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Conserved domains on  [gi|21314755|ref|NP_116191|]
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signal peptide peptidase-like 2A precursor [Homo sapiens]

Protein Classification

PA_hSPPL_like and Peptidase_A22B domain-containing protein( domain architecture ID 10114778)

PA_hSPPL_like and Peptidase_A22B domain-containing protein

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 ...
210-496 2.75e-99

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: 301.14  E-value: 2.75e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314755   210 KKKEEYLTFSPLTVVIFVVICCVMMVLLYFFYK-WLVYVMIAIFCIASAMSLYNCLAALIHKIPYGQCTIACRG-----K 283
Cdd:pfam04258   1 KSSDDFETITKIHAICFPITASCTLLLLYFFFKsLLVYVLTIYFCILGIIALAFCLSPFLTRLFFNKCPLKNIKlpflpG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314755   284 NMEVRLIFLSGLCIAVAVVWAVFRNEdrwaWILQDILGIAFCLNLIKTLKLPNFKSCVILLGLLLLYDVFFVFITPFItk 363
Cdd:pfam04258  81 RFSYSELVALLLCIVFAVWWALKRHE----WILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDIFWVFGSPYI-- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314755   364 NGESIMVELAAGPFGNNEKLPVVIRVPKLiyfSVMSVCLMPVSILGFGDIIVPGLLIAYCRRFDVQTGSS--YIYYVSST 441
Cdd:pfam04258 155 FGTSVMVTVATGPSSTGEDIPMKLVFPRL---SNMFDNWGPFSMLGLGDIVMPGLLIALCLRFDISKKKSthDIYFISTM 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 21314755   442 VAYAIGMILTFVVLVLMKKGQPALLYLVPCTLITASVVAWRRKEMKKFWKGNSYQ 496
Cdd:pfam04258 232 IAYGLGLLITFVALNLFKAAQPALLYLVPCTLGTLLLLALWRGELKKLWNYGEST 286
PA_hSPPL_like cd02129
PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like ...
41-160 1.84e-65

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: 207.63  E-value: 1.84e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314755  41 YCMLYNPYWTALPSTLENATSISLMNLTSTPLCNLSDIPPVGIKSKAVVVPWGSCHFLEKARIAQKGGAEAMLVVNNSVL 120
Cdd:cd02129   1 YCILYNSQWASLPSDLDKATLLPLRNLTSSVLCSASDVPPGGLKGKAVVVMRGNCTFYEKARLAQSLGAEGLLIVSRERL 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 21314755 121 FPPSGNRSEFPDVKILIAFISYKDFRDMNQTLGDNITVKM 160
Cdd:cd02129  81 VPPSGNRSEYEKIDIPVALLSYKDMLDIQQTFGDSVKVAM 120
 
Name Accession Description Interval E-value
Peptidase_A22B pfam04258
Signal peptide peptidase; The members of this family are membrane proteins. In some proteins ...
210-496 2.75e-99

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: 301.14  E-value: 2.75e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314755   210 KKKEEYLTFSPLTVVIFVVICCVMMVLLYFFYK-WLVYVMIAIFCIASAMSLYNCLAALIHKIPYGQCTIACRG-----K 283
Cdd:pfam04258   1 KSSDDFETITKIHAICFPITASCTLLLLYFFFKsLLVYVLTIYFCILGIIALAFCLSPFLTRLFFNKCPLKNIKlpflpG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314755   284 NMEVRLIFLSGLCIAVAVVWAVFRNEdrwaWILQDILGIAFCLNLIKTLKLPNFKSCVILLGLLLLYDVFFVFITPFItk 363
Cdd:pfam04258  81 RFSYSELVALLLCIVFAVWWALKRHE----WILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDIFWVFGSPYI-- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314755   364 NGESIMVELAAGPFGNNEKLPVVIRVPKLiyfSVMSVCLMPVSILGFGDIIVPGLLIAYCRRFDVQTGSS--YIYYVSST 441
Cdd:pfam04258 155 FGTSVMVTVATGPSSTGEDIPMKLVFPRL---SNMFDNWGPFSMLGLGDIVMPGLLIALCLRFDISKKKSthDIYFISTM 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 21314755   442 VAYAIGMILTFVVLVLMKKGQPALLYLVPCTLITASVVAWRRKEMKKFWKGNSYQ 496
Cdd:pfam04258 232 IAYGLGLLITFVALNLFKAAQPALLYLVPCTLGTLLLLALWRGELKKLWNYGEST 286
PSN smart00730
Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic ...
214-483 1.47e-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: 223.28  E-value: 1.47e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314755    214 EYLTFSPLTVVIFVVICCVMMVLLYFFYKWLVYVMIAIFCIASAMSLYNCLAALIHKIpygqctiacrgknMEVRLIFLS 293
Cdd:smart00730   1 EYSLLNSLVAIVFPIVATFVLVLLYKFFKYLVIVLVIYFSSLGVLFLYSLLYPLEVFR-------------VDYPTLLIL 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314755    294 GLCIAVAVVWAVFRnedRWAWILQDILGIAFCLNLIKTLKLPNFKSCVILLGLLLLYDVFFVFITPFitknGESIMVELA 373
Cdd:smart00730  68 LLNFAVVGFWCIHR---KGAWIQQDLIGISLCMAILFILRLPSEWTAWILLGALFIYDIFAVFGTPG----PLRVMVEVA 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314755    374 AGPFGNNEKLPVVIRVPKLiYFSVMSVCLMPVSILGFGDIIVPGLLIAYCRRFDVQTGSSYIYYVSSTVAYAIGMILTFV 453
Cdd:smart00730 141 TGRDEPIKVFPALLYVPRL-VVSFEDDEEERFSMLGLGDIVFPGILVASAARFDVSVRSDSNYFLACFVAYGIGLILTLV 219
                          250       260       270
                   ....*....|....*....|....*....|
gi 21314755    454 VLVLMKKGQPALLYLVPCTLITASVVAWRR 483
Cdd:smart00730 220 LLALFKKAQPALPYLVPFTLVFYLLTALLR 249
PA_hSPPL_like cd02129
PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like ...
41-160 1.84e-65

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: 207.63  E-value: 1.84e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314755  41 YCMLYNPYWTALPSTLENATSISLMNLTSTPLCNLSDIPPVGIKSKAVVVPWGSCHFLEKARIAQKGGAEAMLVVNNSVL 120
Cdd:cd02129   1 YCILYNSQWASLPSDLDKATLLPLRNLTSSVLCSASDVPPGGLKGKAVVVMRGNCTFYEKARLAQSLGAEGLLIVSRERL 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 21314755 121 FPPSGNRSEFPDVKILIAFISYKDFRDMNQTLGDNITVKM 160
Cdd:cd02129  81 VPPSGNRSEYEKIDIPVALLSYKDMLDIQQTFGDSVKVAM 120
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
67-144 1.53e-06

PA domain; The PA (Protease associated) domain is found as an insert domain in diverse proteases. The PA domain is also found in a plant vacuolar sorting receptor Swiss:O22925 and members of the RZF family Swiss:O43567. It has been suggested that this domain forms a lid-like structure that covers the active site in active proteases, and is involved in protein recognition in vacuolar sorting receptors.


Pssm-ID: 460499 [Multi-domain]  Cd Length: 91  Bit Score: 46.35  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314755    67 LTSTPLCNLSD--IPPVGIKSKAVVVPWGSCHFLEKARIAQKGGAEAMLVVNN----SVLFPPSGNRSEFPDVKILIAFI 140
Cdd:pfam02225   4 LVLAPGCYAGDgiPADFDVKGKIVLVRCTFGFRAEKVRNAQAAGAAGVIIYNNveglGGPPGAGGNELYPDGIYIPAVGV 83

                  ....
gi 21314755   141 SYKD 144
Cdd:pfam02225  84 SRAD 87
 
Name Accession Description Interval E-value
Peptidase_A22B pfam04258
Signal peptide peptidase; The members of this family are membrane proteins. In some proteins ...
210-496 2.75e-99

