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Conserved domains on  [gi|446181314|ref|WP_000259169|]
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MULTISPECIES: deubiquitinase ElaD [Escherichia]

Protein Classification

deubiquitinase( domain architecture ID 10013887)

deubiquitinase is a C79 family peptidase, such as Escherichia coli protease ElaD that can act as an efficient and specific deubiquitinating enzyme in vitro; contains active site dyad Cys-His

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11836 PRK11836
deubiquitinase; Provisional
1-402 0e+00

deubiquitinase; Provisional


:

Pssm-ID: 183334  Cd Length: 403  Bit Score: 811.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181314   1 MVTVVSNYCQLSQTQLSQTFAEKFTVTDELLQSLKKTALSGDEESIELLHNIALGYDEFGKKAEDILYHIVRNPTNETLS 80
Cdd:PRK11836   2 MVTVVSNYCQLSQTQLSQTFAEKFTVTEELLQSLKKTALSGDEESIELLHNIALGYDKFGKEAEDILYHIVRNPTNETLS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181314  81 IIRLIKNACLKLYNLAHTATKHPLKSHDSDDLLFKKLFSPSKLMTIIGEDIPLISEKQSLSKVLLNDKNNELSDGTNFWD 160
Cdd:PRK11836  82 IIRLIKNACLKLYNLAHTATNSPLKSHDSDNLLFKKLFSPSKLMTIIGDEIPLISEKQSLSKVLLNDENNELSDGTNFWD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181314 161 KNRQLTTDEIACYLKKIAANAKNTQVNYPTDFYLPNSNSTYLEVALNDNIKSDPLWPKAVQLFPINTGGHWILVSLQKIV 240
Cdd:PRK11836 162 KNRQLTTDEIACYLQKIAANAKNTQVNYPTGLYVPYSTRTHLEDALNENIKSDPSWPKEVQLFPINTGGHWILVSLQKIV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181314 241 NEKNNTQQIKCIIFNSLRALGHEKENSLKRIINSFNSELMGEMSNNNIKVHLTEPEIIFLHADLQQYLSQSCGAFVCMAA 320
Cdd:PRK11836 242 NEKNNTQQIKCVIFNSLRALGHDKENSLKRVINSFNSELMGEMSNNNIKVHLTEPEIIFLHADLQQYLSQSCGAFVCMAA 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181314 321 QEVIEQRESNSDSAPYTLLKNYADRFKKYSAEEQYEIDFQHRQANRNCYLDKYGDANINDYYRDLEIKHSQPQNRASGKR 400
Cdd:PRK11836 322 QEVIEQRESNSDSAPYTLLKNYADRFKKYSAEEQYEIDFQHRLVNRNCYLDKYGDANINHYYRNLEIKHSQPKNRASGKR 401

                 ..
gi 446181314 401 VS 402
Cdd:PRK11836 402 VS 403
 
Name Accession Description Interval E-value
PRK11836 PRK11836
deubiquitinase; Provisional
1-402 0e+00

deubiquitinase; Provisional


Pssm-ID: 183334  Cd Length: 403  Bit Score: 811.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181314   1 MVTVVSNYCQLSQTQLSQTFAEKFTVTDELLQSLKKTALSGDEESIELLHNIALGYDEFGKKAEDILYHIVRNPTNETLS 80
Cdd:PRK11836   2 MVTVVSNYCQLSQTQLSQTFAEKFTVTEELLQSLKKTALSGDEESIELLHNIALGYDKFGKEAEDILYHIVRNPTNETLS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181314  81 IIRLIKNACLKLYNLAHTATKHPLKSHDSDDLLFKKLFSPSKLMTIIGEDIPLISEKQSLSKVLLNDKNNELSDGTNFWD 160
Cdd:PRK11836  82 IIRLIKNACLKLYNLAHTATNSPLKSHDSDNLLFKKLFSPSKLMTIIGDEIPLISEKQSLSKVLLNDENNELSDGTNFWD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181314 161 KNRQLTTDEIACYLKKIAANAKNTQVNYPTDFYLPNSNSTYLEVALNDNIKSDPLWPKAVQLFPINTGGHWILVSLQKIV 240
Cdd:PRK11836 162 KNRQLTTDEIACYLQKIAANAKNTQVNYPTGLYVPYSTRTHLEDALNENIKSDPSWPKEVQLFPINTGGHWILVSLQKIV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181314 241 NEKNNTQQIKCIIFNSLRALGHEKENSLKRIINSFNSELMGEMSNNNIKVHLTEPEIIFLHADLQQYLSQSCGAFVCMAA 320
Cdd:PRK11836 242 NEKNNTQQIKCVIFNSLRALGHDKENSLKRVINSFNSELMGEMSNNNIKVHLTEPEIIFLHADLQQYLSQSCGAFVCMAA 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181314 321 QEVIEQRESNSDSAPYTLLKNYADRFKKYSAEEQYEIDFQHRQANRNCYLDKYGDANINDYYRDLEIKHSQPQNRASGKR 400
Cdd:PRK11836 322 QEVIEQRESNSDSAPYTLLKNYADRFKKYSAEEQYEIDFQHRLVNRNCYLDKYGDANINHYYRNLEIKHSQPKNRASGKR 401

