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Conserved domains on  [gi|254939526|ref|NP_067335|]
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E3 ubiquitin-protein ligase NEURL1 isoform 1 [Mus musculus]

Protein Classification

NEUZ and Neuralized domain-containing protein( domain architecture ID 12216919)

protein containing domains NEUZ, Neuralized, and mRING-HC-C3HC5_NEU1A

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Neuralized pfam07177
Neuralized; This family contains a conserved region approximately 60 residues long within ...
296-447 4.51e-53

Neuralized; This family contains a conserved region approximately 60 residues long within eukaryotic neuralized and neuralized-like proteins. Neuralized belongs to a group of ubiquitin ligases and is required in a subset of Notch pathway-mediated cell fate decisions during development of the Drosophila nervous system. Some family members contain multiple copies of this region.


:

Pssm-ID: 462112 [Multi-domain]  Cd Length: 149  Bit Score: 177.73  E-value: 4.51e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254939526  296 FHALRaGAHVRILDEQTVARLeHGRDERALVFTSRPVRVAETIFIKVTRSGGGRAGALSFGVTTCDPGTLRPADLPFSPE 375
Cdd:pfam07177   1 FHPVH-GKNVRLSNDGRTARR-TNSFNNGLVFSSRPLRPGELFEVRIDKLVDKWSGSLRFGVTSCDPATLRPKALPDLAT 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254939526  376 ALvdRKEFWAVCRVPGPLHSGDILGLVVNADGELHLSHNGAAAG-MQLCVDASQPLWMLFSLHGAITQVRILG 447
Cdd:pfam07177  79 DL--RPGYWVVALSGSYLQEGDRLGFWVTSDGELHFSVNGEDQGvALSGVPDSQPLWAVFDLYGQTTQVSILG 149
NEUZ smart00588
domain in neuralized proteins;
61-183 1.03e-52

domain in neuralized proteins;


:

Pssm-ID: 128856  Cd Length: 123  Bit Score: 175.58  E-value: 1.03e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254939526    61 TPLLFHpHTKGSQILMDLSHKAVKRQAS-FCNAITFSNRPVLIYEQVRLKITKKQCCWSGALRLGFTSKDPSRIHPDSLP 139
Cdd:smart00588   1 GPLRFH-HRHGSNIRLSDSGRVARRSASdFCNALVFSARPLRINELFEVKIEKVVRKWSGALRFGVTTCDPATLRPASLP 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 254939526   140 KYACPDLVSQSGFWAKALPEEFANEGNIIAFWVDKKGRVFYRIN 183
Cdd:smart00588  80 TNACPDLVDMSGFWAKALGEGLAEQGGILGLDVLAEGEVVGVIN 123
mRING-HC-C3HC5_NEU1A cd16785
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1A (NEURL1A) ...
515-573 9.30e-38

Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1A (NEURL1A) and similar proteins; NEURL1A, also known as NEURL1, NEU, neuralized 1, or RING finger protein 67 (RNF67), is a mammalian homolog of the Drosophila neuralized (D-neu) protein. It functions as an E3 ubiquitin-protein ligase that directly interacts with and monoubiquitinates cytoplasmic polyadenylation element-binding protein 3 (CPEB3), an RNA binding protein and a translational regulator of local protein synthesis, which facilitates hippocampal plasticity and hippocampal-dependent memory storage. It also acts as a potential tumor suppressor that causes apoptosis and downregulates Notch target genes in the medulloblastoma. NEURL1A 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: 438439 [Multi-domain]  Cd Length: 59  Bit Score: 133.18  E-value: 9.30e-38
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 254939526 515 GQWSDECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKALHACCPICRRPIKDIIKTYRS 573
Cdd:cd16785    1 GSWSDECTICYENAVDTVIYTCGHMCLCYACGLRLKKMLNACCPICRRAIKDIIKTYRS 59
 
Name Accession Description Interval E-value
Neuralized pfam07177
Neuralized; This family contains a conserved region approximately 60 residues long within ...
296-447 4.51e-53

Neuralized; This family contains a conserved region approximately 60 residues long within eukaryotic neuralized and neuralized-like proteins. Neuralized belongs to a group of ubiquitin ligases and is required in a subset of Notch pathway-mediated cell fate decisions during development of the Drosophila nervous system. Some family members contain multiple copies of this region.


Pssm-ID: 462112 [Multi-domain]  Cd Length: 149  Bit Score: 177.73  E-value: 4.51e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254939526  296 FHALRaGAHVRILDEQTVARLeHGRDERALVFTSRPVRVAETIFIKVTRSGGGRAGALSFGVTTCDPGTLRPADLPFSPE 375
Cdd:pfam07177   1 FHPVH-GKNVRLSNDGRTARR-TNSFNNGLVFSSRPLRPGELFEVRIDKLVDKWSGSLRFGVTSCDPATLRPKALPDLAT 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254939526  376 ALvdRKEFWAVCRVPGPLHSGDILGLVVNADGELHLSHNGAAAG-MQLCVDASQPLWMLFSLHGAITQVRILG 447
Cdd:pfam07177  79 DL--RPGYWVVALSGSYLQEGDRLGFWVTSDGELHFSVNGEDQGvALSGVPDSQPLWAVFDLYGQTTQVSILG 149
NEUZ smart00588
domain in neuralized proteins;
61-183 1.03e-52

domain in neuralized proteins;


Pssm-ID: 128856  Cd Length: 123  Bit Score: 175.58  E-value: 1.03e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254939526    61 TPLLFHpHTKGSQILMDLSHKAVKRQAS-FCNAITFSNRPVLIYEQVRLKITKKQCCWSGALRLGFTSKDPSRIHPDSLP 139
Cdd:smart00588   1 GPLRFH-HRHGSNIRLSDSGRVARRSASdFCNALVFSARPLRINELFEVKIEKVVRKWSGALRFGVTTCDPATLRPASLP 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 254939526   140 KYACPDLVSQSGFWAKALPEEFANEGNIIAFWVDKKGRVFYRIN 183
Cdd:smart00588  80 TNACPDLVDMSGFWAKALGEGLAEQGGILGLDVLAEGEVVGVIN 123
Neuralized pfam07177
Neuralized; This family contains a conserved region approximately 60 residues long within ...
65-217 1.55e-46

Neuralized; This family contains a conserved region approximately 60 residues long within eukaryotic neuralized and neuralized-like proteins. Neuralized belongs to a group of ubiquitin ligases and is required in a subset of Notch pathway-mediated cell fate decisions during development of the Drosophila nervous system. Some family members contain multiple copies of this region.


Pssm-ID: 462112 [Multi-domain]  Cd Length: 149  Bit Score: 160.01  E-value: 1.55e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254939526   65 FHpHTKGSQILMDLSHKAVKRQASFCNAITFSNRPVLIYEQVRLKITKKQCCWSGALRLGFTSKDPSRIHPDSLPkyACP 144
Cdd:pfam07177   1 FH-PVHGKNVRLSNDGRTARRTNSFNNGLVFSSRPLRPGELFEVRIDKLVDKWSGSLRFGVTSCDPATLRPKALP--DLA 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254939526  145 DLVsQSGFWAKALPEEFANEGNIIAFWVDKKGRVFYRINESAAMLFFSGVRTVDPLWALVDVYGLTRGVQLLD 217
Cdd:pfam07177  78 TDL-RPGYWVVALSGSYLQEGDRLGFWVTSDGELHFSVNGEDQGVALSGVPDSQPLWAVFDLYGQTTQVSILG 149
NEUZ smart00588
domain in neuralized proteins;
292-414 5.27e-46

domain in neuralized proteins;


Pssm-ID: 128856  Cd Length: 123  Bit Score: 157.86  E-value: 5.27e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254939526   292 GDLRFHaLRAGAHVRILDEQTVARLEHGRDERALVFTSRPVRVAETIFIKVTRSGGGRAGALSFGVTTCDPGTLRPADLP 371
Cdd:smart00588   1 GPLRFH-HRHGSNIRLSDSGRVARRSASDFCNALVFSARPLRINELFEVKIEKVVRKWSGALRFGVTTCDPATLRPASLP 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 254939526   372 -FSPEALVDRKEFWAVCRVPGPLHSGDILGLVVNADGELHLSHN 414
Cdd:smart00588  80 tNACPDLVDMSGFWAKALGEGLAEQGGILGLDVLAEGEVVGVIN 123
mRING-HC-C3HC5_NEU1A cd16785
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1A (NEURL1A) ...
515-573 9.30e-38

Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1A (NEURL1A) and similar proteins; NEURL1A, also known as NEURL1, NEU, neuralized 1, or RING finger protein 67 (RNF67), is a mammalian homolog of the Drosophila neuralized (D-neu) protein. It functions as an E3 ubiquitin-protein ligase that directly interacts with and monoubiquitinates cytoplasmic polyadenylation element-binding protein 3 (CPEB3), an RNA binding protein and a translational regulator of local protein synthesis, which facilitates hippocampal plasticity and hippocampal-dependent memory storage. It also acts as a potential tumor suppressor that causes apoptosis and downregulates Notch target genes in the medulloblastoma. NEURL1A 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: 438439 [Multi-domain]  Cd Length: 59  Bit Score: 133.18  E-value: 9.30e-38
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 254939526 515 GQWSDECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKALHACCPICRRPIKDIIKTYRS 573
Cdd:cd16785    1 GSWSDECTICYENAVDTVIYTCGHMCLCYACGLRLKKMLNACCPICRRAIKDIIKTYRS 59
SPRY_NHR_like cd12887
SPRY domain in neuralized homology repeat; This family contains the neuralized homology repeat ...
295-446 5.81e-15

SPRY domain in neuralized homology repeat; This family contains the neuralized homology repeat 1 (NHR1) domain similar to the SPRY domain (known to mediate specific protein-protein interactions) at the C-terminus of a conserved region within eukaryotic neuralized and neuralized-like proteins. In Drosophila, the neuralized protein (Neur) belongs to a group of ubiquitin ligases and is required in a subset of Notch pathway-mediated cell fate decisions during development of the nervous system. Neur binds to the Notch receptor ligand Delta through its first NHR1 domain and mediates its ubiquitination for endocytosis. Multiple copies of this region are found in some members of the family.


Pssm-ID: 293945  Cd Length: 161  Bit Score: 72.54  E-value: 5.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254939526 295 RFHALRaGAHVRILDEQTVARLEHGRDERALVFTSRPVRVAETIFIKVTRSGGGRAGALSFGVTTCDPGTLrpaDLPFSP 374
Cdd:cd12887    1 RFHENH-GKNIRLSNDGRTATRVKASFNNGVVFSSRPLRPGELFEVRIDKLVDRWSGSLEIGVTTLNPETL---DLPPSA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254939526 375 EALvdRKEFW--AVCRVP----------GP----LHSGDILGLVVNADGELHLSHNGAAAGMqLCVDASQPLWMLFSLHG 438
Cdd:cd12887   77 TDL--KSGTWilSGSSVFkngnkirenyGPdldrLRVGDRVGVMRTSDGTLHFYVNGEDQGV-AASNVPQPVYAVVDLYG 153

                 ....*...
gi 254939526 439 AITQVRIL 446
Cdd:cd12887  154 QCEQVSIV 161
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
519-567 1.04e-13

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 65.47  E-value: 1.04e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 254939526  519 DECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKaLHACCPICRRPIKDI 567
Cdd:pfam13920   3 LLCVICLDRPRNVVLLPCGHLCLCEECAERLLR-KKKKCPICRQPIESV 50
SPRY_NHR_like cd12887
SPRY domain in neuralized homology repeat; This family contains the neuralized homology repeat ...
65-213 1.61e-11

SPRY domain in neuralized homology repeat; This family contains the neuralized homology repeat 1 (NHR1) domain similar to the SPRY domain (known to mediate specific protein-protein interactions) at the C-terminus of a conserved region within eukaryotic neuralized and neuralized-like proteins. In Drosophila, the neuralized protein (Neur) belongs to a group of ubiquitin ligases and is required in a subset of Notch pathway-mediated cell fate decisions during development of the nervous system. Neur binds to the Notch receptor ligand Delta through its first NHR1 domain and mediates its ubiquitination for endocytosis. Multiple copies of this region are found in some members of the family.


