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Conserved domains on  [gi|1370469427|ref|XP_024306251|]
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RING finger and SPRY domain-containing protein 1 isoform X1 [Homo sapiens]

Protein Classification

RING finger and SPRY domain-containing protein 1( domain architecture ID 11596342)

RING finger and SPRY domain-containing protein 1 (RSPRY1) may be associated with a distinct skeletal dysplasia syndrome

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
390-510 5.83e-93

SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY domain is found at the N-terminus of RING finger domains which are present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RING-finger domain is a type of Zn-finger that binds two Zn atoms and is identified in proteins with a wide range of functions such as viral replication, signal transduction, and development.


:

Pssm-ID: 293941  Cd Length: 121  Bit Score: 281.16  E-value: 5.83e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370469427 390 GVWYYEVTVVTSGVMQIGWATRDSKFLNHEGYGIGDDEYSCAYDGCRQLIWYNARSKPHIHPCWKEGDTVGFLLDLNEKQ 469
Cdd:cd12883     1 GVWYYEVTVLTSGVMQIGWATKDSKFLNHEGYGIGDDEYSCAYDGCRQLIWYNAKSKPHTHPRWKPGDVLGCLLDLNKKQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1370469427 470 MIFFLNGNQLPPEKQVFSSTVSGFFAAASFMSYQQCEFNFG 510
Cdd:cd12883    81 MIFSLNGNRLPPERQVFTSAKSGFFAAASFMSFQQCEFNFG 121
RING-HC_RSPRY1 cd16566
RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) ...
554-596 4.34e-23

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: 92.04  E-value: 4.34e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1370469427 554 RENCCSLCCDEVADTQLKPCGHSDLCMDCALQLETCPLCRKEI 596
Cdd:cd16566     1 REDSCTLCFDKVADTELRPCGHSGFCMECALQLETCPLCRQPI 43
 
Name Accession Description Interval E-value
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
390-510 5.83e-93

SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY domain is found at the N-terminus of RING finger domains which are present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RING-finger domain is a type of Zn-finger that binds two Zn atoms and is identified in proteins with a wide range of functions such as viral replication, signal transduction, and development.


Pssm-ID: 293941  Cd Length: 121  Bit Score: 281.16  E-value: 5.83e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370469427 390 GVWYYEVTVVTSGVMQIGWATRDSKFLNHEGYGIGDDEYSCAYDGCRQLIWYNARSKPHIHPCWKEGDTVGFLLDLNEKQ 469
Cdd:cd12883     1 GVWYYEVTVLTSGVMQIGWATKDSKFLNHEGYGIGDDEYSCAYDGCRQLIWYNAKSKPHTHPRWKPGDVLGCLLDLNKKQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1370469427 470 MIFFLNGNQLPPEKQVFSSTVSGFFAAASFMSYQQCEFNFG 510
Cdd:cd12883    81 MIFSLNGNRLPPERQVFTSAKSGFFAAASFMSFQQCEFNFG 121
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
390-510 2.81e-24

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 98.14  E-value: 2.81e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370469427  390 GVWYYEVTVVTSGVMQIGWATRDSKFlnHEGYGIGDDEYSCAYDGCRQLIWYNARSKPHIHPCWKEGDTVGFLLDLNEKQ 469
Cdd:smart00449   2 GRHYFEVEIGDGGHWRVGVATKSVPR--GYFALLGEDKGSWGYDGDGGKKYHNSTGPEYGLPLQEPGDVIGCFLDLEAGT 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1370469427  470 MIFFLNGNQLpPEKQVFSSTVSG-FFAAASFMSYQQCEFNFG 510
Cdd:smart00449  80 ISFYKNGKYL-HGLAFFDVKFSGpLYPAFSLGSGNSVRLNFG 120
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
391-510 3.23e-23

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 95.10  E-value: 3.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370469427 391 VWYYEVTV--VTSGVMQIGWATRDSKFLNHEGygIGDDEYSCAYDGCRQLIWYNARSKPHIHPCWKEGDTVGFLLDLNEK 468
Cdd:pfam00622   1 RHYFEVEIfgQDGGGWRVGWATKSVPRKGERF--LGDESGSWGYDGWTGKKYWASTSPLTGLPLFEPGDVIGCFLDYEAG 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1370469427 469 QMIFFLNGNQLPPEKQVFSSTvSGFFAAASFMSYQQCEFNFG 510
Cdd:pfam00622  79 TISFTKNGKSLGYAFRDVPFA-GPLFPAVSLGAGEGLKFNFG 119
RING-HC_RSPRY1 cd16566
RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) ...
554-596 4.34e-23

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: 92.04  E-value: 4.34e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1370469427 554 RENCCSLCCDEVADTQLKPCGHSDLCMDCALQLETCPLCRKEI 596
Cdd:cd16566     1 REDSCTLCFDKVADTELRPCGHSGFCMECALQLETCPLCRQPI 43
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
554-599 2.90e-09

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 53.15  E-value: 2.90e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370469427 554 RENCCSLCCDEVADTQLKPCGHSDLCMDCALQLE----TCPLCRKEIVSR 599
Cdd:pfam13920   1 EDLLCVICLDRPRNVVLLPCGHLCLCEECAERLLrkkkKCPICRQPIESV 50
 
Name Accession Description Interval E-value
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
390-510 5.83e-93

SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY domain is found at the N-terminus of RING finger domains which are present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RING-finger domain is a type of Zn-finger that binds two Zn atoms and is identified in proteins with a wide range of functions such as viral replication, signal transduction, and development.


Pssm-ID: 293941  Cd Length: 121  Bit Score: 281.16  E-value: 5.83e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370469427 390 GVWYYEVTVVTSGVMQIGWATRDSKFLNHEGYGIGDDEYSCAYDGCRQLIWYNARSKPHIHPCWKEGDTVGFLLDLNEKQ 469
Cdd:cd12883     1 GVWYYEVTVLTSGVMQIGWATKDSKFLNHEGYGIGDDEYSCAYDGCRQLIWYNAKSKPHTHPRWKPGDVLGCLLDLNKKQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1370469427 470 MIFFLNGNQLPPEKQVFSSTVSGFFAAASFMSYQQCEFNFG 510
Cdd:cd12883    81 MIFSLNGNRLPPERQVFTSAKSGFFAAASFMSFQQCEFNFG 121
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
390-508 8.04e-33

SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L). B30.2 also contains residues in the N-terminus that form a distinct PRY domain structure; i.e. B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil or RBCC core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). TRIM/RBCC proteins are involved in a variety of processes, including apoptosis, cell cycle regulation, cell growth, senescence, viral response, meiosis, cell differentiation, and vesicular transport. Genes belonging to this family are implicated in several human diseases that vary from cancer to rare genetic syndromes. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site. While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Mutations found in the SPRY-containing proteins have shown to cause Mediterranean fever and Opitz syndrome.


Pssm-ID: 293931  Cd Length: 118  Bit Score: 122.15  E-value: 8.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370469427 390 GVWYYEVTVVT--SGVMQIGWATRDSKFLNHEGYGigDDEYSCAYDGCRQLIWYNARSKPHIHPcWKEGDTVGFLLDLNE 467
Cdd:cd11709     1 GKWYWEVRVDSgnGGLIQVGWATKSFSLDGEGGVG--DDEESWGYDGSRLRKGHGGSSGPGGRP-WKSGDVVGCLLDLDE 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1370469427 468 KQMIFFLNGNQLPPEKQVFSSTVSGFFAAASFMSYQQCEFN 508
Cdd:cd11709    78 GTLSFSLNGKDLGVAFTNLFLKGGGLYPAVSLGSGQGVTIN 118
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
380-510 1.52e-30

SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the N-terminus of RING finger protein 123 domain (also known as E3 ubiquitin-protein ligase RNF123). The ring finger domain motif is present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RNF123 displays E3 ubiquitin ligase activity toward the cyclin-dependent kinase inhibitor p27 (Kip1).


Pssm-ID: 293940  Cd Length: 128  Bit Score: 115.89  E-value: 1.52e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370469427 380 SVRCTFCVDAGVWYYEVTVVTSGVMQIGWATRDSKFLNHEgyGIGDDEYSCAYDGCRQLIWyNARSKPHIHPcWKEGDTV 459
Cdd:cd12882     1 SIRANACVYKGKWMYEVTLGTKGIMQIGWATISCRFTQEE--GVGDTRDSYAYDGNRVRKW-NVSTQKYGEP-WVAGDVI 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370469427 460 GFLLDLNEKQMIFFLNGNQLPPE-KQVFSSTVSGFFAAASFMSYQQCEFNFG 510
Cdd:cd12882    77 GCCIDLDKGTISFYRNGRSLGVAfDNVRRGPGLAYFPAVSLSFGERLELNFG 128
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
390-510 2.81e-24

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 98.14  E-value: 2.81e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370469427  390 GVWYYEVTVVTSGVMQIGWATRDSKFlnHEGYGIGDDEYSCAYDGCRQLIWYNARSKPHIHPCWKEGDTVGFLLDLNEKQ 469
Cdd:smart00449   2 GRHYFEVEIGDGGHWRVGVATKSVPR--GYFALLGEDKGSWGYDGDGGKKYHNSTGPEYGLPLQEPGDVIGCFLDLEAGT 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1370469427  470 MIFFLNGNQLpPEKQVFSSTVSG-FFAAASFMSYQQCEFNFG 510
Cdd:smart00449  80 ISFYKNGKYL-HGLAFFDVKFSGpLYPAFSLGSGNSVRLNFG 120
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
391-510 3.23e-23

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 95.10  E-value: 3.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370469427 391 VWYYEVTV--VTSGVMQIGWATRDSKFLNHEGygIGDDEYSCAYDGCRQLIWYNARSKPHIHPCWKEGDTVGFLLDLNEK 468
Cdd:pfam00622   1 RHYFEVEIfgQDGGGWRVGWATKSVPRKGERF--LGDESGSWGYDGWTGKKYWASTSPLTGLPLFEPGDVIGCFLDYEAG 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1370469427 469 QMIFFLNGNQLPPEKQVFSSTvSGFFAAASFMSYQQCEFNFG 510
Cdd:pfam00622  79 TISFTKNGKSLGYAFRDVPFA-GPLFPAVSLGAGEGLKFNFG 119
RING-HC_RSPRY1 cd16566
RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) ...
554-596 4.34e-23

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: 92.04  E-value: 4.34e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1370469427 554 RENCCSLCCDEVADTQLKPCGHSDLCMDCALQLETCPLCRKEI 596
Cdd:cd16566     1 REDSCTLCFDKVADTELRPCGHSGFCMECALQLETCPLCRQPI 43
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
384-510 7.22e-21

SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, The SPRY2 domain has been shown to bind to the dihydropryidine receptor (DHPR) II-III loop and the ASI region of RyR1


Pssm-ID: 240458  Cd Length: 133  Bit Score: 88.90  E-value: 7.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370469427 384 TFCVDAGVWYYEVTVVTSGVMQIGWATRDSkflnHEGYGIGDDEYSCAYDGCRQLIWYNARSkpHIHPCWKEGDTVGFLL 463
Cdd:cd12878     8 TYAVTSGKWYFEFEVLTSGYMRVGWARPGF----RPDLELGSDDLSYAFDGFLARKWHQGSE--SFGKQWQPGDVVGCML 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370469427 464 DLNEKQMIFFLNGNQLppEKQVFSSTV-------SGFFAAASFMSYQQCEFNFG 510
Cdd:cd12878    82 DLVDRTISFTLNGELL--IDSSGSEVAfkdieigEGFVPACSLGVGQKGRLNLG 133
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
362-515 4.90e-16

SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or homeotic discs 2) -like proteins, core components of all mixed-lineage leukemia (MLL) family histone methyltransferases. Ash2 is a member of the trithorax group of transcriptional regulators of the Hox genes. Recent studies show that the SPRY domain of Ash2 mediates the interaction with RbBP5 and has an important role in regulating the methyltransferase activity of MLL complexes. In yeast, Ash2 is involved in histone methylation and is required for the earliest stages of embryogenesis.


Pssm-ID: 293932  Cd Length: 150  Bit Score: 75.63  E-value: 4.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370469427 362 LKISPHGLEARCDaSSFESVRCTFCVDAGVWYYEVTVVTSGVMQ-----IGWATRDSKFlnheGYGIGDDEYSCAY---D 433
Cdd:cd12872     1 LKLSEDRLTVTGE-KGYRMARANHGVREGKWYFEVKILEGGGTEtghvrVGWSRREASL----QAPVGYDKYSYAIrdkD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370469427 434 GCrqlIWYNARSKPHIHPCWKEGDTVGFLLDLNEkqMIFFLNG-NQ------LPPEKqvfsstvsGFFAAAS-FMSyQQC 505
Cdd:cd12872    76 GS---KFHQSRGKPYGEPGFKEGDVIGFLITLPK--IEFFKNGkSQgvafedIYGTG--------GYYPAVSlYKG-ATV 141
                         170
                  ....*....|
gi 1370469427 506 EFNFGaKPFK 515
Cdd:cd12872   142 TINFG-PDFK 150
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
353-513 3.21e-15

SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD box gene, DDX1, an RNA-dependent ATPase involved in HIV-1 Rev function and virus replication. It is suggested that DDX1 acts as a cellular cofactor by promoting oligomerization of Rev on the Rev response element (RRE). DDX1 RNA is overexpressed in breast cancer, data showing a strong and independent association between poor prognosis and deregulation of the DEAD box protein DDX1, thus potentially serving as an effective prognostic biomarker for early recurrence in primary breast cancer. DDX1 also interacts with RelA and enhances nuclear factor kappaB-mediated transcription. DEAD-box proteins are associated with all levels of RNA metabolism and function, and have been implicated in translation initiation, transcription, RNA splicing, ribosome assembly, RNA transport, and RNA decay.


Pssm-ID: 293933  Cd Length: 155  Bit Score: 73.38  E-value: 3.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370469427 353 LNSNDVSEYLKISPHGLEARC-DASSFESVRCTFCV-DAGVWYYEVTVVTSGVMQIGWATRDSKFlnhegyGIGDDEYSC 430
Cdd:cd12873     1 MNPYDRDAALAISPDGLLCQSrEEKGWQGCRATKGVkGKGKYYYEVTVTDEGLCRVGWSTEDASL------DLGTDKFGF 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370469427 431 AYDG------CRQLIWYnarSKPHIHpcwkeGDTVGFLLDLNEKQMIFFLNGNQLPPEKQVFSSTV-SGFFAAASfMSYQ 503
Cdd:cd12873    75 GYGGtgkkshGRQFDDY---GEPFGL-----GDVIGCYLDLDNGTISFSKNGKDLGKAFDIPPHLRnSALFPAVC-LKNA 145
                         170
                  ....*....|
gi 1370469427 504 QCEFNFGAKP 513
Cdd:cd12873   146 EVEFNFGDKP 155
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
392-510 5.19e-11

SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, but no specific function has been found for this first SPRY domain of the RyRs.


Pssm-ID: 240457  Cd Length: 151  Bit Score: 61.17  E-value: 5.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370469427 392 WYYEVTV--VTSGVMQ-----IGWAT---RDSKFLNHEGYG---IGDDEYSCAYDGCRqlIWYNARSK---PHIHPCWKE 455
Cdd:cd12877    20 WYFEVEVdhVEQFTHQpahlrVGWANtsgYVPYPGGGEGWGgngVGDDLYSYGFDGLH--LWTGGRSRrvtSGTQHLLKK 97
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370469427 456 GDTVGFLLDLNEKQMIFFLNGNQLPPEKQVFSSTVsGFFAAASFMSYQQCEFNFG 510
Cdd:cd12877    98 GDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDG-MFFPVMSFSAGVSCRFLLG 151
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
554-599 2.90e-09

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 53.15  E-value: 2.90e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370469427 554 RENCCSLCCDEVADTQLKPCGHSDLCMDCALQLE----TCPLCRKEIVSR 599
Cdd:pfam13920   1 EDLLCVICLDRPRNVVLLPCGHLCLCEECAERLLrkkkKCPICRQPIESV 50
mRING-HC-C3HC5_NEU1 cd16647
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein NEURL1A, ...
558-601 1.58e-08

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: 51.14  E-value: 1.58e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1370469427 558 CSLCCDEVADTQLKPCGHSDLCMDCALQL----ETCPLCRKEIVSRIR 601
Cdd:cd16647     4 CVICYERPVDTVLYRCGHMCMCYDCALQLkrrgGSCPICRAPIKDVIK 51
RING-HC_MYLIP cd16523
RING finger, HC subclass, found in myosin regulatory light chain interacting protein (MYLIP) ...
558-596 6.04e-08

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: 49.49  E-value: 6.04e-08
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1370469427 558 CSLCCDEVADTQLKPCGHSDLCMDCALQLETCPLCRKEI 596
Cdd:cd16523     5 CMVCCEEEINSAFCPCGHMVCCESCAAQLQSCPVCRSRV 43
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
387-510 7.70e-08

SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY domains found in Ran binding proteins (RBP or RanBPM) 9 and 10, SSH4 (suppressor of SHR3 null mutation protein 4), SPRY domain-containing protein 3 (SPRYD3) as well as HECT, a C-terminal catalytic domain of a subclass of ubiquitin-protein ligase (E3). RanBP9 and RanBP10 act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. The SPRY domain in SSH4 may be involved in cargo recognition, either directly or by combination with other adaptors, possibly leading to a higher selectivity. SPRYD3 is highly expressed in most tissues in humans, possibly involved in important cellular processes. HECT E3 mediates the direct transfer of ubiquitin from E2 to substrate.


