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Conserved domains on  [gi|386764495|ref|NP_001245694|]
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uncharacterized protein Dmel_CG9240, isoform B [Drosophila melanogaster]

Protein Classification

S26 family signal peptidase( domain architecture ID 1000376)

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

CATH:  2.10.109.10
EC:  3.4.21.-
Gene Ontology:  GO:0006465|GO:0004252
PubMed:  7845208|12475201

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
sigpep_I_bact super family cl37079
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 1-121 9.18e-24

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]


The actual alignment was detected with superfamily member TIGR02227:

Pssm-ID: 274044 [Multi-domain]  Cd Length: 142  Bit Score: 89.21  E-value: 9.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764495    1 MEPTLHSDNVLLTERLSKHWRTYQPGDIVIAISPIKADQFICKRIVAVSGDQVLIQ--------KPIPiEAEFSGNSDDK 72
Cdd:TIGR02227  13 MEPTLKEGDRILVNKFAYRTSDPKRGDIVVFKDPDTNKNIYVKRIIGLPGDKVEFRdgklyingKKID-EPYLKPNGYLD 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 386764495   73 KKPVMVKDYVPRGHVWIEGDNKGNSSDSRYYGPIPVGLIRSRVLCRIWP 121
Cdd:TIGR02227  92 TSEFNTPVKVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVFYP 140
 
Name Accession Description Interval E-value
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 1-121 9.18e-24

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: 89.21  E-value: 9.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764495    1 MEPTLHSDNVLLTERLSKHWRTYQPGDIVIAISPIKADQFICKRIVAVSGDQVLIQ--------KPIPiEAEFSGNSDDK 72
Cdd:TIGR02227  13 MEPTLKEGDRILVNKFAYRTSDPKRGDIVVFKDPDTNKNIYVKRIIGLPGDKVEFRdgklyingKKID-EPYLKPNGYLD 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 386764495   73 KKPVMVKDYVPRGHVWIEGDNKGNSSDSRYYGPIPVGLIRSRVLCRIWP 121
Cdd:TIGR02227  92 TSEFNTPVKVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVFYP 140
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 1-120 6.10e-21

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: 82.25  E-value: 6.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764495    1 MEPTLHSDNVLLTERLSKHWRTYQPGDIVIAISPIKADQFICKRIVAVSGDQVLIQ--------KPI--PIEAEFSGNSD 70
Cdd:pfam10502  33 MSPTLPIGDYLIVNKFSYGLGEPKRGDIVVFRPPEGPGVPLIKRVIGLPGDRVEYKddqlyingKPVgePYLADRKGRPT 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 386764495   71 DKKKPVMVKDYVPRGHVWIEGDNKGNSSDSRYYGPIPVGLIRSRVLCRIW 120
Cdd:pfam10502 113 FDLPPWQGCRVVPEGEYFVMGDNRDNSLDSRYFGFVPASNIVGRAVFPVW 162
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 1-115 1.31e-20

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: 79.17  E-value: 1.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764495   1 MEPTLHSDNVLLTERLSKHWRTYQPGDIVIAISPIKADQFICKRIVAvsgdqvliqkpipieaefsgnsddkkkpvmvkd 80
Cdd:cd06530   10 MEPTLQPGDLVLVNKLSYGFREPKRGDVVVFKSPGDPGKPIIKRVIG--------------------------------- 56

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 386764495  81 yvprghVWIEGDNKGNSSDSRYYGPIPVGLIRSRV 115
Cdd:cd06530   57 ------YFVLGDNRNNSLDSRYWGPVPEDDIVGKV 85
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 25-121 3.05e-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: 56.07  E-value: 3.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764495  25 PGDIVIAISPIKADQFICKRIVAVSGDQVLIQ--------KPIPIEAEFSgnSDDKKKPVMVKDY-VPRGHVWIEGDNKG 95
Cdd:COG4959   10 PEPLAAERGYLPRGVPLIKRVAALPGDTVCIKggqvyingKPVAEALERD--RAGRPLPVWQGCGvVPEGEYFLLGDNRP 87

                         90       100
                 ....*....|....*....|....*.
gi 386764495  96 NSSDSRYYGPIPVGLIRSRVLCRIWP 121
Cdd:COG4959   88 NSFDSRYFGPVPRSQIIGRAVPLWTP 113
PRK10861 PRK10861
signal peptidase I;
82-107 1.45e-05

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 42.73  E-value: 1.45e-05
                         10        20
                 ....*....|....*....|....*.
gi 386764495  82 VPRGHVWIEGDNKGNSSDSRYYGPIP 107
Cdd:PRK10861 264 VPPGQYFMMGDNRDNSADSRYWGFVP 289
 
Name Accession Description Interval E-value
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 1-121 9.18e-24

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: 89.21  E-value: 9.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764495    1 MEPTLHSDNVLLTERLSKHWRTYQPGDIVIAISPIKADQFICKRIVAVSGDQVLIQ--------KPIPiEAEFSGNSDDK 72
Cdd:TIGR02227  13 MEPTLKEGDRILVNKFAYRTSDPKRGDIVVFKDPDTNKNIYVKRIIGLPGDKVEFRdgklyingKKID-EPYLKPNGYLD 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 386764495   73 KKPVMVKDYVPRGHVWIEGDNKGNSSDSRYYGPIPVGLIRSRVLCRIWP 121
Cdd:TIGR02227  92 TSEFNTPVKVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVFYP 140
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 1-120 6.10e-21

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: 82.25  E-value: 6.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764495    1 MEPTLHSDNVLLTERLSKHWRTYQPGDIVIAISPIKADQFICKRIVAVSGDQVLIQ--------KPI--PIEAEFSGNSD 70
Cdd:pfam10502  33 MSPTLPIGDYLIVNKFSYGLGEPKRGDIVVFRPPEGPGVPLIKRVIGLPGDRVEYKddqlyingKPVgePYLADRKGRPT 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 386764495   71 DKKKPVMVKDYVPRGHVWIEGDNKGNSSDSRYYGPIPVGLIRSRVLCRIW 120
Cdd:pfam10502 113 FDLPPWQGCRVVPEGEYFVMGDNRDNSLDSRYFGFVPASNIVGRAVFPVW 162
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 1-115 1.31e-20

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: 79.17  E-value: 1.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764495   1 MEPTLHSDNVLLTERLSKHWRTYQPGDIVIAISPIKADQFICKRIVAvsgdqvliqkpipieaefsgnsddkkkpvmvkd 80
Cdd:cd06530   10 MEPTLQPGDLVLVNKLSYGFREPKRGDVVVFKSPGDPGKPIIKRVIG--------------------------------- 56

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 386764495  81 yvprghVWIEGDNKGNSSDSRYYGPIPVGLIRSRV 115
Cdd:cd06530   57 ------YFVLGDNRNNSLDSRYWGPVPEDDIVGKV 85
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 25-121 3.05e-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: 56.07  E-value: 3.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764495  25 PGDIVIAISPIKADQFICKRIVAVSGDQVLIQ--------KPIPIEAEFSgnSDDKKKPVMVKDY-VPRGHVWIEGDNKG 95
Cdd:COG4959   10 PEPLAAERGYLPRGVPLIKRVAALPGDTVCIKggqvyingKPVAEALERD--RAGRPLPVWQGCGvVPEGEYFLLGDNRP 87

                         90       100
                 ....*....|....*....|....*.
gi 386764495  96 NSSDSRYYGPIPVGLIRSRVLCRIWP 121
Cdd:COG4959   88 NSFDSRYFGPVPRSQIIGRAVPLWTP 113
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
1-109 4.79e-10

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 54.47  E-value: 4.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764495   1 MEPTLHSDNVLLTERLSKHWRTYQPGDIVIAISPIKADQFICKRIVAVSGDQVLIQ--------KPIPIEAEFSGNSDDK 72
Cdd:COG0681   43 MEPTLLVGDRLLVNKLSYGFGEPKRGDIVVFKYPEDPSKDYIKRVIGLPGDTVEIRdgqvyvngKPLNEPYLEEYYYPVS 122

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 386764495  73 KKPVMVKDYVPRGHVWIEGDNKGNSSDSRYYGPIPVG 109
Cdd:COG0681  123 VDGDVEVPPGEEEVPGGGGDNSNDSRSGDPDDGGGGV 159
sod_Ni_protease TIGR02754
nickel-type superoxide dismutase maturation protease; Members of this protein family are ...
 1-117 1.62e-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: 50.92  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764495    1 MEPTLHSDNVLLTERLSKHWRTYQPGDIVIAISPIKADQFICKRIVAVSgdqvliqkpipieaefsgnsddkkkpvmvkd 80
Cdd:TIGR02754   8 MSPTLPPGDRIIVVPWLKIFRVPPIGNVVVVRHPLQPYGLIIKRLAAVD------------------------------- 56

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 386764495   81 yvpRGHVWIEGDNKGNSSDSRYYGPIPVGLIRSRVLC 117
Cdd:TIGR02754  57 ---DNGLFLLGDNPKASTDSRQLGPVPRSLLLGKVLW 90
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 1-105 4.08e-09

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: 49.96  E-value: 4.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764495   1 MEPTLHSDNVLLTERLSKHwrtYQPGDIVIAISPikADQFICKRIVAVSGDqvliqkpipieaefsgnsddkkkpvmvkd 80
Cdd:cd06462   10 MEPTIPDGDLVLVDKSSYE---PKRGDIVVFRLP--GGELTVKRVIGLPGE----------------------------- 55

                         90       100
                 ....*....|....*....|....*
gi 386764495  81 yvprGHVWIEGDNKgNSSDSRYYGP 105
Cdd:cd06462   56 ----GHYFLLGDNP-NSPDSRIDGP 75
TraF_Ti TIGR02771
conjugative transfer signal peptidase TraF; This protein is found in apparent operons encoding ...
 43-122 3.70e-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: 43.62  E-value: 3.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764495   43 KRIVAVSGDQVLI--------QKPIPIEAEFSGNSDDKKKPVMVKDYVPRGHVWIEGDnKGNSSDSRYYGPIPvgliRSR 114
Cdd:TIGR02771  86 KRVLGLPGDRVTVradvvainGQLLPYSKPLATDSSGRPLPPFPEGVIPPGFFVVHDT-SPTSFDSRYFGPIS----REQ 160


                  ....*...
gi 386764495  115 VLCRIWPI 122
Cdd:TIGR02771 161 VIGRVKPL 168
PRK10861 PRK10861
signal peptidase I;
82-107 1.45e-05

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 42.73  E-value: 1.45e-05
                         10        20
                 ....*....|....*....|....*.
gi 386764495  82 VPRGHVWIEGDNKGNSSDSRYYGPIP 107
Cdd:PRK10861 264 VPPGQYFMMGDNRDNSADSRYWGFVP 289
PRK13838 PRK13838
conjugal transfer pilin processing protease TraF; Provisional
 43-107 1.91e-04

conjugal transfer pilin processing protease TraF; Provisional


Pssm-ID: 172365 [Multi-domain]  Cd Length: 176  Bit Score: 38.82  E-value: 1.91e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386764495  43 KRIVAVSGDQVLIQKPIPIEAEFSGNS-----DDKKKPVMV--KDYVPRGHVWIEGDNKGnSSDSRYYGPIP 107
Cdd:PRK13838  90 KTVAALAGQRVEIGGSVSIDGRPLPSSsvrrrDGEGRPLTPfpGGVVPPGHLFLHSSFAG-SYDSRYFGPVP 160
 
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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