Pssm-ID: 293945  Cd Length: 161  Bit Score: 62.53  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254939526  65 FHPHTkGSQILMDLSHKAVKRQA-SFCNAITFSNRPVLIYEQVRLKITKKQCCWSGALRLGFTSKDPSRIH-PDSLP--- 139
Cdd:cd12887    2 FHENH-GKNIRLSNDGRTATRVKaSFNNGVVFSSRPLRPGELFEVRIDKLVDRWSGSLEIGVTTLNPETLDlPPSATdlk 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254939526 140 ---KYACPDLVSQSGfwaKALPEEFA------NEGNIIAFWVDKKGRVFYRIN----ESAAmlffSGVRTvdPLWALVDV 206
Cdd:cd12887   81 sgtWILSGSSVFKNG---NKIRENYGpdldrlRVGDRVGVMRTSDGTLHFYVNgedqGVAA----SNVPQ--PVYAVVDL 151

                 ....*..
gi 254939526 207 YGLTRGV 213
Cdd:cd12887  152 YGQCEQV 158
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
521-560 3.56e-05

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 40.96  E-value: 3.56e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 254939526   521 CTICYEH-AVDTVIYTCGHMcLCYSCGLRLKKALHACCPIC 560
Cdd:smart00184   1 CPICLEEyLKDPVILPCGHT-FCRSCIRKWLESGNNTCPIC 40
PEX10 COG5574
RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
510-568 1.43e-03

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


Pssm-ID: 227861 [Multi-domain]  Cd Length: 271  Bit Score: 40.65  E-value: 1.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254939526 510 VTPGLGQWSDECTICYEHAVDTVIYTCGHMcLCYSC---GLRLKKALHacCPICRR---PIKDII 568
Cdd:COG5574  207 GLPFIPLADYKCFLCLEEPEVPSCTPCGHL-FCLSClliSWTKKKYEF--CPLCRAkvyPKKVII 268
 
Name Accession Description Interval E-value
Neuralized pfam07177
Neuralized; This family contains a conserved region approximately 60 residues long within ...
296-447 4.51e-53

Neuralized; This family contains a conserved region approximately 60 residues long within eukaryotic neuralized and neuralized-like proteins. Neuralized belongs to a group of ubiquitin ligases and is required in a subset of Notch pathway-mediated cell fate decisions during development of the Drosophila nervous system. Some family members contain multiple copies of this region.


Pssm-ID: 462112 [Multi-domain]  Cd Length: 149  Bit Score: 177.73  E-value: 4.51e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254939526  296 FHALRaGAHVRILDEQTVARLeHGRDERALVFTSRPVRVAETIFIKVTRSGGGRAGALSFGVTTCDPGTLRPADLPFSPE 375
Cdd:pfam07177   1 FHPVH-GKNVRLSNDGRTARR-TNSFNNGLVFSSRPLRPGELFEVRIDKLVDKWSGSLRFGVTSCDPATLRPKALPDLAT 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254939526  376 ALvdRKEFWAVCRVPGPLHSGDILGLVVNADGELHLSHNGAAAG-MQLCVDASQPLWMLFSLHGAITQVRILG 447
Cdd:pfam07177  79 DL--RPGYWVVALSGSYLQEGDRLGFWVTSDGELHFSVNGEDQGvALSGVPDSQPLWAVFDLYGQTTQVSILG 149
NEUZ smart00588
domain in neuralized proteins;
61-183 1.03e-52

domain in neuralized proteins;


Pssm-ID: 128856  Cd Length: 123  Bit Score: 175.58  E-value: 1.03e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254939526    61 TPLLFHpHTKGSQILMDLSHKAVKRQAS-FCNAITFSNRPVLIYEQVRLKITKKQCCWSGALRLGFTSKDPSRIHPDSLP 139
Cdd:smart00588   1 GPLRFH-HRHGSNIRLSDSGRVARRSASdFCNALVFSARPLRINELFEVKIEKVVRKWSGALRFGVTTCDPATLRPASLP 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 254939526   140 KYACPDLVSQSGFWAKALPEEFANEGNIIAFWVDKKGRVFYRIN 183
Cdd:smart00588  80 TNACPDLVDMSGFWAKALGEGLAEQGGILGLDVLAEGEVVGVIN 123
Neuralized pfam07177
Neuralized; This family contains a conserved region approximately 60 residues long within ...
65-217 1.55e-46

Neuralized; This family contains a conserved region approximately 60 residues long within eukaryotic neuralized and neuralized-like proteins. Neuralized belongs to a group of ubiquitin ligases and is required in a subset of Notch pathway-mediated cell fate decisions during development of the Drosophila nervous system. Some family members contain multiple copies of this region.


Pssm-ID: 462112 [Multi-domain]  Cd Length: 149  Bit Score: 160.01  E-value: 1.55e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254939526   65 FHpHTKGSQILMDLSHKAVKRQASFCNAITFSNRPVLIYEQVRLKITKKQCCWSGALRLGFTSKDPSRIHPDSLPkyACP 144
Cdd:pfam07177   1 FH-PVHGKNVRLSNDGRTARRTNSFNNGLVFSSRPLRPGELFEVRIDKLVDKWSGSLRFGVTSCDPATLRPKALP--DLA 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254939526  145 DLVsQSGFWAKALPEEFANEGNIIAFWVDKKGRVFYRINESAAMLFFSGVRTVDPLWALVDVYGLTRGVQLLD 217
Cdd:pfam07177  78 TDL-RPGYWVVALSGSYLQEGDRLGFWVTSDGELHFSVNGEDQGVALSGVPDSQPLWAVFDLYGQTTQVSILG 149
NEUZ smart00588
domain in neuralized proteins;
292-414 5.27e-46

domain in neuralized proteins;


Pssm-ID: 128856  Cd Length: 123  Bit Score: 157.86  E-value: 5.27e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254939526   292 GDLRFHaLRAGAHVRILDEQTVARLEHGRDERALVFTSRPVRVAETIFIKVTRSGGGRAGALSFGVTTCDPGTLRPADLP 371
Cdd:smart00588   1 GPLRFH-HRHGSNIRLSDSGRVARRSASDFCNALVFSARPLRINELFEVKIEKVVRKWSGALRFGVTTCDPATLRPASLP 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 254939526   372 -FSPEALVDRKEFWAVCRVPGPLHSGDILGLVVNADGELHLSHN 414
Cdd:smart00588  80 tNACPDLVDMSGFWAKALGEGLAEQGGILGLDVLAEGEVVGVIN 123
mRING-HC-C3HC5_NEU1A cd16785
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1A (NEURL1A) ...
515-573 9.30e-38

Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1A (NEURL1A) and similar proteins; NEURL1A, also known as NEURL1, NEU, neuralized 1, or RING finger protein 67 (RNF67), is a mammalian homolog of the Drosophila neuralized (D-neu) protein. It functions as an E3 ubiquitin-protein ligase that directly interacts with and monoubiquitinates cytoplasmic polyadenylation element-binding protein 3 (CPEB3), an RNA binding protein and a translational regulator of local protein synthesis, which facilitates hippocampal plasticity and hippocampal-dependent memory storage. It also acts as a potential tumor suppressor that causes apoptosis and downregulates Notch target genes in the medulloblastoma. NEURL1A 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: 438439 [Multi-domain]  Cd Length: 59  Bit Score: 133.18  E-value: 9.30e-38
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 254939526 515 GQWSDECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKALHACCPICRRPIKDIIKTYRS 573
Cdd:cd16785    1 GSWSDECTICYENAVDTVIYTCGHMCLCYACGLRLKKMLNACCPICRRAIKDIIKTYRS 59
mRING-HC-C3HC5_NEU1B cd16786
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1B (NEURL1B); ...
518-573 1.02e-28

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: 108.11  E-value: 1.02e-28
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 254939526 518 SDECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKALHACCPICRRPIKDIIKTYRS 573
Cdd:cd16786    2 NGECTVCFDSEVDTVIYTCGHMCLCNSCGLKLKRQINACCPICRRVIKDVIKIYRP 57
mRING-HC-C3HC5_NEU1 cd16647
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein NEURL1A, ...
518-571 1.45e-26

Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein NEURL1A, NEURL1B, and similar proteins; This subfamily includes Drosophila neuralized (D-neu) protein, and its two mammalian homologs, NEURL1A and NEURL1B. D-neu is a regulator of the developmentally important Notch signaling pathway. NEURL1A, also known as NEURL1, NEU, neuralized 1, or RING finger protein 67 (RNF67), is a mammalian homolog of D-neu. It functions as an E3 ubiquitin-protein ligase that directly interacts with and monoubiquitinates cytoplasmic polyadenylation element-binding protein 3 (CPEB3), an RNA binding protein and a translational regulator of local protein synthesis, which facilitates hippocampal plasticity and hippocampal-dependent memory storage. It also acts as a potential tumor suppressor that causes apoptosis and downregulates Notch target genes in medulloblastoma. NEURL1B, also known as neuralized-2 (NEUR2) or neuralized-like protein 3, is another mammalian homolog of 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 by working cooperatively with another E3 ligase, Mind bomb-1 (Mib1), in Delta endocytosis to hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs)-positive vesicles. Members of this subfamily contain 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: 438309 [Multi-domain]  Cd Length: 53  Bit Score: 101.99  E-value: 1.45e-26
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 254939526 518 SDECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKAlHACCPICRRPIKDIIKTY 571
Cdd:cd16647    1 GSECVICYERPVDTVLYRCGHMCMCYDCALQLKRR-GGSCPICRAPIKDVIKIY 53
SPRY_NHR_like cd12887
SPRY domain in neuralized homology repeat; This family contains the neuralized homology repeat ...
295-446 5.81e-15

SPRY domain in neuralized homology repeat; This family contains the neuralized homology repeat 1 (NHR1) domain similar to the SPRY domain (known to mediate specific protein-protein interactions) at the C-terminus of a conserved region within eukaryotic neuralized and neuralized-like proteins. In Drosophila, the neuralized protein (Neur) belongs to a group of ubiquitin ligases and is required in a subset of Notch pathway-mediated cell fate decisions during development of the nervous system. Neur binds to the Notch receptor ligand Delta through its first NHR1 domain and mediates its ubiquitination for endocytosis. Multiple copies of this region are found in some members of the family.


Pssm-ID: 293945  Cd Length: 161  Bit Score: 72.54  E-value: 5.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254939526 295 RFHALRaGAHVRILDEQTVARLEHGRDERALVFTSRPVRVAETIFIKVTRSGGGRAGALSFGVTTCDPGTLrpaDLPFSP 374
Cdd:cd12887    1 RFHENH-GKNIRLSNDGRTATRVKASFNNGVVFSSRPLRPGELFEVRIDKLVDRWSGSLEIGVTTLNPETL---DLPPSA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254939526 375 EALvdRKEFW--AVCRVP----------GP----LHSGDILGLVVNADGELHLSHNGAAAGMqLCVDASQPLWMLFSLHG 438
Cdd:cd12887   77 TDL--KSGTWilSGSSVFkngnkirenyGPdldrLRVGDRVGVMRTSDGTLHFYVNGEDQGV-AASNVPQPVYAVVDLYG 153

                 ....*...
gi 254939526 439 AITQVRIL 446
Cdd:cd12887  154 QCEQVSIV 161
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
519-567 1.04e-13

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 65.47  E-value: 1.04e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 254939526  519 DECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKaLHACCPICRRPIKDI 567
Cdd:pfam13920   3 LLCVICLDRPRNVVLLPCGHLCLCEECAERLLR-KKKKCPICRQPIESV 50
SPRY_NHR_like cd12887
SPRY domain in neuralized homology repeat; This family contains the neuralized homology repeat ...
65-213 1.61e-11

SPRY domain in neuralized homology repeat; This family contains the neuralized homology repeat 1 (NHR1) domain similar to the SPRY domain (known to mediate specific protein-protein interactions) at the C-terminus of a conserved region within eukaryotic neuralized and neuralized-like proteins. In Drosophila, the neuralized protein (Neur) belongs to a group of ubiquitin ligases and is required in a subset of Notch pathway-mediated cell fate decisions during development of the nervous system. Neur binds to the Notch receptor ligand Delta through its first NHR1 domain and mediates its ubiquitination for endocytosis. Multiple copies of this region are found in some members of the family.


Pssm-ID: 293945  Cd Length: 161  Bit Score: 62.53  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254939526  65 FHPHTkGSQILMDLSHKAVKRQA-SFCNAITFSNRPVLIYEQVRLKITKKQCCWSGALRLGFTSKDPSRIH-PDSLP--- 139
Cdd:cd12887    2 FHENH-GKNIRLSNDGRTATRVKaSFNNGVVFSSRPLRPGELFEVRIDKLVDRWSGSLEIGVTTLNPETLDlPPSATdlk 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254939526 140 ---KYACPDLVSQSGfwaKALPEEFA------NEGNIIAFWVDKKGRVFYRIN----ESAAmlffSGVRTvdPLWALVDV 206
Cdd:cd12887   81 sgtWILSGSSVFKNG---NKIRENYGpdldrlRVGDRVGVMRTSDGTLHFYVNgedqGVAA----SNVPQ--PVYAVVDL 151

                 ....*..
gi 254939526 207 YGLTRGV 213
Cdd:cd12887  152 YGQCEQV 158
RING-HC_CARP cd16500
RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein CARP-1, ...
519-571 7.26e-10

RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein CARP-1, CARP-2 and similar proteins; The CARP subfamily includes CARP-1 and CARP-2 proteins, both of which are E3 ubiquitin ligases that ubiquitinate apical caspases and target them for proteasome-mediated degradation. As a novel group of caspase regulators with a FYVE-type zinc finger domain, they do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8, and caspase 10. Moreover, they stabilize MDM2 by inhibiting MDM2 self-ubiquitination, as well as by targeting 14-3-3sigma for degradation. They work together with MDM2 to enhance p53 degradation, thereby inhibiting p53-mediated cell death. CARPs contain an N-terminal FYVE-like domain that can serve as a membrane-targeting or endosome localizing signal and a C-terminal C3HC4-type RING-HC finger domain.


Pssm-ID: 438163 [Multi-domain]  Cd Length: 48  Bit Score: 54.70  E-value: 7.26e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 254939526 519 DECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKalhacCPICRRPIKDIIKTY 571
Cdd:cd16500    1 DLCKICMDAAIDCVLLECGHMVTCTDCGKKLSE-----CPICRQYVVRVVHFF 48
RING-HC_XBAT35-like cd23129
RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and ...
518-571 3.93e-09

RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and similar proteins; XBAT35, also known as ankyrin repeat domain and RING finger-containing protein XBAT35, or RING-type E3 ubiquitin transferase XBAT35, has no E3 ubiquitin-protein ligase activity observed when associated with the E2 enzyme UBC8 in vitro. It contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438491 [Multi-domain]  Cd Length: 54  Bit Score: 52.65  E-value: 3.93e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 254939526 518 SDECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKAlHACCPICRRPIKDIIKTY 571
Cdd:cd23129    2 RDECVVCMDAPRDAVCVPCGHVAGCMSCLKALMQS-SPLCPICRAPVRQVIKVY 54
mRING-HC-C2H2C4_MDM2-like cd16646
Modified RING finger, HC subclass (C2H2C4-type), found in E3 ubiquitin-protein ligase MDM2, ...
519-569 2.59e-08

Modified RING finger, HC subclass (C2H2C4-type), found in E3 ubiquitin-protein ligase MDM2, protein MDM4 and similar proteins; MDM2 (also known as HDM2) and MDM4 (also known as MDMX or HDMX) are the primary p53 tumor suppressor negative regulators. They have non-redundant roles in the regulation of p53. MDM2 mainly functions to control p53 stability, while MDM4 controls p53 transcriptional activity. Both MDM2 and MDM4 contain an N-terminal p53-binding domain, a RanBP2-type zinc finger (zf-RanBP2) domain near the central acidic region, and a C-terminal modified C2H2C4-type RING-HC finger. Mdm2 can form homo-oligomers through its RING domain and displays E3 ubiquitin ligase activity that catalyzes the attachment of ubiquitin to p53 as an essential step in the regulation of its levels in cells. Despite its RING domain and structural similarity with MDM2, MDM4 does not homo-oligomerize and lacks ubiquitin-ligase function, but inhibits the transcriptional activity of p53. In addition, both their RING domains are responsible for the hetero-oligomerization, which is crucial for the suppression of P53 activity during embryonic development and the recruitment of E2 ubiquitin-conjugating enzymes. Moreover, MDM2 and MDM4 can be phosphorylated and destabilized in response to DNA damage stress. In response to ribosomal stress, MDM2-mediated p53 ubiquitination and degradation can be inhibited through the interaction with ribosomal proteins L5, L11, and L23. However, MDM4 is not bound to ribosomal proteins, suggesting its different response to regulation by small basic proteins such as ribosomal proteins and ARF.


Pssm-ID: 438308 [Multi-domain]  Cd Length: 52  Bit Score: 50.40  E-value: 2.59e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 254939526 519 DECTICYEHAVDTVIY--TCGHMCLCYSCGLRLKKAlHACCPICRRPIKDIIK 569
Cdd:cd16646    1 DLCVICLSRPRTAAIVhgKTGHQVACYTCAKKLKRR-GKPCPVCRRPIQNVIK 52
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
520-560 4.30e-08

HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have a different Cys/His pattern. Some lack a single Cys or His residue at typical Zn ligand positions, especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can chelate Zn in a RING finger as well. This family corresponds to the HC subclass of RING (RING-HC) fingers that are characterized by containing C3HC4-type canonical RING-HC fingers or noncanonical RING-HC finger variants, including C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type modified RING-HC fingers. The canonical RING-HC finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-HC fingers can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle, and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 438113 [Multi-domain]  Cd Length: 41  Bit Score: 49.41  E-value: 4.30e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 254939526 520 ECTICYEHAVDTVIYTCGHMClCYSCGLRLKKALHACCPIC 560
Cdd:cd16449    2 ECPICLERLKDPVLLPCGHVF-CRECIRRLLESGSIKCPIC 41
mRING-HC-C3HC5_MGRN1-like cd16789
Modified RING finger, HC subclass (C3HC5-type), found in mahogunin RING finger protein 1 ...
519-561 4.30e-08

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: 49.22  E-value: 4.30e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 254939526 519 DECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKAlHACCPICR 561
Cdd:cd16789    1 SECVICLSDPRDTAVLPCRHLCLCSDCAEVLRYQ-SNKCPICR 42
RING-HC_CblA-like cd16501
RING finger, HC subclass, found in Dictyostelium discoideum Cbl-like protein A (CblA) and ...
518-571 6.57e-08

RING finger, HC subclass, found in Dictyostelium discoideum Cbl-like protein A (CblA) and similar proteins; CblA is a Dictyostelium homolog of the Cbl proteins which are multi-domain proteins acting as key negative regulators of various receptor and non-receptor tyrosine kinase signaling. CblA upregulates STATc tyrosine phosphorylation by downregulating PTP3, the protein tyrosine phosphatase responsible for dephosphorylating STATc. STATc is a signal transducer and activator of transcription protein. Like other Cbl proteins, CblA contains a tyrosine-kinase-binding domain (TKB), a proline-rich domain, a C3HC4-type RING-HC finger, and an ubiquitin-associated (UBA) domain. TKB, also known as a phosphotyrosine binding PTB domain, is composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain. This family also includes Drosophila melanogaster defense repressor 1 (Dnr1) that was identified as an inhibitor of Dredd activity in the absence of a microbial insult in Drosophila S2 cells. It inhibits the Drosophila initiator caspases Dredd and Dronc. Moreover, Dnr1 acts as a negative regulator of the Imd (immune deficiency) innate immune-response pathway. Its mutations cause neurodegeneration in Drosophila by activating the innate immune response in the brain. Dnr1 contains a FERM N-terminal domain followed by a region rich in glutamine and serine residues, a central FERM domain, and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438164 [Multi-domain]  Cd Length: 53  Bit Score: 49.02  E-value: 6.57e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 254939526 518 SDECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKalhacCPICRRPIKDIIKTY 571
Cdd:cd16501    5 ADLCVVCMDAPIDTVFLECGHLACCRLCSKRLRV-----CPICRQPISRVVRIF 53
RING-HC_RSPRY1 cd16566
RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) ...
519-564 1.60e-07

RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) and similar proteins; RSPRY1 is a hypothetical RING and SPRY domain-containing protein of unknown physiological function. Mutations in its corresponding gene RSPRY1 may associate with a distinct skeletal dysplasia syndrome. RSPRY1 contains a B30.2/SPRY domain and a C3HC4-type RING-HC finger.


Pssm-ID: 438228 [Multi-domain]  Cd Length: 43  Bit Score: 47.74  E-value: 1.60e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 254939526 519 DECTICYEHAVDTVIYTCGHMCLCYSCGLRLKkalhaCCPICRRPI 564
Cdd:cd16566    3 DSCTLCFDKVADTELRPCGHSGFCMECALQLE-----TCPLCRQPI 43
mRING-HC-C3HC5_RNF26 cd16788
Modified RING finger, HC subclass (C3HC5-type), found in RING finger protein 26 (RNF26) and ...
521-571 1.20e-06

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: 45.87  E-value: 1.20e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 254939526 521 CTICYEHAVDTVIYTCGHMCLCYSCG--LRLKKALHACCPICRRPIKDIIKTY 571
Cdd:cd16788    8 CVICQDQSKTVLILPCRHMCLCRQCAniLLQQPVYRRNCPLCRTMILQTLDVY 60
RING-HC_CARP1 cd16706
RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein 1 (CARP1) ...
521-573 1.73e-06

RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein 1 (CARP1) and similar proteins; CARP1, also known as caspase regulator CARP1, FYVE-RING finger protein Momo, RING finger homologous to inhibitor of apoptosis protein (RFI), RING finger protein 34 (RNF34), or RING finger protein RIFF, is a nuclear protein that functions as a specific E3 ubiquitin ligase for the transcriptional coactivator PGC-1alpha, a master regulator of energy metabolism and adaptive thermogenesis in the brown fat cell which negatively regulates brown fat cell metabolism. It is preferentially expressed in esophageal, gastric, and colorectal cancers, suggesting a possible association with the development of digestive tract cancers. It regulates the p53 signaling pathway by degrading 14-3-3 sigma and stabilizing MDM2. CARP1 does not localize to membranes in the cell and is involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10. CARP1 contains an N-terminal FYVE-like domain and a C-terminal C3HC4-type RING-HC finger domain.


Pssm-ID: 438366 [Multi-domain]  Cd Length: 54  Bit Score: 45.40  E-value: 1.73e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 254939526 521 CTICYEHAVDTVIYTCGHMCLCYSCGLRLKKalhacCPICRRPIKDIIKTYRS 573
Cdd:cd16706    7 CRICMDAVIDCVLLECGHMVTCTKCGKRMSE-----CPICRQYVVRAVHVFKS 54
mRING-HC-C3HC5_MAPL cd16648
Modified RING finger, HC subclass (C3HC5-type), found in mitochondrial-anchored protein ligase ...
521-571 1.84e-06

Modified RING finger, HC subclass (C3HC5-type), found in mitochondrial-anchored protein ligase (MAPL) and similar proteins; MAPL, also known as MULAN, mitochondrial ubiquitin ligase activator of NFKB 1, E3 SUMO-protein ligase MUL1, E3 ubiquitin-protein ligase MUL1, growth inhibition and death E3 ligase (GIDE), putative NF-kappa-B-activating protein 266, or RING finger protein 218 (RNF218), is a multifunctional mitochondrial outer membrane protein involved in several processes specific to metazoan (multicellular animal) cells, such as NF-kappaB activation, innate immunity and antiviral signaling, suppression of PINK1/parkin defects, mitophagy in skeletal muscle, and caspase-dependent apoptosis. MAPL contains a unique BAM (beside a membrane)/GIDE (growth inhibition death E3 ligase) domain and a C-terminal modified cytosolic C3HC5-type RING-HC finger which 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: 438310 [Multi-domain]  Cd Length: 52  Bit Score: 45.15  E-value: 1.84e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 254939526 521 CTICYEHAVDTVIYTCGHMCLCYSCglrlKKALHAC--CPICRRPIKDIIKTY 571
Cdd:cd16648    4 CVICLSNPRSCVFLECGHVCSCIEC----YEALPSPkkCPICRSFIKRVVPLY 52
RING-HC_IAPs cd16510
RING finger, HC subclass, found in inhibitor of apoptosis proteins (IAPs); IAPs are frequently ...
521-561 1.87e-06

RING finger, HC subclass, found in inhibitor of apoptosis proteins (IAPs); IAPs are frequently overexpressed in cancer and associated with tumor cell survival, chemoresistance, disease progression, and poor prognosis. They function primarily as negative regulators of cell death. They regulate caspases and apoptosis through the inhibition of specific members of the caspase family of cysteine proteases. In addition, IAPs has been implicated in a multitude of other cellular processes, including inflammatory signalling and immunity, mitogenic kinase signalling, proliferation and mitosis, as well as cell invasion and metastasis. IAPs in this family includes cellular inhibitor of apoptosis protein c-IAP1 (BIRC2) and c-IAP2 (BIRC3), XIAP (BIRC4), BIRC7, and BIRC8, all of which contain three N-terminal baculoviral IAP repeat (BIR) domains that enable interactions with proteins, a ubiquitin-association (UBA) domain that is responsible for the binding of polyubiquitin (polyUb), and a C3HC4-type RING-HC finger at the carboxyl terminus that is required for ubiquitin ligase activity. The UBA domain is only absent in mammalian homologs of BIRC7. Moreover, c-IAPs contains an additional caspase activation and recruitment domain (CARD) between the UBA and C3HC4-type RING-HC domains. The CARD domain may serve as a protein interaction surface.


Pssm-ID: 438173 [Multi-domain]  Cd Length: 40  Bit Score: 44.56  E-value: 1.87e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 254939526 521 CTICYEHAVDTVIYTCGHMCLCYSCGLRLKKalhacCPICR 561
Cdd:cd16510    4 CKICMDREVNIVFLPCGHLVTCAQCAASLRK-----CPICR 39
RING-HC_NEURL3 cd16552
RING finger, HC subclass, found in neuralized-like protein 3 (NEURL3) and similar proteins; ...
519-567 3.43e-06

RING finger, HC subclass, found in neuralized-like protein 3 (NEURL3) and similar proteins; NEURL3, also known as lung-inducible neuralized-related C3HC4 RING domain protein (LINCR), is a novel inflammation-induced E3 ubiquitin-protein ligase encoded by LINCR, a glucocorticoid-attenuated response gene induced in the lung during endotoxemia. It is expressed in alveolar epithelial type II cells, preferentially interacts with the ubiquitin-conjugating enzyme UbcH6, and generates polyubiquitin chains linked via non-canonical lysine residues. Overexpression of NEURL3 in the developing lung epithelium inhibits distal differentiation and induces cystic changes in the Notch signaling pathway. NEURL3 contains an N-terminal neuralized homology repeat (NHR) domain similar to the SPRY (SPla and the RYanodine receptor) domain and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438214 [Multi-domain]  Cd Length: 50  Bit Score: 44.15  E-value: 3.43e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 254939526 519 DECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKALhACCPICRRPIKDI 567
Cdd:cd16552    2 EECAICFHHTANTRLVPCGHSHFCGSCAWHIFRDT-ARCPVCRWQIEEV 49
RING-HC_BIRC2_3_7 cd16713
RING finger, HC subclass, found in apoptosis protein c-IAP1, c-IAP2, livin, and similar ...
521-573 3.97e-06

RING finger, HC subclass, found in apoptosis protein c-IAP1, c-IAP2, livin, and similar proteins; The cellular inhibitor of apoptosis protein c-IAPs function as ubiquitin E3 ligases that mediate the ubiquitination of substrates involved in apoptosis, nuclear factor-kappaB (NF-kappaB) signaling, and oncogenesis. Unlike other IAPs, such as XIAP, c-IAPs exhibit minimal binding to caspases and may not play an important role in the inhibition of these proteases. c-IAP1, also known as baculoviral IAP repeat-containing protein BIRC2, IAP-2, RING finger protein 48, or TNFR2-TRAF-signaling complex protein 2, is a potent regulator of the tumor necrosis factor (TNF) receptor family and NF-kappaB signaling pathways in the cytoplasm. It can also regulate E2F1 transcription factor-mediated control of cyclin transcription in the nucleus. c-IAP2, also known as BIRC3, IAP-1, apoptosis inhibitor 2 (API2), or IAP homolog C, also influences ubiquitin-dependent pathways that modulate innate immune signalling by activation of NF-kappaB. c-IAPs contain three N-terminal baculoviral IAP repeat (BIR) domains that enable interactions with proteins, a ubiquitin-association (UBA) domain that is responsible for the binding of polyubiquitin (polyUb), a caspase activation and recruitment domain (CARD) that serves as a protein interaction surface, and a C3HC4-type RING-HC finger at the carboxyl terminus that is required for ubiquitin ligase activity. Livin, also known as baculoviral IAP repeat-containing protein 7 (BIRC7), kidney inhibitor of apoptosis protein (KIAP), melanoma inhibitor of apoptosis protein (ML-IAP), or RING finger protein 50, was identified as the melanoma IAP. It plays crucial roles in apoptosis, cell proliferation, and cell cycle control. Its anti-apoptotic activity is regulated by the inhibition of caspase-3, -7, and -9. Its E3 ubiquitin-ligase-like activity promotes degradation of Smac/DIABLO, a critical endogenous regulator of all IAPs. Unlike other family members, mammalian livin contains a single BIR domain and a C3HC4-type RING-HC finger. The UBA domain can be detected in non-mammalian homologs of livin.


Pssm-ID: 438373 [Multi-domain]  Cd Length: 57  Bit Score: 44.39  E-value: 3.97e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 254939526 521 CTICYEHAVDTVIYTCGHMCLCYSCGLRLKKalhacCPICRRPIKDIIKTYRS 573
Cdd:cd16713   10 CKVCMDKEVSIVFIPCGHLVVCTECAPSLRK-----CPICRATIKGTVRTFLS 57
RING-HC_MIBs-like cd16520
RING finger, HC subclass, found in mind bomb MIB1, MIB2, RGLG1, RGLG2, and similar proteins; ...
520-564 5.75e-06

RING finger, HC subclass, found in mind bomb MIB1, MIB2, RGLG1, RGLG2, and similar proteins; MIBs are large, multi-domain E3 ubiquitin-protein ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. They are also responsible for TBK1 K63-linked ubiquitination and activation, promoting interferon production and controlling antiviral immunity. Moreover, MIBs selectively control responses to cytosolic RNA and regulate type I interferon transcription. Both MIB1 and MIB2 have similar domain architectures, which consist of two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region, where MIB1 and MIB2 contain three and two C3HC4-type RING-HC fingers, respectively. This model corresponds to the third RING-HC finger of MIB1, as well as the second RING-HC finger of MIB2. In addition to MIB1 and MIB2, the RING-HC fingers of RING domain ligase RGLG1, RGLG2 and similar proteins from plant are also included in this model. RGLG1 is a ubiquitously expressed E3 ubiquitin-protein ligase that interacts with UBC13 and, together with UBC13, catalyzes the formation of K63-linked polyubiquitin chains, which is involved in DNA damage repair. RGLG1 mediates the formation of canonical, K48-linked polyubiquitin chains that target proteins for degradation. It also regulates apical dominance by acting on the auxin transport proteins abundance. RGLG1 has overlapping functions with its closest sequelog, RGLG2. They both function as RING E3 ligases that interact with ethylene response factor 53 (ERF53) in the nucleus and negatively regulate the plant drought stress response. All RGLG proteins contain a Von Willebrand factor type A (vWA) domain and a C3HC4-type RING-HC finger.


Pssm-ID: 438183 [Multi-domain]  Cd Length: 39  Bit Score: 43.43  E-value: 5.75e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 254939526 520 ECTICYEHAVDTViYTCGHmCLCYSCGLRLKKalhacCPICRRPI 564
Cdd:cd16520    2 LCPICMERKKNVV-FLCGH-GTCQKCAEKLKK-----CPICRKPI 39
mRING-HC-C3HC5_MGRN1 cd16816
Modified RING finger, HC subclass (C3HC5-type), found in mahogunin RING finger protein 1 ...
518-569 7.34e-06

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: 43.51  E-value: 7.34e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 254939526 518 SDECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKALHAcCPICRRPIKDIIK 569
Cdd:cd16816    8 SNECVVCLSDLRDTLILPCRHLCLCNSCADTLRYQANN-CPICRLPFRALLQ 58
RING-HC_RNF8 cd16535
RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is ...
520-565 9.10e-06

RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal forkhead-associated (FHA) domain and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438197 [Multi-domain]  Cd Length: 64  Bit Score: 43.54  E-value: 9.10e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 254939526 520 ECTICYEHAVDTVIYTCGHM--CLCYSCGLRLKKAlhacCPICRRPIK 565
Cdd:cd16535    3 QCSICSELFIEAVTLNCSHSfcSYCITEWMKRKKE----CPICRKPIT 46
RING-HC_MEX3 cd16518
RING finger, HC subclass, found in RNA-binding proteins of the evolutionarily-conserved MEX-3 ...
520-571 9.92e-06

RING finger, HC subclass, found in RNA-binding proteins of the evolutionarily-conserved MEX-3 family; MEX-3 phosphoproteins are found in vertebrates. They are mediators of post-transcriptional regulation in different organisms, and have been implicated in many core biological processes, including embryonic development, epithelial homeostasis, immune responses, metabolism, and cancer. They contain two K homology (KH) domains that provide RNA-binding capacity, and a C-terminal C3HC4-type RING-HC finger. They shuttle between the nucleus and the cytoplasm via the CRM1-dependent export pathway. The RNA-binding protein MEX-3 from nematode Caenorhabditis elegans is the founding member of the MEX-3 family. Due to the lack of a RING-HC finger, it is not included here.


Pssm-ID: 438181 [Multi-domain]  Cd Length: 53  Bit Score: 43.13  E-value: 9.92e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 254939526 520 ECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKALHACCPICRRPIKDIIKTY 571
Cdd:cd16518    2 DCVVCFESEVVAALVPCGHNLFCMECANRICEKSDPECPVCHTPVTQAIRIF 53
RING-HC_CARP2 cd16707
RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein 2 (CARP-2) ...
521-562 1.10e-05

RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein 2 (CARP-2) and similar proteins; CARP-2, also known as rififylin, caspase regulator CARP2, FYVE-RING finger protein Sakura (Fring), RING finger and FYVE-like domain-containing protein 1, RING finger protein 189 (RNF189), or RING finger protein 34-like, is an endosome-associated E3 ubiquitin-protein ligase that targets internalized receptor interacting kinase (RIP) for proteasome-mediated degradation. It acts as a negative regulator of tumor necrosis factor (TNF)-induced nuclear factor (NF)-kappaB activation. It also regulates the p53 signaling pathway by degrading 14-3-3sigma and stabilizing MDM2. As a caspase regulator, CARP2 does not localize to membranes in the cell and is involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10. CARP2 contains an N-terminal FYVE-like domain and a C-terminal C3HC4-type RING-HC finger domain.


Pssm-ID: 438367 [Multi-domain]  Cd Length: 50  Bit Score: 42.66  E-value: 1.10e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 254939526 521 CTICYEHAVDTVIYTCGHMCLCYSCGLRLKKalhacCPICRR 562
Cdd:cd16707    5 CKICMDSPIDCVLLECGHMVTCTKCGKRMSE-----CPICRQ 41
RING-HC_MIP1-like cd23128
RING finger, HC subclass, found in Arabidopsis thaliana MND1-interacting protein 1 (MIP1) and ...
520-569 1.43e-05

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: 42.50  E-value: 1.43e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 254939526 520 ECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKALHACCPICRRPIKDIIK 569
Cdd:cd23128    5 ECVMCMEEERSVVFLPCAHQVVCSGCNDLHEKKGMRECPSCRGEIQERIR 54
RING-HC_LRSAM1 cd16515
RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing ...
518-572 1.53e-05

RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing protein 1 (LRSAM1) and similar proteins; LRSAM1, also known as Tsg101-associated ligase (TAL), or RIFLE, is an E3 ubiquitin-protein ligase that physically associates with, and selectively ubiquitylates, Tsg101, an E2-like molecule that regulates vesicular trafficking processes in yeast and mammals. It regulates a Tsg101-associated complex responsible for the sorting of cargo into cytoplasm-containing vesicles that bud at the multivesicular body and at the plasma membrane. LRSAM1 is a multidomain protein containing an N-terminal leucine-rich repeat (LRR), followed by several recognizable motifs, including an ezrin-radixin-moezin (ERM) domain, a coiled-coil (CC) region, a SAM domain, and a C-terminal C3HC4-type RING-HC finger domain.


Pssm-ID: 438178 [Multi-domain]  Cd Length: 48  Bit Score: 42.28  E-value: 1.53e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 254939526 518 SDECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKalhacCPICRrpiKDIIKTYR 572
Cdd:cd16515    1 ESECVVCMDAESQVIFLPCGHVCCCQTCSSSLST-----CPLCR---ADITQRVR 47
RING-HC_MEX3B cd16721
RING finger, HC subclass, found in RNA-binding protein MEX3B; MEX3B, also known as RING finger ...
518-571 1.61e-05

RING finger, HC subclass, found in RNA-binding protein MEX3B; MEX3B, also known as RING finger and KH domain-containing protein 3 (RKHD3), or RING finger protein 195 (RNF195), is an RNA-binding phosphoprotein that localizes in P-bodies and stress granules, which are two structures involved in the storage and turnover of mRNAs. It regulates the spatial organization of the Rap1 pathway that orchestrates Sertoli cell functions. It has a 3' long conserved untranslated region (3'LCU)-mediated fine-tuning system for mRNA regulation in early vertebrate development such as anteroposterior (AP) patterning and signal transduction. MEX3B contains two K homology (KH) domains that provide RNA-binding capacity, and a C-terminal C3HC4-type RING-HC finger. Like other MEX-3 family proteins, MEX3B shuttles between the nucleus and the cytoplasm via the CRM1-dependent export pathway.


Pssm-ID: 438381 [Multi-domain]  Cd Length: 58  Bit Score: 42.74  E-value: 1.61e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 254939526 518 SDECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKALHACCPICRRPIKDIIKTY 571
Cdd:cd16721    4 SRDCSICFESEVIAALVPCGHNLFCMECANRICEKNEPQCPVCHAAVTQAIRIF 57
mRING-HC-C3HC5_RNF157 cd16817
Modified RING finger, HC subclass (C3HC5-type), found in RING finger protein 157 (RNF157) and ...
518-569 1.63e-05

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: 42.77  E-value: 1.63e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 254939526 518 SDECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKALHAcCPICRRPIKDIIK 569
Cdd:cd16817    4 SAECVVCLSDVRDTLILPCRHLCLCNACADTLRYQANN-CPICRLPFRALLQ 54
mRING-HC-C3HC5_CGRF1-like cd16649
Modified RING finger, HC subclass (C3HC5-type), found in RING finger proteins, RNF26, RNF197 ...
519-561 1.90e-05

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: 41.92  E-value: 1.90e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 254939526 519 DECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKalhACCPICR 561
Cdd:cd16649    1 GLCVVCLENPASVLLLPCRHLCLCEVCAKGLRG---KTCPICR 40
RING-HC_MEX3A cd16720
RING finger, HC subclass, found in RNA-binding protein MEX3A; MEX3A, also known as RING finger ...
518-571 2.15e-05

RING finger, HC subclass, found in RNA-binding protein MEX3A; MEX3A, also known as RING finger and KH domain-containing protein 4 (RKHD4), is an RNA-binding phosphoprotein that localizes in P-bodies and stress granules, which are two structures involved in the storage and turnover of mRNAs. It has been implicated in the regulation of tumorigenesis. It controls the polarity and stemness of intestinal epithelial cells through the post-transcriptional regulation of the homeobox transcription factor CDX2, which plays a crucial role in intestinal cell fate specification, both during normal development and in tumorigenic processes involving intestinal reprogramming. Moreover, it exhibits a transforming activity when overexpressed in gastric epithelial cells. MEX3A contains two K homology (KH) domains that provide RNA-binding capacity, and a C-terminal C3HC4-type RING-HC finger. Like other MEX-3 family proteins, MEX3A shuttles between the nucleus and the cytoplasm via the CRM1-dependent export pathway.


Pssm-ID: 438380 [Multi-domain]  Cd Length: 56  Bit Score: 42.25  E-value: 2.15e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 254939526 518 SDECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKALHACCPICRRPIKDIIKTY 571
Cdd:cd16720    2 GRDCMVCFESEVTAALVPCGHNLFCMECAVRICERNEPECPVCHALATQAIRIF 55
mRING-HC-C2H2C4_MDM4 cd16784
Modified RING finger, HC subclass (C2H2C4-type), found in protein MDM4 and similar proteins; ...
537-571 2.56e-05

Modified RING finger, HC subclass (C2H2C4-type), found in protein MDM4 and similar proteins; MDM4, also known as double minute 4 protein (Hdm4), MDM2-like p53-binding protein, protein MDMX, HDMX, or p53-binding protein MDM4, exerts its oncogenic activity predominantly by binding p53 tumor suppressor and blocking its transcriptional activity. MDM4 is phosphorylated and destabilized in response to DNA damage stress. It can also be specifically dephosphorylated by directly interacting with protein phosphatase 1 (PP1), which may increase its stability and thus inhibit p53 activity. Meanwhile, MDM4 has a p53-independent role in tumorigenesis and cell growth regulation. MDM4 contains an N-terminal p53-binding domain and a C-terminal modified C2H2C4-type RING-HC finger responsible for its hetero-oligomerization, which is crucial for the suppression of P53 activity during embryonic development and the recruitment of E2 ubiquitin-conjugating enzymes. MDM4 also harbors a RanBP2-type zinc finger (zf-RanBP2) domain near the central acidic region.


Pssm-ID: 319698  Cd Length: 59  Bit Score: 42.08  E-value: 2.56e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 254939526 537 GHMCLCYSCGLRLKKAlHACCPICRRPIKDIIKTY 571
Cdd:cd16784   24 AHLVTCFHCARRLKKA-GAPCPVCKKEIQMVIKIF 57
mRING-HC-C3HC5_CGRF1 cd16787
Modified RING finger, HC subclass (C3HC5-type), found in cell growth regulator with RING ...
520-561 2.70e-05

Modified RING finger, HC subclass (C3HC5-type), found in cell growth regulator with RING finger domain protein 1 (CGRRF1) and similar proteins; 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. CGRRF1 contains 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: 438441 [Multi-domain]  Cd Length: 38  Bit Score: 41.20  E-value: 2.70e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 254939526 520 ECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKalhacCPICR 561
Cdd:cd16787    2 DCVVCQNAPVNRVLLPCRHACVCDECFKRLQR-----CPMCR 38
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
521-560 3.56e-05

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 40.96  E-value: 3.56e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 254939526   521 CTICYEH-AVDTVIYTCGHMcLCYSCGLRLKKALHACCPIC 560
Cdd:smart00184   1 CPICLEEyLKDPVILPCGHT-FCRSCIRKWLESGNNTCPIC 40
mRING-HC-C2H2C4_MDM2 cd16783
Modified RING finger, HC subclass (C2H2C4-type), found in E3 ubiquitin-protein ligase MDM2 and ...
521-573 8.97e-05

Modified RING finger, HC subclass (C2H2C4-type), found in E3 ubiquitin-protein ligase MDM2 and similar proteins; MDM2, also known as double minute 2 protein (Hdm2), oncoprotein MDM2, or p53-binding protein, exerts its oncogenic activity predominantly by binding p53 tumor suppressor and blocking its transcriptional activity. It forms homo-oligomers and displays E3 ubiquitin ligase activity that catalyzes the attachment of ubiquitin to p53 as an essential step in the regulation of its levels in cells. Moreover, in response to ribosomal stress, MDM2-mediated p53 ubiquitination and degradation can be inhibited through its interaction with ribosomal proteins L5, L11, and L23. MDM2 can be phosphorylated in the DNA damage. Meanwhile, MDM2 has a p53-independent role in tumorigenesis and cell growth regulation. In addition, it binds interferon (IFN) regulatory factor-2 (IRF-2), an IFN-regulated transcription factor, and mediates its ubiquitination. MDM2 contains an N-terminal p53-binding domain, and a C-terminal modified C2H2C4-type RING-HC finger conferring E3 ligase activity that is required for ubiquitination and nuclear export of p53. It is also responsible for the hetero-oligomerization of MDM2, which is crucial for the suppression of P53 activity during embryonic development, and the recruitment of E2 ubiquitin-conjugating enzymes. MDM2 also harbors a RanBP2-type zinc finger (zf-RanBP2) domain, as well as a nuclear localization signal (NLS) and a nuclear export signal (NES), near the central acidic region. The zf-RanBP2 domain plays an important role in mediating MDM2 binding to ribosomal proteins and thus is involved in MDM2-mediated p53 suppression.


Pssm-ID: 438438  Cd Length: 57  Bit Score: 40.31  E-value: 8.97e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 254939526 521 CTICYEHAVDTVIY--TCGHMCLCYSCGLRLKKAlHACCPICRRPIKDIIKTYRS 573
Cdd:cd16783    4 CVICQTRPKNGCIVhgKTGHLMACFTCAKKLKKR-NKPCPVCRQPIQMIVLTYFP 57
RING-HC_ZNF598 cd16615
RING finger, HC subclass, found in zinc finger protein 598 (ZNF598) and similar proteins; ...
519-568 1.20e-04

RING finger, HC subclass, found in zinc finger protein 598 (ZNF598) and similar proteins; ZNF598 associates with eukaryotic initiation factor 4E (eIF4E) homologous protein from mammals (m4EHP) by binding to Grb10-interacting GYF protein 2 (GIGYF2). The m4EHP-GIGYF2 complex functions as a translational repressor and is essential for normal embryonic development of mammalian. ZNF598 harbors a C3HC4-type RING-HC finger at its N-terminus.


Pssm-ID: 438277 [Multi-domain]  Cd Length: 51  Bit Score: 39.90  E-value: 1.20e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 254939526 519 DECTICYEHAVDTVIYTCGHMClCYSCGLRL-----KKAlhacCPICRRPIKDII 568
Cdd:cd16615    1 ETCVICCEEIEYFAVGPCNHPV-CYKCSLRMrvlykDKY----CPICRTELDKVI 50
RING-HC_MYLIP cd16523
RING finger, HC subclass, found in myosin regulatory light chain interacting protein (MYLIP) ...
521-571 1.62e-04

RING finger, HC subclass, found in myosin regulatory light chain interacting protein (MYLIP) and similar proteins; MYLIP, also known as inducible degrader of the low-density lipoprotein (LDL)-receptor (IDOL), or MIR, is an E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR, and LRP8. Its activity depends on E2 ubiquitin-conjugating enzymes of the UBE2D family. MYLIP stimulates clathrin-independent endocytosis and acts as a sterol-dependent inhibitor of cellular cholesterol uptake by binding directly to the cytoplasmic tail of the LDLR and promoting its ubiquitination via the UBE2D1/E1 complex. The ubiquitinated LDLR then enters the multivesicular body (MVB) protein-sorting pathway and is shuttled to the lysosome for degradation. Moreover, MYLIP has been identified as a novel ERM-like protein that affects cytoskeleton interactions regulating cell motility, such as neurite outgrowth. The ERM proteins includes ezrin, radixin, and moesin, which are cytoskeletal effector proteins linking actin to membrane-bound proteins at the cell surface. MYLIP contains an ERM-homology domain and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438186 [Multi-domain]  Cd Length: 52  Bit Score: 39.48  E-value: 1.62e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 254939526 521 CTICYEHAVDTVIYTCGHMCLCYSCGLRLKkalhaCCPICRRPIKDIIKTY 571
Cdd:cd16523    5 CMVCCEEEINSAFCPCGHMVCCESCAAQLQ-----SCPVCRSRVEHVQHVY 50
RING-HC_MEX3D cd16723
RING finger, HC subclass, found in RNA-binding protein MEX3D; MEX3D, also known as RING finger ...
518-571 3.03e-04

RING finger, HC subclass, found in RNA-binding protein MEX3D; MEX3D, also known as RING finger and KH domain-containing protein 1 (RKHD1), RING finger protein 193 (RNF193), or TINO, is an RNA-binding phosphoprotein that controls the stability of the transcripts coding for the anti-apoptotic protein BCL-2, and negatively regulates BCL-2 in HeLa cells. MEX3D contains two K homology (KH) domains that provide RNA-binding capacity, and a C-terminal C3HC4-type RING-HC finger. Like other MEX-3 family proteins, MEX3D shuttles between the nucleus and the cytoplasm via the CRM1-dependent export pathway.


Pssm-ID: 438383 [Multi-domain]  Cd Length: 64  Bit Score: 39.13  E-value: 3.03e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 254939526 518 SDECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKALHACCPICRRPIKDIIKTY 571
Cdd:cd16723   10 ARECVVCFESEVIAALVPCGHNLFCMECAIRICGKSEPECPACHTPATQAIHIF 63
RING-HC_RAD5 cd23131
RING finger, HC subclass, found in radiation sensitivity protein 5 (RAD5) and similar proteins; ...
520-564 3.19e-04

RING finger, HC subclass, found in radiation sensitivity protein 5 (RAD5) and similar proteins; RAD5, also known as revertibility protein 2 (REV2), or DNA repair protein RAD5, is a probable helicase, and a member of the UBC2/RAD6 epistasis group. It functions with the DNA repair protein RAD18 in error-free postreplication DNA repair. It is involved in the maintenance of wild-type rates of instability of simple repetitive sequences such as poly(GT) repeats. It may also be involved in maintaining a balance which acts in favor of error-prone non-homologous joining during DNA double-strand breaks repairs. It recruits the UBC13-MMS2 dimer to chromatin for DNA repair. RAD5 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438493 [Multi-domain]  Cd Length: 65  Bit Score: 38.96  E-value: 3.19e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 254939526 520 ECTICYEHAVD---TVIYTCGHmCLCYSCGL-----RLKKALHACCPICRRPI 564
Cdd:cd23131    5 ECSICTQEPIEvgeVVFTECGH-SFCEDCLLeyiefQNKKKLDLKCPNCREPI 56
RING-HC_CeBARD1-like cd23143
RING finger, HC subclass, found in Caenorhabditis elegans BRCA1-associated RING domain protein ...
520-564 3.84e-04

RING finger, HC subclass, found in Caenorhabditis elegans BRCA1-associated RING domain protein 1 (CeBARD1) and similar proteins; CeBARD1, also called Ce-BRD-1, Cebrd-1, or RING-type E3 ubiquitin transferase BARD1, is a constituent of the CeBCD complex that possesses E3 ubiquitin-protein ligase activity. It plays a role in triggering cellular responses at damage sites in response to DNA damage that may be induced by ionizing radiation. It protects against chromosome non-disjunction and nuclear fragmentation during meiotic double-strand break repair to ensure sister chromatid recombination and aid chromosome stability. CeBARD1 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438505 [Multi-domain]  Cd Length: 47  Bit Score: 38.29  E-value: 3.84e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 254939526 520 ECTICYEHAVDTV-IYTCGHMcLCYSCGLRLKKALHaCCPICRRPI 564
Cdd:cd23143    3 ECVICSEPQIDTFlLSSCGHI-YCWECFTEFIEKRH-MCPSCRFPL 46
RING-HC_MIBs cd16519
RING finger, HC subclass, found in mind bomb MIB1, MIB2, and similar proteins; MIBs are large, ...
520-561 4.19e-04

RING finger, HC subclass, found in mind bomb MIB1, MIB2, and similar proteins; MIBs are large, multi-domain E3 ubiquitin-protein ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. They are also responsible for TBK1 K63-linked ubiquitination and activation, promoting interferon production and controlling antiviral immunity. Moreover, MIBs selectively control responses to cytosolic RNA and regulate type I interferon transcription. Both MIB1 and MIB2 have similar domain architectures, which consist of two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region, where MIB1 and MIB2 contain three and two C3HC4-type RING-HC fingers, respectively. This model corresponds to the first RING-HC finger of MIB1 and MIB2, as well as the second RING-HC finger of MIB1.


Pssm-ID: 438182  Cd Length: 38  Bit Score: 37.84  E-value: 4.19e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 254939526 520 ECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKalhacCPICR 561
Cdd:cd16519    2 ECRVCSDKKALVLFQPCGHVVACEECSLRMKK-----CLQCK 38
RING-HC_BIRC4_8 cd16714
RING finger, HC subclass, found in E3 ubiquitin-protein ligase XIAP, baculoviral IAP ...
521-573 6.00e-04

RING finger, HC subclass, found in E3 ubiquitin-protein ligase XIAP, baculoviral IAP repeat-containing protein 8 (BIRC8) and similar proteins; XIAP, also known as baculoviral IAP repeat-containing protein 4 (BIRC4), IAP-like protein (ILP), inhibitor of apoptosis protein 3 (IAP-3), or X-linked inhibitor of apoptosis protein (X-linked IAP), is a potent suppressor of apoptosis that directly inhibits specific members of the caspase family of cysteine proteases, including caspase-3, -7, and -9. It promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death. The ubiquitin-protein ligase (E3) activity of XIAP also exhibits in the ubiquitination of second mitochondria-derived activator of caspases (Smac). The mitochondrial proteins, Smac/DIABLO and Omi/HtrA2, can inhibit the antiapoptotic activity of XIAP. XIAP has also been implicated in several intracellular signaling cascades involved in the cellular response to stress, such as the c-Jun N-terminal kinase (JNK), the nuclear factor-kappaB (NF-kappaB), and the transforming growth factor-beta (TGF-beta) pathways. Moreover, XIAP can regulate copper homeostasis by interacting with MURR1. BIRC8, also known as inhibitor of apoptosis-like protein 2, IAP-like protein 2, ILP-2, or testis-specific inhibitor of apoptosis, is a tissue-specific homolog of E3 ubiquitin-protein ligase XIAP. It has been implicated in the control of apoptosis in the testis by direct inhibition of caspase 9. Both XIAP and BIRC8 contain three N-terminal baculoviral IAP repeat (BIR) domains, a ubiquitin-association (UBA) domain and a C3HC4-type RING-HC finger at the carboxyl terminus.


Pssm-ID: 438374 [Multi-domain]  Cd Length: 64  Bit Score: 38.20  E-value: 6.00e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 254939526 521 CTICYEHAVDTVIYTCGHMCLCYSCGLRLKKalhacCPICRRPIKDIIKTYRS 573
Cdd:cd16714   17 CKICMDRNISIVFIPCGHLVTCKQCAEALDK-----CPICCTVITFKQKIFMS 64
RING-HC_BRCA1 cd16498
RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and ...
520-564 6.93e-04

RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also known as RING finger protein 53 (RNF53), is a RING finger protein encoded by the tumor suppressor gene BRCA1 that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus.


Pssm-ID: 438161 [Multi-domain]  Cd Length: 94  Bit Score: 39.20  E-value: 6.93e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 254939526 520 ECTICYEHAVDTVIYTCGHMcLCYSCGLRL--KKALHACCPICRRPI 564
Cdd:cd16498   18 ECPICLELLKEPVSTKCDHQ-FCRFCILKLlqKKKKPAPCPLCKKSV 63
RING-HC_MIB2_rpt1 cd16726
first RING finger, HC subclass, found in mind bomb 2 (MIB2) and similar proteins; MIB2, also ...
520-553 7.35e-04

first RING finger, HC subclass, found in mind bomb 2 (MIB2) and similar proteins; MIB2, also known as novel zinc finger protein (Novelzin), putative NF-kappa-B-activating protein 002N, skeletrophin, or zinc finger ZZ type with ankyrin repeat domain protein 1, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands. It promotes Delta ubiquitylation and endocytosis in Notch activation. Overexpression of MIB2 activates NF-kappaB and interferon-stimulated response element (ISRE) reporter activity. Moreover, MIB2 acts as a novel component of the activated B-cell CLL/lymphoma 10 (BCL10) complex and controls BCL10-dependent NF-kappaB activation. It also functions as a founder myoblast-specific protein that regulates myoblast fusion and muscle stability. MIB2 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of two C3HC4-type RING-HC fingers. This model corresponds to the first RING-HC finger.


Pssm-ID: 438386  Cd Length: 38  Bit Score: 37.43  E-value: 7.35e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 254939526 520 ECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKAL 553
Cdd:cd16726    2 ECLVCSELAALVRFEPCQHSIVCEECARRMKKCI 35
RING-HC_MEX3C cd16722
RING finger, HC subclass, found in RNA-binding protein MEX3C; MEX3C, also known as RING finger ...
520-571 7.48e-04

RING finger, HC subclass, found in RNA-binding protein MEX3C; MEX3C, also known as RING finger and KH domain-containing protein 2 (RKHD2), or RING finger protein 194 (RNF194), is an RNA-binding phosphoprotein that acts as a suppressor of chromosomal instability. It functions as an ubiquitin E3 ligase responsible for the post-transcriptional, HLA-A allotype-specific regulation of MHC class I molecules (MHC-I). It also modifies retinoic acid inducible gene-1 (RIG-I) in stress granules and plays a critical role in eliciting antiviral immune responses. Moreover, MEX3C plays an essential role in normal postnatal growth via enhancing the local expression of insulin-like growth factor 1 (IGF1) in bone. It may also be involved in metabolic regulation of energy balance. MEX3C contains two K homology (KH) domains that provide RNA-binding capacity, and a C-terminal C3HC4-type RING-HC finger. Like other MEX-3 family proteins, MEX3C shuttles between the nucleus and the cytoplasm via the CRM1-dependent export pathway.


Pssm-ID: 438382 [Multi-domain]  Cd Length: 55  Bit Score: 37.65  E-value: 7.48e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 254939526 520 ECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKALHACCPICRRPIKDIIKTY 571
Cdd:cd16722    3 DCVICFENEVIAALVPCGHNLFCMECANKICEKETPSCPVCQTAVTQAIQIH 54
RING-HC_RGLG_plant cd16729
RING finger, HC subclass, found in RING domain ligase RGLG1, RGLG2 and similar proteins from ...
518-571 7.88e-04

RING finger, HC subclass, found in RING domain ligase RGLG1, RGLG2 and similar proteins from plant; RGLG1 is a ubiquitously expressed E3 ubiquitin-protein ligase that interacts with UBC13 and, together with UBC13, catalyzes the formation of K63-linked polyubiquitin chains, which is involved in DNA damage repair. RGLG1 mediates the formation of canonical, K48-linked polyubiquitin chains that target proteins for degradation. It also regulates apical dominance by acting on the auxin transport proteins abundance. RGLG1 has overlapping functions with its closest sequelog, RGLG2. They both function as RING E3 ligases that interact with ethylene response factor 53 (ERF53) in the nucleus and negatively regulate the plant drought stress response. Members of this subfamily contain a Von Willebrand factor type A (vWA) domain and a C3HC4-type RING-HC finger.


Pssm-ID: 438389  Cd Length: 48  Bit Score: 37.46  E-value: 7.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 254939526 518 SDECTICYEHAVDtVIYTCGHMClCYSCGLRLKKalhacCPICRRPIKDIIKTY 571
Cdd:cd16729    2 DQLCPICLSNPKD-MAFGCGHQT-CCECGQSLTH-----CPICRQPITTRIKLY 48
RING-HC_RNF222 cd16564
RING finger, HC subclass, found in RING finger protein 222 (RNF222) and similar proteins; ...
520-564 9.83e-04

RING finger, HC subclass, found in RING finger protein 222 (RNF222) and similar proteins; RNF222 is an uncharacterized C3HC4-type RING-HC finger-containing protein. It may function as an E3 ubiquitin-protein ligase.


Pssm-ID: 438226 [Multi-domain]  Cd Length: 50  Bit Score: 37.38  E-value: 9.83e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 254939526 520 ECTICYEHAVD-TVIYTCGHMcLCYSCGLRLKKALHACCPICRRPI 564
Cdd:cd16564    2 ECPVCYEDFDDaPRILSCGHS-FCEDCLVKQLVSMTISCPICRRVT 46
RING-HC_MmTRIM43-like cd23133
RING finger, HC subclass, found in Mus musculus tripartite motif-containing protein 43 (TRIM43) ...
521-564 1.39e-03

RING finger, HC subclass, found in Mus musculus tripartite motif-containing protein 43 (TRIM43) and similar propteins; This subfamily includes TRIM43A, TRIM43B and TRIM43C, which are expressed specifically in mouse preimplantation embryos. They contain a typical C3HC4-type RING-HC finger.


Pssm-ID: 438495 [Multi-domain]  Cd Length: 57  Bit Score: 37.20  E-value: 1.39e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 254939526 521 CTICYEHAVDTVIYTCGHMcLCYSCGLRLKK--ALHACCPICRRPI 564
Cdd:cd23133    6 CSICQGIFMNPVYLRCGHK-FCEACLLLFQEdiKFPAYCPMCRQPF 50
PEX10 COG5574
RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
510-568 1.43e-03

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


Pssm-ID: 227861 [Multi-domain]  Cd Length: 271  Bit Score: 40.65  E-value: 1.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254939526 510 VTPGLGQWSDECTICYEHAVDTVIYTCGHMcLCYSC---GLRLKKALHacCPICRR---PIKDII 568
Cdd:COG5574  207 GLPFIPLADYKCFLCLEEPEVPSCTPCGHL-FCLSClliSWTKKKYEF--CPLCRAkvyPKKVII 268
RING-HC_RNF5-like cd16534
RING finger, HC subclass, found in RING finger protein RNF5, RNF185 and similar proteins; RNF5 ...
520-561 1.47e-03

RING finger, HC subclass, found in RING finger protein RNF5, RNF185 and similar proteins; RNF5 and RNF185 are E3 ubiquitin-protein ligases that are anchored to the outer membrane of the endoplasmic reticulum (ER). RNF5 acts at early stages of cystic fibrosis (CF) transmembrane conductance regulator (CFTR) biosynthesis, and functions as a target for therapeutic modalities to antagonize mutant CFTR proteins in CF patients carrying the F508del allele. RNF185 controls the degradation of CFTR and CFTR F508del allele in a RING- and proteasome-dependent manner, but does not control that of other classical endoplasmic reticulum-associated degradation (ERAD) model substrates. Moreover, both RNF5 and RNF185 play important roles in cell adhesion and migration through the modulation of cell migration by ubiquitinating paxillin. Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) are also included in this family. They possess E3 ubiquitin-protein ligase activity and may play a role in the growth and development of Arabidopsis. All members of this family contain a C3HC4-type RING-HC finger.


Pssm-ID: 438196 [Multi-domain]  Cd Length: 44  Bit Score: 36.51  E-value: 1.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 254939526 520 ECTICYEHAVDTVIYTCGHMcLCYSCGLR--LKKALHACCPICR 561
Cdd:cd16534    2 ECNICLDTASDPVVTMCGHL-FCWPCLYQwlETRPDRQTCPVCK 44
RING-HC_TRIM21_C-IV cd16596
RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar ...
521-563 1.51e-03

RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar proteins; TRIM21, also known as 52 kDa Ro protein, 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Ro(SS-A), RING finger protein 81 (RNF81), or Sjoegren syndrome type A antigen (SS-A), is a ubiquitously expressed E3 ubiquitin-protein ligase and a high affinity antibody receptor uniquely expressed in the cytosol of mammalian cells. As a cytosolic Fc receptor, TRIM21 binds the Fc of virus-associated antibodies and targets the complex in the cytosol for proteasomal degradation in a process known as antibody-dependent intracellular neutralization (ADIN), and provides an intracellular immune response to protect host defense against pathogen infection. It shows remarkably broad isotype specificity as it does not only bind IgG, but also IgM and IgA. Moreover, TRIM21 promotes the cytosolic DNA sensor cGAS and the cytosolic RNA sensor RIG-I sensing of viral genomes during infection by antibody-opsonized virus. It stimulates inflammatory signaling and activates innate transcription factors, such as nuclear factor-kappaB (NF-kappaB). TRIM21 also plays an essential role in p62-regulated redox homeostasis, suggesting it may be a viable target for treating pathological conditions resulting from oxidative damage. Furthermore, TRIM21 may have implications for various autoimmune diseases associated with uncontrolled antiviral signaling through the regulation of Nmi-IFI35 complex-mediated inhibition of innate antiviral response. TRIM21 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438258 [Multi-domain]  Cd Length: 77  Bit Score: 37.57  E-value: 1.51e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 254939526 521 CTICYEHAVDTVIYTCGHmCLCYSCGLRLKKALHACCPICRRP 563
Cdd:cd16596   12 CPICLDPFVEPVSIECGH-SFCQECISQVGKGGGSVCPVCRQR 53
RING-HC_TRIM40-C-V cd16583
RING finger, HC subclass, found in tripartite motif-containing protein 40 (TRIM40) and similar ...
521-563 1.64e-03

RING finger, HC subclass, found in tripartite motif-containing protein 40 (TRIM40) and similar proteins; TRIM40, also known as probable E3 NEDD8-protein ligase or RING finger protein 35 (RNF35), is highly expressed in the gastrointestinal tract including the stomach, small intestine, and large intestine. It enhances neddylation of inhibitor of nuclear factor kappaB kinase subunit gamma (IKKgamma), inhibits the activity of nuclear factor-kappaB (NF-kappaB)-mediated transcription, and thus prevents inflammation-associated carcinogenesis in the gastrointestinal tract. TRIM40 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain.


Pssm-ID: 438245 [Multi-domain]  Cd Length: 63  Bit Score: 37.12  E-value: 1.64e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 254939526 521 CTICYEHAVDTVIYTCGHMcLCYSCGLR-LKKALHA---CCPICRRP 563
Cdd:cd16583    8 CPICQEPLKEAVSTDCGHL-FCRMCLTQhAKKASASgvfSCPVCRKP 53
RING-HC_SPL2-like cd23145
RING finger, HC subclass, found in Arabidopsis thaliana SP1-like protein 2 (SPL2) and similar ...
521-562 1.95e-03

RING finger, HC subclass, found in Arabidopsis thaliana SP1-like protein 2 (SPL2) and similar proteins; SPL2, also known as RING-type E3 ubiquitin transferase SPL2, acts as an E3 ubiquitin-protein ligase that mediates E2-dependent protein ubiquitination. SPL2 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438507 [Multi-domain]  Cd Length: 47  Bit Score: 36.41  E-value: 1.95e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 254939526 521 CTICYEHAVDTVIYTCGHMCLCYSCGLRLKKALHACCPICRR 562
Cdd:cd23145    6 CVVCLLRRRRVAFIECGHRVCCELCARRVTREANPRCPVCRQ 47
RING-HC_RNF113A_B cd16539
RING finger, HC subclass, found in RING finger proteins RNF113A, RNF113B, and similar proteins; ...
521-569 2.22e-03

RING finger, HC subclass, found in RING finger proteins RNF113A, RNF113B, and similar proteins; RNF113A, also known as zinc finger protein 183 (ZNF183), is an E3 ubiquitin-protein ligase that physically interacts with the E2 protein, UBE2U. A nonsense mutation in RNF113A is associated with an X-linked trichothiodystrophy (TTD). Its yeast ortholog Cwc24p is predicted to have a spliceosome function and acts in a complex with Cef1p to participate in pre-U3 snoRNA splicing, indirectly affecting pre-rRNA processing. It is also important for the U2 snRNP binding to primary transcripts and co-migrates with spliceosomes. Moreover, the ortholog of RNF113A in fruit flies may also act as a spliceosome and is hypothesized to be involved in splicing, namely within the central nervous system. The ortholog in Caenorhabditis elegans is involved in DNA repair of inter-strand crosslinks. RNF113B, also known as zinc finger protein 183-like 1, shows high sequence similarity with RNF113A. Both RNF113A and RNF113B contain a CCCH-type zinc finger, which is commonly found in RNA-binding proteins involved in splicing, and a C3HC4-type RING-HC finger, which is frequently found in E3 ubiquitin ligases.


Pssm-ID: 438201 [Multi-domain]  Cd Length: 54  Bit Score: 36.42  E-value: 2.22e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 254939526 521 CTICYEHAVDTVIYTCGHmCLCYSCGLRLKKalHAC-CPICRRPIKDIIK 569
Cdd:cd16539    8 CFICRKPFKNPVVTKCGH-YFCEKCALKHYR--KSKkCFVCGKQTNGVFN 54
RING-HC_HLTF cd16509
RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar ...
519-565 2.28e-03

RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar proteins; HLTF, also known as DNA-binding protein/plasminogen activator inhibitor 1 regulator, HIP116, RING finger protein 80, SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3, or sucrose nonfermenting protein 2-like 3, is a yeast RAD5 homolog found in mammals. It has both E3 ubiquitin ligase and DNA helicase activities, and plays a pivotal role in the template-switching pathway of DNA damage tolerance. It is involved in Lys-63-linked poly-ubiquitination of proliferating cell nuclear antigen (PCNA) at Lys-164 and in the regulation of DNA damage tolerance. It shows double-stranded DNA translocase activity with 3'-5' polarity, thereby facilitating regression of the replication fork. HLTF contains an N-terminal HIRAN (HIP116 and RAD5 N-terminal) domain, a SWI/SNF helicase domain that is divided into N- and C-terminal parts by an insertion of a C3HC4-type RING-HC finger involved in the poly-ubiquitination of PCNA.


Pssm-ID: 438172 [Multi-domain]  Cd Length: 53  Bit Score: 36.51  E-value: 2.28e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 254939526 519 DECTICYEHAVDTVIYTCGHMcLCYSCGLRLKKALHACCPICRRPIK 565
Cdd:cd16509    4 EECAICLDSLTNPVITPCAHV-FCRRCICEVIQREKAKCPMCRAPLS 49
RING-HC_PRT1-like cd23132
RING finger, HC subclass, found in Arabidopsis thaliana proteolysis 1 protein (PRT1) and ...
520-563 2.50e-03

RING finger, HC subclass, found in Arabidopsis thaliana proteolysis 1 protein (PRT1) and similar proteins; PRT1, also called RING-type E3 ubiquitin transferase PRT1, is an E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. It functions in the N-end rule pathway of protein degradation, where it specifically recognizes and ubiquitinates proteins with an N-terminal bulky aromatic amino acid (Phe). It does not act on aliphatic hydrophobic and basic N-terminal residues (Arg or Leu) containing proteins. PRT1 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438494 [Multi-domain]  Cd Length: 52  Bit Score: 36.24  E-value: 2.50e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 254939526 520 ECTICYEHAVDTVIYTCGHMcLCYSCGLRLKKALH-ACCPICRRP 563
Cdd:cd23132    4 LCCICLDLLYKPVVLECGHV-FCFWCVHRCMNGYDeSHCPLCRRP 47
RING-HC_RNF168 cd16550
RING finger, HC subclass, found in RING finger protein 168 (RNF168) and similar proteins; ...
521-564 2.51e-03

RING finger, HC subclass, found in RING finger protein 168 (RNF168) and similar proteins; RNF168 is an E3 ubiquitin-protein ligase that promotes noncanonical K27 ubiquitination to signal DNA damage. It, together with RNF8, functions as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates, such as H2A and H2AX with H2AK13/15 ubiquitylation, facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. Moreover, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF168 contains an N-terminal C3HC4-type RING-HC finger that catalyzes H2A-K15ub and interacts with H2A, and two MIU (motif interacting with ubiquitin) domains responsible for the interaction with K63 linked poly-ubiquitin.


Pssm-ID: 438212 [Multi-domain]  Cd Length: 48  Bit Score: 36.20  E-value: 2.51e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 254939526 521 CTICYEHAVDTVIYTCGHMcLCYSCGLRLKKALHACCPICRRPI 564
Cdd:cd16550    3 CPICLEILVEPVTLPCNHT-LCMPCFQSTVEKASLCCPLCRLRI 45
RING-HC_MIB1_rpt2 cd16725
second RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also ...
519-561 3.27e-03

second RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also known as DAPK-interacting protein 1 (DIP-1) or zinc finger ZZ type with ankyrin repeat domain protein 2, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands, and thus plays an essential role in controlling metazoan development by Notch signaling. It is also involved in Wnt/beta-catenin signaling and nuclear factor (NF)-kappaB signaling, and has been implicated in innate immunity, neuronal function, genomic stability, and cell death. MIB1 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of three C3HC4-type RING-HC fingers. This model corresponds to the second RING-HC finger.


Pssm-ID: 438385  Cd Length: 38  Bit Score: 35.54  E-value: 3.27e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 254939526 519 DECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKalhacCPICR 561
Cdd:cd16725    1 EECVVCSDKKASVLFKPCGHMCACEGCAALMKK-----CVQCR 38
RING-HC_MIB1_rpt1 cd16724
first RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also ...
519-553 3.40e-03

first RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also known as DAPK-interacting protein 1 (DIP-1) or zinc finger ZZ type with ankyrin repeat domain protein 2, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands, and thus plays an essential role in controlling metazoan development by Notch signaling. It is also involved in Wnt/beta-catenin signaling and nuclear factor (NF)-kappaB signaling, and has been implicated in innate immunity, neuronal function, genomic stability, and cell death. MIB1 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of three C3HC4-type RING-HC fingers. This model corresponds to the first RING-HC finger.


Pssm-ID: 438384  Cd Length: 38  Bit Score: 35.54  E-value: 3.40e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 254939526 519 DECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKAL 553
Cdd:cd16724    1 EECMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCL 35
zf-RING_2 pfam13639
Ring finger domain;
519-561 4.40e-03

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 35.46  E-value: 4.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 254939526  519 DECTIC---YEHAVDTVIYTCGHmCLCYSCGLRLKKAlHACCPICR 561
Cdd:pfam13639   1 DECPICleeFEEGDKVVVLPCGH-HFHRECLDKWLRS-SNTCPLCR 44
RING-HC_AtRMA-like cd16745
RING finger, HC subclass, found in Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) ...
520-561 4.95e-03

RING finger, HC subclass, found in Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) and similar proteins; AtRMAs, including AtRma1, AtRma2, and AtRma3, are endoplasmic reticulum (ER)-localized Arabidopsis homologs of human outer membrane of the ER-anchor E3 ubiquitin-protein ligase, RING finger protein 5 (RNF5). AtRMAs possess E3 ubiquitin ligase activity, and may play a role in the growth and development of Arabidopsis. The AtRMA1 and AtRMA3 genes are predominantly expressed in major tissues, such as cotyledons, leaves, shoot-root junction, roots, and anthers, while AtRMA2 expression is restricted to the root tips and leaf hydathodes. AtRma1 probably functions with the Ubc4/5 subfamily of E2. AtRma2 is likely involved in the cellular regulation of ABP1 expression levels through interacting with auxin binding protein 1 (ABP1). AtRMA proteins contain an N-terminal C3HC4-type RING-HC finger and a trans-membrane-anchoring domain in their extreme C-terminal region.


Pssm-ID: 438403 [Multi-domain]  Cd Length: 45  Bit Score: 35.15  E-value: 4.95e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 254939526 520 ECTICYEHAVDTVIYTCGHMcLCYSCglrLKKALHAC-----CPICR 561
Cdd:cd16745    2 ECNICLDLAQDPVVTLCGHL-FCWPC---LHKWLRRQssqpeCPVCK 44
RING-HC_RNF169 cd16551
RING finger, HC subclass, found in RING finger protein 169 (RNF169) and similar proteins; ...
521-563 4.97e-03

RING finger, HC subclass, found in RING finger protein 169 (RNF169) and similar proteins; RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to regulation of the DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. RNF169 contains an N-terminal C3HC4-type RING-HC finger and a C-terminal MIU (motif interacting with ubiquitin) domain.


Pssm-ID: 438213 [Multi-domain]  Cd Length: 55  Bit Score: 35.60  E-value: 4.97e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 254939526 521 CTICYEHAVDTVIYTCGHmCLCYSCGLRLKKALHA--CCPICRRP 563
Cdd:cd16551    4 CAGCLEVPVEPATLPCGH-TLCRGCANRALDAAEAgpTCPRCRAP 47
RING-HC_ScPSH1-like cd16568
RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated ...
520-565 5.47e-03

RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated protein 1 (ScPSH1) and similar proteins; ScPSH1 is a Cse4-specific E3 ubiquitin ligase that interacts with the kinetochore protein Pat1 and targets the degradation of budding yeast centromeric histone H3 variant, CENP-ACse4, which is essential for faithful chromosome segregation. ScPSH1 contains a C3HC4-type RING-HC finger and a DNA directed RNA polymerase domain.


Pssm-ID: 438230 [Multi-domain]  Cd Length: 54  Bit Score: 35.42  E-value: 5.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 254939526 520 ECTICYEHAVDTVIYTCGHMcLCYSCGL-RLKKALHACCPICRRPIK 565
Cdd:cd16568    6 ECIICHEYLYEPMVTTCGHT-YCYTCLNtWFKSNRSLSCPDCRTKIT 51
RING-HC_Cbl-c cd16710
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-c and similar proteins; ...
521-565 6.32e-03

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-c and similar proteins; Cbl-c, also known as RING finger protein 57 (RNF57), SH3-binding protein Cbl-3, SH3-binding protein Cbl-c, or signal transduction protein Cbl-c, is an E3 ubiquitin-protein ligase expressed exclusively in epithelial cells. It contains a tyrosine-kinase-binding domain (TKB, also known as the phosphotyrosine binding PTB domain, composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain), a C3HC4-type RING-HC finger, and a short proline-rich region, but lacks the ubiquitin-associated (UBA) leucine zipper motif that are present in Cbl and Cbl-b. Cbl-c acts as a regulator of epidermal growth factor receptor (EGFR)-mediated signal transduction. It also suppresses v-Src-induced transformation through ubiquitin-dependent protein degradation. Moreover, Cbl-c ubiquitinates and downregulates RETMEN2A and implicates Enigma (PDLIM7) as a positive regulator of RETMEN2A by blocking Cbl-mediated ubiquitination and degradation. The ubiquitin ligase activity of Cbl-c is increased via the interaction of its RING-HC finger domain with a LIM domain of the paxillin homolog, hydrogen peroxide induced construct 5 (Hic-5).


Pssm-ID: 438370 [Multi-domain]  Cd Length: 65  Bit Score: 35.45  E-value: 6.32e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 254939526 521 CTICYEHAVDTVIYTCGHMcLCYSCGLRLKKALHACCPICRRPIK 565
Cdd:cd16710   16 CKICAERDKDVRIEPCGHL-LCSCCLAAWQHSDSQTCPFCRCEIK 59
RING-HC_Cbl cd16708
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl and similar proteins; Cbl, ...
521-565 6.52e-03

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl and similar proteins; Cbl, also known as Casitas B-lineage lymphoma proto-oncogene, proto-oncogene c-Cbl, RING finger protein 55 (RNF55), or signal transduction protein Cbl, is a multi-domain protein that acts as a key negative regulator of various receptor and non-receptor tyrosine kinase signaling. It contains a tyrosine kinase-binding domain (TKB, also known as the phosphotyrosine binding PTB domain, composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain), a proline-rich domain, a C3HC4-type RING-HC finger, and an ubiquitin-associated (UBA) domain. TKB is responsible for the interactions with many tyrosine kinases, such as the colony-stimulating factor-1 (CSF-1) receptor, Syk/ZAP-70, and Src-family of protein tyrosine kinases. The proline-rich domain can recruit proteins with a SH3 domain. Moreover, Cbl functions as an E3 ubiquitin ligase that can bind ubiquitin-conjugating enzymes (E2s) through the RING-HC finger.


Pssm-ID: 438368 [Multi-domain]  Cd Length: 77  Bit Score: 35.83  E-value: 6.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 254939526 521 CTICYEHAVDTVIYTCGHMcLCYSCGLRLKKALHACCPICRRPIK 565
Cdd:cd16708   24 CKICAENDKDVKIEPCGHL-MCTSCLTSWQESEGQGCPFCRCEIK 67
RING-HC_RNF213 cd16561
RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; ...
520-566 6.64e-03

RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; RNF213, also known as ALK lymphoma oligomerization partner on chromosome 17 or Moyamoya steno-occlusive disease-associated AAA+ and RING finger protein (mysterin), is an intracellular soluble protein that functions as an E3 ubiquitin-protein ligase and AAA+ ATPase, which possibly contributes to vascular development through mechanical processes in the cell. It plays a unique role in endothelial cells for proper gene expression in response to inflammatory signals from the environment. Mutations in RNF213 may be associated with Moyamoya disease (MMD), an idiopathic cerebrovascular occlusive disorder prevalent in East Asia. It also acts as a nuclear marker for acanthomorph phylogeny. RNF213 contains two tandem enzymatically active AAA+ ATPase modules and a C3HC4-type RING-HC finger. It can form a huge ring-shaped oligomeric complex.


Pssm-ID: 438223 [Multi-domain]  Cd Length: 50  Bit Score: 34.95  E-value: 6.64e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 254939526 520 ECTICYEHAVDTVIYTCGHMcLCYSCglrLKKAL--HACCPICRRPIKD 566
Cdd:cd16561    4 ECSICLEDLNDPVKLPCDHV-FCEEC---IRQWLpgQMSCPLCRTELPD 48
RING-HC_RNF10 cd16536
RING finger, HC subclass, found in RING finger protein 10 (RNF10) and similar proteins; RNF10 ...
520-565 7.44e-03

RING finger, HC subclass, found in RING finger protein 10 (RNF10) and similar proteins; RNF10 is an E3 ubiquitin-protein ligase that interacts with mesenchyme Homeobox 2 (MEOX2) transcription factor, a regulator of the proliferation, differentiation and migration of vascular smooth muscle cells and cardiomyocytes; it enhances Meox2 activation of the p21 promoter. It also regulates the expression of myelin-associated glycoprotein (MAG) genes and is required for myelin production in Schwann cells of the peripheral nervous system. Moreover, RNF10 regulates retinoic acid-induced neuronal differentiation and the cell cycle exit of P19 embryonic carcinoma cells. RNF10 contains a C3HC4-type RING-HC finger and three putative nuclear localization signals.


Pssm-ID: 438198 [Multi-domain]  Cd Length: 54  Bit Score: 34.91  E-value: 7.44e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 254939526 520 ECTICYEHAVDTVIYTCGHMcLCYSCGLR---LKKALHACCPICRRPIK 565
Cdd:cd16536    2 QCPICLEPPVAPRITRCGHI-FCWPCILRylsLSEKKWRKCPICFESIH 49
mRING-C3HGC3_RFWD3 cd16450
Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing ...
518-571 8.38e-03

Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing protein 3 (RFWD3) and similar proteins; RFWD3, also known as RING finger protein 201 (RNF201) or FLJ10520, is an E3 ubiquitin-protein ligase that forms a complex with Mdm2 and p53 to synergistically ubiquitinate p53 and acts as a positive regulator of p53 stability in response to DNA damage. It is phosphorylated by checkpoint kinase ATM/ATR and the phosphorylation mutant fails to stimulate p53 ubiquitination. RFWD3 also functions as a novel replication protein A (RPA)-associated protein involved in DNA replication checkpoint control. RFWD3 contains an N-terminal SQ-rich region followed by a RING finger domain that exhibits robust E3 ubiquitin ligase activity toward p53, a coiled-coil domain and three WD40 repeats in the C-terminus, the latter two of which may be responsible for protein-protein interaction. The RING finger in this family is a modified C3HGC3-type RING finger, but not a canonical C3H2C3-type RING-H2 finger or C3HC4-type RING-HC finger.


Pssm-ID: 438114 [Multi-domain]  Cd Length: 61  Bit Score: 34.90  E-value: 8.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254939526 518 SDECTICYE-------HAVdtVIYTCGHmCLCYSCglrLKKAL---HACCPICRRPIK--DIIKTY 571
Cdd:cd16450    2 GNTCPICFEpwtssgeHRL--VSLKCGH-LFGYSC---IEKWLkgkGKKCPQCNKKAKrsDIRPLY 61
RING-HC_MIB1_rpt3 cd16727
third RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also ...
521-571 8.64e-03

third RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also known as DAPK-interacting protein 1 (DIP-1) or zinc finger ZZ type with ankyrin repeat domain protein 2, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands, and thus plays an essential role in controlling metazoan development by Notch signaling. It is also involved in Wnt/beta-catenin signaling and nuclear factor (NF)-kappaB signaling, and has been implicated in innate immunity, neuronal function, genomic stability, and cell death. MIB1 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of three C3HC4-type RING-HC fingers. This model corresponds to the third RING-HC finger.


Pssm-ID: 438387  Cd Length: 46  Bit Score: 34.72  E-value: 8.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 254939526 521 CTICYEHaVDTVIYTCGHMClCYSCGLRLKKalhacCPICRRPIKDIIKTY 571
Cdd:cd16727    3 CPVCLDR-LKNMIFLCGHGT-CQLCGDRMSE-----CPICRKAIEKRILLY 46
RING-HC_RNF141 cd16545
RING finger, HC subclass, found in RING finger protein 141 (RNF141) and similar proteins; ...
519-561 9.49e-03

RING finger, HC subclass, found in RING finger protein 141 (RNF141) and similar proteins; RNF141, also known as zinc finger protein 230 (ZNF230), is a RING finger protein present primarily in the nuclei of spermatogonia, the acrosome, and the tail of spermatozoa. It may have a broad function during early development of vertebrates. It plays an important role in spermatogenesis, including spermatogenic cell proliferation and sperm maturation, as well as motility and fertilization. It also exhibits DNA binding activity. RNF141/ZNF230 gene mutations may be associated with azoospermia. RNF141 contains a C3HC4-type RING finger domain that may function as an activator module in transcription.


Pssm-ID: 438207 [Multi-domain]  Cd Length: 40  Bit Score: 34.37  E-value: 9.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 254939526 519 DECTICYEHAVDtVIYTCGHMcLCYSCGLRLkKALHACCPICR 561
Cdd:cd16545    1 EECCICMDRKAD-LILPCAHS-YCQKCIDKW-SDRHRTCPICR 40
 
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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