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Conserved domains on  [gi|37588869|ref|NP_071347|]
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E3 ubiquitin-protein ligase RNF123 [Homo sapiens]

Protein Classification

E3 ubiquitin-protein ligase RNF123( domain architecture ID 11596335)

E3 ubiquitin-protein ligase RNF123 (RING finger protein 123) is the catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase, promoting the ubiquitination and proteasome-mediated degradation of CDKN1B which is the cyclin-dependent kinase inhibitor at the G0-G1 transition of the cell cycle

CATH:  3.30.40.10
EC:  2.3.2.27
Gene Symbol:  RNF123
Gene Ontology:  GO:0008270|GO:0016567|GO:0004842
SCOP:  3000160

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
123-250 4.33e-79

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: 255.71  E-value: 4.33e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37588869  123 TIRSTTCVYKGKWLYEVLISSQGLMQIGWCTISCRFNQEEGVGDTHNSYAYDGNRVRKWNVTTTNYGKAWAAGDIVSCLI 202
Cdd:cd12882    1 SIRANACVYKGKWMYEVTLGTKGIMQIGWATISCRFTQEEGVGDTRDSYAYDGNRVRKWNVSTQKYGEPWVAGDVIGCCI 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 37588869  203 DLDDGTLSFCLNGVSLGTAFENLSRGLGMAYFPAISLSFKESVAFNFG 250
Cdd:cd12882   81 DLDKGTISFYRNGRSLGVAFDNVRRGPGLAYFPAVSLSFGERLELNFG 128
RING-HC_RNF123 cd16541
RING finger, HC subclass, found in RING finger protein 123 (RNF123) and similar proteins; ...
1252-1295 4.91e-27

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


:

Pssm-ID: 438203 [Multi-domain]  Cd Length: 44  Bit Score: 104.31  E-value: 4.91e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 37588869 1252 DLCPICYAHPISAVFQPCGHKSCKACINQHLMNNKDCFFCKTTI 1295
Cdd:cd16541    1 DLCPICYAHPIDAVFLPCGHKSCRSCINRHLMNNKECFFCKATI 44
 
Name Accession Description Interval E-value
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
123-250 4.33e-79

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: 255.71  E-value: 4.33e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37588869  123 TIRSTTCVYKGKWLYEVLISSQGLMQIGWCTISCRFNQEEGVGDTHNSYAYDGNRVRKWNVTTTNYGKAWAAGDIVSCLI 202
Cdd:cd12882    1 SIRANACVYKGKWMYEVTLGTKGIMQIGWATISCRFTQEEGVGDTRDSYAYDGNRVRKWNVSTQKYGEPWVAGDVIGCCI 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 37588869  203 DLDDGTLSFCLNGVSLGTAFENLSRGLGMAYFPAISLSFKESVAFNFG 250
Cdd:cd12882   81 DLDKGTISFYRNGRSLGVAFDNVRRGPGLAYFPAVSLSFGERLELNFG 128
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
134-252 7.54e-29

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: 112.05  E-value: 7.54e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37588869    134 KWLYEVLISSQ--GLMQIGWCTISCRFNQEEGVGDTHNSYAYDGNRVRK-WNVTTTNYGKA-WAAGDIVSCLIDLDDGTL 209
Cdd:pfam00622    1 RHYFEVEIFGQdgGGWRVGWATKSVPRKGERFLGDESGSWGYDGWTGKKyWASTSPLTGLPlFEPGDVIGCFLDYEAGTI 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 37588869    210 SFCLNGVSLGTAFENLSRGLGmaYFPAISLSFKESVAFNFGSR 252
Cdd:pfam00622   81 SFTKNGKSLGYAFRDVPFAGP--LFPAVSLGAGEGLKFNFGLR 121
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
132-251 4.43e-28

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: 110.08  E-value: 4.43e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37588869     132 KGKWLYEVLISSQGLMQIGWCTISCRFNQEEGVGDTHNSYAYDGNRVRKW-NVTTTNYGKAWA-AGDIVSCLIDLDDGTL 209
Cdd:smart00449    1 SGRHYFEVEIGDGGHWRVGVATKSVPRGYFALLGEDKGSWGYDGDGGKKYhNSTGPEYGLPLQePGDVIGCFLDLEAGTI 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 37588869     210 SFCLNGVSL-GTAFENLSrgLGMAYFPAISLSFKESVAFNFGS 251
Cdd:smart00449   81 SFYKNGKYLhGLAFFDVK--FSGPLYPAFSLGSGNSVRLNFGP 121
RING-HC_RNF123 cd16541
RING finger, HC subclass, found in RING finger protein 123 (RNF123) and similar proteins; ...
1252-1295 4.91e-27

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


Pssm-ID: 438203 [Multi-domain]  Cd Length: 44  Bit Score: 104.31  E-value: 4.91e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 37588869 1252 DLCPICYAHPISAVFQPCGHKSCKACINQHLMNNKDCFFCKTTI 1295
Cdd:cd16541    1 DLCPICYAHPIDAVFLPCGHKSCRSCINRHLMNNKECFFCKATI 44
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
1250-1298 4.31e-12

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 62.01  E-value: 4.31e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 37588869   1250 EEDLCPICYAHPISAVFQPCGHKS-CKACINQHLMNNKDCFFCKTTIVSV 1298
Cdd:pfam13920    1 EDLLCVICLDRPRNVVLLPCGHLClCEECAERLLRKKKKCPICRQPIESV 50
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
1254-1291 7.71e-06

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


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 44.04  E-value: 7.71e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 37588869    1254 CPICYAHPISAVFQ-PCGHKSCKACINQHLMNNKD-CFFC 1291
Cdd:smart00184    1 CPICLEEYLKDPVIlPCGHTFCRSCIRKWLESGNNtCPIC 40
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
1250-1294 3.52e-03

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


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 41.54  E-value: 3.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 37588869 1250 EEDLCPICYAHPISAVFQPCGHKSCKACI--NQHLMNNKDCFFCKTT 1294
Cdd:COG5236   60 ENMNCQICAGSTTYSARYPCGHQICHACAvrLRALYMQKGCPLCRTE 106
 
Name Accession Description Interval E-value
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
123-250 4.33e-79

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: 255.71  E-value: 4.33e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37588869  123 TIRSTTCVYKGKWLYEVLISSQGLMQIGWCTISCRFNQEEGVGDTHNSYAYDGNRVRKWNVTTTNYGKAWAAGDIVSCLI 202
Cdd:cd12882    1 SIRANACVYKGKWMYEVTLGTKGIMQIGWATISCRFTQEEGVGDTRDSYAYDGNRVRKWNVSTQKYGEPWVAGDVIGCCI 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 37588869  203 DLDDGTLSFCLNGVSLGTAFENLSRGLGMAYFPAISLSFKESVAFNFG 250
Cdd:cd12882   81 DLDKGTISFYRNGRSLGVAFDNVRRGPGLAYFPAVSLSFGERLELNFG 128
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
133-248 4.37e-39

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: 141.41  E-value: 4.37e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37588869  133 GKWLYEVLI--SSQGLMQIGWCTISCRFNQEEGVGDTHNSYAYDGNRVRKWNVTT-TNYGKAWAAGDIVSCLIDLDDGTL 209
Cdd:cd11709    1 GKWYWEVRVdsGNGGLIQVGWATKSFSLDGEGGVGDDEESWGYDGSRLRKGHGGSsGPGGRPWKSGDVVGCLLDLDEGTL 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 37588869  210 SFCLNGVSLGTAFENLSRgLGMAYFPAISLSFKESVAFN 248
Cdd:cd11709   81 SFSLNGKDLGVAFTNLFL-KGGGLYPAVSLGSGQGVTIN 118
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
130-250 7.25e-32

