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Conserved domains on  [gi|2175849874|ref|NP_001386465|]
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minor histocompatibility antigen H13 isoform 1 [Rattus norvegicus]

Protein Classification

A22B family peptidase( domain architecture ID 10515244)

A22B family peptidase catalyzes intramembrane proteolysis of some signal peptides after they have been cleaved from a preprotein, resulting in the release of the fragment from the ER membrane into the cytoplasm

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_A22B pfam04258
Signal peptide peptidase; The members of this family are membrane proteins. In some proteins ...
62-350 5.31e-116

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: 339.28  E-value: 5.31e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175849874  62 SSSDMPETITSRDAARFPIIASCTLLGLYLFFKLFsqeyINLLLSMYFFVLGILALSHTISPFMNKFFPANFPNRQYQLL 141
Cdd:pfam04258   1 KSSDDFETITKIHAICFPITASCTLLLLYFFFKSL----LVYVLTIYFCILGIIALAFCLSPFLTRLFFNKCPLKNIKLP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175849874 142 FTQGsgenkeeiinyEFDTKDLVCLGLSSVVGVWYLLRKH-WIANNLFGLAFSLNGVELLHLNNVSTGCILLGGLFIYDI 220
Cdd:pfam04258  77 FLPG-----------RFSYSELVALLLCIVFAVWWALKRHeWILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDI 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175849874 221 FWVFG------TNVMVTVAK-----SFEAPIKLVFPQdLLEKGLEADNFAMLGLGDIVIPGIFIALLLRFDISLKKNTH- 288
Cdd:pfam04258 146 FWVFGspyifgTSVMVTVATgpsstGEDIPMKLVFPR-LSNMFDNWGPFSMLGLGDIVMPGLLIALCLRFDISKKKSTHd 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2175849874 289 TYFYTSFAAYIFGLGLTIFIMHIFKHAQPALLYLVPACIGFPVLVALVKGEVAEMFSYESSA 350
Cdd:pfam04258 225 IYFISTMIAYGLGLLITFVALNLFKAAQPALLYLVPCTLGTLLLLALWRGELKKLWNYGEST 286
 
Name Accession Description Interval E-value
Peptidase_A22B pfam04258
Signal peptide peptidase; The members of this family are membrane proteins. In some proteins ...
62-350 5.31e-116

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: 339.28  E-value: 5.31e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175849874  62 SSSDMPETITSRDAARFPIIASCTLLGLYLFFKLFsqeyINLLLSMYFFVLGILALSHTISPFMNKFFPANFPNRQYQLL 141
Cdd:pfam04258   1 KSSDDFETITKIHAICFPITASCTLLLLYFFFKSL----LVYVLTIYFCILGIIALAFCLSPFLTRLFFNKCPLKNIKLP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175849874 142 FTQGsgenkeeiinyEFDTKDLVCLGLSSVVGVWYLLRKH-WIANNLFGLAFSLNGVELLHLNNVSTGCILLGGLFIYDI 220
Cdd:pfam04258  77 FLPG-----------RFSYSELVALLLCIVFAVWWALKRHeWILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDI 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175849874 221 FWVFG------TNVMVTVAK-----SFEAPIKLVFPQdLLEKGLEADNFAMLGLGDIVIPGIFIALLLRFDISLKKNTH- 288
Cdd:pfam04258 146 FWVFGspyifgTSVMVTVATgpsstGEDIPMKLVFPR-LSNMFDNWGPFSMLGLGDIVMPGLLIALCLRFDISKKKSTHd 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2175849874 289 TYFYTSFAAYIFGLGLTIFIMHIFKHAQPALLYLVPACIGFPVLVALVKGEVAEMFSYESSA 350
Cdd:pfam04258 225 IYFISTMIAYGLGLLITFVALNLFKAAQPALLYLVPCTLGTLLLLALWRGELKKLWNYGEST 286
PSN smart00730
Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic ...
66-337 1.41e-69

