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Conserved domains on  [gi|1512630185|gb|RNN97024|]
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serine protease [Raoultella planticola]

Protein Classification

trypsin-like serine peptidase( domain architecture ID 10007588)

trypsin-like serine protease catalyzes the cleavage of specific peptide bonds in protein substrates using an active site serine as the nucleophile

CATH:  2.40.10.10
EC:  3.4.21.-
PubMed:  7845208|7733651
SCOP:  3000114

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
54-270 2.57e-44

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


:

Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 148.29  E-value: 2.57e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512630185  54 AIGQLET-ASGNLCTATLISPNLALTAGHCLLTPPKGKPDKPVALRFISRKGGWVYEiHGIEGRVDPslgkrlkadgdGW 132
Cdd:COG3591     1 AVGRLETdGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPGYNGGPYGTA-TATRFRVPP-----------GW 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512630185 133 iVPSAAAPWDFGLIVLRYAPGGIT-PIPLFSGDKAAltaalkvSERKVTQSGYPEDHLDNLYSHQDCIVTGWaQTTVLSH 211
Cdd:COG3591    69 -VASGDAGYDYALLRLDEPLGDTTgWLGLAFNDAPL-------AGEPVTIIGYPGDRPKDLSLDCSGRVTGV-QGNRLSY 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512630185 212 QCDTLPGDSGSPLLLKTDTGWQVIAVQSSAPGAKdrwraDNRAISVT-GFRDKLEALASE 270
Cdd:COG3591   140 DCDTTGGSSGSPVLDDSDGGGRVVGVHSAGGADR-----ANTGVRLTsAIVAALRAWASA 194
 
Name Accession Description Interval E-value
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
54-270 2.57e-44

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 148.29  E-value: 2.57e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512630185  54 AIGQLET-ASGNLCTATLISPNLALTAGHCLLTPPKGKPDKPVALRFISRKGGWVYEiHGIEGRVDPslgkrlkadgdGW 132
Cdd:COG3591     1 AVGRLETdGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPGYNGGPYGTA-TATRFRVPP-----------GW 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512630185 133 iVPSAAAPWDFGLIVLRYAPGGIT-PIPLFSGDKAAltaalkvSERKVTQSGYPEDHLDNLYSHQDCIVTGWaQTTVLSH 211
Cdd:COG3591    69 -VASGDAGYDYALLRLDEPLGDTTgWLGLAFNDAPL-------AGEPVTIIGYPGDRPKDLSLDCSGRVTGV-QGNRLSY 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512630185 212 QCDTLPGDSGSPLLLKTDTGWQVIAVQSSAPGAKdrwraDNRAISVT-GFRDKLEALASE 270
Cdd:COG3591   140 DCDTTGGSSGSPVLDDSDGGGRVVGVHSAGGADR-----ANTGVRLTsAIVAALRAWASA 194
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
66-237 4.17e-06

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 45.49  E-value: 4.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512630185  66 CTATLISPN-LALTAGHCLltppKGKPDKPVALRFISRKGGWVYEihgiegrvdpslGKRLKADGDgwivpsaaapWDFG 144
Cdd:pfam13365   1 GTGFVVSSDgLVLTNAHVV----DDAEEAAVELVSVVLADGREYP------------ATVVARDPD----------LDLA 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512630185 145 LIVLRYAPGGITPIPLFSGDKAALTAALKV------SERKVTQSGYpedhldnlYSHQDCIVTGWAQTTVLSHQCDTLPG 218
Cdd:pfam13365  55 LLRVSGDGRGLPPLPLGDSEPLVGGERVYAvgyplgGEKLSLSEGI--------VSGVDEGRDGGDDGRVIQTDAALSPG 126
                         170
                  ....*....|....*....
gi 1512630185 219 DSGSPLLlktDTGWQVIAV 237
Cdd:pfam13365 127 SSGGPVF---DADGRVVGI 142
 
Name Accession Description Interval E-value
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
54-270 2.57e-44

