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Conserved domains on  [gi|261862305|ref|NP_001159874|]
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tumor necrosis factor alpha-induced protein 3 isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OTU_TNFAIP3 cd22766
OTU (ovarian tumor) domain of tumor necrosis factor alpha induced protein 3; Tumor necrosis ...
 78-298 3.89e-143

OTU (ovarian tumor) domain of tumor necrosis factor alpha induced protein 3; Tumor necrosis factor (TNF) alpha-induced protein 3 (TNFAIP3) is also called OTU domain-containing protein 7C (OTUD7C), DNA-binding protein A20, or zinc finger protein A20. It is a ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) activities. It antagonizes IKK [IkappaB (inhibitor of kappaB) kinase] activation by modulating Lys63-linked polyubiquitination of cytokine-receptor-associated factors including TRAF2/6 (tumour-necrosis-factor-receptor-associated factor 2/6) and RIP1 (receptor-interacting protein 1). It can also inhibit IKK through a non-catalytic mechanism which involves polyubiquitin. In vitro, TNFAIP3 is able to deubiquitinate 'Lys-11'-, 'Lys-48'- and 'Lys-63' polyubiquitin chains. TNFAIP3 contains several A20-type zinc fingers that mediate the ubiquitin ligase activity and an OTU (ovarian tumor) domain that contains the DUB activity. It belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C64 cysteine protease by MEROPS.


:

Pssm-ID: 438603  Cd Length: 220  Bit Score: 420.51  E-value: 3.89e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305  78 KTMHRYTLEMFRTCQFCPQFREIIHKALIDRSVQASLESQKKLNWCREVRKLVALKTNGDGNCLMHAACQYMWGVQDTDL 157
Cdd:cd22766    1 LTMHRYTLQLPRLCQFPPDFREFLQKALIDRNIQRTLEEAKKLNWCREVRKLVPLKTTGDGNCLLHAVSLYMWGVQDTDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305 158 VLRKALCSTLKETDTRNFKFRWQLESLKSQEFVETGLCYDTRNWNDEWDNLVKMASADTPAARSGLQYNSLEEIHIFVLS 237
Cdd:cd22766   81 VLRKALYEALVETDTRNFKLRWQRERLKSQEFVGTGLRYDTREWEEEWDNVVKMASPESKPAAGGLPYNSLEEIHIFVLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261862305 238 NILRRPIIVISDKMLRSLEsGSNFAPLKVGGIYLPLHWPAQECYRYPIVLGYDSQHFVPLV 298
Cdd:cd22766  161 NILRRPIIVIADDMLRSLE-GSSLAPLNFGGIYLPLHWPPQECYKYPIVLGYDSQHFTPLV 220
ZnF_A20 smart00259
A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger ...
 781-806 1.31e-05

A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappaB activation.


:

Pssm-ID: 128555  Cd Length: 26  Bit Score: 42.57  E-value: 1.31e-05
                           10        20
                   ....*....|....*....|....*.
gi 261862305   781 KQRCRAPACDHFGNAKCNGYCNECYQ 806
Cdd:smart00259   1 PIKCRRPGCGFFGNPATEGLCSKCFK 26
ZnF_A20 smart00259
A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger ...
 504-528 2.29e-05

A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappaB activation.


:

Pssm-ID: 128555  Cd Length: 26  Bit Score: 41.80  E-value: 2.29e-05
                           10        20
                   ....*....|....*....|....*
gi 261862305   504 AMKCRSPGCPFTLNVQHNGFCERCH 528
Cdd:smart00259   1 PIKCRRPGCGFFGNPATEGLCSKCF 25
ZnF_A20 smart00259
A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger ...
 421-446 9.69e-05

A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappaB activation.


:

Pssm-ID: 128555  Cd Length: 26  Bit Score: 39.88  E-value: 9.69e-05
                           10        20
                   ....*....|....*....|....*.
gi 261862305   421 DIKCETPNCPFFMSVNTQPLCHECSE 446
Cdd:smart00259   1 PIKCRRPGCGFFGNPATEGLCSKCFK 26
ZnF_A20 smart00259
A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger ...
 626-651 1.58e-04

A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappaB activation.


:

Pssm-ID: 128555  Cd Length: 26  Bit Score: 39.49  E-value: 1.58e-04
                           10        20
                   ....*....|....*....|....*.
gi 261862305   626 TSKCRKAGCMYFGTPENKGFCTLCFI 651
Cdd:smart00259   1 PIKCRRPGCGFFGNPATEGLCSKCFK 26
ZnF_A20 smart00259
A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger ...
 678-701 9.26e-04

A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappaB activation.


