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Conserved domains on  [gi|394255894|gb|EJE00832|]
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glutamyl endopeptidase [Staphylococcus epidermidis NIHLM040]

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, ...
87-276 9.98e-35

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


:

Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 124.02  E-value: 9.98e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394255894  87 AVSFIYIPTEGGYmsASGVVVGENEILTNKHVVNGAKGN--PRNISVHPsakNENDYPNGKFVGQEIIPYPG-------N 157
Cdd:COG3591    1 AVGRLETDGGGGV--CTGTLIGPNLVLTAGHCVYDGAGGgwATNIVFVP---GYNGGPYGTATATRFRVPPGwvasgdaG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394255894 158 SDLAILRVspnerNQHIGQVVKPATISSNTDTRINENITVTGYPGDKPLATMWESVGKVVYIGGEELRYDLSTVGGNSGS 237
Cdd:COG3591   76 YDYALLRL-----DEPLGDTTGWLGLAFNDAPLAGEPVTIIGYPGDRPKDLSLDCSGRVTGVQGNRLSYDCDTTGGSSGS 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 394255894 238 PVFN---GKNQVIGIHYGGVNNKYNSSVYINDFVQQFLRNNI 276
Cdd:COG3591  151 PVLDdsdGGGRVVGVHSAGGADRANTGVRLTSAIVAALRAWA 192
 
Name Accession Description Interval E-value
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
87-276 9.98e-35

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 124.02  E-value: 9.98e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394255894  87 AVSFIYIPTEGGYmsASGVVVGENEILTNKHVVNGAKGN--PRNISVHPsakNENDYPNGKFVGQEIIPYPG-------N 157
Cdd:COG3591    1 AVGRLETDGGGGV--CTGTLIGPNLVLTAGHCVYDGAGGgwATNIVFVP---GYNGGPYGTATATRFRVPPGwvasgdaG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394255894 158 SDLAILRVspnerNQHIGQVVKPATISSNTDTRINENITVTGYPGDKPLATMWESVGKVVYIGGEELRYDLSTVGGNSGS 237
Cdd:COG3591   76 YDYALLRL-----DEPLGDTTGWLGLAFNDAPLAGEPVTIIGYPGDRPKDLSLDCSGRVTGVQGNRLSYDCDTTGGSSGS 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 394255894 238 PVFN---GKNQVIGIHYGGVNNKYNSSVYINDFVQQFLRNNI 276
Cdd:COG3591  151 PVLDdsdGGGRVVGVHSAGGADRANTGVRLTSAIVAALRAWA 192
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
102-249 6.38e-22

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 89.02  E-value: 6.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394255894  102 ASGVVVGEN-EILTNKHVVNGAKGNPRNisvhpsaKNENDYPNGKFVGQEIIPYPGNSDLAILRVSPNERNqhigqvVKP 180
Cdd:pfam13365   1 GTGFVVSSDgLVLTNAHVVDDAEEAAVE-------LVSVVLADGREYPATVVARDPDLDLALLRVSGDGRG------LPP 67
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 394255894  181 ATISSNTDTRINENITVTGYPGDKPLATM------WESVGKVVYIGGEELRYDLSTVGGNSGSPVFNGKNQVIGI 249
Cdd:pfam13365  68 LPLGDSEPLVGGERVYAVGYPLGGEKLSLsegivsGVDEGRDGGDDGRVIQTDAALSPGSSGGPVFDADGRVVGI 142
 
Name Accession Description Interval E-value
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
87-276 9.98e-35

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 124.02  E-value: 9.98e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394255894  87 AVSFIYIPTEGGYmsASGVVVGENEILTNKHVVNGAKGN--PRNISVHPsakNENDYPNGKFVGQEIIPYPG-------N 157
Cdd:COG3591    1 AVGRLETDGGGGV--CTGTLIGPNLVLTAGHCVYDGAGGgwATNIVFVP---GYNGGPYGTATATRFRVPPGwvasgdaG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394255894 158 SDLAILRVspnerNQHIGQVVKPATISSNTDTRINENITVTGYPGDKPLATMWESVGKVVYIGGEELRYDLSTVGGNSGS 237
Cdd:COG3591   76 YDYALLRL-----DEPLGDTTGWLGLAFNDAPLAGEPVTIIGYPGDRPKDLSLDCSGRVTGVQGNRLSYDCDTTGGSSGS 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 394255894 238 PVFN---GKNQVIGIHYGGVNNKYNSSVYINDFVQQFLRNNI 276
Cdd:COG3591  151 PVLDdsdGGGRVVGVHSAGGADRANTGVRLTSAIVAALRAWA 192
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
102-249 6.38e-22

