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Conserved domains on  [gi|446601030|ref|WP_000678376|]
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MULTISPECIES: papain-like cysteine protease family protein [Bacillus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_C70 super family cl24120
Papain-like cysteine protease AvrRpt2; This is a family of cysteine proteases, found in ...
 116-251 6.44e-12

Papain-like cysteine protease AvrRpt2; This is a family of cysteine proteases, found in actinobacteria, protobacteria and firmicutes. Papain-like cysteine proteases play a crucial role in plant-pathogen/pest interactions. On entering the host they act on non-self substrates, thereby manipulating the host to evade proteolysis. AvrRpt2 from Pseudomonas syringae pv. tomato DC3000 triggers resistance to P. syringae-2-dependent defence responses, including hypersensitive cell death, by cleaving the Arabidopsis RIN4 protein which is monitored by the cognate resistance protein RPS2.


The actual alignment was detected with superfamily member pfam12385:

Pssm-ID: 403550 [Multi-domain]  Cd Length: 143  Bit Score: 61.71  E-value: 6.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601030  116 KLSVPNILQERSNWCWAGTSVSVLNYFGKTP-SQDQYVRYVKGGS-YNNPATSREIQYGLSGYGVSS-AISSGAKSYDWF 192
Cdd:pfam12385   4 ALDVPYNVQQAAMGCWAASASMIAGYRGQKPiDPSEIAALVPGWSqYDTGLNGPEDIALAEKWGLGNvPEPPQSYSIDAL 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446601030  193 KSQINSNQPMIVLIMWQNGAnIGHFLVLDGFYKGTNGtdyITYMDPWYGDHYNHNFSTF 251
Cdd:pfam12385  84 VKLLRAYGPLWCAIAWPGGF-VGHAIVLTGIDEDGTP---VYYHDPWSGPRREVSLASF 138
 
Name Accession Description Interval E-value
Peptidase_C70 pfam12385
Papain-like cysteine protease AvrRpt2; This is a family of cysteine proteases, found in ...
 116-251 6.44e-12

Papain-like cysteine protease AvrRpt2; This is a family of cysteine proteases, found in actinobacteria, protobacteria and firmicutes. Papain-like cysteine proteases play a crucial role in plant-pathogen/pest interactions. On entering the host they act on non-self substrates, thereby manipulating the host to evade proteolysis. AvrRpt2 from Pseudomonas syringae pv. tomato DC3000 triggers resistance to P. syringae-2-dependent defence responses, including hypersensitive cell death, by cleaving the Arabidopsis RIN4 protein which is monitored by the cognate resistance protein RPS2.


Pssm-ID: 403550 [Multi-domain]  Cd Length: 143  Bit Score: 61.71  E-value: 6.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601030  116 KLSVPNILQERSNWCWAGTSVSVLNYFGKTP-SQDQYVRYVKGGS-YNNPATSREIQYGLSGYGVSS-AISSGAKSYDWF 192
Cdd:pfam12385   4 ALDVPYNVQQAAMGCWAASASMIAGYRGQKPiDPSEIAALVPGWSqYDTGLNGPEDIALAEKWGLGNvPEPPQSYSIDAL 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446601030  193 KSQINSNQPMIVLIMWQNGAnIGHFLVLDGFYKGTNGtdyITYMDPWYGDHYNHNFSTF 251
Cdd:pfam12385  84 VKLLRAYGPLWCAIAWPGGF-VGHAIVLTGIDEDGTP---VYYHDPWSGPRREVSLASF 138
Peptidase_C39A cd02549
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 124-251 5.01e-05

A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature or have different domain architectures.


Pssm-ID: 239109 [Multi-domain]  Cd Length: 141  Bit Score: 42.40  E-value: 5.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601030 124 QERSNWCWAGTSVSVLNYFGKTPSQDQYVRYVKGGSYNNPatsreiQYGLSGYGVSSAIssgAKSYDWFKSQINSNQPMI 203
Cdd:cd02549    1 PQLENGCGPTSLAMVLSYLGVKVTKPQLAAEGNTYDFAKD------GYGTYPKPIVSAA---ARKYGLVVRPLTGLLALL 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446601030 204 --------VLIMWQNGANI---GHFLVLDGFykgtNGTDYITYMDPWYGDHYNHNFSTF 251
Cdd:cd02549   72 rqlaaghpVIVSVNLGVSItpsGHAMVVIGY----DRKGNVYVNDPGGGRRLVVSFDEF 126
YvpB COG4990
Predicted cysteine peptidase, C39 family [General function prediction only];
8-251 3.69e-03

Predicted cysteine peptidase, C39 family [General function prediction only];


Pssm-ID: 444014 [Multi-domain]  Cd Length: 303  Bit Score: 38.25  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601030   8 IVCMVLLFFTFSFIGVQKIIAEEVEFSGTTAPLNVN--VREAKSLNANIVDVIPGNTKvsfkGWEYGEAVKDYWTGNLDN 85
Cdd:COG4990    8 LLSFILGGGTAGSTYFKKVETKKTGDKIARVLLALTltKVLKTVLKKVAVDSLALKEK----TKAALGLARVYGVSSYGL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601030  86 RWFYYFKDG-KKVYVTSAYINGNPPSTPIDRKLSVPNILQERS--NWCWAGTSVSVLNYFGKTPSQDQYVRYVK------ 156
Cdd:COG4990   84 ARSAVRVSLtGELPAPGMKKIIYPKPNPDSVLLNVPYISQLPElpTGCEVTSLAMLLNYYGIDVTKDELAEYLPkvplpy 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601030 157 GGSYNNPAT--SREIQYGLSGYGVS-SAISSGAKSYDWFK-------------SQINSNQPMIVLI-----------MWQ 209
Cdd:COG4990  164 NGYGGNPNKgfVGDPYGSDPGYGVYaPPIAQLAKKYLPGKavdltgasfedilDELASGNPVIVWTtldfsppsafrSWT 243

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 446601030 210 --NGANI-----GHFLVLDGFYKgtngtDYITYMDPWYGD-HYNHNFSTF 251
Cdd:COG4990  244 tpDGKTFdftanEHAVVVTGYDD-----EGVYVNDPLGGNkYVKYSRSLF 288
 
Name Accession Description Interval E-value
Peptidase_C70 pfam12385
Papain-like cysteine protease AvrRpt2; This is a family of cysteine proteases, found in ...
 116-251 6.44e-12

Papain-like cysteine protease AvrRpt2; This is a family of cysteine proteases, found in actinobacteria, protobacteria and firmicutes. Papain-like cysteine proteases play a crucial role in plant-pathogen/pest interactions. On entering the host they act on non-self substrates, thereby manipulating the host to evade proteolysis. AvrRpt2 from Pseudomonas syringae pv. tomato DC3000 triggers resistance to P. syringae-2-dependent defence responses, including hypersensitive cell death, by cleaving the Arabidopsis RIN4 protein which is monitored by the cognate resistance protein RPS2.


Pssm-ID: 403550 [Multi-domain]  Cd Length: 143  Bit Score: 61.71  E-value: 6.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601030  116 KLSVPNILQERSNWCWAGTSVSVLNYFGKTP-SQDQYVRYVKGGS-YNNPATSREIQYGLSGYGVSS-AISSGAKSYDWF 192
Cdd:pfam12385   4 ALDVPYNVQQAAMGCWAASASMIAGYRGQKPiDPSEIAALVPGWSqYDTGLNGPEDIALAEKWGLGNvPEPPQSYSIDAL 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446601030  193 KSQINSNQPMIVLIMWQNGAnIGHFLVLDGFYKGTNGtdyITYMDPWYGDHYNHNFSTF 251
Cdd:pfam12385  84 VKLLRAYGPLWCAIAWPGGF-VGHAIVLTGIDEDGTP---VYYHDPWSGPRREVSLASF 138
Peptidase_C39_2 pfam13529
Peptidase_C39 like family;
119-238 7.26e-08

Peptidase_C39 like family;


Pssm-ID: 379241 [Multi-domain]  Cd Length: 139  Bit Score: 50.52  E-value: 7.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601030  119 VPNILQ--ERSNWCwAGTSVS-VLNYFGKTPSQDQYVRYVKGGSYNNPATSREI-QYGLSGYGVSS------AISSGAKS 188
Cdd:pfam13529   2 VPYYNQldELPNGC-GPTSLAmVLSYLGITVTQDELAKEIGTNPDGNPNTGFVGnPYDKSGYGVYNppivalAEKYGLKV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446601030  189 YDWF-------KSQINSNQPMIVLIMWQN-----GANIGHFLVLDGFykgTNGTDYITYMDP 238
Cdd:pfam13529  81 TDITgssfdevIRLLDAGIPVVVSTTTFGplnyyFTSSGHLVVIVGY---DDKGDYVYVNDP 139
Peptidase_C39A cd02549
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 124-251 5.01e-05

A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature or have different domain architectures.


Pssm-ID: 239109 [Multi-domain]  Cd Length: 141  Bit Score: 42.40  E-value: 5.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601030 124 QERSNWCWAGTSVSVLNYFGKTPSQDQYVRYVKGGSYNNPatsreiQYGLSGYGVSSAIssgAKSYDWFKSQINSNQPMI 203
Cdd:cd02549    1 PQLENGCGPTSLAMVLSYLGVKVTKPQLAAEGNTYDFAKD------GYGTYPKPIVSAA---ARKYGLVVRPLTGLLALL 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446601030 204 --------VLIMWQNGANI---GHFLVLDGFykgtNGTDYITYMDPWYGDHYNHNFSTF 251
Cdd:cd02549   72 rqlaaghpVIVSVNLGVSItpsGHAMVVIGY----DRKGNVYVNDPGGGRRLVVSFDEF 126
YvpB COG4990
Predicted cysteine peptidase, C39 family [General function prediction only];
8-251 3.69e-03

Predicted cysteine peptidase, C39 family [General function prediction only];


Pssm-ID: 444014 [Multi-domain]  Cd Length: 303  Bit Score: 38.25  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601030   8 IVCMVLLFFTFSFIGVQKIIAEEVEFSGTTAPLNVN--VREAKSLNANIVDVIPGNTKvsfkGWEYGEAVKDYWTGNLDN 85
Cdd:COG4990    8 LLSFILGGGTAGSTYFKKVETKKTGDKIARVLLALTltKVLKTVLKKVAVDSLALKEK----TKAALGLARVYGVSSYGL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601030  86 RWFYYFKDG-KKVYVTSAYINGNPPSTPIDRKLSVPNILQERS--NWCWAGTSVSVLNYFGKTPSQDQYVRYVK------ 156
Cdd:COG4990   84 ARSAVRVSLtGELPAPGMKKIIYPKPNPDSVLLNVPYISQLPElpTGCEVTSLAMLLNYYGIDVTKDELAEYLPkvplpy 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601030 157 GGSYNNPAT--SREIQYGLSGYGVS-SAISSGAKSYDWFK-------------SQINSNQPMIVLI-----------MWQ 209
Cdd:COG4990  164 NGYGGNPNKgfVGDPYGSDPGYGVYaPPIAQLAKKYLPGKavdltgasfedilDELASGNPVIVWTtldfsppsafrSWT 243

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 446601030 210 --NGANI-----GHFLVLDGFYKgtngtDYITYMDPWYGD-HYNHNFSTF 251
Cdd:COG4990  244 tpDGKTFdftanEHAVVVTGYDD-----EGVYVNDPLGGNkYVKYSRSLF 288
 
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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