NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|22327839|ref|NP_680437|]
View 

Trypsin family protein [Arabidopsis thaliana]

Protein Classification

serine protease( domain architecture ID 10595581)

serine protease such as Arabidopsis thaliana DegS which functions as a trimer to catalyze the initial rate-limiting step in a proteolytic cascade that ultimately activates transcription of stress response genes in the cytoplasm

Gene Ontology:  GO:0008236|GO:0008233|GO:0006508
PubMed:  29180814

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 72-180 2.05e-13

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


:

Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 64.36  E-value: 2.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327839    72 SGFAIS-GRRILTNAHVVGDHSYLQVRKHGSPTK----YKAEVKAFG----------IFGARRYTFI----------GET 126
Cdd:pfam13365   2 TGFVVSsDGLVLTNAHVVDDAEEAAVELVSVVLAdgreYPATVVARDpdldlallrvSGDGRGLPPLplgdseplvgGER 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 22327839   127 IYALGYPRDGDIISVTKGIVTRVEPQKYAHSSIEIltIQTDACINGGKSGGPVV 180
Cdd:pfam13365  82 VYAVGYPLGGEKLSLSEGIVSGVDEGRDGGDDGRV--IQTDAALSPGSSGGPVF 133
 
Name Accession Description Interval E-value
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 72-180 2.05e-13

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 64.36  E-value: 2.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327839    72 SGFAIS-GRRILTNAHVVGDHSYLQVRKHGSPTK----YKAEVKAFG----------IFGARRYTFI----------GET 126
Cdd:pfam13365   2 TGFVVSsDGLVLTNAHVVDDAEEAAVELVSVVLAdgreYPATVVARDpdldlallrvSGDGRGLPPLplgdseplvgGER 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 22327839   127 IYALGYPRDGDIISVTKGIVTRVEPQKYAHSSIEIltIQTDACINGGKSGGPVV 180
Cdd:pfam13365  82 VYAVGYPLGGEKLSLSEGIVSGVDEGRDGGDDGRV--IQTDAALSPGSSGGPVF 133
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 72-180 2.64e-12

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: 63.63  E-value: 2.64e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327839  72 SGFAISGR-RILTNAHVVGDHSYLQVRKHGSpTKYKAEVKAFG------------------IFGARRYTFIGETIYALGY 132
Cdd:COG0265   4 SGVIISPDgYILTNNHVVEGADEITVTLADG-REYPAKVVGRDpltdlavlkidakdlpaaPLGDSDKLRVGDWVLAIGN 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 22327839 133 PRDGDIiSVTKGIVTRVE-PQKYAHSSIEILTIQTDACINGGKSGGPVV 180
Cdd:COG0265  83 PFGLGQ-TVTAGIVSALGrSIGSSGGGTYDDFIQTDAAINPGNSGGPLV 130
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 31-190 2.99e-06

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: 46.72  E-value: 2.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327839   31 ATPRALRDidlAQDSVVKI----FSFSREPnvvqpwqttekeySSSGFAISGRRILTNAHVVGDHSYLQVRKHGSPTkYK 106
Cdd:NF033740 185 ATSPAVRR---ARPSVVKVrgtaPSCGRAL-------------EGSGFVVAPDRVMTNAHVVAGTDEVTVETVGGGT-LD 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327839  107 AEVKAF------------------GIFG---ARRytfiGETIYALGYPRDG----------DIISVT------KGIVTRv 149
Cdd:NF033740 248 ARVVYYdpdrdiavlavpglglppLPFAdepAET----GDDAIVLGYPEGGpftatparvrERIALSgpdiygSGTVTR- 322

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 22327839  150 epqkyahssiEILTIQTDacINGGKSGGPVV-MGNKVAGVVF 190
Cdd:NF033740 323 ----------EVYTLRGT--VRPGNSGGPLLdPDGRVLGVVF 352
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 50-180 5.59e-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: 42.98  E-value: 5.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327839    50 FSFSREPNvvQPWQTTEKEYSS--SGFAIS-GRRILTNAHVVGDHSYLQVRKHgSPTKYKAE--------------VKAF 112
Cdd:TIGR02037  39 FFGDDMPD--FPRQQREQKVRGlgSGVIISaDGYVLTNNHVVDGADEITVTLS-DGREFKAKlvgkdprtdiavlkIDAK 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327839   113 GI-----FGARRYTFIGETIYALGYPRdGDIISVTKGIVTRVepqkyAHSSIEILT----IQTDACINGGKSGGPVV 180
Cdd:TIGR02037 116 KNlpvikLGDSDKLRVGDWVLAIGNPF-GLGQTVTSGIVSAL-----GRSGLGIGDyenfIQTDAAINPGNSGGPLV 186
 