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: 121.25  E-value: 7.25e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37588869  130 VYKGKWLYEVLISSQGLMQIGWCTISCRfnQEEGVGDTHNSYAYDGNRVRKWNVTTTNYGKAWAAGDIVSCLIDLDDGTL 209
Cdd:cd12878   11 VTSGKWYFEFEVLTSGYMRVGWARPGFR--PDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCMLDLVDRTI 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 37588869  210 SFCLNGV----SLG--TAFENLSRGLGmaYFPAISLSFKESVAFNFG 250
Cdd:cd12878   89 SFTLNGEllidSSGseVAFKDIEIGEG--FVPACSLGVGQKGRLNLG 133
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
134-252 7.54e-29

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: 112.05  E-value: 7.54e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37588869    134 KWLYEVLISSQ--GLMQIGWCTISCRFNQEEGVGDTHNSYAYDGNRVRK-WNVTTTNYGKA-WAAGDIVSCLIDLDDGTL 209
Cdd:pfam00622    1 RHYFEVEIFGQdgGGWRVGWATKSVPRKGERFLGDESGSWGYDGWTGKKyWASTSPLTGLPlFEPGDVIGCFLDYEAGTI 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 37588869    210 SFCLNGVSLGTAFENLSRGLGmaYFPAISLSFKESVAFNFGSR 252
Cdd:pfam00622   81 SFTKNGKSLGYAFRDVPFAGP--LFPAVSLGAGEGLKFNFGLR 121
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
132-251 4.43e-28

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: 110.08  E-value: 4.43e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37588869     132 KGKWLYEVLISSQGLMQIGWCTISCRFNQEEGVGDTHNSYAYDGNRVRKW-NVTTTNYGKAWA-AGDIVSCLIDLDDGTL 209
Cdd:smart00449    1 SGRHYFEVEIGDGGHWRVGVATKSVPRGYFALLGEDKGSWGYDGDGGKKYhNSTGPEYGLPLQePGDVIGCFLDLEAGTI 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 37588869     210 SFCLNGVSL-GTAFENLSrgLGMAYFPAISLSFKESVAFNFGS 251
Cdd:smart00449   81 SFYKNGKYLhGLAFFDVK--FSGPLYPAFSLGSGNSVRLNFGP 121
RING-HC_RNF123 cd16541
RING finger, HC subclass, found in RING finger protein 123 (RNF123) and similar proteins; ...
1252-1295 4.91e-27

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


Pssm-ID: 438203 [Multi-domain]  Cd Length: 44  Bit Score: 104.31  E-value: 4.91e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 37588869 1252 DLCPICYAHPISAVFQPCGHKSCKACINQHLMNNKDCFFCKTTI 1295
Cdd:cd16541    1 DLCPICYAHPIDAVFLPCGHKSCRSCINRHLMNNKECFFCKATI 44
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
125-253 1.00e-25

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: 104.58  E-value: 1.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37588869  125 RSTTCVY-KGKWLYEVLISSQGLMQIGWCTISCRFNqeegVGDTHNSYAYDGNRVRKWNVTTTNYGKAWAAGDIVSCLID 203
Cdd:cd12873   31 RATKGVKgKGKYYYEVTVTDEGLCRVGWSTEDASLD----LGTDKFGFGYGGTGKKSHGRQFDDYGEPFGLGDVIGCYLD 106
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 37588869  204 LDDGTLSFCLNGVSLGTAFENLSRGLGMAYFPAISLSFKEsVAFNFGSRP 253
Cdd:cd12873  107 LDNGTISFSKNGKDLGKAFDIPPHLRNSALFPAVCLKNAE-VEFNFGDKP 155
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
133-250 2.84e-24

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: 98.96  E-value: 2.84e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37588869  133 GKWLYEVLISSQGLMQIGWCTISCRFNQEE--GVGDTHNSYAYDGNRVRKW-NVTTTNYG-KAWAAGDIVSCLIDLDDGT 208
Cdd:cd12883    1 GVWYYEVTVLTSGVMQIGWATKDSKFLNHEgyGIGDDEYSCAYDGCRQLIWyNAKSKPHThPRWKPGDVLGCLLDLNKKQ 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 37588869  209 LSFCLNGVSLG---TAFENLSRGLgmayFPAISLSFKESVAFNFG 250
Cdd:cd12883   81 MIFSLNGNRLPperQVFTSAKSGF----FAAASFMSFQQCEFNFG 121
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
122-250 1.92e-19

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: 85.79  E-value: 1.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37588869  122 GTIRSTTCVYKGKWLY--EVLI---SSQGLMQIGWCTISCRFNQeeGVGDTHNSYAYDGN--RVRKWNVTTTNYGKAWAA 194
Cdd:cd12885    1 GSVRADHPIPPKVPVFyfEVTIldlGEKGIVSIGFCTSGFPLNR--MPGWEDGSYGYHGDdgRVYLGGGEGENYGPPFGT 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 37588869  195 GDIVSCLIDLDDGTLSFCLNGVSLGTAFENLSRGLgmaYFPAISLSFK-ESVAFNFG 250
Cdd:cd12885   79 GDVVGCGINFKTGEVFFTKNGELLGTAFENVVKGR---LYPTVGLGSPgVKVRVNFG 132
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
117-250 9.92e-19

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: 84.11  E-value: 9.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37588869  117 GHSNFGTIRSTTCVYKGKWLYEVLISSQGLMQ-----IGWCTISCRFnqEEGVG-DTHnSYAY---DGNRVRKWNVtTTN 187
Cdd:cd12872   12 GEKGYRMARANHGVREGKWYFEVKILEGGGTEtghvrVGWSRREASL--QAPVGyDKY-SYAIrdkDGSKFHQSRG-KPY 87
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37588869  188 YGKAWAAGDIVSCLIDLddGTLSFCLNGVSLGTAFENLSRGLGmaYFPAISLSFKESVAFNFG 250
Cdd:cd12872   88 GEPGFKEGDVIGFLITL--PKIEFFKNGKSQGVAFEDIYGTGG--YYPAVSLYKGATVTINFG 146
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
124-253 8.65e-18

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: 82.25  E-value: 8.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37588869  124 IRSTTCVYKGKWLYEVLISS-------------QGLMQIGWCTISCRFNqeegVGDTHNSYAYDGNRvRKW-NVTTTNYG 189
Cdd:cd12884   36 ARATYGVTKGKVCFEVKVTEnlpvkhlpteetdPHVVRVGWSVDSSSLQ----LGEEEFSYGYGSTG-KKStNCKFEDYG 110
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37588869  190 KAWAAGDIVSCLIDLD--DGTLSFCLNGVSLGTAFEnLSRGL--GMAYFPAIsLSFKESVAFNFGSRP 253
Cdd:cd12884  111 EPFGENDVIGCYLDFEsePVEISFSKNGKDLGVAFK-ISKEElgGKALFPHV-LTKNCAVEVNFGQKE 176
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
122-251 7.42e-13

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: 67.16  E-value: 7.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37588869  122 GTIRSTTCVYK--GKWLYEVLISS---QGLMQIGWCTISCRFNQ----EEgvgdthNSYAY---DGNRVRKWNvTTTNYG 189
Cdd:cd12909   12 AAVRANHPIPPqcGIYYFEVKIISkgrDGYIGIGFSTKDVNLNRlpgwEP------HSWGYhgdDGHSFCSSG-TGKPYG 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37588869  190 KAWAAGDIVSCLIDLDDGTLSFCLNGVSLGTAFENLSrglGMAYFPAISL-SFKESVAFNFGS 251
Cdd:cd12909   85 PTFTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIK---KGNLYPTVGLrTPGEHVEANFGQ 144
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
1250-1298 4.31e-12

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 62.01  E-value: 4.31e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 37588869   1250 EEDLCPICYAHPISAVFQPCGHKS-CKACINQHLMNNKDCFFCKTTIVSV 1298
Cdd:pfam13920    1 EDLLCVICLDRPRNVVLLPCGHLClCEECAERLLRKKKKCPICRQPIESV 50
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
121-250 4.64e-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: 62.33  E-value: 4.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37588869  121 FGTIRSTTcVYKgKWLYEVLISSQGLM-------QIGWCTISCRFNQE--------EGVGDTHNSYAYDGNRV---RKWN 182
Cdd:cd12877    8 VGVVEGSA-QYK-KWYFEVEVDHVEQFthqpahlRVGWANTSGYVPYPgggegwggNGVGDDLYSYGFDGLHLwtgGRSR 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37588869  183 VTTTNYGKAWAAGDIVSCLIDLDDGTLSFCLNGVSLGTAFENLSrgLGMAYFPAISLSFKESVAFNFG 250
Cdd:cd12877   86 RVTSGTQHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFN--LDGMFFPVMSFSAGVSCRFLLG 151
SPRY_like cd12886
SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ...
133-250 1.28e-10

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: 60.21  E-value: 1.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37588869  133 GKWLYEVLISSQGL---MQIGWCTISCRFNQEEGVGDTH----NSYAYDGNRVRKWNVTTTnYGKAWAAGDIVSCLIDLD 205
Cdd:cd12886    1 GKWYWEVTVVSSAAstyAGIGVANAAATGNNGLNGIELSsigySLGVYSGNKLSNGSSVAT-YGAGFTAGDVIGVALDLD 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 37588869  206 DGTLSFCLNGVSLGT---AFENLSRGLGMAYFPAISL--SFKESVAFNFG 250
Cdd:cd12886   80 AGKIWFYKNGVWQGGgdpAPGTNPAFAGTAMYPAVTGgsSTGGSFTANFG 129
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
1254-1291 9.71e-08

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


Pssm-ID: 438113 [Multi-domain]  Cd Length: 41  Bit Score: 49.41  E-value: 9.71e-08
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 37588869 1254 CPICYAHPISAVFQPCGHKSCKACINQHLM-NNKDCFFC 1291
Cdd:cd16449    3 CPICLERLKDPVLLPCGHVFCRECIRRLLEsGSIKCPIC 41
RING-HC_RNF8 cd16535
RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is ...
1254-1297 2.26e-06

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


Pssm-ID: 438197 [Multi-domain]  Cd Length: 64  Bit Score: 46.23  E-value: 2.26e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 37588869 1254 CPICYAHPISAVFQPCGHKSCKACINQHLMNNKDCFFCKTTIVS 1297
Cdd:cd16535    4 CSICSELFIEAVTLNCSHSFCSYCITEWMKRKKECPICRKPITS 47
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
1254-1291 7.71e-06

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


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 44.04  E-value: 7.71e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 37588869    1254 CPICYAHPISAVFQ-PCGHKSCKACINQHLMNNKD-CFFC 1291
Cdd:smart00184    1 CPICLEEYLKDPVIlPCGHTFCRSCIRKWLESGNNtCPIC 40
RING-HC_COP1 cd16504
RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and ...
1253-1295 1.50e-05

RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and similar proteins; COP1, also known as RING finger and WD repeat domain protein 2 (RFWD2) or RING finger protein 200 (RNF200), is a central regulator of photomorphogenic development in plants, which targets key transcription factors for proteasome-dependent degradation. It is localized predominantly in the nucleus, but may also be present in the cytosol. Mammalian COP1 functions as an E3 ubiquitin-protein ligase that interacts with Jun transcription factors and modulates their transcriptional activity. It also interacts with and negatively regulates the tumor-suppressor protein p53. Moreover, COP1 associates with COP9 signalosome subunit 6 (CSN6), and is involved in 14-3-3sigma ubiquitin-mediated degradation. The CSN6-COP1 link enhances ubiquitin-mediated degradation of p27(Kip1), a critical CDK inhibitor involved in cell cycle regulation, to promote cancer cell growth. Furthermore, COP1 functions as the negative regulator of ETV1 and influences prognosis in triple-negative breast cancer. COP1 contains an N-terminal extension, a C3HC4-type RING-HC finger, a coiled coil domain, and seven WD40 repeats. In human COP1, a classic leucine-rich NES, and a novel bipartite NLS is bridged by the RING-HC finger.


Pssm-ID: 438167 [Multi-domain]  Cd Length: 47  Bit Score: 43.38  E-value: 1.50e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 37588869 1253 LCPICYaHPISAVF-QPCGHKSCKACINQHLMNNKDCFFCKTTI 1295
Cdd:cd16504    4 LCPICF-DIIKEAFvTKCGHSFCYKCIVKHLEQKNRCPKCNFYL 46
SPRY_SOCS1-2-4 cd12906
SPRY domain in the suppressor of cytokine signaling 1, 2, 4 families (SOCS1, SOCS2, SOCS4); ...
164-238 2.11e-05

SPRY domain in the suppressor of cytokine signaling 1, 2, 4 families (SOCS1, SOCS2, SOCS4); 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 only SPSB1, SPSB2, and SPSB4 interact with prostate apoptosis response protein 4 (Par-4). They are negative regulators that recruit the ECS E3 ubiquitin ligase complex to polyubiquitinate inducible nitric-oxide synthase (iNOS), resulting in its proteasomal degradation, thus contributing to protection against the cytotoxic effect of iNOS in activated macrophages. It has been shown that SPSB1 and SPSB4 induce the degradation of iNOS more strongly than SPSB2. The Drosophila melanogaster SPSB1 homolog, GUSTAVUS, interacts with the DEAD box RNA helicase Vasa. Suppressor of cytokine signaling (SOCS) proteins negatively regulate signaling from JAK-associated cytokine receptor complexes, and play key roles in the regulation of immune homeostasis.


Pssm-ID: 293963  Cd Length: 174  Bit Score: 46.46  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37588869  164 VGDTHNSYAYDGNRVR-------KWNVTTTNY---GKAWAAGDIVSCLIDLDDGTLSFCLNGVSLGTAFenlsRGL-GMA 232
Cdd:cd12906   80 VGSNEESWGWDIGRNKlyhdsknQPGWTYPAFlepDENFVVPDKFLVVLDMDEGTLSFVVDGQYLGVAF----RGLkGKK 155

                 ....*.
gi 37588869  233 YFPAIS 238
Cdd:cd12906  156 LYPIVS 161
RING-HC_SpRad8-like cd16572
RING finger, HC subclass, found in Schizosaccharomyces pombe DNA repair protein Rad8 (SpRad8) ...
1254-1296 2.46e-05

RING finger, HC subclass, found in Schizosaccharomyces pombe DNA repair protein Rad8 (SpRad8) and similar proteins; SpRad8 is a conserved protein homologous to Saccharomyces cerevisiae DNA repair protein Rad5 and human helicase-like transcription factor (HLTF) that is required for error-free postreplication repair by contributing to polyubiquitylation of PCNA. SpRad8 contains a C3HC4-type RING-HC finger responsible for the E3 ubiquitin ligase activity, a SNF2-family helicase domain including an ATP binding site, and a family-specific HIRAN domain (HIP116, Rad5p N-terminal domain) that contributes to nuclear localization.


Pssm-ID: 438234 [Multi-domain]  Cd Length: 61  Bit Score: 43.27  E-value: 2.46e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 37588869 1254 CPICYAHPIS--AVfQPCGHKSCKACINQHLMNNKD------CFFCKTTIV 1296
Cdd:cd16572    7 CPICAEEPISelAL-TRCWHSACKDCLLDHIEFQKSknevplCPTCRQPIN 56
RING-HC_MIBs-like cd16520
RING finger, HC subclass, found in mind bomb MIB1, MIB2, RGLG1, RGLG2, and similar proteins; ...
1253-1295 2.91e-05

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: 42.28  E-value: 2.91e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 37588869 1253 LCPICYAHPISAVFQpCGHKSCKACiNQHLmnnKDCFFCKTTI 1295
Cdd:cd16520    2 LCPICMERKKNVVFL-CGHGTCQKC-AEKL---KKCPICRKPI 39
RING-HC_TRIM40-C-V cd16583
RING finger, HC subclass, found in tripartite motif-containing protein 40 (TRIM40) and similar ...
1250-1282 2.94e-05

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


Pssm-ID: 438245 [Multi-domain]  Cd Length: 63  Bit Score: 42.89  E-value: 2.94e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 37588869 1250 EEDLCPICYAHPISAVFQPCGHKSCKACINQHL 1282
Cdd:cd16583    4 EEGVCPICQEPLKEAVSTDCGHLFCRMCLTQHA 36
SPRY_HERC1 cd12881
SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to ...
172-238 5.18e-05

SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to chromosome condensation regulator RCC1. It is widely expressed in many tissues, playing an important role in intracellular membrane trafficking in the cytoplasm as well as Golgi apparatus. HERC1 also interacts with tuberous sclerosis 2 (TSC2, tuberin), which suppresses cell growth, and results in the destabilization of TSC2. However, the biological function of HERC1 has yet to be defined.


