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Conserved domains on  [gi|1907142653|ref|XP_036018348|]
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signal peptide peptidase-like 2A isoform X1 [Mus musculus]

Protein Classification

PA and Peptidase_A22B domain-containing protein( domain architecture ID 11978233)

PA 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 ...
214-517 2.61e-112

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: 335.04  E-value: 2.61e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653 214 KKKDDYLTFSPLTVVVFVVICCIMIVLLYFFYR-WLVYVMIAIFCIASSMSLYNCLSALIHRMPCGQCTI-----LCCGK 287
Cdd:pfam04258   1 KSSDDFETITKIHAICFPITASCTLLLLYFFFKsLLVYVLTIYFCILGIIALAFCLSPFLTRLFFNKCPLkniklPFLPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653 288 NIKVSLIFLSGLCISVAVVWAVFRNEdrwaWILQDILGIAFCLNLIKTMKLPNFMSCVILLGLLLIYDVFFVFITPFItk 367
Cdd:pfam04258  81 RFSYSELVALLLCIVFAVWWALKRHE----WILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDIFWVFGSPYI-- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653 368 NGESIMVELAAGPFENAEKndgnfveatalhtaphekLPVVIRVPKlmgYSVMSVCSVPVSVLGFGDIIVPGLLIAYCRR 447
Cdd:pfam04258 155 FGTSVMVTVATGPSSTGED------------------IPMKLVFPR---LSNMFDNWGPFSMLGLGDIVMPGLLIALCLR 213
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907142653 448 FDVQTGS---SIYYISSTIAYAVGMIITFVVLMVMKTGQPALLYLVPCTLITVSVVAWSRKEMKKFWKGSSYQ 517
Cdd:pfam04258 214 FDISKKKsthDIYFISTMIAYGLGLLITFVALNLFKAAQPALLYLVPCTLGTLLLLALWRGELKKLWNYGEST 286
PA super family cl28883
PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ...
44-163 3.57e-48

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: 162.95  E-value: 3.57e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653  44 YCMYYNNNWTRLPSSLENATSLSLMNLTGTALCHLSDIPPDGIRNKAVVVHWGPCHFLEKARIAQEGGAAALLIANNSVL 123
Cdd:cd02129     1 YCILYNSQWASLPSDLDKATLLPLRNLTSSVLCSASDVPPGGLKGKAVVVMRGNCTFYEKARLAQSLGAEGLLIVSRERL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907142653 124 IPSSRNKSTFQNVTVLIAVITQKDFKDMKETLGDDITVKM 163
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 ...
214-517 2.61e-112

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: 335.04  E-value: 2.61e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653 214 KKKDDYLTFSPLTVVVFVVICCIMIVLLYFFYR-WLVYVMIAIFCIASSMSLYNCLSALIHRMPCGQCTI-----LCCGK 287
Cdd:pfam04258   1 KSSDDFETITKIHAICFPITASCTLLLLYFFFKsLLVYVLTIYFCILGIIALAFCLSPFLTRLFFNKCPLkniklPFLPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653 288 NIKVSLIFLSGLCISVAVVWAVFRNEdrwaWILQDILGIAFCLNLIKTMKLPNFMSCVILLGLLLIYDVFFVFITPFItk 367
Cdd:pfam04258  81 RFSYSELVALLLCIVFAVWWALKRHE----WILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDIFWVFGSPYI-- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653 368 NGESIMVELAAGPFENAEKndgnfveatalhtaphekLPVVIRVPKlmgYSVMSVCSVPVSVLGFGDIIVPGLLIAYCRR 447
Cdd:pfam04258 155 FGTSVMVTVATGPSSTGED------------------IPMKLVFPR---LSNMFDNWGPFSMLGLGDIVMPGLLIALCLR 213
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907142653 448 FDVQTGS---SIYYISSTIAYAVGMIITFVVLMVMKTGQPALLYLVPCTLITVSVVAWSRKEMKKFWKGSSYQ 517
Cdd:pfam04258 214 FDISKKKsthDIYFISTMIAYGLGLLITFVALNLFKAAQPALLYLVPCTLGTLLLLALWRGELKKLWNYGEST 286
PSN smart00730
Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic ...
219-504 3.19e-65

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: 212.50  E-value: 3.19e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653  219 YLTFSPLTVVVFVVICCIMIVLLYFFYRWLVYVMIAIFCIASSMSLYNCLSALIHRMPcgqctilccgkniKVSLIFLSG 298
Cdd:smart00730   2 YSLLNSLVAIVFPIVATFVLVLLYKFFKYLVIVLVIYFSSLGVLFLYSLLYPLEVFRV-------------DYPTLLILL 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653  299 LCISVAVVWAVFRnedRWAWILQDILGIAFCLNLIKTMKLPNFMSCVILLGLLLIYDVFFVFITPFitknGESIMVELAA 378
Cdd:smart00730  69 LNFAVVGFWCIHR---KGAWIQQDLIGISLCMAILFILRLPSEWTAWILLGALFIYDIFAVFGTPG----PLRVMVEVAT 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653  379 GPFENAekndgnfveatalhtaphEKLPVVIRVPKlMGYSVMSVCSVPVSVLGFGDIIVPGLLIAYCRRFDVQTGS-SIY 457
Cdd:smart00730 142 GRDEPI------------------KVFPALLYVPR-LVVSFEDDEEERFSMLGLGDIVFPGILVASAARFDVSVRSdSNY 202
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1907142653  458 YISSTIAYAVGMIITFVVLMVMKTGQPALLYLVPCTLITVSVVAWSR 504
Cdd:smart00730 203 FLACFVAYGIGLILTLVLLALFKKAQPALPYLVPFTLVFYLLTALLR 249
PA_hSPPL_like cd02129
PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like ...
44-163 3.57e-48

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: 162.95  E-value: 3.57e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653  44 YCMYYNNNWTRLPSSLENATSLSLMNLTGTALCHLSDIPPDGIRNKAVVVHWGPCHFLEKARIAQEGGAAALLIANNSVL 123
Cdd:cd02129     1 YCILYNSQWASLPSDLDKATLLPLRNLTSSVLCSASDVPPGGLKGKAVVVMRGNCTFYEKARLAQSLGAEGLLIVSRERL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907142653 124 IPSSRNKSTFQNVTVLIAVITQKDFKDMKETLGDDITVKM 163
Cdd:cd02129    81 VPPSGNRSEYEKIDIPVALLSYKDMLDIQQTFGDSVKVAM 120
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
82-120 2.53e-04

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: 40.19  E-value: 2.53e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907142653  82 PPDGIRNKAVVVHWGPCHFLEKARIAQEGGAAALLIANN 120
Cdd:pfam02225  18 ADFDVKGKIVLVRCTFGFRAEKVRNAQAAGAAGVIIYNN 56
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
96-175 5.19e-04

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 43.11  E-value: 5.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653   96 GPCHFLEKARIAQEGGAAALLIANNSVLIPSSRNKStfqNVTVLIAV--ITQKDFKDMKETL-GDDITVKMYSPSWPNFD 172
Cdd:NF038112   554 GTCDFTVKALNAQNAGAIGVIIANNAAGAAPGLGGT---DPAVTIPAlsITQADGNAWKAALaNGPVTVRLRREPALDRD 630

                   ...
gi 1907142653  173 YTL 175
Cdd:NF038112   631 GTL 633
 
Name Accession Description Interval E-value
Peptidase_A22B pfam04258
Signal peptide peptidase; The members of this family are membrane proteins. In some proteins ...
214-517 2.61e-112

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: 335.04  E-value: 2.61e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653 214 KKKDDYLTFSPLTVVVFVVICCIMIVLLYFFYR-WLVYVMIAIFCIASSMSLYNCLSALIHRMPCGQCTI-----LCCGK 287
Cdd:pfam04258   1 KSSDDFETITKIHAICFPITASCTLLLLYFFFKsLLVYVLTIYFCILGIIALAFCLSPFLTRLFFNKCPLkniklPFLPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653 288 NIKVSLIFLSGLCISVAVVWAVFRNEdrwaWILQDILGIAFCLNLIKTMKLPNFMSCVILLGLLLIYDVFFVFITPFItk 367
Cdd:pfam04258  81 RFSYSELVALLLCIVFAVWWALKRHE----WILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDIFWVFGSPYI-- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653 368 NGESIMVELAAGPFENAEKndgnfveatalhtaphekLPVVIRVPKlmgYSVMSVCSVPVSVLGFGDIIVPGLLIAYCRR 447
Cdd:pfam04258 155 FGTSVMVTVATGPSSTGED------------------IPMKLVFPR---LSNMFDNWGPFSMLGLGDIVMPGLLIALCLR 213
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907142653 448 FDVQTGS---SIYYISSTIAYAVGMIITFVVLMVMKTGQPALLYLVPCTLITVSVVAWSRKEMKKFWKGSSYQ 517
Cdd:pfam04258 214 FDISKKKsthDIYFISTMIAYGLGLLITFVALNLFKAAQPALLYLVPCTLGTLLLLALWRGELKKLWNYGEST 286
PSN smart00730
Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic ...
219-504 3.19e-65

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: 212.50  E-value: 3.19e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653  219 YLTFSPLTVVVFVVICCIMIVLLYFFYRWLVYVMIAIFCIASSMSLYNCLSALIHRMPcgqctilccgkniKVSLIFLSG 298
Cdd:smart00730   2 YSLLNSLVAIVFPIVATFVLVLLYKFFKYLVIVLVIYFSSLGVLFLYSLLYPLEVFRV-------------DYPTLLILL 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653  299 LCISVAVVWAVFRnedRWAWILQDILGIAFCLNLIKTMKLPNFMSCVILLGLLLIYDVFFVFITPFitknGESIMVELAA 378
Cdd:smart00730  69 LNFAVVGFWCIHR---KGAWIQQDLIGISLCMAILFILRLPSEWTAWILLGALFIYDIFAVFGTPG----PLRVMVEVAT 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653  379 GPFENAekndgnfveatalhtaphEKLPVVIRVPKlMGYSVMSVCSVPVSVLGFGDIIVPGLLIAYCRRFDVQTGS-SIY 457
Cdd:smart00730 142 GRDEPI------------------KVFPALLYVPR-LVVSFEDDEEERFSMLGLGDIVFPGILVASAARFDVSVRSdSNY 202
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1907142653  458 YISSTIAYAVGMIITFVVLMVMKTGQPALLYLVPCTLITVSVVAWSR 504
Cdd:smart00730 203 FLACFVAYGIGLILTLVLLALFKKAQPALPYLVPFTLVFYLLTALLR 249
PA_hSPPL_like cd02129
PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like ...
44-163 3.57e-48

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: 162.95  E-value: 3.57e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653  44 YCMYYNNNWTRLPSSLENATSLSLMNLTGTALCHLSDIPPDGIRNKAVVVHWGPCHFLEKARIAQEGGAAALLIANNSVL 123
Cdd:cd02129     1 YCILYNSQWASLPSDLDKATLLPLRNLTSSVLCSASDVPPGGLKGKAVVVMRGNCTFYEKARLAQSLGAEGLLIVSRERL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907142653 124 IPSSRNKSTFQNVTVLIAVITQKDFKDMKETLGDDITVKM 163
Cdd:cd02129    81 VPPSGNRSEYEKIDIPVALLSYKDMLDIQQTFGDSVKVAM 120
PA cd00538
PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ...
57-164 2.36e-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: 2.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653  57 SSLENATSLSLMNLTGTALCHLSDIPPDG--IRNKAVVVHWGPCHFLEKARIAQEGGAAALLIANN--SVLIPSSRNKST 132
Cdd:cd00538    14 LLFNPPSSPVGVVAGPLVGCGYGTTDDSGadVKGKIVLVRRGGCSFSEKVKNAQKAGAKAVIIYNNgdDPGPQMGSVGLE 93
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907142653 133 FQNVTVLIAVITQKDFKDMKETLGDDITVKMY 164
Cdd:cd00538    94 STDPSIPTVGISYADGEALLSLLEAGKTVTVD 125
PA_GO-like cd02132
PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on ...
53-120 2.33e-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: 44.34  E-value: 2.33e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907142653  53 TRLPSSLENATSLSLMNLTGTALCHLSDIPPDGirnKAVVVHWGPCHFLEKARIAQEGGAAALLIANN 120
Cdd:cd02132    28 ASLPSKEDNANKTRAVLANPLDCCSPSTSKLSG---SIALVERGECAFTEKAKIAEAGGASALLIIND 92
PA_SaNapH_like cd04816
PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus ...
72-164 3.24e-05

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: 43.47  E-value: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653  72 GTALCHLSD---IPPDGirnKAVVVHWGPCHFLEKARIAQEGGAAALLIANNS---VLIPS--SRNKstfqNVTVLIAVI 143
Cdd:cd04816    28 RPAGCDASDydgLDVKG---AIVLVDRGGCPFADKQKVAAARGAVAVIVVNNSdggGTAGTlgAPNI----DLKVPVGVI 100
                          90       100
                  ....*....|....*....|.
gi 1907142653 144 TQKDFKDMKETLGDDITVKMY 164
Cdd:cd04816   101 TKAAGAALRRRLGAGETLELD 121
PA_VSR cd02125
PA_VSR: Protease-associated (PA) domain-containing plant vacuolar sorting receptor (VSR). This ...
96-163 4.54e-05

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: 43.24  E-value: 4.54e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907142653  96 GPCHFLEKARIAQEGGAAALLIANNSV--LI-----PSSRNKSTFQNVTVLIAVITQKDFKDMKETL--GDDITVKM 163
Cdd:cd02125    51 GGCFFTLKAWNAQQAGAAAVLVADNVDepLLtmdtpEESGSADYIEKITIPSALITKAFGEKLKKAIsnGEMVVIKL 127
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
82-120 2.53e-04

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: 40.19  E-value: 2.53e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907142653  82 PPDGIRNKAVVVHWGPCHFLEKARIAQEGGAAALLIANN 120
Cdd:pfam02225  18 ADFDVKGKIVLVRCTFGFRAEKVRNAQAAGAAGVIIYNN 56
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
96-175 5.19e-04

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 43.11  E-value: 5.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653   96 GPCHFLEKARIAQEGGAAALLIANNSVLIPSSRNKStfqNVTVLIAV--ITQKDFKDMKETL-GDDITVKMYSPSWPNFD 172
Cdd:NF038112   554 GTCDFTVKALNAQNAGAIGVIIANNAAGAAPGLGGT---DPAVTIPAlsITQADGNAWKAALaNGPVTVRLRREPALDRD 630

                   ...
gi 1907142653  173 YTL 175
Cdd:NF038112   631 GTL 633
PA_PoS1_like cd02124
PA_PoS1_like: Protease-associated (PA) domain PoS1-like. This group includes various PA ...
78-163 1.07e-03

PA_PoS1_like: Protease-associated (PA) domain PoS1-like. This group includes various PA domain-containing proteins similar to Pleurotus ostreatus (Po)S1. PoSl, the main extracellular protease in P. ostreatus is a subtilisin-like serine protease belonging to the peptidase S8 family. Ca2+ and Mn2+ both stimulate the protease activity of (Po)S1. Ca2+ protects PoS1 from autolysis. PoS1 is a monomeric glycoprotein, which may play a role in the regulation of laccases in lignin formation. (Po)S1 participates in the degradation of POXA1b, and in the activation of POXA3, (POXA1b and POXA3 are laccase isoenzymes), but its effect may be indirect. The significance of the PA domain to PoS1 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: 239039  Cd Length: 129  Bit Score: 39.23  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653  78 LSDIPPDgIRNKAVVVHWGPCHFLEKARIAQEGGAAALLIANNSvlipSSRNKSTFQNVTVLIAVITQKDFKDMKETL-- 155
Cdd:cd02124    47 LPDDTPD-LSGYIVLVRRGTCTFATKAANAAAKGAKYVLIYNNG----SGPTDQVGSDADSIIAAVTPEDGEAWIDALaa 121

                  ....*...
gi 1907142653 156 GDDITVKM 163
Cdd:cd02124   122 GSNVTVDF 129
PA_C5a_like cd02133
PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a ...
89-162 1.46e-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: 39.19  E-value: 1.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907142653  89 KAVVVHWGPCHFLEKARIAQEGGAAALLIANNsvlIPSSRNKSTFQNVTVLIAVITQKDFKDMKETLGDDITVK 162
Cdd:cd02133    49 KIALIQRGEITFVEKIANAKAAGAVGVIIYNN---VDGLIPGTLGEAVFIPVVFISKEDGEALKAALESSKKLT 119
PA_1 cd04813
PA_1: Protease-associated (PA) domain subgroup 1. A subgroup of PA-domain containing proteins. ...
86-152 2.15e-03

PA_1: Protease-associated (PA) domain subgroup 1. A subgroup of PA-domain containing proteins. Proteins in this subgroup contain a RING-finger (Really Interesting New Gene) domain C-terminal to this 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 in this group contain a C-terminal RING-finger domain. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases: such as hSPPL2a and 2b, ii) various E3 ubiquitin ligases similar to human GRAIL (gene related to anergy in lymphocytes) protein, iii) various proteins containing a RING finger motif such as Arabidopsis ReMembR-H2 protein, iv) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), v) various plant vacuolar sorting receptors such as Pisum sativum BP-80, vi) prostate-specific membrane antigen (PSMA), vii) yeast aminopeptidase Y viii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, ix) various subtilisin-like proteases such as Cucumisin from the juice of melon fruits, and x) human TfR (transferrin receptor) 1 and human TfR2. The proteins listed above belong to other subgroups; relatively little is known about proteins in this subgroup.


Pssm-ID: 240117 [Multi-domain]  Cd Length: 117  Bit Score: 38.14  E-value: 2.15e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142653  86 IRNKAVVVHWGPCHFLEKARIAQEGGAAALLIANNSV---LIPSSRNKSTfQNVTVLIAVITQKDFKDMK 152
Cdd:cd04813    38 IDGKVALVLRGGCGFLDKVMWAQRRGAKAVIVGDDEPgrgLITMFSNGDT-DNVTIPAMFTSRTSYHLLS 106
 
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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