Name Accession Description Interval E-value
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 72-180 2.05e-13

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 64.36  E-value: 2.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327839    72 SGFAIS-GRRILTNAHVVGDHSYLQVRKHGSPTK----YKAEVKAFG----------IFGARRYTFI----------GET 126
Cdd:pfam13365   2 TGFVVSsDGLVLTNAHVVDDAEEAAVELVSVVLAdgreYPATVVARDpdldlallrvSGDGRGLPPLplgdseplvgGER 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 22327839   127 IYALGYPRDGDIISVTKGIVTRVEPQKYAHSSIEIltIQTDACINGGKSGGPVV 180
Cdd:pfam13365  82 VYAVGYPLGGEKLSLSEGIVSGVDEGRDGGDDGRV--IQTDAALSPGSSGGPVF 133
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 72-180 2.64e-12

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: 63.63  E-value: 2.64e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327839  72 SGFAISGR-RILTNAHVVGDHSYLQVRKHGSpTKYKAEVKAFG------------------IFGARRYTFIGETIYALGY 132
Cdd:COG0265   4 SGVIISPDgYILTNNHVVEGADEITVTLADG-REYPAKVVGRDpltdlavlkidakdlpaaPLGDSDKLRVGDWVLAIGN 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 22327839 133 PRDGDIiSVTKGIVTRVE-PQKYAHSSIEILTIQTDACINGGKSGGPVV 180
Cdd:COG0265  83 PFGLGQ-TVTAGIVSALGrSIGSSGGGTYDDFIQTDAAINPGNSGGPLV 130
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 31-190 2.99e-06

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: 46.72  E-value: 2.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327839   31 ATPRALRDidlAQDSVVKI----FSFSREPnvvqpwqttekeySSSGFAISGRRILTNAHVVGDHSYLQVRKHGSPTkYK 106
Cdd:NF033740 185 ATSPAVRR---ARPSVVKVrgtaPSCGRAL-------------EGSGFVVAPDRVMTNAHVVAGTDEVTVETVGGGT-LD 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327839  107 AEVKAF------------------GIFG---ARRytfiGETIYALGYPRDG----------DIISVT------KGIVTRv 149
Cdd:NF033740 248 ARVVYYdpdrdiavlavpglglppLPFAdepAET----GDDAIVLGYPEGGpftatparvrERIALSgpdiygSGTVTR- 322

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 22327839  150 epqkyahssiEILTIQTDacINGGKSGGPVV-MGNKVAGVVF 190
Cdd:NF033740 323 ----------EVYTLRGT--VRPGNSGGPLLdPDGRVLGVVF 352
Trypsin pfam00089
Trypsin;
60-190 1.69e-05

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 43.97  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327839    60 QPWQ----TTEKEYSSSGFAISGRRILTNAHVVGDHSYLQVR------KHGSPTKYKAEVKafGIFGARRYTF------- 122
Cdd:pfam00089  12 FPWQvslqLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVlgahniVLREGGEQKFDVE--KIIVHPNYNPdtldndi 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327839   123 ----------------------------IGETIYALGYPR---DGDIISVTKGIVTRVEPQKYAHSSIEILT---IQTDA 168
Cdd:pfam00089  90 allklespvtlgdtvrpiclpdassdlpVGTTCTVSGWGNtktLGPSDTLQEVTVPVVSRETCRSAYGGTVTdtmICAGA 169

                         170       180
                  ....*....|....*....|....*.
gi 22327839   169 C---INGGKSGGPVV-MGNKVAGVVF 190
Cdd:pfam00089 170 GgkdACQGDSGGPLVcSDGELIGIVS 195
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 50-180 5.59e-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: 42.98  E-value: 5.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327839    50 FSFSREPNvvQPWQTTEKEYSS--SGFAIS-GRRILTNAHVVGDHSYLQVRKHgSPTKYKAE--------------VKAF 112
Cdd:TIGR02037  39 FFGDDMPD--FPRQQREQKVRGlgSGVIISaDGYVLTNNHVVDGADEITVTLS-DGREFKAKlvgkdprtdiavlkIDAK 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327839   113 GI-----FGARRYTFIGETIYALGYPRdGDIISVTKGIVTRVepqkyAHSSIEILT----IQTDACINGGKSGGPVV 180
Cdd:TIGR02037 116 KNlpvikLGDSDKLRVGDWVLAIGNPF-GLGQTVTSGIVSAL-----GRSGLGIGDyenfIQTDAAINPGNSGGPLV 186
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH