NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|63054452|ref|NP_588346|]
View 

ubiquitin-protein ligase E3 [Schizosaccharomyces pombe]

Protein Classification

zinc finger family protein( domain architecture ID 706824)

zinc finger family protein may be involved in transcriptional regulation; similar to Schizosaccharomyces pombe E3 ubiquitin-protein ligase hel2, which that plays a key role in the ribosome quality control (RQC), and Homo sapiens histone H4 transcription factor

Gene Ontology:  GO:0008270
PubMed:  11179890

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COG5236 super family cl28715
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
7-383 8.28e-167

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


The actual alignment was detected with superfamily member COG5236:

Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 489.15  E-value: 8.28e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054452   7 NLNNKEHNRASEKKNSRTHNKKTNRNQSKEKPVSSRsvETPKNAVCLEPVgtdpvsnvaTVDASKEEQDEDEQICFICAE 86
Cdd:COG5236   1 MSESVKENVTPTRNFRRTQGPQNNTKPHNDRKNFRR--KQKKNNLSAEPN---------LTTSSADDTDEENMNCQICAG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054452  87 GITYSCVLPCNHRMCHVCALRLRALYKTKECTFCKTEWDTVLITKDHEIDIHDVDLAKLpfQDEKLGIVYSDEHAQEESN 166
Cdd:COG5236  70 STTYSARYPCGHQICHACAVRLRALYMQKGCPLCRTETEAVVFTASSPADITDRRQWKG--REEKVGIFYEGEDVRDEME 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054452 167 LLLQFNCPEDACDITCKGWFDLKLHAKVKHHKFFCDLCVKNKKVFTHEHTLFSKKGLTKHNEVGDQGSdleitGFKGHPK 246
Cdd:COG5236 148 DLLSFKCPKSKCHRRCGSLKELKKHYKAQHGFVLCSECIGNKKDFWNEIRLFRSSTLRDHKNGGLEEE-----GFKGHPL 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054452 247 CEFCNTHFYDDDELFKHCREKHERCYICDQVaGRPTHQYFKNYDSLERHFEKDHYICRERECLERKFVVFGTEIDLKAHQ 326
Cdd:COG5236 223 CIFCKIYFYDDDELRRHCRLRHEACHICDMV-GPIRYQYFKSYEDLEAHFRNAHYCCTFQTCRVGKCYVFPYHTELLEHL 301

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054452 327 LDEHPHNFTQRELREARRI----------------IPQFSYDPPGASGRNRRERTSSTPSEQSTSVNETANSL 383
Cdd:COG5236 302 TRFHKVNARLSEIPRPGRCsipvmdpfkrkkaparVSVIDPSGGNARAPMAHRGGSRQDTASPSTEAELPKYL 374
 
Name Accession Description Interval E-value
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
7-383 8.28e-167

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


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 489.15  E-value: 8.28e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054452   7 NLNNKEHNRASEKKNSRTHNKKTNRNQSKEKPVSSRsvETPKNAVCLEPVgtdpvsnvaTVDASKEEQDEDEQICFICAE 86
Cdd:COG5236   1 MSESVKENVTPTRNFRRTQGPQNNTKPHNDRKNFRR--KQKKNNLSAEPN---------LTTSSADDTDEENMNCQICAG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054452  87 GITYSCVLPCNHRMCHVCALRLRALYKTKECTFCKTEWDTVLITKDHEIDIHDVDLAKLpfQDEKLGIVYSDEHAQEESN 166
Cdd:COG5236  70 STTYSARYPCGHQICHACAVRLRALYMQKGCPLCRTETEAVVFTASSPADITDRRQWKG--REEKVGIFYEGEDVRDEME 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054452 167 LLLQFNCPEDACDITCKGWFDLKLHAKVKHHKFFCDLCVKNKKVFTHEHTLFSKKGLTKHNEVGDQGSdleitGFKGHPK 246
Cdd:COG5236 148 DLLSFKCPKSKCHRRCGSLKELKKHYKAQHGFVLCSECIGNKKDFWNEIRLFRSSTLRDHKNGGLEEE-----GFKGHPL 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054452 247 CEFCNTHFYDDDELFKHCREKHERCYICDQVaGRPTHQYFKNYDSLERHFEKDHYICRERECLERKFVVFGTEIDLKAHQ 326
Cdd:COG5236 223 CIFCKIYFYDDDELRRHCRLRHEACHICDMV-GPIRYQYFKSYEDLEAHFRNAHYCCTFQTCRVGKCYVFPYHTELLEHL 301

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054452 327 LDEHPHNFTQRELREARRI----------------IPQFSYDPPGASGRNRRERTSSTPSEQSTSVNETANSL 383
Cdd:COG5236 302 TRFHKVNARLSEIPRPGRCsipvmdpfkrkkaparVSVIDPSGGNARAPMAHRGGSRQDTASPSTEAELPKYL 374
RING-HC_ZNF598 cd16615
RING finger, HC subclass, found in zinc finger protein 598 (ZNF598) and similar proteins; ...
 80-129 2.83e-21

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: 87.28  E-value: 2.83e-21
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 63054452  80 ICFICAEGITYSCVLPCNHRMCHVCALRLRALYKTKECTFCKTEWDTVLI 129
Cdd:cd16615   2 TCVICCEEIEYFAVGPCNHPVCYKCSLRMRVLYKDKYCPICRTELDKVIF 51
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
77-127 2.76e-07

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 47.76  E-value: 2.76e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 63054452    77 DEQICFICAEGITYSCVLPCNHR-MCHVCALRLRAlyKTKECTFCKTEWDTV 127
Cdd:pfam13920   1 EDLLCVICLDRPRNVVLLPCGHLcLCEECAERLLR--KKKKCPICRQPIESV 50
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 81-120 9.15e-03

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: 34.79  E-value: 9.15e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 63054452     81 CFICAEGITYSCV-LPCNHRMCHVCALRLRaLYKTKECTFC 120
Cdd:smart00184   1 CPICLEEYLKDPViLPCGHTFCRSCIRKWL-ESGNNTCPIC 40
 
Name Accession Description Interval E-value
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
7-383 8.28e-167

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


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 489.15  E-value: 8.28e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054452   7 NLNNKEHNRASEKKNSRTHNKKTNRNQSKEKPVSSRsvETPKNAVCLEPVgtdpvsnvaTVDASKEEQDEDEQICFICAE 86
Cdd:COG5236   1 MSESVKENVTPTRNFRRTQGPQNNTKPHNDRKNFRR--KQKKNNLSAEPN---------LTTSSADDTDEENMNCQICAG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054452  87 GITYSCVLPCNHRMCHVCALRLRALYKTKECTFCKTEWDTVLITKDHEIDIHDVDLAKLpfQDEKLGIVYSDEHAQEESN 166
Cdd:COG5236  70 STTYSARYPCGHQICHACAVRLRALYMQKGCPLCRTETEAVVFTASSPADITDRRQWKG--REEKVGIFYEGEDVRDEME 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054452 167 LLLQFNCPEDACDITCKGWFDLKLHAKVKHHKFFCDLCVKNKKVFTHEHTLFSKKGLTKHNEVGDQGSdleitGFKGHPK 246
Cdd:COG5236 148 DLLSFKCPKSKCHRRCGSLKELKKHYKAQHGFVLCSECIGNKKDFWNEIRLFRSSTLRDHKNGGLEEE-----GFKGHPL 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054452 247 CEFCNTHFYDDDELFKHCREKHERCYICDQVaGRPTHQYFKNYDSLERHFEKDHYICRERECLERKFVVFGTEIDLKAHQ 326
Cdd:COG5236 223 CIFCKIYFYDDDELRRHCRLRHEACHICDMV-GPIRYQYFKSYEDLEAHFRNAHYCCTFQTCRVGKCYVFPYHTELLEHL 301