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: 301.14  E-value: 2.75e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314755   210 KKKEEYLTFSPLTVVIFVVICCVMMVLLYFFYK-WLVYVMIAIFCIASAMSLYNCLAALIHKIPYGQCTIACRG-----K 283
Cdd:pfam04258   1 KSSDDFETITKIHAICFPITASCTLLLLYFFFKsLLVYVLTIYFCILGIIALAFCLSPFLTRLFFNKCPLKNIKlpflpG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314755   284 NMEVRLIFLSGLCIAVAVVWAVFRNEdrwaWILQDILGIAFCLNLIKTLKLPNFKSCVILLGLLLLYDVFFVFITPFItk 363
Cdd:pfam04258  81 RFSYSELVALLLCIVFAVWWALKRHE----WILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDIFWVFGSPYI-- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314755   364 NGESIMVELAAGPFGNNEKLPVVIRVPKLiyfSVMSVCLMPVSILGFGDIIVPGLLIAYCRRFDVQTGSS--YIYYVSST 441
Cdd:pfam04258 155 FGTSVMVTVATGPSSTGEDIPMKLVFPRL---SNMFDNWGPFSMLGLGDIVMPGLLIALCLRFDISKKKSthDIYFISTM 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 21314755   442 VAYAIGMILTFVVLVLMKKGQPALLYLVPCTLITASVVAWRRKEMKKFWKGNSYQ 496
Cdd:pfam04258 232 IAYGLGLLITFVALNLFKAAQPALLYLVPCTLGTLLLLALWRGELKKLWNYGEST 286
PSN smart00730
Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic ...
214-483 1.47e-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: 223.28  E-value: 1.47e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314755    214 EYLTFSPLTVVIFVVICCVMMVLLYFFYKWLVYVMIAIFCIASAMSLYNCLAALIHKIpygqctiacrgknMEVRLIFLS 293
Cdd:smart00730   1 EYSLLNSLVAIVFPIVATFVLVLLYKFFKYLVIVLVIYFSSLGVLFLYSLLYPLEVFR-------------VDYPTLLIL 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314755    294 GLCIAVAVVWAVFRnedRWAWILQDILGIAFCLNLIKTLKLPNFKSCVILLGLLLLYDVFFVFITPFitknGESIMVELA 373
Cdd:smart00730  68 LLNFAVVGFWCIHR---KGAWIQQDLIGISLCMAILFILRLPSEWTAWILLGALFIYDIFAVFGTPG----PLRVMVEVA 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314755    374 AGPFGNNEKLPVVIRVPKLiYFSVMSVCLMPVSILGFGDIIVPGLLIAYCRRFDVQTGSSYIYYVSSTVAYAIGMILTFV 453
Cdd:smart00730 141 TGRDEPIKVFPALLYVPRL-VVSFEDDEEERFSMLGLGDIVFPGILVASAARFDVSVRSDSNYFLACFVAYGIGLILTLV 219
                          250       260       270
                   ....*....|....*....|....*....|
gi 21314755    454 VLVLMKKGQPALLYLVPCTLITASVVAWRR 483
Cdd:smart00730 220 LLALFKKAQPALPYLVPFTLVFYLLTALLR 249
PA_hSPPL_like cd02129
PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like ...
41-160 1.84e-65

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: 207.63  E-value: 1.84e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314755  41 YCMLYNPYWTALPSTLENATSISLMNLTSTPLCNLSDIPPVGIKSKAVVVPWGSCHFLEKARIAQKGGAEAMLVVNNSVL 120
Cdd:cd02129   1 YCILYNSQWASLPSDLDKATLLPLRNLTSSVLCSASDVPPGGLKGKAVVVMRGNCTFYEKARLAQSLGAEGLLIVSRERL 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 21314755 121 FPPSGNRSEFPDVKILIAFISYKDFRDMNQTLGDNITVKM 160
Cdd:cd02129  81 VPPSGNRSEYEKIDIPVALLSYKDMLDIQQTFGDSVKVAM 120
PA cd00538
PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ...
73-161 2.74e-08

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: 52.52  E-value: 2.74e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314755  73 CNLSDI--PPVGIKSKAVVVPWGSCHFLEKARIAQKGGAEAMLVVNNSVLFPP-SGNRSEFPDV-KILIAFISYKDFRDM 148
Cdd:cd00538  33 CGYGTTddSGADVKGKIVLVRRGGCSFSEKVKNAQKAGAKAVIIYNNGDDPGPqMGSVGLESTDpSIPTVGISYADGEAL 112
                        90
                ....*....|...
gi 21314755 149 NQTLGDNITVKMY 161
Cdd:cd00538 113 LSLLEAGKTVTVD 125
PA_SaNapH_like cd04816
PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus ...
70-161 1.27e-06

PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus N-acetylpuromycin N-acetylhydrolase (SaNapH).This group contains various PA domain-containing proteins similar SaNapH. Proteins in this group belong to the peptidase M28 family. NapH is a terminal enzyme in the puromycin biosynthetic pathway; NapH hydrolyzes N-acetylpuromycin to the active antibiotic. The significance of the PA domain to these proteins 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: 240120 [Multi-domain]  Cd Length: 122  Bit Score: 47.32  E-value: 1.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314755  70 TPLCNLSDIPPVGIKSKAVVVPWGSCHFLEKARIAQKGGAEAMLVVNNSVLFPPSGN-RSEFPDVKILIAFISYKDFRDM 148
Cdd:cd04816  29 PAGCDASDYDGLDVKGAIVLVDRGGCPFADKQKVAAARGAVAVIVVNNSDGGGTAGTlGAPNIDLKVPVGVITKAAGAAL 108
                        90
                ....*....|...
gi 21314755 149 NQTLGDNITVKMY 161
Cdd:cd04816 109 RRRLGAGETLELD 121
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
67-144 1.53e-06

PA domain; The PA (Protease associated) domain is found as an insert domain in diverse proteases. The PA domain is also found in a plant vacuolar sorting receptor Swiss:O22925 and members of the RZF family Swiss:O43567. It has been suggested that this domain forms a lid-like structure that covers the active site in active proteases, and is involved in protein recognition in vacuolar sorting receptors.


Pssm-ID: 460499 [Multi-domain]  Cd Length: 91  Bit Score: 46.35  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314755    67 LTSTPLCNLSD--IPPVGIKSKAVVVPWGSCHFLEKARIAQKGGAEAMLVVNN----SVLFPPSGNRSEFPDVKILIAFI 140
Cdd:pfam02225   4 LVLAPGCYAGDgiPADFDVKGKIVLVRCTFGFRAEKVRNAQAAGAAGVIIYNNveglGGPPGAGGNELYPDGIYIPAVGV 83

                  ....
gi 21314755   141 SYKD 144
Cdd:pfam02225  84 SRAD 87
PA_EDEM3_like cd02126
PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This ...
83-145 1.06e-05

PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This group contains various PA domain-containing proteins similar to mouse EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein). EDEM3 contains a region, similar to Class I alpha-mannosidases (gylcosyl hydrolase family 47), N-terminal to the PA domain. EDEM3 accelerates glycoprotein ERAD (ER-associated degradation). In transfected mammalian cells, overexpression of EDEM3 enhances the mannose trimming from the N-glycans, of a model misfolded protein [alpha1-antitrypsin null (Hong Kong)] as well as, from total glycoproteins. Mannose trimming appears to be involved in the selection of ERAD substrates. EDEM3 has a different specificity of trimming than ER alpha-mannosidase 1. The significance of the PA domain to EDEM3 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: 239041 [Multi-domain]  Cd Length: 126  Bit Score: 45.04  E-value: 1.06e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21314755  83 IKSKAVVVPWGSCHFLEKARIAQKGGAEAMLVVNN--------SVLFPPSGNRSEFPDVKILIAFISYKDF 145
Cdd:cd02126  39 VKGKIAIMERGDCMFVEKARRVQKAGAIGGIVIDNnegsssdtAPMFAMSGDGDSTDDVTIPVVFLFSKEG 109
PA_C_RZF_like cd02123
PA_C-RZF_ like: Protease-associated (PA) domain C_RZF-like. This group includes various PA ...
85-167 1.08e-05

PA_C-RZF_ like: Protease-associated (PA) domain C_RZF-like. This group includes various PA domain-containing proteins similar to C-RZF (chicken embryo RING zinc finger) protein. These proteins contain a C3H2C3 RING finger. C-RZF is expressed in embryo cells and is restricted mainly to brain and heart, it is localized to both the nucleus and endosomes. Additional C3H2C3 RING finger proteins belonging to this group, include Arabidopsis ReMembR-H2 protein and mouse sperizin. ReMembR-H2 is likely to be an integral membrane protein, and to traffic through the endosomal pathway. Sperizin is expressed in haploid germ cells and localized in the cytoplasm, it may participate in spermatogenesis. The significance of the PA domain to these proteins 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: 239038 [Multi-domain]  Cd Length: 153  Bit Score: 45.41  E-value: 1.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314755  85 SKAVVVPWGSCHFLEKARIAQKGGAEAMLVVNNS--VLFPPSGNRSEFPDVKILIAFISYKDFRDMNQTLGDNITVKMYS 162
Cdd:cd02123  68 SFIVLIRRGNCSFETKVRNAQRAGYKAAIVYNDEsnDLISMSGNDQEIKGIDIPSVFVGKSTGEILKKYASYEKGVILIP 147

                ....*
gi 21314755 163 PSWPN 167
Cdd:cd02123 148 DLPLK 152
PA_GO-like cd02132
PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on ...
50-117 6.63e-05

PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on protein GRO10. This group contains various PA domain-containing proteins similar to the functionally uncharacterized Arabidopsis GRO10. The PA domain 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: 239047 [Multi-domain]  Cd Length: 139  Bit Score: 42.80  E-value: 6.63e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21314755  50 TALPSTLENATSISLMNLTSTPLCNLSDIPpvgIKSKAVVVPWGSCHFLEKARIAQKGGAEAMLVVNN 117
Cdd:cd02132  28 ASLPSKEDNANKTRAVLANPLDCCSPSTSK---LSGSIALVERGECAFTEKAKIAEAGGASALLIIND 92
PA_subtilisin_1 cd04818
PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. ...
86-158 1.80e-03

PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. A subgroup of PA domain-containing subtilisin-like 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 subtilisin-like proteases: i) melon cucumisin, ii) Arabidopsis thaliana Ara12, iii) Alnus glutinosa ag12, iv) members of the tomato P69 family, and v) tomato LeSBT2. However, these proteins belong to other subtilisin-like subgroups. Relatively little is known about proteins in this subgroup.


Pssm-ID: 240122 [Multi-domain]  Cd Length: 118  Bit Score: 38.46  E-value: 1.80e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21314755  86 KAVVVPWGSCHFLEKARIAQKGGAEAMLVVNNSVLFPPSGNRSEFPDVKILIAFISYKDFRDMNQTLGDNITV 158
Cdd:cd04818  42 KIALIDRGTCNFTVKVLNAQNAGAIAVIVANNVAGGAPITMGGDDPDITIPAVMISQADGDALKAALAAGGTV 114
PA_C5a_like cd02133
PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a ...
81-159 3.35e-03

PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a peptidase. This group contains various PA domain-containing proteins similar to S. pyogenes C5a, including, i) Vpr, a minor extracellular serine protease from Bacillus subtilis, ii) a large molecular mass collagenolytic protease from Geobacillus collagenovorans MO-1, and iii) PrtS, a cell envelope protease from Streptococcus thermophilus CNRZ 385. Proteins in this group belong to the peptidase S8 family. C5a peptidase is a cell surface serine protease which specifically inactivates C5a [a chemotactic peptide, which attracts polymorphonuclear leukocytes (PMNs)], by cleaving it to release a 7-residue carboxy-terminal fragment which contains the PMN binding site. The significance of the PA domain to these proteins 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: 239048 [Multi-domain]  Cd Length: 143  Bit Score: 38.04  E-value: 3.35e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21314755  81 VGIKSKAVVVPWGSCHFLEKARIAQKGGAEAMLVVNNSvlfPPSGNRSEFPDVKILIAFISYKDFRDMNQTLGDNITVK 159
Cdd:cd02133  44 KDVKGKIALIQRGEITFVEKIANAKAAGAVGVIIYNNV---DGLIPGTLGEAVFIPVVFISKEDGEALKAALESSKKLT 119
 
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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