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 148.29  E-value: 2.57e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512630185  54 AIGQLET-ASGNLCTATLISPNLALTAGHCLLTPPKGKPDKPVALRFISRKGGWVYEiHGIEGRVDPslgkrlkadgdGW 132
Cdd:COG3591     1 AVGRLETdGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPGYNGGPYGTA-TATRFRVPP-----------GW 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512630185 133 iVPSAAAPWDFGLIVLRYAPGGIT-PIPLFSGDKAAltaalkvSERKVTQSGYPEDHLDNLYSHQDCIVTGWaQTTVLSH 211
Cdd:COG3591    69 -VASGDAGYDYALLRLDEPLGDTTgWLGLAFNDAPL-------AGEPVTIIGYPGDRPKDLSLDCSGRVTGV-QGNRLSY 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512630185 212 QCDTLPGDSGSPLLLKTDTGWQVIAVQSSAPGAKdrwraDNRAISVT-GFRDKLEALASE 270
Cdd:COG3591   140 DCDTTGGSSGSPVLDDSDGGGRVVGVHSAGGADR-----ANTGVRLTsAIVAALRAWASA 194
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
48-244 3.91e-08

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 53.11  E-value: 3.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512630185  48 AEEPWDAIGQLETASG---NLCTATLISPNLALTAGHCLLTPPKGKpdkpVALRFisrkggwvyeihgieGRVDPSLGKR 124
Cdd:COG5640    38 TVGEYPWMVALQSSNGpsgQFCGGTLIAPRWVLTAAHCVDGDGPSD----LRVVI---------------GSTDLSTSGG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512630185 125 LKADGDGWIVP----SAAAPWDFGLIVLRYAPGGITPIPLF-SGDKAALTAALKVS---ERKVTQSGYPED--HLD-NLY 193
Cdd:COG5640    99 TVVKVARIVVHpdydPATPGNDIALLKLATPVPGVAPAPLAtSADAAAPGTPATVAgwgRTSEGPGSQSGTlrKADvPVV 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1512630185 194 SHQDC-----------IVTGWAQTTVlshqcDTLPGDSGSPLLLKTDTGWQVIAVQSSAPGA 244
Cdd:COG5640   179 SDATCaayggfdggtmLCAGYPEGGK-----DACQGDSGGPLVVKDGGGWVLVGVVSWGGGP 235
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
66-237 4.17e-06

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 45.49  E-value: 4.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512630185  66 CTATLISPN-LALTAGHCLltppKGKPDKPVALRFISRKGGWVYEihgiegrvdpslGKRLKADGDgwivpsaaapWDFG 144
Cdd:pfam13365   1 GTGFVVSSDgLVLTNAHVV----DDAEEAAVELVSVVLADGREYP------------ATVVARDPD----------LDLA 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512630185 145 LIVLRYAPGGITPIPLFSGDKAALTAALKV------SERKVTQSGYpedhldnlYSHQDCIVTGWAQTTVLSHQCDTLPG 218
Cdd:pfam13365  55 LLRVSGDGRGLPPLPLGDSEPLVGGERVYAvgyplgGEKLSLSEGI--------VSGVDEGRDGGDDGRVIQTDAALSPG 126
                         170
                  ....*....|....*....
gi 1512630185 219 DSGSPLLlktDTGWQVIAV 237
Cdd:pfam13365 127 SSGGPVF---DADGRVVGI 142
Trypsin pfam00089
Trypsin;
46-225 1.48e-04

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 42.04  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512630185  46 NPAEEPWDAIGQLETaSGNLCTATLISPNLALTAGHCLltppKGKPDKPVAL--RFISRKGGWVYEIHGIEGRVDPSLGK 123
Cdd:pfam00089   8 QPGSFPWQVSLQLSS-GKHFCGGSLISENWVLTAAHCV----SGASDVKVVLgaHNIVLREGGEQKFDVEKIIVHPNYNP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512630185 124 RlKADGDGWIVpSAAAPWDFGLivlryapgGITPIPLfsgdkAALTAALKVsERKVTQSGYPEDHLDN-----------L 192
Cdd:pfam00089  83 D-TLDNDIALL-KLESPVTLGD--------TVRPICL-----PDASSDLPV-GTTCTVSGWGNTKTLGpsdtlqevtvpV 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1512630185 193 YSHQDCivTGWAQTTVLSHQ-C------DTLPGDSGSPLL 225
Cdd:pfam00089 147 VSRETC--RSAYGGTVTDTMiCagaggkDACQGDSGGPLV 184
 
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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