80
Cdd:PRK13884    5 LKRITAGVAVAGLAALLLAAL----GYAAGARVNTTKSIPVGLYWTSSAPVEKGAYVLFCPPQRGVFDDAKERGYIGAGF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915350477  81 CPGGYGEMMKRILAAKGDEVAFRDDGVYVNGQLLPYSKPLSVDPGGRKLPAIR-EVYTLGKSELLLMTDRSASSFDGRYF 159
Cdd:PRK13884   81 CPGGYGYMMKRVLAAKGDAVSVTDDGVRVNGELLPLSKPILADGAGRPLPRYQaNSYTLGESELLLMSDVSATSFDGRYF 160
                         170
                  ....*....|....*...
gi 1915350477 160 GAVTKSQIISTILPVMTW 177
Cdd:PRK13884  161 GPINRSQIKTVIRPVITW 178
TraF_Ti TIGR02771
conjugative transfer signal peptidase TraF; This protein is found in apparent operons encoding ...
10-177 6.30e-64

conjugative transfer signal peptidase TraF; This protein is found in apparent operons encoding elements of conjugative transfer systems. This family is homologous to a broader family of signal (leader) peptidases such as lepB. This family is present in both Ti-type and I-type conjugative systems.


Pssm-ID: 131818 [Multi-domain]  Cd Length: 171  Bit Score: 194.24  E-value: 6.30e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915350477  10 IGVISASLIGAVVCGFgYAAGLRINTSKSIPVGLYKISQKAP-EKGDYVIFCPPEKAIFSLAQKRGYIGSGFCPGGYGEM 88
Cdd:TIGR02771   6 LGIAGLALSGLTILGL-YCVGARINTTKSLPLGLYWTTSSKPvERGDYVVFCPPDNPQFEEARERGYLREGLCPGGFGPL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915350477  89 MKRILAAKGDEVAFRDDGVYVNGQLLPYSKPLSVDPGGRKLPAIRE-VYTLGkseLLLMTDRSASSFDGRYFGAVTKSQI 167
Cdd:TIGR02771  85 LKRVLGLPGDRVTVRADVVAINGQLLPYSKPLATDSSGRPLPPFPEgVIPPG---FFVVHDTSPTSFDSRYFGPISREQV 161
                         170
                  ....*....|
gi 1915350477 168 ISTILPVMTW 177
Cdd:TIGR02771 162 IGRVKPLFTW 171
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
53-177 9.66e-35

Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, chaperones, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443985 [Multi-domain]  Cd Length: 114  Bit Score: 118.09  E-value: 9.66e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915350477  53 KGDYVIFCPPEKaifsLAQKRGYIGSGFcpggygEMMKRILAAKGDEVAFRDDGVYVNGQLLPYSKPlsVDPGGRKLPAI 132
Cdd:COG4959     1 RGDLVAFRPPEP----LAAERGYLPRGV------PLIKRVAALPGDTVCIKGGQVYINGKPVAEALE--RDRAGRPLPVW 68
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1915350477 133 REVYTLGKSELLLMTDRSASSFDGRYFGAVTKSQIISTILPVMTW 177
Cdd:COG4959    69 QGCGVVPEGEYFLLGDNRPNSFDSRYFGPVPRSQIIGRAVPLWTP 113
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
4-168 9.21e-30

Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases which function in the processing of newly-synthesized secreted proteins. Peptidase S26 removes the hydrophobic, N-terminal, signal peptides as proteins are translocated across membranes. The active site residues take the form of a catalytic dyad that is Ser, Lys in subfamily S26A; the Ser is the nucleophile in catalysis, and the Lys is the general base.