Pssm-ID: 293939  Cd Length: 162  Bit Score: 45.03  E-value: 5.18e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37588869  172 AYDGN---RVRKWNVTTTNYgkawAAGDIVSCLIDLDDGTLSFCLNGVSLGTAFENLsrgLGMAYFPAIS 238
Cdd:cd12881   85 AYNGNlyhNGEQLLRLSSKF----HQGDYITVVLDMEEGTLSFGKNGEEPGVAFEDV---DATELYPCVM 147
RING-HC_CARP cd16500
RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein CARP-1, ...
1252-1298 6.56e-05

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: 41.60  E-value: 6.56e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 37588869 1252 DLCPICYAHPISAVFQPCGHK-SCKACINQhlMNnkDCFFCKTTIVSV 1298
Cdd:cd16500    1 DLCKICMDAAIDCVLLECGHMvTCTDCGKK--LS--ECPICRQYVVRV 44
RING-HC_BIRC4_8 cd16714
RING finger, HC subclass, found in E3 ubiquitin-protein ligase XIAP, baculoviral IAP ...
1250-1296 7.40e-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: 42.05  E-value: 7.40e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 37588869 1250 EEDLCPICYAHPISAVFQPCGH----KSCKACINQhlmnnkdCFFCKTTIV 1296
Cdd:cd16714   13 EEKLCKICMDRNISIVFIPCGHlvtcKQCAEALDK-------CPICCTVIT 56
RING-HC_AtBRCA1-like cd23147
RING finger, HC subclass, found in Arabidopsis thaliana protein BREAST CANCER SUSCEPTIBILITY 1 ...
1254-1292 9.30e-05

RING finger, HC subclass, found in Arabidopsis thaliana protein BREAST CANCER SUSCEPTIBILITY 1 homolog (AtBRCA1) and similar proteins; AtBRCA1 plays a role in DNA repair and in cell-cycle control. It is required for the repair of DNA double-strand breaks (DSBs), both natural and induced by genotoxic stress, by homologous recombination (HR). AtBRCA1 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438509 [Multi-domain]  Cd Length: 54  Bit Score: 41.30  E-value: 9.30e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 37588869 1254 CPICYAHPISAVFQPCGHKSCKACINQHLMNNKDCFFCK 1292
Cdd:cd23147    7 CPICLSLFKSAANLSCNHCFCAGCIGESLKLSAICPVCK 45
RING-HC_TRIM35_C-IV cd16599
RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar ...
1250-1278 9.59e-05

RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar proteins; TRIM35, also known as hemopoietic lineage switch protein 5 (HLS5), is a putative hepatocellular carcinoma (HCC) suppressor that inhibits phosphorylation of pyruvate kinase isoform M2 (PKM2), which is involved in aerobic glycolysis of cancer cells and further suppresses the Warburg effect and tumorigenicity in HCC. It also negatively regulates Toll-like receptor 7 (TLR7)- and TLR9-mediated type I interferon production by suppressing the stability of interferon regulatory factor 7 (IRF7). Moreover, TRIM35 regulates erythroid differentiation by modulating globin transcription factor 1 (GATA-1) activity. TRIM35 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438261 [Multi-domain]  Cd Length: 66  Bit Score: 41.68  E-value: 9.59e-05
                         10        20
                 ....*....|....*....|....*....
gi 37588869 1250 EEDLCPICYAHPISAVFQPCGHKSCKACI 1278
Cdd:cd16599    3 EELLCPICYEPFREAVTLRCGHNFCKGCV 31
RING-HC_RNF213 cd16561
RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; ...
1250-1299 1.32e-04

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


Pssm-ID: 438223 [Multi-domain]  Cd Length: 50  Bit Score: 40.72  E-value: 1.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 37588869 1250 EEDLCPICYAHPISAVFQPCGHKSCKACINQHLMNNKDCFFCKTTIVSVE 1299
Cdd:cd16561    1 GEQECSICLEDLNDPVKLPCDHVFCEECIRQWLPGQMSCPLCRTELPDDF 50
RING-HC_RNF10 cd16536
RING finger, HC subclass, found in RING finger protein 10 (RNF10) and similar proteins; RNF10 ...
1254-1288 1.52e-04

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


Pssm-ID: 438198 [Multi-domain]  Cd Length: 54  Bit Score: 40.68  E-value: 1.52e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 37588869 1254 CPICYAHPISAVFQPCGHKSCKACINQHLMNNKDC 1288
Cdd:cd16536    3 CPICLEPPVAPRITRCGHIFCWPCILRYLSLSEKK 37
SPRY_SOCS3 cd12876
SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY ...
185-238 1.60e-04

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: 44.07  E-value: 1.60e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 37588869  185 TTNYG-KAWAAGDIVSCLIDLDDGTLSFCLNGVSLGTAFENLSRGLGmaYFPAIS 238
Cdd:cd12876  104 SRPYTsPFGNQGTIIGVHLDMWRGTLTFYKNGKPLGVAFTGLNGVKP--LYPMVS 156
RING-HC_XBAT31-like cd23144
RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 1 (XBAT31) and ...
1249-1298 2.16e-04

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: 40.69  E-value: 2.16e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37588869 1249 SEEDLCPICYAHPISAVFQPCGHKSCKACINQHLMNNKD-----------CFFCKTTIVSV 1298
Cdd:cd23144    4 SDEDVCCICFEHLCTIEIKDCGHQMCATCALKLCCHNKPnpssspprppaCPFCRQDIASL 64
RING-HC_ScRAD18-like cd23148
RING finger, HC subclass, found in Saccharomyces cerevisiae radiation sensitivity protein 18 ...
1254-1295 5.17e-04

RING finger, HC subclass, found in Saccharomyces cerevisiae radiation sensitivity protein 18 (RAD18) and similar proteins; RAD18, also called RING-type E3 ubiquitin transferase RAD18, acts as a postreplication repair E3 ubiquitin-protein ligase that associates with the E2 ubiquitin conjugating enzyme UBC2/RAD6 to form the UBC2-RAD18 ubiquitin ligase complex involved in postreplicative repair (PRR) of damaged DNA. The UBC2-RAD18 complex cooperates with RAD5 and the UBC13-MMS2 dimer to attach mono-ubiquitin chains on 'Lys-164' of POL30, which is necessary for PRR. The UBC2-RAD18 complex is also involved in prevention of spontaneous mutations caused by 7,8-dihydro-8-oxoguanine. RAD18 is an E3 RING-finger protein belonging to the UBC2/RAD6 epistasis group. It contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438510 [Multi-domain]  Cd Length: 52  Bit Score: 39.05  E-value: 5.17e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 37588869 1254 CPICYAHPISAVFQPCGHKSCKACINQHLMNNKDCFFCKTTI 1295
Cdd:cd23148    6 CHICKDLLKAPMRTPCNHTFCSFCIRTHLNNDARCPLCKAEV 47
RING-HC_HLTF cd16509
RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar ...
1249-1292 6.03e-04

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


Pssm-ID: 438172 [Multi-domain]  Cd Length: 53  Bit Score: 38.83  E-value: 6.03e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 37588869 1249 SEEDlCPICYAHPISAVFQPCGHKSCKACINQHLMNNKD-CFFCK 1292
Cdd:cd16509    2 SDEE-CAICLDSLTNPVITPCAHVFCRRCICEVIQREKAkCPMCR 45
mRING-HC-C3HC5_NEU1 cd16647
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein NEURL1A, ...
1254-1298 6.25e-04

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: 38.82  E-value: 6.25e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 37588869 1254 CPICYAHPISAVFQPCGHK-SCKACINQHLMNNKDCFFCKTTIVSV 1298
Cdd:cd16647    4 CVICYERPVDTVLYRCGHMcMCYDCALQLKRRGGSCPICRAPIKDV 49
RING-HC_TRIM39_C-IV cd16601
RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar ...
1251-1291 6.70e-04

RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar proteins; TRIM39, also known as RING finger protein 23 (RNF23) or testis-abundant finger protein, is an E3 ubiquitin-protein ligase that plays a role in controlling DNA damage-induced apoptosis through inhibition of the anaphase promoting complex (APC/C), a multiprotein ubiquitin ligase that controls multiple cell cycle regulators, including cyclins, geminin, and others. TRIM39 also functions as a regulator of several key processes in the proliferative cycle. It directly regulates p53 stability. It modulates cell cycle progression and DNA damage responses via stabilizing p21. Moreover, TRIM39 negatively regulates the nuclear factor kappaB (NFkappaB)-mediated signaling pathway through stabilization of Cactin, an inhibitor of NFkappaB- and Toll-like receptor (TLR)-mediated transcription, which is induced by inflammatory stimulants such as tumor necrosis factor alpha. Furthermore, TRIM39 is a MOAP-1-binding protein that can promote apoptosis signaling through stabilization of MOAP-1 via the inhibition of its poly-ubiquitination process. TRIM39 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438263 [Multi-domain]  Cd Length: 44  Bit Score: 38.62  E-value: 6.70e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 37588869 1251 EDLCPICYAHPISAVFQPCGHKSCKACINQHLMNNKDCFFC 1291
Cdd:cd16601    1 EASCSLCKEYLKDPVIIECGHNFCRACITRFWEELDGDFPC 41
RING-HC_RNF39 cd16592
RING finger, HC subclass, found in RING finger protein 39 (RNF39) and similar proteins; RNF39, ...
1250-1281 7.25e-04

RING finger, HC subclass, found in RING finger protein 39 (RNF39) and similar proteins; RNF39, also called protein HZFw, may play a role in prolonged long term-potentiation (LTP) maintenance. It is involved in the etiology of Behcet's disease (BD). It may also be involved in HIV-1 replication. RNF39 acts as an E3 ubiquitin ligase that inhibits retinoic acid-inducible gene-I (RIG-I)-like receptor (RLR) pathways by mediating K48-linked ubiquitination and proteasomal degradation of DDX3X (DEAD-box RNA helicase 3, X-linked). RNF39 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438254 [Multi-domain]  Cd Length: 58  Bit Score: 38.97  E-value: 7.25e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 37588869 1250 EEDLCPICYAHPISAVFQPCGHKSCKACINQH 1281
Cdd:cd16592    3 EETTCPICLGYFKDPVILDCEHSFCRACIARH 34
RING-HC_XBAT35-like cd23129
RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and ...
1250-1298 8.90e-04

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: 38.40  E-value: 8.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 37588869 1250 EEDLCPICYAHPISAVFQPCGHKS-CKACINQHLMNNKDCFFCKTTIVSV 1298
Cdd:cd23129    1 QRDECVVCMDAPRDAVCVPCGHVAgCMSCLKALMQSSPLCPICRAPVRQV 50
RING-HC_RNFT1 cd16741
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 1 ...
1251-1295 1.17e-03

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 1 (RNFT1); RNFT1, also known as protein PTD016, is a multi-pass membrane protein containing a C3HC4-type RING-HC finger. Its biological role remains unclear.


Pssm-ID: 438399 [Multi-domain]  Cd Length: 58  Bit Score: 38.33  E-value: 1.17e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 37588869 1251 EDLCPICYAHPISAVFQPCGHKSCKACINQHLMNNKDCFFCKTTI 1295
Cdd:cd16741   14 DDICAICQAEFRKPILLICQHVFCEECISLWFNREKTCPLCRTVI 58
RING-HC_RNF168 cd16550
RING finger, HC subclass, found in RING finger protein 168 (RNF168) and similar proteins; ...
1253-1297 1.25e-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: 38.13  E-value: 1.25e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 37588869 1253 LCPICYAHPISAVFQPCGHKSCKACINQHLMN-NKDCFFCKTTIVS 1297
Cdd:cd16550    2 LCPICLEILVEPVTLPCNHTLCMPCFQSTVEKaSLCCPLCRLRISS 47
RING-HC_DTX3L cd16712
RING finger, HC subclass, found in protein Deltex-3-like (DTX3L) and similar proteins; DTX3L, ...
1250-1293 1.38e-03

RING finger, HC subclass, found in protein Deltex-3-like (DTX3L) and similar proteins; DTX3L, also known as B-lymphoma- and BAL-associated protein (BBAP) or Rhysin-2 (Rhysin2), is a RING-domain E3 ubiquitin-protein ligase that regulates endosomal sorting of the G protein-coupled receptor CXCR4 from endosomes to lysosomes. It also regulates subcellular localization of its partner protein, B aggressive lymphoma (BAL), by a dynamic nucleocytoplasmic trafficking mechanism. DTX3L has a unique N-terminus, but lacks the highly basic N-terminal motif and the central proline-rich motif present in other Deltex (DTX) family members, such as DTX1, DTX2, and DTX4. Moreover, its C-terminal region is highly homologous to DTX3. It includes a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain. DTX3L can associate with DTX1 through its unique N-terminus and further enhance self-ubiquitination.


Pssm-ID: 438372 [Multi-domain]  Cd Length: 56  Bit Score: 38.18  E-value: 1.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 37588869 1250 EEDLCPICYAHPISA-VFQPCGHKSCKACINQHLMNNKDCFFCKT 1293
Cdd:cd16712    2 EEDECPICMDRISNKkVLPKCKHVFCAACIDKAMKYKPVCPVCGT 46
RING-HC_RSPRY1 cd16566
RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) ...
1251-1295 1.60e-03

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: 37.34  E-value: 1.60e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 37588869 1251 EDLCPICYAHPISAVFQPCGHKS-CKACINQHlmnnKDCFFCKTTI 1295
Cdd:cd16566    2 EDSCTLCFDKVADTELRPCGHSGfCMECALQL----ETCPLCRQPI 43
zf-RING_UBOX pfam13445
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.
1254-1291 1.65e-03

RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.


Pssm-ID: 463881 [Multi-domain]  Cd Length: 38  Bit Score: 37.38  E-value: 1.65e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 37588869   1254 CPIC---YAHPISavfqPCGHkS-CKACINQHLMNNKDCFFC 1291
Cdd:pfam13445    1 CPIClelFTDPVL----PCGH-TfCRECLEEMSQKKGGKFKC 37
RING-H2_RNF139-like cd16476
RING finger, H2 subclass, found in RING finger proteins RNF139, RNF145, and similar proteins; ...
1252-1291 1.90e-03

RING finger, H2 subclass, found in RING finger proteins RNF139, RNF145, and similar proteins; RNF139, also known as translocation in renal carcinoma on chromosome 8 protein (TRC8), is an endoplasmic reticulum (ER)-resident multi-transmembrane protein that functions as a potent growth suppressor in mammalian cells, inducing G2/M arrest, decreased DNA synthesis and increased apoptosis. It is a tumor suppressor that has been implicated in a novel regulatory relationship linking the cholesterol/lipid biosynthetic pathway with cellular growth control. A mutation in RNF139 has been identified in families with hereditary renal (RCC) and thyroid cancers. RNF145 is an uncharacterized RING finger protein encoded by the RNF145 gene, which is expressed in T lymphocytes, and its expression is altered in acute myelomonocytic and acute promyelocytic leukemias. Although its biological function remains unclear, RNF145 shows high sequence similarity with RNF139. Both RNF139 and RNF145 contain a C3H2C3-type RING-H2 finger with possible E3-ubiquitin ligase activity.