:

Pssm-ID: 128555  Cd Length: 26  Bit Score: 37.18  E-value: 9.26e-04
                           10        20
                   ....*....|....*....|....
gi 261862305   678 PCLGRECGTLGSTMFEGYCQKCFI 701
Cdd:smart00259   3 KCRRPGCGFFGNPATEGLCSKCFK 26
 
Name Accession Description Interval E-value
OTU_TNFAIP3 cd22766
OTU (ovarian tumor) domain of tumor necrosis factor alpha induced protein 3; Tumor necrosis ...
 78-298 3.89e-143

OTU (ovarian tumor) domain of tumor necrosis factor alpha induced protein 3; Tumor necrosis factor (TNF) alpha-induced protein 3 (TNFAIP3) is also called OTU domain-containing protein 7C (OTUD7C), DNA-binding protein A20, or zinc finger protein A20. It is a ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) activities. It antagonizes IKK [IkappaB (inhibitor of kappaB) kinase] activation by modulating Lys63-linked polyubiquitination of cytokine-receptor-associated factors including TRAF2/6 (tumour-necrosis-factor-receptor-associated factor 2/6) and RIP1 (receptor-interacting protein 1). It can also inhibit IKK through a non-catalytic mechanism which involves polyubiquitin. In vitro, TNFAIP3 is able to deubiquitinate 'Lys-11'-, 'Lys-48'- and 'Lys-63' polyubiquitin chains. TNFAIP3 contains several A20-type zinc fingers that mediate the ubiquitin ligase activity and an OTU (ovarian tumor) domain that contains the DUB activity. It belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C64 cysteine protease by MEROPS.


Pssm-ID: 438603  Cd Length: 220  Bit Score: 420.51  E-value: 3.89e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305  78 KTMHRYTLEMFRTCQFCPQFREIIHKALIDRSVQASLESQKKLNWCREVRKLVALKTNGDGNCLMHAACQYMWGVQDTDL 157
Cdd:cd22766    1 LTMHRYTLQLPRLCQFPPDFREFLQKALIDRNIQRTLEEAKKLNWCREVRKLVPLKTTGDGNCLLHAVSLYMWGVQDTDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305 158 VLRKALCSTLKETDTRNFKFRWQLESLKSQEFVETGLCYDTRNWNDEWDNLVKMASADTPAARSGLQYNSLEEIHIFVLS 237
Cdd:cd22766   81 VLRKALYEALVETDTRNFKLRWQRERLKSQEFVGTGLRYDTREWEEEWDNVVKMASPESKPAAGGLPYNSLEEIHIFVLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261862305 238 NILRRPIIVISDKMLRSLEsGSNFAPLKVGGIYLPLHWPAQECYRYPIVLGYDSQHFVPLV 298
Cdd:cd22766  161 NILRRPIIVIADDMLRSLE-GSSLAPLNFGGIYLPLHWPPQECYKYPIVLGYDSQHFTPLV 220
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
 135-294 7.44e-32

OTU-like cysteine protease; This family is comprised of a group of predicted cysteine proteases, homologous to the Ovarian Tumour (OTU) gene in Drosophila. Members include proteins from eukaryotes, viruses and pathogenic bacterium. The conserved cysteine and histidine, and possibly the aspartate, represent the catalytic residues in this putative group of proteases.


Pssm-ID: 426728 [Multi-domain]  Cd Length: 127  Bit Score: 120.25  E-value: 7.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305  135 NGDGNCLMHAACQYMWGVQDtdlVLRKALCSTLKETDTRNFKfrwqleslksQEFVETGLCYDtrnwnDEWDNLVKMASA 214
Cdd:pfam02338   1 PGDGNCLYRSISHQLWGVHD---VLRKMLVQELRETLAEYMR----------EHKEEFEPFLE-----DDETGDIIEIEQ 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305  215 DTpaarsglqyNSLEEIHIFVLSNILRRPIIVISDkmlrslESGSNFAPLKVGGIYLPLHWPAQECYRYPIVLGYDSQHF 294
Cdd:pfam02338  63 TG---------AWGGEIEIFALAHILRRPIIVYKS------EGGEELGGLKEYGIYLPLGWDPSLCLVYPRHLYYLGGHY 127
ZnF_A20 smart00259
A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger ...
 781-806 1.31e-05

A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappaB activation.


