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Conserved domains on  [gi|332194506|gb|AEE32627|]
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DegP protease 6 [Arabidopsis thaliana]

Protein Classification

S1 family peptidase( domain architecture ID 10595581)

S1 family peptidase is a serine endopeptidase containing the catalytic triad His, Asp and Ser; such as peroxisomal leader peptide-processing protease

EC:  3.4.21.-
Gene Ontology:  GO:0008236|GO:0008233|GO:0006508|GO:0004252
MEROPS:  S1
PubMed:  9383148|25664608|29785722|31895561|9374470

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 85-201 4.25e-15

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


:

Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 69.37  E-value: 4.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332194506   85 SGFAIS-GRRILTNAHVVGDHLYLQVRKHGSPTK----YKAEVKAFRYGCDLAILGIDSEEFWEDINPLELGGIPFIGET 159
Cdd:pfam13365   2 TGFVVSsDGLVLTNAHVVDDAEEAAVELVSVVLAdgreYPATVVARDPDLDLALLRVSGDGRGLPPLPLGDSEPLVGGER 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 332194506  160 VYALGYPRGGDTISVTKGIVTRVEPQKYSHSSIKMYVYT-------SGG 201
Cdd:pfam13365  82 VYAVGYPLGGEKLSLSEGIVSGVDEGRDGGDDGRVIQTDaalspgsSGG 130
 
Name Accession Description Interval E-value
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 85-201 4.25e-15

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 69.37  E-value: 4.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332194506   85 SGFAIS-GRRILTNAHVVGDHLYLQVRKHGSPTK----YKAEVKAFRYGCDLAILGIDSEEFWEDINPLELGGIPFIGET 159
Cdd:pfam13365   2 TGFVVSsDGLVLTNAHVVDDAEEAAVELVSVVLAdgreYPATVVARDPDLDLALLRVSGDGRGLPPLPLGDSEPLVGGER 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 332194506  160 VYALGYPRGGDTISVTKGIVTRVEPQKYSHSSIKMYVYT-------SGG 201
Cdd:pfam13365  82 VYAVGYPLGGEKLSLSEGIVSGVDEGRDGGDDGRVIQTDaalspgsSGG 130
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 85-182 1.61e-13

Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440035 [Multi-domain]  Cd Length: 274  Bit Score: 67.48  E-value: 1.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332194506  85 SGFAISGR-RILTNAHVVGDHLYLQVRKHGSpTKYKAEVKAFRYGCDLAILGIDSeefwEDINPLELG--GIPFIGETVY 161
Cdd:COG0265    4 SGVIISPDgYILTNNHVVEGADEITVTLADG-REYPAKVVGRDPLTDLAVLKIDA----KDLPAAPLGdsDKLRVGDWVL 78

                         90       100
                 ....*....|....*....|.
gi 332194506 162 ALGYPRGGDTiSVTKGIVTRV 182
Cdd:COG0265   79 AIGNPFGLGQ-TVTAGIVSAL 98
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 85-169 3.08e-07

MarP family serine protease; The founding member of this family of membrane-spanning serine proteases, which is restricted to Actinobacteria, is the acid resistance periplasmic serine protease MarP of Mycobacterium tuberculosis. Recent work shows that MarP is required to cleave and activate the peptidoglycan hydrolase RipA, and loss of RipA activity creates a defect in progeny separation during cell division. Therefore, the requirement for MarP in order to survive acidic conditions may be a consequence of peptidoglycan hydrolysis requirements, explaining why MarP family members are distributed more broadly in the Actinobacteria than the subset of species capable of surviving intracellularly as pathogens.


Pssm-ID: 468161 [Multi-domain]  Cd Length: 390  Bit Score: 49.80  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332194506  85 SGFAISGRRILTNAHVVG--DHLYLQVRkhGSPTkYKAEVKAFRYGCDLAILGIDSeefwEDINPLELGGIP-FIGETVY 161
Cdd:NF033740 214 SGFVVAPDRVMTNAHVVAgtDEVTVETV--GGGT-LDARVVYYDPDRDIAVLAVPG----LGLPPLPFADEPaETGDDAI 286


                 ....*...
gi 332194506 162 ALGYPRGG 169
Cdd:NF033740 287 VLGYPEGG 294
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 63-179 2.01e-05

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 44.52  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332194506   63 FSFSREPNvvQPWQTTEKEYSS--SGFAIS-GRRILTNAHVVGDHLYLQVRKHgSPTKYKAEV--KAFRYgcDLAILGID 137
Cdd:TIGR02037  39 FFGDDMPD--FPRQQREQKVRGlgSGVIISaDGYVLTNNHVVDGADEITVTLS-DGREFKAKLvgKDPRT--DIAVLKID 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 332194506  138 SEEfwedinplELGGIPF-------IGETVYALGYPRGGDTiSVTKGIV 179
Cdd:TIGR02037 114 AKK--------NLPVIKLgdsdklrVGDWVLAIGNPFGLGQ-TVTSGIV 153
 
Name Accession Description Interval E-value
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 85-201 4.25e-15

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 69.37  E-value: 4.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332194506   85 SGFAIS-GRRILTNAHVVGDHLYLQVRKHGSPTK----YKAEVKAFRYGCDLAILGIDSEEFWEDINPLELGGIPFIGET 159
Cdd:pfam13365   2 TGFVVSsDGLVLTNAHVVDDAEEAAVELVSVVLAdgreYPATVVARDPDLDLALLRVSGDGRGLPPLPLGDSEPLVGGER 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 332194506  160 VYALGYPRGGDTISVTKGIVTRVEPQKYSHSSIKMYVYT-------SGG 201
Cdd:pfam13365  82 VYAVGYPLGGEKLSLSEGIVSGVDEGRDGGDDGRVIQTDaalspgsSGG 130
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 85-182 1.61e-13

Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440035 [Multi-domain]  Cd Length: 274  Bit Score: 67.48  E-value: 1.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332194506  85 SGFAISGR-RILTNAHVVGDHLYLQVRKHGSpTKYKAEVKAFRYGCDLAILGIDSeefwEDINPLELG--GIPFIGETVY 161
Cdd:COG0265    4 SGVIISPDgYILTNNHVVEGADEITVTLADG-REYPAKVVGRDPLTDLAVLKIDA----KDLPAAPLGdsDKLRVGDWVL 78

                         90       100
                 ....*....|....*....|.
gi 332194506 162 ALGYPRGGDTiSVTKGIVTRV 182
Cdd:COG0265   79 AIGNPFGLGQ-TVTAGIVSAL 98
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 85-169 3.08e-07

MarP family serine protease; The founding member of this family of membrane-spanning serine proteases, which is restricted to Actinobacteria, is the acid resistance periplasmic serine protease MarP of Mycobacterium tuberculosis. Recent work shows that MarP is required to cleave and activate the peptidoglycan hydrolase RipA, and loss of RipA activity creates a defect in progeny separation during cell division. Therefore, the requirement for MarP in order to survive acidic conditions may be a consequence of peptidoglycan hydrolysis requirements, explaining why MarP family members are distributed more broadly in the Actinobacteria than the subset of species capable of surviving intracellularly as pathogens.


Pssm-ID: 468161 [Multi-domain]  Cd Length: 390  Bit Score: 49.80  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332194506  85 SGFAISGRRILTNAHVVG--DHLYLQVRkhGSPTkYKAEVKAFRYGCDLAILGIDSeefwEDINPLELGGIP-FIGETVY 161
Cdd:NF033740 214 SGFVVAPDRVMTNAHVVAgtDEVTVETV--GGGT-LDARVVYYDPDRDIAVLAVPG----LGLPPLPFADEPaETGDDAI 286


                 ....*...
gi 332194506 162 ALGYPRGG 169
Cdd:NF033740 287 VLGYPEGG 294
Trypsin pfam00089
Trypsin;
73-169 1.01e-05

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 44.74  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332194506   73 QPWQ----TTEKEYSSSGFAISGRRILTNAHVVGDHLYLQVR------KHGSPTKYKAEVKAF---------RYGCDLAI 133
Cdd:pfam00089  12 FPWQvslqLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVlgahniVLREGGEQKFDVEKIivhpnynpdTLDNDIAL 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 332194506  134 LGIDSE-EFWEDINPLEL---GGIPFIGETVYALGYPRGG 169
Cdd:pfam00089  92 LKLESPvTLGDTVRPICLpdaSSDLPVGTTCTVSGWGNTK 131
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 63-179 2.01e-05

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 44.52  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332194506   63 FSFSREPNvvQPWQTTEKEYSS--SGFAIS-GRRILTNAHVVGDHLYLQVRKHgSPTKYKAEV--KAFRYgcDLAILGID 137
Cdd:TIGR02037  39 FFGDDMPD--FPRQQREQKVRGlgSGVIISaDGYVLTNNHVVDGADEITVTLS-DGREFKAKLvgKDPRT--DIAVLKID 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 332194506  138 SEEfwedinplELGGIPF-------IGETVYALGYPRGGDTiSVTKGIV 179
Cdd:TIGR02037 114 AKK--------NLPVIKLgdsdklrVGDWVLAIGNPFGLGQ-TVTSGIV 153
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 85-202 2.69e-04

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 40.43  E-value: 2.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332194506  85 SGFAISGRRILTNAHVV--------------------GDHLYLQVRKHGSPTKYKAEvkaFRYGCDLAILGIDsEEFWED 144
Cdd:COG3591   15 TGTLIGPNLVLTAGHCVydgagggwatnivfvpgyngGPYGTATATRFRVPPGWVAS---GDAGYDYALLRLD-EPLGDT 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332194506 145 INPLELG--GIPFIGETVYALGYPRG-GDTISVTK-GIVTRVEPQKYSHSsikmyVYTSGGS 202
Cdd:COG3591   91 TGWLGLAfnDAPLAGEPVTIIGYPGDrPKDLSLDCsGRVTGVQGNRLSYD-----CDTTGGS 147
 
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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