NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1063890168|ref|WP_069455482|]
View 

MULTISPECIES: signal peptidase I [Shewanella]

Protein Classification

S26 family signal peptidase( domain architecture ID 10008982)

S26 family signal peptidase is a membrane-bound serine protease which frees proteins tethered to inner or mitochondrial membranes by cleaving off signal peptides during polypeptide translocation

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 50-157 7.82e-21

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: 81.88  E-value: 7.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063890168  50 RDRLIAFNLP----VDTPYFKKGSRWIKKLVGVPGDRVIVRIDEVLINGKSYKNNMRQLLMKIELseSAIIREFVLAEDE 125
Cdd:COG4959     1 RGDLVAFRPPeplaAERGYLPRGVPLIKRVAALPGDTVCIKGGQVYINGKPVAEALERDRAGRPL--PVWQGCGVVPEGE 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1063890168 126 YFMVGET-PLSYDSRFWGVVHAQDMIGDAYAVL 157
Cdd:COG4959    79 YFLLGDNrPNSFDSRYFGPVPRSQIIGRAVPLW 111
 
Name Accession Description Interval E-value
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 50-157 7.82e-21

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: 81.88  E-value: 7.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063890168  50 RDRLIAFNLP----VDTPYFKKGSRWIKKLVGVPGDRVIVRIDEVLINGKSYKNNMRQLLMKIELseSAIIREFVLAEDE 125
Cdd:COG4959     1 RGDLVAFRPPeplaAERGYLPRGVPLIKRVAALPGDTVCIKGGQVYINGKPVAEALERDRAGRPL--PVWQGCGVVPEGE 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1063890168 126 YFMVGET-PLSYDSRFWGVVHAQDMIGDAYAVL 157
Cdd:COG4959    79 YFLLGDNrPNSFDSRYFGPVPRSQIIGRAVPLW 111
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 1-157 8.68e-17

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: 72.62  E-value: 8.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063890168   1 MKNVIPSFsLIAVVILLLASKF---TLAVPSQ--EYSCLFARYFLVDKTNITI---KRDRLIAFNLPVDTpyfkkGSRWI 72
Cdd:pfam10502   1 LLEWVKAI-VIALLLALLIRTFlfePYVVPGGsmSPTLPIGDYLIVNKFSYGLgepKRGDIVVFRPPEGP-----GVPLI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063890168  73 KKLVGVPGDRVIVRIDEVLINGKSYKNN-MRQLLMKIELSESAIIREFVLAEDEYFMVGET-PLSYDSRFWGVVHAQDMI 150
Cdd:pfam10502  75 KRVIGLPGDRVEYKDDQLYINGKPVGEPyLADRKGRPTFDLPPWQGCRVVPEGEYFVMGDNrDNSLDSRYFGFVPASNIV 154


                  ....*..
gi 1063890168 151 GDAYAVL 157
Cdd:pfam10502 155 GRAVFPV 161
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 47-157 4.54e-11

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: 57.24  E-value: 4.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063890168  47 TIK-RDRLIAFNLPVDTPYFKKG------------SRWIKKLVGVPGDRVIVRIDEVLINGK----SYKNNMRQLLMKIE 109
Cdd:TIGR02227  16 TLKeGDRILVNKFAYRTSDPKRGdivvfkdpdtnkNIYVKRIIGLPGDKVEFRDGKLYINGKkidePYLKPNGYLDTSEF 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1063890168 110 lsesaiIREFVLAEDEYFMVGE-TPLSYDSRFWGVVHAQDMIGDAYAVL 157
Cdd:TIGR02227  96 ------NTPVKVPPGHYFVLGDnRDNSLDSRYFGFVPIDQIIGKVSFVF 138
PRK10861 PRK10861
signal peptidase I;
118-156 2.13e-03

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 37.34  E-value: 2.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1063890168 118 EFVLAEDEYFMVGET-PLSYDSRFWGVVHAQDMIGDAYAV 156
Cdd:PRK10861  261 TWVVPPGQYFMMGDNrDNSADSRYWGFVPEANLVGKATAI 300
 
Name Accession Description Interval E-value
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 50-157 7.82e-21