                 ..
gi 446181314 401 VS 402
Cdd:PRK11836 402 VS 403
Peptidase_C48 pfam02902
Ulp1 protease family, C-terminal catalytic domain; This domain contains the catalytic triad ...
163-361 1.03e-26

Ulp1 protease family, C-terminal catalytic domain; This domain contains the catalytic triad Cys-His-Asn.


Pssm-ID: 397169  Cd Length: 202  Bit Score: 105.62  E-value: 1.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181314  163 RQLTTDEIACYLKKIA-----ANAKNTQVNYPTDFYLPN--SNSTYLE---------VALNDNIKSDPLWPKAVQLFPIN 226
Cdd:pfam02902   1 EWLNDTVIDFYLKLLAhrlesEDYKNERVHFLNSFFYSKltSKVSFKWgkkkdfyngVRRWTRKNKKWLFDVDIIYIPIN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181314  227 TGG-HWILVslqkIVNEKNNTqqikCIIFNSLRalGHEKENSLKRIINSFNSELMGEMSNNNIK-VHLTEPEIIFLHADL 304
Cdd:pfam02902  81 WDGkHWVLL----IINLPKKT----ITILDSLI--SLHTDKEYIRPINAMLPYLMSEALKKEQDdPDLTPFEIKRLTKVP 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446181314  305 QQYLSQSCGAFVCMAAQEVIEQRESNSDSapytllKNYADRFKKYSAEEQYEIDFQH 361
Cdd:pfam02902 151 QQPNSGDCGPYVLKFIELLAEGVPFEFLT------EKDVDRFRKKLAVDIYEILLSR 201
 
Name Accession Description Interval E-value
PRK11836 PRK11836
deubiquitinase; Provisional
1-402 0e+00

deubiquitinase; Provisional


Pssm-ID: 183334  Cd Length: 403  Bit Score: 811.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181314   1 MVTVVSNYCQLSQTQLSQTFAEKFTVTDELLQSLKKTALSGDEESIELLHNIALGYDEFGKKAEDILYHIVRNPTNETLS 80
Cdd:PRK11836   2 MVTVVSNYCQLSQTQLSQTFAEKFTVTEELLQSLKKTALSGDEESIELLHNIALGYDKFGKEAEDILYHIVRNPTNETLS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181314  81 IIRLIKNACLKLYNLAHTATKHPLKSHDSDDLLFKKLFSPSKLMTIIGEDIPLISEKQSLSKVLLNDKNNELSDGTNFWD 160
Cdd:PRK11836  82 IIRLIKNACLKLYNLAHTATNSPLKSHDSDNLLFKKLFSPSKLMTIIGDEIPLISEKQSLSKVLLNDENNELSDGTNFWD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181314 161 KNRQLTTDEIACYLKKIAANAKNTQVNYPTDFYLPNSNSTYLEVALNDNIKSDPLWPKAVQLFPINTGGHWILVSLQKIV 240
Cdd:PRK11836 162 KNRQLTTDEIACYLQKIAANAKNTQVNYPTGLYVPYSTRTHLEDALNENIKSDPSWPKEVQLFPINTGGHWILVSLQKIV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181314 241 NEKNNTQQIKCIIFNSLRALGHEKENSLKRIINSFNSELMGEMSNNNIKVHLTEPEIIFLHADLQQYLSQSCGAFVCMAA 320
Cdd:PRK11836 242 NEKNNTQQIKCVIFNSLRALGHDKENSLKRVINSFNSELMGEMSNNNIKVHLTEPEIIFLHADLQQYLSQSCGAFVCMAA 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181314 321 QEVIEQRESNSDSAPYTLLKNYADRFKKYSAEEQYEIDFQHRQANRNCYLDKYGDANINDYYRDLEIKHSQPQNRASGKR 400
Cdd:PRK11836 322 QEVIEQRESNSDSAPYTLLKNYADRFKKYSAEEQYEIDFQHRLVNRNCYLDKYGDANINHYYRNLEIKHSQPKNRASGKR 401

