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Conserved domains on  [gi|612012207|ref|XP_007489391|]
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signal peptide peptidase-like 2B isoform X4 [Monodelphis domestica]

Protein Classification

A22B family peptidase( domain architecture ID 10114778)

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 ...
210-499 5.31e-113

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: 335.81  E-value: 5.31e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612012207  210 DETVDVTPIMIGVFVVMCCSMLVLLYYFYD-HLVYMIITIFCLASSTSLYSCLYPCIKRLPFGKCRVPDNNLPYFHKRPQ 288
Cdd:pfam04258   4 DDFETITKIHAICFPITASCTLLLLYFFFKsLLVYVLTIYFCILGIIALAFCLSPFLTRLFFNKCPLKNIKLPFLPGRFS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612012207  289 IRMLLLAIFCITVSIIWGVFRNEdqwaWVLQDALGIAFCLYMLKTIRLPTFKACTLLLLVLFIYDVFFVFITPFltKSGN 368
Cdd:pfam04258  84 YSELVALLLCIVFAVWWALKRHE----WILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDIFWVFGSPY--IFGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612012207  369 SIMVEVAAGPSDstTHEKLPMVLKVPRLnsSPLALCDRPFSLLGFGDILVPGLLVAYCHRFDIQVQSSR--VYFVACTIA 446
Cdd:pfam04258 158 SVMVTVATGPSS--TGEDIPMKLVFPRL--SNMFDNWGPFSMLGLGDIVMPGLLIALCLRFDISKKKSThdIYFISTMIA 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 612012207  447 YGIGLLITFVALAWMQRGQPALLYLVPCTVITSFVIALWRKELRMFWTGSGFA 499
Cdd:pfam04258 234 YGLGLLITFVALNLFKAAQPALLYLVPCTLGTLLLLALWRGELKKLWNYGEST 286
PA_hSPPL_like cd02129
PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like ...
38-157 6.82e-67

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: 211.10  E-value: 6.82e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612012207  38 YCILYNSQWAHLPPGLGKASLLQLQDQTTSVLCSQSDVPSGGFNNRIPMVMRGNCTFYEKVKLAQMNGARGLLVVSREKL 117
Cdd:cd02129    1 YCILYNSQWASLPSDLDKATLLPLRNLTSSVLCSASDVPPGGLKGKAVVVMRGNCTFYEKARLAQSLGAEGLLIVSRERL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 612012207 118 VPPGGNKTQYDEIGIPVALLSYKDMLDICKTFGHSVRVAL 157
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 ...
210-499 5.31e-113

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: 335.81  E-value: 5.31e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612012207  210 DETVDVTPIMIGVFVVMCCSMLVLLYYFYD-HLVYMIITIFCLASSTSLYSCLYPCIKRLPFGKCRVPDNNLPYFHKRPQ 288
Cdd:pfam04258   4 DDFETITKIHAICFPITASCTLLLLYFFFKsLLVYVLTIYFCILGIIALAFCLSPFLTRLFFNKCPLKNIKLPFLPGRFS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612012207  289 IRMLLLAIFCITVSIIWGVFRNEdqwaWVLQDALGIAFCLYMLKTIRLPTFKACTLLLLVLFIYDVFFVFITPFltKSGN 368
Cdd:pfam04258  84 YSELVALLLCIVFAVWWALKRHE----WILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDIFWVFGSPY--IFGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612012207  369 SIMVEVAAGPSDstTHEKLPMVLKVPRLnsSPLALCDRPFSLLGFGDILVPGLLVAYCHRFDIQVQSSR--VYFVACTIA 446
Cdd:pfam04258 158 SVMVTVATGPSS--TGEDIPMKLVFPRL--SNMFDNWGPFSMLGLGDIVMPGLLIALCLRFDISKKKSThdIYFISTMIA 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 612012207  447 YGIGLLITFVALAWMQRGQPALLYLVPCTVITSFVIALWRKELRMFWTGSGFA 499
Cdd:pfam04258 234 YGLGLLITFVALNLFKAAQPALLYLVPCTLGTLLLLALWRGELKKLWNYGEST 286
PSN smart00730
Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic ...
211-486 2.68e-80