Pssm-ID: 431321 [Multi-domain]  Cd Length: 162  Bit Score: 106.91  E-value: 9.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915350477   4 MTRYAAIGVIsASLIGAVVCGFgYAAGLRI---NTSKSIPVGLYKISQKA------PEKGDYVIFCPPEkaifslaqkrg 74
Cdd:pfam10502   1 LLEWVKAIVI-ALLLALLIRTF-LFEPYVVpggSMSPTLPIGDYLIVNKFsyglgePKRGDIVVFRPPE----------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915350477  75 yiGSGFcpggygEMMKRILAAKGDEVAFRDDGVYVNGQllPYSKPLSVDPGGRK---LPAIREVYTLGKSELLLMTDRSA 151
Cdd:pfam10502  68 --GPGV------PLIKRVIGLPGDRVEYKDDQLYINGK--PVGEPYLADRKGRPtfdLPPWQGCRVVPEGEYFVMGDNRD 137
                         170
                  ....*....|....*..
gi 1915350477 152 SSFDGRYFGAVTKSQII 168
Cdd:pfam10502 138 NSLDSRYFGFVPASNIV 154
PRK13838 PRK13838
conjugal transfer pilin processing protease TraF; Provisional
4-177 3.28e-29

conjugal transfer pilin processing protease TraF; Provisional


Pssm-ID: 172365 [Multi-domain]  Cd Length: 176  Bit Score: 105.84  E-value: 3.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915350477   4 MTRYAAIGVISAS-LIGAVVCGFGYAAGLRINTSKSIPVGLYKIS--QKAPEKGDYVIFCPPEKAIFSLAQKRGYIGSGF 80
Cdd:PRK13838    1 MRRRRALLLLAVAaVAASGLAATAWIGGYRINLTPSEPLGLWRIEalDRPVAVGDLVFICPPETAAFREARERGYLRRGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915350477  81 CPGGYGEMMKRILAAKGDEVAFRdDGVYVNGQLLPYS---------KPLSVDPGGrKLPAirevytlgksELLLMTDRSA 151
Cdd:PRK13838   81 CPGGFAPLIKTVAALAGQRVEIG-GSVSIDGRPLPSSsvrrrdgegRPLTPFPGG-VVPP----------GHLFLHSSFA 148
                         170       180
                  ....*....|....*....|....*.
gi 1915350477 152 SSFDGRYFGAVTKSQIISTILPVMTW 177
Cdd:PRK13838  149 GSYDSRYFGPVPASGLLGLARPVLTF 174
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
49-168 3.92e-08

signal peptidase I, bacterial type; This model represents signal peptidase I from most bacteria. Eukaryotic sequences are likely organellar. Several bacteria have multiple paralogs, but these represent isozymes of signal peptidase I. Virtually all known bacteria may be presumed to A related model finds a simlar protein in many archaea and a few bacteria, as well as a microsomal (endoplasmic reticulum) protein in eukaryotes. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274044 [Multi-domain]  Cd Length: 142  Bit Score: 49.92  E-value: 3.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915350477  49 KAPEKGDYVIF-CPPEKAIFslaqkrgYIgsgfcpggygemmKRILAAKGDEVAFRDDGVYVNGQL-----LPYSKPLSV 122
Cdd:TIGR02227  33 SDPKRGDIVVFkDPDTNKNI-------YV-------------KRIIGLPGDKVEFRDGKLYINGKKidepyLKPNGYLDT 92
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1915350477 123 DP--GGRKLPAirevytlGKseLLLMTDRSASSFDGRYFGAVTKSQII 168
Cdd:TIGR02227  93 SEfnTPVKVPP-------GH--YFVLGDNRDNSLDSRYFGFVPIDQII 131
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
51-160 1.15e-03

Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 37.91  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915350477  51 PEKGDYVIFCPPEKAifslaqKRGYIgsgfcpggygemmKRILAAKGDEVAFRDDGVYVNGQLLPYSKPLSVDPGGRKLP 130
Cdd:COG0681    65 PKRGDIVVFKYPEDP------SKDYI-------------KRVIGLPGDTVEIRDGQVYVNGKPLNEPYLEEYYYPVSVDG 125
                          90       100       110
                  ....*....|....*....|....*....|
gi 1915350477 131 AIREVYTLGKSELLLMTDRSASSFDGRYFG 160
Cdd:COG0681   126 DVEVPPGEEEVPGGGGDNSNDSRSGDPDDG 155
 
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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