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 89.02  E-value: 6.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394255894  102 ASGVVVGEN-EILTNKHVVNGAKGNPRNisvhpsaKNENDYPNGKFVGQEIIPYPGNSDLAILRVSPNERNqhigqvVKP 180
Cdd:pfam13365   1 GTGFVVSSDgLVLTNAHVVDDAEEAAVE-------LVSVVLADGREYPATVVARDPDLDLALLRVSGDGRG------LPP 67
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 394255894  181 ATISSNTDTRINENITVTGYPGDKPLATM------WESVGKVVYIGGEELRYDLSTVGGNSGSPVFNGKNQVIGI 249
Cdd:pfam13365  68 LPLGDSEPLVGGERVYAVGYPLGGEKLSLsegivsGVDEGRDGGDDGRVIQTDAALSPGSSGGPVFDADGRVVGI 142
Trypsin pfam00089
Trypsin;
96-272 1.38e-07

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 50.90  E-value: 1.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394255894   96 EGGYMSASGVVVGENEILTNKHVVNGAKGNPRNISVHPSAKNENDYPNGKfvGQEIIPYPG------NSDLAILRVSPNE 169
Cdd:pfam00089  21 SSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFD--VEKIIVHPNynpdtlDNDIALLKLESPV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394255894  170 RnqhIGQVVKPATI-SSNTDTRINENITVTGYP---GDKPLATMWESVGKVV-------YIGGEELR-------YDLSTV 231
Cdd:pfam00089  99 T---LGDTVRPICLpDASSDLPVGTTCTVSGWGntkTLGPSDTLQEVTVPVVsretcrsAYGGTVTDtmicagaGGKDAC 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 394255894  232 GGNSGSPVFNGKNQVIGIHYGGVN----NKYnsSVYINdfVQQFL 272
Cdd:pfam00089 176 QGDSGGPLVCSDGELIGIVSWGYGcasgNYP--GVYTP--VSSYL 216
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
101-249 5.79e-07

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: 49.76  E-value: 5.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394255894 101 SASGVVVGEN-EILTNKHVVNGAkgnpRNISVHpsaknendYPNGKFVGQEIIPYPGNSDLAILRVSPNErnqhigqvVK 179
Cdd:COG0265    2 LGSGVIISPDgYILTNNHVVEGA----DEITVT--------LADGREYPAKVVGRDPLTDLAVLKIDAKD--------LP 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394255894 180 PATISSNTDTRINENITVTGYPGDkpLATmweSV--------GKVVYIGGEELRYDL-----STVGGNSGSPVFNGKNQV 246
Cdd:COG0265   62 AAPLGDSDKLRVGDWVLAIGNPFG--LGQ---TVtagivsalGRSIGSSGGGTYDDFiqtdaAINPGNSGGPLVNLNGEV 136

                 ...
gi 394255894 247 IGI 249
Cdd:COG0265  137 IGI 139
Peptidase_S46 pfam10459
Peptidase S46; Dipeptidyl-peptidase 7 (DPP-7) is the best characterized member of this family. ...
228-254 1.07e-04

Peptidase S46; Dipeptidyl-peptidase 7 (DPP-7) is the best characterized member of this family. It is a serine peptidase that is located on the cell surface and is predicted to have two N-terminal transmembrane domains.


Pssm-ID: 431297  Cd Length: 695  Bit Score: 43.40  E-value: 1.07e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 394255894  228 LSTV---GGNSGSPVFNGKNQVIGIHYGGV 254
Cdd:pfam10459 623 LSTNditGGNSGSPVLNGKGELVGLAFDGN 652
 
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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