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Conserved domains on  [gi|755549545|ref|XP_011243591|]
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rING finger protein 212B isoform X1 [Mus musculus]

Protein Classification

bZIP transcription factor( domain architecture ID 11616590)

basic leucine zipper (bZIP) transcription factor binds to the promoter regions of genes to control their expression; similar to Crassostrea hongkongensis NFIL3 (nuclear factor interleukin 3-regulated) that mediates a variety of immune responses

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RING-HC_RNF212B cd16747
RING finger, HC subclass, found in RING finger protein 212B (RNF212B) and similar proteins; ...
4-40 7.54e-19

RING finger, HC subclass, found in RING finger protein 212B (RNF212B) and similar proteins; RNF212B is an uncharacterized protein with high sequence similarity with RNF212, a dosage-sensitive regulator of crossing-over during mammalian meiosis. RNF212B contains an N-terminal C3HC4-type RING-HC finger.


:

Pssm-ID: 438405  Cd Length: 37  Bit Score: 77.84  E-value: 7.54e-19
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 755549545   4 FHCNQCFRKDGAHFFVTSCGHIFCKKCMTLEKCAVCG 40
Cdd:cd16747    1 FHCNKCFRRDGASFFITSCGHIFCEKCIKAEKCTVCG 37
bZIP super family cl21462
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
93-124 4.73e-03

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


The actual alignment was detected with superfamily member cd14810:

Pssm-ID: 473870  Cd Length: 52  Bit Score: 34.54  E-value: 4.73e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 755549545  93 KDRITKLEAAVKEAQEMAASQNKELSALRKEN 124
Cdd:cd14810   20 KEYITQLEEQVADRDAEIEQLRAELRALRNEN 51
 
Name Accession Description Interval E-value
RING-HC_RNF212B cd16747
RING finger, HC subclass, found in RING finger protein 212B (RNF212B) and similar proteins; ...
4-40 7.54e-19

RING finger, HC subclass, found in RING finger protein 212B (RNF212B) and similar proteins; RNF212B is an uncharacterized protein with high sequence similarity with RNF212, a dosage-sensitive regulator of crossing-over during mammalian meiosis. RNF212B contains an N-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438405  Cd Length: 37  Bit Score: 77.84  E-value: 7.54e-19
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 755549545   4 FHCNQCFRKDGAHFFVTSCGHIFCKKCMTLEKCAVCG 40
Cdd:cd16747    1 FHCNKCFRRDGASFFITSCGHIFCEKCIKAEKCTVCG 37
zf-RING_5 pfam14634
zinc-RING finger domain;
5-40 2.26e-07

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 46.65  E-value: 2.26e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 755549545    5 HCNQCFRK--DGAHFFVTSCGHIFCKKCMTLE----KCAVCG 40
Cdd:pfam14634   1 HCNKCFKElsKTRPFYLTSCGHIFCEECLTRLlqerQCPICK 42
bZIP_u1 cd14810
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
93-124 4.73e-03

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; uncharacterized subfamily; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269872  Cd Length: 52  Bit Score: 34.54  E-value: 4.73e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 755549545  93 KDRITKLEAAVKEAQEMAASQNKELSALRKEN 124
Cdd:cd14810   20 KEYITQLEEQVADRDAEIEQLRAELRALRNEN 51
 
Name Accession Description Interval E-value
RING-HC_RNF212B cd16747
RING finger, HC subclass, found in RING finger protein 212B (RNF212B) and similar proteins; ...
4-40 7.54e-19

RING finger, HC subclass, found in RING finger protein 212B (RNF212B) and similar proteins; RNF212B is an uncharacterized protein with high sequence similarity with RNF212, a dosage-sensitive regulator of crossing-over during mammalian meiosis. RNF212B contains an N-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438405  Cd Length: 37  Bit Score: 77.84  E-value: 7.54e-19
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 755549545   4 FHCNQCFRKDGAHFFVTSCGHIFCKKCMTLEKCAVCG 40
Cdd:cd16747    1 FHCNKCFRRDGASFFITSCGHIFCEKCIKAEKCTVCG 37
RING-HC_RNF212-like cd16560
RING finger, HC subclass, found in RING finger proteins RNF212, RNF212B and similar proteins; ...
4-40 7.21e-13

RING finger, HC subclass, found in RING finger proteins RNF212, RNF212B and similar proteins; This subfamily includes RING finger protein RNF212, RNF212B, and their homologs. RNF212 is a dosage-sensitive regulator of crossing-over during mammalian meiosis. It plays a central role in designating crossover sites and coupling chromosome synapsis to the formation of crossover-specific recombination complexes. It also functions as an E3 ligase for small ubiquitin-related modifier (SUMO) modification. RNF212B shows high sequence similarity with RNF212, but its biological function remains unclear. Members of this subfamily contain an N-terminal C3HC4-type RING-HC finger. Also included are two homologs of RNF212, meiotic procrossover factors Zip3 and ZHP-3, which have been identified in Saccharomyces cerevisiae and Caenorhabditis elegans, respectively. Budding yeast Zip3 is a small ubiquitin-related modifier (SUMO) E3 ligase implicated in the SUMO pathway of post-translational modification. It sumoylates chromosome axis proteins, thus promoting synaptonemal complex polymerization. It also acts as an Smt3 E3 ligase. Zip3 includes a SUMO Interacting Motif (SIM) and a modified C3HCHC2-type RING-HC finger that are important for Zip3 in vitro E3 ligase activity and necessary for SC polymerization and correct sporulation. ZHP-3 acts at crossovers to couple meiotic recombination with synaptonemal complex disassembly and chiasma formation in Caenorhabditis elegans. It possesses a C3HC4-type RING-HC finger.


Pssm-ID: 438222  Cd Length: 42  Bit Score: 61.79  E-value: 7.21e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 755549545   4 FHCNQCFRKDG--AHFFVTSCGHIFCKKCMTL---EKCAVCG 40
Cdd:cd16560    1 VHCNTCFQLPGdtSKFFLTSCGHIYCDACVGKgkrNKCKICG 42
zf-RING_5 pfam14634
zinc-RING finger domain;
5-40 2.26e-07

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 46.65  E-value: 2.26e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 755549545    5 HCNQCFRK--DGAHFFVTSCGHIFCKKCMTLE----KCAVCG 40
Cdd:pfam14634   1 HCNKCFKElsKTRPFYLTSCGHIFCEECLTRLlqerQCPICK 42
RING-HC_RNF212 cd16746
RING finger, HC subclass, found in RING finger protein 212 (RNF212) and similar proteins; ...
3-44 3.19e-06

RING finger, HC subclass, found in RING finger protein 212 (RNF212) and similar proteins; RNF212 is a dosage-sensitive regulator of crossing-over during mammalian meiosis. It plays a central role in designating crossover sites and coupling chromosome synapsis to the formation of crossover-specific recombination complexes. It also functions as an E3 ligase for SUMO modification. RNF212 contains an N-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438404  Cd Length: 48  Bit Score: 43.58  E-value: 3.19e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 755549545   3 WFHCNQCF---RKDGAHFFVTSCGHIFCKKCM---TLEKCAVCGNLCK 44
Cdd:cd16746    1 RVFCNFCFqqpRPNCPSFILTNCGHVVCEACLqkgKKNECLVCKAPCR 48
RING-HC_ITT1-like cd23134
RING finger, HC subclass, found in Saccharomyces cerevisiae translation termination inhibitor ...
4-32 7.54e-04

RING finger, HC subclass, found in Saccharomyces cerevisiae translation termination inhibitor protein ITT1 and similar proteins; ITT1 is a protein that modulates the efficiency of translation termination, resulting in the readthrough of all three types of nonsense codons UAA, UAG and UGA. ITT1 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438496  Cd Length: 60  Bit Score: 36.91  E-value: 7.54e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 755549545   4 FHCNQCFR-KDGAHFFVTSCGHIFCKKCMT 32
Cdd:cd23134    5 YHCGICFEeKKGSDFIKLPCGHVFCRECLQ 34
RING-HC_RBR_RNF14 cd16628
RING finger, HC subclass, found in RING finger protein 14 (RNF14) and similar proteins; RNF14, ...
2-32 3.92e-03

RING finger, HC subclass, found in RING finger protein 14 (RNF14) and similar proteins; RNF14, also known as androgen receptor-associated protein 54 (ARA54), HFB30, or Triad2 protein, is an RBR-type E3 ubiquitin-protein ligase that is highly expressed in the testis and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3). Its differential localization may play an important role in testicular development and spermatogenesis in humans. RNF14 functions as a transcriptional regulator of mitochondrial and immune function in muscle. It is a ligand-dependent androgen receptor (AR) co-activator and may also may participate in enhancing cell cycle progression and cell proliferation via induction of cyclin D1. Moreover, RNF14 is crucial for colon cancer cell survival. It acts as a new enhancer of the Wnt-dependent transcriptional outputs that acts at the level of the T-cell factor/lymphoid enhancer factor (TCF/LEF)-beta-catenin complex. RNF14 contains an N-terminal RWD domain and a C-terminal RBR domain. The RBR domain 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 corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) 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 function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a C3HC4-type RING-HC finger required for RBR-mediated ubiquitination.


Pssm-ID: 438290  Cd Length: 59  Bit Score: 34.98  E-value: 3.92e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 755549545   2 DWFHCNQCF-RKDGAHFF-VTSCGHIFCKKCMT 32
Cdd:cd16628    4 KIFTCNICFlDKLGSECMyFKDCGHVYCKECLK 36
bZIP_u1 cd14810
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
93-124 4.73e-03

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; uncharacterized subfamily; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269872  Cd Length: 52  Bit Score: 34.54  E-value: 4.73e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 755549545  93 KDRITKLEAAVKEAQEMAASQNKELSALRKEN 124
Cdd:cd14810   20 KEYITQLEEQVADRDAEIEQLRAELRALRNEN 51
 
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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