Pssm-ID: 293943  Cd Length: 132  Bit Score: 51.51  E-value: 7.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370469427 387 VDAGVWYYEVTVV---TSGVMQIGWATRDSKFLNHegygIGDDEYSCAY---DGCrqlIWYNARSKPHIHPCWKEGDTVG 460
Cdd:cd12885    11 PKVPVFYFEVTILdlgEKGIVSIGFCTSGFPLNRM----PGWEDGSYGYhgdDGR---VYLGGGEGENYGPPFGTGDVVG 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370469427 461 FLLDLNEKQMIFFLNGNQLPPekqVFSSTVSG-FFAAASFmSYQQCEF--NFG 510
Cdd:cd12885    84 CGINFKTGEVFFTKNGELLGT---AFENVVKGrLYPTVGL-GSPGVKVrvNFG 132
RING-HC_CARP cd16500
RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein CARP-1, ...
556-601 1.26e-07

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: 48.15  E-value: 1.26e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1370469427 556 NCCSLCCDEVADTQLKPCGHSDLCMDCALQLETCPLCRKEIVSRIR 601
Cdd:cd16500     1 DLCKICMDAAIDCVLLECGHMVTCTDCGKKLSECPICRQYVVRVVH 46
RING-HC_IAPs cd16510
RING finger, HC subclass, found in inhibitor of apoptosis proteins (IAPs); IAPs are frequently ...
555-594 2.35e-07

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: 47.25  E-value: 2.35e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1370469427 555 ENCCSLCCDEVADTQLKPCGHSDLCMDCALQLETCPLCRK 594
Cdd:cd16510     1 EKLCKICMDREVNIVFLPCGHLVTCAQCAASLRKCPICRT 40
RING-HC_LRSAM1 cd16515
RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing ...
558-601 8.26e-07

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: 46.13  E-value: 8.26e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1370469427 558 CSLCCDEVADTQLKPCGHSDLCMDCALQLETCPLCRKEIVSRIR 601
Cdd:cd16515     4 CVVCMDAESQVIFLPCGHVCCCQTCSSSLSTCPLCRADITQRVR 47
RING-HC_BIRC2_3_7 cd16713
RING finger, HC subclass, found in apoptosis protein c-IAP1, c-IAP2, livin, and similar ...
555-601 1.76e-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: 45.16  E-value: 1.76e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1370469427 555 ENCCSLCCDEVADTQLKPCGHSDLCMDCALQLETCPLCRKEIVSRIR 601
Cdd:cd16713     7 ERTCKVCMDKEVSIVFIPCGHLVVCTECAPSLRKCPICRATIKGTVR 53
RING-HC_XBAT35-like cd23129
RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and ...
558-601 1.94e-06

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: 44.95  E-value: 1.94e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1370469427 558 CSLCCDEVADTQLKPCGHSDLCMDCALQL----ETCPLCRKEIVSRIR 601
Cdd:cd23129     5 CVVCMDAPRDAVCVPCGHVAGCMSCLKALmqssPLCPICRAPVRQVIK 52
RING-HC_NEURL3 cd16552
RING finger, HC subclass, found in neuralized-like protein 3 (NEURL3) and similar proteins; ...
558-596 6.10e-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: 43.76  E-value: 6.10e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1370469427 558 CSLCCDEVADTQLKPCGHSDLCMDCALQL----ETCPLCRKEI 596
Cdd:cd16552     4 CAICFHHTANTRLVPCGHSHFCGSCAWHIfrdtARCPVCRWQI 46
RING-HC_CARP1 cd16706
RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein 1 (CARP1) ...
555-600 1.57e-05

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: 42.70  E-value: 1.57e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1370469427 555 ENCCSLCCDEVADTQLKPCGHSDLCMDCALQLETCPLCRKEIVSRI 600
Cdd:cd16706     4 DNLCRICMDAVIDCVLLECGHMVTCTKCGKRMSECPICRQYVVRAV 49
RING-HC_MIBs cd16519
RING finger, HC subclass, found in mind bomb MIB1, MIB2, and similar proteins; MIBs are large, ...
558-593 1.66e-05

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: 42.08  E-value: 1.66e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1370469427 558 CSLCCDEVADTQLKPCGHSDLCMDCALQLETCPLCR 593
Cdd:cd16519     3 CRVCSDKKALVLFQPCGHVVACEECSLRMKKCLQCK 38
mRING-HC-C3HC5_NEU1B cd16786
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1B (NEURL1B); ...
558-601 1.72e-05

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: 42.63  E-value: 1.72e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370469427 558 CSLCCDEVADTQLKPCGHSDLCMDCALQLE-----TCPLCRKEIVSRIR 601
Cdd:cd16786     5 CTVCFDSEVDTVIYTCGHMCLCNSCGLKLKrqinaCCPICRRVIKDVIK 53
mRING-HC-C3HC5_NEU1A cd16785
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1A (NEURL1A) ...
558-601 2.61e-05

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: 42.28  E-value: 2.61e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370469427 558 CSLCCDEVADTQLKPCGHSDLCMDCALQLE-----TCPLCRKEIVSRIR 601
Cdd:cd16785     7 CTICYENAVDTVIYTCGHMCLCYACGLRLKkmlnaCCPICRRAIKDIIK 55
RING-HC_CARP2 cd16707
RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein 2 (CARP-2) ...
555-600 5.33e-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: 41.12  E-value: 5.33e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1370469427 555 ENCCSLCCDEVADTQLKPCGHSDLCMDCALQLETCPLCRKEIVSRI 600
Cdd:cd16707     2 ENLCKICMDSPIDCVLLECGHMVTCTKCGKRMSECPICRQYVIRAV 47
RING-HC_CblA-like cd16501
RING finger, HC subclass, found in Dictyostelium discoideum Cbl-like protein A (CblA) and ...
556-603 5.56e-05

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: 40.93  E-value: 5.56e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1370469427 556 NCCSLCCDEVADTQLKPCGHSDLCMDCALQLETCPLCRKEIvSRIRQI 603
Cdd:cd16501     6 DLCVVCMDAPIDTVFLECGHLACCRLCSKRLRVCPICRQPI-SRVVRI 52
RING-HC_MEX3B cd16721
RING finger, HC subclass, found in RNA-binding protein MEX3B; MEX3B, also known as RING finger ...
558-604 6.29e-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: 41.20  E-value: 6.29e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370469427 558 CSLCCDEVADTQLKPCGHSDLCMDCALQL-----ETCPLCRKEIVSRIRQIS 604
Cdd:cd16721     7 CSICFESEVIAALVPCGHNLFCMECANRIceknePQCPVCHAAVTQAIRIFS 58
RING-HC_BIRC4_8 cd16714
RING finger, HC subclass, found in E3 ubiquitin-protein ligase XIAP, baculoviral IAP ...
554-601 6.56e-05

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: 41.28  E-value: 6.56e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1370469427 554 RENCCSLCCDEVADTQLKPCGHSDLCMDCALQLETCPLCRKEIVSRIR 601
Cdd:cd16714    13 EEKLCKICMDRNISIVFIPCGHLVTCKQCAEALDKCPICCTVITFKQK 60
RING-HC_MEX3 cd16518
RING finger, HC subclass, found in RNA-binding proteins of the evolutionarily-conserved MEX-3 ...
558-601 6.60e-05

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: 40.81  E-value: 6.60e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370469427 558 CSLCCDEVADTQLKPCGHSDLCMDCALQL-----ETCPLCRKEIVSRIR 601
Cdd:cd16518     3 CVVCFESEVVAALVPCGHNLFCMECANRIceksdPECPVCHTPVTQAIR 51
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
362-513 7.80e-05

SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1 (also known as HNRPUL1 ) which is a major constituent of nuclear matrix or scaffold and binds directly to DNA sequences through the N-terminal acidic region named serum amyloid P (SAP). Its function is specifically modulated by E1B-55kDa in adenovirus-infected cells. HNRPUL1 also participates in ATR protein kinase signaling pathways during adenovirus infection. Two transcript variants encoding different isoforms have been found for this gene. When associated with bromodomain-containing protein 7 (BRD7), it activates transcription of glucocorticoid-responsive promoter in the absence of ligand-stimulation.


Pssm-ID: 293942  Cd Length: 177  Bit Score: 43.73  E-value: 7.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370469427 362 LKISPHGLEARCD-----ASSFESVRCTFCVDAGVWYYEVTVV-------------TSGVMQIGWATRDSKFLnhegygI 423
Cdd:cd12884    12 LKISKDRYSASPLtdegfAYLWAGARATYGVTKGKVCFEVKVTenlpvkhlpteetDPHVVRVGWSVDSSSLQ------L 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370469427 424 GDDEYSCAYDGcRQLIWYNARSKPHIHPcWKEGDTVGFLLDLN--EKQMIFFLNGNQLPPEKQVFSSTVSGffaAASF-- 499
Cdd:cd12884    86 GEEEFSYGYGS-TGKKSTNCKFEDYGEP-FGENDVIGCYLDFEsePVEISFSKNGKDLGVAFKISKEELGG---KALFph 160
                         170
                  ....*....|....*.
gi 1370469427 500 --MSYQQCEFNFGAKP 513
Cdd:cd12884   161 vlTKNCAVEVNFGQKE 176
RING-HC_MEX3D cd16723
RING finger, HC subclass, found in RNA-binding protein MEX3D; MEX3D, also known as RING finger ...
552-604 8.02e-05

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: 41.06  E-value: 8.02e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370469427 552 SIREncCSLCCDEVADTQLKPCGHSDLCMDCALQL-----ETCPLCRKEIVSRIRQIS 604
Cdd:cd16723     9 SARE--CVVCFESEVIAALVPCGHNLFCMECAIRIcgksePECPACHTPATQAIHIFS 64
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
557-592 8.34e-05

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: 40.16  E-value: 8.34e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1370469427 557 CCSLCCDEVADTQLKPCGHSdLCMDCALQL-----ETCPLC 592
Cdd:cd16449     2 ECPICLERLKDPVLLPCGHV-FCRECIRRLlesgsIKCPIC 41
RING-HC_TRIM9-like_C-I cd16576
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM9, TRIM67, and ...
558-594 1.03e-04

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM9, TRIM67, and similar proteins; Tripartite motif-containing proteins TRIM9 and TRIM67 belong 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, consisting of three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. TRIM9 (the human ortholog of rat Spring), also known as RING finger protein 91 (RNF91), is a brain-specific E3 ubiquitin-protein ligase collaborating with an E2 ubiquitin conjugating enzyme UBCH5b. TRIM9 plays an important role in the regulation of neuronal functions and participates in neurodegenerative disorders through its ligase activity. TRIM67, also known as TRIM9-like protein (TNL), is a protein selectively expressed in the cerebellum. It interacts with PRG-1, an important molecule in the control of hippocampal excitability dependent on presynaptic LPA2 receptor signaling, and 80K-H, also known as glucosidase II beta, a protein kinase C substrate.


Pssm-ID: 438238 [Multi-domain]  Cd Length: 42  Bit Score: 40.09  E-value: 1.03e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1370469427 558 CSLCCDEVADTQLKPCGHSdLCMDCALQLE-TCPLCRK 594
Cdd:cd16576     6 CPVCGSLFTEPVILPCSHN-LCLGCALNIQlTCPICHK 42
SPRY_like cd12886
SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ...
390-510 1.46e-04

SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in bacterial and are mostly uncharacterized. SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 eukaryotic protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L).


Pssm-ID: 293944  Cd Length: 129  Bit Score: 42.11  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370469427 390 GVWYYEVTVVTSGV---MQIGWA----TRDSKFLNHEGYGIGDDEYScaYDGcrqLIWYNARSKPHIHPCWKEGDTVGFL 462
Cdd:cd12886     1 GKWYWEVTVVSSAAstyAGIGVAnaaaTGNNGLNGIELSSIGYSLGV--YSG---NKLSNGSSVATYGAGFTAGDVIGVA 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370469427 463 LDLNEKQMIFFLNG------NQLPPEKQVFSSTvsGFFAAASFMSYQQCEF--NFG 510
Cdd:cd12886    76 LDLDAGKIWFYKNGvwqgggDPAPGTNPAFAGT--AMYPAVTGGSSTGGSFtaNFG 129
RING-HC_MEX3C cd16722
RING finger, HC subclass, found in RNA-binding protein MEX3C; MEX3C, also known as RING finger ...
558-601 2.00e-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: 39.58  E-value: 2.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370469427 558 CSLCCDEVADTQLKPCGHSDLCMDCALQ-----LETCPLCRKEIVSRIR 601
Cdd:cd16722     4 CVICFENEVIAALVPCGHNLFCMECANKicekeTPSCPVCQTAVTQAIQ 52
RING-HC_RGLG_plant cd16729
RING finger, HC subclass, found in RING domain ligase RGLG1, RGLG2 and similar proteins from ...
558-601 2.23e-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: 39.00  E-value: 2.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1370469427 558 CSLCCDEVADTQLKpCGHSDlCMDCALQLETCPLCRKEIVSRIR 601
Cdd:cd16729     5 CPICLSNPKDMAFG-CGHQT-CCECGQSLTHCPICRQPITTRIK 46
RING-HC_EHV1-like cd23130
RING finger, HC subclass, found in Equid alphaherpesvirus 1 (Equine herpesvirus 1/EHV-1) ...
558-602 4.24e-04

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: 38.49  E-value: 4.24e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370469427 558 CSLCCDEVAD-TQLKPCGHSdLCMDCAL----QLETCPLCRKEIVSRIRQ 602
Cdd:cd23130     3 CPICLDDPEDeAITLPCLHQ-FCYTCILrwlqTSPTCPLCKTPVTSIIHS 51
SPRYD7 cd12880
SPRY domain-containing protein 7; This family contains SPRY domain-containing protein 7 (also ...
393-480 4.35e-04

SPRY domain-containing protein 7; This family contains SPRY domain-containing protein 7 (also known as SPRY domain-containing protein 7 or CLL deletion region gene 6 protein homolog or CLLD6 or chronic lymphocytic leukemia deletion region gene 6 protein homolog). In humans, CLLD6 is highly expressed in heart, skeletal muscle, and testis as well as cancer cell lines. It also has cross-species conservation, suggesting that it is likely to carry out important cellular processes.


Pssm-ID: 293938  Cd Length: 160  Bit Score: 41.03  E-value: 4.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370469427 393 YYEVTVVTSGVMQIGWATRDSKFLNHEGygiGDDEYSCA--YDGCrqlIWYNARSKPHIHPCWKEGDTVGFLLD---LNe 467
Cdd:cd12880    32 YFEVKIQSTGVWGVGLATRKTDLNRVPL---GNDAESWVlrSDGT---IWHNGEVIHKLKQLVEEGDVIGVTYDhveLN- 104
                          90
                  ....*....|...
gi 1370469427 468 kqmiFFLNGNQLP 480
Cdd:cd12880   105 ----FYLNGKPLD 113
mRING-HC-C3HC5_CGRF1-like cd16649
Modified RING finger, HC subclass (C3HC5-type), found in RING finger proteins, RNF26, RNF197 ...
558-593 4.63e-04

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: 38.07  E-value: 4.63e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1370469427 558 CSLCCDEVADTQLKPCGHSDLCMDCALQL--ETCPLCR 593
Cdd:cd16649     3 CVVCLENPASVLLLPCRHLCLCEVCAKGLrgKTCPICR 40
Prok-RING_4 pfam14447
Prokaryotic RING finger family 4; RING finger family domain found sporadically in bacteria. ...
558-596 5.35e-04

Prokaryotic RING finger family 4; RING finger family domain found sporadically in bacteria. The finger is fused to an N-terminal alpha-helical domain, ROT/Trove-like repeats and a C-terminal TerD domain. The architecture suggests a possible role in an RNA-processing complex.


Pssm-ID: 433959 [Multi-domain]  Cd Length: 46  Bit Score: 38.18  E-value: 5.35e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1370469427 558 CSLCCDEVADTQLKPCGHSdLCMDC--ALQLETCPLCRKEI 596
Cdd:pfam14447   1 CVLCGRNGTVHALIPCGHL-VCRDCfdGSDFSACPICRRRI 40
mRING-HC-C3HC5_MGRN1-like cd16789
Modified RING finger, HC subclass (C3HC5-type), found in mahogunin RING finger protein 1 ...
558-593 5.52e-04

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: 37.67  E-value: 5.52e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1370469427 558 CSLCCDEVADTQLKPCGHSDLCMDCALQLET----CPLCR 593
Cdd:cd16789     3 CVICLSDPRDTAVLPCRHLCLCSDCAEVLRYqsnkCPICR 42
RING-HC_MIB1_rpt1 cd16724
first RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also ...
558-593 5.81e-04

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: 37.85  E-value: 5.81e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1370469427 558 CSLCCDEVADTQLKPCGHSDLCMDCALQLETCPLCR 593
Cdd:cd16724     3 CMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICK 38
RING-HC_MIBs-like cd16520
RING finger, HC subclass, found in mind bomb MIB1, MIB2, RGLG1, RGLG2, and similar proteins; ...
557-596 6.80e-04

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: 37.65  E-value: 6.80e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1370469427 557 CCSLCCDEVADTQLKpCGHSdLCMDCALQLETCPLCRKEI 596
Cdd:cd16520     2 LCPICMERKKNVVFL-CGHG-TCQKCAEKLKKCPICRKPI 39
RING-HC_MIP1-like cd23128
RING finger, HC subclass, found in Arabidopsis thaliana MND1-interacting protein 1 (MIP1) and ...
554-601 7.50e-04

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


Pssm-ID: 438490 [Multi-domain]  Cd Length: 55  Bit Score: 37.87  E-value: 7.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370469427 554 RENCCSLCCDEVADTQLKPCGHSDLCMDCALQLE-----TCPLCRKEIVSRIR 601
Cdd:cd23128     2 RERECVMCMEEERSVVFLPCAHQVVCSGCNDLHEkkgmrECPSCRGEIQERIR 54
SPRY_SOCS3 cd12876
SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY ...
381-476 1.09e-03

SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY domain-containing SOCS box protein family (SPSB1-4, also known as SSB-1 to -4) is composed of a central SPRY protein interaction domain and a C-terminal SOCS box. All four SPSB proteins interact with c-Met, the hepatocyte growth factor receptor, but SOCS3 regulates cellular response to a variety of cytokines such as leukemia inhibitory factor (LIF) and interleukin 6. SOCS3, along with SOCS1, are expressed by immune cells and cells of the central nervous system (CNS) and have the potential to impact immune processes within the CNS. In non-small cell lung cancer (NSCLC), SOCS3 is silenced and proline-rich tyrosine kinase 2 (Pyk2) is over-expressed; it has been suggested that SOCS3 could be an effective way to prevent the progression of NSCLC due to its role in regulating Pyk2 expression.


Pssm-ID: 293936  Cd Length: 185  Bit Score: 40.22  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370469427 381 VRCTFCVDAGVWYYEVTVV-----TSgvMQIGWATRDSKfLNHEGY----GIGDDEYSC--AYDGcrqLIWYNARSKPHI 449
Cdd:cd12876    35 VRGTKPLTNGQHYWEIKMSspvygTD--MMVGVGTKKAD-LHAYRYefcsLLGEDEESWglSYKG---LLWHDGQSRPYT 108
                          90       100
                  ....*....|....*....|....*..
gi 1370469427 450 HPCWKEGDTVGFLLDLNEKQMIFFLNG 476
Cdd:cd12876   109 SPFGNQGTIIGVHLDMWRGTLTFYKNG 135
RING-HC_MEX3A cd16720
RING finger, HC subclass, found in RNA-binding protein MEX3A; MEX3A, also known as RING finger ...
558-604 1.52e-03

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: 37.25  E-value: 1.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370469427 558 CSLCCDEVADTQLKPCGHSDLCMDCALQL-----ETCPLCRKEIVSRIRQIS 604
Cdd:cd16720     5 CMVCFESEVTAALVPCGHNLFCMECAVRIcernePECPVCHALATQAIRIFS 56
RING-HC_ZNF598 cd16615
RING finger, HC subclass, found in zinc finger protein 598 (ZNF598) and similar proteins; ...
556-596 1.68e-03

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: 36.82  E-value: 1.68e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1370469427 556 NCCSLCCDEVADTQLKPCGHSdLCMDCALQLET------CPLCRKEI 596
Cdd:cd16615     1 ETCVICCEEIEYFAVGPCNHP-VCYKCSLRMRVlykdkyCPICRTEL 46
RING-HC_XBAT31-like cd23144
RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 1 (XBAT31) and ...
555-598 2.75e-03

RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 1 (XBAT31) and similar proteins; XBAT31, also called ankyrin repeat domain and RING finger-containing protein XBAT31, or RING-type E3 ubiquitin transferase XB31, has no E3 ubiquitin-protein ligase activity observed when associated with the E2 enzyme UBC8 in vitro. XBAT31 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438506  Cd Length: 65  Bit Score: 36.45  E-value: 2.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370469427 555 ENCCSLCCDEVADTQLKPCGHSdLCMDCALQL---------------ETCPLCRKEIVS 598
Cdd:cd23144     6 EDVCCICFEHLCTIEIKDCGHQ-MCATCALKLcchnkpnpssspprpPACPFCRQDIAS 63
RING-HC_RNF168 cd16550
RING finger, HC subclass, found in RING finger protein 168 (RNF168) and similar proteins; ...
558-598 2.90e-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: 35.81  E-value: 2.90e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1370469427 558 CSLCCDEVADTQLKPCGHSdLCMDCALQ-LE----TCPLCRKEIVS 598
Cdd:cd16550     3 CPICLEILVEPVTLPCNHT-LCMPCFQStVEkaslCCPLCRLRISS 47
RING-HC_MIB2_rpt1 cd16726
first RING finger, HC subclass, found in mind bomb 2 (MIB2) and similar proteins; MIB2, also ...
558-592 3.02e-03

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: 35.50  E-value: 3.02e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1370469427 558 CSLCCDEVADTQLKPCGHSDLCMDCALQLETCPLC 592
Cdd:cd16726     3 CLVCSELAALVRFEPCQHSIVCEECARRMKKCIKC 37
RING-HC_Cbl-c cd16710
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-c and similar proteins; ...
558-599 3.05e-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: 36.60  E-value: 3.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1370469427 558 CSLCCDEVADTQLKPCGHSdLCMDC--ALQ---LETCPLCRKEIVSR 599
Cdd:cd16710    16 CKICAERDKDVRIEPCGHL-LCSCClaAWQhsdSQTCPFCRCEIKGR 61
RING-HC_Cbl-like cd16502
RING finger, HC subclass, found in Casitas B-lineage lymphoma (Cbl) proteins; The Cbl adaptor ...
558-593 3.07e-03

RING finger, HC subclass, found in Casitas B-lineage lymphoma (Cbl) proteins; The Cbl adaptor protein family contains a small class of RING-type E3 ubiquitin ligases with oncogenic activity, which is represented by three mammalian members, c-Cbl, Cbl-b and Cbl-c, as well as two invertebrate Cbl-family proteins, D-Cbl in Drosophila and Sli-1 in C. elegans. Cbl proteins function as potent negative regulators of various signaling cascades in a wide range of cell types. They play roles in ubiquitinating activated tyrosine kinases and targeting them for degradation. D-Cbl associates with the Drosophila epidermal growth factor receptor (EGFR) and overexpression of D-Cbl in the eye of Drosophila embryos inhibits EGFR-dependent photoreceptor cell development. Sli-1 is a negative regulator of the Let-23 receptor tyrosine kinase, an EGFR homolog, in vulva development. Cbl proteins in this subfamily consist of a highly conserved N-terminal half that includes 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) and a C3HC4-type RING-HC finger, both of which are required for Cbl-mediated downregulation of RTKs, and a divergent C-terminal region.


Pssm-ID: 438165 [Multi-domain]  Cd Length: 43  Bit Score: 35.79  E-value: 3.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1370469427 558 CSLCCDEVADTQLKPCGHSdLCMDCALQLE-----TCPLCR 593
Cdd:cd16502     4 CKICAENDKDVRIEPCGHL-LCTPCLTSWQdsdgqTCPFCR 43
zf-RING_2 pfam13639
Ring finger domain;
556-593 3.11e-03

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 35.85  E-value: 3.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1370469427 556 NCCSLCCDEV---ADTQLKPCGHSdLCMDCALQL----ETCPLCR 593
Cdd:pfam13639   1 DECPICLEEFeegDKVVVLPCGHH-FHRECLDKWlrssNTCPLCR 44
mRING-HC-C3HC5_CGRF1 cd16787
Modified RING finger, HC subclass (C3HC5-type), found in cell growth regulator with RING ...
558-593 3.79e-03

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: 35.42  E-value: 3.79e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1370469427 558 CSLCCDEVADTQLKPCGHSDLCMDCALQLETCPLCR 593
Cdd:cd16787     3 CVVCQNAPVNRVLLPCRHACVCDECFKRLQRCPMCR 38
vRING-HC-C4C4_RBBP6 cd16620
Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) ...
557-598 3.98e-03

Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) and similar proteins; RBBP6, also known as proliferation potential-related protein, protein P2P-R, retinoblastoma-binding Q protein 1 (RBQ-1), or p53-associated cellular protein of testis (PACT), is a nuclear E3 ubiquitin-protein ligase involved in multiple processes, such as the control of gene expression, mitosis, cell differentiation, and cell apoptosis. It plays a role in both promoting and inhibiting apoptosis in many human cancers, including esophageal, lung, hepatocellular, and colon cancers, familial myeloproliferative neoplasms, as well as in human immunodeficiency virus-associated nephropathy (HIVAN). It functions as an Rb- and p53-binding protein that plays an important role in chaperone-mediated ubiquitination and possibly in protein quality control. It acts as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in an increase of MDM2-mediated ubiquitination and degradation of p53/TP53, and leading to both apoptosis and cell growth. It is also a double-stranded RNA-binding protein that plays a role in mRNA processing by regulating the human polyadenylation machinery and modulating expression of mRNAs with AU-rich 3' untranslated regions (UTRs). Moreover, RBBP6 ubiquitinates and destabilizes the transcriptional repressor ZBTB38 that negatively regulates transcription and levels of the MCM10 replication factor on chromatin. Furthermore, RBBP6 is involved in tunicamycin-induced apoptosis by mediating protein kinase (PKR) activation. RBBP6 contains an N-terminal ubiquitin-like domain and a C4C4-type RING finger, whose overall folding is similar to that of the typical C3HC4-type RING-HC finger. RBBP6 interacts with chaperones Hsp70 and Hsp40 through its N-terminal ubiquitin-like domain. It promotes the ubiquitination of p53 by Hdm2 in an E4-like manner through its RING finger. It also interacts directly with the pro-proliferative transcription factor Y-box-binding protein-1 (YB-1) via its RING finger.


Pssm-ID: 438282 [Multi-domain]  Cd Length: 55  Bit Score: 35.84  E-value: 3.98e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1370469427 557 CCSLCCDEVADTQLKPCGHSDLCMDCALQLE-----TCPLCRKEIVS 598
Cdd:cd16620     5 KCPICKDLMKDAVLTPCCGNSFCDECIRTALleedfTCPTCKEPDVS 51
mRING-HC-C3HC5_RNF26 cd16788
Modified RING finger, HC subclass (C3HC5-type), found in RING finger protein 26 (RNF26) and ...
558-596 7.18e-03

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


Pssm-ID: 438442 [Multi-domain]  Cd Length: 60  Bit Score: 35.08  E-value: 7.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1370469427 558 CSLCCDEVADTQLKPCGHSDLCMDCALQLET-------CPLCRKEI 596
Cdd:cd16788     8 CVICQDQSKTVLILPCRHMCLCRQCANILLQqpvyrrnCPLCRTMI 53
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
374-480 7.26e-03

SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding protein (RBP or RanBPM) 9 and 10, and similar proteins. RanBP9 (also known as RanBPM), a binding partner of Ran, is a small Ras-like GTPase that exerts multiple functions via interactions with various proteins. RanBP9 and RanBP10 also act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. SPRY domain of RanBPM forms a complex with CD39, a prototypic member of the NTPDase family, thus down-regulating activity substantially. RanBP10 enhances the transcriptional activity of AR in a ligand-dependent manner and exhibits a protein expression pattern different from RanBPM in various cell lines. RanBP10 is highly expressed in AR-positive prostate cancer LNCaP cells, while RanBPM is abundant in WI-38 and MCF-7 cells.


Pssm-ID: 293966  Cd Length: 144  Bit Score: 37.12  E-value: 7.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370469427 374 DASSfesVRCTFCVDA--GVWYYEVTVVTSGV---MQIGWATRDSKfLNH------EGYGI-GDD--EYSCAYDGcrqli 439
Cdd:cd12909    10 DAAA---VRANHPIPPqcGIYYFEVKIISKGRdgyIGIGFSTKDVN-LNRlpgwepHSWGYhGDDghSFCSSGTG----- 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1370469427 440 wynarsKPHiHPCWKEGDTVGFLLDLNEKQMIFFLNGNQLP 480
Cdd:cd12909    81 ------KPY-GPTFTTGDVIGCGINFRDNTAFYTKNGVNLG 114
mRING-HC-C3HC5_MAPL cd16648
Modified RING finger, HC subclass (C3HC5-type), found in mitochondrial-anchored protein ligase ...
555-596 7.80e-03

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: 34.75  E-value: 7.80e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1370469427 555 ENCCSLCCDEVADTQLKPCGHSDLCMDC--AL-QLETCPLCRKEI 596
Cdd:cd16648     1 DNACVICLSNPRSCVFLECGHVCSCIECyeALpSPKKCPICRSFI 45
RING-HC_MIB2_rpt2 cd16728
second RING finger, HC subclass, found in mind bomb 2 (MIB2) and similar proteins; MIB2, also ...
558-601 7.99e-03

second 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. Especially, 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 second RING-HC finger.


Pssm-ID: 438388  Cd Length: 51  Bit Score: 34.84  E-value: 7.99e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1370469427 558 CSLCCDEVADTQLKpCGHSDlCMDCALQLETCPLCRKEIVSRIR 601
Cdd:cd16728     7 CPICIDNHIKLVFQ-CGHGS-CIECSSALKACPICRQAIRERIQ 48
 
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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