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054452 327 LDEHPHNFTQRELREARRI----------------IPQFSYDPPGASGRNRRERTSSTPSEQSTSVNETANSL 383
Cdd:COG5236 302 TRFHKVNARLSEIPRPGRCsipvmdpfkrkkaparVSVIDPSGGNARAPMAHRGGSRQDTASPSTEAELPKYL 374
RING-HC_ZNF598 cd16615
RING finger, HC subclass, found in zinc finger protein 598 (ZNF598) and similar proteins; ...
 80-129 2.83e-21

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: 87.28  E-value: 2.83e-21
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 63054452  80 ICFICAEGITYSCVLPCNHRMCHVCALRLRALYKTKECTFCKTEWDTVLI 129
Cdd:cd16615   2 TCVICCEEIEYFAVGPCNHPVCYKCSLRMRVLYKDKYCPICRTELDKVIF 51
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
77-127 2.76e-07

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 47.76  E-value: 2.76e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 63054452    77 DEQICFICAEGITYSCVLPCNHR-MCHVCALRLRAlyKTKECTFCKTEWDTV 127
Cdd:pfam13920   1 EDLLCVICLDRPRNVVLLPCGHLcLCEECAERLLR--KKKKCPICRQPIESV 50
RING-HC_TRIM36_C-I cd16756
RING finger, HC subclass, found in tripartite motif-containing protein 36 (TRIM36) and similar ...
 76-125 3.11e-05

RING finger, HC subclass, found in tripartite motif-containing protein 36 (TRIM36) and similar proteins; TRIM36, the human ortholog of mouse Haprin, also known as RING finger protein 98 (RNF98) or zinc-binding protein Rbcc728, is an E3 ubiquitin-protein ligase expressed in the germ plasm. It has been implicated in acrosome reaction, fertilization, and embryogenesis, as well as in carcinogenesis. TRIM36 functions upstream of Wnt/beta-catenin activation, and plays a role in controlling the stability of proteins regulating microtubule polymerization during cortical rotation, and subsequently dorsal axis formation. It is also potentially associated with chromosome segregation by interacting with the kinetochore protein centromere protein-H (CENP-H), and colocalizing with the microtubule protein alpha-tubulin. Its overexpression may cause chromosomal instability and carcinogenesis. It is, thus, a novel regulator affecting cell cycle progression. Moreover, TRIM36 plays a critical role in the arrangement of somites during embryogenesis. TRIM36 belongs to the C-I 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, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, a PRY domain and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438414 [Multi-domain]  Cd Length: 49  Bit Score: 41.82  E-value: 3.11e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 63054452  76 EDEQICFICAEGITYSCVLPCNHRMCHVCalrLRALYKTKECTFCKTEWD 125
Cdd:cd16756   1 ERELICPSCKELFTHPLILPCQHSVCHKC---VKELLTTFPCPGCQHDVD 47
RING-HC_EHV1-like cd23130
RING finger, HC subclass, found in Equid alphaherpesvirus 1 (Equine herpesvirus 1/EHV-1) ...
 80-128 1.51e-03

RING finger, HC subclass, found in Equid alphaherpesvirus 1 (Equine herpesvirus 1/EHV-1) regulatory protein and similar proteins; EHV-1 regulatory protein belongs to the Vmw110 (IPC0) protein family. It contains a typical C3HC4-type RING-HC finger and binds zinc stably.


