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Conserved domains on  [gi|1691716723|ref|XP_029411054|]
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mitochondrial inner membrane protease subunit 1 isoform X1 [Nannospalax galili]

Protein Classification

S26 family signal peptidase( domain architecture ID 10158224)

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

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List of domain hits

 Name Accession Description Interval E-value
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 33-141 2.40e-35

The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4.21.89) family members are essential membrane-bound serine proteases that function to cleave the amino-terminal signal peptide extension from proteins that are translocated across biological membranes. The bacterial signal peptidase I, which is the most intensively studied, has two N-terminal transmembrane segments inserted in the plasma membrane and a hydrophilic, C-terminal catalytic region that is located in the periplasmic space. Although the bacterial signal peptidase I is monomeric, signal peptidases of eukaryotic cells commonly function as oligomeric complexes containing two divergent copies of the catalytic monomer. These are the IMP1 and IMP2 signal peptidases of the mitochondrial inner membrane that remove leader peptides from nuclear- and mitochondrial-encoded proteins. Also, two components of the endoplasmic reticulum signal peptidase in mammals (18-kDa and 21-kDa) belong to this family and they process many proteins that enter the ER for retention or for export to the Golgi apparatus, secretory vesicles, plasma membranes or vacuole. An atypical member of the S26 SPase type I family is the TraF peptidase which has the remarkable activity of producing a cyclic protein of the Pseudomonas pilin system. The type I signal peptidases are unique serine proteases that utilize a serine/lysine catalytic dyad mechanism in place of the classical serine/histidine/aspartic acid catalytic triad mechanism.


:

Pssm-ID: 119398 [Multi-domain]  Cd Length: 85  Bit Score: 120.77  E-value: 2.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691716723  33 VVMCSGPSMEPTIQNSDIVFAENLSRHFYGIQRGDIVIAKSPSDPKSNICKRVIGlegdkilttspsdffkshsyvprgh 112
Cdd:cd06530     2 PVVVPGGSMEPTLQPGDLVLVNKLSYGFREPKRGDVVVFKSPGDPGKPIIKRVIG------------------------- 56

                          90       100
                  ....*....|....*....|....*....
gi 1691716723 113 VWLEGDNLQNSTDSRYYGPIPYGLIRGRI 141
Cdd:cd06530    57 YFVLGDNRNNSLDSRYWGPVPEDDIVGKV 85
 
Name Accession Description Interval E-value
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 33-141 2.40e-35

The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4.21.89) family members are essential membrane-bound serine proteases that function to cleave the amino-terminal signal peptide extension from proteins that are translocated across biological membranes. The bacterial signal peptidase I, which is the most intensively studied, has two N-terminal transmembrane segments inserted in the plasma membrane and a hydrophilic, C-terminal catalytic region that is located in the periplasmic space. Although the bacterial signal peptidase I is monomeric, signal peptidases of eukaryotic cells commonly function as oligomeric complexes containing two divergent copies of the catalytic monomer. These are the IMP1 and IMP2 signal peptidases of the mitochondrial inner membrane that remove leader peptides from nuclear- and mitochondrial-encoded proteins. Also, two components of the endoplasmic reticulum signal peptidase in mammals (18-kDa and 21-kDa) belong to this family and they process many proteins that enter the ER for retention or for export to the Golgi apparatus, secretory vesicles, plasma membranes or vacuole. An atypical member of the S26 SPase type I family is the TraF peptidase which has the remarkable activity of producing a cyclic protein of the Pseudomonas pilin system. The type I signal peptidases are unique serine proteases that utilize a serine/lysine catalytic dyad mechanism in place of the classical serine/histidine/aspartic acid catalytic triad mechanism.


Pssm-ID: 119398 [Multi-domain]  Cd Length: 85  Bit Score: 120.77  E-value: 2.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691716723  33 VVMCSGPSMEPTIQNSDIVFAENLSRHFYGIQRGDIVIAKSPSDPKSNICKRVIGlegdkilttspsdffkshsyvprgh 112
Cdd:cd06530     2 PVVVPGGSMEPTLQPGDLVLVNKLSYGFREPKRGDVVVFKSPGDPGKPIIKRVIG------------------------- 56

                          90       100
                  ....*....|....*....|....*....
gi 1691716723 113 VWLEGDNLQNSTDSRYYGPIPYGLIRGRI 141
Cdd:cd06530    57 YFVLGDNRNNSLDSRYWGPVPEDDIVGKV 85
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 29-145 3.16e-32

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: 114.63  E-value: 3.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691716723  29 YVGGVVMCSGPSMEPTIQNSDIVFAENLSRHFYGIQRGDIVIAKSPSDPKSNICKRVIGLEGDKI--------------- 93
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFAYRTSDPKRGDIVVFKDPDTNKNIYVKRIIGLPGDKVefrdgklyingkkid 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1691716723  94 ---LTTSPSDFFKSHSY---VPRGHVWLEGDNLQNSTDSRYYGPIPYGLIRGRIFFKL 145
Cdd:TIGR02227  81 epyLKPNGYLDTSEFNTpvkVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVF 138
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 38-145 2.07e-26

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: 100.36  E-value: 2.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691716723  38 GPSMEPTIQNSDIVFAENLSRHFYGIQRGDIVIAKSPSDPKSNICKRVIGLEGDKI------LT---------------- 95
Cdd:pfam10502  30 GGSMSPTLPIGDYLIVNKFSYGLGEPKRGDIVVFRPPEGPGVPLIKRVIGLPGDRVeykddqLYingkpvgepyladrkg 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1691716723  96 TSPSDF--FKSHSYVPRGHVWLEGDNLQNSTDSRYYGPIPYGLIRGRIFFKL 145
Cdd:pfam10502 110 RPTFDLppWQGCRVVPEGEYFVMGDNRDNSLDSRYFGFVPASNIVGRAVFPV 161
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
38-143 2.73e-17

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 76.81  E-value: 2.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691716723  38 GPSMEPTIQNSDIVFAENLSRHFYGIQRGDIVIAKSPSDPKSNICKRVIGLEGDKI-------------------LTTSP 98
Cdd:COG0681    40 SGSMEPTLLVGDRLLVNKLSYGFGEPKRGDIVVFKYPEDPSKDYIKRVIGLPGDTVeirdgqvyvngkplnepylEEYYY 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1691716723  99 SDFFKSHSYVPRGHVWLEGDNLQNSTDSRYYGPIPYGLIRGRIFF 143
Cdd:COG0681   120 PVSVDGDVEVPPGEEEVPGGGGDNSNDSRSGDPDDGGGGVGVDGV 164
PRK10861 PRK10861
signal peptidase I;
37-133 2.49e-09

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 56.60  E-value: 2.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691716723  37 SGpSMEPTIQNSDIVFAENLSrhfYGI---------------QRGDIVIAKSPSDPKSNICKRVIGLEGDKI-------- 93
Cdd:PRK10861   89 SG-SMMPTLLIGDFILVEKFA---YGIkdpitqttlietghpKRGDIVVFKYPEDPKLDYIKRVVGLPGDKVtydpvske 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691716723  94 ------------------LTTS---PSDFFKSHSY--------------------------------------------- 107
Cdd:PRK10861  165 vtiqpgcssgqacenalpVTYSnvePSDFVQTFSRrnggeatsgffqvplnetkengirlserketlgdvthriltvpga 244

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1691716723 108 -------------------VPRGHVWLEGDNLQNSTDSRYYGPIP 133
Cdd:PRK10861  245 qdqvgmyyqqpgqplatwvVPPGQYFMMGDNRDNSADSRYWGFVP 289
 
Name Accession Description Interval E-value
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 33-141 2.40e-35

The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4.21.89) family members are essential membrane-bound serine proteases that function to cleave the amino-terminal signal peptide extension from proteins that are translocated across biological membranes. The bacterial signal peptidase I, which is the most intensively studied, has two N-terminal transmembrane segments inserted in the plasma membrane and a hydrophilic, C-terminal catalytic region that is located in the periplasmic space. Although the bacterial signal peptidase I is monomeric, signal peptidases of eukaryotic cells commonly function as oligomeric complexes containing two divergent copies of the catalytic monomer. These are the IMP1 and IMP2 signal peptidases of the mitochondrial inner membrane that remove leader peptides from nuclear- and mitochondrial-encoded proteins. Also, two components of the endoplasmic reticulum signal peptidase in mammals (18-kDa and 21-kDa) belong to this family and they process many proteins that enter the ER for retention or for export to the Golgi apparatus, secretory vesicles, plasma membranes or vacuole. An atypical member of the S26 SPase type I family is the TraF peptidase which has the remarkable activity of producing a cyclic protein of the Pseudomonas pilin system. The type I signal peptidases are unique serine proteases that utilize a serine/lysine catalytic dyad mechanism in place of the classical serine/histidine/aspartic acid catalytic triad mechanism.


Pssm-ID: 119398 [Multi-domain]  Cd Length: 85  Bit Score: 120.77  E-value: 2.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691716723  33 VVMCSGPSMEPTIQNSDIVFAENLSRHFYGIQRGDIVIAKSPSDPKSNICKRVIGlegdkilttspsdffkshsyvprgh 112
Cdd:cd06530     2 PVVVPGGSMEPTLQPGDLVLVNKLSYGFREPKRGDVVVFKSPGDPGKPIIKRVIG------------------------- 56

                          90       100
                  ....*....|....*....|....*....
gi 1691716723 113 VWLEGDNLQNSTDSRYYGPIPYGLIRGRI 141
Cdd:cd06530    57 YFVLGDNRNNSLDSRYWGPVPEDDIVGKV 85
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 29-145 3.16e-32

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: 114.63  E-value: 3.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691716723  29 YVGGVVMCSGPSMEPTIQNSDIVFAENLSRHFYGIQRGDIVIAKSPSDPKSNICKRVIGLEGDKI--------------- 93
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFAYRTSDPKRGDIVVFKDPDTNKNIYVKRIIGLPGDKVefrdgklyingkkid 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1691716723  94 ---LTTSPSDFFKSHSY---VPRGHVWLEGDNLQNSTDSRYYGPIPYGLIRGRIFFKL 145
Cdd:TIGR02227  81 epyLKPNGYLDTSEFNTpvkVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVF 138
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 38-145 2.07e-26

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: 100.36  E-value: 2.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691716723  38 GPSMEPTIQNSDIVFAENLSRHFYGIQRGDIVIAKSPSDPKSNICKRVIGLEGDKI------LT---------------- 95
Cdd:pfam10502  30 GGSMSPTLPIGDYLIVNKFSYGLGEPKRGDIVVFRPPEGPGVPLIKRVIGLPGDRVeykddqLYingkpvgepyladrkg 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1691716723  96 TSPSDF--FKSHSYVPRGHVWLEGDNLQNSTDSRYYGPIPYGLIRGRIFFKL 145
Cdd:pfam10502 110 RPTFDLppWQGCRVVPEGEYFVMGDNRDNSLDSRYFGFVPASNIVGRAVFPV 161
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 33-141 1.53e-22

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.


Pssm-ID: 119396 [Multi-domain]  Cd Length: 84  Bit Score: 87.70  E-value: 1.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691716723  33 VVMCSGPSMEPTIQNSDIVFAEnlsRHFYGIQRGDIVIAKSPSDpkSNICKRVIGLEGDkilttspsdffkshsyvprGH 112
Cdd:cd06462     2 ALRVEGDSMEPTIPDGDLVLVD---KSSYEPKRGDIVVFRLPGG--ELTVKRVIGLPGE-------------------GH 57