                 ..
gi 446181314 401 VS 402
Cdd:PRK11836 402 VS 403
PRK14848 PRK14848
type III secretion system effector deubiquitinase SseL;
26-363 7.73e-33

type III secretion system effector deubiquitinase SseL;


Pssm-ID: 184850  Cd Length: 317  Bit Score: 125.53  E-value: 7.73e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181314  26 VTDELLQSLKKTALSGDEESIELLHNIALGYDEFGKKAEDILYHIVRNPTNETLSIIRLIKNACLKLYNLAHTATKhplk 105
Cdd:PRK14848   1 VSDEALALLIGEVENGNQNCIDLLCNLALRNDDLGHKVEKLLFDLFSGKRSGSPDIDKKINQACLVLHQIANNDIT---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181314 106 shdSDDLLFKKLFSPSKLMTIIGEDIPLISEKQSLSKVLLNDK----NNELSDGTNFWDKNRQLTTDEIACYLKKIAANA 181
Cdd:PRK14848  77 ---KNNTEWKKLHAPSRLLYMAGSATTDLSKKIGIAHKIMGDQfaqtDQEQVGVENLWCGARMLSSDELAAATQGLVQES 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181314 182 KNTQVNYPTDFYLPNSNSTYLEVALNDNIKSDPLWPKavQLFPINTGGHWILVSLQKIvneknnTQQIKCIIFNSLRALg 261
Cdd:PRK14848 154 PLLSVNYPIGLIHPTTKENILSTQLLEKIAQSGLSHN--EVFLINTGDHWLLCLFYKL------AEKIKCLIFNTYYDL- 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181314 262 heKENSLKRIINSFNSELMGEmsnnnikvhltEPEIIFLHADLQQYLSQSCGAFvCMAAQEVIEQRESNSdsaPYTLLKN 341
Cdd:PRK14848 225 --NENTKQEIIEAAKIAGISE-----------NEDVNFIETNLQNNVPNGCGLF-CYHTIQLLSNAGQND---PATTLRE 287
                        330       340
                 ....*....|....*....|..
gi 446181314 342 YADRFKKYSAEEQYEIDFQHRQ 363
Cdd:PRK14848 288 FAENFLTLSVEEQTLFNTQTRR 309
Peptidase_C48 pfam02902
Ulp1 protease family, C-terminal catalytic domain; This domain contains the catalytic triad ...
163-361 1.03e-26

Ulp1 protease family, C-terminal catalytic domain; This domain contains the catalytic triad Cys-His-Asn.


Pssm-ID: 397169  Cd Length: 202  Bit Score: 105.62  E-value: 1.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181314  163 RQLTTDEIACYLKKIA-----ANAKNTQVNYPTDFYLPN--SNSTYLE---------VALNDNIKSDPLWPKAVQLFPIN 226
Cdd:pfam02902   1 EWLNDTVIDFYLKLLAhrlesEDYKNERVHFLNSFFYSKltSKVSFKWgkkkdfyngVRRWTRKNKKWLFDVDIIYIPIN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181314  227 TGG-HWILVslqkIVNEKNNTqqikCIIFNSLRalGHEKENSLKRIINSFNSELMGEMSNNNIK-VHLTEPEIIFLHADL 304
Cdd:pfam02902  81 WDGkHWVLL----IINLPKKT----ITILDSLI--SLHTDKEYIRPINAMLPYLMSEALKKEQDdPDLTPFEIKRLTKVP 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446181314  305 QQYLSQSCGAFVCMAAQEVIEQRESNSDSapytllKNYADRFKKYSAEEQYEIDFQH 361
Cdd:pfam02902 151 QQPNSGDCGPYVLKFIELLAEGVPFEFLT------EKDVDRFRKKLAVDIYEILLSR 201
 
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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