Pssm-ID: 438139 [Multi-domain]  Cd Length: 41  Bit Score: 37.44  E-value: 1.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 37588869 1252 DLCPICYAHPISAVFQPCGHKSCKACINQHLMNNKDCFFC 1291
Cdd:cd16476    1 DVCAICYQEMKEARITPCNHFFHGLCLRKWLYVQDTCPLC 40
RING-HC_Cbl-like cd16502
RING finger, HC subclass, found in Casitas B-lineage lymphoma (Cbl) proteins; The Cbl adaptor ...
1253-1292 2.39e-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: 36.94  E-value: 2.39e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 37588869 1253 LCPICYAHPISAVFQPCGHKSCKACINQHLMNNK-DCFFCK 1292
Cdd:cd16502    3 LCKICAENDKDVRIEPCGHLLCTPCLTSWQDSDGqTCPFCR 43
RING-HC_RAD18 cd16529
RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; ...
1254-1297 2.61e-03

RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; RAD18, also known as HR18 or RING finger protein 73 (RNF73), is an E3 ubiquitin-protein ligase involved in post replication repair of UV-damaged DNA via its recruitment to stalled replication forks. It associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on K164. It also interacts with another E2 ubiquitin conjugating enzyme RAD6 to form a complex that monoubiquitinates proliferating cell nuclear antigen at stalled replication forks in DNA translesion synthesis. Moreover, Rad18 is a key factor in double-strand break DNA damage response (DDR) pathways via its association with K63-linked polyubiquitylated chromatin proteins. It can function as a mediator for DNA damage response signals to activate the G2/M checkpoint in order to maintain genome integrity and cell survival after ionizing radiation (IR) exposure. RAD18 contains a C3HC4-type RING-HC finger, a ubiquitin-binding zinc finger domain (UBZ), a SAP (SAF-A/B, Acinus and PIAS) domain, and a RAD6-binding domain (R6BD).


Pssm-ID: 438192 [Multi-domain]  Cd Length: 54  Bit Score: 37.28  E-value: 2.61e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 37588869 1254 CPICYAH-PISAVFQPCGHKSCKACINQHLMNNKDCFFCKTTIVS 1297
Cdd:cd16529    7 CPICFEYfNTAMMITQCSHNYCSLCIRRFLSYKTQCPTCRAAVTE 51
RING-HC_DTX3-like cd16506
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3), Deltex-3-like ...
1252-1293 3.08e-03

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3), Deltex-3-like (DTX3L) and similar proteins; This subfamily contains Deltex3 (DTX3) and Deltex-3-like (DTX3L), both of which are E3 ubiquitin-protein ligases belonging to the Deltex (DTX) family. DTX3, also known as RING finger protein 154 (RNF154), has a biological function that remains unclear. DTX3L, also known as B-lymphoma- and BAL-associated protein (BBAP) or Rhysin-2 (Rhysin2), regulates endosomal sorting of the G protein-coupled receptor CXCR4 from endosomes to lysosomes. It also regulates subcellular localization of its partner protein, B aggressive lymphoma (BAL), by a dynamic nucleocytoplasmic trafficking mechanism. In contrast to other DTXs, both DTX3 and DTX3L contain a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain. DTX3L can associate with DTX1 through its unique N termini and further enhance self-ubiquitination.


Pssm-ID: 438169 [Multi-domain]  Cd Length: 45  Bit Score: 36.96  E-value: 3.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 37588869 1252 DLCPICYAhPISA--VFQPCGHKSCKACINQHLMNNKDCFFCKT 1293
Cdd:cd16506    1 DTCPICLD-EIQNkkTLEKCKHSFCEDCIDRALQVKPVCPVCGV 43
RING-HC_RNF5-like cd16534
RING finger, HC subclass, found in RING finger protein RNF5, RNF185 and similar proteins; RNF5 ...
1254-1292 3.08e-03

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


Pssm-ID: 438196 [Multi-domain]  Cd Length: 44  Bit Score: 36.89  E-value: 3.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 37588869 1254 CPICYAHPISAVFQPCGHKSCKACINQHLMNNKD---CFFCK 1292
Cdd:cd16534    3 CNICLDTASDPVVTMCGHLFCWPCLYQWLETRPDrqtCPVCK 44
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
1254-1291 3.22e-03

Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C where X is any amino acid. Many proteins containing a RING finger play a key role in the ubiquitination pathway.


Pssm-ID: 395049 [Multi-domain]  Cd Length: 40  Bit Score: 36.56  E-value: 3.22e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 37588869   1254 CPICYAHPISAVFQ-PCGHKSCKACINQHLM-NNKDCFFC 1291
Cdd:pfam00097    1 CPICLEEPKDPVTLlPCGHLFCSKCIRSWLEsGNVTCPLC 40
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
1250-1294 3.52e-03

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


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 41.54  E-value: 3.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 37588869 1250 EEDLCPICYAHPISAVFQPCGHKSCKACI--NQHLMNNKDCFFCKTT 1294
Cdd:COG5236   60 ENMNCQICAGSTTYSARYPCGHQICHACAvrLRALYMQKGCPLCRTE 106
RING-HC_RNF169 cd16551
RING finger, HC subclass, found in RING finger protein 169 (RNF169) and similar proteins; ...
1254-1282 3.56e-03

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


Pssm-ID: 438213 [Multi-domain]  Cd Length: 55  Bit Score: 36.75  E-value: 3.56e-03
                         10        20
                 ....*....|....*....|....*....
gi 37588869 1254 CPICYAHPISAVFQPCGHKSCKACINQHL 1282
Cdd:cd16551    4 CAGCLEVPVEPATLPCGHTLCRGCANRAL 32
RING-HC_IRC20-like cd23135
RING finger, HC subclass, found in Saccharomyces cerevisiae increased recombination centers ...
1254-1292 3.64e-03

RING finger, HC subclass, found in Saccharomyces cerevisiae increased recombination centers protein 20 (IRC20) and similar proteins; IRC20 is an uncharacterized ATP-dependent helicase that is probably involved in a pathway contributing to genomic integrity. IRC20 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438497 [Multi-domain]  Cd Length: 44  Bit Score: 36.72  E-value: 3.64e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 37588869 1254 CPICYAHPISAVFQPCGHKSCKACINQHLMNNKDCFFCK 1292
Cdd:cd23135    6 CSICFSEIRSGAILKCGHFFCLSCIASWLREKSTCPLCK 44
SPRY_PRY_TRIM67_9 cd12889
PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, ...
195-239 3.81e-03

PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM9 proteins. TRIM9 protein is expressed mainly in the cerebral cortex, and functions as an E3 ubiquitin ligase. It has been shown that TRIM9 is localized to the neurons in the normal human brain and its immunoreactivity in affected brain areas in Parkinson's disease and dementia with Lewy bodies is severely decreased, possibly playing an important role in the regulation of neuronal function and participating in pathological process of Lewy body disease through its ligase. TRIM67 negatively regulates Ras activity via degradation of 80K-H, leading to neural differentiation, including neuritogenesis.


Pssm-ID: 293947  Cd Length: 172  Bit Score: 39.53  E-value: 3.81e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 37588869  195 GDIVSCLIDLDDGTLSFCLNGVSLGT-AFENLSrGLgmaYFPAISL 239
Cdd:cd12889  116 GSVVGVLLDLDRHTLSFYVNDEPQGPiAFRNLP-GV---FYPAVSL 157
RING-HC_RBR_TRIAD1 cd16773
RING finger, HC subclass, found in two RING fingers and DRIL [double RING finger linked] 1 ...
1254-1284 4.08e-03

RING finger, HC subclass, found in two RING fingers and DRIL [double RING finger linked] 1 (TRIAD1); TRIAD1, also known as ariadne-2 (ARI-2), protein ariadne-2 homolog, Ariadne RBR E3 ubiquitin protein ligase 2 (ARIH2), or UbcM4-interacting protein 48, is an RBR-type E3 ubiquitin-protein ligase that catalyzes the formation of polyubiquitin chains linked via lysine-48, as well as lysine-63 residues. Its auto-ubiquitylation can be catalyzed by the E2 conjugating enzyme UBCH7. TRIAD1 has been implicated in hematopoiesis, specifically in myelopoiesis, as well as in embryogenesis. It functions as a regulator of endosomal transport and is required for the proper function of multivesicular bodies. It also acts as a novel ubiquitination target for proteasome-dependent degradation by murine double minute 2 (MDM2). As a proapoptotic protein, TRIAD1 promotes p53 activation, and inhibits MDM2-mediated p53 ubiquitination and degradation. Furthermore, TRIAD1 can inhibit the ubiquitination and proteasomal degradation of growth factor independence 1 (Gfi1), a transcriptional repressor essential for the function and development of many different hematopoietic lineages. TRIAD1 contains an RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a C3HC4-type RING-HC finger required for RBR-mediated ubiquitination.


Pssm-ID: 438429 [Multi-domain]  Cd Length: 54  Bit Score: 36.56  E-value: 4.08e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 37588869 1254 CPICYAH-PISAVFQ-PCGHKSCKACINQHLMN 1284
Cdd:cd16773    3 CGVCCEDvPKDELFSlACGHYFCNDCWKQYLTV 35
mRING-HC-C3HC3D_TRAF6 cd16643
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
1254-1282 4.10e-03

Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 6 (TRAF6) and similar proteins; TRAF6, also known as interleukin-1 signal transducer or RING finger protein 85 (RNF85), is a cytoplasmic adapter protein that mediates signals induced by the tumor necrosis factor receptor (TNFR) superfamily and Toll-like receptor (TLR)/interleukin-1 receptor (IL-1R) family. It functions as a mediator involved in the activation of mitogen-activated protein kinase (MAPK), phosphoinositide 3-kinase (PI3K), and interferon regulatory factor pathways, as well as in IL-1R-mediated activation of NF-kappaB. TRAF6 is also an oncogene that plays a vital role in K-RAS-mediated oncogenesis. TRAF6 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and several zinc fingers, and a C-terminal TRAF domain that comprises a coiled coil domain and a conserved TRAF-C domain.


Pssm-ID: 438305 [Multi-domain]  Cd Length: 58  Bit Score: 36.97  E-value: 4.10e-03
                         10        20
                 ....*....|....*....|....*....
gi 37588869 1254 CPICYAHPISAVFQPCGHKSCKACINQHL 1282
Cdd:cd16643    4 CPICLMALREPVQTPCGHRFCKACILKSI 32
RING-HC_BRCA1 cd16498
RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and ...
1254-1295 4.23e-03

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


Pssm-ID: 438161 [Multi-domain]  Cd Length: 94  Bit Score: 38.05  E-value: 4.23e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 37588869 1254 CPICY---AHPISAvfqPCGHKSCKACINQhLMNNKD----CFFCKTTI 1295
Cdd:cd16498   19 CPICLellKEPVST---KCDHQFCRFCILK-LLQKKKkpapCPLCKKSV 63
RING-H2_RNF145 cd16684
RING finger, H2 subclass, found in RING finger protein 145 (RNF145) and similar proteins; ...
1252-1291 4.26e-03

RING finger, H2 subclass, found in RING finger protein 145 (RNF145) and similar proteins; RNF145 is an uncharacterized RING finger protein encoded by the RNF145 gene, which is expressed in T lymphocytes, and its expression is altered in acute myelomonocytic and acute promyelocytic leukemias. Although its biological function remains unclear, RNF145 shows high sequence similarity with RNF139, an endoplasmic reticulum (ER)-resident multi-transmembrane protein that functions as a potent growth suppressor in mammalian cells, inducing G2/M arrest, decreased DNA synthesis and increased apoptosis. Like RNF139, RNF145 contains a C3H2C3-type RING-H2 finger with possible E3-ubiquitin ligase activity.


Pssm-ID: 319598 [Multi-domain]  Cd Length: 43  Bit Score: 36.19  E-value: 4.26e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 37588869 1252 DLCPICYAHPISAVFQPCGHKSCKACINQHLMNNKDCFFC 1291
Cdd:cd16684    3 DICSICYQDMKSAVITPCSHFFHAGCLKKWLYVQETCPLC 42
RING-HC_IAPs cd16510
RING finger, HC subclass, found in inhibitor of apoptosis proteins (IAPs); IAPs are frequently ...
1251-1277 4.92e-03

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: 36.08  E-value: 4.92e-03
                         10        20
                 ....*....|....*....|....*...
gi 37588869 1251 EDLCPICYAHPISAVFQPCGH-KSCKAC 1277
Cdd:cd16510    1 EKLCKICMDREVNIVFLPCGHlVTCAQC 28
mRING-HC-C3HC5_MAPL cd16648
Modified RING finger, HC subclass (C3HC5-type), found in mitochondrial-anchored protein ligase ...
1254-1298 5.16e-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: 36.29  E-value: 5.16e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 37588869 1254 CPICYAHPISAVFQPCGHK-SCKACInQHLMNNKDCFFCKTTIVSV 1298
Cdd:cd16648    4 CVICLSNPRSCVFLECGHVcSCIECY-EALPSPKKCPICRSFIKRV 48
RING-HC_EHV1-like cd23130
RING finger, HC subclass, found in Equid alphaherpesvirus 1 (Equine herpesvirus 1/EHV-1) ...
1252-1298 5.45e-03

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


Pssm-ID: 438492 [Multi-domain]  Cd Length: 51  Bit Score: 36.18  E-value: 5.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 37588869 1252 DLCPICYAHP-ISAVFQPCGHKSCKACINQHLMNNKDCFFCKTTIVSV 1298
Cdd:cd23130    1 DVCPICLDDPeDEAITLPCLHQFCYTCILRWLQTSPTCPLCKTPVTSI 48
RING-HC_ZNF598 cd16615
RING finger, HC subclass, found in zinc finger protein 598 (ZNF598) and similar proteins; ...
1252-1293 6.49e-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: 36.05  E-value: 6.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 37588869 1252 DLCPICyAHPISAV-FQPCGHKSCKACINQH--LMNNKDCFFCKT 1293
Cdd:cd16615    1 ETCVIC-CEEIEYFaVGPCNHPVCYKCSLRMrvLYKDKYCPICRT 44
RING-HC_LONFs_rpt2 cd16514
second RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger ...
1254-1295 6.57e-03

second RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger protein family; The LON peptidase N-terminal domain and RING finger protein family includes LONRF1 (also known as RING finger protein 191 or RNF191), LONRF2 (also known as RING finger protein 192, RNF192, or neuroblastoma apoptosis-related protease), LONRF3 (also known as RING finger protein 127 or RNF127), which are characterized by containing two C3HC4-type RING-HC fingers, four tetratricopeptide (TPR) repeats, and an ATP-dependent protease La (LON) substrate-binding domain at the C-terminus. Their biological functions remain unclear. This model corresponds to the second RING-HC finger.


Pssm-ID: 438177 [Multi-domain]  Cd Length: 45  Bit Score: 35.71  E-value: 6.57e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 37588869 1254 CPICYAHPISAVFQPCGHKSCKACINQHLMNNKDCFFCKTTI 1295
Cdd:cd16514    4 CSLCLRLLYEPVTTPCGHTFCRACLERCLDHSPKCPLCRTSL 45
RING-HC_ScPSH1-like cd16568
RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated ...
1254-1297 6.74e-03

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


Pssm-ID: 438230 [Multi-domain]  Cd Length: 54  Bit Score: 36.19  E-value: 6.74e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 37588869 1254 CPICYahpiSAVFQP----CGHKSCKACINQHL--MNNKDCFFCKTTIVS 1297
Cdd:cd16568    7 CIICH----EYLYEPmvttCGHTYCYTCLNTWFksNRSLSCPDCRTKITT 52
RING-HC_Topors cd16574
RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein ...
1251-1293 7.52e-03

RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein (Topors) and similar proteins; Topors, also known as topoisomerase I-binding RING finger protein, tumor suppressor p53- binding protein 3, or p53-binding protein 3 (p53BP3), is a ubiquitously expressed nuclear E3 ubiquitin-protein ligase that can ligate both ubiquitin and small ubiquitin-like modifier (SUMO) to substrate proteins in the nucleus. It contains an N-terminal C3HC4-type RING-HC finger which ligates ubiquitin to its target proteins including DNA topoisomerase I, p53, NKX3.1, H2AX, and the AAV-2 Rep78/68 proteins. As a RING-dependent E3 ubiquitin ligase, Topors works with the E2 enzymes UbcH5a, UbcH5c, and UbcH6, but not with UbcH7, CDC34, or UbcH2b. Topors acts as a tumor suppressor in various malignancies. It regulates p53 modification, suggesting it may be responsible for astrocyte elevated gene-1 (AEG-1, also known as metadherin, or LYRIC) ubiquitin modification. Plk1-mediated phosphorylation of Topors inhibits Topors-mediated sumoylation of p53, whereas p53 ubiquitination is enhanced, leading to p53 degradation. It also functions as a negative regulator of the prostate tumor suppressor NKX3.1. Moreover, Topors is associated with promyelocytic leukemia nuclear bodies, and may be involved in the cellular response to camptothecin. It also plays a key role in the turnover of H2AX protein, discriminating the type of DNA damaging stress. Furthermore, Topors is a cilia-centrosomal protein associated with autosomal dominant retinal degeneration. Mutations in TOPORS cause autosomal dominant retinitis pigmentosa (adRP).


Pssm-ID: 438236 [Multi-domain]  Cd Length: 47  Bit Score: 35.72  E-value: 7.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 37588869 1251 EDLCPICYAHPIS--AVFQPCGHKSCKACINQHLMNNKDCFFCKT 1293
Cdd:cd16574    1 DSSCPICLDRFENekAFLDGCFHAFCFTCILEWSKVKNECPLCKQ 45
RING-HC_TRIM65_C-IV cd16609
RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar ...
1250-1281 7.75e-03

RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar proteins; TRIM65 is an E3 ubiquitin-protein ligase that interacts with the innate immune receptor MDA5, enhancing its ability to stimulate interferon-beta signaling. It functions as a potential oncogenic protein that negatively regulates p53 through ubiquitination, providing insight into the development of novel approaches targeting TRIM65 for non-small cell lung carcinoma (NSCLC) treatment, and also overcoming chemotherapy resistance. Moreover, TRIM65 negatively regulates microRNA-driven suppression of mRNA translation by targeting TNRC6 proteins for ubiquitination and degradation. TRIM65 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438271 [Multi-domain]  Cd Length: 58  Bit Score: 36.20  E-value: 7.75e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 37588869 1250 EEDL-CPIC---YAHPISAvfqPCGHKSCKACINQH 1281
Cdd:cd16609    1 EEELtCSIClglYQDPVTL---PCQHSFCRACIEDH 33
RING-HC_TRIM8_C-V cd16580
RING finger, HC subclass, found in tripartite motif-containing protein 8 (TRIM8) and similar ...
1250-1280 8.23e-03

RING finger, HC subclass, found in tripartite motif-containing protein 8 (TRIM8) and similar proteins; TRIM8, also known as glioblastoma-expressed RING finger protein (GERP) or RING finger protein 27 (RNF27), is a probable E3 ubiquitin-protein ligase that may promote proteasomal degradation of suppressor of cytokine signaling 1 (SOCS1) and further regulate interferon-gamma signaling. It functions as a new p53 modulator that stabilizes p53 impairing its association with MDM2 and inducing the reduction of cell proliferation. TRIM8 deficit dramatically impairs p53 stabilization and activation in response to chemotherapeutic drugs. TRIM8 also modulates tumor necrosis factor-alpha (TNFalpha) and interleukin-1beta (IL-1beta)-triggered nuclear factor-kappaB (NF- kappa B) activation by targeting transforming growth factor beta (TGFbeta) activated kinase 1 (TAK1) for K63-linked polyubiquitination. Moreover, TRIM8 modulates translocation of phosphorylated STAT3 into the nucleus through interaction with Hsp90beta and consequently regulates transcription of Nanog in embryonic stem cells. It also interacts with protein inhibitor of activated STAT3 (PIAS3), which inhibits IL-6-dependent activation of STAT3. TRIM8 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as an uncharacterized region positioned C-terminal to the RBCC domain. The coiled coil domain is required for homodimerization and the region immediately C-terminal to the RING motif is sufficient to mediate the interaction with SOCS1.


Pssm-ID: 438242 [Multi-domain]  Cd Length: 67  Bit Score: 36.41  E-value: 8.23e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 37588869 1250 EEDLCPICYAHPISAVFQPCGHKSCKACINQ 1280
Cdd:cd16580   10 EELICPICLHVFVEPVQLPCKHNFCRGCIGE 40
RING-HC_RBR_RNF19 cd16629
RING finger, HC subclass, found in the family of RING finger proteins RNF19A, RNF19B and ...
1254-1282 9.85e-03

RING finger, HC subclass, found in the family of RING finger proteins RNF19A, RNF19B and similar proteins; The family includes RING finger protein RNF19A and RNF19B, both of which are transmembrane (TM) domain-containing RBR-type E3 ubiquitin-protein ligases. RNF19A, also known as double ring-finger protein (Dorfin) or p38, localizes to the ubiquitylated inclusions in Parkinson's disease (PD), dementia with Lewy bodies, multiple system atrophy, and amyotrophic lateral sclerosis (ALS). It interacts with Psmc3, a protein component of the 19S regulatory cap of the 26S proteasome, and further participates in the ubiquitin-proteasome system in acrosome biogenesis, spermatid head shaping, and development of the head-tail coupling apparatus and tail. It modulates the ubiquitination and degradation of calcium-sensing receptor (CaR), which may contribute to a general mechanism for CaR quality control during biosynthesis. Moreover, RNF19A can also ubiquitylate mutant superoxide dismutase 1 (SOD1), the causative gene of familial ALS. It may associate with endoplasmic reticulum-associated degradation (ERAD) pathway, which is related to the pathogenesis of neurodegenerative disorders, such as PD or Alzheimer's disease. RNF19B, also known as IBR domain-containing protein 3 or natural killer lytic-associated molecule (NKLAM), plays a role in controlling tumor dissemination and metastasis. It is involved in the cytolytic function of natural killer (NK) cells and cytotoxic T lymphocytes (CTLs). It interacts with ubiquitin conjugates UbcH7 and UbcH8, and ubiquitinates uridine kinase like-1 (URKL-1) protein, targeting it for degradation. Moreover, RNF19B is a novel component of macrophage phagosomes and plays a role in macrophage anti-bacterial activity. It functions as a novel modulator of macrophage inducible nitric oxide synthase (iNOS) expression. Both RNF19A and RNF19B contain an RBR domain followed by three TMs. The RBR domain was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a C3HC4-type RING-HC finger required for RBR-mediated ubiquitination.


Pssm-ID: 438291 [Multi-domain]  Cd Length: 56  Bit Score: 35.89  E-value: 9.85e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 37588869 1254 CPICYAhPISAVFQP----CGHKSCKACINQHL 1282
Cdd:cd16629    3 CPLCLD-DLSPEFFPillsCEHRSCRDCLRQYL 34
 
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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