Pssm-ID: 438492 [Multi-domain]  Cd Length: 51  Bit Score: 36.95  E-value: 1.51e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 63054452  80 ICFICAEGI-TYSCVLPCNHRMCHVCALRLRALYKTkeCTFCKTEWDTVL 128
Cdd:cd23130   2 VCPICLDDPeDEAITLPCLHQFCYTCILRWLQTSPT--CPLCKTPVTSII 49
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
 80-120 2.06e-03

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: 36.31  E-value: 2.06e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 63054452  80 ICFICAEGITYSCVLPCNHRMCHVCALRLRALyKTKECTFC 120
Cdd:cd16449   2 ECPICLERLKDPVLLPCGHVFCRECIRRLLES-GSIKCPIC 41
RING-HC_TRIM46_C-I cd16757
RING finger, HC subclass, found in tripartite motif-containing protein 46 (TRIM46) and similar ...
 76-105 2.07e-03

RING finger, HC subclass, found in tripartite motif-containing protein 46 (TRIM46) and similar proteins; TRIM46, also known as gene Y protein (GeneY) or tripartite, fibronectin type-III and C-terminal SPRY motif protein (TRIFIC), is a microtubule-associated protein that specifically localizes to the proximal axon, partly overlaps with the axon initial segment (AIS) at later stages, and organizes uniform microtubule orientation in axons. It controls neuronal polarity and axon specification by driving the formation of parallel microtubule arrays. TRIM46 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins, which 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, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, a PRY domain and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438415 [Multi-domain]  Cd Length: 43  Bit Score: 36.33  E-value: 2.07e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 63054452  76 EDEQICFICAEGITYSCVLPCNHRMCHVCA 105
Cdd:cd16757   2 ERELLCPVCKEMYKQPLVLPCMHNVCQVCA 31
RING-HC_RNF123 cd16541
RING finger, HC subclass, found in RING finger protein 123 (RNF123) and similar proteins; ...
 79-123 5.22e-03

RING finger, HC subclass, found in RING finger protein 123 (RNF123) and similar proteins; RNF123, also known as Kip1 ubiquitination-promoting complex protein 1 (KPC1), is an E3 ubiquitin-protein ligase that mediates ubiquitination and proteasomal processing of the nuclear factor-kappaB 1 (NF-kappaB1) precursor p105 to the p50 active subunit that restricts tumor growth. It also regulates degradation of heterochromatin protein 1alpha (HP1alpha) and 1beta (HP1beta) in lamin A/C knock-down cells. Moreover, RNF123, together with Kip1 ubiquitylation-promoting complex 2 (KPC2), forms the Kip1 ubiquitination-promoting complex (KPC), acting as a cytoplasmic ubiquitin ligase that regulates degradation of the cyclin-dependent kinase inhibitor p27 (Kip1) at the G1 phase of the cell cycle. RNF123 may also function as a clinically relevant, peripheral state marker of depression. RNF123 contains a C3HC4-type RING-HC finger at the C-terminus.


Pssm-ID: 438203 [Multi-domain]  Cd Length: 44  Bit Score: 35.35  E-value: 5.22e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 63054452  79 QICFICAEGITYSCVLPCNHRMCHVCAlrLRALYKTKECTFCKTE 123
Cdd:cd16541   1 DLCPICYAHPIDAVFLPCGHKSCRSCI--NRHLMNNKECFFCKAT 43
mRING-HC-C3HC5_MGRN1-like cd16789
Modified RING finger, HC subclass (C3HC5-type), found in mahogunin RING finger protein 1 ...
 81-121 5.33e-03

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


Pssm-ID: 438443 [Multi-domain]  Cd Length: 42  Bit Score: 35.36  E-value: 5.33e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 63054452  81 CFICAEGITYSCVLPCNHR-MCHVCALRLRalYKTKECTFCK 121
Cdd:cd16789   3 CVICLSDPRDTAVLPCRHLcLCSDCAEVLR--YQSNKCPICR 42
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 81-120 9.15e-03

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: 34.79  E-value: 9.15e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 63054452     81 CFICAEGITYSCV-LPCNHRMCHVCALRLRaLYKTKECTFC 120
Cdd:smart00184   1 CPICLEEYLKDPViLPCGHTFCRSCIRKWL-ESGNNTCPIC 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH