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Conserved domains on  [gi|528471247|ref|XP_005163524|]
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OTU deubiquitinase with linear linkage specificity b isoform X1 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
OTU_OTUL cd22799
OTU (ovarian tumor) domain of ubiquitin thioesterase otulin and similar proteins; Otulin, also ...
120-381 1.36e-171

OTU (ovarian tumor) domain of ubiquitin thioesterase otulin and similar proteins; Otulin, also called FAM105B, deubiquitinating enzyme otulin, OTU domain-containing deubiquitinase with linear linkage specificity, or ubiquitin thioesterase Gumby, is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that specifically removes linear ('Met-1'-linked) polyubiquitin chains to substrates and acts as a regulator of angiogenesis and innate immune response. It acts as a key negative regulator of inflammation by restricting spontaneous inflammation and maintaining immune homeostasis. Otulin belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in some cases an aspartate, as the catalytic dyad (or triad).


:

Pssm-ID: 438620  Cd Length: 266  Bit Score: 480.02  E-value: 1.36e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247 120 SSVSAAEDLQTYSEKEWRGNTTKSQLIRKGYEAIASEF-RLCRVRGDNYCALRATLFQVLSQSKKLPAWLQDSDIVKWPK 198
Cdd:cd22799    1 LSVAPEMDILDYCKKEWRGNTQKATCMKKGYEEVSQKFtSIRRVRGDNYCALRATLFQALSQAVGLPPWLQDPELMLLPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247 199 ELHSDENFLKEWQFPLE---SKKNNVQHLEQCLDLLKKKWQEAVQCKSLAERERMSQQVFRGLNEEYELLEALKFLMLRT 275
Cdd:cd22799   81 KLISKYNWIKQWKLGLKfdgKNEDLVDKLKEYLTLLKKKWAGLAEMRTAEERQIACDELFTNEAEEYSLYEAVKFLMLNR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247 276 AAQLHLNMEKGSDVPEFCWLLFARDSSKCPKTFLTNHLRHVGFSGGLEQVEMCLLGHSLQQTIKVFRLYKCDTEEFITYY 355
Cdd:cd22799  161 AIELYNDKEKGKEVPFFSWLLFARDTSNNPGQLLRNHLNQVGHSGGLEQVEMFLLGYALQHTIQVYRLYKYNTEEFITVY 240
                        250       260
                 ....*....|....*....|....*.
gi 528471247 356 PNDHKNDWPHLVLLTEDDRHYNALIP 381
Cdd:cd22799  241 PTDPPKDWPVVTLITEDDRHYNIPVR 266
 
Name Accession Description Interval E-value
OTU_OTUL cd22799
OTU (ovarian tumor) domain of ubiquitin thioesterase otulin and similar proteins; Otulin, also ...
120-381 1.36e-171

OTU (ovarian tumor) domain of ubiquitin thioesterase otulin and similar proteins; Otulin, also called FAM105B, deubiquitinating enzyme otulin, OTU domain-containing deubiquitinase with linear linkage specificity, or ubiquitin thioesterase Gumby, is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that specifically removes linear ('Met-1'-linked) polyubiquitin chains to substrates and acts as a regulator of angiogenesis and innate immune response. It acts as a key negative regulator of inflammation by restricting spontaneous inflammation and maintaining immune homeostasis. Otulin belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in some cases an aspartate, as the catalytic dyad (or triad).


Pssm-ID: 438620  Cd Length: 266  Bit Score: 480.02  E-value: 1.36e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247 120 SSVSAAEDLQTYSEKEWRGNTTKSQLIRKGYEAIASEF-RLCRVRGDNYCALRATLFQVLSQSKKLPAWLQDSDIVKWPK 198
Cdd:cd22799    1 LSVAPEMDILDYCKKEWRGNTQKATCMKKGYEEVSQKFtSIRRVRGDNYCALRATLFQALSQAVGLPPWLQDPELMLLPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247 199 ELHSDENFLKEWQFPLE---SKKNNVQHLEQCLDLLKKKWQEAVQCKSLAERERMSQQVFRGLNEEYELLEALKFLMLRT 275
Cdd:cd22799   81 KLISKYNWIKQWKLGLKfdgKNEDLVDKLKEYLTLLKKKWAGLAEMRTAEERQIACDELFTNEAEEYSLYEAVKFLMLNR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247 276 AAQLHLNMEKGSDVPEFCWLLFARDSSKCPKTFLTNHLRHVGFSGGLEQVEMCLLGHSLQQTIKVFRLYKCDTEEFITYY 355
Cdd:cd22799  161 AIELYNDKEKGKEVPFFSWLLFARDTSNNPGQLLRNHLNQVGHSGGLEQVEMFLLGYALQHTIQVYRLYKYNTEEFITVY 240
                        250       260
                 ....*....|....*....|....*.
gi 528471247 356 PNDHKNDWPHLVLLTEDDRHYNALIP 381
Cdd:cd22799  241 PTDPPKDWPVVTLITEDDRHYNIPVR 266
Peptidase_C101 pfam16218
Peptidase family C101; This is a family of cysteine-peptidases that is conserved in ...
121-380 9.95e-171

Peptidase family C101; This is a family of cysteine-peptidases that is conserved in vertebrates. The key residues as found in SwissProt:Q96BN8 are Asp126, Cys129, His339 and Asn341.


Pssm-ID: 465075  Cd Length: 265  Bit Score: 477.96  E-value: 9.95e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247  121 SVSAAEDLQTYSEKEWRGNTTKSQLIRKGYEAIASEFR-LCRVRGDNYCALRATLFQVLSQSKKLPAWLQDSDIVKWPKE 199
Cdd:pfam16218   2 SVAPEVDILDYSEREWRGNTAKAALMRKGYEEVSQKFSsLRRVRGDNYCALRATLFQILSQSTQLPSWLQDEDILMLPEK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247  200 LHSDENFLKEWQFPLE---SKKNNVQHLEQCLDLLKKKWQEAVQCKSLAERERMSQQVFRGLNEEYELLEALKFLMLRTA 276
Cdd:pfam16218  82 LQTKYNWIKQWTFPPEcpyGGKNAVEKLKECLELLKTKWQEAVECKTHEERQSACDELFSGEEEEYKLYEALKFLMLNTA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247  277 AQLHLNMEKGSDVPEFCWLLFARDSSKCPKTFLTNHLRHVGFSGGLEQVEMCLLGHSLQQTIKVFRLYKCDTEEFITYYP 356
Cdd:pfam16218 162 IELYEDMEKGKEVPVFCWLLFARDTSSDPESFLMNHLNQVGDSGGLEQVEMFLLGYALEVTIQVYRLYKYNTEEFITYYP 241
                         250       260
                  ....*....|....*....|....
gi 528471247  357 NDHKNDWPHLVLLTEDDRHYNALI 380
Cdd:pfam16218 242 DDHRDDWPVVTLITEDDRHYNVPV 265
 
Name Accession Description Interval E-value
OTU_OTUL cd22799
OTU (ovarian tumor) domain of ubiquitin thioesterase otulin and similar proteins; Otulin, also ...
120-381 1.36e-171

OTU (ovarian tumor) domain of ubiquitin thioesterase otulin and similar proteins; Otulin, also called FAM105B, deubiquitinating enzyme otulin, OTU domain-containing deubiquitinase with linear linkage specificity, or ubiquitin thioesterase Gumby, is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that specifically removes linear ('Met-1'-linked) polyubiquitin chains to substrates and acts as a regulator of angiogenesis and innate immune response. It acts as a key negative regulator of inflammation by restricting spontaneous inflammation and maintaining immune homeostasis. Otulin belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in some cases an aspartate, as the catalytic dyad (or triad).


Pssm-ID: 438620  Cd Length: 266  Bit Score: 480.02  E-value: 1.36e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247 120 SSVSAAEDLQTYSEKEWRGNTTKSQLIRKGYEAIASEF-RLCRVRGDNYCALRATLFQVLSQSKKLPAWLQDSDIVKWPK 198
Cdd:cd22799    1 LSVAPEMDILDYCKKEWRGNTQKATCMKKGYEEVSQKFtSIRRVRGDNYCALRATLFQALSQAVGLPPWLQDPELMLLPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247 199 ELHSDENFLKEWQFPLE---SKKNNVQHLEQCLDLLKKKWQEAVQCKSLAERERMSQQVFRGLNEEYELLEALKFLMLRT 275
Cdd:cd22799   81 KLISKYNWIKQWKLGLKfdgKNEDLVDKLKEYLTLLKKKWAGLAEMRTAEERQIACDELFTNEAEEYSLYEAVKFLMLNR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247 276 AAQLHLNMEKGSDVPEFCWLLFARDSSKCPKTFLTNHLRHVGFSGGLEQVEMCLLGHSLQQTIKVFRLYKCDTEEFITYY 355
Cdd:cd22799  161 AIELYNDKEKGKEVPFFSWLLFARDTSNNPGQLLRNHLNQVGHSGGLEQVEMFLLGYALQHTIQVYRLYKYNTEEFITVY 240
                        250       260
                 ....*....|....*....|....*.
gi 528471247 356 PNDHKNDWPHLVLLTEDDRHYNALIP 381
Cdd:cd22799  241 PTDPPKDWPVVTLITEDDRHYNIPVR 266
Peptidase_C101 pfam16218
Peptidase family C101; This is a family of cysteine-peptidases that is conserved in ...
121-380 9.95e-171

Peptidase family C101; This is a family of cysteine-peptidases that is conserved in vertebrates. The key residues as found in SwissProt:Q96BN8 are Asp126, Cys129, His339 and Asn341.


Pssm-ID: 465075  Cd Length: 265  Bit Score: 477.96  E-value: 9.95e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247  121 SVSAAEDLQTYSEKEWRGNTTKSQLIRKGYEAIASEFR-LCRVRGDNYCALRATLFQVLSQSKKLPAWLQDSDIVKWPKE 199
Cdd:pfam16218   2 SVAPEVDILDYSEREWRGNTAKAALMRKGYEEVSQKFSsLRRVRGDNYCALRATLFQILSQSTQLPSWLQDEDILMLPEK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247  200 LHSDENFLKEWQFPLE---SKKNNVQHLEQCLDLLKKKWQEAVQCKSLAERERMSQQVFRGLNEEYELLEALKFLMLRTA 276
Cdd:pfam16218  82 LQTKYNWIKQWTFPPEcpyGGKNAVEKLKECLELLKTKWQEAVECKTHEERQSACDELFSGEEEEYKLYEALKFLMLNTA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247  277 AQLHLNMEKGSDVPEFCWLLFARDSSKCPKTFLTNHLRHVGFSGGLEQVEMCLLGHSLQQTIKVFRLYKCDTEEFITYYP 356
Cdd:pfam16218 162 IELYEDMEKGKEVPVFCWLLFARDTSSDPESFLMNHLNQVGDSGGLEQVEMFLLGYALEVTIQVYRLYKYNTEEFITYYP 241
                         250       260
                  ....*....|....*....|....
gi 528471247  357 NDHKNDWPHLVLLTEDDRHYNALI 380
Cdd:pfam16218 242 DDHRDDWPVVTLITEDDRHYNVPV 265
OTU_OTUL-like cd22790
OTU (ovarian tumor) domain of ubiquitin thioesterase otulin family; Otulin family includes ...
131-380 3.45e-105

OTU (ovarian tumor) domain of ubiquitin thioesterase otulin family; Otulin family includes otulin and otulinl. Otulin, also called FAM105B, deubiquitinating enzyme otulin, OTU domain-containing deubiquitinase with linear linkage specificity, or ubiquitin thioesterase Gumby, is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that specifically removes linear ('Met-1'-linked) polyubiquitin chains to substrates and acts as a regulator of angiogenesis and innate immune response. It acts as a key negative regulator of inflammation by restricting spontaneous inflammation and maintaining immune homeostasis. Otulinl, also called FAM105A, is an OTU-class pseudo-deubiquitinase with a disrupted catalytic triad and undetectable cleavage activity for any diubiquitin linkage. It may play a role in endoplasmic reticulum (ER)-organelle communication. Otulin and otulinl belong to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in some cases an aspartate, as the catalytic dyad (or triad).


Pssm-ID: 438611  Cd Length: 258  Bit Score: 311.08  E-value: 3.45e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247 131 YSEKEWRGNTTKSQLIRKGYEAIASEF---RLCRVRGDNYCALRATLFQVLSQSKKLPAWlqDSDIVKWPKELHS--DEN 205
Cdd:cd22790    2 YAEREWKGETPKAKTIKKGYEEIPRLLgckYLRRIRGDNYCAIRAALFQVLSQGIPVPSK--WPALEQIPEKLLNsyGCS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247 206 FLKEWQFP--LESKKNNV-QHLEQCLDLLKKKWQEAVQCKSLAERERMSQQVF-RGLNEEYELLEALKFLMLRTAAQLHL 281
Cdd:cd22790   80 WLQQWSFAnrLPYTGEDVlSGLRECLLTLDSQVEELESMSTEEDREDALLSLLnSDPTLDLKLMEAVKLLMLVSAIELYN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247 282 NMEKGSDVPEFCWLLFARDSSKCPKTFLTNHLRHVGFSGGLEQVEMCLLGHSLQQTIKVFRLYKCDTEEFITYYPNDHKN 361
Cdd:cd22790  160 RMQKGEDVPLFAWLLFARDTSSTPKDFLKNHLNPVGDTAGLEQVEMFLLGYSLGVTIRVFRPSQFGQEDFICYYPDEEDD 239
                        250
                 ....*....|....*....
gi 528471247 362 DWPHLVLLTEDDRHYNALI 380
Cdd:cd22790  240 DWPEVTLIAEDDRHYNVPV 258
OTU_OTULL cd22798
OTU (ovarian tumor) domain of inactive ubiquitin thioesterase Otulinl; Otulinl, also called ...
127-381 1.70e-88

OTU (ovarian tumor) domain of inactive ubiquitin thioesterase Otulinl; Otulinl, also called FAM105A, is an OTU-class pseudo-deubiquitinase with a disrupted catalytic triad and undetectable cleavage activity for any diubiquitin linkage. It may play a role in endoplasmic reticulum (ER)-organelle communication. Otulinl belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in some cases an aspartate, as the catalytic dyad (or triad).


Pssm-ID: 438619  Cd Length: 261  Bit Score: 268.98  E-value: 1.70e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247 127 DLQTYSEKEWRGNTTKSQLIRKGYEAIASEFR---LCRVRGDNYCALRATLFQVLSQSKKLPAWLQDSDIVKWPKELHSD 203
Cdd:cd22798    1 DLLEYCAREWKGETPRAKQMRKAYEELFWRHHikyVRQVRGDNYCALRAVLFQIFSQGIPFPSWMKEQDILKLPEKLLYS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247 204 E--NFLKEWQFPLES--KKNNVQHLEQCLDLLKKKWQEAVQCKSLAERERMSQQVFRGLNEEYELLEALKFLMLRTAAQL 279
Cdd:cd22798   81 QgcNWIQQYSFGPEKytGPNVFGKLRKCVETLKTQWTEISGIKDYEKRGKMCNTLFSDEAKEYKLYEAIKFLMLYQVIEV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247 280 HLNMEKGSDVPEFCWLLFARDSSKCPKTFLTNHLRHVGFSGGLEQVEMCLLGHSLQQTIKVFRLYKCDTEEFITYYPNDH 359
Cdd:cd22798  161 YEQMKTGQDVPNFFSLLFSRDTSSDPLSFMMNHLNSIGDTGGLEQIEMFLLGYTLEVKIKVFRLYKFNTEEFEVCYPEEY 240
                        250       260
                 ....*....|....*....|..
gi 528471247 360 KNDWPHLVLLTEDDRHYNalIP 381
Cdd:cd22798  241 LRDWPEISLLTEDDRHYN--IP 260
Otubain_C65 cd22749
Otubain subfamily of ubiquitin thioesterases; The otubain subfamily is composed of otubain-1 ...
122-380 4.48e-06

Otubain subfamily of ubiquitin thioesterases; The otubain subfamily is composed of otubain-1 (also called ubiquitin thioesterase OTUB1 or OTU domain-containing ubiquitin aldehyde-binding protein 1), otubain-2 (also called ubiquitin thioesterase OTUB2 or OTU domain-containing ubiquitin aldehyde-binding protein 2), and similar proteins. They function as deubiquitylases (DUBs)/ubiquitin thioesterases (EC 3.4.19.12). OTUB1 can specifically remove 'Lys-48'-linked conjugated ubiquitin from protein substrates, while OTUB2 mediates the deubiquitination of 'Lys-11'-,'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, with a preference for 'Lys-63'-linked polyubiquitin chains. The otubain subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. Members of this subfamily are classified as family C65 cysteine proteases by MEROPS.


Pssm-ID: 438586 [Multi-domain]  Cd Length: 232  Bit Score: 47.33  E-value: 4.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247 122 VSAAEDLQTYsEKEWRGNTT---KSQLIRKGYeaiaSEFRlcRVRGDNYCALRATLFQVLSQskklpawLQDSDIVKWPK 198
Cdd:cd22749    2 VGEKEPLSAL-AEEYAGNPIflqKIKELKKKY----SGFR--RVRGDGNCFYRAFAFSYLEL-------LLKNQDPAELE 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247 199 ELHSdenFLKEWQFPLESKKNNVQHLEQCLDLLKKKWQEAVQCKSLAERErmsQQVFRGLNEEYELLEALKFLMLRTAAQ 278
Cdd:cd22749   68 RLLA---RLESLKNLLEALGFEELVFEDFYEEFLELLKKLRNSKERELTE---EELLELFNDEETSNYIVVFLRLLTSAY 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471247 279 LHLN-------MEKGSDVPEFCwllfardsskcpktfltnhLRHVGFSG-GLEQVEMCLLGHSLQQTIKVFRLYKCDTEE 350
Cdd:cd22749  142 LKTNaddyepfLFEGMSVEEFC-------------------EREVEPMGkEADHLQITALANALGVPVRVEYLDRSAGGE 202
                        250       260       270
                 ....*....|....*....|....*....|..
gi 528471247 351 FITY-YPNDHKNDWPHLVLL-TEDdrHYNALI 380
Cdd:cd22749  203 VNFHeFPPEDSDSLPVITLLyRPG--HYDILY 232
 
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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