                          90       100
                  ....*....|....*....|....*....
gi 1691716723 113 VWLEGDNlQNSTDSRYYGPiPYGLIRGRI 141
Cdd:cd06462    58 YFLLGDN-PNSPDSRIDGP-PELDIVGVV 84
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
38-143 2.73e-17

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 76.81  E-value: 2.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691716723  38 GPSMEPTIQNSDIVFAENLSRHFYGIQRGDIVIAKSPSDPKSNICKRVIGLEGDKI-------------------LTTSP 98
Cdd:COG0681    40 SGSMEPTLLVGDRLLVNKLSYGFGEPKRGDIVVFKYPEDPSKDYIKRVIGLPGDTVeirdgqvyvngkplnepylEEYYY 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1691716723  99 SDFFKSHSYVPRGHVWLEGDNLQNSTDSRYYGPIPYGLIRGRIFF 143
Cdd:COG0681   120 PVSVDGDVEVPPGEEEVPGGGGDNSNDSRSGDPDDGGGGVGVDGV 164
sod_Ni_protease TIGR02754
nickel-type superoxide dismutase maturation protease; Members of this protein family are ...
 38-141 3.72e-13

nickel-type superoxide dismutase maturation protease; Members of this protein family are apparent proteases encoded adjacent to the genes for a nickel-type superoxide dismutase. This family belongs to the same larger family (see pfam00717) as signal peptidase I, an unusual serine protease suggested to have a Ser/Lys catalytic dyad. [Cellular processes, Detoxification, Protein fate, Protein modification and repair]


Pssm-ID: 274282 [Multi-domain]  Cd Length: 90  Bit Score: 63.24  E-value: 3.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691716723  38 GPSMEPTIQNSDIVFAENLSRHFYGIQRGDIVIAKSPSDPKSNICKRVIGlegdkilttspsdffkshsyVPRGHVWLEG 117
Cdd:TIGR02754   5 GVSMSPTLPPGDRIIVVPWLKIFRVPPIGNVVVVRHPLQPYGLIIKRLAA--------------------VDDNGLFLLG 64

                          90       100
                  ....*....|....*....|....
gi 1691716723 118 DNLQNSTDSRYYGPIPYGLIRGRI 141
Cdd:TIGR02754  65 DNPKASTDSRQLGPVPRSLLLGKV 88
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 65-143 7.22e-11

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: 57.61  E-value: 7.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691716723  65 RGDIVIAKSPSDPKSNIC---------KRVIGLEGDKI-------------LTTS--------PSDFFKSHSYVPRGHVW 114
Cdd:COG4959     1 RGDLVAFRPPEPLAAERGylprgvpliKRVAALPGDTVcikggqvyingkpVAEAlerdragrPLPVWQGCGVVPEGEYF 80

                          90       100
                  ....*....|....*....|....*....
gi 1691716723 115 LEGDNLQNSTDSRYYGPIPYGLIRGRIFF 143
Cdd:COG4959    81 LLGDNRPNSFDSRYFGPVPRSQIIGRAVP 109
PRK10861 PRK10861
signal peptidase I;
37-133 2.49e-09

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 56.60  E-value: 2.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691716723  37 SGpSMEPTIQNSDIVFAENLSrhfYGI---------------QRGDIVIAKSPSDPKSNICKRVIGLEGDKI-------- 93
Cdd:PRK10861   89 SG-SMMPTLLIGDFILVEKFA---YGIkdpitqttlietghpKRGDIVVFKYPEDPKLDYIKRVVGLPGDKVtydpvske 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691716723  94 ------------------LTTS---PSDFFKSHSY--------------------------------------------- 107
Cdd:PRK10861  165 vtiqpgcssgqacenalpVTYSnvePSDFVQTFSRrnggeatsgffqvplnetkengirlserketlgdvthriltvpga 244

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1691716723 108 -------------------VPRGHVWLEGDNLQNSTDSRYYGPIP 133
Cdd:PRK10861  245 qdqvgmyyqqpgqplatwvVPPGQYFMMGDNRDNSADSRYWGFVP 289
sigpep_I_arch TIGR02228
signal peptidase I, archaeal type; This model represents signal peptidase I from most archaea, ...
 32-87 7.05e-05

signal peptidase I, archaeal type; This model represents signal peptidase I from most archaea, a subunit of the eukaryotic endoplasmic reticulum signal peptidase I complex, and an apparent signal peptidase I from a small number of bacteria. It is related to but does not overlap in hits with TIGR02227, the bacterial and mitochondrial signal peptidase I.


