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Conserved domains on  [gi|6807862|emb|CAB70704|]
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hypothetical protein, partial [Homo sapiens]

Protein Classification

E3 ubiquitin-protein ligase( domain architecture ID 1909272)

RBR-type E3 ubiquitin-protein ligase mediates through its RING domain the ubiquitination of target proteins by bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ariadne super family cl44843
Ariadne domain; This entry represents the Ariadne domain found in the Ariadne subfamily E3 ...
 36-164 3.04e-12

Ariadne domain; This entry represents the Ariadne domain found in the Ariadne subfamily E3 ubiquitin ligase proteins. The C-terminal Ariadne domain adopts an elongated four-helix bundle consisting of an antiparallel arrangement of seven-to-ten-turn long helices. The Ariadne domain is straddled on one side by the IBR domain, and on the other by the RING2 domain. Notably, the Ariadne domain embraces the surface of RING2 containing the catalytic Cys357. The ariadne Domain Masks the HHARI Catalytic Cys357 and Inhibits Intrinsic E3 Activity.


The actual alignment was detected with superfamily member pfam19422:

Pssm-ID: 466073  Cd Length: 261  Bit Score: 66.98  E-value: 3.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807862     36 EAEKKHKRFQ-ELDRFMHYYTRFKNHEHSYQLEQRLLKTAKEKMEQlsraLKETEGGCPDTTFIEDAVHVLLKTRRILKC 114
Cdd:pfam19422   3 DREKKAERAKrDLYRYMHYHNRYKAHTDSFKLESKLKETIQEKISI----LEERDSKLRDFSWVTNGLYRLFRSRRVLSY 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6807862    115 SYPYGFFL------------EPKSTKKEIFELMQTDLEMVTEDLAQKVNRPYLRTPRHKIIK 164
Cdd:pfam19422  79 SYPFAFYMfgdelfkdemtkEEREIKQNLFEDQQQQLEANVEKLSKFLEEPFDEYSEDKVME 140
BRcat_Rcat_RBR super family cl45895
BRcat (benign-catalytic) and Rcat (required-for-catalysis) domains, part of the RBR ...
 1-21 3.38e-09

BRcat (benign-catalytic) and Rcat (required-for-catalysis) domains, part of the RBR (RING1-BRcat-Rcat) domain; The RBR family of RING-type E3 ligases are characterized by containing an RBR (RING1-BRcat-Rcat) domain, which was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. It is composed of an extended RING domain (RING1) followed by an in-between RING (IBR) domain and the catalytic domain, which is structurally an IBR domain but is commonly designated as RING2. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBRs has been changed to RING1-BRcat (benign-catalytic)-Rcat (required-for-catalysis), where the IBR and RING2 domains have been renamed as BRcat and Rcat domains, respectively. The RBR domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase functions to facilitate the ubiquitination reaction. The BRcat domain adopts the same fold as the Rcat domain while lacking the catalytic cysteine residue and ubiquitination activity. RBR family members play roles in protein quality control and can indirectly regulate transcription. Evidence suggests that RBR proteins are often parts of cullin-containing ubiquitin ligase complexes.


The actual alignment was detected with superfamily member cd20361:

Pssm-ID: 459240  Cd Length: 62  Bit Score: 52.85  E-value: 3.38e-09
                        10        20
                ....*....|....*....|.
gi 6807862    1 LEEWKKHSSSTGGYYRCTRYE 21
Cdd:cd20361  42 LEEWKKHSSSTGGYFRCNRYE 62
 
Name Accession Description Interval E-value
Ariadne pfam19422
Ariadne domain; This entry represents the Ariadne domain found in the Ariadne subfamily E3 ...
 36-164 3.04e-12

Ariadne domain; This entry represents the Ariadne domain found in the Ariadne subfamily E3 ubiquitin ligase proteins. The C-terminal Ariadne domain adopts an elongated four-helix bundle consisting of an antiparallel arrangement of seven-to-ten-turn long helices. The Ariadne domain is straddled on one side by the IBR domain, and on the other by the RING2 domain. Notably, the Ariadne domain embraces the surface of RING2 containing the catalytic Cys357. The ariadne Domain Masks the HHARI Catalytic Cys357 and Inhibits Intrinsic E3 Activity.


Pssm-ID: 466073  Cd Length: 261  Bit Score: 66.98  E-value: 3.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807862     36 EAEKKHKRFQ-ELDRFMHYYTRFKNHEHSYQLEQRLLKTAKEKMEQlsraLKETEGGCPDTTFIEDAVHVLLKTRRILKC 114
Cdd:pfam19422   3 DREKKAERAKrDLYRYMHYHNRYKAHTDSFKLESKLKETIQEKISI----LEERDSKLRDFSWVTNGLYRLFRSRRVLSY 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6807862    115 SYPYGFFL------------EPKSTKKEIFELMQTDLEMVTEDLAQKVNRPYLRTPRHKIIK 164
Cdd:pfam19422  79 SYPFAFYMfgdelfkdemtkEEREIKQNLFEDQQQQLEANVEKLSKFLEEPFDEYSEDKVME 140
Rcat_RBR_ANKIB1 cd20361
Rcat domain found in ankyrin repeat and IBR domain-containing protein 1 (ANKIB1) and similar ...
 1-21 3.38e-09

Rcat domain found in ankyrin repeat and IBR domain-containing protein 1 (ANKIB1) and similar proteins; ANKIB1 is an RBR-type E3 ubiquitin-protein ligase that may function as part of an E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates. It contains N-terminal ankyrin repeats, and an RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been changed to RING1-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase functions to facilitate the ubiquitination reaction. This model corresponds to the Rcat domain of ANKIB1 that is essential for RBR E3 ligase activity and adopts the same fold as the BRcat domain.


Pssm-ID: 439022  Cd Length: 62  Bit Score: 52.85  E-value: 3.38e-09
                        10        20
                ....*....|....*....|.
gi 6807862    1 LEEWKKHSSSTGGYYRCTRYE 21
Cdd:cd20361  42 LEEWKKHSSSTGGYFRCNRYE 62
 
Name Accession Description Interval E-value
Ariadne pfam19422
Ariadne domain; This entry represents the Ariadne domain found in the Ariadne subfamily E3 ...
 36-164 3.04e-12

Ariadne domain; This entry represents the Ariadne domain found in the Ariadne subfamily E3 ubiquitin ligase proteins. The C-terminal Ariadne domain adopts an elongated four-helix bundle consisting of an antiparallel arrangement of seven-to-ten-turn long helices. The Ariadne domain is straddled on one side by the IBR domain, and on the other by the RING2 domain. Notably, the Ariadne domain embraces the surface of RING2 containing the catalytic Cys357. The ariadne Domain Masks the HHARI Catalytic Cys357 and Inhibits Intrinsic E3 Activity.


Pssm-ID: 466073  Cd Length: 261  Bit Score: 66.98  E-value: 3.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807862     36 EAEKKHKRFQ-ELDRFMHYYTRFKNHEHSYQLEQRLLKTAKEKMEQlsraLKETEGGCPDTTFIEDAVHVLLKTRRILKC 114
Cdd:pfam19422   3 DREKKAERAKrDLYRYMHYHNRYKAHTDSFKLESKLKETIQEKISI----LEERDSKLRDFSWVTNGLYRLFRSRRVLSY 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6807862    115 SYPYGFFL------------EPKSTKKEIFELMQTDLEMVTEDLAQKVNRPYLRTPRHKIIK 164
Cdd:pfam19422  79 SYPFAFYMfgdelfkdemtkEEREIKQNLFEDQQQQLEANVEKLSKFLEEPFDEYSEDKVME 140
Rcat_RBR_ANKIB1 cd20361
Rcat domain found in ankyrin repeat and IBR domain-containing protein 1 (ANKIB1) and similar ...
 1-21 3.38e-09

Rcat domain found in ankyrin repeat and IBR domain-containing protein 1 (ANKIB1) and similar proteins; ANKIB1 is an RBR-type E3 ubiquitin-protein ligase that may function as part of an E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates. It contains N-terminal ankyrin repeats, and an RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been changed to RING1-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase functions to facilitate the ubiquitination reaction. This model corresponds to the Rcat domain of ANKIB1 that is essential for RBR E3 ligase activity and adopts the same fold as the BRcat domain.


Pssm-ID: 439022  Cd Length: 62  Bit Score: 52.85  E-value: 3.38e-09
                        10        20
                ....*....|....*....|.
gi 6807862    1 LEEWKKHSSSTGGYYRCTRYE 21
Cdd:cd20361  42 LEEWKKHSSSTGGYFRCNRYE 62
Rcat_RBR_ARI7-like cd22583
Rcat domain found in E3 ubiquitin-protein ligase ARI7 and similar proteins; This subfamily ...
 1-20 8.46e-04

Rcat domain found in E3 ubiquitin-protein ligase ARI7 and similar proteins; This subfamily contains probable RBR-type E3 ubiquitin-protein ligases (EC 2.3.2.31) including Arabidopsis thaliana ARI5, ARI6, ARI7, and ARI8, as well as Dictyostelium discoideum RbrA (also called Ariadne-like ubiquitin ligase). They may function as part of E3 complexes, which accept ubiquitin from E2 ubiquitin-conjugating enzymes and then transfer it to substrates. RbrA may be required for normal cell-type proportioning and cell sorting during multicellular development, and is also necessary for spore cell viability. Members of this subfamily contain an RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been changed to RING1-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase functions to facilitate the ubiquitination reaction. This model corresponds to the Rcat domain of ARI7-like proteins that are essential for RBR E3 ligase activity and adopt the same fold as the BRcat domain.


Pssm-ID: 439034  Cd Length: 55  Bit Score: 37.43  E-value: 8.46e-04
                        10        20
                ....*....|....*....|
gi 6807862    1 LEEWKKHSSSTGGYYRCTRY 20
Cdd:cd22583  36 LGPWSEHGERTGGFYACNRY 55
 
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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