Pssm-ID: 128555  Cd Length: 26  Bit Score: 42.57  E-value: 1.31e-05
                           10        20
                   ....*....|....*....|....*.
gi 261862305   781 KQRCRAPACDHFGNAKCNGYCNECYQ 806
Cdd:smart00259   1 PIKCRRPGCGFFGNPATEGLCSKCFK 26
ZnF_A20 smart00259
A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger ...
 504-528 2.29e-05

A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappaB activation.


Pssm-ID: 128555  Cd Length: 26  Bit Score: 41.80  E-value: 2.29e-05
                           10        20
                   ....*....|....*....|....*
gi 261862305   504 AMKCRSPGCPFTLNVQHNGFCERCH 528
Cdd:smart00259   1 PIKCRRPGCGFFGNPATEGLCSKCF 25
ZnF_A20 smart00259
A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger ...
 421-446 9.69e-05

A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappaB activation.


Pssm-ID: 128555  Cd Length: 26  Bit Score: 39.88  E-value: 9.69e-05
                           10        20
                   ....*....|....*....|....*.
gi 261862305   421 DIKCETPNCPFFMSVNTQPLCHECSE 446
Cdd:smart00259   1 PIKCRRPGCGFFGNPATEGLCSKCFK 26
ZnF_A20 smart00259
A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger ...
 626-651 1.58e-04

A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappaB activation.


Pssm-ID: 128555  Cd Length: 26  Bit Score: 39.49  E-value: 1.58e-04
                           10        20
                   ....*....|....*....|....*.
gi 261862305   626 TSKCRKAGCMYFGTPENKGFCTLCFI 651
Cdd:smart00259   1 PIKCRRPGCGFFGNPATEGLCSKCFK 26
zf-A20 pfam01754
A20-like zinc finger; The A20 Zn-finger of bovine/human Rabex5/rabGEF1 is a Ubiquitin Binding ...
 782-806 3.96e-04

A20-like zinc finger; The A20 Zn-finger of bovine/human Rabex5/rabGEF1 is a Ubiquitin Binding Domain. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappa B activation.


Pssm-ID: 460313  Cd Length: 24  Bit Score: 38.25  E-value: 3.96e-04
                          10        20
                  ....*....|....*....|....*
gi 261862305  782 QRCRAPaCDHFGNAKCNGYCNECYQ 806
Cdd:pfam01754   1 LLCRNG-CGFYGSPATNGLCSKCYK 24
ZnF_A20 smart00259
A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger ...
 678-701 9.26e-04

A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappaB activation.


Pssm-ID: 128555  Cd Length: 26  Bit Score: 37.18  E-value: 9.26e-04
                           10        20
                   ....*....|....*....|....
gi 261862305   678 PCLGRECGTLGSTMFEGYCQKCFI 701
Cdd:smart00259   3 KCRRPGCGFFGNPATEGLCSKCFK 26
 
Name Accession Description Interval E-value
OTU_TNFAIP3 cd22766
OTU (ovarian tumor) domain of tumor necrosis factor alpha induced protein 3; Tumor necrosis ...
 78-298 3.89e-143

OTU (ovarian tumor) domain of tumor necrosis factor alpha induced protein 3; Tumor necrosis factor (TNF) alpha-induced protein 3 (TNFAIP3) is also called OTU domain-containing protein 7C (OTUD7C), DNA-binding protein A20, or zinc finger protein A20. It is a ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) activities. It antagonizes IKK [IkappaB (inhibitor of kappaB) kinase] activation by modulating Lys63-linked polyubiquitination of cytokine-receptor-associated factors including TRAF2/6 (tumour-necrosis-factor-receptor-associated factor 2/6) and RIP1 (receptor-interacting protein 1). It can also inhibit IKK through a non-catalytic mechanism which involves polyubiquitin. In vitro, TNFAIP3 is able to deubiquitinate 'Lys-11'-, 'Lys-48'- and 'Lys-63' polyubiquitin chains. TNFAIP3 contains several A20-type zinc fingers that mediate the ubiquitin ligase activity and an OTU (ovarian tumor) domain that contains the DUB activity. It belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C64 cysteine protease by MEROPS.


Pssm-ID: 438603  Cd Length: 220  Bit Score: 420.51  E-value: 3.89e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305  78 KTMHRYTLEMFRTCQFCPQFREIIHKALIDRSVQASLESQKKLNWCREVRKLVALKTNGDGNCLMHAACQYMWGVQDTDL 157
Cdd:cd22766    1 LTMHRYTLQLPRLCQFPPDFREFLQKALIDRNIQRTLEEAKKLNWCREVRKLVPLKTTGDGNCLLHAVSLYMWGVQDTDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305 158 VLRKALCSTLKETDTRNFKFRWQLESLKSQEFVETGLCYDTRNWNDEWDNLVKMASADTPAARSGLQYNSLEEIHIFVLS 237
Cdd:cd22766   81 VLRKALYEALVETDTRNFKLRWQRERLKSQEFVGTGLRYDTREWEEEWDNVVKMASPESKPAAGGLPYNSLEEIHIFVLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261862305 238 NILRRPIIVISDKMLRSLEsGSNFAPLKVGGIYLPLHWPAQECYRYPIVLGYDSQHFVPLV 298
Cdd:cd22766  161 NILRRPIIVIADDMLRSLE-GSSLAPLNFGGIYLPLHWPPQECYKYPIVLGYDSQHFTPLV 220
OTU_C64 cd22750
OTU (ovarian tumor) domain of family C64 cysteine proteases; This group includes proteins ...
 108-298 1.86e-79

OTU (ovarian tumor) domain of family C64 cysteine proteases; This group includes proteins classified as family C64 cysteine protease by MEROPS, such as tumor necrosis factor (TNF) alpha-induced protein 3 (TNFAIP3), ZRANB1, OTU domain-containing protein 7A (OTUD7A), and OTUD7B. It also includes VCIP135. These proteins are deubiquitinases (DUBs)/ubiquitin thioesterases (EC 3.4.19.12) that mediates the deubiquitination of protein substrates. TNFAIP3 also contains ubiquitin ligase activity. It antagonizes IKK [IkappaB (inhibitor of kappaB) kinase] activation by modulating Lys63-linked polyubiquitination of cytokine-receptor-associated factors including TRAF2/6 (tumour-necrosis-factor-receptor-associated factor 2/6) and RIP1 (receptor-interacting protein 1). ZRANB1 binds, deubiquitinates, and stabilizes EZH2, which is the catalytic component of the Polycomb repressive complex 2 (PRC2) that silences gene transcription by methylating histone H3 at lysine 27 and is mutated or highly expressed in many types of cancer, including lymphoma, melanoma, prostate cancer, ovarian cancer, and breast cancer. OTUD7A has been identified as a critical gene for brain function, while OTUD7B functions as a negative regulator of the non-canonical NF-kappaB pathway by mediating the deubiquitination of TRAF3, an inhibitor of the NF-kappaB pathway, resulting in preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappaB. VCIP135 controls Golgi membrane dynamics in the cell cycle and is required for Golgi and ER assembly. This group belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad.


Pssm-ID: 438587  Cd Length: 185  Bit Score: 253.42  E-value: 1.86e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305 108 RSVQASLESQKKLNWCREVRKLVALKTNGDGNCLMHAACQYMWGVQDTDLVLRKALCSTLKETDTRNFKFRWQLESLKSQ 187
Cdd:cd22750    1 RDLKDDLESEKVINWCRGVSRLVPLHTRGDGNCLLHAVSLALWGVEDRDLLLRSALHETLQNDQERRFRARWRRQQLKSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305 188 EfvETGLCYDTRNWNDEWDNLVKMASADTPAARSGlqyNSLEEIHIFVLSNILRRPIIVISDKMLRSLEsGSNFAPLKVG 267
Cdd:cd22750   81 Q--ELGLSLDEEALQAEWEEILKAAETPTVPAGPG---SYLEEIHIFVLANVLRRPIIVLADDSARSLE-GSALQDNGMS 154

                        170       180       190
                 ....*....|....*....|....*....|.
gi 261862305 268 GIYLPLHWPAQECYRYPIVLGYDSQHFVPLV 298
Cdd:cd22750  155 GIYLPLLWPPSECSRSPLALGYSNGHFSPLV 185
OTU_OTUD7 cd22768
OTU (ovarian tumor) domain of OTU domain-containing proteins 7A, 7B, and similar proteins; ...
 108-298 7.00e-63

OTU (ovarian tumor) domain of OTU domain-containing proteins 7A, 7B, and similar proteins; This subfamily consists of OTU domain-containing protein 7A (OTUD7A), OTUD7B, and similar proteins. OTUD7A and OTUD7B are deubiquitinases (DUBs)/ubiquitin thioesterases (EC 3.4.19.12) that specifically target Lys11-linked polyubiquitin. OTUD7A, also called zinc finger protein Cezanne 2, has been identified as a critical gene for brain function. It localizes to dendritic and spine compartments in cortical neurons, and its reduced levels contributed to dendritic spine and dendrite outgrowth deficits. OTUD7B, also called zinc finger protein Cezanne, functions as a negative regulator of the non-canonical NF-kappaB pathway by mediating the deubiquitination of TRAF3, an inhibitor of the NF-kappaB pathway, resulting in preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappaB. OTUD7 proteins belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. They are classified as family C64 cysteine proteases by MEROPS.


Pssm-ID: 438605  Cd Length: 208  Bit Score: 209.85  E-value: 7.00e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305 108 RSVQASLESQKKLNWCREVR---KLVALKTNGDGNCLMHAACQYMWGVQDTDLVLRKALCSTLKETDTRN-FKFRW---Q 180
Cdd:cd22768    1 TSTLVSLEQAGRLNWWAKDGgcqRLLPLATTGDGNCLLHAASLGMWGFHDRLLTLRKALYETLTSSAAKEaLKRRWrwqQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305 181 LESLKsqefvETGLCYDTRNWNDEWDNLVKMASADTPAARSG---------------LQYNSLEEIHIFVLSNILRRPII 245
Cdd:cd22768   81 TQVNK-----EAGLVYSEEEWEREWKSLLKLASTEPRSQPSPssgseleevienssdPTYESLEEIHVFVLAHVLRRPII 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 261862305 246 VISDKMLRSLeSGSNFAPLKVGGIYLPLHWPAQECYRYPIVLGYDSQHFVPLV 298
Cdd:cd22768  156 VVADTMLRDS-NGEPLAPIPFGGIYLPLECPPSECHRSPLVLAYDAAHFSALV 207
OTU_OTUD7B cd22772
OTU (ovarian tumor) domain of OTU domain-containing protein 7B; OTU domain-containing protein ...
 108-299 1.89e-54

OTU (ovarian tumor) domain of OTU domain-containing protein 7B; OTU domain-containing protein 7B (OTUD7B) is also called cellular zinc finger anti-NF-kappa-B protein, zinc finger A20 domain-containing protein 1, or zinc finger protein Cezanne. It is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that specifically targets Lys11-linked polyubiquitin. It functions as a negative regulator of the non-canonical NF-kappaB pathway by mediating the deubiquitination of TRAF3, an inhibitor of the NF-kappaB pathway, resulting in preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappaB. OTUD7B also deubiquitinates ZAP70, and thus, regulates T cell receptor (TCR) signaling. It belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C64 cysteine protease by MEROPS.


Pssm-ID: 438609  Cd Length: 207  Bit Score: 187.16  E-value: 1.89e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305 108 RSVQASLESQKKLNWCREV----RKLVALKTNGDGNCLMHAACQYMWGVQDTDLVLRKALCSTLK---ETDTRNFKFRWQ 180
Cdd:cd22772    1 QSMLVALEQAGRLNWWVSVdptcQRLLPLATTGDGNCLLHAASLGMWGFHDRDLMLRKALYALMEkgvEKEALKRRWRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305 181 leslKSQEFVETGLCYDTRNWNDEWDNLVKMASAD-------TPAARSGLQ------YNSLEEIHIFVLSNILRRPIIVI 247
Cdd:cd22772   81 ----QTQQNKESGLVYTEDEWQKEWNELIKLASSEprmhygtNGANCGGVEsseepvYESLEEFHVFVLAHVLRRPIVVV 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 261862305 248 SDKMLRSlESGSNFAPLKVGGIYLPLHWPAQECYRYPIVLGYDSQHFVPLVT 299
Cdd:cd22772  157 ADTMLRD-SGGEAFAPIPFGGIYLPLEVPASKCHRSPLVLAYDQAHFSALVS 207
OTU_OTUD7A cd22773
OTU (ovarian tumor) domain of OTU domain-containing protein 7A; OTU domain-containing protein ...
 108-299 2.14e-49

OTU (ovarian tumor) domain of OTU domain-containing protein 7A; OTU domain-containing protein 7A (OTUD7A), also called zinc finger protein Cezanne 2, is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that specifically targets Lys11-linked polyubiquitin. OTUD7A has been identified as a critical gene for brain function. It localizes to dendritic and spine compartments in cortical neurons, and its reduced levels contributed to dendritic spine and dendrite outgrowth deficits. A homozygous OTUD7A missense variant located within the OTU catalytic domain is linked to early-onset epileptic encephalopathy and proteasome dysfunction. OTUD7A belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C64 cysteine protease by MEROPS.


Pssm-ID: 438610  Cd Length: 207  Bit Score: 172.94  E-value: 2.14e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305 108 RSVQASLESQKKLNW----CREVRKLVALKTNGDGNCLMHAACQYMWGVQDTDLVLRKALCSTLK---ETDTRNFKFRWQ 180
Cdd:cd22773    1 QSTMVALEQAGRLNWwstvCTSCKRLLPLATTGDGNCLLHAASLGMWGFHDRDLVLRKALYTMMKsgaEREALKRRWRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305 181 leslKSQEFVETGLCYDTRNWNDEWDNLVKMASAD-------TPAARSGLQ------YNSLEEIHIFVLSNILRRPIIVI 247
Cdd:cd22773   81 ----QTQQNKESGLVYTEEEWEREWNELLKLASSEprthfskNGGTGGGVDnsedpvYESLEEFHVFVLAHILRRPIVVV 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 261862305 248 SDKMLRSlESGSNFAPLKVGGIYLPLHWPAQECYRYPIVLGYDSQHFVPLVT 299
Cdd:cd22773  157 ADTMLRD-SGGEAFAPIPFGGIYLPLEVPPNRCHCSPLVLAYDQAHFSALVS 207
OTU_ZRANB1 cd22767
OTU (ovarian tumor) domain of Ubiquitin thioesterase ZRANB1 and similar proteins; ZRANB1 is ...
 108-298 9.89e-41

OTU (ovarian tumor) domain of Ubiquitin thioesterase ZRANB1 and similar proteins; ZRANB1 is also called TRAF-binding domain-containing protein, Trabid, or zinc finger Ran-binding domain-containing protein 1. It is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that specifically hydrolyzes 'Lys-29'-linked and 'Lys-33'-linked diubiquitin; it also cleaves 'Lys-63'-linked chains with less efficiency. ZRANB1 binds, deubiquitinates, and stabilizes EZH2, which is the catalytic component of the Polycomb repressive complex 2 (PRC2) that silences gene transcription by methylating histone H3 at lysine 27 and is mutated or highly expressed in many types of cancer, including lymphoma, melanoma, prostate cancer, ovarian cancer, and breast cancer. Drosophila Trabid interacts with TGF-beta Activating Kinase 1 (TAK1), which triggers both immunity and apoptosis, resulting in reduced immune signaling output and K63-linked ubiquitination. ZRANB1 belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. ZRANB1 does not contain the conserved aspartate, and uses cysteine and histidine as a catalytic dyad. It is classified as a family C64 cysteine protease by MEROPS.


Pssm-ID: 438604  Cd Length: 185  Bit Score: 147.83  E-value: 9.89e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305 108 RSVQASLESQ-KKLNWCREV-----RKLVALKTNGDGNCLMHAACQYMWGVQDTDLVLRKALCSTLKETDTRnFKFRWQ- 180
Cdd:cd22767    1 RDVQKELEEEsPIINWSLELtdrlgSRLYALWNRTAGDCLLDSVLQATWGVFDRDNVLRRALADSLHDCAHW-FYSRWKe 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305 181 LESLKSQEFvetGLCYDTRNWNDEWDNLVKMASadTPAArsglqynSLEEIHIFVLSNILRRPIIVISDKMLRSLEsGSN 260
Cdd:cd22767   80 YESWQAQSL---GYSLEEEQWQKDWAFLLSLAS--QPGA-------SLEQTHIFALAHILRRPIIVYGVKYVKSFR-GET 146

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 261862305 261 FAPLKVGGIYLPLHWPAQECYRYPIVLGYDSQHFVPLV 298
Cdd:cd22767  147 LGYARFQGVYLPLLWEQSFCWKSPIALGYTRGHFSALV 184
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
 135-294 7.44e-32

OTU-like cysteine protease; This family is comprised of a group of predicted cysteine proteases, homologous to the Ovarian Tumour (OTU) gene in Drosophila. Members include proteins from eukaryotes, viruses and pathogenic bacterium. The conserved cysteine and histidine, and possibly the aspartate, represent the catalytic residues in this putative group of proteases.