Pssm-ID: 131283  Cd Length: 158  Bit Score: 42.04  E-value: 7.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1691716723  32 GVVMCSGPSMEPTIQNSDIVFAEnlSRHFYGIQRGDIVIAKSPSDPKSnICKRVIG 87
Cdd:TIGR02228  32 PVVVVLSGSMEPTFNTGDLILVT--GADPNDIQVGDVITYKSPGFNTP-VTHRVIE 84
TraF_Ti TIGR02771
conjugative transfer signal peptidase TraF; This protein is found in apparent operons encoding ...
 63-141 8.88e-04

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: 39.00  E-value: 8.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691716723  63 IQRGDIVIAKSPSDP-----------KSNIC--------KRVIGLEGDKILTTS----------PSDFFKSHS------- 106
Cdd:TIGR02771  47 VERGDYVVFCPPDNPqfeearergylREGLCpggfgpllKRVLGLPGDRVTVRAdvvaingqllPYSKPLATDssgrplp 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1691716723 107 -----YVPRGHVWLEGDNLQnSTDSRYYGPIPYGLIRGRI 141
Cdd:TIGR02771 127 pfpegVIPPGFFVVHDTSPT-SFDSRYFGPISREQVIGRV 165
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 33-93 2.59e-03

Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: prophages, transposons];


Pssm-ID: 442176  Cd Length: 121  Bit Score: 36.86  E-value: 2.59e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1691716723  33 VVMCSGPSMEPTIQNSDIVFAEnlsRHFYGIQRGDIVIAKspsDPKSNICKRVIGLEGDKI 93
Cdd:COG2932    37 AVRVSGDSMEPTIRDGDIVLVD---PSDTEIRDGGIYVVR---TDGELLVKRLQRRPDGKL 91
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 33-93 3.23e-03

Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of single-stranded DNA within the bacterial cell. This family includes: 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 LexA-like proteins contain two-domains: an N-terminal DNA binding domain and a C-terminal domain (CTD) that provides LexA dimerization as well as cleavage activity. They undergo autolysis, cleaving at an Ala-Gly or a Cys-Gly bond, separating the DNA-binding domain from the rest of the protein. In the presence of single-stranded DNA, the LexA, UmuD and MucA proteins interact with RecA, activating self cleavage, thus either derepressing transcription in the case of LexA or activating the lesion-bypass polymerase in the case of UmuD and MucA. The LexA proteins are 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. LexA sequence homologs are found in almost all of the bacterial genomes sequenced to date, covering a large number of phyla, suggesting both, an ancient origin and a widespread distribution of lexA and the SOS response.


Pssm-ID: 119397 [Multi-domain]  Cd Length: 81  Bit Score: 35.61  E-value: 3.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1691716723  33 VVMCSGPSMEPTIQNSDIVFAeNLSRHfygIQRGDIVIAKSPSDPksnICKRVIGLEGDKI 93
Cdd:cd06529     2 ALRVKGDSMEPTIPDGDLVLV-DPSDT---PRDGDIVVARLDGEL---TVKRLQRRGGGRL 55
Peptidase_S24 pfam00717
Peptidase S24-like;
33-93 7.05e-03

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 35.26  E-value: 7.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1691716723  33 VVMCSGPSMEPTIQNSDIVFAENlSRHfygIQRGDIVIAKSPSDPksnICKRVIgLEGDKI 93
Cdd:pfam00717  37 ALRVKGDSMEPGIPDGDLVLVDP-SRE---ARNGDIVVARLDGEA---TVKRLY-RDGGGI 89
 
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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