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: 250.25  E-value: 2.68e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612012207   211 ETVDVTPIMIGVFVVMCCSMLVLLYYFYDHLVYMIITIFCLASSTSLYSCLYPCIKRLPFgkcrvpdnnlpyfhkrpqIR 290
Cdd:smart00730   1 EYSLLNSLVAIVFPIVATFVLVLLYKFFKYLVIVLVIYFSSLGVLFLYSLLYPLEVFRVD------------------YP 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612012207   291 MLLLAIFCITVSIIWGVFRNedqWAWVLQDALGIAFCLYMLKTIRLPTFKACTLLLLVLFIYDVFFVFITPFltksGNSI 370
Cdd:smart00730  63 TLLILLLNFAVVGFWCIHRK---GAWIQQDLIGISLCMAILFILRLPSEWTAWILLGALFIYDIFAVFGTPG----PLRV 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612012207   371 MVEVAAGPSDSTthEKLPMVLKVPRLNSSPLALCDRPFSLLGFGDILVPGLLVAYCHRFDIQVQSSRVYFVACTIAYGIG 450
Cdd:smart00730 136 MVEVATGRDEPI--KVFPALLYVPRLVVSFEDDEEERFSMLGLGDIVFPGILVASAARFDVSVRSDSNYFLACFVAYGIG 213
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 612012207   451 LLITFVALAWMQRGQPALLYLVPCTVITSFVIALWR 486
Cdd:smart00730 214 LILTLVLLALFKKAQPALPYLVPFTLVFYLLTALLR 249
PA_hSPPL_like cd02129
PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like ...
38-157 6.82e-67

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: 211.10  E-value: 6.82e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612012207  38 YCILYNSQWAHLPPGLGKASLLQLQDQTTSVLCSQSDVPSGGFNNRIPMVMRGNCTFYEKVKLAQMNGARGLLVVSREKL 117
Cdd:cd02129    1 YCILYNSQWASLPSDLDKATLLPLRNLTSSVLCSASDVPPGGLKGKAVVVMRGNCTFYEKARLAQSLGAEGLLIVSRERL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 612012207 118 VPPGGNKTQYDEIGIPVALLSYKDMLDICKTFGHSVRVAL 157
Cdd:cd02129   81 VPPSGNRSEYEKIDIPVALLSYKDMLDIQQTFGDSVKVAM 120
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
70-145 1.06e-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: 46.74  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612012207   70 CSQSDVPSGGFN--NRIPMVMRGNCTFYEKVKLAQMNGARGLLVVSREKLVPP----GGNKTQYDEIGIPVALLSYKDML 143
Cdd:pfam02225  10 CYAGDGIPADFDvkGKIVLVRCTFGFRAEKVRNAQAAGAAGVIIYNNVEGLGGppgaGGNELYPDGIYIPAVGVSRADGE 89

                  ..
gi 612012207  144 DI 145
Cdd:pfam02225  90 AL 91
T9SSA_dep_M36 NF038113
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
75-141 1.32e-05

T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal T9SS type A sorting domain (see TIGR04131).


Pssm-ID: 468356 [Multi-domain]  Cd Length: 868  Bit Score: 48.11  E-value: 1.32e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612012207  75 VPSGGFNNRIPMVMRGNCTFYEKVKLAQMNGARGLLVVSREKLVPPGGNKTQYDE-IGIPVALLSYKD 141
Cdd:NF038113 462 LNAAALAGKIAVIRRGSCEFAVKVLNAQNAGAIAVIIVNNVPGEPIVMGGGDTGPpITIPSIMISQAD 529
 
Name Accession Description Interval E-value
Peptidase_A22B pfam04258
Signal peptide peptidase; The members of this family are membrane proteins. In some proteins ...
210-499 5.31e-113

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: 335.81  E-value: 5.31e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612012207  210 DETVDVTPIMIGVFVVMCCSMLVLLYYFYD-HLVYMIITIFCLASSTSLYSCLYPCIKRLPFGKCRVPDNNLPYFHKRPQ 288
Cdd:pfam04258   4 DDFETITKIHAICFPITASCTLLLLYFFFKsLLVYVLTIYFCILGIIALAFCLSPFLTRLFFNKCPLKNIKLPFLPGRFS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612012207  289 IRMLLLAIFCITVSIIWGVFRNEdqwaWVLQDALGIAFCLYMLKTIRLPTFKACTLLLLVLFIYDVFFVFITPFltKSGN 368
Cdd:pfam04258  84 YSELVALLLCIVFAVWWALKRHE----WILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDIFWVFGSPY--IFGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612012207  369 SIMVEVAAGPSDstTHEKLPMVLKVPRLnsSPLALCDRPFSLLGFGDILVPGLLVAYCHRFDIQVQSSR--VYFVACTIA 446
Cdd:pfam04258 158 SVMVTVATGPSS--TGEDIPMKLVFPRL--SNMFDNWGPFSMLGLGDIVMPGLLIALCLRFDISKKKSThdIYFISTMIA 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 612012207  447 YGIGLLITFVALAWMQRGQPALLYLVPCTVITSFVIALWRKELRMFWTGSGFA 499
Cdd:pfam04258 234 YGLGLLITFVALNLFKAAQPALLYLVPCTLGTLLLLALWRGELKKLWNYGEST 286
PSN smart00730
Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic ...
211-486 2.68e-80

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: 250.25  E-value: 2.68e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612012207   211 ETVDVTPIMIGVFVVMCCSMLVLLYYFYDHLVYMIITIFCLASSTSLYSCLYPCIKRLPFgkcrvpdnnlpyfhkrpqIR 290
Cdd:smart00730   1 EYSLLNSLVAIVFPIVATFVLVLLYKFFKYLVIVLVIYFSSLGVLFLYSLLYPLEVFRVD------------------YP 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612012207   291 MLLLAIFCITVSIIWGVFRNedqWAWVLQDALGIAFCLYMLKTIRLPTFKACTLLLLVLFIYDVFFVFITPFltksGNSI 370
Cdd:smart00730  63 TLLILLLNFAVVGFWCIHRK---GAWIQQDLIGISLCMAILFILRLPSEWTAWILLGALFIYDIFAVFGTPG----PLRV 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612012207   371 MVEVAAGPSDSTthEKLPMVLKVPRLNSSPLALCDRPFSLLGFGDILVPGLLVAYCHRFDIQVQSSRVYFVACTIAYGIG 450
Cdd:smart00730 136 MVEVATGRDEPI--KVFPALLYVPRLVVSFEDDEEERFSMLGLGDIVFPGILVASAARFDVSVRSDSNYFLACFVAYGIG 213
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 612012207   451 LLITFVALAWMQRGQPALLYLVPCTVITSFVIALWR 486
Cdd:smart00730 214 LILTLVLLALFKKAQPALPYLVPFTLVFYLLTALLR 249
PA_hSPPL_like cd02129
PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like ...
38-157 6.82e-67

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: 211.10  E-value: 6.82e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612012207  38 YCILYNSQWAHLPPGLGKASLLQLQDQTTSVLCSQSDVPSGGFNNRIPMVMRGNCTFYEKVKLAQMNGARGLLVVSREKL 117
Cdd:cd02129    1 YCILYNSQWASLPSDLDKATLLPLRNLTSSVLCSASDVPPGGLKGKAVVVMRGNCTFYEKARLAQSLGAEGLLIVSRERL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 612012207 118 VPPGGNKTQYDEIGIPVALLSYKDMLDICKTFGHSVRVAL 157
Cdd:cd02129   81 VPPSGNRSEYEKIDIPVALLSYKDMLDIQQTFGDSVKVAM 120
PA cd00538
PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ...
74-159 3.66e-10

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: 57.53  E-value: 3.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612012207  74 DVPSGGFNNRIPMVMRGNCTFYEKVKLAQMNGARGLLVVSREK--LVPPGGNKTQYDEIGIPVALLSYKDMLDICKTFGH 151
Cdd:cd00538   39 DDSGADVKGKIVLVRRGGCSFSEKVKNAQKAGAKAVIIYNNGDdpGPQMGSVGLESTDPSIPTVGISYADGEALLSLLEA 118

                 ....*...
gi 612012207 152 SVRVALYA 159
Cdd:cd00538  119 GKTVTVDL 126
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
70-145 1.06e-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: 46.74  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612012207   70 CSQSDVPSGGFN--NRIPMVMRGNCTFYEKVKLAQMNGARGLLVVSREKLVPP----GGNKTQYDEIGIPVALLSYKDML 143
Cdd:pfam02225  10 CYAGDGIPADFDvkGKIVLVRCTFGFRAEKVRNAQAAGAAGVIIYNNVEGLGGppgaGGNELYPDGIYIPAVGVSRADGE 89

                  ..
gi 612012207  144 DI 145
Cdd:pfam02225  90 AL 91
PA_GO-like cd02132
PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on ...
70-138 1.09e-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: 45.11  E-value: 1.09e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612012207  70 CSQSDVPsggFNNRIPMVMRGNCTFYEKVKLAQMNGARGLLVVS-REKLVPPGGNKTQYD-EIGIPVALLS 138
Cdd:cd02132   51 CSPSTSK---LSGSIALVERGECAFTEKAKIAEAGGASALLIINdQEELYKMVCEDNDTSlNISIPVVMIP 118
T9SSA_dep_M36 NF038113
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
75-141 1.32e-05

T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal T9SS type A sorting domain (see TIGR04131).


Pssm-ID: 468356 [Multi-domain]  Cd Length: 868  Bit Score: 48.11  E-value: 1.32e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612012207  75 VPSGGFNNRIPMVMRGNCTFYEKVKLAQMNGARGLLVVSREKLVPPGGNKTQYDE-IGIPVALLSYKD 141
Cdd:NF038113 462 LNAAALAGKIAVIRRGSCEFAVKVLNAQNAGAIAVIIVNNVPGEPIVMGGGDTGPpITIPSIMISQAD 529
PA_GRAIL_like cd02122
PA _GRAIL_like: Protease-associated (PA) domain GRAIL-like. This group includes PA domain ...
84-125 3.50e-05

PA _GRAIL_like: Protease-associated (PA) domain GRAIL-like. This group includes PA domain containing E3 (ubiquitin ligases) similar to human GRAIL (gene related to anergy in lymphocytes) protein. Proteins in this group contain a C3H2C3 RING finger. E3 ubiquitin ligase is part of an enzymic cascade, the end result of which is the ubiquitination of proteins. In this cascade, E1 activates the ubiquitin, the activated ubiquitin is carried by E2, and E3 recognizes the acceptor protein as well as catalyzes the transfer of the activated ubiquitin from E2 to this acceptor. GRAIL, a transmembrane protein localized in the endosomes, controls the development of T cell clonal anergy, and may ubiquitinate membrane-associated targets for T cell activation. GRAIL1 is associated with, and regulated by, two isoforms of otubain 1 (the ubiquitin-specific protease). Additional E3s belonging to this group include human (h)Goliath and Xenopus GREUL1 (Goliath Related E3 Ubiquitin Ligase 1). hGoliath and GRAIL both have the property of self-ubiquitination. hGoliath is expressed in leukocytes; its expression and localization is not modified in leukemia. GREUL1 may play a role in the generation of anterior ectoderm. 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: 239037 [Multi-domain]  Cd Length: 138  Bit Score: 43.83  E-value: 3.50e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 612012207  84 IPMVMRGNCTFYEKVKLAQMNGARGLLVVSreklVPPGGNKT 125
Cdd:cd02122   63 IALIQRGNCTFEEKIKLAAERNASAVVIYN----NPGTGNET 100
PA_SaNapH_like cd04816
PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus ...
50-159 4.23e-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: 43.08  E-value: 4.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612012207  50 PPGLGKASLLQLQDQTTSVlCSQSD---VPSGGfnnRIPMVMRGNCTFYEKVKLAQMNGARGLLVVSREKL-VPPGGNKT 125
Cdd:cd04816   13 PPGGVTAPLVPLDPERPAG-CDASDydgLDVKG---AIVLVDRGGCPFADKQKVAAARGAVAVIVVNNSDGgGTAGTLGA 88
                         90       100       110
                 ....*....|....*....|....*....|....
gi 612012207 126 QYDEIGIPVALLSYKDMLDICKTFGHSVRVALYA 159
Cdd:cd04816   89 PNIDLKVPVGVITKAAGAALRRRLGAGETLELDA 122
PA_1 cd04813
PA_1: Protease-associated (PA) domain subgroup 1. A subgroup of PA-domain containing proteins. ...
72-141 7.49e-05

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: 42.37  E-value: 7.49e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612012207  72 QSDVPSGGFNNRIPMVMRGNCTFYEKVKLAQMNGARGLLVVSREklvPPGGNKTQY-----DEIGIPVALLSYKD 141
Cdd:cd04813   30 CSLQEHAEIDGKVALVLRGGCGFLDKVMWAQRRGAKAVIVGDDE---PGRGLITMFsngdtDNVTIPAMFTSRTS 101
PA_subtilisin_1 cd04818
PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. ...
80-145 1.37e-04

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: 41.55  E-value: 1.37e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612012207  80 FNNRIPMVMRGNCTFYEKVKLAQMNGARGLLV---VSREKLVPPGGNKTQydeIGIPVALLSYKDMLDI 145
Cdd:cd04818   39 FAGKIALIDRGTCNFTVKVLNAQNAGAIAVIVannVAGGAPITMGGDDPD---ITIPAVMISQADGDAL 104
PA_C_RZF_like cd02123
PA_C-RZF_ like: Protease-associated (PA) domain C_RZF-like. This group includes various PA ...
89-157 4.02e-04

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: 40.79  E-value: 4.02e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612012207  89 RGNCTFYEKVKLAQMNGARGLLVVSREK--LVPPGGNKTQYDEIGIPVALLSYKDMLDICKTFGHSVRVAL 157
Cdd:cd02123   75 RGNCSFETKVRNAQRAGYKAAIVYNDESndLISMSGNDQEIKGIDIPSVFVGKSTGEILKKYASYEKGVIL 145
PA_EDEM3_like cd02126
PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This ...
83-137 2.38e-03

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: 38.11  E-value: 2.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612012207  83 RIPMVMRGNCTFYEKVKLAQMNGARGLLVVSREklvpPG------------GNKTQYDEIGIPVALL 137
Cdd:cd02126   42 KIAIMERGDCMFVEKARRVQKAGAIGGIVIDNN----EGsssdtapmfamsGDGDSTDDVTIPVVFL 104
PA_ScAPY_like cd02130
PA_ScAPY_like: Protease-associated domain containing proteins like Saccharomyces cerevisiae ...
70-141 7.35e-03

PA_ScAPY_like: Protease-associated domain containing proteins like Saccharomyces cerevisiae aminopeptidase Y (ScAPY). This group contains various PA domain-containing proteins similar to the S. cerevisiae APY, including Trichophyton rubrum leucine aminopeptidase 1(LAP1). Proteins in this group belong to the peptidase M28 family. ScAPY hydrolyzes amino acid-4-methylcoumaryl-7-amides (MCAs). ScAPY more rapidly hydrolyzes dipeptidyl-MCAs. Hydrolysis of amino acid-MCAs or dipeptides is stimulated by Co2+ while the hydrolysis of dipeptidyl-MCAs, tripeptides, and longer peptides is inhibited by Co2+. ScAPY is vacuolar and is activated by proteolytic processing. LAP1 is a secreted leucine aminopeptidase. 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: 239045 [Multi-domain]  Cd Length: 122  Bit Score: 36.47  E-value: 7.35e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612012207  70 CSQSDVPSGGFNNrIPMVMRGNCTFYEKVKLAQMNGARGLLVVSREKLVPPGGNKTQYDEIGIPVALLSYKD 141
Cdd:cd02130   34 CDAADYPASVAGN-IALIERGECPFGDKSALAGAAGAAAAIIYNNVPAGGLSGTLGEPSGPYVPTVGISQED 104
 
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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