Pssm-ID: 426728 [Multi-domain]  Cd Length: 127  Bit Score: 120.25  E-value: 7.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305  135 NGDGNCLMHAACQYMWGVQDtdlVLRKALCSTLKETDTRNFKfrwqleslksQEFVETGLCYDtrnwnDEWDNLVKMASA 214
Cdd:pfam02338   1 PGDGNCLYRSISHQLWGVHD---VLRKMLVQELRETLAEYMR----------EHKEEFEPFLE-----DDETGDIIEIEQ 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305  215 DTpaarsglqyNSLEEIHIFVLSNILRRPIIVISDkmlrslESGSNFAPLKVGGIYLPLHWPAQECYRYPIVLGYDSQHF 294
Cdd:pfam02338  63 TG---------AWGGEIEIFALAHILRRPIIVYKS------EGGEELGGLKEYGIYLPLGWDPSLCLVYPRHLYYLGGHY 127
OTU_VCIP135 cd22769
OTU (ovarian tumor) domain of deubiquitinating protein VCIP135; Deubiquitinating protein ...
 107-298 4.03e-13

OTU (ovarian tumor) domain of deubiquitinating protein VCIP135; Deubiquitinating protein VCIP135 is also called valosin-containing protein p97/p47 complex-interacting protein 1, valosin-containing protein p97/p47 complex-interacting protein p135, or VCP/p47 complex-interacting 135-kDa protein. It is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that hydrolyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitin chains. It is necessary for VCP-mediated reassembly of Golgi stacks after mitosis, and may play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER). VCIP135 controls Golgi membrane dynamics in the cell cycle and is required for Golgi and ER assembly. It belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. Not all members of this subfamily contain the active site. It is closely related to proteins classified as family C64 cysteine protease by MEROPS, such as TNFAIP3, ZRANB1, and OTUD7A/B.


Pssm-ID: 438606  Cd Length: 197  Bit Score: 68.86  E-value: 4.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305 107 DRSV-----QASLESQKKLNWCREVrkLVALKTNGDGNCLMHAACQymwgvqdtDLVLRKALCSTLKEtdtrNFK--FRW 179
Cdd:cd22769   20 DRSGslsylHDTLEEIKKANDNEER--LIPIHADGDGHCLVHAVSR--------ALVGRELFWHALRE----NLKqhFKE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305 180 QLESLKS--QEFVETglcydtrnwnDEWDNLVKMASAD-TPAARSGLqynSLEEIHIFVLSNILRRPIIVISDkmLRSLE 256
Cdd:cd22769   86 NLDQYKAlfQDFIDD----------SEWPDIIAECDPDfVPPEGEPL---GLRNIHIFGLANVLKRPIILLDS--LSGMQ 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 261862305 257 SGSNFAplkvgGIYLPLHWPAQEC------YRYPIVLGYDS---QHFVPLV 298
Cdd:cd22769  151 SSGDYS-----AIFLPGLVPPEKCrgkdglLNKPICIAWSSsgrNHFIPLV 196
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
 136-297 9.27e-10

OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation.


Pssm-ID: 438581 [Multi-domain]  Cd Length: 128  Bit Score: 57.06  E-value: 9.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305 136 GDGNCLMHAACQYMWGVQDTDLVLRKALCSTLKEtdtrnfkfRWQLESlksqefvetGLCYDTRNWNDEWDNLV-KMASA 214
Cdd:cd22744    7 GDGNCLFRALAHALYGDQESHRELRQEVVDYLRE--------NPDLYE---------PAELADEDDGEDFDEYLqRMRKP 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305 215 DTPAarsglqynslEEIHIFVLSNILRRPIIVISDkmlrslesgsnfaplkvGGIYLPLHW--PAQECYRYPIVLGYDS- 291
Cdd:cd22744   70 GTWG----------GELELQALANALNVPIVVYSE-----------------DGGFLPVSVfgPGPGPSGRPIHLLYTGg 122


                 ....*.
gi 261862305 292 QHFVPL 297
Cdd:cd22744  123 NHYDAL 128
ZnF_A20 smart00259
A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger ...
 781-806 1.31e-05

A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappaB activation.


Pssm-ID: 128555  Cd Length: 26  Bit Score: 42.57  E-value: 1.31e-05
                           10        20
                   ....*....|....*....|....*.
gi 261862305   781 KQRCRAPACDHFGNAKCNGYCNECYQ 806
Cdd:smart00259   1 PIKCRRPGCGFFGNPATEGLCSKCFK 26
ZnF_A20 smart00259
A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger ...
 504-528 2.29e-05

A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappaB activation.


Pssm-ID: 128555  Cd Length: 26  Bit Score: 41.80  E-value: 2.29e-05
                           10        20
                   ....*....|....*....|....*
gi 261862305   504 AMKCRSPGCPFTLNVQHNGFCERCH 528
Cdd:smart00259   1 PIKCRRPGCGFFGNPATEGLCSKCF 25
ZnF_A20 smart00259
A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger ...
 421-446 9.69e-05

A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappaB activation.


Pssm-ID: 128555  Cd Length: 26  Bit Score: 39.88  E-value: 9.69e-05
                           10        20
                   ....*....|....*....|....*.
gi 261862305   421 DIKCETPNCPFFMSVNTQPLCHECSE 446
Cdd:smart00259   1 PIKCRRPGCGFFGNPATEGLCSKCFK 26
OTU_232R-like cd22758
OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase ...
 136-297 1.39e-04

OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase 232R and similar proteins; This subfamily contains putative ubiquitin thioesterases 232R from Invertebrate iridescent virus and L96 from Tipula iridescent virus (TIV), Dictyostelium discoideum OTU domain-containing protein DDB_G0284757, and similar proteins. L96 may be involved in TIV genomic DNA packaging in a manner related to the Gag polyproteins of the mammalian viruses. Proteins in this subfamily contain an OTU domain. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438595 [Multi-domain]  Cd Length: 135  Bit Score: 42.64  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305 136 GDGNCLMHA-ACQ-YMWGVQDTDLVLRKALCSTLKETdtrnfkfrwqleslkSQEFVETGLCYDTRnwNDEWDN-LVKMA 212
Cdd:cd22758   13 GDGNCFFHAvSDQlYGNGIEHSHKELRQQAVNYLREN---------------PELYDGFFLSEFDE--EESWEEyLNRMS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305 213 SADTPAarsglqynslEEIHIFVLSNILRRPIIVISdkmlrSLESGSNFaplkvggIYLPLHWPAQEcyryPIVLGY-DS 291
Cdd:cd22758   76 KDGTWG----------DHIILQAAANLFNVRIVIIS-----SDGSDETT-------IIEPGNSKNGR----TIYLGHiGE 129


                 ....*.
gi 261862305 292 QHFVPL 297
Cdd:cd22758  130 NHYVSL 135
ZnF_A20 smart00259
A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger ...
 626-651 1.58e-04

A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappaB activation.


Pssm-ID: 128555  Cd Length: 26  Bit Score: 39.49  E-value: 1.58e-04
                           10        20
                   ....*....|....*....|....*.
gi 261862305   626 TSKCRKAGCMYFGTPENKGFCTLCFI 651
Cdd:smart00259   1 PIKCRRPGCGFFGNPATEGLCSKCFK 26
zf-A20 pfam01754
A20-like zinc finger; The A20 Zn-finger of bovine/human Rabex5/rabGEF1 is a Ubiquitin Binding ...
 782-806 3.96e-04

A20-like zinc finger; The A20 Zn-finger of bovine/human Rabex5/rabGEF1 is a Ubiquitin Binding Domain. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappa B activation.


Pssm-ID: 460313  Cd Length: 24  Bit Score: 38.25  E-value: 3.96e-04
                          10        20
                  ....*....|....*....|....*
gi 261862305  782 QRCRAPaCDHFGNAKCNGYCNECYQ 806
Cdd:pfam01754   1 LLCRNG-CGFYGSPATNGLCSKCYK 24
ZnF_A20 smart00259
A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger ...
 678-701 9.26e-04

A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappaB activation.


Pssm-ID: 128555  Cd Length: 26  Bit Score: 37.18  E-value: 9.26e-04
                           10        20
                   ....*....|....*....|....
gi 261862305   678 PCLGRECGTLGSTMFEGYCQKCFI 701
Cdd:smart00259   3 KCRRPGCGFFGNPATEGLCSKCFK 26
OTU_CeDUB-like cd22755
OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and ...
 136-271 2.35e-03

OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and OTU domains, and similar proteins; This subfamily is composed of mostly uncharacterized proteins containing an OTU domain, similar to Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and OTU domains. OTU domain-containing proteins function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438592 [Multi-domain]  Cd Length: 132  Bit Score: 38.78  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862305 136 GDGNCLMHAACQYMWGVQDTDLVLRKALCSTLKE-TDTRNFKFRWQLESLKsqEFVETGLCYDTRNWndewdnlvkmASa 214
Cdd:cd22755    8 GDGNCFFRALSYAITGSEKYHRKIRKAIVDFLEKnPDEFRNLLRSDYESVE--EYLEKSRMRYDGTW----------AT- 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261862305 215 dtpaarsglqynsleEIHIFVLSNILRRPIIVISDKMLR----SLESGSNFAPLKVGGIYL 271
Cdd:cd22755   75 ---------------DVEIFAAATLLGVDIYVYSKGGYKwllySPRFKLGKRNGSREAIYL 120
 
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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