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Conserved domains on  [gi|212646300|ref|NP_001129886|]
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RING-type domain-containing protein [Caenorhabditis elegans]

Protein Classification

RING finger protein( domain architecture ID 10621631)

RING finger protein may function as an E3 ubiquitin protein ligase that mediates 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

CATH:  3.30.40.10
EC:  2.3.2.27
Gene Ontology:  GO:0016567|GO:0061630|GO:0008270
PubMed:  19489725|11007473|22154517

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
45-94 6.52e-07

Zinc finger, C3HC4 type (RING finger);


:

Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 42.36  E-value: 6.52e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 212646300  45 RLQCFLCKLTEKRVLLRPCNHLCFCEPCNDTFQKQIPlLCPICHMHVQSF 94
Cdd:pfam13920  2 DLLCVICLDRPRNVVLLPCGHLCLCEECAERLLRKKK-KCPICRQPIESV 50
 
Name Accession Description Interval E-value
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
45-94 6.52e-07

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 42.36  E-value: 6.52e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 212646300  45 RLQCFLCKLTEKRVLLRPCNHLCFCEPCNDTFQKQIPlLCPICHMHVQSF 94
Cdd:pfam13920  2 DLLCVICLDRPRNVVLLPCGHLCLCEECAERLLRKKK-KCPICRQPIESV 50
RING-HC_MIP1-like cd23128
RING finger, HC subclass, found in Arabidopsis thaliana MND1-interacting protein 1 (MIP1) and ...
 45-92 2.60e-04

RING finger, HC subclass, found in Arabidopsis thaliana MND1-interacting protein 1 (MIP1) and similar proteins; This subfamily includes Arabidopsis thaliana MIP1, RING finger protein 4 (RF4) and RING finger protein 298 (RF298). MIP1 interacts with MND1, HOP2 and XRI1. RF4 and RF298 are putative E3 ubiquitin-protein ligase that may mediate E2-dependent protein ubiquitination. Members of this subfamily contain a typical C3HC4-type RING-HC finger.


Pssm-ID: 438490 [Multi-domain]  Cd Length: 55  Bit Score: 35.95  E-value: 2.60e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 212646300 45 RLQCFLCKLTEKRVLLRPCNHLCFCEPCNDTFQKQIPLLCPICHMHVQ 92
Cdd:cd23128   3 ERECVMCMEEERSVVFLPCAHQVVCSGCNDLHEKKGMRECPSCRGEIQ 50
PEX10 COG5574
RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
 40-97 3.23e-04

RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227861 [Multi-domain]  Cd Length: 271  Bit Score: 37.95  E-value: 3.23e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 212646300  40 SINEARLQCFLCKLTEKRVLLRPCNHLcFCEPC-NDTFQKQIPLLCPICHMHVQSFEIV 97
Cdd:COG5574  210 FIPLADYKCFLCLEEPEVPSCTPCGHL-FCLSClLISWTKKKYEFCPLCRAKVYPKKVI 267
 
Name Accession Description Interval E-value
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
45-94 6.52e-07

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 42.36  E-value: 6.52e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 212646300  45 RLQCFLCKLTEKRVLLRPCNHLCFCEPCNDTFQKQIPlLCPICHMHVQSF 94
Cdd:pfam13920  2 DLLCVICLDRPRNVVLLPCGHLCLCEECAERLLRKKK-KCPICRQPIESV 50
RING-HC_MIP1-like cd23128
RING finger, HC subclass, found in Arabidopsis thaliana MND1-interacting protein 1 (MIP1) and ...
 45-92 2.60e-04

RING finger, HC subclass, found in Arabidopsis thaliana MND1-interacting protein 1 (MIP1) and similar proteins; This subfamily includes Arabidopsis thaliana MIP1, RING finger protein 4 (RF4) and RING finger protein 298 (RF298). MIP1 interacts with MND1, HOP2 and XRI1. RF4 and RF298 are putative E3 ubiquitin-protein ligase that may mediate E2-dependent protein ubiquitination. Members of this subfamily contain a typical C3HC4-type RING-HC finger.


Pssm-ID: 438490 [Multi-domain]  Cd Length: 55  Bit Score: 35.95  E-value: 2.60e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 212646300 45 RLQCFLCKLTEKRVLLRPCNHLCFCEPCNDTFQKQIPLLCPICHMHVQ 92
Cdd:cd23128   3 ERECVMCMEEERSVVFLPCAHQVVCSGCNDLHEKKGMRECPSCRGEIQ 50
PEX10 COG5574
RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
 40-97 3.23e-04

RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227861 [Multi-domain]  Cd Length: 271  Bit Score: 37.95  E-value: 3.23e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 212646300  40 SINEARLQCFLCKLTEKRVLLRPCNHLcFCEPC-NDTFQKQIPLLCPICHMHVQSFEIV 97
Cdd:COG5574  210 FIPLADYKCFLCLEEPEVPSCTPCGHL-FCLSClLISWTKKKYEFCPLCRAKVYPKKVI 267
mRING-HC-C3HC5_RNF26 cd16788
Modified RING finger, HC subclass (C3HC5-type), found in RING finger protein 26 (RNF26) and ...
 43-93 1.83e-03

Modified RING finger, HC subclass (C3HC5-type), found in RING finger protein 26 (RNF26) and similar proteins; RNF26 is an E3 ubiquitin ligase that temporally regulates virus-triggered type I interferon induction by increasing the stability of Mediator of IRF3 activation, MITA, also known as STING, through K11-linked polyubiquitination of MITA after viral infection, and promoting the degradation of IRF3, another important component required for virus-triggered interferon induction. Although RNF26 substrates of ubiquitination remain unclear at present, RNF26 upregulation in gastric cancer might be implicated in carcinogenesis through dysregulation of growth regulators. RNF26 contains an N-terminal leucine zipper domain and a C-terminal modified C3HC5-type RING-HC finger, which is distinguished from typical C3HC4 RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 438442 [Multi-domain]  Cd Length: 60  Bit Score: 33.93  E-value: 1.83e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 212646300 43 EARLQCFLCKLTEKRVLLRPCNHLCFCEPCNDTFQKQIPL--LCPICHMHVQS 93
Cdd:cd16788   3 RDKKKCVICQDQSKTVLILPCRHMCLCRQCANILLQQPVYrrNCPLCRTMILQ 55
mRING-HC-C3HC5_CGRF1-like cd16649
Modified RING finger, HC subclass (C3HC5-type), found in RING finger proteins, RNF26, RNF197 ...
 48-87 1.87e-03

Modified RING finger, HC subclass (C3HC5-type), found in RING finger proteins, RNF26, RNF197 (CGRRF1), RNF156 (MGRN1), RNF157 and similar proteins; This subfamily corresponds to a group of RING finger proteins containing a modified C3HC5-type RING-HC finger, which is distinguished from typical C3HC4 RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain. Cell growth regulator with RING finger domain protein 1 (CGRRF1), also known as cell growth regulatory gene 19 protein (CGR19) or RING finger protein 197 (RNF197), functions as a novel biomarker to monitor endometrial sensitivity and response to insulin-sensitizing drugs, such as metformin, in the context of obesity. RNF26 is an E3 ubiquitin ligase that temporally regulates virus-triggered type I interferon induction by increasing the stability of Mediator of IRF3 activation, MITA, also known as STING, through K11-linked polyubiquitination after viral infection and promoting degradation of IRF3, another important component required for virus-triggered interferon induction. Mahogunin ring finger-1 (MGRN1), also known as RING finger protein 156 (RNF156), is a cytosolic E3 ubiquitin-protein ligase that inhibits signaling through the G protein-coupled melanocortin receptors-1 (MC1R), -2 (MC2R) and -4 (MC4R) via ubiquitylation-dependent and -independent processes. It suppresses chaperone-associated misfolded protein aggregation and toxicity. RNF157 is a cytoplasmic E3 ubiquitin ligase predominantly expressed in the brain. It is a homolog of the E3 ligase MGRN1. In cultured neurons, it promotes neuronal survival in an E3 ligase-dependent manner. In contrast, it supports growth and maintenance of dendrites independent of its E3 ligase activity. RNF157 interacts with and ubiquitinates the adaptor protein APBB1 (amyloid beta precursor protein-binding, family B, member 1 or Fe65), which regulates neuronal survival, but not dendritic growth downstream of RNF157. The nuclear localization of APBB1 together with its interaction partner RNA-binding protein SART3 (squamous cell carcinoma antigen recognized by T cells 3 or Tip110) is crucial to trigger apoptosis.


Pssm-ID: 438311 [Multi-domain]  Cd Length: 40  Bit Score: 33.45  E-value: 1.87e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 212646300 48 CFLCKLTEKRVLLRPCNHLCFCEPCNDTFQKQIpllCPIC 87
Cdd:cd16649   3 CVVCLENPASVLLLPCRHLCLCEVCAKGLRGKT---CPIC 39
mRING-HC-C3HC5_NEU1B cd16786
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1B (NEURL1B); ...
 47-87 2.19e-03

Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1B (NEURL1B); NEURL1B, also known as neuralized-2 (NEUR2) or neuralized-like protein 3, is a mammalian homolog of the Drosophila neuralized (D-neu) protein. It functions as an E3 ubiquitin-protein ligase that interacts with and ubiquitinates Delta. Thus, it plays a role in the endocytic pathways for Notch signaling through working cooperatively with another E3 ligase, Mind bomb-1 (Mib1), in Delta endocytosis to hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs)-positive vesicles. NEURL1B contains two neuralized homology regions (NHRs) responsible for Neural-ligand interactions and a modified C3HC5-type RING-HC finger required for ubiquitin ligase activity. The C3HC5-type RING-HC finger is distinguished from typical C3HC4-type RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 438440 [Multi-domain]  Cd Length: 57  Bit Score: 33.38  E-value: 2.19e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 212646300 47 QCFLCKLTEKRVLLRPCNHLCFCEPCNDTFQKQIPLLCPIC 87
Cdd:cd16786   4 ECTVCFDSEVDTVIYTCGHMCLCNSCGLKLKRQINACCPIC 44
mRING-HC-C3HC5_MGRN1 cd16816
Modified RING finger, HC subclass (C3HC5-type), found in mahogunin RING finger protein 1 ...
 38-89 2.84e-03

Modified RING finger, HC subclass (C3HC5-type), found in mahogunin RING finger protein 1 (MGRN1) and similar proteins; MGRN1, also known as RING finger protein 156 (RNF156), is a cytosolic E3 ubiquitin-protein ligase that inhibits signaling through the G protein-coupled melanocortin receptors-1 (MC1R), -2 (MC2R) and -4 (MC4R) via ubiquitylation-dependent and -independent processes. It suppresses chaperone-associated misfolded protein aggregation and toxicity. MGRN1 interacts with cytosolic prion proteins (PrPs) that are linked with neurodegeneration. It also interacts with expanded polyglutamine proteins, and suppresses misfolded polyglutamine aggregation and cytotoxicity. Moreover, MGRN1 inhibits melanocortin receptor signaling by competition with Galphas, suggesting a novel pathway for melanocortin signaling from the cell surface to the nucleus. Furthermore, MGRN1 interacts with and ubiquitylates TSG101, a key component of the endosomal sorting complex required for transport (ESCRT)-I, and regulates endosomal trafficking. A null mutation in the gene encoding MGRN1 causes spongiform neurodegeneration, suggesting a link between dysregulation of endosomal trafficking and spongiform neurodegeneration. MGRN1 contains a modified C3HC5-type RING-HC finger, a conserved PSAP motif necessary for interaction between MGRN1 and TSG101. In addition, MGRN1 harbors a functionally uncharacterized region, as known as the domain associated with RING2 (DAR2), N-terminal to the RING finger. The C3HC5-type RING-HC finger is distinguished from typical C3HC4 RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 438465  Cd Length: 58  Bit Score: 33.11  E-value: 2.84e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 212646300 38 EDSINEARLQCFLCKLTEKRVLLRPCNHLCFCEPCNDTFQKQIPlLCPICHM 89
Cdd:cd16816   1 DDENSDNSNECVVCLSDLRDTLILPCRHLCLCNSCADTLRYQAN-NCPICRL 51
mRING-HC-C3HC5_RNF157 cd16817
Modified RING finger, HC subclass (C3HC5-type), found in RING finger protein 157 (RNF157) and ...
 47-89 7.01e-03

Modified RING finger, HC subclass (C3HC5-type), found in RING finger protein 157 (RNF157) and similar proteins; RNF157 is a cytoplasmic E3 ubiquitin ligase predominantly expressed in brain. It is a homolog of the E3 ligase mahogunin ring finger-1 (MGRN1). In cultured neurons, it promotes neuronal survival in an E3 ligase-dependent manner. In contrast, it supports growth and maintenance of dendrites independent of its E3 ligase activity. RNF157 interacts with and ubiquitinates the adaptor protein APBB1 (amyloid beta precursor protein-binding, family B, member 1 or Fe65), which regulates neuronal survival, but not dendritic growth downstream of RNF157. The nuclear localization of APBB1 together with its interaction partner RNA-binding protein SART3 (squamous cell carcinoma antigen recognized by T cells 3 or Tip110) is crucial to trigger apoptosis. RNF157 contains a modified C3HC5-type RING-HC finger, and a functionally uncharacterized region, known as domain associated with RING2 (DAR2), N-terminal to the RING finger. The C3HC5-type RING-HC finger is distinguished from typical C3HC4 RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 438466 [Multi-domain]  Cd Length: 60  Bit Score: 32.37  E-value: 7.01e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 212646300 47 QCFLCKLTEKRVLLRPCNHLCFCEPCNDTFQKQIPlLCPICHM 89
Cdd:cd16817   6 ECVVCLSDVRDTLILPCRHLCLCNACADTLRYQAN-NCPICRL 47
mRING-HC-C3HC5_MGRN1-like cd16789
Modified RING finger, HC subclass (C3HC5-type), found in mahogunin RING finger protein 1 ...
 48-87 9.24e-03

Modified RING finger, HC subclass (C3HC5-type), found in mahogunin RING finger protein 1 (MGRN1), RING finger protein 157 (RNF157) and similar proteins; MGRN1, also known as RING finger protein 156 (RNF156), is a cytosolic E3 ubiquitin-protein ligase that inhibits signaling through the G protein-coupled melanocortin receptors-1 (MC1R), -2 (MC2R) and -4 (MC4R) via ubiquitylation-dependent and -independent processes. It suppresses chaperone-associated misfolded protein aggregation and toxicity. MGRN1 interacts with cytosolic prion proteins (PrPs) that are linked with neurodegeneration. It also interacts with expanded polyglutamine proteins, and suppresses misfolded polyglutamine aggregation and cytotoxicity. Moreover, MGRN1 inhibits melanocortin receptor signaling by competition with Galphas, suggesting a novel pathway for melanocortin signaling from the cell surface to the nucleus. MGRN1 also interacts with and ubiquitylates TSG101, a key component of the endosomal sorting complex required for transport (ESCRT)-I, and regulates endosomal trafficking. A null mutation in the gene encoding MGRN1 causes spongiform neurodegeneration, suggesting a link between dysregulation of endosomal trafficking and spongiform neurodegeneration. RNF157 is a cytoplasmic E3 ubiquitin ligase predominantly expressed in the brain. It is a homolog of the E3 ligase mahogunin ring finger-1 (MGRN1). In cultured neurons, it promotes neuronal survival in an E3 ligase-dependent manner. In contrast, it supports growth and maintenance of dendrites independent of its E3 ligase activity. RNF157 interacts with and ubiquitinates the adaptor protein APBB1 (amyloid beta precursor protein-binding, family B, member 1 or Fe65), which regulates neuronal survival, but not dendritic growth downstream of RNF157. The nuclear localization of APBB1 together with its interaction partner RNA-binding protein SART3 (squamous cell carcinoma antigen recognized by T cells 3 or Tip110) is crucial to trigger apoptosis. Both MGRN1 and RNF157 contain a modified C3HC5-type RING-HC finger, and a functionally uncharacterized region, known as domain associated with RING2 (DAR2), N-terminal to the RING finger. The C3HC5-type RING-HC finger is distinguished from typical C3HC4 RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 438443 [Multi-domain]  Cd Length: 42  Bit Score: 31.50  E-value: 9.24e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 212646300 48 CFLCKLTEKRVLLRPCNHLCFCEPCNDTFQKQIPlLCPIC 87
Cdd:cd16789   3 CVICLSDPRDTAVLPCRHLCLCSDCAEVLRYQSN-KCPIC 41
 
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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