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Conserved domains on  [gi|1229776473|ref|XP_022141359|]
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chloroplast processing peptidase-like isoform X1 [Momordica charantia]

Protein Classification

S26 family signal peptidase( domain architecture ID 12106434)

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

EC:  3.4.21.-
Gene Ontology:  GO:0004252|GO:0006465|GO:0016020|GO:0006508|GO:0008236
MEROPS:  S26
PubMed:  22031009|16126156|10982814

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 37-179 1.13e-47

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: 153.13  E-value: 1.13e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473  37 FLVVLILWSMLLEIHYIPSSSMYPTLRVGDRILVEKASYYIRNPAIDDIITFRDPTqqsgRREENIVvKRVVATSGDMVE 116
Cdd:pfam10502  12 LLLALLIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGLGEPKRGDIVVFRPPE----GPGVPLI-KRVIGLPGDRVE 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473 117 VCEGCLYVNGIAQKENFLADQPTYTTKS-------TQVPEGHVYVLGDNRNNSYDSHIWGPLPIKNIVGR 179
Cdd:pfam10502  87 YKDDQLYINGKPVGEPYLADRKGRPTFDlppwqgcRVVPEGEYFVMGDNRDNSLDSRYFGFVPASNIVGR 156
 
Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 37-179 1.13e-47

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: 153.13  E-value: 1.13e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473  37 FLVVLILWSMLLEIHYIPSSSMYPTLRVGDRILVEKASYYIRNPAIDDIITFRDPTqqsgRREENIVvKRVVATSGDMVE 116
Cdd:pfam10502  12 LLLALLIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGLGEPKRGDIVVFRPPE----GPGVPLI-KRVIGLPGDRVE 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473 117 VCEGCLYVNGIAQKENFLADQPTYTTKS-------TQVPEGHVYVLGDNRNNSYDSHIWGPLPIKNIVGR 179
Cdd:pfam10502  87 YKDDQLYINGKPVGEPYLADRKGRPTFDlppwqgcRVVPEGEYFVMGDNRDNSLDSRYFGFVPASNIVGR 156
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 47-182 2.96e-41

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: 136.20  E-value: 2.96e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473  47 LLEIHYIPSSSMYPTLRVGDRILVEKASYYIRNPAIDDIITFRDPTQqsgrrEENIVVKRVVATSGDMVEVCEGCLYVNG 126
Cdd:TIGR02227   2 VFFPYKIPGGSMEPTLKEGDRILVNKFAYRTSDPKRGDIVVFKDPDT-----NKNIYVKRIIGLPGDKVEFRDGKLYING 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473 127 IAQKENFLADQPTYTTKSTQ----VPEGHVYVLGDNRNNSYDSHIWGPLPIKNIVGRYLW 182
Cdd:TIGR02227  77 KKIDEPYLKPNGYLDTSEFNtpvkVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSF 136
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
34-178 7.56e-31

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 111.10  E-value: 7.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473  34 LFRFLVVLILWSMLLEIHYIPSSSMYPTLRVGDRILVEKASYYIRNPAIDDIITFRDPTQqsgrrEENIVVKRVVATSGD 113
Cdd:COG0681    19 VIALLLALLIRTFVFEPFVIPSGSMEPTLLVGDRLLVNKLSYGFGEPKRGDIVVFKYPED-----PSKDYIKRVIGLPGD 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473 114 MVEVCEGCLYVNGIAQKENFLADQ-----PTYTTKSTQVPEGHVYVLGDNRNNSYDSHIWGPLPIKNIVG 178
Cdd:COG0681    94 TVEIRDGQVYVNGKPLNEPYLEEYyypvsVDGDVEVPPGEEEVPGGGGDNSNDSRSGDPDDGGGGVGVDG 163
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 49-179 5.26e-26

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: 95.35  E-value: 5.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473  49 EIHYIPSSSMYPTLRVGDRILVEKASYYIRNPAIDDIITFRDPtqqsgRREENIVVKRVVAtsgdmvevcegclyvngia 128
Cdd:cd06530     1 EPVVVPGGSMEPTLQPGDLVLVNKLSYGFREPKRGDVVVFKSP-----GDPGKPIIKRVIG------------------- 56

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1229776473 129 qkenfladqptyttkstqvpeghVYVLGDNRNNSYDSHIWGPLPIKNIVGR 179
Cdd:cd06530    57 -----------------------YFVLGDNRNNSLDSRYWGPVPEDDIVGK 84
PRK10861 PRK10861
signal peptidase I;
38-179 1.13e-19

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 84.34  E-value: 1.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473  38 LVVLILWSMLLEIHYIPSSSMYPTLRVGDRILVEKASYYIRNPAID------------DIITFRDPTQQSGRreeniVVK 105
Cdd:PRK10861   72 AIVLIVRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAYGIKDPITQttlietghpkrgDIVVFKYPEDPKLD-----YIK 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473 106 RVVATSGDMV------------------EVCEGCLYV------------------------------------NGIAQKE 131
Cdd:PRK10861  147 RVVGLPGDKVtydpvskevtiqpgcssgQACENALPVtysnvepsdfvqtfsrrnggeatsgffqvplnetkeNGIRLSE 226

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473 132 ----------NFLA-----DQP-TYTTKSTQ------VPEGHVYVLGDNRNNSYDSHIWGPLPIKNIVGR 179
Cdd:PRK10861  227 rketlgdvthRILTvpgaqDQVgMYYQQPGQplatwvVPPGQYFMMGDNRDNSADSRYWGFVPEANLVGK 296
 
Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 37-179 1.13e-47

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: 153.13  E-value: 1.13e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473  37 FLVVLILWSMLLEIHYIPSSSMYPTLRVGDRILVEKASYYIRNPAIDDIITFRDPTqqsgRREENIVvKRVVATSGDMVE 116
Cdd:pfam10502  12 LLLALLIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGLGEPKRGDIVVFRPPE----GPGVPLI-KRVIGLPGDRVE 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473 117 VCEGCLYVNGIAQKENFLADQPTYTTKS-------TQVPEGHVYVLGDNRNNSYDSHIWGPLPIKNIVGR 179
Cdd:pfam10502  87 YKDDQLYINGKPVGEPYLADRKGRPTFDlppwqgcRVVPEGEYFVMGDNRDNSLDSRYFGFVPASNIVGR 156
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 47-182 2.96e-41

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: 136.20  E-value: 2.96e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473  47 LLEIHYIPSSSMYPTLRVGDRILVEKASYYIRNPAIDDIITFRDPTQqsgrrEENIVVKRVVATSGDMVEVCEGCLYVNG 126
Cdd:TIGR02227   2 VFFPYKIPGGSMEPTLKEGDRILVNKFAYRTSDPKRGDIVVFKDPDT-----NKNIYVKRIIGLPGDKVEFRDGKLYING 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473 127 IAQKENFLADQPTYTTKSTQ----VPEGHVYVLGDNRNNSYDSHIWGPLPIKNIVGRYLW 182
Cdd:TIGR02227  77 KKIDEPYLKPNGYLDTSEFNtpvkVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSF 136
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
34-178 7.56e-31

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 111.10  E-value: 7.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473  34 LFRFLVVLILWSMLLEIHYIPSSSMYPTLRVGDRILVEKASYYIRNPAIDDIITFRDPTQqsgrrEENIVVKRVVATSGD 113
Cdd:COG0681    19 VIALLLALLIRTFVFEPFVIPSGSMEPTLLVGDRLLVNKLSYGFGEPKRGDIVVFKYPED-----PSKDYIKRVIGLPGD 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473 114 MVEVCEGCLYVNGIAQKENFLADQ-----PTYTTKSTQVPEGHVYVLGDNRNNSYDSHIWGPLPIKNIVG 178
Cdd:COG0681    94 TVEIRDGQVYVNGKPLNEPYLEEYyypvsVDGDVEVPPGEEEVPGGGGDNSNDSRSGDPDDGGGGVGVDG 163
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 49-179 5.26e-26

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: 95.35  E-value: 5.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473  49 EIHYIPSSSMYPTLRVGDRILVEKASYYIRNPAIDDIITFRDPtqqsgRREENIVVKRVVAtsgdmvevcegclyvngia 128
Cdd:cd06530     1 EPVVVPGGSMEPTLQPGDLVLVNKLSYGFREPKRGDVVVFKSP-----GDPGKPIIKRVIG------------------- 56

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1229776473 129 qkenfladqptyttkstqvpeghVYVLGDNRNNSYDSHIWGPLPIKNIVGR 179
Cdd:cd06530    57 -----------------------YFVLGDNRNNSLDSRYWGPVPEDDIVGK 84
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 84-179 6.89e-23

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: 88.04  E-value: 6.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473  84 DIITFRDP----TQQSGRREENIVVKRVVATSGDMVEVCEGCLYVNGIAQKENFLAD----QPTYTTKSTQVPEGHVYVL 155
Cdd:COG4959     3 DLVAFRPPeplaAERGYLPRGVPLIKRVAALPGDTVCIKGGQVYINGKPVAEALERDragrPLPVWQGCGVVPEGEYFLL 82

                          90       100
                  ....*....|....*....|....
gi 1229776473 156 GDNRNNSYDSHIWGPLPIKNIVGR 179
Cdd:COG4959    83 GDNRPNSFDSRYFGPVPRSQIIGR 106
PRK10861 PRK10861
signal peptidase I;
38-179 1.13e-19

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 84.34  E-value: 1.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473  38 LVVLILWSMLLEIHYIPSSSMYPTLRVGDRILVEKASYYIRNPAID------------DIITFRDPTQQSGRreeniVVK 105
Cdd:PRK10861   72 AIVLIVRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAYGIKDPITQttlietghpkrgDIVVFKYPEDPKLD-----YIK 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473 106 RVVATSGDMV------------------EVCEGCLYV------------------------------------NGIAQKE 131
Cdd:PRK10861  147 RVVGLPGDKVtydpvskevtiqpgcssgQACENALPVtysnvepsdfvqtfsrrnggeatsgffqvplnetkeNGIRLSE 226

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473 132 ----------NFLA-----DQP-TYTTKSTQ------VPEGHVYVLGDNRNNSYDSHIWGPLPIKNIVGR 179
Cdd:PRK10861  227 rketlgdvthRILTvpgaqDQVgMYYQQPGQplatwvVPPGQYFMMGDNRDNSADSRYWGFVPEANLVGK 296
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 52-179 1.86e-15

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: 68.06  E-value: 1.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473  52 YIPSSSMYPTLRVGDRILVEKASYYIRNpaiDDIITFRDPtqqsgrrEENIVVKRVVATSGdmvevcegclyvngiaqke 131
Cdd:cd06462     4 RVEGDSMEPTIPDGDLVLVDKSSYEPKR---GDIVVFRLP-------GGELTVKRVIGLPG------------------- 54

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1229776473 132 nfladqptyttkstqvpEGHVYVLGDNrNNSYDSHIWGPlPIKNIVGR 179
Cdd:cd06462    55 -----------------EGHYFLLGDN-PNSPDSRIDGP-PELDIVGV 83
sod_Ni_protease TIGR02754
nickel-type superoxide dismutase maturation protease; Members of this protein family are ...
 57-182 1.45e-09

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: 52.84  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473  57 SMYPTLRVGDRILVEKASYYIRNPAIDDIITFRDPTQQSGRreeniVVKRVVatsgdmvevcegclyvngiaqkenflad 136
Cdd:TIGR02754   7 SMSPTLPPGDRIIVVPWLKIFRVPPIGNVVVVRHPLQPYGL-----IIKRLA---------------------------- 53

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1229776473 137 qptyttkstQVPEGHVYVLGDNRNNSYDSHIWGPLPIKNIVGRYLW 182
Cdd:TIGR02754  54 ---------AVDDNGLFLLGDNPKASTDSRQLGPVPRSLLLGKVLW 90
sigpep_I_arch TIGR02228
signal peptidase I, archaeal type; This model represents signal peptidase I from most archaea, ...
 55-181 5.13e-04

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: 38.96  E-value: 5.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473  55 SSSMYPTLRVGDRILVEKASYyiRNPAIDDIITFRDPTqqsgrrEENIVVKRVVatsgdmvevcegclyvngiaqKENFL 134
Cdd:TIGR02228  38 SGSMEPTFNTGDLILVTGADP--NDIQVGDVITYKSPG------FNTPVTHRVI---------------------EINNS 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1229776473 135 ADQPTYTTKstqvpeghvyvlGDNrNNSYDSHiwgPLPIKNIVGRYL 181
Cdd:TIGR02228  89 GGELGFITK------------GDN-NPAPDGE---PVPSENVIGKYL 119
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 57-117 5.97e-04

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


Pssm-ID: 442176  Cd Length: 121  Bit Score: 38.02  E-value: 5.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229776473  57 SMYPTLRVGDRILVEKASYYIRNpaiDDIITFRDptqqsgrrEENIVVKRVVATSGDMVEV 117
Cdd:COG2932    44 SMEPTIRDGDIVLVDPSDTEIRD---GGIYVVRT--------DGELLVKRLQRRPDGKLRL 93
PRK13838 PRK13838
conjugal transfer pilin processing protease TraF; Provisional
 104-178 4.95e-03

conjugal transfer pilin processing protease TraF; Provisional


Pssm-ID: 172365 [Multi-domain]  Cd Length: 176  Bit Score: 36.12  E-value: 4.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473 104 VKRVVATSGDMVEVCEGcLYVNGIAQKENFLADQ-----PTYTTKSTQVPEGHVYVLGDNRNnSYDSHIWGPLPIKNIVG 178
Cdd:PRK13838   89 IKTVAALAGQRVEIGGS-VSIDGRPLPSSSVRRRdgegrPLTPFPGGVVPPGHLFLHSSFAG-SYDSRYFGPVPASGLLG 166
PRK13884 PRK13884
conjugal transfer peptidase TraF; Provisional
 70-178 6.34e-03

conjugal transfer peptidase TraF; Provisional


Pssm-ID: 184368  Cd Length: 178  Bit Score: 35.77  E-value: 6.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229776473  70 VEKASYYIRNPaiDDIITFRDptqqsGRREENI-----------VVKRVVATSGDMVEVCEGCLYVNG--IAQKENFLAD 136
Cdd:PRK13884   51 VEKGAYVLFCP--PQRGVFDD-----AKERGYIgagfcpggygyMMKRVLAAKGDAVSVTDDGVRVNGelLPLSKPILAD 123

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1229776473 137 Q-----PTYTTKSTQVPEGHVYVLGDNRNNSYDSHIWGPLPIKNIVG 178
Cdd:PRK13884  124 GagrplPRYQANSYTLGESELLLMSDVSATSFDGRYFGPINRSQIKT 170
 
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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