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Conserved domains on  [gi|126722669|ref|NP_001076004|]
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signal peptide peptidase-like 2C isoform b precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_A22B super family cl01342
Signal peptide peptidase; The members of this family are membrane proteins. In some proteins ...
254-538 8.29e-81

Signal peptide peptidase; The members of this family are membrane proteins. In some proteins this region is found associated with pfam02225. This family corresponds with Merops subfamily A22B, the type example of which is signal peptide peptidase. There is a sequence-similarity relationship with pfam01080.


The actual alignment was detected with superfamily member pfam04258:

Pssm-ID: 470165  Cd Length: 286  Bit Score: 255.31  E-value: 8.29e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722669  254 EDAPMDFTPAMTGAVVTMSCSIMILLYFFYD-CFVYVMIGIFSLGASTGLYSCLAPILCHLPLWR---YQWVLPGQRVSV 329
Cdd:pfam04258   3 SDDFETITKIHAICFPITASCTLLLLYFFFKsLLVYVLTIYFCILGIIALAFCLSPFLTRLFFNKcplKNIKLPFLPGRF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722669  330 TWPLLLLAGLCAMVTVLWVIHRNEdhwaWLLQDTLGVAYCLFVLRRVRLPTFKNCTLFLLALLAFDVFFVFITPLftKTG 409
Cdd:pfam04258  83 SYSELVALLLCIVFAVWWALKRHE----WILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDIFWVFGSPY--IFG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722669  410 ESIMVEVASGPADSSshERLPMVLKVPRLSFSALtlCNQPFSILGFGDIVVPGFLVAYCHRFDMQV--QSRQVYYMACTV 487
Cdd:pfam04258 157 TSVMVTVATGPSSTG--EDIPMKLVFPRLSNMFD--NWGPFSMLGLGDIVMPGLLIALCLRFDISKkkSTHDIYFISTMI 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 126722669  488 AYAVGLLVTFVAMILMQMGQPALLYLVSSTLLTSLAVATCRQEFTLFWTGQ 538
Cdd:pfam04258 233 AYGLGLLITFVALNLFKAAQPALLYLVPCTLGTLLLLALWRGELKKLWNYG 283
PA super family cl28883
PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ...
44-181 1.76e-43

PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases including, hSPPL2a and 2b which catalyze the intramembrane proteolysis of tumor necrosis factor alpha, ii) various proteins containing a C3H2C3 RING finger including, Arabidopsis ReMembR-H2 protein and various E3 ubiquitin ligases such as human GRAIL (gene related to anergy in lymphocytes), iii) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), iv) various plant vacuolar sorting receptors such as Pisum sativum BP-80, v) glutamate carboxypeptidase II (GCPII), vi) yeast aminopeptidase Y, vii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, viii) lactocepin (a cell envelope-associated protease from Lactobacillus paracasei subsp. paracasei NCDO 151), ix) various subtilisin-like proteases such as melon Cucumisin, and x) human TfR (transferrin receptor) 1 and 2.


The actual alignment was detected with superfamily member cd02129:

Pssm-ID: 333703 [Multi-domain]  Cd Length: 120  Bit Score: 151.00  E-value: 1.76e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722669  44 YCVLYSSDYVNLPRDLHHAPLLSLHDGTKTPWCPDEDSfhqaqdsspRQRPLHQTTTMVTRGNCSFYAKGWLAQDQGAQG 123
Cdd:cd02129    1 YCILYNSQWASLPSDLDKATLLPLRNLTSSVLCSASDV---------PPGGLKGKAVVVMRGNCTFYEKARLAQSLGAEG 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 126722669 124 LLIVSRARNQQCSDTISKPQDpskpwpaLTIPVAVLRYTDMLDIVSHTyGDTdVRVAM 181
Cdd:cd02129   72 LLIVSRERLVPPSGNRSEYEK-------IDIPVALLSYKDMLDIQQTF-GDS-VKVAM 120
 
Name Accession Description Interval E-value
Peptidase_A22B pfam04258
Signal peptide peptidase; The members of this family are membrane proteins. In some proteins ...
254-538 8.29e-81

Signal peptide peptidase; The members of this family are membrane proteins. In some proteins this region is found associated with pfam02225. This family corresponds with Merops subfamily A22B, the type example of which is signal peptide peptidase. There is a sequence-similarity relationship with pfam01080.


Pssm-ID: 282158  Cd Length: 286  Bit Score: 255.31  E-value: 8.29e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722669  254 EDAPMDFTPAMTGAVVTMSCSIMILLYFFYD-CFVYVMIGIFSLGASTGLYSCLAPILCHLPLWR---YQWVLPGQRVSV 329
Cdd:pfam04258   3 SDDFETITKIHAICFPITASCTLLLLYFFFKsLLVYVLTIYFCILGIIALAFCLSPFLTRLFFNKcplKNIKLPFLPGRF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722669  330 TWPLLLLAGLCAMVTVLWVIHRNEdhwaWLLQDTLGVAYCLFVLRRVRLPTFKNCTLFLLALLAFDVFFVFITPLftKTG 409
Cdd:pfam04258  83 SYSELVALLLCIVFAVWWALKRHE----WILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDIFWVFGSPY--IFG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722669  410 ESIMVEVASGPADSSshERLPMVLKVPRLSFSALtlCNQPFSILGFGDIVVPGFLVAYCHRFDMQV--QSRQVYYMACTV 487
Cdd:pfam04258 157 TSVMVTVATGPSSTG--EDIPMKLVFPRLSNMFD--NWGPFSMLGLGDIVMPGLLIALCLRFDISKkkSTHDIYFISTMI 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 126722669  488 AYAVGLLVTFVAMILMQMGQPALLYLVSSTLLTSLAVATCRQEFTLFWTGQ 538
Cdd:pfam04258 233 AYGLGLLITFVALNLFKAAQPALLYLVPCTLGTLLLLALWRGELKKLWNYG 283
PSN smart00730
Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic ...
259-528 1.98e-72

Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic membrane proteins, whose genes are mutated in some individuals with Alzheimer's disease. Distant homologues, present in eukaryotes and archaea, also contain conserved aspartic acid residues which are predicted to contribute to catalysis. At least one member of this family has been shown to possess signal peptide peptidase activity.


Pssm-ID: 214793  Cd Length: 249  Bit Score: 232.14  E-value: 1.98e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722669   259 DFTPAMTGAVVTMSCSIMILLYFFYDCFVYVMIGIFSLGASTGLYSCLAPILCHLplwryqwvlpgqrvsVTWPLLLLAG 338
Cdd:smart00730   4 LLNSLVAIVFPIVATFVLVLLYKFFKYLVIVLVIYFSSLGVLFLYSLLYPLEVFR---------------VDYPTLLILL 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722669   339 LCAMVTVLWVIHRNedhWAWLLQDTLGVAYCLFVLRRVRLPTFKNCTLFLLALLAFDVFFVFITPLftktGESIMVEVAS 418
Cdd:smart00730  69 LNFAVVGFWCIHRK---GAWIQQDLIGISLCMAILFILRLPSEWTAWILLGALFIYDIFAVFGTPG----PLRVMVEVAT 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722669   419 GPADSSshERLPMVLKVPRLSFSALTLCNQPFSILGFGDIVVPGFLVAYCHRFDMQVQSRQVYYMACTVAYAVGLLVTFV 498
Cdd:smart00730 142 GRDEPI--KVFPALLYVPRLVVSFEDDEEERFSMLGLGDIVFPGILVASAARFDVSVRSDSNYFLACFVAYGIGLILTLV 219
                          250       260       270
                   ....*....|....*....|....*....|
gi 126722669   499 AMILMQMGQPALLYLVSSTLLTSLAVATCR 528
Cdd:smart00730 220 LLALFKKAQPALPYLVPFTLVFYLLTALLR 249
PA_hSPPL_like cd02129
PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like ...
44-181 1.76e-43

PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like (hSPPL)-like. This group contains various PA domain-containing proteins similar to hSPPL2a and 2b. These SPPLs are GxGD aspartic proteases. SPPL2a is sorted to the late endosomes, SPPL2b to the plasma membrane. In activated dendritic cells, hSPPL2a and 2b catalyze the intramembrane proteolysis of tumor necrosis factor alpha triggering IL-12 production. hSPPL2a and 2b may have a broad substrate spectrum. The significance of the PA domain to these SPPLs has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239044 [Multi-domain]  Cd Length: 120  Bit Score: 151.00  E-value: 1.76e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722669  44 YCVLYSSDYVNLPRDLHHAPLLSLHDGTKTPWCPDEDSfhqaqdsspRQRPLHQTTTMVTRGNCSFYAKGWLAQDQGAQG 123
Cdd:cd02129    1 YCILYNSQWASLPSDLDKATLLPLRNLTSSVLCSASDV---------PPGGLKGKAVVVMRGNCTFYEKARLAQSLGAEG 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 126722669 124 LLIVSRARNQQCSDTISKPQDpskpwpaLTIPVAVLRYTDMLDIVSHTyGDTdVRVAM 181
Cdd:cd02129   72 LLIVSRERLVPPSGNRSEYEK-------IDIPVALLSYKDMLDIQQTF-GDS-VKVAM 120
 
Name Accession Description Interval E-value
Peptidase_A22B pfam04258
Signal peptide peptidase; The members of this family are membrane proteins. In some proteins ...
254-538 8.29e-81

Signal peptide peptidase; The members of this family are membrane proteins. In some proteins this region is found associated with pfam02225. This family corresponds with Merops subfamily A22B, the type example of which is signal peptide peptidase. There is a sequence-similarity relationship with pfam01080.


Pssm-ID: 282158  Cd Length: 286  Bit Score: 255.31  E-value: 8.29e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722669  254 EDAPMDFTPAMTGAVVTMSCSIMILLYFFYD-CFVYVMIGIFSLGASTGLYSCLAPILCHLPLWR---YQWVLPGQRVSV 329
Cdd:pfam04258   3 SDDFETITKIHAICFPITASCTLLLLYFFFKsLLVYVLTIYFCILGIIALAFCLSPFLTRLFFNKcplKNIKLPFLPGRF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722669  330 TWPLLLLAGLCAMVTVLWVIHRNEdhwaWLLQDTLGVAYCLFVLRRVRLPTFKNCTLFLLALLAFDVFFVFITPLftKTG 409
Cdd:pfam04258  83 SYSELVALLLCIVFAVWWALKRHE----WILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDIFWVFGSPY--IFG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722669  410 ESIMVEVASGPADSSshERLPMVLKVPRLSFSALtlCNQPFSILGFGDIVVPGFLVAYCHRFDMQV--QSRQVYYMACTV 487
Cdd:pfam04258 157 TSVMVTVATGPSSTG--EDIPMKLVFPRLSNMFD--NWGPFSMLGLGDIVMPGLLIALCLRFDISKkkSTHDIYFISTMI 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 126722669  488 AYAVGLLVTFVAMILMQMGQPALLYLVSSTLLTSLAVATCRQEFTLFWTGQ 538
Cdd:pfam04258 233 AYGLGLLITFVALNLFKAAQPALLYLVPCTLGTLLLLALWRGELKKLWNYG 283
PSN smart00730
Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic ...
259-528 1.98e-72

Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic membrane proteins, whose genes are mutated in some individuals with Alzheimer's disease. Distant homologues, present in eukaryotes and archaea, also contain conserved aspartic acid residues which are predicted to contribute to catalysis. At least one member of this family has been shown to possess signal peptide peptidase activity.


Pssm-ID: 214793  Cd Length: 249  Bit Score: 232.14  E-value: 1.98e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722669   259 DFTPAMTGAVVTMSCSIMILLYFFYDCFVYVMIGIFSLGASTGLYSCLAPILCHLplwryqwvlpgqrvsVTWPLLLLAG 338
Cdd:smart00730   4 LLNSLVAIVFPIVATFVLVLLYKFFKYLVIVLVIYFSSLGVLFLYSLLYPLEVFR---------------VDYPTLLILL 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722669   339 LCAMVTVLWVIHRNedhWAWLLQDTLGVAYCLFVLRRVRLPTFKNCTLFLLALLAFDVFFVFITPLftktGESIMVEVAS 418
Cdd:smart00730  69 LNFAVVGFWCIHRK---GAWIQQDLIGISLCMAILFILRLPSEWTAWILLGALFIYDIFAVFGTPG----PLRVMVEVAT 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722669   419 GPADSSshERLPMVLKVPRLSFSALTLCNQPFSILGFGDIVVPGFLVAYCHRFDMQVQSRQVYYMACTVAYAVGLLVTFV 498
Cdd:smart00730 142 GRDEPI--KVFPALLYVPRLVVSFEDDEEERFSMLGLGDIVFPGILVASAARFDVSVRSDSNYFLACFVAYGIGLILTLV 219
                          250       260       270
                   ....*....|....*....|....*....|
gi 126722669   499 AMILMQMGQPALLYLVSSTLLTSLAVATCR 528
Cdd:smart00730 220 LLALFKKAQPALPYLVPFTLVFYLLTALLR 249
PA_hSPPL_like cd02129
PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like ...
44-181 1.76e-43

PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like (hSPPL)-like. This group contains various PA domain-containing proteins similar to hSPPL2a and 2b. These SPPLs are GxGD aspartic proteases. SPPL2a is sorted to the late endosomes, SPPL2b to the plasma membrane. In activated dendritic cells, hSPPL2a and 2b catalyze the intramembrane proteolysis of tumor necrosis factor alpha triggering IL-12 production. hSPPL2a and 2b may have a broad substrate spectrum. The significance of the PA domain to these SPPLs has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239044 [Multi-domain]  Cd Length: 120  Bit Score: 151.00  E-value: 1.76e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722669  44 YCVLYSSDYVNLPRDLHHAPLLSLHDGTKTPWCPDEDSfhqaqdsspRQRPLHQTTTMVTRGNCSFYAKGWLAQDQGAQG 123
Cdd:cd02129    1 YCILYNSQWASLPSDLDKATLLPLRNLTSSVLCSASDV---------PPGGLKGKAVVVMRGNCTFYEKARLAQSLGAEG 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 126722669 124 LLIVSRARNQQCSDTISKPQDpskpwpaLTIPVAVLRYTDMLDIVSHTyGDTdVRVAM 181
Cdd:cd02129   72 LLIVSRERLVPPSGNRSEYEK-------IDIPVALLSYKDMLDIQQTF-GDS-VKVAM 120
PA cd00538
PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ...
101-181 7.39e-06

PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases including, hSPPL2a and 2b which catalyze the intramembrane proteolysis of tumor necrosis factor alpha, ii) various proteins containing a C3H2C3 RING finger including, Arabidopsis ReMembR-H2 protein and various E3 ubiquitin ligases such as human GRAIL (gene related to anergy in lymphocytes), iii) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), iv) various plant vacuolar sorting receptors such as Pisum sativum BP-80, v) glutamate carboxypeptidase II (GCPII), vi) yeast aminopeptidase Y, vii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, viii) lactocepin (a cell envelope-associated protease from Lactobacillus paracasei subsp. paracasei NCDO 151), ix) various subtilisin-like proteases such as melon Cucumisin, and x) human TfR (transferrin receptor) 1 and 2.


Pssm-ID: 238300 [Multi-domain]  Cd Length: 126  Bit Score: 45.58  E-value: 7.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722669 101 MVTRGNCSFYAKGWLAQDQGAQGLLIVsrarNQQCSDTISKpQDPSKPWPALTIPVAVLRYTDMLDIVSHTYGDTDVRVA 180
Cdd:cd00538   51 LVRRGGCSFSEKVKNAQKAGAKAVIIY----NNGDDPGPQM-GSVGLESTDPSIPTVGISYADGEALLSLLEAGKTVTVD 125

                 .
gi 126722669 181 M 181
Cdd:cd00538  126 L 126
PA_VSR cd02125
PA_VSR: Protease-associated (PA) domain-containing plant vacuolar sorting receptor (VSR). This ...
71-127 2.31e-03

PA_VSR: Protease-associated (PA) domain-containing plant vacuolar sorting receptor (VSR). This group includes various PA domain-containing VSRs such as garden pea BP-80, pumpkin PV72, and various Arabidopsis VSRs including AtVSR1. In contrast to most eukaryotes, which only have one or two VSRs, plants have several. This may in part be a reflection of having a more complex vacuolar system with both lytic vacuoles and storage vacuoles. The lytic vacuole is thought to be equivalent to the mammalian lysosome and the yeast vacuole. Pea BP-80 is a type 1 transmembrane protein, involved in the targeting of proteins to the lytic vacuole; it has been suggested that this protein also mediates targeting to the storage vacuole. PV72 and AtVSR1 may mediate transport of seed storage proteins to protein storage vacuoles. The significance of the PA domain to VSRs has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239040 [Multi-domain]  Cd Length: 127  Bit Score: 38.23  E-value: 2.31e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 126722669  71 TKTPWCPDEDSFHQAQDSSPRQRPlhqTTTMVTRGNCSFYAKGWLAQDQGAQGLLIV 127
Cdd:cd02125   20 ENRTGCKEFDVFFKPKKSEPGRRP---VILLLDRGGCFFTLKAWNAQQAGAAAVLVA 73
 
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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