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Conserved domains on  [gi|54039634|sp|P67812|]
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RecName: Full=Signal peptidase complex catalytic subunit SEC11A; AltName: Full=Endopeptidase SP18; AltName: Full=Microsomal signal peptidase 18 kDa subunit; Short=SPase 18 kDa subunit; AltName: Full=SEC11 homolog A; AltName: Full=SEC11-like protein 1; AltName: Full=SPC18

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 ...
 38-150 1.56e-24

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 TIGR02228:

Pssm-ID: 447902  Cd Length: 158  Bit Score: 93.27  E-value: 1.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54039634    38 GLMVITGSESPIVVVLSGSMEPAFHRGDLLFLTNRVEDPIRVGEIVVFRIEGREIPIVHRVLKIhEKQNGHIKFLTKGDN 117
Cdd:TIGR02228  22 GLVSKASGPDPVVVVLSGSMEPTFNTGDLILVTGADPNDIQVGDVITYKSPGFNTPVTHRVIEI-NNSGGELGFITKGDN 100

                          90       100       110
                  ....*....|....*....|....*....|...
gi 54039634   118 NAVDDrglykqgQHWLEKKDVVGRARGFVPYIG 150
Cdd:TIGR02228 101 NPAPD-------GEPVPSENVIGKYLGFTIPFA 126
 
Name Accession Description Interval E-value
sigpep_I_arch TIGR02228
signal peptidase I, archaeal type; This model represents signal peptidase I from most archaea, ...
 38-150 1.56e-24

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: 93.27  E-value: 1.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54039634    38 GLMVITGSESPIVVVLSGSMEPAFHRGDLLFLTNRVEDPIRVGEIVVFRIEGREIPIVHRVLKIhEKQNGHIKFLTKGDN 117
Cdd:TIGR02228  22 GLVSKASGPDPVVVVLSGSMEPTFNTGDLILVTGADPNDIQVGDVITYKSPGFNTPVTHRVIEI-NNSGGELGFITKGDN 100

                          90       100       110
                  ....*....|....*....|....*....|...
gi 54039634   118 NAVDDrglykqgQHWLEKKDVVGRARGFVPYIG 150
Cdd:TIGR02228 101 NPAPD-------GEPVPSENVIGKYLGFTIPFA 126
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 48-142 3.56e-18

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: 74.93  E-value: 3.56e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54039634  48 PIVVVLSGSMEPAFHRGDLLFLTN--RVEDPIRVGEIVVFRIEGR-EIPIVHRVlkihekqnghIKFLTKGDN--NAVDD 122
Cdd:cd06530   1 EPVVVPGGSMEPTLQPGDLVLVNKlsYGFREPKRGDVVVFKSPGDpGKPIIKRV----------IGYFVLGDNrnNSLDS 70

                        90       100
                ....*....|....*....|
gi 54039634 123 RGLYKqgqhwLEKKDVVGRA 142
Cdd:cd06530  71 RYWGP-----VPEDDIVGKV 85
Peptidase_S24 pfam00717
Peptidase S24-like;
40-123 6.89e-07

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 46.04  E-value: 6.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54039634    40 MVITGSESPIVVVLSGSMEPAFHRGDLLFLtnRVEDPIRVGEIVVFRIEGreIPIVHRVlkihEKQNGHIKFLTkgDNNA 119
Cdd:pfam00717  28 LLSPPGNLFALRVKGDSMEPGIPDGDLVLV--DPSREARNGDIVVARLDG--EATVKRL----YRDGGGIRLIS--LNPE 97


                  ....
gi 54039634   120 VDDR 123
Cdd:pfam00717  98 YPPI 101
 
Name Accession Description Interval E-value
sigpep_I_arch TIGR02228
signal peptidase I, archaeal type; This model represents signal peptidase I from most archaea, ...
 38-150 1.56e-24

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: 93.27  E-value: 1.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54039634    38 GLMVITGSESPIVVVLSGSMEPAFHRGDLLFLTNRVEDPIRVGEIVVFRIEGREIPIVHRVLKIhEKQNGHIKFLTKGDN 117
Cdd:TIGR02228  22 GLVSKASGPDPVVVVLSGSMEPTFNTGDLILVTGADPNDIQVGDVITYKSPGFNTPVTHRVIEI-NNSGGELGFITKGDN 100

                          90       100       110
                  ....*....|....*....|....*....|...
gi 54039634   118 NAVDDrglykqgQHWLEKKDVVGRARGFVPYIG 150
Cdd:TIGR02228 101 NPAPD-------GEPVPSENVIGKYLGFTIPFA 126
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 48-142 3.56e-18

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: 74.93  E-value: 3.56e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54039634  48 PIVVVLSGSMEPAFHRGDLLFLTN--RVEDPIRVGEIVVFRIEGR-EIPIVHRVlkihekqnghIKFLTKGDN--NAVDD 122
Cdd:cd06530   1 EPVVVPGGSMEPTLQPGDLVLVNKlsYGFREPKRGDVVVFKSPGDpGKPIIKRV----------IGYFVLGDNrnNSLDS 70

                        90       100
                ....*....|....*....|
gi 54039634 123 RGLYKqgqhwLEKKDVVGRA 142
Cdd:cd06530  71 RYWGP-----VPEDDIVGKV 85
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 48-142 1.44e-14

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: 65.36  E-value: 1.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54039634  48 PIVVVLSGSMEPAFHRGDLLFLtNRVEDPIRVGEIVVFRIEGREiPIVHRVLKIHekqnGHIKFLTKGDNNAVDDRGLYK 127
Cdd:cd06462   1 FALRVEGDSMEPTIPDGDLVLV-DKSSYEPKRGDIVVFRLPGGE-LTVKRVIGLP----GEGHYFLLGDNPNSPDSRIDG 74

                        90
                ....*....|....*
gi 54039634 128 qgqhwLEKKDVVGRA 142
Cdd:cd06462  75 -----PPELDIVGVV 84
Peptidase_S24 pfam00717
Peptidase S24-like;
40-123 6.89e-07

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 46.04  E-value: 6.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54039634    40 MVITGSESPIVVVLSGSMEPAFHRGDLLFLtnRVEDPIRVGEIVVFRIEGreIPIVHRVlkihEKQNGHIKFLTkgDNNA 119
Cdd:pfam00717  28 LLSPPGNLFALRVKGDSMEPGIPDGDLVLV--DPSREARNGDIVVARLDG--EATVKRL----YRDGGGIRLIS--LNPE 97


                  ....
gi 54039634   120 VDDR 123
Cdd:pfam00717  98 YPPI 101
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 56-90 9.09e-04

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: 36.38  E-value: 9.09e-04
                        10        20        30
                ....*....|....*....|....*....|....*
gi 54039634  56 SMEPAFHRGDLLFLtnRVEDPIRVGEIVVFRIEGR 90
Cdd:cd06529   9 SMEPTIPDGDLVLV--DPSDTPRDGDIVVARLDGE 41
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 49-86 7.58e-03

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: 35.28  E-value: 7.58e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 54039634    49 IVVVLSGSMEPAFHRGDLLFLT--NRVEDPIRVGEIVVFR 86
Cdd:TIGR02227   5 PYKIPGGSMEPTLKEGDRILVNkfAYRTSDPKRGDIVVFK 44
 
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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