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: 81.88  E-value: 7.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063890168  50 RDRLIAFNLP----VDTPYFKKGSRWIKKLVGVPGDRVIVRIDEVLINGKSYKNNMRQLLMKIELseSAIIREFVLAEDE 125
Cdd:COG4959     1 RGDLVAFRPPeplaAERGYLPRGVPLIKRVAALPGDTVCIKGGQVYINGKPVAEALERDRAGRPL--PVWQGCGVVPEGE 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1063890168 126 YFMVGET-PLSYDSRFWGVVHAQDMIGDAYAVL 157
Cdd:COG4959    79 YFLLGDNrPNSFDSRYFGPVPRSQIIGRAVPLW 111
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 1-157 8.68e-17

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: 72.62  E-value: 8.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063890168   1 MKNVIPSFsLIAVVILLLASKF---TLAVPSQ--EYSCLFARYFLVDKTNITI---KRDRLIAFNLPVDTpyfkkGSRWI 72
Cdd:pfam10502   1 LLEWVKAI-VIALLLALLIRTFlfePYVVPGGsmSPTLPIGDYLIVNKFSYGLgepKRGDIVVFRPPEGP-----GVPLI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063890168  73 KKLVGVPGDRVIVRIDEVLINGKSYKNN-MRQLLMKIELSESAIIREFVLAEDEYFMVGET-PLSYDSRFWGVVHAQDMI 150
Cdd:pfam10502  75 KRVIGLPGDRVEYKDDQLYINGKPVGEPyLADRKGRPTFDLPPWQGCRVVPEGEYFVMGDNrDNSLDSRYFGFVPASNIV 154


                  ....*..
gi 1063890168 151 GDAYAVL 157
Cdd:pfam10502 155 GRAVFPV 161
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 47-157 4.54e-11

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: 57.24  E-value: 4.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063890168  47 TIK-RDRLIAFNLPVDTPYFKKG------------SRWIKKLVGVPGDRVIVRIDEVLINGK----SYKNNMRQLLMKIE 109
Cdd:TIGR02227  16 TLKeGDRILVNKFAYRTSDPKRGdivvfkdpdtnkNIYVKRIIGLPGDKVEFRDGKLYINGKkidePYLKPNGYLDTSEF 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1063890168 110 lsesaiIREFVLAEDEYFMVGE-TPLSYDSRFWGVVHAQDMIGDAYAVL 157
Cdd:TIGR02227  96 ------NTPVKVPPGHYFVLGDnRDNSLDSRYFGFVPIDQIIGKVSFVF 138
TraF_Ti TIGR02771
conjugative transfer signal peptidase TraF; This protein is found in apparent operons encoding ...
 72-157 1.02e-06

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: 45.93  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063890168  72 IKKLVGVPGDRVIVRIDEVLINGKSYKNNmrqllmKIELSES-----AIIREFVLAEDEYFMVGETPLSYDSRFWGVVHA 146
Cdd:TIGR02771  85 LKRVLGLPGDRVTVRADVVAINGQLLPYS------KPLATDSsgrplPPFPEGVIPPGFFVVHDTSPTSFDSRYFGPISR 158

                          90
                  ....*....|.
gi 1063890168 147 QDMIGDAYAVL 157
Cdd:TIGR02771 159 EQVIGRVKPLF 169
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
38-142 1.13e-04

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 40.61  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063890168  38 YFLVDKTNI---TIKRDRLIAFNLPVDtpyfkKGSRWIKKLVGVPGDRVIVRIDEVLINGKSYKNNMRQLLMKIELSESA 114
Cdd:COG0681    52 RLLVNKLSYgfgEPKRGDIVVFKYPED-----PSKDYIKRVIGLPGDTVEIRDGQVYVNGKPLNEPYLEEYYYPVSVDGD 126

                          90       100
                  ....*....|....*....|....*...
gi 1063890168 115 IIREFVLAEDEYFMVGETPLSYDSRFWG 142
Cdd:COG0681   127 VEVPPGEEEVPGGGGDNSNDSRSGDPDD 154
PRK10861 PRK10861
signal peptidase I;
118-156 2.13e-03

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 37.34  E-value: 2.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1063890168 118 EFVLAEDEYFMVGET-PLSYDSRFWGVVHAQDMIGDAYAV 156
Cdd:PRK10861  261 TWVVPPGQYFMMGDNrDNSADSRYWGFVPEANLVGKATAI 300
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH