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Conserved domains on  [gi|1496472645|ref|NP_001353848|]
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probable E3 SUMO-protein ligase RNF212 isoform e [Homo sapiens]

Protein Classification

RING finger protein; RING finger protein 130( domain architecture ID 11616577)

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| RING finger protein 130 (RNF130) acts as an E3 ubiquitin-protein ligase that may have a role during the programmed cell death of hematopoietic cells

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RING-HC_RNF212 cd16746
RING finger, HC subclass, found in RING finger protein 212 (RNF212) and similar proteins; ...
 4-50 7.79e-24

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: 90.96  E-value: 7.79e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1496472645   4 WVFCNRCFQPPHR-TSCFSLTNCGHVYCDACLGKGKKNECLICKAPCR 50
Cdd:cd16746     1 RVFCNFCFQQPRPnCPSFILTNCGHVVCEACLQKGKKNECLVCKAPCR 48
 
Name Accession Description Interval E-value
RING-HC_RNF212 cd16746
RING finger, HC subclass, found in RING finger protein 212 (RNF212) and similar proteins; ...
 4-50 7.79e-24

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: 90.96  E-value: 7.79e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1496472645   4 WVFCNRCFQPPHR-TSCFSLTNCGHVYCDACLGKGKKNECLICKAPCR 50
Cdd:cd16746     1 RVFCNFCFQQPRPnCPSFILTNCGHVVCEACLQKGKKNECLVCKAPCR 48
zf-RING_5 pfam14634
zinc-RING finger domain;
6-46 3.21e-09

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 51.66  E-value: 3.21e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1496472645   6 FCNRCFQPPHRTSCFSLTNCGHVYCDACLGKGKKN-ECLICK 46
Cdd:pfam14634   1 HCNKCFKELSKTRPFYLTSCGHIFCEECLTRLLQErQCPICK 42
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
10-62 8.81e-03

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 37.31  E-value: 8.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1496472645  10 CFQPPHRTSCFSLTNCGHVYCDACLGKG----KKNECLICKAPCRTVLLSKHTDADI 62
Cdd:COG5236    64 CQICAGSTTYSARYPCGHQICHACAVRLralyMQKGCPLCRTETEAVVFTASSPADI 120
 
Name Accession Description Interval E-value
RING-HC_RNF212 cd16746
RING finger, HC subclass, found in RING finger protein 212 (RNF212) and similar proteins; ...
 4-50 7.79e-24

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: 90.96  E-value: 7.79e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1496472645   4 WVFCNRCFQPPHR-TSCFSLTNCGHVYCDACLGKGKKNECLICKAPCR 50
Cdd:cd16746     1 RVFCNFCFQQPRPnCPSFILTNCGHVVCEACLQKGKKNECLVCKAPCR 48
RING-HC_RNF212-like cd16560
RING finger, HC subclass, found in RING finger proteins RNF212, RNF212B and similar proteins; ...
 5-46 2.65e-19

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: 78.74  E-value: 2.65e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1496472645   5 VFCNRCFQPPHRTSCFSLTNCGHVYCDACLGKGKKNECLICK 46
Cdd:cd16560     1 VHCNTCFQLPGDTSKFFLTSCGHIYCDACVGKGKRNKCKICG 42
zf-RING_5 pfam14634
zinc-RING finger domain;
6-46 3.21e-09

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 51.66  E-value: 3.21e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1496472645   6 FCNRCFQPPHRTSCFSLTNCGHVYCDACLGKGKKN-ECLICK 46
Cdd:pfam14634   1 HCNKCFKELSKTRPFYLTSCGHIFCEECLTRLLQErQCPICK 42
RING-HC_RNF212B cd16747
RING finger, HC subclass, found in RING finger protein 212B (RNF212B) and similar proteins; ...
 7-46 1.49e-05

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: 41.24  E-value: 1.49e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1496472645   7 CNRCFQppHRTSCFSLTNCGHVYCDACLgkgKKNECLICK 46
Cdd:cd16747     3 CNKCFR--RDGASFFITSCGHIFCEKCI---KAEKCTVCG 37
RING-HC_BARD1 cd16496
RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar ...
 7-78 4.37e-04

RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar proteins; BARD-1 is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an C3HC4-type RING-HC finger that binds BRCA1 at its N-terminus and three tandem ankyrin repeats and tandem BRCT repeat domains at its C-terminus. The BRCT repeats bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage.


Pssm-ID: 438159 [Multi-domain]  Cd Length: 86  Bit Score: 38.47  E-value: 4.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1496472645   7 CNRC---FQPPhrtscFSLTNCGHVYCDACLGKGKKNECLICKAPCRTvllskhTDADIQAFFMSIDSLCKKYSR 78
Cdd:cd16496    18 CSRCasiLKEP-----VTLGGCEHVFCRSCVGDRLGNGCPVCDTPAWA------RDLQINRQLDSMVQLCRKLRN 81
RING-HC_RBR_RNF14 cd16628
RING finger, HC subclass, found in RING finger protein 14 (RNF14) and similar proteins; RNF14, ...
 7-48 3.98e-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: 3.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1496472645   7 CNRCFQPPHRTSCFSLTNCGHVYCDACLGK--------GKKNeCLICKAP 48
Cdd:cd16628     8 CNICFLDKLGSECMYFKDCGHVYCKECLKEyfevqirdGNVT-SLNCPEP 56
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
10-62 8.81e-03

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 37.31  E-value: 8.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1496472645  10 CFQPPHRTSCFSLTNCGHVYCDACLGKG----KKNECLICKAPCRTVLLSKHTDADI 62
Cdd:COG5236    64 CQICAGSTTYSARYPCGHQICHACAVRLralyMQKGCPLCRTETEAVVFTASSPADI 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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