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: 219.43  E-value: 1.41e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175849874   66 MPETITSRDAARFPIIASCTLLGLYLFFKlfsqeYINLLLSMYFFVLGILALSHTISPFMNKFFpanfpnrqyqllftqg 145
Cdd:smart00730   1 EYSLLNSLVAIVFPIVATFVLVLLYKFFK-----YLVIVLVIYFSSLGVLFLYSLLYPLEVFRV---------------- 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175849874  146 sgenkeeiinyeFDTKDLVCLGLSSVVGVWYLLRK-HWIANNLFGLAFSLNGVELLHLNNVSTGCILLGGLFIYDIFWVF 224
Cdd:smart00730  60 ------------DYPTLLILLLNFAVVGFWCIHRKgAWIQQDLIGISLCMAILFILRLPSEWTAWILLGALFIYDIFAVF 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175849874  225 GT----NVMVTVAKSFEAPIkLVFPQDLLEK-------GLEADNFAMLGLGDIVIPGIFIALLLRFDISlKKNTHTYFYT 293
Cdd:smart00730 128 GTpgplRVMVEVATGRDEPI-KVFPALLYVPrlvvsfeDDEEERFSMLGLGDIVFPGILVASAARFDVS-VRSDSNYFLA 205
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2175849874  294 SFAAYIFGLGLTIFIMHIFKHAQPALLYLVPACIGFPVLVALVK 337
Cdd:smart00730 206 CFVAYGIGLILTLVLLALFKKAQPALPYLVPFTLVFYLLTALLR 249
 
Name Accession Description Interval E-value
Peptidase_A22B pfam04258
Signal peptide peptidase; The members of this family are membrane proteins. In some proteins ...
62-350 5.31e-116

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: 339.28  E-value: 5.31e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175849874  62 SSSDMPETITSRDAARFPIIASCTLLGLYLFFKLFsqeyINLLLSMYFFVLGILALSHTISPFMNKFFPANFPNRQYQLL 141
Cdd:pfam04258   1 KSSDDFETITKIHAICFPITASCTLLLLYFFFKSL----LVYVLTIYFCILGIIALAFCLSPFLTRLFFNKCPLKNIKLP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175849874 142 FTQGsgenkeeiinyEFDTKDLVCLGLSSVVGVWYLLRKH-WIANNLFGLAFSLNGVELLHLNNVSTGCILLGGLFIYDI 220
Cdd:pfam04258  77 FLPG-----------RFSYSELVALLLCIVFAVWWALKRHeWILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDI 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175849874 221 FWVFG------TNVMVTVAK-----SFEAPIKLVFPQdLLEKGLEADNFAMLGLGDIVIPGIFIALLLRFDISLKKNTH- 288
Cdd:pfam04258 146 FWVFGspyifgTSVMVTVATgpsstGEDIPMKLVFPR-LSNMFDNWGPFSMLGLGDIVMPGLLIALCLRFDISKKKSTHd 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2175849874 289 TYFYTSFAAYIFGLGLTIFIMHIFKHAQPALLYLVPACIGFPVLVALVKGEVAEMFSYESSA 350
Cdd:pfam04258 225 IYFISTMIAYGLGLLITFVALNLFKAAQPALLYLVPCTLGTLLLLALWRGELKKLWNYGEST 286
PSN smart00730
Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic ...
66-337 1.41e-69

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: 219.43  E-value: 1.41e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175849874   66 MPETITSRDAARFPIIASCTLLGLYLFFKlfsqeYINLLLSMYFFVLGILALSHTISPFMNKFFpanfpnrqyqllftqg 145
Cdd:smart00730   1 EYSLLNSLVAIVFPIVATFVLVLLYKFFK-----YLVIVLVIYFSSLGVLFLYSLLYPLEVFRV---------------- 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175849874  146 sgenkeeiinyeFDTKDLVCLGLSSVVGVWYLLRK-HWIANNLFGLAFSLNGVELLHLNNVSTGCILLGGLFIYDIFWVF 224
Cdd:smart00730  60 ------------DYPTLLILLLNFAVVGFWCIHRKgAWIQQDLIGISLCMAILFILRLPSEWTAWILLGALFIYDIFAVF 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175849874  225 GT----NVMVTVAKSFEAPIkLVFPQDLLEK-------GLEADNFAMLGLGDIVIPGIFIALLLRFDISlKKNTHTYFYT 293
Cdd:smart00730 128 GTpgplRVMVEVATGRDEPI-KVFPALLYVPrlvvsfeDDEEERFSMLGLGDIVFPGILVASAARFDVS-VRSDSNYFLA 205
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2175849874  294 SFAAYIFGLGLTIFIMHIFKHAQPALLYLVPACIGFPVLVALVK 337
Cdd:smart00730 206 CFVAYGIGLILTLVLLALFKKAQPALPYLVPFTLVFYLLTALLR 249
 
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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