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Conserved domains on  [gi|1039796541|ref|XP_017173901|]
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E3 ubiquitin-protein ligase Midline-1 isoform X4 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPRY super family cl02614
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 460-636 4.51e-127

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.


The actual alignment was detected with superfamily member cd12892:

Pssm-ID: 470632  Cd Length: 177  Bit Score: 372.04  E-value: 4.51e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 460 PFRLDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAGQGSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPK 539
Cdd:cd12892     1 PFKLDPKSAHRKLKVSHDNLTVERDETSSKKSHTPERFTSQGSYGVAGNVFIDSGRHYWEVVISGSTWYAIGIAYKSAPK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 540 HEWIGKNAASWALCRCHNHWAVRHDGKETPIAPAPHLRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQPVCPTFTVW 619
Cdd:cd12892    81 HEWIGKNSASWVLCRCNNNWVVRHNSKEIPIEPSPHLRRVGILLDYDNGSLSFYDALNSIHLYTFDIAFAQPVCPTFTVW 160

                         170
                  ....*....|....*..
gi 1039796541 620 NKCLTIVTGLPIPDHLD 636
Cdd:cd12892   161 NKCLTILTGLPIPDHLD 177
RING_Ubox super family cl17238
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
 3-74 3.71e-45

RING finger (Really Interesting New Gene) domain and U-box domain superfamily; 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 different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC fingers. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are more closely related to RING-H2 fingers. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerate RING fingers of the Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His residues. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. RING finger/U-box-containing proteins are 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 enable efficient transfer of ubiquitin from E2 to the substrates.


The actual alignment was detected with superfamily member cd16753:

Pssm-ID: 473075 [Multi-domain]  Cd Length: 72  Bit Score: 154.81  E-value: 3.71e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796541   3 TLESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATNEPVESINAFQCPTCRHVITLSQRGLDGLK 74
Cdd:cd16753     1 TLESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCASNESVESITAFQCPTCRYVITLNQRGLEGLK 72
Bbox1_MID1_C-I cd19836
B-box-type 1 zinc finger found in midline-1 (MID1) and similar proteins; MID1, also termed ...
 115-164 1.13e-30

B-box-type 1 zinc finger found in midline-1 (MID1) and similar proteins; MID1, also termed midin, or midline 1 RING finger protein, or putative transcription factor XPRF, or RING finger protein 59 (RNF59), or tripartite motif-containing protein 18 (TRI18), is a microtubule-associated E3 ubiquitin-protein ligase implicated in epithelial-mesenchymal differentiation, cell migration and adhesion, and programmed cell death along specific regions of the ventral midline during embryogenesis. It monoubiquinates the alpha4 subunit of protein phosphatase 2A (PP2A), promoting proteosomal degradation of the catalytic subunit of PP2A (PP2Ac) and preventing the A and B subunits from forming an active complex. It promotes allergen and rhinovirus-induced asthma through the inhibition of PP2A activity. It is strongly upregulated in cytotoxic lymphocytes (CTLs) and directs lytic granule exocytosis and cytotoxicity of killer T cells. Loss-of-function mutations in MID1 lead to the human X-linked Opitz G/BBB (XLOS) syndrome characterized by defective midline development during embryogenesis. MID1 belongs to the C-I subclass of 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 RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, the fibronectin type III domain and the SPRY/B30.2 domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. MID1 heterodimerizes in vitro with its paralog MID2.


:

Pssm-ID: 380894  Cd Length: 50  Bit Score: 114.00  E-value: 1.13e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039796541 115 EKVLCQFCDQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEP 164
Cdd:cd19836     1 EKVLCQFCDQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEP 50
COS pfam18568
TRIM C-terminal subgroup One Signature domain; This domain is found in the C-terminal region ...
 285-336 7.32e-27

TRIM C-terminal subgroup One Signature domain; This domain is found in the C-terminal region of the TRIM subgroup C-1 proteins such as E3 ubiquitin-protein ligase Midline-1 protein which is required for the proper development during embryogenesis. Mutations of MID1 are associated with X-linked Opitz G syndrome, characterized by midline anomalies. This domain is also found in MURF1-3 proteins that do not contain the FNIII and B30.2 domains. MUF1-3 proteins are also associated with microtubules. Deletion of the COS domain does not affect MID1 dimerization but disrupts the localization to the microtubules.


:

Pssm-ID: 465805  Cd Length: 52  Bit Score: 103.09  E-value: 7.32e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039796541 285 NDHARFLQTAKNITERVSMATASSQVLIPEINLNDTFDTFALDFSREKKLLE 336
Cdd:pfam18568   1 TDHARFLQTAKNVHERVSMATASSQVLIPDINLNDAFENFALDFSREKKLLE 52
CC_brat-like super family cl29238
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
 182-306 1.26e-20

coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family contains the coiled-coil (CC) region of Drosophila brain tumor (Brat), a translational repressor that belongs to the tripartite motif (TRIM) protein superfamily. TRIM proteins play important roles in various cellular processes and are involved in many diseases which consists of two B-box domains and a coiled-coil (CC) domain at the N-terminal region, and an NHL domain at the C-terminus. Brat localizes at the basal cortex during asymmetric division of Drosophila neuroblasts by directly interacting with the scaffolding protein Miranda (Mira), which it does through the CC-NHL domain tandem, indicating that the function of the Brat CC domain is to assemble Brat-NHL in dimeric form which is necessary for Mira binding. Brat CC forms an elongated antiparallel dimer similar to its other TRIM protein counterparts, but the overall length of Brat CC dimer is shorter than the TRIMs.


The actual alignment was detected with superfamily member smart00502:

Pssm-ID: 475168  Cd Length: 127  Bit Score: 88.09  E-value: 1.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541  182 KQNLESNLTNLIKRNTELETLLAKLIQTCQHVEVNASRQEAKLTEECDLLIEIIQQRRQIIGTKIKEGKVIRLRKLAQQI 261
Cdd:smart00502   2 REALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQL 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1039796541  262 ANCKQCLERSASLISQAEHSLKENDHARFLQTAKNITERVSMATA 306
Cdd:smart00502  82 ESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLLK 126
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 357-456 2.00e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 54.81  E-value: 2.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 357 SYDTITVHWT--SEDEFSVVSYELQYTIfTGQANVVNVAcdgtcllgsaglcnsadswmiVPNIKQNHYTVHGLQSGTKY 434
Cdd:cd00063    13 TSTSVTLSWTppEDDGGPITGYVVEYRE-KGSGDWKEVE---------------------VTPGSETSYTLTGLKPGTEY 70

                          90       100
                  ....*....|....*....|...
gi 1039796541 435 IFTVKAINQAG-SRSSEPGKLKT 456
Cdd:cd00063    71 EFRVRAVNGGGeSPPSESVTVTT 93
 
Name Accession Description Interval E-value
SPRY_PRY_TRIM18 cd12892
PRY/SPRY domain of TRIM18/MID1, also known as FXY or RNF59; This domain, consisting of the ...
 460-636 4.51e-127

PRY/SPRY domain of TRIM18/MID1, also known as FXY or RNF59; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is at the C-terminus of the overall domain architecture of MID1 (also known as FXY, RNF59, TRIM18) gene represented by a RING finger domain (RING), two B-box motifs (BBOX), coiled-coil C-terminal to Bbox domain (BBC) and fibronectin type 3 domain (FN3). Mutations in the human MID1 gene result in X-linked Opitz G/BBB syndrome (OS), a disorder affecting development of midline structures, causing craniofacial, urogenital, gastrointestinal and cardiovascular abnormalities. A unique MID1 gene mutation located in a variable loop in the SPRY domain alters conformation of the binding pocket and may affect the binding affinity to the PRY/SPRY domain.


Pssm-ID: 240472  Cd Length: 177  Bit Score: 372.04  E-value: 4.51e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 460 PFRLDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAGQGSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPK 539
Cdd:cd12892     1 PFKLDPKSAHRKLKVSHDNLTVERDETSSKKSHTPERFTSQGSYGVAGNVFIDSGRHYWEVVISGSTWYAIGIAYKSAPK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 540 HEWIGKNAASWALCRCHNHWAVRHDGKETPIAPAPHLRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQPVCPTFTVW 619
Cdd:cd12892    81 HEWIGKNSASWVLCRCNNNWVVRHNSKEIPIEPSPHLRRVGILLDYDNGSLSFYDALNSIHLYTFDIAFAQPVCPTFTVW 160

                         170
                  ....*....|....*..
gi 1039796541 620 NKCLTIVTGLPIPDHLD 636
Cdd:cd12892   161 NKCLTILTGLPIPDHLD 177
RING-HC_MID1 cd16753
RING finger, HC subclass, found in midline-1 (MID1) and similar proteins; MID1, also known as ...
 3-74 3.71e-45

RING finger, HC subclass, found in midline-1 (MID1) and similar proteins; MID1, also known as midin, midline 1 RING finger protein, putative transcription factor XPRF, RING finger protein 59 (RNF59), or tripartite motif-containing protein 18 (TRIM18), is a microtubule-associated E3 ubiquitin-protein ligase implicated in epithelial-mesenchymal differentiation, cell migration and adhesion, and programmed cell death along specific regions of the ventral midline during embryogenesis. It monoubiquinates the alpha4 subunit of protein phosphatase 2A (PP2A), promoting proteosomal degradation of the catalytic subunit of PP2A (PP2Ac) and preventing the A and B subunits from forming an active complex. It promotes allergen and rhinovirus-induced asthma through the inhibition of PP2A activity. It is strongly upregulated in cytotoxic lymphocytes (CTLs) and directs lytic granule exocytosis and cytotoxicity of killer T cells. Loss-of-function mutations in MID1 lead to the human X-linked Opitz G/BBB (XLOS) syndrome characterized by defective midline development during embryogenesis. MID1 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. MID1 hetero-dimerizes in vitro with its paralog MID2.


Pssm-ID: 438411 [Multi-domain]  Cd Length: 72  Bit Score: 154.81  E-value: 3.71e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796541   3 TLESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATNEPVESINAFQCPTCRHVITLSQRGLDGLK 74
Cdd:cd16753     1 TLESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCASNESVESITAFQCPTCRYVITLNQRGLEGLK 72
Bbox1_MID1_C-I cd19836
B-box-type 1 zinc finger found in midline-1 (MID1) and similar proteins; MID1, also termed ...
 115-164 1.13e-30

B-box-type 1 zinc finger found in midline-1 (MID1) and similar proteins; MID1, also termed midin, or midline 1 RING finger protein, or putative transcription factor XPRF, or RING finger protein 59 (RNF59), or tripartite motif-containing protein 18 (TRI18), is a microtubule-associated E3 ubiquitin-protein ligase implicated in epithelial-mesenchymal differentiation, cell migration and adhesion, and programmed cell death along specific regions of the ventral midline during embryogenesis. It monoubiquinates the alpha4 subunit of protein phosphatase 2A (PP2A), promoting proteosomal degradation of the catalytic subunit of PP2A (PP2Ac) and preventing the A and B subunits from forming an active complex. It promotes allergen and rhinovirus-induced asthma through the inhibition of PP2A activity. It is strongly upregulated in cytotoxic lymphocytes (CTLs) and directs lytic granule exocytosis and cytotoxicity of killer T cells. Loss-of-function mutations in MID1 lead to the human X-linked Opitz G/BBB (XLOS) syndrome characterized by defective midline development during embryogenesis. MID1 belongs to the C-I subclass of 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 RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, the fibronectin type III domain and the SPRY/B30.2 domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. MID1 heterodimerizes in vitro with its paralog MID2.


Pssm-ID: 380894  Cd Length: 50  Bit Score: 114.00  E-value: 1.13e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039796541 115 EKVLCQFCDQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEP 164
Cdd:cd19836     1 EKVLCQFCDQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEP 50
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 513-631 4.64e-27

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: 106.22  E-value: 4.64e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541  513 SGRHYWEVVTSGSTWYAIGLAYRSAPKHE--WIGKNAASWA--LCRCHNHWAVRhdGKETPIAPAPHLRRVGVLLDYDNG 588
Cdd:smart00449   1 SGRHYFEVEIGDGGHWRVGVATKSVPRGYfaLLGEDKGSWGydGDGGKKYHNST--GPEYGLPLQEPGDVIGCFLDLEAG 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1039796541  589 SIAFYDALSSVH-LHTFHAALAQPVCPTFTVWNKCLTIVTGLPI 631
Cdd:smart00449  79 TISFYKNGKYLHgLAFFDVKFSGPLYPAFSLGSGNSVRLNFGPL 122
COS pfam18568
TRIM C-terminal subgroup One Signature domain; This domain is found in the C-terminal region ...
 285-336 7.32e-27

TRIM C-terminal subgroup One Signature domain; This domain is found in the C-terminal region of the TRIM subgroup C-1 proteins such as E3 ubiquitin-protein ligase Midline-1 protein which is required for the proper development during embryogenesis. Mutations of MID1 are associated with X-linked Opitz G syndrome, characterized by midline anomalies. This domain is also found in MURF1-3 proteins that do not contain the FNIII and B30.2 domains. MUF1-3 proteins are also associated with microtubules. Deletion of the COS domain does not affect MID1 dimerization but disrupts the localization to the microtubules.


Pssm-ID: 465805  Cd Length: 52  Bit Score: 103.09  E-value: 7.32e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039796541 285 NDHARFLQTAKNITERVSMATASSQVLIPEINLNDTFDTFALDFSREKKLLE 336
Cdd:pfam18568   1 TDHARFLQTAKNVHERVSMATASSQVLIPDINLNDAFENFALDFSREKKLLE 52
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 515-630 2.97e-21

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: 89.71  E-value: 2.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 515 RHYWEVV--TSGSTWYAIGLAYRSAP--KHEWIGKNAASWALCRC--HNHWAVRHDGKETPIAPAPhlRRVGVLLDYDNG 588
Cdd:pfam00622   1 RHYFEVEifGQDGGGWRVGWATKSVPrkGERFLGDESGSWGYDGWtgKKYWASTSPLTGLPLFEPG--DVIGCFLDYEAG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1039796541 589 SIAFYDALSSvHLHTFH-AALAQPVCPTFTV-WNKCLTIVTGLP 630
Cdd:pfam00622  79 TISFTKNGKS-LGYAFRdVPFAGPLFPAVSLgAGEGLKFNFGLR 121
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
 182-306 1.26e-20

B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains


Pssm-ID: 128778  Cd Length: 127  Bit Score: 88.09  E-value: 1.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541  182 KQNLESNLTNLIKRNTELETLLAKLIQTCQHVEVNASRQEAKLTEECDLLIEIIQQRRQIIGTKIKEGKVIRLRKLAQQI 261
Cdd:smart00502   2 REALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQL 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1039796541  262 ANCKQCLERSASLISQAEHSLKENDHARFLQTAKNITERVSMATA 306
Cdd:smart00502  82 ESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLLK 126
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 357-456 2.00e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 54.81  E-value: 2.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 357 SYDTITVHWT--SEDEFSVVSYELQYTIfTGQANVVNVAcdgtcllgsaglcnsadswmiVPNIKQNHYTVHGLQSGTKY 434
Cdd:cd00063    13 TSTSVTLSWTppEDDGGPITGYVVEYRE-KGSGDWKEVE---------------------VTPGSETSYTLTGLKPGTEY 70

                          90       100
                  ....*....|....*....|...
gi 1039796541 435 IFTVKAINQAG-SRSSEPGKLKT 456
Cdd:cd00063    71 EFRVRAVNGGGeSPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 359-446 1.57e-08

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 52.23  E-value: 1.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541  359 DTITVHWTSEDEFSVVSYELQYTIFTGQANvvnvacdgtcllgsaglcnsaDSWMIVP-NIKQNHYTVHGLQSGTKYIFT 437
Cdd:smart00060  15 TSVTLSWEPPPDDGITGYIVGYRVEYREEG---------------------SEWKEVNvTPSSTSYTLTGLKPGTEYEFR 73


                   ....*....
gi 1039796541  438 VKAINQAGS 446
Cdd:smart00060  74 VRAVNGAGE 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
342-460 3.29e-07

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 53.47  E-value: 3.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 342 TAPNPPAireELcTASYDT---ITVHWTSEDEFSVVSYELQYTIftgqanvvnvacdgtcllgsaglcNSADSWMIVPNI 418
Cdd:COG3401   231 TPPSAPT---GL-TATADTpgsVTLSWDPVTESDATGYRVYRSN------------------------SGDGPFTKVATV 282

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1039796541 419 KQNHYTVHGLQSGTKYIFTVKAINQAGSRS--SEPGKLKTNSQP 460
Cdd:COG3401   283 TTTSYTDTGLTNGTTYYYRVTAVDAAGNESapSNVVSVTTDLTP 326
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
 4-89 1.06e-06

DNA repair protein rad18; All proteins in this family for which functions are known are involved in nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273165 [Multi-domain]  Cd Length: 397  Bit Score: 51.54  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541   4 LESELTCPICLELFEDPLLLPCAHSLCFNCAHRilvshCATNEPvesinafQCPTCRHVITLSQrgldgLKRNVTLQNII 83
Cdd:TIGR00599  23 LDTSLRCHICKDFFDVPVLTSCSHTFCSLCIRR-----CLSNQP-------KCPLCRAEDQESK-----LRSNWLVSEIV 85


                  ....*.
gi 1039796541  84 DRFQKA 89
Cdd:TIGR00599  86 ESFKNL 91
fn3 pfam00041
Fibronectin type III domain;
359-445 3.75e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.48  E-value: 3.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 359 DTITVHWTSEDEFS--VVSYELQYtiftgqanvvnVACDGtcllgsaglcNSADSWMIVPNIkQNHYTVHGLQSGTKYIF 436
Cdd:pfam00041  14 TSLTVSWTPPPDGNgpITGYEVEY-----------RPKNS----------GEPWNEITVPGT-TTSVTLTGLKPGTEYEV 71


                  ....*....
gi 1039796541 437 TVKAINQAG 445
Cdd:pfam00041  72 RVQAVNGGG 80
PLN03208 PLN03208
E3 ubiquitin-protein ligase RMA2; Provisional
 7-98 1.17e-05

E3 ubiquitin-protein ligase RMA2; Provisional


Pssm-ID: 178747 [Multi-domain]  Cd Length: 193  Bit Score: 46.62  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541   7 ELTCPICLELFEDPLLLPCAHSLCFNCAHRILVshcATNEPVESINAF-------QCPTCRHVITlsqrgldglkrNVTL 79
Cdd:PLN03208   18 DFDCNICLDQVRDPVVTLCGHLFCWPCIHKWTY---ASNNSRQRVDQYdhkreppKCPVCKSDVS-----------EATL 83

                          90
                  ....*....|....*....
gi 1039796541  80 QNIIDRFQKASVSGPNSPS 98
Cdd:PLN03208   84 VPIYGRGQKAPQSGSNVPS 102
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 10-59 1.30e-05

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


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 42.50  E-value: 1.30e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039796541   10 CPICLELF-EDPLLLPCAHSLCFNCAHRILVSHCATnepvesinafqCPTC 59
Cdd:smart00184   1 CPICLEEYlKDPVILPCGHTFCRSCIRKWLESGNNT-----------CPIC 40
zf-RING_UBOX pfam13445
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.
 10-57 2.72e-05

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: 41.62  E-value: 2.72e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1039796541  10 CPICLELFEDPlLLPCAHSLCFNCAHRILVShcatnepveSINAFQCP 57
Cdd:pfam13445   1 CPICLELFTDP-VLPCGHTFCRECLEEMSQK---------KGGKFKCP 38
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 176-309 7.38e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.65  E-value: 7.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541  176 LEHEDEKQNLESNLTNLIKRNTELETLLAKLIQtcQHVEVNASRQEAKLTEECDLLIEIIQQrRQIIGTKIKEGKVIRLR 255
Cdd:TIGR00618  249 REAQEEQLKKQQLLKQLRARIEELRAQEAVLEE--TQERINRARKAAPLAAHIKAVTQIEQQ-AQRIHTELQSKMRSRAK 325

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039796541  256 KLAQQIANCKQCLERSASLISQAEHSLKENDHARFLQTAKNITERVSMATASSQ 309
Cdd:TIGR00618  326 LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ 379
RAD18 COG5432
RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];
4-60 2.46e-03

RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];


Pssm-ID: 227719 [Multi-domain]  Cd Length: 391  Bit Score: 40.84  E-value: 2.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796541   4 LESELTCPICLELFEDPLLLPCAHSLCFNCAHRILvshcaTNEPVesinafqCPTCR 60
Cdd:COG5432    22 LDSMLRCRICDCRISIPCETTCGHTFCSLCIRRHL-----GTQPF-------CPVCR 66
BBOX smart00336
B-Box-type zinc finger;
114-152 4.01e-03

B-Box-type zinc finger;


Pssm-ID: 197662 [Multi-domain]  Cd Length: 42  Bit Score: 35.39  E-value: 4.01e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1039796541  114 AEKVLCQFCDQdpaQDAVKTCVTCEVSYCDECLKATHPN 152
Cdd:smart00336   1 QRAPKCDSHGD---EPAEFFCEECGALLCRTCDEAEHRG 36
 
Name Accession Description Interval E-value
SPRY_PRY_TRIM18 cd12892
PRY/SPRY domain of TRIM18/MID1, also known as FXY or RNF59; This domain, consisting of the ...
 460-636 4.51e-127

PRY/SPRY domain of TRIM18/MID1, also known as FXY or RNF59; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is at the C-terminus of the overall domain architecture of MID1 (also known as FXY, RNF59, TRIM18) gene represented by a RING finger domain (RING), two B-box motifs (BBOX), coiled-coil C-terminal to Bbox domain (BBC) and fibronectin type 3 domain (FN3). Mutations in the human MID1 gene result in X-linked Opitz G/BBB syndrome (OS), a disorder affecting development of midline structures, causing craniofacial, urogenital, gastrointestinal and cardiovascular abnormalities. A unique MID1 gene mutation located in a variable loop in the SPRY domain alters conformation of the binding pocket and may affect the binding affinity to the PRY/SPRY domain.


Pssm-ID: 240472  Cd Length: 177  Bit Score: 372.04  E-value: 4.51e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 460 PFRLDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAGQGSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPK 539
Cdd:cd12892     1 PFKLDPKSAHRKLKVSHDNLTVERDETSSKKSHTPERFTSQGSYGVAGNVFIDSGRHYWEVVISGSTWYAIGIAYKSAPK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 540 HEWIGKNAASWALCRCHNHWAVRHDGKETPIAPAPHLRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQPVCPTFTVW 619
Cdd:cd12892    81 HEWIGKNSASWVLCRCNNNWVVRHNSKEIPIEPSPHLRRVGILLDYDNGSLSFYDALNSIHLYTFDIAFAQPVCPTFTVW 160

                         170
                  ....*....|....*..
gi 1039796541 620 NKCLTIVTGLPIPDHLD 636
Cdd:cd12892   161 NKCLTILTGLPIPDHLD 177
SPRY_PRY_TRIM1 cd13739
PRY/SPRY domain of tripartite motif-binding protein 1 (TRIM1) or MID2; This domain, consisting ...
 461-630 6.41e-91

PRY/SPRY domain of tripartite motif-binding protein 1 (TRIM1) or MID2; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM1 (also known as MID2 or midline 2). MID2 and its close homolog, TRIM18 (also known as MID1), both contain a B30.2-like domain at their C-terminus and a single fibronectin type III (FN3) motif between it and their N-terminal RBCC domain. MID2 and MID1 coiled-coil motifs mediate both homo- and heterodimerization, a prerequisite for association of the rapamycin-sensitive PP2A regulatory subunit Alpha 4 with microtubules. Mutations in MID1 have shown to cause Opitz syndrome, a disorder causing congenital anomalies such as cleft lip and palate as well as heart defects.


Pssm-ID: 293974  Cd Length: 170  Bit Score: 278.82  E-value: 6.41e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 461 FRLDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAGQGSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPKH 540
Cdd:cd13739     1 FKLDPKMAHKKLKISNDGLQMEKDESSLKKSHTPERFSGTGCYGAAGNIFIDSGCHYWEVVVGSSTWYAIGIAYKSAPKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 541 EWIGKNAASWALCRCHNHWAVRHDGKETPIAPAPHLRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQPVCPTFTVWN 620
Cdd:cd13739    81 EWIGKNSSSWVFSRCNNNFVVRHNNKEMLVDVPPQLKRLGVLLDYDNNMLSFYDPANSLHLHTFEVSFILPVCPTFTIWN 160

                         170
                  ....*....|
gi 1039796541 621 KCLTIVTGLP 630
Cdd:cd13739   161 KSLMILSGLP 170
SPRY_PRY_C-II cd13734
PRY/SPRY domain in tripartite motif-containing proteins 1, 9, 18, 36, 46, 67,76 (TRIM1, TRIM9, ...
 461-626 5.01e-82

PRY/SPRY domain in tripartite motif-containing proteins 1, 9, 18, 36, 46, 67,76 (TRIM1, TRIM9, TRIM18, TRIM36, TRIM46, TRIM67, TRIM76); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several Class I TRIM proteins, including TRIM1, TRIM9, TRIM18, TRIM36, TRIM46, TRIM67 and TRIM76. TRIM1 (also known as MID2) and its close homolog, TRIM18 (also known as MID1), both contain a B30.2-like domain at their C-terminus and a single fibronectin type III (FN3) motif between it and their N-terminal RBCC domain. Their coiled-coil motifs mediate both homo- and heterodimerization, a prerequisite for association of the rapamycin-sensitive PP2A regulatory subunit Alpha 4 with microtubules. Mutations in TRIM18 have shown to cause Opitz syndrome, a disorder causing congenital anomalies such as cleft lip and palate as well as heart defects. TRIM9 is expressed mainly in the cerebral cortex, and functions as an E3 ubiquitin ligase. Its immunoreactivity is severely decreased in affected brain areas in Parkinson's disease and dementia with Lewy bodies, possibly playing an important role in the regulation of neuronal function and participating in pathological process of Lewy body disease through its ligase. TRIM36 interacts with centromere protein-H, one of the kinetochore proteins and possibly associates with chromosome segregation; an excess of TRIM36 may cause chromosomal instability. TRIM46 has not yet been characterized. TRIM67 negatively regulates Ras activity via degradation of 80K-H, leading to neural differentiation, including neuritogenesis. TRIM76 (also known as cardiomyopathy-associated protein 5 or CMYA5) is a muscle-specific member of the TRIM superfamily, but lacks the RING domain. It is possibly involved in protein kinase A signaling as well as vesicular trafficking. It has also been implicated in Duchenne muscular dystrophy and cardiac disease. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site.


Pssm-ID: 293969 [Multi-domain]  Cd Length: 166  Bit Score: 255.67  E-value: 5.01e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 461 FRLDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAGQGSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPKH 540
Cdd:cd13734     1 FKLDPKTAHRKLRLSNDNLTVEYDPEGSKDQAAVLPRRFTGSPAVLGDVAISSGRHYWEVSVSRSTSYRVGVAYKSAPRD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 541 EWIGKNAASWALCRCHNHWAVRHDGKETPIAPAPHLRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQPVCPTFTVWN 620
Cdd:cd13734    81 EDLGKNSTSWCLSRDNNRYTARHDGKVVDLRVTGHPARIGVLLDYDNGTLSFYDAESKQHLYTFHVDFEGPVCPAFAVWN 160


                  ....*.
gi 1039796541 621 KCLTIV 626
Cdd:cd13734   161 GSLTLH 166
RING-HC_MID1 cd16753
RING finger, HC subclass, found in midline-1 (MID1) and similar proteins; MID1, also known as ...
 3-74 3.71e-45

RING finger, HC subclass, found in midline-1 (MID1) and similar proteins; MID1, also known as midin, midline 1 RING finger protein, putative transcription factor XPRF, RING finger protein 59 (RNF59), or tripartite motif-containing protein 18 (TRIM18), is a microtubule-associated E3 ubiquitin-protein ligase implicated in epithelial-mesenchymal differentiation, cell migration and adhesion, and programmed cell death along specific regions of the ventral midline during embryogenesis. It monoubiquinates the alpha4 subunit of protein phosphatase 2A (PP2A), promoting proteosomal degradation of the catalytic subunit of PP2A (PP2Ac) and preventing the A and B subunits from forming an active complex. It promotes allergen and rhinovirus-induced asthma through the inhibition of PP2A activity. It is strongly upregulated in cytotoxic lymphocytes (CTLs) and directs lytic granule exocytosis and cytotoxicity of killer T cells. Loss-of-function mutations in MID1 lead to the human X-linked Opitz G/BBB (XLOS) syndrome characterized by defective midline development during embryogenesis. MID1 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. MID1 hetero-dimerizes in vitro with its paralog MID2.


Pssm-ID: 438411 [Multi-domain]  Cd Length: 72  Bit Score: 154.81  E-value: 3.71e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796541   3 TLESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATNEPVESINAFQCPTCRHVITLSQRGLDGLK 74
Cdd:cd16753     1 TLESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCASNESVESITAFQCPTCRYVITLNQRGLEGLK 72
RING-HC_MID2 cd16754
RING finger, HC subclass, found in midline-2 (MID2) and similar proteins; MID2, also known as ...
 1-70 8.77e-39

RING finger, HC subclass, found in midline-2 (MID2) and similar proteins; MID2, also known as midin-2, midline defect 2, RING finger protein 60 (RNF60), or tripartite motif-containing protein 1 (TRIM1), is a probable E3 ubiquitin-protein ligase and is highly related to MID1 that associates with cytoplasmic microtubules along their length and throughout the cell cycle. Like MID1, MID2 associates with the microtubule network and may at least partially compensate for the loss of MID1. Both MID1 and MID2 interacts with Alpha 4, which is a regulatory subunit of PP2-type phosphatases, such as PP2A, and an integral component of the rapamycin-sensitive signaling pathway. MID2 can also substitute for MID1 to control exocytosis of lytic granules in cytotoxic T cells. Loss-of-function mutations in MID2 lead to the human X-linked intellectual disability (XLID). MID2 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxy-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. MID2 hetero-dimerizes in vitro with its paralog MID1.


Pssm-ID: 438412 [Multi-domain]  Cd Length: 70  Bit Score: 137.04  E-value: 8.77e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541   1 METLESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATNEPVESINAFQCPTCRHVITLSQRGL 70
Cdd:cd16754     1 METLESELTCPICLELFEDPLLLPCAHSLCFSCAHRILTSGCASGESIEPPSAFQCPTCRYVISLNHRGL 70
SPRY_PRY_C-I_2 cd12891
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM14-like, ...
 463-625 5.42e-37

PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM14-like, TRIM16-like, TRIM25-like, TRIM47-like, TRIM65 and RNF135, and stonustoxin; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several Class I TRIM proteins, including TRIM14, TRIM16 and TRIM25, TRIM47 as well as RING finger protein RNF135 and stonustoxin, a secreted poisonous protein of the stonefish Synanceja horrida. TRIM16 (also known as estrogen-responsive B box protein or EBBP) has E3 ubiquitin ligase activity. It is a regulator of keratinocyte differentiation and a tumor suppressor in retinoid-sensitive neuroblastoma. TRIM25 (also called Efp) ubiquitinates the N terminus of the viral RNA receptor retinoic acid-inducible gene-I (RIG-I) in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. It has been shown that the influenza A virus targets TRIM25 and disables its antiviral function. TRIM47, also known as GOA (Gene overexpressed in astrocytoma protein) or RNF100 (RING finger protein 100), is highly expressed in kidney tubular cells, but low expressed in most tissue. It is overexpressed in astrocytoma tumor cells and plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis. RNF135 ubiquitinates RIG-I (retinoic acid-inducible gene-I) to promote interferon-beta induction during the early phase of viral infection. Stonustoxin (STNX) is a hypotensive and lethal protein factor that also possesses other biological activities such as species-specific hemolysis (due to its ability to form pores in the cell membrane) and platelet aggregation, edema-induction, and endothelium-dependent vasorelaxation (mediated by the nitric oxide pathway and activation of potassium channels). The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site.


Pssm-ID: 293949 [Multi-domain]  Cd Length: 167  Bit Score: 135.84  E-value: 5.42e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAgqgSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPKHE- 541
Cdd:cd12891     3 LDPNTAHNNLALSGDLKTVTCSSENQHYPDSPERFT---HSQVLSTQSFSSGRHYWEVEVSESGGWSVGVAYPSIERKGd 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 542 --WIGKNAASWALCRCHNHWAVRHDGKETPIAPAPHlRRVGVLLDYDNGSIAFYDALSSV-HLHTFHAALAQPVCPTFTV 618
Cdd:cd12891    80 esRIGRNDKSWCLEWQDKSFSAWHNNEETPLPSVSS-RRLGVYLDYEAGRLSFYELSDPIrHLHTFTATFTEPLHPAFWV 158


                  ....*...
gi 1039796541 619 W-NKCLTI 625
Cdd:cd12891   159 LeGGWIRI 166
SPRY_PRY cd12874
PRY/SPRY domain, also known as B30.2; This domain contains residues in the N-terminus that ...
 463-619 5.50e-36

PRY/SPRY domain, also known as B30.2; This domain contains residues in the N-terminus that form a distinct PRY domain structure such that the 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 core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). 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. Among the TRIM proteins, also known as the N-terminal RING finger/B-box/coiled coil (RBCC) family, only Classes I and II contain the B30.2 domain that has evolved under positive selection. Class I TRIM proteins include multiple members involved in antiviral immunity at various levels of interferon signaling cascade. Among the 75 human TRIMs, roughly half enhance immune response, which they do at multiple levels in signaling pathways. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site.


Pssm-ID: 293934 [Multi-domain]  Cd Length: 168  Bit Score: 132.82  E-value: 5.50e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFagQGSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPKHEW 542
Cdd:cd12874     3 FDPDTAHLNLILSDDLRSVRVGDISQHPPEPPPRF--FECWQVLGSQSFSSGRHYWEVDVQDDSSWYVGVTYKSLPRKGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 543 ---IGKNAASWALCRCHNHWAVRHDGKETPIAPAPHlRRVGVLLDYDNGSIAFYDALSSV-HLHTFHAALAQPVCPTFTV 618
Cdd:cd12874    81 msnLGRNNGSWCLEWRENEFSAWHNNPETRLPVTPP-RRLGVFLDCDGGSLSFYGVTDGVqLLYTFKAKFTEPLYPAFWL 159


                  .
gi 1039796541 619 W 619
Cdd:cd12874   160 G 160
SPRY_PRY_FSD1 cd12901
Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This ...
 461-633 7.15e-35

Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This domain is part of the fibronectin type III and SPRY domain containing 1 (FSD1) and FSD1-like (FSD1L) proteins. These are centrosome-associated proteins that are characterized by an N-terminal coiled-coil region downstream of B-box (BBC) domain, a central fibronectin type III (FN3) domain, and C-terminal repeats in PRY/SPRY domain. The FSD1 protein associates with a subset of microtubules and may be involved in the stability and organization of microtubules during cytokinesis.


Pssm-ID: 293958  Cd Length: 207  Bit Score: 131.10  E-value: 7.15e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 461 FRLDPKSAHRKLKVshDNLTVERDESSSK------------KSHAP----------------------ERFAGQgSYGVA 506
Cdd:cd12901     1 FKLDASSSHQNLKV--EDLSVEWDATGGKvlqkikgrendgRSRTAsprnssarcqspkrmpsarggrDRFTAE-SYTVL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 507 GNVFIDSGRHYWEV-VTSGSTWYAIGLAYRSAPKHEWIGKNAASWALcrcH-NHW-----AVRHDGKETPI-APAPHlrR 578
Cdd:cd12901    78 GDTLIDGGQHYWEVrAQKDSKAFSVGVAYRSLGKFDQLGKTNASWCL---HvNNWlqnsfAAKHNNKAKTLdVPVPD--R 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039796541 579 VGVLLDYDNGSIAFYDALSSVHLHTFHAALAQPVCPTFTVWNKCLTIVTGLPIPD 633
Cdd:cd12901   153 IGVYCDFDEGQLSFYNARTKQLLHTFKMKFTQPVLPAFMVWCGGLSVSTGLQVPS 207
SPRY_PRY_SNTX cd16040
Stonustoxin subunit alpha or SNTX subunit alpha; This domain, consisting of the distinct ...
 463-619 2.14e-32

Stonustoxin subunit alpha or SNTX subunit alpha; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of Stonustoxin alpha proteins. Stonustoxin (SNTX) is a multifunctional lethal protein isolated from venom elaborated by the stonefish. It comprises two subunits, termed alpha and beta. SNTX elicits an array of biological responses, particularly a potent hypotension and respiratory difficulties.


Pssm-ID: 294002 [Multi-domain]  Cd Length: 180  Bit Score: 123.36  E-value: 2.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAG-------QGSygvagnvfidSGRHYWEVVTSGSTWYaIGLAYR 535
Cdd:cd16040    13 LDPNTAHRNLSLSEGNRKVTRVKEEQPYPDHPERFDYwpqvlcrEGL----------SGRCYWEVEWSGGGVD-IAVAYK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 536 SAPKHE-----WIGKNAASWALCRCHNHWAVRHDGKETPIA-PAPHLRRVGVLLDYDNGSIAFYDALSSV-HLHTFHAAL 608
Cdd:cd16040    82 GISRKGdgddsRFGYNDKSWSLECSPSGYSFWHNNKKTEISvPSSSSSRVGVYLDHSAGTLSFYSVSDTMtLLHTVQTTF 161

                         170
                  ....*....|.
gi 1039796541 609 AQPVCPTFTVW 619
Cdd:cd16040   162 TEPLYPGFGVG 172
RING-HC_MID_C-I cd16575
RING finger, HC subclass, found in midline-1 (MID1), midline-2 (MID2) and similar proteins; ...
 8-61 5.96e-31

RING finger, HC subclass, found in midline-1 (MID1), midline-2 (MID2) and similar proteins; MID1, also known as midin, midline 1 RING finger protein, putative transcription factor XPRF, RING finger protein 59 (RNF59), or tripartite motif-containing protein 18 (TRIM18), is a microtubule-associated E3 ubiquitin-protein ligase implicated in epithelial-mesenchymal differentiation, cell migration and adhesion, and programmed cell death along specific regions of the ventral midline during embryogenesis. MID2, also known as midin-2, midline defect 2, RING finger protein 60 (RNF60), or tripartite motif-containing protein 1 (TRIM1), associates with the microtubule network and may at least partially compensate for the loss of MID1. Both MID1 and MID2 interacts with Alpha 4, which is a regulatory subunit of PP2-type phosphatases, such as PP2A, and an integral component of the rapamycin-sensitive signaling pathway. They also play a central role in the regulation of granule exocytosis. Functional redundancy exists between MID1 and MID2 in cytotoxic lymphocytes (CTL). Both MID1 and MID2 belong to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438237 [Multi-domain]  Cd Length: 54  Bit Score: 114.64  E-value: 5.96e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039796541   8 LTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATNEPVESINAFQCPTCRH 61
Cdd:cd16575     1 LTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCASNESVESITAFQCPTCRY 54
Bbox1_MID1_C-I cd19836
B-box-type 1 zinc finger found in midline-1 (MID1) and similar proteins; MID1, also termed ...
 115-164 1.13e-30

B-box-type 1 zinc finger found in midline-1 (MID1) and similar proteins; MID1, also termed midin, or midline 1 RING finger protein, or putative transcription factor XPRF, or RING finger protein 59 (RNF59), or tripartite motif-containing protein 18 (TRI18), is a microtubule-associated E3 ubiquitin-protein ligase implicated in epithelial-mesenchymal differentiation, cell migration and adhesion, and programmed cell death along specific regions of the ventral midline during embryogenesis. It monoubiquinates the alpha4 subunit of protein phosphatase 2A (PP2A), promoting proteosomal degradation of the catalytic subunit of PP2A (PP2Ac) and preventing the A and B subunits from forming an active complex. It promotes allergen and rhinovirus-induced asthma through the inhibition of PP2A activity. It is strongly upregulated in cytotoxic lymphocytes (CTLs) and directs lytic granule exocytosis and cytotoxicity of killer T cells. Loss-of-function mutations in MID1 lead to the human X-linked Opitz G/BBB (XLOS) syndrome characterized by defective midline development during embryogenesis. MID1 belongs to the C-I subclass of 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 RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, the fibronectin type III domain and the SPRY/B30.2 domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. MID1 heterodimerizes in vitro with its paralog MID2.


Pssm-ID: 380894  Cd Length: 50  Bit Score: 114.00  E-value: 1.13e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039796541 115 EKVLCQFCDQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEP 164
Cdd:cd19836     1 EKVLCQFCDQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEP 50
SPRY_PRY_C-I_1 cd13733
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM5, TRIM6, TRIM7, ...
 460-616 5.54e-29

PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM5, TRIM6, TRIM7, TRIM10, TRIM11, TRIM17, TRIM20, TRIM21, TRIM27, TRIM35, TRIM38, TRIM41, TRIM50, TRIM58, TRIM60, TRIM62, TRIM69, TRIM72, NF7 and bloodthirsty; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several Class IV TRIM proteins, including TRIM7, TRIM35, TRIM41, TRIM50, TRIM62, TRIM69, TRIM72, TRIM protein NF7 and bloodthirsty (bty). TRIM7 interacts with glycogenin and stimulates its self-glucosylating activity via its SPRY domain. TRIM35 may play a role as a tumor suppressor and is implicated in the cell death mechanism. TRIM41 is localized to speckles in the cytoplasm and nucleus, and functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C. TRIM50, an E3 ubiquitin ligase, is deleted in Williams-Beuren (WBS) syndrome, a multi-system neurodevelopmental disorder caused by the deletion of contiguous genes at chromosome region 7q11.23. TRIM62 is involved in the morphogenesis of the mammary gland; loss of TRIM62 gene expression in breast is associated with increased risk of recurrence in early-onset breast cancer. TRIM69 is a novel testis E3 ubiquitin ligase that may function to ubiquitinate its particular substrates during spermatogenesis. In humans, TRIM69 localizes in the cytoplasm and nucleus, and requires an intact RING finger domain to function. TRIM protein NF7, which also contains a chromodomain (CHD) at the N-terminus and an RFP (Ret finger protein)-like domain at the C-terminus, is required for its association with transcriptional units of RNA polymerase II which is mediated by a trimeric B box. In Xenopus oocyte, xNF7 has been identified as a nuclear microtubule-associated protein (MAP) whose microtubule-bundling activity, but not E3-ligase activity, contributes to microtubule organization and spindle integrity. Bloodthirsty (bty) is a novel gene identified in zebrafish and has been shown to likely play a role in in regulation of the terminal steps of erythropoiesis. TRIM72 has been shown to perform a critical function in membrane repair following acute muscle injury by nucleating the assembly of the repair machinery at injury sites. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site.


Pssm-ID: 293968 [Multi-domain]  Cd Length: 174  Bit Score: 113.34  E-value: 5.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 460 PFRLDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFagQGSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPK 539
Cdd:cd13733     1 DVTLDPDTAHPNLILSEDLKSVRYGDKRQNLPDNPERF--DTCVCVLGSEGFSSGRHYWEVEVGGKTDWDLGVARESVNR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 540 HEWIGKNAAS--WALCRCHNH--WAvrHDGKETPIAPAPHLRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQPVCPT 615
Cdd:cd13733    79 KGKITLSPENgyWTVGLRNGNeyKA--LTSPSTPLSLREKPQKVGVFLDYEEGQVSFYNVDDGSHIYTFTDCFTEKLYPY 156


                  .
gi 1039796541 616 F 616
Cdd:cd13733   157 F 157
Bbox1_MID2_C-I cd19837
B-box-type 1 zinc finger found in midline-2 (MID2) and similar proteins; MID2, also known as ...
 115-167 2.54e-28

B-box-type 1 zinc finger found in midline-2 (MID2) and similar proteins; MID2, also known as midin-2, midline defect 2, RING finger protein 60 (RNF60), or tripartite motif-containing protein 1 (TRIM1), is a probable E3 ubiquitin-protein ligase that is highly related to MID1, which associates with cytoplasmic microtubules along their length and throughout the cell cycle. Like MID1, MID2 associates with the microtubule network and may at least partially compensate for the loss of MID1. Both MID1 and MID2 interacts with alpha4, a regulatory subunit of PP2-type phosphatases, such as PP2A, and an integral component of the rapamycin-sensitive signaling pathway. MID2 can also substitute for MID1 to control exocytosis of lytic granules in cytotoxic T cells. Loss-of-function mutations in MID2 lead to human X-linked intellectual disability (XLID). MID2 belongs to the C-I subclass of 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 RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxy-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. MID2 heterodimerizes in vitro with its paralog MID1.


Pssm-ID: 380895  Cd Length: 53  Bit Score: 107.44  E-value: 2.54e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039796541 115 EKVLCQFCDQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEPIPD 167
Cdd:cd19837     1 ERIACQFCEQEPPRDAVKTCITCEVSYCDRCLRATHPNKKPFTSHRLVEPVPD 53
SPRY_PRY_TRIM14 cd13738
PRY/SPRY domain of tripartite motif-binding protein 14 (TRIM14); This is a TRIM14 domain ...
 463-625 3.74e-28

PRY/SPRY domain of tripartite motif-binding protein 14 (TRIM14); This is a TRIM14 domain family contains residues in the N-terminus that form a distinct PRY domain structure such that the B30.2 domain consists of PRY and SPRY subdomains. TRIM14 domains have yet to be characterized. These B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. It belongs to Class IV TRIM protein family which has members involved in antiviral immunity at various levels of interferon signaling cascade.


Pssm-ID: 293973 [Multi-domain]  Cd Length: 173  Bit Score: 111.03  E-value: 3.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFagQGSYGVAGNVFIDSGRHYWEV--VTSGSTWYaIGLAYRS---- 536
Cdd:cd13738     3 LEPDTLHPRLRLSDDRLTVSCGWLGTLGLCPPQRF--DKLWQVLSRDSFFSGRHYWEVdlQEAGAGWW-VGAAYPSigrk 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 537 -APKHEWIGKNAASWALCRCHNHWAVRHDGKETPIAPAPHLRRVGVLLDYDNGSIAFYDALSSV-HLHTFHAALAQPVCP 614
Cdd:cd13738    80 gDSEAARLGWNRQSWCLKRYDLEYWAFHDGQRSRLRPEDDPDRLGVFLDYEAGILSFYDVTGGMtHLHTFRATFQEPLYP 159

                         170
                  ....*....|.
gi 1039796541 615 TFTVWNKCLTI 625
Cdd:cd13738   160 ALRLWEGSISI 170
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 513-631 4.64e-27

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: 106.22  E-value: 4.64e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541  513 SGRHYWEVVTSGSTWYAIGLAYRSAPKHE--WIGKNAASWA--LCRCHNHWAVRhdGKETPIAPAPHLRRVGVLLDYDNG 588
Cdd:smart00449   1 SGRHYFEVEIGDGGHWRVGVATKSVPRGYfaLLGEDKGSWGydGDGGKKYHNST--GPEYGLPLQEPGDVIGCFLDLEAG 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1039796541  589 SIAFYDALSSVH-LHTFHAALAQPVCPTFTVWNKCLTIVTGLPI 631
Cdd:smart00449  79 TISFYKNGKYLHgLAFFDVKFSGPLYPAFSLGSGNSVRLNFGPL 122
COS pfam18568
TRIM C-terminal subgroup One Signature domain; This domain is found in the C-terminal region ...
 285-336 7.32e-27

TRIM C-terminal subgroup One Signature domain; This domain is found in the C-terminal region of the TRIM subgroup C-1 proteins such as E3 ubiquitin-protein ligase Midline-1 protein which is required for the proper development during embryogenesis. Mutations of MID1 are associated with X-linked Opitz G syndrome, characterized by midline anomalies. This domain is also found in MURF1-3 proteins that do not contain the FNIII and B30.2 domains. MUF1-3 proteins are also associated with microtubules. Deletion of the COS domain does not affect MID1 dimerization but disrupts the localization to the microtubules.


Pssm-ID: 465805  Cd Length: 52  Bit Score: 103.09  E-value: 7.32e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039796541 285 NDHARFLQTAKNITERVSMATASSQVLIPEINLNDTFDTFALDFSREKKLLE 336
Cdd:pfam18568   1 TDHARFLQTAKNVHERVSMATASSQVLIPDINLNDAFENFALDFSREKKLLE 52
SPRY_PRY_TRIM7_like cd12888
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7)-like, including TRIM7, TRIM10, ...
 463-619 4.95e-26

PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7)-like, including TRIM7, TRIM10, TRIM15, TRIM26, TRIM39, TRIM41; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several tripartite motif-containing (TRIM) proteins, including TRIM7 (also referred to as glycogenin-interacting protein, RING finger protein 90 or RNF90), TRIM10, TRIM15, TRIM26, TRIM39 and TRIM41. TRIM7 or GNIP interacts with glycogenin and stimulates its self-glucosylating activity via its SPRY domain. TRIM10 (also known as hematopoietic RING finger 1 (HERF1) or TRIM10/HERF1) plays a key role in definitive erythroid development; downregulation of the Spi-1/PU.1 oncogene induces the expression of TRIM10/HERF1, a key factor required for terminal erythroid cell differentiation and survival. Antiviral activity of TRIM15 is dependent on the ability of its B-box to interact with the MLV Gag precursor protein; downregulation of TRIM15, along with TRIM11, enhances virus release suggesting that these proteins contribute to the endogenous restriction of retroviruses in cells. Tripartite motif-containing 26 (TRIM26) function is as yet unknown; however, since it is localized in the human histocompatibility complex (MHC) class I region, TRIM26 may play a role in immune response although studies show no association between TRIM26 polymorphisms and the risk of aspirin-exacerbated respiratory disease. TRIM39 is a MOAP-1 (Modulator of Apoptosis)-binding protein that stabilizes MOAP-1 through inhibition of its poly-ubiquitination process. TRIM41 (also known as RING finger-interacting protein with C kinase or RINCK) functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C.


Pssm-ID: 293946 [Multi-domain]  Cd Length: 169  Bit Score: 104.95  E-value: 4.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAGqgSYGVAGNVFIDSGRHYWEV-VTSGSTWyAIGLAYRSAPKHE 541
Cdd:cd12888     4 LDPDTAHPRLVLSEDRKSVRWGDTRQDLPDNPERFDT--WPCVLGCEGFTSGRHYWEVeVGDGGGW-AVGVARESVRRKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 542 WIGKNAAS--WALCRCHN-HWAVRHDGKETPIAPAPhlRRVGVLLDYDNGSIAFYDALSSVHLHTFHAA--LAQPVCPTF 616
Cdd:cd12888    81 EISFSPEEgiWAVGQWGGqYWALTSPETPLPLSEVP--RRIRVYLDYEGGQVAFFDADNEAPIFTFPPAsfAGERIFPWF 158


                  ...
gi 1039796541 617 TVW 619
Cdd:cd12888   159 WVG 161
SPRY_PRY_SPRYD4 cd12903
PRY/SPRY domain containing protein 4 (SPRYD4); This domain, consisting of the distinct ...
 461-620 2.19e-25

PRY/SPRY domain containing protein 4 (SPRYD4); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain and is encoded by the SPRYD4 gene. SPRYD4 (SPRY containing domain 4) is ubiquitously expressed in many human tissues, most strongly in kidney, bladder, brain, thymus and stomach. Subcellular localization demonstrates that SPRYD4 protein is localized in the nucleus when overexpressed in COS-7 green monkey cell. It has remained uncharacterized thus far.


Pssm-ID: 293960  Cd Length: 169  Bit Score: 102.91  E-value: 2.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 461 FRLDPKSAHRKLK-------VSHDNLTVErdesSSKKSHAPERFagQGSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGLA 533
Cdd:cd12903     1 FKLDERTAHSSLDlfkkdtgVIYRMLGVD----PTKVPQNPERF--RDWAVVLGDTPVTSGRHYWEVTVKRSQEFRIGVA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 534 YRSAPKHEWIGKNAASWALCRCHNHWAVRHDGKETPIAPAPHLRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQPVC 613
Cdd:cd12903    75 DVDMSRDECIGTNESSWVFAYAQRKWYAMVANETVPVPLVGKPDRVGLLLDYEAGKLSLVDVEKNSVVHTMSAEFRGPVV 154


                  ....*..
gi 1039796541 614 PTFTVWN 620
Cdd:cd12903   155 PAFALWD 161
SPRY_PRY_TRIM35 cd12893
PRY/SPRY domain in tripartite motif-containing protein 35 (TRIM35); This PRY/SPRY domain is ...
 460-626 2.93e-25

PRY/SPRY domain in tripartite motif-containing protein 35 (TRIM35); This PRY/SPRY domain is found at the C-terminus of the overall domain architecture of tripartite motif 35, TRIM35 (also known as hemopoietic lineage switch protein), which includes a RING finger domain (RING) and a B-box motif (BBOX). TRIM35 may play a role as a tumor suppressor and is implicated in the cell death mechanism.


Pssm-ID: 293950 [Multi-domain]  Cd Length: 171  Bit Score: 102.71  E-value: 2.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 460 PFRLDPKSAHRKLKVShDNLTVERDesSSKKSHA---PERFagQGSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRS 536
Cdd:cd12893     1 PVTLDPNTAHPWLSLS-EDLTSVRY--SSEKQQLpdnPERF--DPYPCVLGSEGFTSGKHSWDVEVGDNTSWMLGVAKES 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 537 APKHEWIGKNAAS--WALCRCHNHWAVRHDGKE-TPIAPAPHLRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQPVC 613
Cdd:cd12893    76 VQRKGKFTLSPESgfWTIGFSEGKYSARTSPEPrTPLRVKQKPQRIRVQLDWDRGKVSFSDPDTNTHIHTFTHTFTERVF 155

                         170
                  ....*....|....*
gi 1039796541 614 PTFTVWNKC--LTIV 626
Cdd:cd12893   156 PYFYTGCKSepLRIL 170
SPRY_PRY_TRIM76_like cd12899
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76)-like; This domain is ...
 461-629 6.43e-24

PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76)-like; This domain is similar to the distinct PRY/SPRY subdomain found at the C-terminus of TRIM76, a Class I TRIM protein. TRIM76 (also known as cardiomyopathy-associated protein 5 or CMYA5 or myospryn or SPRYD2) is a muscle-specific member of the TRIM superfamily, but lacks the RING domain. It has been suggested that TRIM76 is involved in two distinct processes, protein kinase A signaling and vesicular trafficking.


Pssm-ID: 293956 [Multi-domain]  Cd Length: 176  Bit Score: 99.09  E-value: 6.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 461 FRLDPKSAHRKLKVSHDNLTVERDESSSKKSHAPE---RFAGqgSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSA 537
Cdd:cd12899     2 FHLNEDTAHPLLSISEDGFTVVYGEEELPARDLSFsdnSFTR--CVAVMGSLIPVRGKHYWEVEVDEQTEYRVGVAFEDT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 538 PKHEWIGKNAASWalCRCHNHWAVR------HDGKETPIAPAPHLRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQP 611
Cdd:cd12899    80 QRNGYLGANNTSW--CMRHIITPSRhkyeflHNGWTPDIRITVPPKKIGILLDYDSGRLSFFNVDLAQHLYTFSCQFQHF 157

                         170
                  ....*....|....*....
gi 1039796541 612 VCPTFTVWNK-CLTIVTGL 629
Cdd:cd12899   158 VHPCFSLEKPgALKVHNGI 176
SPRY_PRY_TRIM41 cd13741
PRY/SPRY domain in tripartite motif-binding protein 41 (TRIM41); This domain, consisting of ...
 463-621 2.42e-23

PRY/SPRY domain in tripartite motif-binding protein 41 (TRIM41); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of tripartite motif-containing protein 41 (TRIM41). TRIM41 (also known as RING finger-interacting protein with C kinase or RINCK) is localized to speckles in the cytoplasm and nucleus, and functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C.


Pssm-ID: 240499 [Multi-domain]  Cd Length: 199  Bit Score: 98.30  E-value: 2.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAGqgSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPKHEW 542
Cdd:cd13741     4 LDPDTAHPALLLSPDRRGVRLAERRQEVPEHPKRFSA--DCCVLGAQGFRSGRHYWEVEVGGRRGWAVGAARESTHHKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 543 IGKNAASW----ALCRCHNH-----------------WAVRHDGK---------ETPIAPAPHLRRVGVLLDYDNGSIAF 592
Cdd:cd13741    82 VGSGGSSVssgdASSSRHHHrrrrlhlpqqpllqrevWCVGTNGKryqaqssteQTLLSPSEKPRRFGVYLDYEAGRLGF 161

                         170       180       190
                  ....*....|....*....|....*....|
gi 1039796541 593 YDALSSVHLHTFHAA-LAQPVCPTFTVWNK 621
Cdd:cd13741   162 YNAETLAHVHTFSAAfLGERVFPFFRVLSK 191
SPRY_PRY_TRIM65 cd12896
PRY/SPRY domain in tripartite motif-containing domain 65 (TRIM65); This domain, consisting of ...
 452-616 2.87e-23

PRY/SPRY domain in tripartite motif-containing domain 65 (TRIM65); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM65 proteins (composed of RING/B-box/coiled-coil core and also known as RBCC proteins). The SPRY/PRY combination is a possible component of immune defense. This protein family has not been characterized.


Pssm-ID: 293953 [Multi-domain]  Cd Length: 182  Bit Score: 97.52  E-value: 2.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 452 GKLKTNSQPFRLDPKSAHRKLKVSHDNLTVERdesssKKSHAPERFAGQGSY---GVAGNVFIDSGRHYWEVVTSgSTWY 528
Cdd:cd12896     3 AELWKDYRNLTFDPRTANKYLELSRQNRRAKH-----GRSAARGVPASPGSFelwQVQCTQSFQHGHHYWEVEVS-SHSV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 529 AIGLAYRSAPKHEW------IGKNAASWALC---RCHNHWavrHDGKETPIaPAPHLRRVGVLLDYDNGSIAFY-DALSS 598
Cdd:cd12896    77 TLGVTYPGLPRHKQgghkdnIGRNPCSWGLQiqeDSLQAW---HNGRAQKL-QGVSYRLLGVDLDLEAGTLTFYgLEPGT 152

                         170
                  ....*....|....*...
gi 1039796541 599 VHLHTFHAALAQPVCPTF 616
Cdd:cd12896   153 QRLHTFHAIFTQPLYPVF 170
SPRY_PRY_A33L cd12905
zinc-binding protein A33-like; This domain, consisting of the distinct N-terminal PRY ...
 460-617 1.07e-22

zinc-binding protein A33-like; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM69 and TRIM proteins NF7 and bloodthirsty (bty). TRIM69 is a novel testis E3 ubiquitin ligase that may function to ubiquitinate its particular substrates during spermatogenesis. In humans, TRIM69 localizes in the cytoplasm and nucleus, and requires an intact RING finger domain to function. TRIM protein NF7, which also contains a chromodomain (CHD) at the N-terminus and an RFP (Ret finger protein)-like domain at the C-terminus, is required for its association with transcriptional units of RNA polymerase II which is mediated by a trimeric B box. In Xenopus oocyte, xNF7 has been identified as a nuclear microtubule-associated protein (MAP) whose microtubule-bundling activity, but not E3-ligase activity, contributes to microtubule organization and spindle integrity. Bloodthirsty (bty) is a novel gene identified in zebrafish and has been shown to likely play a role in in regulation of the terminal steps of erythropoiesis.


Pssm-ID: 293962 [Multi-domain]  Cd Length: 178  Bit Score: 95.56  E-value: 1.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 460 PFRLDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFagQGSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGLAyrsapk 539
Cdd:cd12905     5 PLTFDPETAHPSLILSRDLTAVTESDEMQPYPRSPKRF--LQCVNVLASQGFQSGRHYWEVWVGSKTKWDLGVA------ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 540 HEWIGKnAASWALCRCHNHWAVR-HDGKE--------TPIAPAPHLRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQ 610
Cdd:cd12905    77 SESVDR-QARVKLCPENGYWTLRlRNGDEywagtqpwTRLRVTSRPQRIGVFLDCEERKVSFYNADDMSLLYSFHQGPRG 155


                  ....*..
gi 1039796541 611 PVCPTFT 617
Cdd:cd12905   156 KVFPFFS 162
Bbox1_MID cd19801
B-box-type 1 zinc finger found in the midline (MID) family; The MID family includes MID1 and ...
 116-164 2.14e-22

B-box-type 1 zinc finger found in the midline (MID) family; The MID family includes MID1 and MID2. MID1, also known as midin, midline 1 RING finger protein, putative transcription factor XPRF, RING finger protein 59 (RNF59), or tripartite motif-containing protein 18 (TRIM18), is a microtubule-associated E3 ubiquitin-protein ligase implicated in epithelial-mesenchymal differentiation, cell migration and adhesion, and programmed cell death along specific regions of the ventral midline during embryogenesis. MID2, also known as midin-2, midline defect 2, RING finger protein 60 (RNF60), or tripartite motif-containing protein 1 (TRIM1), is highly related to MID1. It associates with the microtubule network and may at least partially compensate for the loss of MID1. Both MID1 and MID2 interacts with alpha4, a regulatory subunit of PP2-type phosphatases, such as PP2A, and an integral component of the rapamycin-sensitive signaling pathway. They also play a central role in the regulation of granule exocytosis, and functional redundancy exists between MID1 and MID2 in cytotoxic lymphocytes (CTL). Both MID1 and MID2 belong to the C-I subclass of 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 RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


Pssm-ID: 380859  Cd Length: 49  Bit Score: 90.52  E-value: 2.14e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1039796541 116 KVLCQFCDQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEP 164
Cdd:cd19801     1 LVPCDVCEKEPPRKAVKTCLTCEVSYCKRCLEATHPNRGPFATHRLVEP 49
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 515-630 2.97e-21

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: 89.71  E-value: 2.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 515 RHYWEVV--TSGSTWYAIGLAYRSAP--KHEWIGKNAASWALCRC--HNHWAVRHDGKETPIAPAPhlRRVGVLLDYDNG 588
Cdd:pfam00622   1 RHYFEVEifGQDGGGWRVGWATKSVPrkGERFLGDESGSWGYDGWtgKKYWASTSPLTGLPLFEPG--DVIGCFLDYEAG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1039796541 589 SIAFYDALSSvHLHTFH-AALAQPVCPTFTV-WNKCLTIVTGLP 630
Cdd:pfam00622  79 TISFTKNGKS-LGYAFRdVPFAGPLFPAVSLgAGEGLKFNFGLR 121
SPRY_PRY_BTN1_2 cd15819
butyrophilin subfamily member A1 and A2 (BTN1A and BTN2A); This domain, consisting of the ...
 463-626 3.31e-21

butyrophilin subfamily member A1 and A2 (BTN1A and BTN2A); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of butyrophilin family 1A and 2A (BTN1A and BTN2A). BTNs belong to receptor glycoproteins of immunoglobulin (Ig) superfamily, characterized by the presence of extracellular Ig-like domains (IgV and/or IgC). BTN1A plays a role in the secretion, formation and stabilization of milk fat globules. The B30.2 domain of BTN1A1 binds the enzyme xanthine oxidoreductase (XOR) in order to participate in milk fat globule secretion; this interaction may lead to the production of reactive oxygen species, which have immunomodulatory and antimicrobial functions. Duplication events have led to three paralogs of BTN2A in primates: BTN2A1, BTN2A2, and BTN2A3. In humans, only BTN2A1 has been functionally characterized; it has been detected on epithelial cells and leukocytes, and identified as a novel ligand of dendritic cell-specific ICAM-3 grabbing nonintegrin (DCSIGN), a C-type lectin receptor that acts as an internalization receptor for HIV-1, HCV, and other pathogens. BTN2A2 mRNA has been shown to be expressed in circulating human immune cells.


Pssm-ID: 293991 [Multi-domain]  Cd Length: 172  Bit Score: 91.13  E-value: 3.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAGQGSygVAGNVFIDSGRHYWEVvtsgstwyAIGlayrsapkhew 542
Cdd:cd15819     6 LDPDTAHPALILSEDGRSVTWGETRQDLPENPERFDSLPC--VLGQEGFTSGRHYWEV--------EVG----------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 543 igkNAASWALCRCHNH---------------WAVRHDGKE--------TPIAPAPHLRRVGVLLDYDNGSIAFYDALSSV 599
Cdd:cd15819    65 ---DRTSWDLGVCRDNvmrkgrvtlspengfWAIRLYGNEywaltspeTPLTLKEPPRRVGIFLDYEAGDVSFYNMTDGS 141

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1039796541 600 HLHTF-HAALAQPVCPTFTVWN---KCLTIV 626
Cdd:cd15819   142 HIYTFpQTAFSGPLRPFFRLWSsdsGPLTIC 172
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
 182-306 1.26e-20

B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains


Pssm-ID: 128778  Cd Length: 127  Bit Score: 88.09  E-value: 1.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541  182 KQNLESNLTNLIKRNTELETLLAKLIQTCQHVEVNASRQEAKLTEECDLLIEIIQQRRQIIGTKIKEGKVIRLRKLAQQI 261
Cdd:smart00502   2 REALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQL 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1039796541  262 ANCKQCLERSASLISQAEHSLKENDHARFLQTAKNITERVSMATA 306
Cdd:smart00502  82 ESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLLK 126
SPRY_BSPRY cd12904
SPRY domain in Ro-Ret family; This domain, named BSPRY, has been identified in the Ro-Ret ...
 462-626 4.12e-20

SPRY domain in Ro-Ret family; This domain, named BSPRY, has been identified in the Ro-Ret family, since the protein is composed of a B-box, an alpha-helical coiled coil and a SPRY domain. The gene for BSPRY resides on human chromosome 9 and is specifically expressed in testis. The function of BSPRY is not known, but several related proteins of the RING-Box-coiled-coil (RBCC) family have been implicated in cell transformation.


Pssm-ID: 293961 [Multi-domain]  Cd Length: 171  Bit Score: 87.86  E-value: 4.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 462 RLDPKSAHRKLKVSHDNLTVERDESSSKKSHA--PERFAGQGSyGVAGNVFiDSGRHYWEVVTSGSTWYAIGLAYRSAPK 539
Cdd:cd12904     2 RFDERTVSPLLSLSEDRRTLTFSPKKARQSPPddPERFDHWPN-ALASLSF-SSGTHAWVVDVGKSCAYKVGVCYGSLER 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 540 -----HEWIGKNAASWALCRCHNHWAVRHDGKETPIAPAPHLRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQPVCP 614
Cdd:cd12904    80 kgsgnEARLGYNAFSWVFSRYDGEFSFSHNGQHVPLELLKCPARVGVLLDWPSQELLFYDPDSCTVLHSHREAFAAPLLP 159

                         170
                  ....*....|..
gi 1039796541 615 TFTVWNKCLTIV 626
Cdd:cd12904   160 VFAVADQSISIV 171
SPRY_PRY_TRIM15 cd15826
PRY/SPRY domain in tripartite motif-binding protein 15 (TRIM15); This domain, consisting of ...
 463-625 1.76e-19

PRY/SPRY domain in tripartite motif-binding protein 15 (TRIM15); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of tripartite motif-containing protein 15 (TRIM15), also referred to as RING finger protein 93 (RNF93) or Zinc finger protein B7 or 178 (ZNFB7 or ZNF178). TRIM15 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. The PRY and SPRY/B30.2 domains can function as immune defense components and in pathogen sensing. TRIM15 has been shown to regulate inflammatory and innate immune signaling, in addition to displaying antiviral activities. Down-regulation of TRIM15, as well as TRIM11, enhances virus release, suggesting that these proteins contribute to the endogenous restriction of retroviruses in cells. TRIM15 is also a regulatory component of focal adhesion turnover and cell migration.


Pssm-ID: 293998 [Multi-domain]  Cd Length: 170  Bit Score: 86.07  E-value: 1.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAGQGsyGVAGNVFIDSGRHYW--EVVTSGSTWYAIGLAYRSAPKH 540
Cdd:cd15826     4 LDPQTASGSLVLSEDRKSVRYTRQKQNLPDSPLRFDGLP--AVLGSPGFSSGRHRWqvEVQLGDGGGCTVGVAGESVRRK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 541 EWIGKNAAS--WALCRCHNH-WAVRHDGKETPIAPAPhlRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQPVCPTFT 617
Cdd:cd15826    82 GEMGLSAEDgvWAVILSHQQcWASTSPGTDLPLSEIP--RRVGVALDYEAGTVTLTNAETQEPIFTFTASFSGKVFPFFA 159

                         170
                  ....*....|
gi 1039796541 618 VWNK--CLTI 625
Cdd:cd15826   160 VWKKgsRLTL 169
SPRY_PRY_BTN3 cd15820
PRY/SPRY domain of butyrophilin 3 (BTN3), includes BTN3A1, BTN3A2, BTN3A3 as well as BTN-like ...
 463-630 3.31e-19

PRY/SPRY domain of butyrophilin 3 (BTN3), includes BTN3A1, BTN3A2, BTN3A3 as well as BTN-like 3 (BTNL3); BTN3A also known as CD277; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of butyrophilin family 3A (BTN3A); duplication events have led to three paralogs in primates: BTN3A1, BTN3A2, and BTN3A3. BTNs belong to receptor glycoproteins of immunoglobulin (Ig) superfamily, characterized by the presence of extracellular Ig-like domains (IgV and/or IgC). BTN3 transcripts are ubiquitously present in all immune cells (T cells, B cells, NK cells, monocytes, dendritic cells, and hematopoietic precursors) with different expression levels; BTN3A1 and BTN3A2 are expressed mainly by CD4+ and CD8+ T cells, BTN3A2 is the major form expressed in NK cells, and BTN3A3 is poorly expressed in these immune cells. The PRY/SPRY domain of the BTN3A1 isoform mediates phosphoantigen (pAg)-induced activation by binding directly to the pAg.


Pssm-ID: 293992 [Multi-domain]  Cd Length: 176  Bit Score: 85.56  E-value: 3.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFagQGSYGVAGNVFIDSGRHYWEV-VTSGSTWYaIGLAYRSAPKHE 541
Cdd:cd15820     8 LDPDTANPILLISEDQRSLQWADEPQNLPDNPKRF--DWHYCVLGCKSFTSGRHFWEVeVGDRKEWY-VGVCRENVERKL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 542 WIGKNAAS--WALCRCH-NHWAVRHDGKETPIAPAPhLRRVGVLLDYDNGSIAFYDALSSVHLHTF-HAALAQPVCPTFT 617
Cdd:cd15820    85 WVKMAPENgfWTIGLSDgNDYQALTDPRTKLTIANP-PQRVGVFLDYETGEVSFYNAMDGSHIYTFpHTSFSGPLYPVFR 163

                         170
                  ....*....|...
gi 1039796541 618 VWNKCLTIVTGLP 630
Cdd:cd15820   164 LLSWDPTALTICP 176
SPRY_PRY_RFPL cd15821
Ret finger protein-like (RFPL), includes RFP1, 2, 3, 4; This domain, consisting of the ...
 463-616 3.99e-19

Ret finger protein-like (RFPL), includes RFP1, 2, 3, 4; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of RFPL protein family, which includes RFPL1, RFPL2, RFPL3 and RFPL4. In humans, RFPL transcripts can be detected at the onset of neurogenesis in differentiating human embryonic stem cells, and in the developing human neocortex. The human RFPL1, 2, 3 genes have a role in neocortex development. RFPL1 is a primate-specific target gene of Pax6, a key transcription factor for pancreas, eye and neocortex development; human RFPL1 decreases cell number through its RFPL-defining motif (RDM) and SPRY domains. The RFPL4 (also known as RFPL4A) gene encodes a putative E3 ubiquitin-protein ligase expressed in adult germ cells and interacts with oocyte proteins of the ubiquitin-proteasome degradation pathway.


Pssm-ID: 293993 [Multi-domain]  Cd Length: 178  Bit Score: 85.44  E-value: 3.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFagQGSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPKHEW 542
Cdd:cd15821     8 LDVDTANNYLIISEDLRSVRCGCFRQNRKELAERF--DDALCVLGSPRFTSGRHYWEVDVGTSTEWDLGVCRESVNRQGP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 543 IgknaaswALCRCHNHWAVRHDGKE---------TPIAPAPHLRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQ-PV 612
Cdd:cd15821    86 I-------ELSPEHGFWTVSLRDGSvffastvplTVLWVNPRLHRVGIFLDMEMGTISFYDVSDGSHIFTFTKISAEePL 158


                  ....
gi 1039796541 613 CPTF 616
Cdd:cd15821   159 RPFF 162
SPRY_PRY_TRIM75 cd15829
PRY/SPRY domain of tripartite motif-binding protein 75 (TRIM75); This domain, consisting of ...
 459-618 2.01e-18

PRY/SPRY domain of tripartite motif-binding protein 75 (TRIM75); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM75, also known as Gm794. TRIM75 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. TRIM75 has a single site of positive selection in its RING domain associated with E3 ubiquitin ligase activity. It has not been detectably expressed experimentally due to their constant turnover by the proteasome, and therefore not been characterized.


Pssm-ID: 294001  Cd Length: 187  Bit Score: 83.49  E-value: 2.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 459 QPFR----LDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAGqgSYGVAGNVFIDSGRHYWEV-VTSGSTWyAIGLA 533
Cdd:cd15829    15 KKFRvdvtLDPETAHPNLLVSEDKKCVTFTKKKQRVPDSPKRFTV--NPVVLGFPGFHSGRHFWEVeVGDKPEW-AVGVC 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 534 YRSAPKhewiGKNAASWALCRChnhWAV--RHDGKETP-IAPAPHL-----RRVGVLLDYDNGSIAFYDALSSVHLHTFH 605
Cdd:cd15829    92 KDSLST----KARRPPSGQQGC---WRIqlQGGDYDAPgAVPPPLLlevkpRGIGVFLDYELGEISFYNMPEKSHIHTFT 164

                         170
                  ....*....|...
gi 1039796541 606 AALAQPVCPTFTV 618
Cdd:cd15829   165 DTFSGPLRPYFYV 177
SPRY_PRY_TRIM76 cd12898
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76), also called ...
 461-616 7.69e-18

PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76), also called cardiomyopathy-associated protein 5; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM76, a Class I TRIM protein. TRIM76 (also known as cardiomyopathy-associated protein 5 or CMYA5 or myospryn or SPRYD2) is a muscle-specific member of the TRIM superfamily, but lacks the RING domain. It has been suggested that TRIM76 is involved in two distinct processes, protein kinase A signaling and vesicular trafficking. It has also been implicated in Duchenne muscular dystrophy and cardiac disease; gene polymorphism of TRIM76 is associated with left ventricular wall thickness in patients with hypertension while its interactions with M-band titin and calpain 3 link it to tibial and limb-girdle muscular dystrophies.


Pssm-ID: 293955  Cd Length: 171  Bit Score: 81.51  E-value: 7.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 461 FRLDPKSAHRKLKVSHDNLTV----ERDESSSKKSHAPErfagqgsygVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRS 536
Cdd:cd12898     4 FLLLRETAHPALHISSDRGTViyfhERRRKMSSLTECPS---------VLGEELPSCGQYYWETTVTRCPAYRLGICSSS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 537 APKHEWIGKNAASWAL--------CRCHnhwaVRHDGKETPIAPAPHLRRVGVLLDYDNGSIAFYDALSSVHLHTFHAAL 608
Cdd:cd12898    75 ASQAGALGEGSTSWCLhcvptsepCRYT----LLHSGIVSDVFVTERPARVGTLLDYNNGRLIFINAESGQLLGIFRHRF 150


                  ....*...
gi 1039796541 609 AQPVCPTF 616
Cdd:cd12898   151 AQPCHPAF 158
SPRY_PRY_TRIM58 cd15816
PRY/SPRY domain in tripartite motif-binding protein 58 (TRIM58), also known as BIA2; This ...
 462-618 3.60e-17

PRY/SPRY domain in tripartite motif-binding protein 58 (TRIM58), also known as BIA2; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM58, also known as BIA2. TRIM58 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins.It is implicated by genome-wide association studies (GWAS) to regulate erythrocyte traits, including cell size and number. Trim58 facilitates erythroblast enucleation by inducing proteolytic degradation of the microtubule motor dynein.


Pssm-ID: 293988 [Multi-domain]  Cd Length: 168  Bit Score: 79.45  E-value: 3.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 462 RLDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAGQGSygVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPKHe 541
Cdd:cd15816     3 KLDPATAHPSLLLTADLRSVQDGELWRDVPGNPERFDTWPC--VLGLQSFSSGRHYWEVAVGEKAEWGLGVCQDSAPRK- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 542 wiGKNAAS-----WALcrchnhWAVRHDGK---ETPIAPAPHL---RRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQ 610
Cdd:cd15816    80 --GETTPSpengvWAV------WLLKGNEYmvlASPSVPLLQLrrpRRVGVFLDYEAGEISFYNVTAGSHIYTFRQLFSG 151


                  ....*...
gi 1039796541 611 PVCPTFTV 618
Cdd:cd15816   152 ILRPYFFV 159
SPRY_PRY_TRIM39 cd13745
PRY/SPRY domain in tripartite motif-binding protein 39 (TRIM39) and TRIM39-like; This domain, ...
 463-616 5.44e-17

PRY/SPRY domain in tripartite motif-binding protein 39 (TRIM39) and TRIM39-like; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of pyrin, several tripartite motif-containing proteins (TRIMs), including E3 ubiquitin-protein ligase (TRIM21), RET finger protein (RFP)/tripartite motif protein 27 (TRIM27), as well as butyrophilin (Btns) and butyrophilin-like (Btnl) family members, with the exception of Btnl2. Btn and Btnl family members are novel regulators of immune responses, with many of the genes located within the MHC. They are implicated in T-cell inhibition and modulation of epithelial cell-T cell interactions. TRIM21 (also known as RO52, SSA1 or RNF81) is a major autoantigen in autoimmune diseases such as rheumatoid arthritis, systemic lupus erythematosus, and Sjorgen's syndrome. TRIM27 (also known as Ret finger protein, RFP or RNF76) negatively regulates CD4 T-cells by ubiquitinating and inhibiting the class II phosphatidylinositol 3 kinase C2beta (PI3K-C2beta), a kinase critical for KCa3.1 channel activation. The PRY/SPRY domain of Pyrin, which is mutated in familial Mediterranean fever patients, interacts with inflammasome components and inhibits proIL-1beta processing.


Pssm-ID: 293979 [Multi-domain]  Cd Length: 177  Bit Score: 79.21  E-value: 5.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAgqgSYG-VAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPKHE 541
Cdd:cd13745     7 LDPDTAHPNLVLSEDRKSVRHGDTRQDLPDNPERFD---TYPcVLGAEGFTGGRHYWEVEVGDKTEWTLGVCRESVSRKG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 542 WIgknaaswALCRCHNHWAVRHDGKE--------TPIAPAPHLRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQPVC 613
Cdd:cd13745    84 EV-------TLSPENGYWTVWLRDGKyealtsppTPLPVSVRPSRVGIFLDYEAGEVSFYNVTDRSHLFTFTDTFSGTLR 156


                  ...
gi 1039796541 614 PTF 616
Cdd:cd13745   157 PYF 159
SPRY_PRY_TRIM60_75 cd15817
PRY/SPRY domain of tripartite motif-binding protein 60 and 75 (TRIM60 and TRIM75); This domain, ...
 463-618 7.66e-17

PRY/SPRY domain of tripartite motif-binding protein 60 and 75 (TRIM60 and TRIM75); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM60 and TRIM75, both composed of RING/B-box/coiled-coil core and also known as RBCC proteins. TRIM60 domain is also known as RING finger protein 33 (RNF33) or 129 (RNF129). Based on its expression profile, RNF33 likely plays an important role in the spermatogenesis process, the development of the pre-implantation embryo, and in testicular functions; Rnf33 is temporally transcribed in the unfertilized egg and the pre-implantation embryo, and is permanently silenced before the blastocyst stage. Mice experiments have shown that RNF33 associates with the cytoplasmic motor proteins, kinesin-2 family members 3A (KIF3A) and 3B (KIF3B), suggesting possible contribution to cargo movement along the microtubule in the expressed sites. TRIM75, also known as Gm794, has a single site of positive selection in its RING domain associated with E3 ubiquitin ligase activity. It has not been detectably expressed experimentally due to their constant turnover by the proteasome, and therefore not been characterized.


Pssm-ID: 293989 [Multi-domain]  Cd Length: 168  Bit Score: 78.36  E-value: 7.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAGQGSygVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPKHEW 542
Cdd:cd15817     4 LDPETAHPNLIVSEDRKAVRYRRMKPNCPYDPRRFTVYPA--VLGSEGFDSGRHFWEVEVGGKGEWILGVCKDSLPRNAQ 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796541 543 I--GKNAASWALCRCHNHWAVrHDGKETPIAPAPHLRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQPVCPTFTV 618
Cdd:cd15817    82 DppSPLGGCWQIGRYMSGYVA-SGPKTTQLLPVVKPSRIGIFLDYELGEVSFYNMNDRSHLYTFTDTFTGKLIPYFYV 158
SPRY_PRY_TRIM62 cd13744
PRY/SPRY domain in tripartite motif-binding protein 62 (TRIM62); This domain, consisting of ...
 463-617 8.49e-17

PRY/SPRY domain in tripartite motif-binding protein 62 (TRIM62); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM62. It is also called DEAR1 ductal epithelium (associated RING chromosome 1) and is involved in the morphogenesis of the mammary gland; loss of TRIM62 gene expression in breast is associated with increased risk of recurrence in early-onset breast cancer and thus, making TRIM62 a predictive biomarker. Non-small cell lung cancer lesions show a step-wise loss of TRIM62 levels during disease progression, indicating that it may play a role in the evolution of lung cancer. Decreased levels of TRIM62 also represent an independent adverse prognostic factor in AML.


Pssm-ID: 293978  Cd Length: 188  Bit Score: 78.89  E-value: 8.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVERDESSSKK-SHAPERFAGQGSygVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPKHE 541
Cdd:cd13744    16 LDPVTAHQRLILSDDCTIVAYGNLHPQPlQDSPKRFDVEVS--VLGSEGFSGGVHYWEVVVSEKTQWMIGLAHEAVSRKG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 542 WIGKNAASWALCrchnhwAVRHDGKETPIAPAP--------HLRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQPVC 613
Cdd:cd13744    94 SIQIQPGRGFYC------IVMHDGNQYSACTEPwtrlnvksKLEKVGVYLDYDKGLLIFYNADDMSWLYTFREKFPGKLC 167


                  ....
gi 1039796541 614 PTFT 617
Cdd:cd13744   168 SYFS 171
SPRY_PRY_TRIM60 cd15828
PRY/SPRY domain of tripartite motif-binding protein 60 (TRIM60) also known as RING finger ...
 463-616 1.42e-16

PRY/SPRY domain of tripartite motif-binding protein 60 (TRIM60) also known as RING finger protein 33 (RNF33); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM60, which is also known as RING finger protein 33 (RNF33) or 129 (RNF129). TRIM60 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. Based on its expression profile, RNF33 likely plays an important role in the spermatogenesis process, the development of the pre-implantation embryo, and in testicular functions; Rnf33 is temporally transcribed in the unfertilized egg and the pre-implantation embryo, and is permanently silenced before the blastocyst stage. Mice experiments have shown that RNF33 associates with the cytoplasmic motor proteins, kinesin-2 family members 3A (KIF3A) and 3B (KIF3B), suggesting possible contribution to cargo movement along the microtubule in the expressed sites.


Pssm-ID: 294000 [Multi-domain]  Cd Length: 180  Bit Score: 78.10  E-value: 1.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERF----AGQGSYGvagnvfIDSGRHYWEV-VTSGSTWyAIGLAYRSA 537
Cdd:cd15828    14 LDPETAHPQLTVSEDRKSVLYGEMKQNVCYNPRRFylcpAVLGSEG------FHSGRQYWEVeVGDKPEW-TLGVCQDCL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 538 PKhEWigKNAAS-----WALCRCHNHWAVRHDGKETPIAPAPHLRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQPV 612
Cdd:cd15828    87 PR-NW--SNQPSvqdglWAIGRYSESNYVALGPKKIQLLPKVRPSKIGIFLDYELGEVSFYNMNDRSLLYTFSDSFTGTL 163


                  ....
gi 1039796541 613 CPTF 616
Cdd:cd15828   164 WPYF 167
SPRY_PRY_RNF135 cd12902
PRY/SPRY domain in RING finger protein RNF135; This domain, consisting of the distinct ...
 464-625 1.52e-16

PRY/SPRY domain in RING finger protein RNF135; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of the RING finger protein RNF135 (also known as Riplet/RNF135), which ubiquitinates RIG-I (retinoic acid-inducible gene-I) to promote interferon-beta induction during the early phase of viral infection. Normally, RIG-I is activated by TRIM25 in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. However, RNF135, consisting of an N-terminal RING finger domain, C-terminal SPRY and PRY motifs and showing sequence similarity to TRIM25, acts as an alternative factor that promotes RIG-I activation independent of TRIM25.


Pssm-ID: 293959 [Multi-domain]  Cd Length: 168  Bit Score: 77.56  E-value: 1.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 464 DPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAgqgsygvAGNVF----IDSGRHYWEVVTSGSTWYAIGLAYRSAPK 539
Cdd:cd12902     4 DLRSLSCSLEVSEDSRKVTVSHGPQAYAWSPDRFS-------ISQVLcsqaFSSGQHYWEVDTRQCSHWAVGVASWEMSR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 540 HEWIGKNAASWALcrchnHWAVR------HDGKETPI-APAPhlRRVGVLLDYDNGSIAFYDALSSVHL-HTFHAALAQP 611
Cdd:cd12902    77 DQMLGRTMDSWCI-----EWKGTgqlsawHMNKETVLgSDKP--RVVGIWLDLEEGKLAFYSVANQERLlHECEVSASSP 149

                         170
                  ....*....|....*...
gi 1039796541 612 VCPTFTV----WNKCLTI 625
Cdd:cd12902   150 LHPAFWLyglePGNSLII 167
SPRY_PRY_TRIM69 cd15818
PRY/SPRY domain in tripartite motif-binding protein 69 (TRIM69), also known as RING finger ...
 460-616 1.74e-16

PRY/SPRY domain in tripartite motif-binding protein 69 (TRIM69), also known as RING finger protein 36 (RNF36); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM69, which is also known as RING finger protein 36 (RNF36) or testis-specific ring finger (Trif). TRIM69 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It is a novel testis E3 ubiquitin ligase that may function to ubiquitinate its particular substrates during spermatogenesis. In humans, TRIM69 localizes in the cytoplasm and nucleus, and requires an intact RING finger domain to function. The mouse ortholog of this gene is specifically expressed in germ cells at the round spermatid stages during spermatogenesis and, when overexpressed, induces apoptosis. TRIM69 has been shown to be a novel regulator of mitotic spindle assembly in tumor cells; it associates with spindle poles and promotes centrosomal clustering, and is therefore essential for formation of a bipolar spindle.


Pssm-ID: 293990 [Multi-domain]  Cd Length: 187  Bit Score: 77.92  E-value: 1.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 460 PFRLDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFagQGSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPK 539
Cdd:cd15818    14 LITLDPKTAHPNLILSEDLTCVWHGDTKQMLPDNPERF--DSSVAVLGSEGFTSGKHYWEVEVAKKTKWTLGVVRESINR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 540 HewigknaASWALCRCHNHWAVR----HDGKETPIAP-----APHLRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQ 610
Cdd:cd15818    92 K-------GNCPLSPEDGFWLLRlrnqNELKALDVPSfsltlTSNLNKVGIYLDYEGGQVSFYNANTMSHIYTFSDTFTE 164


                  ....*.
gi 1039796541 611 PVCPTF 616
Cdd:cd15818   165 KIYPYF 170
SPRY_PRY_TRIM16 cd12890
PRY/SPRY domain in tripartite motif-containing protein 16 (TRIM16); This domain, consisting of ...
 460-616 2.24e-16

PRY/SPRY domain in tripartite motif-containing protein 16 (TRIM16); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM16 and TRIM-like proteins. TRIM16 (also known as estrogen-responsive B box protein or EBBP) does not possess a RING domain like the other TRIM proteins, but contains two B-box domains and can heterodimerize with other TRIM proteins such as TRIM24, Promyelocytic leukemia (PML) protein and Midline-1 (MID1 or TRIM18). It is a regulator of keratinocyte differentiation and a tumor suppressor in retinoid-sensitive neuroblastoma. It has been shown that loss of TRIM16 expression plays an important role in the development of cutaneous squamous cell carcinoma (SCC) and is a determinant of retinoid sensitivity. TRIM16 also has E3 ubiquitin ligase activity.


Pssm-ID: 293948  Cd Length: 182  Bit Score: 77.51  E-value: 2.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 460 PFRLDPKSAHRKLKVSHDNLTVErdeSSSKKSHA----PERF-------AGQGSYgvagnvfidSGRHYWEVVTSGSTWY 528
Cdd:cd12890    10 PLTFDPDTAHRYLRLTEDNRKVT---NTTPWEHPypdhPERFehwrqvlSQQSLY---------LGRYYFEVEISGEGTY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 529 aIGLAYRS-----APKHEWIGKNAASWALcrchnHWAVR-----HDGKETPiAPAPHLRRVGVLLDYDNGSIAFY--DAL 596
Cdd:cd12890    78 -VGLTYKSidrkgSESNSCISGNNFSWCL-----QWNGKefsawHSDVETP-LKKGPFTRLGIYLDYPGGTLSFYgvEDD 150

                         170       180
                  ....*....|....*....|
gi 1039796541 597 SSVHLHTFHAALAQPVCPTF 616
Cdd:cd12890   151 GMTLLHKFQCKFTEPLYPAF 170
SPRY_PRY_TRIM7 cd13740
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7); This domain, consisting of the ...
 462-618 2.32e-16

PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of tripartite motif-containing protein 7 (TRIM7), also referred to as glycogenin-interacting protein (GNIP) or RING finger protein 90 (RNF90). TRIM7 or GNIP interacts with glycogenin and stimulates its self-glucosylating activity via its SPRY domain. The GNIP gene encodes at least four distinct isoforms of GNIP, of which three (GNIP1, GNIP2, and GNIP3) have the B30.2 domain.


Pssm-ID: 293975 [Multi-domain]  Cd Length: 169  Bit Score: 76.92  E-value: 2.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 462 RLDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAGQGSygVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPKHE 541
Cdd:cd13740     3 TLDPDSANPRLILSLDLKSVRLGERAQDLPNHPCRFDTNTR--VLASCGFSSGRHHWEVEVGSKDGWAFGVARESVRRKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 542 W--IGKNAASWAL-CRCHNHWAVRHDgKETPIAPApHLRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQPVCPTFTV 618
Cdd:cd13740    81 LtpFTPEEGVWALqLNGGQYWAVTSP-ERTPLSCG-HLSRVRVALDLEVGAVSFYAAEDMRHIYTFRVNFQERVFPLFSV 158
SPRY_PRY_TRIM25 cd13736
PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25); This domain, consisting of ...
 463-620 1.68e-15

PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM25 proteins (composed of RING/B-box/coiled-coil core and also known as RBCC proteins). TRIM25 (also called Efp) ubiquitinates the N terminus of the viral RNA receptor retinoic acid-inducible gene-I (RIG-I) in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. It has been shown that the influenza A virus targets TRIM25 and disables its antiviral function.


Pssm-ID: 293971 [Multi-domain]  Cd Length: 169  Bit Score: 74.53  E-value: 1.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAGQGSygVAGNVFIDSGRHYWEVVTSGSTWYAIGLAY----RSAP 538
Cdd:cd13736     3 FDYNTAHNKVSLSENYTKASVSDDPQNYREHPQRFTYCSQ--VLGLHCFKQGIHYWEVELQKNNFCGVGICYgsmdRQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 539 KHEwIGKNAASWALCRCHNHWAVRHDGKETPIaPAPHLRRVGVLLDYDNGSIAFYDALSSVHL-HTFHAALAQPVCPTFT 617
Cdd:cd13736    81 ESR-LGRNSESWCVEWFNVKISAWHNNVEKTL-PSTKATRVGVLLNCDHGFVIFFAVQDKVHLmYKFKVDFTEALYPAFW 158


                  ...
gi 1039796541 618 VWN 620
Cdd:cd13736   159 VFS 161
SPRY_PRY_TRIM50_72 cd12897
PRY/SPRY domain in tripartite motif-binding (TRIM) proteins TRIM50 and TRIM72; This domain, ...
 462-620 2.99e-15

PRY/SPRY domain in tripartite motif-binding (TRIM) proteins TRIM50 and TRIM72; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several TRIM proteins, including TRIM72 and TRIM50. TRIM72 (also known as MG53) has been shown to perform a critical function in membrane repair following acute muscle injury by nucleating the assembly of the repair machinery at injury sites. It is expressed specifically in skeletal muscle and heart, and tethered to the plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine. TRIM50, an E3 ubiquitin ligase, is deleted in Williams-Beuren (WBS) syndrome, a multi-system neurodevelopmental disorder caused by the deletion of contiguous genes at chromosome region 7q11.23.


Pssm-ID: 293954  Cd Length: 191  Bit Score: 74.57  E-value: 2.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 462 RLDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFagQGSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPKHe 541
Cdd:cd12897    15 TFDPATAHPLLVVSSGGTVVECGLQKQRRASQPERF--DKSTCVVASQGFSEGEHYWEVVVGDKPRWALGVIKGTASRK- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 542 wiGKNAAS-----WAL-CRCHNHWAVRHDGKETPIAPAP-HLRRVGVLLDYDNGSIAFYDALSS---VHLHTFHAALAQP 611
Cdd:cd12897    92 --GKLHASpshgvWLIgLKEGKVYEAHGEPKEPRPLRVAgRPHRIGVYLSFEDGVLSFFDASDPddlRTLYTFQERFQGK 169

                         170
                  ....*....|
gi 1039796541 612 VCPTFTV-WN 620
Cdd:cd12897   170 LYPFFDVcWH 179
SPRY_PRY_TRIM4 cd15809
PRY/SPRY domain in tripartite motif-binding protein 4 (TRIM4), also known as RING finger ...
 486-632 4.39e-15

PRY/SPRY domain in tripartite motif-binding protein 4 (TRIM4), also known as RING finger protein 87 (RNF87); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM4 which is also known as RING finger protein 87 (RNF87). TRIM4 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. It is a positive regulator of RIG-I-mediated interferon (IFN) induction. It regulates virus-induced IFN induction and cellular antiviral innate immunity by targeting RIG-I for K63-linked poly-ubiquitination. Over-expression of TRIM4 enhances virus-triggered activation of transcription factors IRF3 and NF-kappaB, as well as IFN-beta induction. Expression of TRIM4 differs significantly in Huntington's Disease (HD) neural cells when compared with wild-type controls, possibly impacting down-regulation of the Huntingtin (HTT) gene, which is involved in the regulation of diverse cellular activities that are impaired in Huntington's Disease (HD) cells.


Pssm-ID: 293981  Cd Length: 191  Bit Score: 74.10  E-value: 4.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 486 SSSKKSHAPERFagQGSYGVAG-NVFIdSGRHYWEVVTSGSTWYAIGLAYRSA---PKHEWIGKNAASWALCRCHNHWAV 561
Cdd:cd15809    49 NPQKTTQFVERF--QHLPCVLGkNVFT-SGKHYWEVENRDSLEIAVGVCREDVmgiTDGSEMSPHVGIWAICWSSAGYRP 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039796541 562 RHDGKETPIAPAPHLRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQPVCPTFtvWnkcLTIVTGLPIP 632
Cdd:cd15809   126 LTSSPVSPTKQEPALHRVGVFLDHGAGEVSFYSAVDGVHLHTFSCPLVSRLRPFF--W---LSPLASLVIP 191
SPRY_PRY_TRIM50 cd13743
PRY/SPRY domain in tripartite motif-binding protein 50 (TRIM50); This domain, consisting of ...
 462-619 1.88e-14

PRY/SPRY domain in tripartite motif-binding protein 50 (TRIM50); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM50. TRIM50, an E3 ubiquitin ligase, is deleted in Williams-Beuren (WBS) syndrome, a multi-system neurodevelopmental disorder caused by the deletion of contiguous genes at chromosome region 7q11.23. It is specifically expressed in gastric parietal cells and may play an essential role in tubulovesicular dynamics. It also interacts with and increases the level of p62, a multifunctional adaptor protein that is implicated in various cellular processes such as the autophagy clearance of polyubiquitinated protein aggregates.


Pssm-ID: 293977  Cd Length: 189  Bit Score: 72.14  E-value: 1.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 462 RLDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAGqgSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPKHE 541
Cdd:cd13743    15 KLDPLTAHPMLELSKGNTVVECGLLAQRLPSNPERFDY--SNCVLASRGFSSGKHYWEVVVGSKSKWRLGLIKGTTSRKG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 542 WIGKNAAswalcrcHNHWAV-RHDGK----------ETPIAPAPHlrRVGVLLDYDNGSIAFYDALSS---VHLHTFHAA 607
Cdd:cd13743    93 KLNKSPE-------NGVWLIgLKEGRvyeafanprvPLPLSTRPQ--RIGVFLDYEKGELTFYNADSPdelVPIYTFQAE 163

                         170
                  ....*....|...
gi 1039796541 608 LAQPVCPTFTV-W 619
Cdd:cd13743   164 FQGKLYPLLDVcW 176
SPRY_PRY_TRIM11 cd15811
PRY/SPRY domain of tripartite motif-binding protein 11 (TRIM11), also known as RING finger ...
 463-604 3.22e-14

PRY/SPRY domain of tripartite motif-binding protein 11 (TRIM11), also known as RING finger protein 92 (RNF92); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM11, also known as RING finger protein 92 (RNF92) or BIA1. TRIM11 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It localizes to the nucleus and the cytoplasm; it is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. TRIM11 increases expression of dopamine beta-hydroxylase gene by interacting with the homeodomain transcription factor, PHOX2B, via the B30.2/SPRY domain, thus playing a potential role in the specification of noradrenergic (NA) neuron phenotype. It has also been shown that TRIM11 plays a critical role in the clearance of mutant PHOX2B, which causes congenital central hypoventilation syndrome, via the proteasome. TRIM11 binds a key component of the activator-mediated cofactor complex (ARC105), and destabilizes it, through the ubiquitin-proteasome system; ARC105 mediates chromatin-directed transcription activation and is a key regulatory factor for transforming growth factor beta (TGFbeta) signaling.


Pssm-ID: 293983 [Multi-domain]  Cd Length: 169  Bit Score: 70.76  E-value: 3.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFagQGSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPKHEw 542
Cdd:cd15811     4 LDPDTANPELVLSEDRRSVRRGDLRQALPDSPERF--DPGPCVLGRERFTSGRHYWEVEVGDRTSWALGVCKENVNRKE- 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039796541 543 IGKNAAS---WALCRCHNHWAvRHDGKETPIAPAPhlRRVGVLLDYDNGSIAFYDALSSVHLHTF 604
Cdd:cd15811    81 KGELSAGngfWILVFLGNYYS-SERRTFAPLRDPP--RRVGIFLDYEAGHLSFYSATDGSLLFIF 142
SPRY_PRY_TRIM20 cd15813
PRY/SPRY domain in tripartite motif-binding protein 20 (TRIM20), also known as pyrin; This ...
 463-616 6.16e-14

PRY/SPRY domain in tripartite motif-binding protein 20 (TRIM20), also known as pyrin; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM20, which is also known as pyrin or marenostrin. Unlike TRIM domains that are composed of RING/B-box/coiled-coil core, the N-terminal RING domain in TRIM20 is exchanged by a PYRIN domain (PYD), a prime mediator of protein interactions necessary for apoptosis, inflammation and innate immune signaling pathway, and it also harbors a C-terminal B30.2 domain. Mutations in pyrin (TRIM20) are associated with familial Mediterranean fever (FMF), a recessively hereditary periodic fever syndrome, characterized by episodes of inflammation and fever. These mutations cluster in the C-terminal B30.2 domain and therefore it is assumed that pyrin plays a role in the innate immune system by possibly effecting caspase-1-dependent IL-1beta maturation.


Pssm-ID: 293985  Cd Length: 184  Bit Score: 70.56  E-value: 6.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFagQGSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPKHew 542
Cdd:cd15813    13 LDPETAHPNLIFSDDLKSVRLGNKWDRLPDNPERF--DSCIIVLGSPSFTSGRHYWEVEVGDKTGWILGVCKASVSRK-- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 543 iGKNAASWAlcrcHNHWAVRHDGK---ETPIAPAPHL------RRVGVLLDYDNGSIAFYDALSSVHLHTF-HAALAQPV 612
Cdd:cd15813    89 -GSMTLSPE----NGYWVVMMTKRneyQASTSPPTRLwlreppRRVGIFLDYEAGDISFYNVTAKSHIYTFtSFSSSGPL 163


                  ....
gi 1039796541 613 CPTF 616
Cdd:cd15813   164 QPIF 167
RING-HC_TRIM25_C-IV cd16597
RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar ...
 4-85 6.15e-12

RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar proteins; TRIM25, also known as estrogen-responsive finger protein (EFP), RING finger protein 147 (RNF147), or RING-type E3 ubiquitin transferase, is an E3 ubiquitin/ISG15 ligase that is induced by estrogen and is therefore particularly abundant in placenta and uterus. TRIM25 regulates various cellular processes through E3 ubiquitin ligase activity, transferring ubiquitin and ISG15 to target proteins. It mediates K63-linked polyubiquitination of retinoic acid inducible gene I (RIG-I) that is crucial for downstream antiviral interferon signaling. It is also required for melanoma differentiation-associated gene 5 (MDA5) and mitochondrial antiviral signaling (MAVS, also known as IPS-1, VISA, Cardiff) mediated activation of nuclear factor-kappaB (NF-kappaB) and interferon production. Upon UV irradiation, TRIM25 interacts with mono-ubiquitinated PCNA and promotes its ISG15 modification (ISGylation), suggesting a crucial role in termination of error-prone translesion DNA synthesis. TRIM25 also functions as a novel regulator of p53 and Mdm2. It enhances p53 and Mdm2 abundance by inhibiting their ubiquitination and degradation in 26S proteasomes. Meanwhile, it inhibits p53's transcriptional activity and dampens the response to DNA damage, and is essential for medaka development and this dependence is rescued by silencing of p53. Moreover, TRIM25 is involved in the host cellular innate immune response against retroviral infection. It interferes with the late stage of feline leukemia virus (FeLV) replication. Furthermore, TRIM25 acts as an oncogene in gastric cancer. Its blockade by RNA interference inhibits migration and invasion of gastric cancer cells through transforming growth factor-beta (TGF-beta) signaling, suggesting it presents a novel target for the detection and treatment of gastric cancer. In addition, TRIM25 acts as an RNA-specific activator for Lin28a/TuT4-mediated uridylation. TRIM25 belongs to the C-IV subclass of 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: 438259 [Multi-domain]  Cd Length: 71  Bit Score: 61.17  E-value: 6.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541   4 LESELTCPICLELFEDPLLLPCAHSLCFNCAhrilvshCATNEPVESiNAFQCPTCRHVITLSQRgldgLKRNVTLQNII 83
Cdd:cd16597     2 LEEELTCSICLELFKDPVTLPCGHNFCGVCI-------EKTWDSQHG-SEYSCPQCRATFPRRPE----LHKNTVLRNIV 69


                  ..
gi 1039796541  84 DR 85
Cdd:cd16597    70 EQ 71
SPRY_PRY_TRIM38 cd15815
PRY/SPRY domain of tripartite motif-binding protein 38 (TRIM38), also known as Ring finger ...
 463-607 6.47e-12

PRY/SPRY domain of tripartite motif-binding protein 38 (TRIM38), also known as Ring finger protein 15 (RNF15); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM38, which is also known as RING finger protein 15 (RNF15) or RORET. TRIM38 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. TRIM38 has been shown to act as a suppressor in TOLL-like receptor (TLR)-mediated interferon (IFN)-beta induction by promoting degradation of TRAF6 and NAP1 through the ubiquitin-proteasome system. Another study has shown that TRIM38 may act as a novel negative regulator for TLR3-mediated IFN-beta signaling by targeting TRIF for degradation. TRIM38 has been identified as a critical negative regulator in TNFalpha- and IL-1beta-triggered activation of NF-kappaB and MAP Kinases (MAPKs); it causes degradation of two essential cellular components, TGFbeta-associated kinase 1 (TAK1)-associating chaperones 2 and 3 (TAB2/3). The degradation is promoted through a lysosomal-dependent pathway, which requires the C-terminal PRY-SPRY of TRIM38. Enterovirus 71 infection induces degradation of TRIM38, suggesting that TRIM38 may play a role in viral infections.


Pssm-ID: 293987 [Multi-domain]  Cd Length: 182  Bit Score: 64.68  E-value: 6.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAGqgSYGVAGNVFIDSGRHYWEV-VTSGSTWyAIGLAYRSAPKHE 541
Cdd:cd15815    17 LDPDTAHPELTLSKDQRQVTYGRCQENLDASPKRFTV--LPCVLGCEGFTSGRHYFEVdVGEGTGW-DVGVCLENVQRGF 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039796541 542 WIGKNAASwalcrchNHWAVRHDGKETPIA----PAP-HLRR----VGVLLDYDNGSIAFYDALSSVHLHTFHAA 607
Cdd:cd15815    94 GMKQEPEF-------GFWTIRLCEEDGYVAltspPTPlPLREkplvVGVFLDYEAGLVSFYNMTTGSHIFTFPKA 161
SPRY_PRY_TRIM27 cd15814
PRY/SPRY domain in tripartite motif-containing protein 27 (TRIM27), also known as RING finger ...
 463-618 7.86e-12

PRY/SPRY domain in tripartite motif-containing protein 27 (TRIM27), also known as RING finger protein 76 (RNF76); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM27, also known as RING finger protein 76 (RNF76) or RET finger protein (RFP). TRIM27 domain is composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It is highly expressed in the spleen, thymus and in cells of the hematopoietic compartment. TRIM27 exhibits either nuclear or cytosolic localization depending on the cell type. TRIM27 negatively regulates nucleotide-binding oligomerization domain containing 2 (NOD2)-mediated signaling by proteasomal degradation of NOD2, suggesting that TRIM27 could be a new target for therapeutic intervention in NOD2-associated diseases such as Crohn's. High expression of TRIM27 is observed in several human cancers, including breast and endometrial cancer, where elevated TRIM27 expression predicts poor prognosis. Also, TRIM27 forms an oncogenic fusion protein with Ret proto-oncogene. It is involved in different stages of spermatogenesis and its significant expression in male germ cells and seminomas, suggests that TRIM27 may be associated with the regulation of testicular germ cell proliferation and histological-type of germ cell tumors. TRIM27 could also be a predictive marker for chemoresistance in ovarian cancer patients. In the neurotoxin model of Parkinson's disease (PD), deficiency of TRIM27 decreases apoptosis and protects dopaminergic neurons, making TRIM27 an effective potential target during the treatment of PD.


Pssm-ID: 293986 [Multi-domain]  Cd Length: 177  Bit Score: 64.33  E-value: 7.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAGQGSygVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPKHEW 542
Cdd:cd15814     6 LDPDTAYPSLILSDNLRQVRYSYLQQDLPDNPERFNLFPC--VLGSPCFIAGRHYWEVEVGDKAKWTIGVCEDSVCRKGG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 543 IGKNAAS--WALCRCH--NHWAVRHDGKETPIAPAphLRRVGVLLDYDNGSIAFYDALSSVHLHTF-HAALAQPVCPTFT 617
Cdd:cd15814    84 VTSAPQNgfWAVSLWYgkEYWALTSPMTALPLRTP--LQRVGIFLDYDAGEVSFYNVTERCHTFTFsHATFCGPVRPYFS 161


                  .
gi 1039796541 618 V 618
Cdd:cd15814   162 L 162
RING-HC_TRIM13_C-V cd16762
RING finger, HC subclass, found in tripartite motif-containing protein 13 (TRIM13) and similar ...
 5-60 9.62e-12

RING finger, HC subclass, found in tripartite motif-containing protein 13 (TRIM13) and similar proteins; TRIM13, also known as B-cell chronic lymphocytic leukemia tumor suppressor Leu5, leukemia-associated protein 5, putative tumor suppressor RFP2, RING finger protein 77 (RNF77), or Ret finger protein 2, is an endoplasmic reticulum (ER) membrane anchored E3 ubiquitin-protein ligase that interacts with proteins localized to the ER, including valosin-containing protein (VCP), a protein indispensable for ER-associated degradation (ERAD). It also targets the known ER proteolytic substrate CD3-delta, but not the N-end rule substrate Ub-R-YFP (yellow fluorescent protein) for degradation. Moreover, TRIM13 regulates ubiquitination and degradation of NEMO to suppress tumor necrosis factor (TNF) induced nuclear factor-kappaB (NF- kappa B) activation. It is also involved in NF-kappaB p65 activation and nuclear factor of activated T-cells (NFAT)-dependent activation of c-Rel upon T-cell receptor engagement. Furthermore, TRIM13 negatively regulates melanoma differentiation-associated gene 5 (MDA5)-mediated type I interferon production. It also regulates caspase-8 ubiquitination, translocation to autophagosomes, and activation during ER stress induced cell death. Meanwhile, TRIM13 enhances ionizing radiation-induced apoptosis by increasing p53 stability and decreasing AKT kinase activity through MDM2 and AKT degradation. TRIM13 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. In addition, TRIM13 contains a C-terminal transmembrane domain.


Pssm-ID: 438418 [Multi-domain]  Cd Length: 56  Bit Score: 60.32  E-value: 9.62e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796541   5 ESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVshcATNEPVESINAFQCPTCR 60
Cdd:cd16762     1 EEDLTCPICCCLFDDPRVLPCSHNFCKKCLEGILE---GNVRTMLWRPPFKCPTCR 53
SPRY_PRY_TRIM72 cd13742
PRY/SPRY domain in tripartite motif-binding protein 72 (TRIM72); This domain, consisting of ...
 464-618 2.23e-11

PRY/SPRY domain in tripartite motif-binding protein 72 (TRIM72); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM72. Muscle-specific TRIM72 (also known as Mitsugumin 53 or MG53) has been shown to perform a critical function in membrane repair following acute muscle injury by nucleating the assembly of the repair machinery at injury sites. It is expressed specifically in skeletal muscle and heart, and tethered to the plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine. TRIM72 interacts with dysferlin, a sarcolemmal protein whose deficiency causes Miyoshi myopathy (MM) and limb girdle muscular dystrophy type 2B (LGMD2B); this coordination plays an important role in the repair of sarcolemma damage.


Pssm-ID: 293976 [Multi-domain]  Cd Length: 192  Bit Score: 63.34  E-value: 2.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 464 DPKSAHRKLKVSHDNLTVE-RDESSSKKSHAPERFaGQGSYGVAGNVFIDsGRHYWEVVTSGSTWYAIGLAYRSAPKHew 542
Cdd:cd13742    17 DPDTAHPYLVVSSDGKRVEcADQKQAVSSDDPNRF-DKANCVVSHQSFSE-GEHYWEVIVGDKPRWALGVISAEAGRK-- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 543 iGKNAAS-----WAL-CRCHNHWAVRHDGKEtPIAPAPHLR--RVGVLLDYDNGSIAFYDALSS---VHLHTFHAALAQP 611
Cdd:cd13742    93 -GRLHALpsngfWLLgCKEGKVYEAHVEHKE-PRALRVEGRptRIGVYLSFSDGVLSFYDASDEdnlVQLFAFHERFPGP 170


                  ....*..
gi 1039796541 612 VCPTFTV 618
Cdd:cd13742   171 LYPFFDV 177
RING-HC_TRIM65_C-IV cd16609
RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar ...
 5-60 3.71e-11

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: 58.54  E-value: 3.71e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796541   5 ESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVshcatnepVESINAFQCPTCR 60
Cdd:cd16609     1 EEELTCSICLGLYQDPVTLPCQHSFCRACIEDHWR--------QKDEGSFSCPECR 48
RING-HC_TRIM9 cd16755
RING finger, HC subclass, found in tripartite motif-containing protein 9 (TRIM9) and similar ...
 5-59 5.19e-11

RING finger, HC subclass, found in tripartite motif-containing protein 9 (TRIM9) and similar proteins; TRIM9, human ortholog of rat Spring, also known as RING finger protein 91 (RNF91), is a brain-specific E3 ubiquitin-protein ligase collaborating with an E2 ubiquitin conjugating enzyme UBCH5b. TRIM9 plays an important role in the regulation of neuronal functions and participates in the neurodegenerative disorders through its ligase activity. It interacts with the WD repeat region of beta-transducin repeat-containing protein (beta-TrCP) through its N-terminal degron motif depending on the phosphorylation status, and thus negatively regulates nuclear factor-kappaB (NF-kappaB) activation in the NF-kappaB pro-inflammatory signaling pathway. Moreover, TRIM9 acts as a critical catalytic link between Netrin-1 and the exocytic soluble NSF attachment receptor protein (SNARE) machinery in murine cortical neurons. It promotes SNARE-mediated vesicle fusion and axon branching in a Netrin-dependent manner. TRIM9 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438413 [Multi-domain]  Cd Length: 55  Bit Score: 58.12  E-value: 5.19e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039796541   5 ESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATNEPVESINafqCPTC 59
Cdd:cd16755     1 EEELKCPVCGSFYREPIILPCSHNLCLACARNILVQTPEAESPQSCLT---CPQC 52
Bbox1_TRIM67_C-I cd19844
B-box-type 1 zinc finger found in tripartite motif-containing protein 67 (TRIM67) and similar ...
 119-164 8.35e-11

B-box-type 1 zinc finger found in tripartite motif-containing protein 67 (TRIM67) and similar proteins; TRIM67, also termed TRIM9-like protein (TNL), is a protein selectively expressed in the cerebellum. It interacts with PRG-1, an important molecule in the control of hippocampal excitability dependent on presynaptic LPA2 receptor signaling, and 80K-H (also known as glucosidase II beta), a protein kinase C substrate. It negatively regulates Ras signaling in cell proliferation via degradation of 80K-H, leading to neural differentiation including neuritogenesis. TRIM67 belongs to the C-I subclass of 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 RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, the fibronectin type III domain and the SPRY/B30.2 domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


Pssm-ID: 380902  Cd Length: 49  Bit Score: 57.36  E-value: 8.35e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1039796541 119 CQFCDQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEP 164
Cdd:cd19844     4 CQLCDRNPPEPAAVLCEQCDVLYCSACQLKCHPTRGPFAKHRLVPP 49
SPRY_PRY_TRIM25-like cd13737
PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25)-like; This domain, ...
 514-618 2.49e-10

PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25)-like; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of proteins similar to TRIM25 (composed of RING/B-box/coiled-coil core and also known as RBCC proteins). TRIM25 (also called Efp) ubiquitinates the N terminus of the viral RNA receptor retinoic acid-inducible gene-I (RIG-I) in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. It has been shown that the influenza A virus targets TRIM25 and disables its antiviral function.


Pssm-ID: 293972  Cd Length: 172  Bit Score: 59.89  E-value: 2.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 514 GRHYWEVVTSGStWYAIGLAYRSAPKHE------WIGKNAASWALCRCHNHWAVRHDGKETPIAPAPHlRRVGVLLDYDN 587
Cdd:cd13737    53 GCHYWEAEVSNS-WVCLGVTYSYSHPTGkscifyLIGRNPYSWCLEWDSLKFSVWHNNIQTVVHGSYY-KTIGVLLDYAA 130

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1039796541 588 GSIAFYDALSSVHL-HTFHAALAQPVCPTFTV 618
Cdd:cd13737   131 GSLTFYGVANTMNLiYRFLTTFTEPLYPAVMV 162
RING-HC_TRIM67 cd16758
RING finger, HC subclass, found in tripartite motif-containing protein 67 (TRIM67) and similar ...
 5-59 4.10e-10

RING finger, HC subclass, found in tripartite motif-containing protein 67 (TRIM67) and similar proteins; TRIM67, also known as TRIM9-like protein (TNL), is selectively expressed in the cerebellum. It interacts with PRG-1, an important molecule in the control of hippocampal excitability dependent on presynaptic LPA2 receptor signaling, and 80K-H (also known as glucosidase II beta), a protein kinase C substrate. It negatively regulates Ras signaling in cell proliferation via degradation of 80K-H, leading to neural differentiation including neuritogenesis. TRIM67 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438416 [Multi-domain]  Cd Length: 57  Bit Score: 55.86  E-value: 4.10e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039796541   5 ESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATNEPVESINAFQCPTC 59
Cdd:cd16758     1 EEELKCPVCGSLFREPIILPCSHNVCLPCARTIAVQTPESEQHLPHSSSITCPQC 55
RING-HC_TRIM13_like_C-V cd16581
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and ...
 6-60 4.75e-10

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and similar proteins; TRIM13 and TRIM59, two closely related tripartite motif-containing proteins, belong 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, followed by a C-terminal transmembrane domain. TRIM13, also known as B-cell chronic lymphocytic leukemia tumor suppressor Leu5, leukemia-associated protein 5, putative tumor suppressor RFP2, RING finger protein 77 (RNF77), or Ret finger protein 2, is an endoplasmic reticulum (ER) membrane anchored E3 ubiquitin-protein ligase that interacts with proteins localized to the ER, including valosin-containing protein (VCP), a protein indispensable for ER-associated degradation (ERAD). TRIM59, also known as RING finger protein 104 (RNF104) or tumor suppressor TSBF-1, is a putative E3 ubiquitin-protein ligase that functions as a novel multiple cancer biomarker for immunohistochemical detection of early tumorigenesis.


Pssm-ID: 438243 [Multi-domain]  Cd Length: 50  Bit Score: 55.21  E-value: 4.75e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039796541   6 SELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATnepveSINAFQCPTCR 60
Cdd:cd16581     1 EELTCSICYNIFDDPKILPCSHTFCKNCLEKLLAASGYY-----LLASLKCPTCR 50
RING-HC_TRIM59_C-V cd16763
RING finger, HC subclass, found in tripartite motif-containing protein 59 (TRIM59) and similar ...
 5-60 5.06e-10

RING finger, HC subclass, found in tripartite motif-containing protein 59 (TRIM59) and similar proteins; TRIM59, also known as RING finger protein 104 (RNF104) or tumor suppressor TSBF-1, is a putative E3 ubiquitin-protein ligase that functions as a novel multiple cancer biomarker for immunohistochemical detection of early tumorigenesis. It is upregulated in gastric cancer and promotes gastric carcinogenesis by interacting with and targeting the P53 tumor suppressor for its ubiquitination and degradation. It also acts as a novel accessory molecule involved in cytotoxicity of BCG-activated macrophages (BAM). Moreover, TRIM59 may serve as a multifunctional regulator for innate immune signaling pathways. It interacts with ECSIT and negatively regulates nuclear factor-kappaB (NF- kappa B) and interferon regulatory factor (IRF)-3/7-mediated signal pathways. TRIM59 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. In addition, TRIM59 contains a C-terminal transmembrane domain.


Pssm-ID: 438419 [Multi-domain]  Cd Length: 56  Bit Score: 55.30  E-value: 5.06e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796541   5 ESELTCPICLELFEDPLLLPCAHSLCFNCAHRIL--VSHCATNEPVESinAFQCPTCR 60
Cdd:cd16763     1 EEDLTCSVCYSLFEDPRVLPCSHTFCRNCLENILqvSGNFSIWRPLRP--PLKCPNCR 56
RING-HC_TRIM4_C-IV cd16590
RING finger, HC subclass, found in tripartite motif-containing protein TRIM4 and similar ...
 2-61 5.67e-10

RING finger, HC subclass, found in tripartite motif-containing protein TRIM4 and similar proteins; TRIM4 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, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM4, also known as RING finger protein 87 (RNF87), is a cytoplasmic E3 ubiquitin-protein ligase that has recently evolved and is present only in higher mammals. It transiently interacts with mitochondria, induces mitochondrial aggregation and sensitizes the cells to hydrogen peroxide (H2O2) induced death. Its interaction with peroxiredoxin 1 (PRX1) is critical for the regulation of H2O2 induced cell death. Moreover, TRIM4 functions as a positive regulator of RIG-I-mediated type I interferon induction. It regulates the K63-linked ubiquitination of RIG-1 and assembly of antiviral signaling complex at the mitochondria.


Pssm-ID: 438252 [Multi-domain]  Cd Length: 61  Bit Score: 55.42  E-value: 5.67e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541   2 ETLESELTCPICLELFEDPLLLPCAHSLCFNCAHRilvSHCATNEPvesinaFQCPTCRH 61
Cdd:cd16590     1 EDIQEELTCPICLDYFQDPVSIECGHNFCRGCLHR---NWAPGGGP------FPCPECRH 51
Bbox1_TRIM9-like_C-I cd19803
B-box-type 1 zinc finger found in tripartite motif-containing proteins, TRIM9, TRIM67 and ...
 119-164 7.40e-10

B-box-type 1 zinc finger found in tripartite motif-containing proteins, TRIM9, TRIM67 and similar proteins; This family includes a group of tripartite motif-containing proteins, including TRIM9 and TRIM67, both of which belong to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, consisting of three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. TRIM9 (the human ortholog of rat Spring), also known as RING finger protein 91 (RNF91), is a brain-specific E3 ubiquitin-protein ligase collaborating with an E2 ubiquitin conjugating enzyme UBCH5b. It plays an important role in the regulation of neuronal functions and participates in the neurodegenerative disorders through its ligase activity. TRIM67, also termed TRIM9-like protein (TNL), is a protein selectively expressed in the cerebellum. It interacts with PRG-1, an important molecule in the control of hippocampal excitability dependent on presynaptic LPA2 receptor signaling, and 80K-H (also known as glucosidase II beta), a protein kinase C substrate. It negatively regulates Ras signaling in cell proliferation via degradation of 80K-H, leading to neural differentiation including neuritogenesis.


Pssm-ID: 380861  Cd Length: 47  Bit Score: 54.62  E-value: 7.40e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1039796541 119 CQFCDQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEP 164
Cdd:cd19803     2 CQLCEKSPPKEASVFCEQCEVFYCDSCRESCHPPRGPLAKHTLVSP 47
RING-HC_TRIM36_C-I cd16756
RING finger, HC subclass, found in tripartite motif-containing protein 36 (TRIM36) and similar ...
 5-65 8.60e-10

RING finger, HC subclass, found in tripartite motif-containing protein 36 (TRIM36) and similar proteins; TRIM36, the human ortholog of mouse Haprin, also known as RING finger protein 98 (RNF98) or zinc-binding protein Rbcc728, is an E3 ubiquitin-protein ligase expressed in the germ plasm. It has been implicated in acrosome reaction, fertilization, and embryogenesis, as well as in carcinogenesis. TRIM36 functions upstream of Wnt/beta-catenin activation, and plays a role in controlling the stability of proteins regulating microtubule polymerization during cortical rotation, and subsequently dorsal axis formation. It is also potentially associated with chromosome segregation by interacting with the kinetochore protein centromere protein-H (CENP-H), and colocalizing with the microtubule protein alpha-tubulin. Its overexpression may cause chromosomal instability and carcinogenesis. It is, thus, a novel regulator affecting cell cycle progression. Moreover, TRIM36 plays a critical role in the arrangement of somites during embryogenesis. TRIM36 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, a PRY domain and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438414 [Multi-domain]  Cd Length: 49  Bit Score: 54.53  E-value: 8.60e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039796541   5 ESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVShcatnepvesinaFQCPTCRHVITL 65
Cdd:cd16756     1 ERELICPSCKELFTHPLILPCQHSVCHKCVKELLTT-------------FPCPGCQHDVDL 48
RING-HC_MuRF2 cd16760
RING finger, HC subclass, found in muscle-specific RING finger protein 2 (MuRF-2) and similar ...
 5-61 1.12e-09

RING finger, HC subclass, found in muscle-specific RING finger protein 2 (MuRF-2) and similar proteins; MuRF-2, also known as tripartite motif-containing protein 55 (TRIM55) or RING finger protein 29 (RNF29), is a muscle-specific E3 ubiquitin-protein ligase in ubiquitin-mediated muscle protein turnover and is also a ligand of the transactivation domain of the serum response transcription factor (SRF). It is predominantly slow-fibre associated and highly expressed in embryonic skeletal muscle. MuRF-2 associates transiently with microtubules, myosin, and titin during sarcomere assembly. It has been implicated in microtubule, intermediate filament, and sarcomeric M-line maintenance in striated muscle development, as well as in signaling from the sarcomere to the nucleus. It plays an important role in the earliest stages of skeletal muscle differentiation and myofibrillogenesis. It is developmentally downregulated and is assembled at the M-line region of the sarcomere and with microtubules. MuRF-2 belongs to the C-II subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain. It also harbors a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains.


Pssm-ID: 438417 [Multi-domain]  Cd Length: 64  Bit Score: 54.61  E-value: 1.12e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039796541   5 ESELTCPICLELFEDP-LLLPCAHSLCFNCAHRILVSH-----CATNEPVESINAFQCPTCRH 61
Cdd:cd16760     1 EKQLICPICLEMFTKPvVILPCQHNLCRKCANDIFQASnpylpTRGGTTVASGGRFRCPSCRH 63
RING-HC_MuRF1 cd16759
RING finger, HC subclass, found in muscle-specific RING finger protein 1 (MuRF-1) and similar ...
 5-61 1.75e-09

RING finger, HC subclass, found in muscle-specific RING finger protein 1 (MuRF-1) and similar proteins; MuRF-1, also known as tripartite motif-containing protein 63 (TRIM63), RING finger protein 28 (RNF28), iris RING finger protein, or striated muscle RING zinc finger, is an E3 ubiquitin-protein ligase in ubiquitin-mediated muscle protein turnover. It is predominantly fast (type II) fibre-associated in skeletal muscle and can bind to many myofibrillar proteins, including titin, nebulin, the nebulin-related protein NRAP, troponin-I (TnI), troponin-T (TnT), myosin light chain 2 (MLC-2), myotilin, and T-cap. The early and robust upregulation of MuRF-1 is triggered by disuse, denervation, starvation, sepsis, or steroid administration resulting in skeletal muscle atrophy. It also plays a role in maintaining titin M-line integrity. It associates with the periphery of the M-line lattice and may be involved in the regulation of the titin kinase domain. It also participates in muscle stress response pathways and gene expression. MuRF-1 belongs to the C-II subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain. It also harbors a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains.


Pssm-ID: 319673 [Multi-domain]  Cd Length: 63  Bit Score: 54.26  E-value: 1.75e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039796541   5 ESELTCPICLELFEDP-LLLPCAHSLCFNCAHRILVS-----HCATNEPVESINAFQCPTCRH 61
Cdd:cd16759     1 EKQLICPICLEMFTKPvVILPCQHNLCRKCANDIFQAanpywQSRGTSMLGSGGRFRCPSCRH 63
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 357-456 2.00e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 54.81  E-value: 2.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 357 SYDTITVHWT--SEDEFSVVSYELQYTIfTGQANVVNVAcdgtcllgsaglcnsadswmiVPNIKQNHYTVHGLQSGTKY 434
Cdd:cd00063    13 TSTSVTLSWTppEDDGGPITGYVVEYRE-KGSGDWKEVE---------------------VTPGSETSYTLTGLKPGTEY 70

                          90       100
                  ....*....|....*....|...
gi 1039796541 435 IFTVKAINQAG-SRSSEPGKLKT 456
Cdd:cd00063    71 EFRVRAVNGGGeSPPSESVTVTT 93
SPRY_PRY_TRIM67_9 cd12889
PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, ...
 461-593 2.14e-09

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: 56.87  E-value: 2.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 461 FRLDPKSAHRKLKVSHDNLTVerdeSSSKKSHapeRFagqgsygVAGNVFIDSGRHYWEVVT---SGSTWYAIGLAYRSA 537
Cdd:cd12889    10 FTFDPSTSHPDIILSNDNMTV----TCNSYED---RV-------VLGSVGFSRGVHYWEVTIdryDGHPDPAFGVARIDV 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796541 538 PKHEWIGKNAASWAL-----------CRCHNHwavRHDGKETPIApaphlrRVGVLLDYDNGSIAFY 593
Cdd:cd12889    76 NKDKMLGKDDKGWSMyidnnrswflhNNEHSN---RTEGGITVGS------VVGVLLDLDRHTLSFY 133
SPRY_PRY_TRIM5_6_22_34 cd15810
PRY/SPRY domain of tripartite motif-binding protein 5, 6, 22 and 34 (TRIM5, TRIM6, TRIM22 and ...
 463-620 3.00e-09

PRY/SPRY domain of tripartite motif-binding protein 5, 6, 22 and 34 (TRIM5, TRIM6, TRIM22 and TRIM34); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of very close paralogs, TRIM5, TRIM6, TRIM22 and TRIM34. These domains are composed of RING/B-box/coiled-coil core and are also known as RBCC proteins. They form a locus of four closely related TRIM genes within an olfactory receptor-rich region on chromosome 11 of the human genome. Genetic analysis of this locus indicates that these four genes have evolved by gene duplication from a common ancestral gene. All genes in the TRIM6/TRIM34/TRIM5/TRIM22 locus are type I interferon inducible, with TRIM5 and TRIM22 possessing antiviral properties. TRIM5 promotes innate immune signaling by activating the TAK1 kinase complex by cooperating with the heterodimeric E2, UBC13/UEV1A. It also stimulates NFkB and AP-1 signaling, and the transcription of inflammatory cytokines and chemokines, amplifying these activities upon retroviral infection. Interaction of its PRY-SPRY or cyclophilin domains with the retroviral capsid lattice stimulates the formation of a complementary lattice by TRIM5, with greatly increased TRIM5 E3 activity, and host cell signal transduction. TRIM6 is selectively expressed in embryonic stem (ES) cells and interacts with the proto-oncogene product Myc, maintaining the pluripotency of the ES cells. TRIM6, together with E2 Ubiquitin conjugase (UbE2K) and K48-linked poly-Ub chains, is critical for the IkappaB kinase epsilon (IKKepsilon) branch of type I interferon (IFN-I) signaling pathway and subsequent establishment of a protective antiviral response. TRIM22 plays an integral role in the host innate immune response to viruses; it has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. Altered TRIM22 expression has also been associated with multiple sclerosis, cancer, and autoimmune disease. While the PRY-SPRY domain of TRIM5a provides specificity and the capsid recognition motif to retroviral restriction, TRIM34 binds HIV-1 capsid but does not restrict HIV-1 infection.


Pssm-ID: 293982 [Multi-domain]  Cd Length: 189  Bit Score: 57.10  E-value: 3.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFagqGSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGL-AYRSAPKHE 541
Cdd:cd15810     4 LNPVNISLNIVISEDQRQVRIVPPQTSGQALTNNN---YDFGVLGSQYFSSGKHYWEVDVSKKSAWILGVcSHKRSDAMT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 542 WIGKNAASWalcrcHN----------HWAV------RHDGKETPIAPAPHL---------RRVGVLLDYDNGSIAFYDAl 596
Cdd:cd15810    81 KSNANQINH-----QNvysryqpqygYWVIglqnesEYNAFEDSSSFNPHVltlsvtvppHRVGVFLDYEAGTVSFFNV- 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1039796541 597 ssvhlhTFHAAL---------AQPVCPTFTVWN 620
Cdd:cd15810   155 ------TNHGSLiykfskccfSTTVCPYFNPWN 181
RING-HC_TRIM7-like_C-IV cd16594
RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM7, TRIM11 and ...
 3-68 3.20e-09

RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM7, TRIM11 and TRIM27, and similar proteins; TRIM7, TRIM11 and TRIM27, closely related tripartite motif-containing proteins, belong 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, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM7, also known as glycogenin-interacting protein (GNIP) or RING finger protein 90 (RNF90), is an E3 ubiquitin-protein ligase that mediates c-Jun/AP-1 activation by Ras signalling. Its phosphorylation and activation by MSK1 in response to direct activation by the Ras-Raf-MEK-ERK pathway can stimulate TRIM7 E3 ubiquitin ligase activity in mediating Lys63-linked ubiquitination of the AP-1 coactivator RACO-1, leading to RACO-1 protein stabilization. Moreover, TRIM7 binds and activates glycogenin, the self-glucosylating initiator of glycogen biosynthesis. TRIM11, also known as protein BIA1, or RING finger protein 92 (RNF92), is an E3 ubiquitin-protein ligase involved in the development of the central nervous system. It is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. TRIM11 acts as a potential therapeutic target for congenital central hypoventilation syndrome (CCHS) by mediating the degradation of CCHS-associated polyalanine-expanded Phox2b. TRIM11 modulates the function of neurogenic transcription factor Pax6 through the ubiquitin-proteosome system, and thus plays an essential role for Pax6-dependent neurogenesis. It also binds to and destabilizes a key component of the activator-mediated cofactor complex (ARC105), humanin, a neuroprotective peptide against Alzheimer's disease-relevant insults, and further regulates ARC105 function in transforming growth factor beta (TGFbeta) signaling. Moreover, TRIM11 negatively regulates retinoic acid-inducible gene-I (RIG-I)-mediated interferon-beta (IFNbeta) production and antiviral activity by targeting TANK-binding kinase-1 (TBK1). It may contribute to the endogenous restriction of retroviruses in cells. It enhances N-tropic murine leukemia virus (N-MLV) entry by interfering with Ref1 restriction. It also suppresses the early steps of human immunodeficiency virus HIV-1 transduction, resulting in decreased reverse transcripts. TRIM27, also known as RING finger protein 76 (RNF76), RET finger protein (RFP), or zinc finger protein RFP, is a nuclear E3 ubiquitin-protein ligase that is highly expressed in testis and in various tumor cell lines. Expression of TRIM27 is associated with prognosis of colon and endometrial cancers. TRIM27 was first identified as a fusion partner of the RET receptor tyrosine kinase. It functions as a transcriptional repressor and associates with several proteins involved in transcriptional activity, such as enhancer of polycomb 1 (Epc1), a member of the Polycomb group proteins, and Mi-2beta, a main component of the nucleosome remodeling and deacetylase (NuRD) complex, and the cell cycle regulator retinoblastoma protein (RB1). It also interacts with HDAC1, leading to downregulation of thioredoxin binding protein 2 (TBP-2), which inhibits the function of thioredoxin. Moreover, TRIM27 mediates Pax7-induced ubiquitination of MyoD in skeletal muscle atrophy. In addition, it inhibits muscle differentiation by modulating serum response factor (SRF) and Epc1. TRIM27 promotes a non-canonical polyubiquitination of PTEN, a lipid phosphatase that catalyzes PtdIns(3,4,5)P3 (PIP3) to PtdIns(4,5)P2 (PIP2). It is an IKKepsilon-interacting protein that regulates IkappaB kinase (IKK) function and negatively regulates signaling involved in the antiviral response and inflammation. TRIM27 also forms a protein complex with MBD4 or MBD2 or MBD3, and thus plays an important role in the enhancement of transcriptional repression through MBD proteins in tumorigenesis, spermatogenesis, and embryogenesis. It is a component of an estrogen receptor 1 (ESR1) regulatory complex that is involved in estrogen receptor-mediated transcription in MCF-7 cells.


Pssm-ID: 438256 [Multi-domain]  Cd Length: 61  Bit Score: 53.07  E-value: 3.20e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796541   3 TLESELTCPICLELFEDPLLLPCAHSLCFNCahrilVSHCATnepvESINAFQCPTCRHVITLSQR 68
Cdd:cd16594     1 SLQEELTCPICLDYFTDPVTLDCGHSFCRAC-----IARCWE----EPETSASCPQCRETCPQRNL 57
RING-HC_TRIM9-like_C-I cd16576
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM9, TRIM67, and ...
 5-60 3.27e-09

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


Pssm-ID: 438238 [Multi-domain]  Cd Length: 42  Bit Score: 52.80  E-value: 3.27e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796541   5 ESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVShcatnepvesinafqCPTCR 60
Cdd:cd16576     1 EEELKCPVCGSLFTEPVILPCSHNLCLGCALNIQLT---------------CPICH 41
RING-HC_MuRF_C-II cd16577
RING finger, HC subclass, found in muscle-specific RING finger proteins TRIM63/MuRF-1, TRIM55 ...
 8-60 1.26e-08

RING finger, HC subclass, found in muscle-specific RING finger proteins TRIM63/MuRF-1, TRIM55/MuRF-2 and TRIM54/MuRF-3; This subfamily corresponds to a group of striated muscle-specific tripartite motif (TRIM) proteins, including TRIM63/MuRF-1, TRIM55/MuRF-2, and TRIM54/MuRF-3, which function as E3 ubiquitin ligases in ubiquitin-mediated muscle protein turnover. They are tightly developmentally regulated in skeletal muscle and associate with different cytoskeleton components, such as microtubules, Z-disks and M-bands, as well as with metabolic enzymes and nuclear proteins. They also cooperate with diverse proteins implicated in selective protein degradation by the proteasome and autophagosome, and target proteins of metabolic regulation, sarcomere assembly and transcriptional regulation. Moreover, MURFs display variable fibre-type preferences. TRIM63/MuRF-1 is predominantly fast (type II) fibre-associated in skeletal muscle. TRIM55/MuRF-2 is predominantly slow-fibre associated. TRIM54/MuRF-3 is ubiquitously present. They play an active role in microtubule-mediated sarcomere assembly. MuRFs belong to the C-II subclass of the TRIM family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain positioned C-terminal to the RBCC domain. They also harbor a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains.


Pssm-ID: 438239 [Multi-domain]  Cd Length: 56  Bit Score: 51.43  E-value: 1.26e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796541   8 LTCPICLELFEDP-LLLPCAHSLCFNCAHRILVSH--CATNEPVESINAFQCPTCR 60
Cdd:cd16577     1 LICPICLEMFTKPvVILPCQHNLCRKCANDIFQARnpYWPTTTMGSGGRFRCPSCR 56
Bbox1_TRIM8-like cd19802
B-box-type 1 zinc finger found in tripartite motif-containing proteins, TRIM8, TRIM16, TRIM25, ...
 118-164 1.29e-08

B-box-type 1 zinc finger found in tripartite motif-containing proteins, TRIM8, TRIM16, TRIM25, TRIM29, TRIM44, TRIM47 and similar proteins; This family includes a group of tripartite motif-containing proteins, including TRIM8, TRIM16, TRIM25, TRIM29, TRIM44 and TRIM47. 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. TRIM16, also termed estrogen-responsive B box protein (EBBP), may play a role in the regulation of keratinocyte differentiation. It may also act as a tumor suppressor by affecting cell proliferation and migration or tumorigenicity in carcinogenesis. TRIM25, also termed estrogen-responsive finger protein (EFP), or ubiquitin/ISG15-conjugating enzyme TRIM25, or zinc finger protein 147 (ZNF147), or E3 ubiquitin/ISG15 ligase TRIM25, is induced by estrogen and is particularly abundant in placenta and uterus. It has been implicated in cell proliferation, protein modification, and the retinoic acid inducible gene I (RIG-I)-mediated antiviral signaling pathway. It functions as an E3-ubiquitin ligase able to transfer ubiquitin and ISG15 to target proteins. TRIM29, also termed ataxia telangiectasia group D-associated protein (ATDC), plays a crucial role in the regulation of macrophage activation in response to viral or bacterial infections within the respiratory tract. TRIM44, also termed protein DIPB, functions as a critical regulator in tumor metastasis and progression. TRIM47, also known as gene overexpressed in astrocytoma protein (GOA) or RING finger protein 100 (RNF100), plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis. The TRIM (tripartite motif) family of proteins are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


Pssm-ID: 380860  Cd Length: 46  Bit Score: 51.27  E-value: 1.29e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1039796541 118 LCQFCDQDPAQDAVKTCVTCEVSYCDECLKAtHPNKKPFTGHRLIEP 164
Cdd:cd19802     1 LCDFCDPGKALKAVKSCLTCEASLCEIHLRP-HLESPALKSHQLVEP 46
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
 8-59 1.32e-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: 50.95  E-value: 1.32e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039796541   8 LTCPICLELFEDPLLLPCAHSLCFNCAHRILvshcatnepveSINAFQCPTC 59
Cdd:cd16449     1 LECPICLERLKDPVLLPCGHVFCRECIRRLL-----------ESGSIKCPIC 41
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 359-446 1.57e-08

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 52.23  E-value: 1.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541  359 DTITVHWTSEDEFSVVSYELQYTIFTGQANvvnvacdgtcllgsaglcnsaDSWMIVP-NIKQNHYTVHGLQSGTKYIFT 437
Cdd:smart00060  15 TSVTLSWEPPPDDGITGYIVGYRVEYREEG---------------------SEWKEVNvTPSSTSYTLTGLKPGTEYEFR 73


                   ....*....
gi 1039796541  438 VKAINQAGS 446
Cdd:smart00060  74 VRAVNGAGE 82
Bbox1_TRIM36_C-I cd19848
B-box-type 1 zinc finger found in tripartite motif-containing protein 36 (TRIM36) and similar ...
 113-164 2.28e-08

B-box-type 1 zinc finger found in tripartite motif-containing protein 36 (TRIM36) and similar proteins; TRIM36, the human ortholog of mouse Haprin, also known as RING finger protein 98 (RNF98) or zinc-binding protein Rbcc728, is an E3 ubiquitin-protein ligase expressed in the germ plasm. It has been implicated in acrosome reaction, fertilization, and embryogenesis, as well as in carcinogenesis. TRIM36 functions upstream of Wnt/beta-catenin activation, and plays a role in controlling the stability of proteins regulating microtubule polymerization during cortical rotation, and subsequent dorsal axis formation. It is also potentially associated with chromosome segregation by interacting with the kinetochore protein centromere protein-H (CENP-H), and colocalizing with the microtubule protein alpha-tubulin. Its overexpression may cause chromosomal instability and carcinogenesis. It is, thus, a novel regulator affecting cell cycle progression. Moreover, TRIM36 plays a critical role in the arrangement of somites during embryogenesis. TRIM36 belongs to the C-I subclass of 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 RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


Pssm-ID: 380906  Cd Length: 55  Bit Score: 50.83  E-value: 2.28e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039796541 113 SAEKVLCQFCdQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEP 164
Cdd:cd19848     1 AATAIMCDLC-KPPPQESTKSCMDCKASYCNECFKIHHPWGTPKAQHEYVGP 51
RING-HC_MuRF3 cd16761
RING finger, HC subclass, found in muscle-specific RING finger protein 3 (MuRF-3) and similar ...
 8-60 3.21e-08

RING finger, HC subclass, found in muscle-specific RING finger protein 3 (MuRF-3) and similar proteins; MuRF-3, also known as tripartite motif-containing protein 54 (TRIM54), or RING finger protein 30 (RNF30), is an E3 ubiquitin-protein ligase in ubiquitin-mediated muscle protein turnover. It is ubiquitously detected in all fibre types, is developmentally upregulated, associates with microtubules, the sarcomeric M-line and Z-line, and is required for microtubule stability and myogenesis. It associates with glutamylated microtubules during skeletal muscle development, and is required for skeletal myoblast differentiation and development of cellular microtubular networks. MuRF-3 controls the degradation of four-and-a-half LIM domain (FHL2) and gamma-filamin and is required for maintenance of ventricular integrity after myocardial infarction (MI). MuRF-3 belongs to the C-II subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain. It also harbors a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains.


Pssm-ID: 319675 [Multi-domain]  Cd Length: 59  Bit Score: 50.42  E-value: 3.21e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796541   8 LTCPICLELFEDP-LLLPCAHSLCFNCAHRILVS-----HCATNEPVESINAFQCPTCR 60
Cdd:cd16761     1 LICPICLEMFTKPvVILPCQHNLCRKCANDVFQAsnplwQSRGSSTVSSGGRFRCPSCR 59
RING-HC_RNF39 cd16592
RING finger, HC subclass, found in RING finger protein 39 (RNF39) and similar proteins; RNF39, ...
 4-63 4.81e-08

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: 49.76  E-value: 4.81e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039796541   4 LESELTCPICLELFEDPLLLPCAHSLCFNCAHRilvsHCATN-EPVESINAFQCPTCRHVI 63
Cdd:cd16592     1 LQEETTCPICLGYFKDPVILDCEHSFCRACIAR----HWGQEaMEGNGAEGVFCPQCGEPC 57
RING-HC_TRIM32_C-VII cd16587
RING finger, HC subclass, found in tripartite motif-containing protein 32 (TRIM32) and similar ...
 8-62 5.28e-08

RING finger, HC subclass, found in tripartite motif-containing protein 32 (TRIM32) and similar proteins; TRIM32, also known as 72 kDa Tat-interacting protein, zinc finger protein HT2A, or BBS11, is an E3 ubiquitin-protein ligase that promotes degradation of several targets, including actin, PIASgamma, Abl interactor 2, dysbindin, X-linked inhibitor of apoptosis (XIAP), p73 transcription factor, thin filaments and Z-bands during fasting. It plays important roles in neuronal differentiation of neural progenitor cells, as well as in controlling cell fate in skeletal muscle progenitor cells. It reduces PI3K-Akt-FoxO signaling in muscle atrophy by promoting plakoglobin-PI3K dissociation. It also functions as a pluripotency-reprogramming roadblock that facilitates cellular transition towards differentiation by modulating the levels of Oct4 and cMyc. Moreover, TRIM32 is an intrinsic influenza A virus (IAV) restriction factor which senses and targets the polymerase basic protein 1 (PB1) for ubiquitination and protein degradation. It also plays a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo, binds specifically to the activation domain of HIV-1 Tat, and can also interact with the HIV-2 and EIAV Tat proteins in vivo. Furthermore, TRIM32 regulates myoblast proliferation by controlling turnover of NDRG2 (N-myc downstream-regulated gene). It negatively regulates tumor suppressor p53 to promote tumorigenesis. It also facilitates degradation of MYCN on spindle poles and induces asymmetric cell division in human neuroblastoma cells. In addition, TRIM32 plays important roles in regulation of hyperactivities and positively regulates the development of anxiety and depression disorders induced by chronic stress. It also plays a role in regeneration by affecting satellite cell cycle progression via modulation of the SUMO ligase PIASy (PIAS4). Defects in TRIM32 leads to limb-girdle muscular dystrophy type 2H (LGMD2H), sarcotubular myopathies (STM) and Bardet-Biedl syndrome. TRIM32 belongs to the C-VII subclass of the TRIM (tripartite motif)-NHL family that is 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 a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The NHL domain mediates the interaction with Argonaute proteins and consequently allows TRIM32 to modulate the activity of certain miRNAs.


Pssm-ID: 438249 [Multi-domain]  Cd Length: 51  Bit Score: 49.71  E-value: 5.28e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796541   8 LTCPICLELFED----PLLLPCAHSLCFNCAHRILVShcatnepvESINAFQCPTCRHV 62
Cdd:cd16587     1 LECPICLESFDEgqlrPKLLHCGHTICEQCLEKLLAS--------LSINGVRCPFCRKV 51
Bbox1_TRIM9_C-I cd19843
B-box-type 1 zinc finger found in tripartite motif-containing protein 9 (TRIM9) and similar ...
 119-164 8.71e-08

B-box-type 1 zinc finger found in tripartite motif-containing protein 9 (TRIM9) and similar proteins; TRIM9 (the human ortholog of rat Spring), also termed RING finger protein 91 (RNF91), is a brain-specific E3 ubiquitin-protein ligase collaborating with an E2 ubiquitin conjugating enzyme UBCH5b. TRIM9 plays an important role in the regulation of neuronal functions and participates in neurodegenerative disorders through its ligase activity. It interacts with the WD repeat region of beta-transducer repeat-containing protein (beta-TCP) through its N-terminal degron motif depending on the phosphorylation status, and thus negatively regulate nuclear factor-kappaB (NF-kappaB) activation in the NF-kappaB pro-inflammatory signaling pathway. Moreover, TRIM9 acts as a critical catalytic link between Netrin-1 and exocytosis soluble NSF attachment receptor protein (SNARE) machinery in murine cortical neurons. It promotes SNARE-mediated vesicle fusion and axon branching in a Netrin-dependent manner. TRIM9 belongs to the C-I subclass of 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 RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, the fibronectin type III domain and the SPRY/B30.2 domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


Pssm-ID: 380901  Cd Length: 47  Bit Score: 48.84  E-value: 8.71e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1039796541 119 CQFCDQDPaQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEP 164
Cdd:cd19843     3 CQLCEKSP-KEATVMCEQCDVFYCDPCRLRCHPPRGPLAKHRLVPP 47
SPRY_PRY_TRIM21 cd12900
PRY/SPRY domain in tripartite motif-binding protein 21 (TRIM21) also known as 52kD ...
 463-618 8.77e-08

PRY/SPRY domain in tripartite motif-binding protein 21 (TRIM21) also known as 52kD Ribonucleoprotein Autoantigen (Ro52); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM21, which is also known as Sjogren Syndrome Antigen A (SSA), SSA1, 52kD Ribonucleoprotein Autoantigen (Ro52, Ro/SSA, SS-A/Ro) or RING finger protein 81 (RNF81). TRIM21 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. As an E3 ligase, TRIM21 mediates target specificity in ubiquitination; it regulates type 1 interferon and proinflammatory cytokines via ubiquitination of interferon regulatory factors (IRFs). It is up-regulated at the site of autoimmune inflammation, such as cutaneous lupus lesions, indicating a central role in the tissue destructive inflammatory process. It interacts with auto-antigens in patients with Sjogren syndrome and systemic lupus erythematosus, a chronic systemic autoimmune disease characterized by the presence of autoantibodies against the protein component of the human intracellular ribonucleoprotein-RNA complexes and more specifically TRIM21, Ro60/TROVE2 and La/SSB proteins. It binds the Fc part of IgG molecules via its PRY-SPRY domain with unexpectedly high affinity.


Pssm-ID: 293957  Cd Length: 180  Bit Score: 52.58  E-value: 8.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAgqgSYG-VAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPK-- 539
Cdd:cd12900     7 LDPDTANPWLILSKDRRQVRLGDTHQNVPENEERFD---NYPmVLGAQRFNSGKHYWEVDVTGKEAWDLGVCRDSVRRkg 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 540 HEWIGKNAASWALCRchnhWAVRHDGKETPIAPApHL----RRVGVLLDYDNGSIAFYDALSSVHL-HTF-HAALAQPVC 613
Cdd:cd12900    84 QFLLSPENGFWTIWL----WNKKYEAGTSPQTTL-HLqvppCQVGIFLDYEAGVVSFYNITDHGSLiYTFsECAFTGPLR 158


                  ....*
gi 1039796541 614 PTFTV 618
Cdd:cd12900   159 PFFNP 163
RING-HC_RFPL4B cd16623
RING finger, HC subclass, found in Ret finger protein-like 4B (RFPL4B) and similar proteins; ...
 4-62 9.18e-08

RING finger, HC subclass, found in Ret finger protein-like 4B (RFPL4B) and similar proteins; RFPL4B, also called RING finger protein 211 (RNF211), is an uncharacterized RING finger protein containing a typical C3HC4-type RING-HC finger.


Pssm-ID: 438285 [Multi-domain]  Cd Length: 63  Bit Score: 49.04  E-value: 9.18e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796541   4 LESELTCPICLELFEDPLLLPCAHSLCFNCAHRILvshcATNEPVESInafqCPTCRHV 62
Cdd:cd16623     5 LEMEATCPICLDFFSHPISLSCAHIFCFDCIQKWM----TKREDSILT----CPLCRKE 55
SPRY_PRY_TRIM10 cd15827
PRY/SPRY domain of tripartite motif-binding protein 10 (TRIM10) also known as hematopoietic ...
 463-621 1.37e-07

PRY/SPRY domain of tripartite motif-binding protein 10 (TRIM10) also known as hematopoietic RING finger 1 (HERF1); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM10, also known as RING finger protein 9 (RNF9) or hematopoietic RING finger 1 (HERF1). TRIM10 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. TRIM10/HERF1 is predominantly expressed during definitive erythropoiesis and in embryonic liver, and minimally expressed in adult liver, kidney, and colon. It is critical for erythroid cell differentiation and its down-regulation leads to cell death; inhibition of TRIM10 expression blocks terminal erythroid differentiation, while its over-expression in erythroid cells induces beta-major globin expression and erythroid differentiation.


Pssm-ID: 293999 [Multi-domain]  Cd Length: 172  Bit Score: 51.76  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFagQGSYGVAGNVFIDSGRHYWEV----VTSGSTwyAIGLA----- 533
Cdd:cd15827     6 LDPQTSHPKLLLSEDHQRARFSYKWQNSPDNPQRF--DRATCVLAHDGFTGGRHTWVVsvdlAHGGSC--TVGVVsedvr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 534 ----YRSAPKhEWIGKNAASWALCRCHNHWAVRHDGKETPiapaphlRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALA 609
Cdd:cd15827    82 rkgeLRLRPE-EGVWAVRLAWGFVSALGSFPTRLALEEQP-------RQVRVSLDYEVGWVTFVNAVTQEPIYTFTASFT 153

                         170
                  ....*....|..
gi 1039796541 610 QPVCPTFTVWNK 621
Cdd:cd15827   154 QKVFPFFGLWGR 165
Bbox1_TRIM42_C-III cd19808
B-box-type 1 zinc finger found in tripartite motif-containing protein 42 (TRIM42) and similar ...
 117-164 2.11e-07

B-box-type 1 zinc finger found in tripartite motif-containing protein 42 (TRIM42) and similar proteins; TRIM42 belongs to the C-III subclass of 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 RING finger, Bbox1 and Bbox2, and a coiled coil domain. It also has a novel cysteine-rich motif N-terminal to the RBCC domain, as well as a COS (carboxyl-terminal subgroup one signature) box and a fibronectin type-III (FN3) domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. TRIM42 can interact with TRIM27, a known cancer-associated protein. Its precise biological function remains unclear.


Pssm-ID: 380866  Cd Length: 47  Bit Score: 47.88  E-value: 2.11e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1039796541 117 VLCQFCDQDpAQDAVKTCVTCEVSYCDECLKATHPNKKpFTGHRLIEP 164
Cdd:cd19808     2 IFCQICTQK-RESAVKRCITCRLNLCNKCLRKLHGNKA-FQDHILTDP 47
RING-HC_TRIM77_C-IV cd16543
RING finger, HC subclass, found in tripartite motif-containing protein 77 (TRIM77) and similar ...
 5-33 2.24e-07

RING finger, HC subclass, found in tripartite motif-containing protein 77 (TRIM77) and similar proteins; TRIM77 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 two consecutive zinc-binding domains, a C3HC4-type RING-HC finger and Bbox2, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438205 [Multi-domain]  Cd Length: 54  Bit Score: 47.77  E-value: 2.24e-07
                          10        20
                  ....*....|....*....|....*....
gi 1039796541   5 ESELTCPICLELFEDPLLLPCAHSLCFNC 33
Cdd:cd16543     1 EDQLTCSICLDLLKDPVTIPCGHSFCMNC 29
RING-HC_RNF222 cd16564
RING finger, HC subclass, found in RING finger protein 222 (RNF222) and similar proteins; ...
 9-66 2.35e-07

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


Pssm-ID: 438226 [Multi-domain]  Cd Length: 50  Bit Score: 47.78  E-value: 2.35e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796541   9 TCPICLELFED-PLLLPCAHSLCFNCAHRILVSHcatnepvesinAFQCPTCRHVITLS 66
Cdd:cd16564     2 ECPVCYEDFDDaPRILSCGHSFCEDCLVKQLVSM-----------TISCPICRRVTFIS 49
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
342-460 3.29e-07

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 53.47  E-value: 3.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 342 TAPNPPAireELcTASYDT---ITVHWTSEDEFSVVSYELQYTIftgqanvvnvacdgtcllgsaglcNSADSWMIVPNI 418
Cdd:COG3401   231 TPPSAPT---GL-TATADTpgsVTLSWDPVTESDATGYRVYRSN------------------------SGDGPFTKVATV 282

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1039796541 419 KQNHYTVHGLQSGTKYIFTVKAINQAGSRS--SEPGKLKTNSQP 460
Cdd:COG3401   283 TTTSYTDTGLTNGTTYYYRVTAVDAAGNESapSNVVSVTTDLTP 326
RING-HC_TRIM50_like_C-IV cd16605
RING finger, HC subclass, found in tripartite motif-containing protein TRIM50, TRIM73, TRIM74 ...
 8-60 5.51e-07

RING finger, HC subclass, found in tripartite motif-containing protein TRIM50, TRIM73, TRIM74 and similar proteins; TRIM50 is a stomach-specific E3 ubiquitin-protein ligase, encoded by the Williams-Beuren syndrome (WBS) TRIM50 gene, which regulates vesicular trafficking for acid secretion in gastric parietal cells. It colocalizes, interacts with, and increases the level of p62/SQSTM1, a multifunctional adaptor protein implicated in various cellular processes including the autophagy clearance of polyubiquitinated protein aggregates. It also promotes the formation and clearance of aggresome-associated polyubiquitinated proteins through the interaction with histone deacetylase 6 (HDAC6), a tubulin specific deacetylase that regulates microtubule-dependent aggresome formation. TRIM50 can be acetylated by PCAF and p300. TRIM50 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. This subfamily also includes two paralogs of TRIM50, tripartite motif-containing protein 73 (TRIM73), also known as tripartite motif-containing protein 50B (TRIM50B), and tripartite motif-containing protein 74 (TRIM74), also known as tripartite motif-containing protein 50C (TRIM50C), both of which are WBS-related genes encoding proteins that may also act as E3 ligases. In contrast with TRIM50, TRIM73 and TRIM74 belong to the C-V subclass of TRIM family of proteins that are defined by N-terminal RBCC domains only.


Pssm-ID: 438267 [Multi-domain]  Cd Length: 45  Bit Score: 46.29  E-value: 5.51e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039796541   8 LTCPICLELFEDPLLLPCAHSLCFNCAHRILvshcatnepVESINAFQCPTCR 60
Cdd:cd16605     1 LLCPICLEVFKEPLMLQCGHSYCKSCLVSLS---------GELDGQLLCPVCR 44
RING-HC_TRIM46_C-I cd16757
RING finger, HC subclass, found in tripartite motif-containing protein 46 (TRIM46) and similar ...
 4-60 5.85e-07

RING finger, HC subclass, found in tripartite motif-containing protein 46 (TRIM46) and similar proteins; TRIM46, also known as gene Y protein (GeneY) or tripartite, fibronectin type-III and C-terminal SPRY motif protein (TRIFIC), is a microtubule-associated protein that specifically localizes to the proximal axon, partly overlaps with the axon initial segment (AIS) at later stages, and organizes uniform microtubule orientation in axons. It controls neuronal polarity and axon specification by driving the formation of parallel microtubule arrays. TRIM46 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins, which are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, a PRY domain and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438415 [Multi-domain]  Cd Length: 43  Bit Score: 46.34  E-value: 5.85e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796541   4 LESELTCPICLELFEDPLLLPCAHSLCFNCAHRILvshcatnepvesinaFQCPTCR 60
Cdd:cd16757     1 MERELLCPVCKEMYKQPLVLPCMHNVCQVCASEVL---------------FPCPPCQ 42
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 514-593 7.39e-07

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: 48.20  E-value: 7.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 514 GRHYWEV--VTSGSTWYAIGLAYRSAP--KHEWIGKNAASWAL-CRCHNHWAVRHDGKETPIAPAPHlrRVGVLLDYDNG 588
Cdd:cd11709     1 GKWYWEVrvDSGNGGLIQVGWATKSFSldGEGGVGDDEESWGYdGSRLRKGHGGSSGPGGRPWKSGD--VVGCLLDLDEG 78


                  ....*
gi 1039796541 589 SIAFY 593
Cdd:cd11709    79 TLSFS 83
Bbox_SF cd00021
B-box-type zinc finger superfamily; The B-box-type zinc finger is a short zinc binding domain ...
 118-164 7.66e-07

B-box-type zinc finger superfamily; The B-box-type zinc finger is a short zinc binding domain of around 40 amino acid residues in length. It has been found in transcription factors, ribonucleoproteins and proto-oncoproteins, such as in TRIM (tripartite motif) proteins that consist of an N-terminal RING finger (originally called an A-box), followed by 1-2 B-box domains and a coiled-coil domain (also called RBCC for Ring, B-box, Coiled-Coil). The B-box-type zinc finger often presents in combination with other motifs, like RING zinc finger, NHL motif, coiled-coil or RFP domain in functionally unrelated proteins, most likely mediating protein-protein interactions. Based on different consensus sequences and the spacing of the 7-8 zinc-binding residues, B-box-type zinc fingers can be divided into two groups, type 1 (Bbox1: C6H2) and type 2 (Bbox2: CHC3H2).


Pssm-ID: 380813 [Multi-domain]  Cd Length: 39  Bit Score: 46.05  E-value: 7.66e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1039796541 118 LCQFCDQDPAqdaVKTCVTCEVSYCDECLK-ATHPNkkpftgHRLIEP 164
Cdd:cd00021     1 MCQEHDEEKA---NKYCVTCEVLYCALCKKsGAHPD------HEVAPL 39
RING-HC_COP1 cd16504
RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and ...
 6-64 7.71e-07

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: 46.08  E-value: 7.71e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796541   6 SELTCPICLELFEDPLLLPCAHSLCFNCAHRILVshcatnepvesiNAFQCPTCRHVIT 64
Cdd:cd16504     1 NDFLCPICFDIIKEAFVTKCGHSFCYKCIVKHLE------------QKNRCPKCNFYLT 47
Bbox1_TRIM36-like cd19807
B-box-type 1 zinc finger found in tripartite motif-containing proteins, TRIM36, TRIM46 and ...
 117-151 9.06e-07

B-box-type 1 zinc finger found in tripartite motif-containing proteins, TRIM36, TRIM46 and similar proteins; The family includes tripartite motif-containing proteins, TRIM36 and TRIM46, both of which belong to the C-I subclass of 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 RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. TRIM36, the human ortholog of mouse Haprin, also known as RING finger protein 98 (RNF98) or zinc-binding protein Rbcc728, is an E3 ubiquitin-protein ligase expressed in the germ plasm. It has been implicated in acrosome reaction, fertilization, and embryogenesis, as well as in carcinogenesis. TRIM36 functions upstream of Wnt/beta-catenin activation, and plays a role in controlling the stability of proteins regulating microtubule polymerization during cortical rotation, and subsequent dorsal axis formation. It is also potentially associated with chromosome segregation by interacting with the kinetochore protein centromere protein-H (CENP-H), and colocalizing with the microtubule protein alpha-tubulin. Its overexpression may cause chromosomal instability and carcinogenesis. It is, thus, a novel regulator affecting cell cycle progression. Moreover, TRIM36 plays a critical role in the arrangement of somites during embryogenesis. TRIM46, also known as gene Y protein (GeneY) or tripartite, fibronectin type-III and C-terminal SPRY motif protein (TRIFIC), is a microtubule-associated protein that specifically localizes to the proximal axon, partly overlaps with the axon initial segment (AIS) at later stages, and organizes uniform microtubule orientation in axons. It controls neuronal polarity and axon specification by driving the formation of parallel microtubule arrays.


Pssm-ID: 380865  Cd Length: 52  Bit Score: 45.96  E-value: 9.06e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1039796541 117 VLCQFCdQDPAQDAVKTCVTCEVSYCDECLKATHP 151
Cdd:cd19807     2 IKCQLC-KPPPQEATKSCADCVASFCNECFKVVHP 35
RING-HC_RNF138 cd16544
RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; ...
 7-68 1.05e-06

RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; RNF138, also known as Nemo-like kinase-associated RING finger protein (NARF) or NLK-associated RING finger protein, is an E3 ubiquitin-protein ligase that plays an important role in glioma cell proliferation, apoptosis, and cell cycle. It specifically cooperates with the E2 conjugating enzyme E2-25K (Hip-2/UbcH1), regulates the ubiquitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF), and further suppresses Wnt-beta-catenin signaling. RNF138, together with three closely related proteins: RNF114, RNF125 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM).


Pssm-ID: 438206 [Multi-domain]  Cd Length: 53  Bit Score: 45.86  E-value: 1.05e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039796541   7 ELTCPICLELFEDPL-LLPCAHSLCFNCAHRILVShcatnepvesiNAFQCPTCRHVITLSQR 68
Cdd:cd16544     2 ELTCPVCQEVLKDPVeLPPCRHIFCKACILLALRS-----------SGARCPLCRGPVGKTER 53
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
 4-89 1.06e-06

DNA repair protein rad18; All proteins in this family for which functions are known are involved in nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273165 [Multi-domain]  Cd Length: 397  Bit Score: 51.54  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541   4 LESELTCPICLELFEDPLLLPCAHSLCFNCAHRilvshCATNEPvesinafQCPTCRHVITLSQrgldgLKRNVTLQNII 83
Cdd:TIGR00599  23 LDTSLRCHICKDFFDVPVLTSCSHTFCSLCIRR-----CLSNQP-------KCPLCRAEDQESK-----LRSNWLVSEIV 85


                  ....*.
gi 1039796541  84 DRFQKA 89
Cdd:TIGR00599  86 ESFKNL 91
RING-HC_TRIM72_C-IV cd16612
RING finger, HC subclass, found in tripartite motif-containing protein 72 (TRIM72) and similar ...
 4-60 1.45e-06

RING finger, HC subclass, found in tripartite motif-containing protein 72 (TRIM72) and similar proteins; TRIM72, also known as Mitsugumin-53 (MG53), is a muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at muscle injury sites. It is required in repair of alveolar epithelial cells under plasma membrane stress failure. It interacts with dysferlin to regulate sarcolemmal repair. Upregulation of TRIM72 develops obesity, systemic insulin resistance, dyslipidemia, and hyperglycemia, as well as induces diabetic cardiomyopathy through transcriptional activation of the peroxisome proliferation-activated receptor alpha (PPAR-alpha) signaling pathway. Compensation for the absence of AKT signaling by ERK signaling during TRIM72 overexpression leads to pathological hypertrophy. Moreover, TRIM72 functions as a novel negative feedback regulator of myogenesis by targeting insulin receptor substrate-1 (IRS-1). It is transcriptionally activated by the synergism of myogenin (MyoD) and myocyte enhancer factor 2 (MEF2). TRIM72 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: 438274 [Multi-domain]  Cd Length: 60  Bit Score: 45.88  E-value: 1.45e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796541   4 LESELTCPICLELFEDPLLLPCAHSLCFNCAHRIlvshcATNepvESINAFQCPTCR 60
Cdd:cd16612     1 MHQDLSCPLCLKLFQSPVTTECGHTFCQDCLSRV-----PKE---EDGGSTSCPTCQ 49
Bbox1_TRIM46_C-I cd19849
B-box-type 1 zinc finger found in tripartite motif-containing protein 46 (TRIM46) and similar ...
 117-164 1.77e-06

B-box-type 1 zinc finger found in tripartite motif-containing protein 46 (TRIM46) and similar proteins; TRIM46, also known as gene Y protein (GeneY) or tripartite, fibronectin type-III and C-terminal SPRY motif protein (TRIFIC), is a microtubule-associated protein that specifically localizes to the proximal axon, partly overlaps with the axon initial segment (AIS) at later stages, and organizes uniform microtubule orientation in axons. It controls neuronal polarity and axon specification by driving the formation of parallel microtubule arrays. TRIM46 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins, which are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


Pssm-ID: 380907  Cd Length: 52  Bit Score: 45.40  E-value: 1.77e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1039796541 117 VLCQFCdQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEP 164
Cdd:cd19849     2 IMCQFC-KPPQLEATKGCTECRASFCNECFKLYHPWGTQKAQHEPTPP 48
RING-HC_TRIM8_C-V cd16580
RING finger, HC subclass, found in tripartite motif-containing protein 8 (TRIM8) and similar ...
 4-62 1.86e-06

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: 45.65  E-value: 1.86e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796541   4 LESELTCPICLELFEDPLLLPCAHSLCFNCahrilVSHCATNEPVESinafQCPTCRHV 62
Cdd:cd16580     8 FEEELICPICLHVFVEPVQLPCKHNFCRGC-----IGEAWAKDAGLV----RCPECNQA 57
RING-HC_RNF168 cd16550
RING finger, HC subclass, found in RING finger protein 168 (RNF168) and similar proteins; ...
 9-60 1.94e-06

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: 45.06  E-value: 1.94e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039796541   9 TCPICLELFEDPLLLPCAHSLCFNCahrilvshcaTNEPVESINaFQCPTCR 60
Cdd:cd16550     2 LCPICLEILVEPVTLPCNHTLCMPC----------FQSTVEKAS-LCCPLCR 42
RING-HC_NHL-1-like cd16524
RING finger, HC subclass, found in Caenorhabditis elegans RING finger protein NHL-1 and ...
 4-60 2.24e-06

RING finger, HC subclass, found in Caenorhabditis elegans RING finger protein NHL-1 and similar proteins; NHL-1 functions as an E3 ubiquitin-protein ligase in the presence of both UBC-13 and UBC-1 within the ubiquitin pathway of Caenorhabditis elegans. It acts in chemosensory neurons to promote stress resistance in distal tissues by the transcription factor DAF-16 activation but is dispensable for the activation of heat shock factor 1 (HSF-1). NHL-1 belongs to the TRIM (tripartite motif)-NHL 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 NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438187 [Multi-domain]  Cd Length: 53  Bit Score: 45.11  E-value: 2.24e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796541   4 LESELTCPICLELFEDPLLLPCAHSLCFncahrilvSHCATNEPVESINAFQCPTCR 60
Cdd:cd16524     2 IEQLLTCPICLDRYRRPKLLPCQHTFCL--------SPCLEGLVDYVTRKLKCPECR 50
SPRY_PRY_TRIM17 cd15812
PRY/SPRY domain of tripartite motif-binding protein 17 (TRIM17), also known as testis RING ...
 492-616 2.26e-06

PRY/SPRY domain of tripartite motif-binding protein 17 (TRIM17), also known as testis RING finger protein (terf); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM17, also known as RING finger protein 16 (RNF16) or testis RING finger protein (terf). TRIM17 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein, expressed almost exclusively in the testis. It exhibits E3 ligase activity, causing protein degradation of ZW10 interacting protein (ZWINT), a known component of the kinetochore complex required for the mitotic spindle checkpoint, and negatively regulates proliferation of breast cancer cells. TRIM17 undergoes ubiquitination in COS7 fibroblast-like cells but is inhibited and stabilized by TRIM44.


Pssm-ID: 293984 [Multi-domain]  Cd Length: 176  Bit Score: 48.34  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 492 HAPERFAGqgsYGVA-GNVFIDSGRHYWEV--VTSGSTWYAIGLAYRSAPKHEWIGKnaaswalCRCHNHWAVRHDGKET 568
Cdd:cd15812    33 CSKDRFLA---YPCAvGQETFSSGRHYWEVgmNLTGDALWALGVCRDNVSRKDRVPK-------SPENGFWVVQLSKGKK 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796541 569 PIAPAPHLRRV---------GVLLDYDNGSIAFYDALSSVHLHTF-HAALAQPVCPTF 616
Cdd:cd15812   103 YLSAMSALTPVtlteppshmGIFLDFEAGEVSFYSVNDGSHLHTYsQAAFPGPLQPFF 160
Bbox1 cd19757
B-box-type 1 zinc finger (Bbox1); The B-box-type zinc finger is a short zinc binding domain of ...
 118-163 2.38e-06

B-box-type 1 zinc finger (Bbox1); The B-box-type zinc finger is a short zinc binding domain of around 40 amino acid residues in length. It has been found in transcription factors, ribonucleoproteins and proto-oncoproteins, such as in TRIM (tripartite motif) proteins that consist of an N-terminal RING finger (originally called an A-box), followed by 1-2 B-box domains and a coiled-coil domain (also called RBCC for Ring, B-box, Coiled-Coil). The B-box-type zinc finger often presents in combination with other motifs, like RING zinc finger, NHL motif, coiled-coil or RFP domain, in functionally unrelated proteins, most likely mediating protein-protein interactions. Based on different consensus sequences and the spacing of the 7-8 zinc-binding residues, the B-box-type zinc fingers can be divided into two groups, type 1 (Bbox1: C6H2) and type 2 (Bbox2: CHC3H2). This family corresponds to the type 1 B-box (Bbox1).


Pssm-ID: 380815 [Multi-domain]  Cd Length: 44  Bit Score: 44.79  E-value: 2.38e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1039796541 118 LCQFCDQDPAqdaVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIE 163
Cdd:cd19757     1 LCDECEEREA---TVYCLECEEFLCDDCSDAIHRRGKLTRSHKLVP 43
RING-HC_TRIM5-like_C-IV cd16591
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, ...
 4-84 2.60e-06

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, TRIM34 and similar proteins; TRIM5, TRIM6, TRIM22, and TRIM34, four closely related tripartite motif-containing proteins, belong 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. TRIM5, also known as RING finger protein 88 (RNF88), is a capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses in a species-specific manner by binding to and destabilizing the retroviral capsid lattice before reverse transcription is completed. Its retroviral restriction activity correlates with the ability to activate TAK1-dependent innate immune signaling. TRIM5 also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Moreover, TRIM5 plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. It also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction. TRIM6, also known as RING finger protein 89 (RNF89), is an E3-ubiquitin ligase that cooperates with the E2-ubiquitin conjugase UbE2K to catalyze the synthesis of unanchored K48-linked polyubiquitin chains, and further stimulates the interferon-I kappa B kinase epsilon (IKKepsilon) kinase-mediated antiviral response. It also regulates the transcriptional activity of Myc during the maintenance of embryonic stem (ES) cell pluripotency, and may act as a novel regulator for Myc-mediated transcription in ES cells. TRIM22, also known as 50 kDa-stimulated trans-acting factor (Staf-50) or RING finger protein 94 (RNF94), is an E3 ubiquitin-protein ligase that plays an integral role in the host innate immune response to viruses. It has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 acts as a suppressor of basal HIV-1 long terminal repeat (LTR)-driven transcription by preventing the transcription factor specificity protein 1 (Sp1) binding to the HIV-1 promoter. It also controls FoxO4 activity and cell survival by directing Toll-like receptor 3 (TLR3)-stimulated cells toward type I interferon (IFN) type I gene induction or apoptosis. Moreover, TRIM22 can activate the noncanonical nuclear factor-kappaB (NF-kappaB) pathway by activating I kappa B kinase alpha (IKKalpha). It also regulates nucleotide binding oligomerization domain containing 2 (NOD2)-dependent activation of interferon-beta signaling and nuclear factor-kappaB. TRIM34, also known as interferon-responsive finger protein 1 or RING finger protein 21 (RNF21), may function as antiviral protein that contribute to the defense against retroviral infections.


Pssm-ID: 438253 [Multi-domain]  Cd Length: 72  Bit Score: 45.51  E-value: 2.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541   4 LESELTCPICLELFEDPLLLPCAHSLCFNCahrILVSHcatNEPVESINAFQCPTCRhvitlSQRGLDGLKRNVTLQNII 83
Cdd:cd16591     3 IKEEVTCPICLELLTEPLSLDCGHSFCQAC---ITANH---KESVNQEGESSCPVCR-----TSYQPENLRPNRHLANIV 71


                  .
gi 1039796541  84 D 84
Cdd:cd16591    72 E 72
RING-HC_TRIM26_C-IV cd16598
RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar ...
 4-60 2.63e-06

RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar proteins; TRIM26, also known as acid finger protein (AFP), RING finger protein 95 (RNF95), or zinc finger protein 173 (ZNF173), is an E3 ubiquitin-protein ligase that negatively regulates interferon-beta production and antiviral response through polyubiquitination and degradation of nuclear transcription factor IRF3. It functions as an important regulator for RNA virus-triggered innate immune response by bridging TBK1 to NEMO (NF-kappaB essential modulator, also known as IKKgamma) and mediating TBK1 activation. It also acts as a novel tumor suppressor of hepatocellular carcinoma by regulating cancer cell proliferation, colony forming ability, migration, and invasion. TRIM26 belongs 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, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438260 [Multi-domain]  Cd Length: 64  Bit Score: 45.15  E-value: 2.63e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796541   4 LESELTCPICLELFEDPLLLPCAHSLCFNCahriLVSHCATNEPVEsinAFQCPTCR 60
Cdd:cd16598     1 LEEEVTCSICLDYLRDPVTIDCGHNFCRSC----ITDYCPISGGHE---RPVCPLCR 50
RING-HC_TRIM47-like_C-IV cd16604
RING finger, HC subclass, found in tripartite motif-containing protein 47 (TRIM47) and similar ...
 8-60 2.79e-06

RING finger, HC subclass, found in tripartite motif-containing protein 47 (TRIM47) and similar proteins; TRIM47, also known as gene overexpressed in astrocytoma protein (GOA) or RING finger protein 100 (RNF100), 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, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. It plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis. This subfamily also includes RING finger protein 135 (RNF135). RNF135, also known as RIG-I E3 ubiquitin ligase (REUL) or Riplet, is a widely expressed E3 ubiquitin-protein ligase that consists of an N-terminal C3HC4-type RING-HC finger and C-terminal B30.2/SPRY and PRY motifs, but lacks the B-box and coiled-coil domains that are also typically present in TRIM proteins. RNF135 serves as a specific retinoic acid-inducible gene-I (RIG-I)-interacting protein that ubiquitinates RIG-I and specifically stimulates RIG-I-mediated innate antiviral activity to produce antiviral type-I interferon (IFN) during the early phase of viral infection. It also has been identified as a bio-marker and therapy target of glioblastoma. It associates with the ERK signal transduction pathway and plays a role in glioblastoma cell proliferation, migration and cell cycle.


Pssm-ID: 438266 [Multi-domain]  Cd Length: 49  Bit Score: 44.72  E-value: 2.79e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039796541   8 LTCPICLELFEDPLLLPCAHSLCfncahrilvSHCATNE-PVESINAFQCPTCR 60
Cdd:cd16604     1 LSCPICLDLLKDPVTLPCGHSFC---------MGCLGALwGAGRGGRASCPLCR 45
fn3 pfam00041
Fibronectin type III domain;
359-445 3.75e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.48  E-value: 3.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 359 DTITVHWTSEDEFS--VVSYELQYtiftgqanvvnVACDGtcllgsaglcNSADSWMIVPNIkQNHYTVHGLQSGTKYIF 436
Cdd:pfam00041  14 TSLTVSWTPPPDGNgpITGYEVEY-----------RPKNS----------GEPWNEITVPGT-TTSVTLTGLKPGTEYEV 71


                  ....*....
gi 1039796541 437 TVKAINQAG 445
Cdd:pfam00041  72 RVQAVNGGG 80
RING-HC_TRIM69_C-IV cd16611
RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar ...
 4-33 3.76e-06

RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar proteins; TRIM69, also known as RFP-like domain-containing protein trimless or RING finger protein 36 (RNF36), is a testis E3 ubiquitin-protein ligase that plays a specific role in apoptosis and may also play an important role in germ cell homeostasis during spermatogenesis. TRIM69 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: 438273 [Multi-domain]  Cd Length: 59  Bit Score: 44.36  E-value: 3.76e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 1039796541   4 LESELTCPICLELFEDPLLLPCAHSLCFNC 33
Cdd:cd16611     1 LTEELHCPLCLDFFRDPVMLSCGHNFCQSC 30
RING-HC_PRT1-like cd23132
RING finger, HC subclass, found in Arabidopsis thaliana proteolysis 1 protein (PRT1) and ...
 7-42 4.20e-06

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


Pssm-ID: 438494 [Multi-domain]  Cd Length: 52  Bit Score: 44.33  E-value: 4.20e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1039796541   7 ELTCPICLELFEDPLLLPCAHSLCFNCAHRIL----VSHC 42
Cdd:cd23132     2 EFLCCICLDLLYKPVVLECGHVFCFWCVHRCMngydESHC 41
RING-HC_TRIM17_C-IV cd16595
RING finger, HC subclass, found in tripartite motif-containing protein TRIM17 and similar ...
 4-62 4.27e-06

RING finger, HC subclass, found in tripartite motif-containing protein TRIM17 and similar proteins; TRIM17, also known as RING finger protein 16 (RNF16) or testis RING finger protein (Terf), is a crucial E3 ubiquitin ligase that is necessary and sufficient for neuronal apoptosis and contributes to Mcl-1 ubiquitination in cerebellar granule neurons (CGNs). It interacts in a SUMO-dependent manner with nuclear factor of activated T cell NFATc3 transcription factor, and thus inhibits the activity of NFATc3 by preventing its nuclear localization. In contrast, it binds to and inhibits NFATc4 transcription factor in a SUMO-independent manner. Moreover, TRIM17 stimulates degradation of kinetochore protein ZW10 interacting protein (ZWINT), a known component of the kinetochore complex required for the mitotic spindle checkpoint, and negatively regulates cell proliferation. TRIM17 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: 438257 [Multi-domain]  Cd Length: 70  Bit Score: 44.60  E-value: 4.27e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796541   4 LESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATNEPVESINAFQCPTCRHV 62
Cdd:cd16595     2 LQEEATCSICLDYFTDPVMTTCGHNFCRACIQLSWEKARGKKGRRKQKGSFPCPECREM 60
RING-HC_TRIM62_C-IV cd16608
RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar ...
 4-62 4.56e-06

RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar proteins; TRIM62, also known as Ductal Epithelium Associated Ring Chromosome 1 (DEAR1), is a cytoplasmic E3 ubiquitin-protein ligase that was identified as a dominant regulator of acinar morphogenesis in the mammary gland. It is implicated in the inflammatory response of immune cells by regulating the Toll-like receptor 4 (TLR4) signaling pathway, leading to increased activity of the activator protein 1 (AP-1) transcription factor in primary macrophages. It is also involved in muscular protein homeostasis, especially during inflammation-induced atrophy, and may play a role in the pathogenesis of ICU-acquired weakness (ICUAW) by activating and maintaining inflammation in myocytes. Moreover, TRIM62 facilitates K27-linked poly-ubiquitination of CARD9 and also regulates CARD9-mediated anti-fungal immunity and intestinal inflammation. It also functions as a chromosome 1p35 tumor suppressor and negatively regulates transforming growth factor beta (TGFbeta)-driven epithelial-mesenchymal transition (EMT) by binding to and promoting the ubiquitination of SMAD3, a major effector of TGFbeta-mediated EMT. TRIM62 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: 438270 [Multi-domain]  Cd Length: 52  Bit Score: 44.03  E-value: 4.56e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796541   4 LESELTCPICLELFEDPLLLPCAHSLCFNCahriLVSHCATNEpvesinAFQCPTCRHV 62
Cdd:cd16608     3 LKDELLCSICLSIYQDPVSLGCEHYFCRQC----ITEHWSRSE------HRDCPECRRT 51
RING-HC_TRIM35_C-IV cd16599
RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar ...
 4-83 6.60e-06

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: 43.99  E-value: 6.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541   4 LESELTCPICLELFEDPLLLPCAHSLCFNCahrilVSHCATNEPVESinafqCPTCRHVITlsqrgLDGLKRNVTLQNII 83
Cdd:cd16599     1 FKEELLCPICYEPFREAVTLRCGHNFCKGC-----VSRSWERQPRAP-----CPVCKEASS-----SDDLRTNHTLNNLV 65
RING-HC_AtBARD1-like cd23146
RING finger, HC subclass, found in Arabidopsis thaliana BRCA1-associated RING domain protein 1 ...
 4-35 6.62e-06

RING finger, HC subclass, found in Arabidopsis thaliana BRCA1-associated RING domain protein 1 (AtBARD1) and similar proteins; AtBARD1, also called protein REPRESSOR OF WUSCHEL 1, binds specifically to H3K4me3 regions of target gene (e.g. WUS and WOX5) promoters to repress their transcription via chromatin remodeling. It is required for the shoot apical meristem (SAM) organization and maintenance, by confining WUS expression to the organizing center, and for the quiescent center (QC) development in the root apical meristem (RAM), by repressing WOX5 expression in the root proximal meristem. AtBARD1 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). AtBARD1 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438508 [Multi-domain]  Cd Length: 54  Bit Score: 43.61  E-value: 6.62e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1039796541   4 LESELTCPICLELFEDPLLLPCAHSLCFNCAH 35
Cdd:cd23146     1 MELELKCPICLKLLNRPVLLPCDHIFCSSCIT 32
RING-HC_LONFs_rpt2 cd16514
second RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger ...
 7-63 8.08e-06

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: 43.02  E-value: 8.08e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796541   7 ELTCPICLELFEDPLLLPCAHSLCFNCAHRilvshCATNEPvesinafQCPTCRHVI 63
Cdd:cd16514     1 DLECSLCLRLLYEPVTTPCGHTFCRACLER-----CLDHSP-------KCPLCRTSL 45
PLN03208 PLN03208
E3 ubiquitin-protein ligase RMA2; Provisional
 7-98 1.17e-05

E3 ubiquitin-protein ligase RMA2; Provisional


Pssm-ID: 178747 [Multi-domain]  Cd Length: 193  Bit Score: 46.62  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541   7 ELTCPICLELFEDPLLLPCAHSLCFNCAHRILVshcATNEPVESINAF-------QCPTCRHVITlsqrgldglkrNVTL 79
Cdd:PLN03208   18 DFDCNICLDQVRDPVVTLCGHLFCWPCIHKWTY---ASNNSRQRVDQYdhkreppKCPVCKSDVS-----------EATL 83

                          90
                  ....*....|....*....
gi 1039796541  80 QNIIDRFQKASVSGPNSPS 98
Cdd:PLN03208   84 VPIYGRGQKAPQSGSNVPS 102
RING-HC_PML_C-V cd16579
RING finger, HC subclass, found in promyelocytic leukemia protein (PML) and similar proteins; ...
 8-60 1.28e-05

RING finger, HC subclass, found in promyelocytic leukemia protein (PML) and similar proteins; Protein PML, also known as RING finger protein 71 (RNF71) or tripartite motif-containing protein 19 (TRIM19), is predominantly a nuclear protein with a broad intrinsic antiviral activity. It is the eponymous component of PML nuclear bodies (PML NBs) and has been implicated in a wide variety of cell processes, including DNA damage signaling, apoptosis, and transcription. PML interferes with the replication of many unrelated viruses, including human immunodeficiency virus 1 (HIV-1), human foamy virus (HFV), poliovirus, influenza virus, rabies virus, EMCV, adeno-associated virus (AAV), and vesicular stomatitis virus (VSV). It also selectively interacts with misfolded proteins through distinct substrate recognition sites and conjugates these proteins with the small ubiquitin-like modifiers (SUMOs) through its SUMO ligase activity. PML 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: 438241 [Multi-domain]  Cd Length: 52  Bit Score: 42.93  E-value: 1.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039796541   8 LTCPICLELFEDPLLLPCAHSLCFNCAHrilvshcATNEPVESINAFQCPTCR 60
Cdd:cd16579     5 LRCPGCKAEYKCPKLLPCLHTVCSGCLE-------ALAEQASETTEFQCPICK 50
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 10-59 1.30e-05

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


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 42.50  E-value: 1.30e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039796541   10 CPICLELF-EDPLLLPCAHSLCFNCAHRILVSHCATnepvesinafqCPTC 59
Cdd:smart00184   1 CPICLEEYlKDPVILPCGHTFCRSCIRKWLESGNNT-----------CPIC 40
RING-HC_RNF169 cd16551
RING finger, HC subclass, found in RING finger protein 169 (RNF169) and similar proteins; ...
 7-60 1.59e-05

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: 42.53  E-value: 1.59e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039796541   7 ELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCAtnepvesinAFQCPTCR 60
Cdd:cd16551     1 ELTCAGCLEVPVEPATLPCGHTLCRGCANRALDAAEA---------GPTCPRCR 45
RING-HC_TRIM58_C-IV cd16606
RING finger, HC subclass, found in tripartite motif-containing protein TRIM58 and similar ...
 7-60 1.66e-05

RING finger, HC subclass, found in tripartite motif-containing protein TRIM58 and similar proteins; TRIM58, also known as protein BIA2, is an erythroid E3 ubiquitin-protein ligase induced during late erythropoiesis. It binds and ubiquitinates the intermediate chain of the microtubule motor dynein (DYNC1LI1/DYNC1LI2), stimulating the degradation of the dynein holoprotein complex. It may participate in the erythroblast enucleation process through regulation of nuclear polarization. TRIM58 belongs to the C-IV subclass of 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: 438268 [Multi-domain]  Cd Length: 53  Bit Score: 42.54  E-value: 1.66e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039796541   7 ELTCPICLELFEDPLLLPCAHSLCFNCahriLVSHCATNEPVESiNAFQCPTCR 60
Cdd:cd16606     2 EARCPVCLDFLQEPVSVDCGHSFCLRC----ISEFCEKSDSAQG-GVYACPQCR 50
RING-HC_TRIM31_C-V cd16582
RING finger, HC subclass, found in tripartite motif-containing protein 31 (TRIM31) and similar ...
 7-59 1.68e-05

RING finger, HC subclass, found in tripartite motif-containing protein 31 (TRIM31) and similar proteins; TRIM31 is an E3 ubiquitin-protein ligase that primarily localizes to the cytoplasm, but is also associated with the mitochondria. It can negatively regulate cell proliferation and may be a potential biomarker of gastric cancer as it is overexpressed from the early stage of gastric carcinogenesis. TRIM31 is downregulated in non-small cell lung cancer and serves as a potential tumor suppressor. It interacts with p52 (Shc) and inhibits Src-induced anchorage-independent growth. TRIM31 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: 438244 [Multi-domain]  Cd Length: 44  Bit Score: 42.12  E-value: 1.68e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039796541   7 ELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATnepvesinaFQCPTC 59
Cdd:cd16582     1 EVICPICLDILQKPVTIDCGHNFCLQCITQIGETSCGF---------FKCPLC 44
RING-HC_MmTRIM43-like cd23133
RING finger, HC subclass, found in Mus musculus tripartite motif-containing protein 43 (TRIM43) ...
 5-64 1.74e-05

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


Pssm-ID: 438495 [Multi-domain]  Cd Length: 57  Bit Score: 42.59  E-value: 1.74e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541   5 ESELTCPICLELFEDPLLLPCAHSLCFNCahrILVSHCATNEPVesinafQCPTCRHVIT 64
Cdd:cd23133     1 EETLTCSICQGIFMNPVYLRCGHKFCEAC---LLLFQEDIKFPA------YCPMCRQPFN 51
RING-HC_TRIM45_C-VII cd16588
RING finger, HC subclass, found in tripartite motif-containing protein 45 (TRIM45) and similar ...
 10-59 2.09e-05

RING finger, HC subclass, found in tripartite motif-containing protein 45 (TRIM45) and similar proteins; TRIM45, also known as RING finger protein 99 (RNF99), is a novel receptor for activated C-kinase (RACK1)-interacting protein that suppresses transcriptional activities of Elk-1 and AP-1 and downregulates mitogen-activated protein kinase (MAPK) signal transduction through inhibiting RACK1/PKC (protein kinase C) complex formation. It also negatively regulates tumor necrosis factor alpha (TNFalpha)-induced nuclear factor-kappaB (NF-kappa B)-mediated transcription and suppresses cell proliferation. TRIM45 belongs to the C-VII subclass of the TRIM (tripartite motif) family that is 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 filamin-type immunoglobulin (IG-FLMN) domain and NHL repeats positioned C-terminal to the RBCC domain.


Pssm-ID: 438250 [Multi-domain]  Cd Length: 59  Bit Score: 42.51  E-value: 2.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039796541  10 CPICLELFEDPLLLPCAHSLCFNCAHRIL-VSHCATNEPVESIN---AFQCPTC 59
Cdd:cd16588     3 CPVCGKLFQEPRLLPCLHTLCSPCLRQLEpFSVCGLRGGDRSEKsnySVLCPVC 56
SPRY_Fbox cd12907
SPRY domain in the F-box family Fbxo45; Fbxo45 is a novel synaptic E3 and ubiquitin ligase, ...
 500-592 2.26e-05

SPRY domain in the F-box family Fbxo45; Fbxo45 is a novel synaptic E3 and ubiquitin ligase, related to the suppressor of cytokine signaling (SOCS) proteins and located N-terminal to a SPRY (SPla and the ryanodine receptor) domain. Fbxo45 induces the degradation of a synaptic vesicle-priming factor, Munc13-1, via the SPRY domain, thus playing an important role in the regulation of neurotransmission by modulating Munc13-1 at the synapse. F-box motifs are found in proteins that function as the substrate recognition component of SCF E3 complexes.


Pssm-ID: 293964  Cd Length: 175  Bit Score: 45.46  E-value: 2.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 500 QGSYGVAGNVFIDSGRHYWEVVTSG--STWYAIGLAYRSAPKH-----EWIGKNAASWALCRCHNHwaVRHDGKetPIAP 572
Cdd:cd12907    28 QSTDGARGKIGFSSGRHAWEVWWEGplGTVAVVGIATKHAPLQcqgyvALLGSDDQSWGWNLVDNH--LLHNGD--SQGN 103

                          90       100
                  ....*....|....*....|....*....
gi 1039796541 573 APHL---------RRVGVLLDYDNGSIAF 592
Cdd:cd12907   104 YPQCnnapkyqvgERIRVILDCEDNTLAF 132
RING-HC_RNF114 cd16540
RING finger, HC subclass, found in RING finger protein 114 (RNF114) and similar proteins; ...
 8-38 2.69e-05

RING finger, HC subclass, found in RING finger protein 114 (RNF114) and similar proteins; RNF114, also known as zinc finger protein 228 (ZNF228) or zinc finger protein 313 (ZNF313), is a p21(WAF1)-targeting ubiquitin E3 ligase that interacts with X-linked inhibitor of apoptosis (XIAP)-associated factor 1 (XAF1) and may play a role in p53-mediated cell-fate decisions. It is involved in the immune response to double-stranded RNA in disease pathogenesis. Moreover, RNF114 interacts with A20 and modulates its ubiquitylation. It negatively regulates nuclear factor-kappaB (NF-kappaB)-dependent transcription and positively regulates T-cell activation. RNF114 may play a putative role in the regulation of immune responses, since it corresponds to a novel psoriasis susceptibility gene, ZNF313. RNF114, together with three closely related proteins: RNF125, RNF138 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM).


Pssm-ID: 438202 [Multi-domain]  Cd Length: 46  Bit Score: 41.67  E-value: 2.69e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1039796541   8 LTCPICLELFEDPLLLPCAHSLCFNCAHRIL 38
Cdd:cd16540     2 FTCPVCLEIFETPVRVPCGHVFCNACLQECL 32
zf-RING_UBOX pfam13445
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.
 10-57 2.72e-05

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: 41.62  E-value: 2.72e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1039796541  10 CPICLELFEDPlLLPCAHSLCFNCAHRILVShcatnepveSINAFQCP 57
Cdd:pfam13445   1 CPICLELFTDP-VLPCGHTFCRECLEEMSQK---------KGGKFKCP 38
Bbox1_TRIM25-like_C-IV cd19842
B-box-type 1 zinc finger found in tripartite motif-containing proteins, TRIM25, TRIM47 and ...
 118-167 2.74e-05

B-box-type 1 zinc finger found in tripartite motif-containing proteins, TRIM25, TRIM47 and similar proteins; The family includes tripartite motif-containing proteins, TRIM25 and TRIM47, both of which belong to the C-IV subclass of 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 RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. TRIM25, also termed estrogen-responsive finger protein (EFP), or ubiquitin/ISG15-conjugating enzyme TRIM25, or zinc finger protein 147 (ZNF147), or E3 ubiquitin/ISG15 ligase TRIM25, is induced by estrogen and is particularly abundant in placenta and uterus. It has been implicated in cell proliferation, protein modification, and the retinoic acid inducible gene I (RIG-I)-mediated antiviral signaling pathway. It functions as an E3-ubiquitin ligase able to transfer ubiquitin and ISG15 to target proteins. TRIM47, also known as gene overexpressed in astrocytoma protein (GOA) or RING finger protein 100 (RNF100), plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis.


Pssm-ID: 380900  Cd Length: 49  Bit Score: 41.69  E-value: 2.74e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039796541 118 LCQFCdQDPAQDAVKTCVTCEVSYCDECLKAtHPNKKPFTGHRLIEPIPD 167
Cdd:cd19842     1 LCDLC-LGRELAAAKTCLTCLASFCPEHLEP-HLSSPAFRSHRLCPPERD 48
SPRY_PRY_TRIM6 cd15823
PRY/SPRY domain in tripartite motif-binding protein 6 (TRIM6), also known as RING finger ...
 463-626 2.79e-05

PRY/SPRY domain in tripartite motif-binding protein 6 (TRIM6), also known as RING finger protein 89 (RNF89); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM6, also known as RING finger protein 89 (RNF89). TRIM6 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. It is selectively expressed in embryonic stem (ES) cells and interacts with the proto-oncogene product Myc, maintaining the pluripotency of the ES cells. TRIM6, together with E2 Ubiquitin conjugase (UbE2K) and K48-linked poly-Ub chains, is critical for the IkappaB kinase epsilon (IKKepsilon) branch of type I interferon (IFN-I) signaling pathway and subsequent establishment of a protective antiviral response.


Pssm-ID: 293995  Cd Length: 188  Bit Score: 45.24  E-value: 2.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVErdeSSSKKSHAPERFAGQGSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRS-----A 537
Cdd:cd15823     7 LNPHTANLNLVLSKNRRQVR---FVGAKLSGPSYLEEHYDCSVLGSQHFSSGKHYWEVDVTKKTAWILGVCSHSlgptfS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 538 PKHEWIGKNAAS--------WALCRCHNHWAVRHDGKETP----IAPAPhlRRVGVLLDYDNGSIAFYDALS-SVHLHTF 604
Cdd:cd15823    84 FNQYAQNHNAYSryqpqsgyWVIGLQHNHEYRAYEDSSTSlllsMTVPP--RRVGVFLDYEAGTVSFYNVTNhGFPIYTF 161

                         170       180
                  ....*....|....*....|...
gi 1039796541 605 HA-ALAQPVCPTFtvwNKCLTIV 626
Cdd:cd15823   162 SKyYFPTTLCPYF---NPCNCVV 181
RING-HC_BAH1-like cd23127
RING finger, HC subclass, found in Arabidopsis thaliana protein BENZOIC ACID HYPERSENSITIVE 1 ...
 4-60 2.93e-05

RING finger, HC subclass, found in Arabidopsis thaliana protein BENZOIC ACID HYPERSENSITIVE 1 (BAH1) and similar proteins; This subfamily includes Arabidopsis thaliana BAH1 and BAH1-like. BAH1, also known as protein NITROGEN LIMITATION ADAPTATION (NLA), or RING-type E3 ubiquitin transferase BAH1, acts as an E3 ubiquitin-protein ligase that mediates E2-dependent protein ubiquitination. It plays a role in salicylic acid-mediated negative feedback regulation of salicylic acid (SA) accumulation. It may be involved in the overall regulation of SA, benzoic acid and phenylpropanoid biosynthesis. It controls the adaptability to nitrogen limitation by channeling the phenylpropanoid metabolic flux to the induced anthocyanin synthesis. BAH1-like, also known as RING finger protein 178, or RING-type E3 ubiquitin transferase BAH1-like, is a probable E3 ubiquitin-protein ligase. Members of this subfamily contain a typical C3HC4-type RING-HC finger.


Pssm-ID: 438489 [Multi-domain]  Cd Length: 74  Bit Score: 42.39  E-value: 2.93e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796541   4 LESELTCPICLELFEDPLLLPCAHSLCFNCAhrilvshCATnepvESINAFQ----------CPTCR 60
Cdd:cd23127     5 LEFDLTCSICLDTVFDPVALGCGHLFCNSCA-------CSA----ASVLIFQglkaappeakCPLCR 60
Bbox1_TRIM16 cd19839
B-box-type 1 zinc finger found in tripartite motif-containing protein 16 (TRIM16) and similar ...
 117-164 3.00e-05

B-box-type 1 zinc finger found in tripartite motif-containing protein 16 (TRIM16) and similar proteins; TRIM16, also termed estrogen-responsive B box protein (EBBP), is a regulator that may play a role in the regulation of keratinocyte differentiation. It may also act as a tumor suppressor by affecting cell proliferation and migration or tumorigenicity in carcinogenesis. TRIM16 belongs to an unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers and thus lack the characteristic tripartite (RING (R), B-box, and coiled coil (CC)) RBCC motif. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


Pssm-ID: 380897  Cd Length: 46  Bit Score: 41.75  E-value: 3.00e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1039796541 117 VLCQFCdQDPAQDAVKTCVTCEVSYCDECLKATHPNKKpFTGHRLIEP 164
Cdd:cd19839     1 VLCDFC-LEAKVKAVKSCLTCMVSYCEGHLRPHLENSK-LQAHQLCDP 46
RING-HC_TRIM38_C-IV cd16600
RING finger, HC subclass, found in tripartite motif-containing protein 38 (TRIM38) and similar ...
 7-60 3.91e-05

RING finger, HC subclass, found in tripartite motif-containing protein 38 (TRIM38) and similar proteins; TRIM38, also known as RING finger protein 15 (RNF15) or zinc finger protein RoRet, is an E3 ubiquitin-protein ligase that promotes K63- and K48-linked ubiquitination of cellular proteins and also catalyzes self-ubiquitination. It negatively regulates Tumor necrosis factor alpha (TNF-alpha)- and interleukin-1beta-triggered Nuclear factor-kappaB (NF-kappaB) activation by mediating lysosomal-dependent degradation of transforming growth factor beta (TGFbeta)-activated kinase 1 (TAK1)-binding protein (TAB)2/3, two critical components of the TAK1 kinase complex. It also inhibits TLR3/4-mediated activation of NF-kappaB and interferon regulatory factor 3 (IRF3) by mediating ubiquitin-proteasomal degradation of TNF receptor-associated factor 6 (Traf6) and NAK-associated protein 1 (Nap1), respectively. Moreover, TRIM38 negatively regulates TLR3-mediated interferon beta (IFN-beta) signaling by targeting ubiquitin-proteasomal degradation of TIR domain-containing adaptor inducing IFN-beta (TRIF). It functions as a valid target for autoantibodies in primary Sjogren's Syndrome. TRIM38 belongs 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, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438262 [Multi-domain]  Cd Length: 58  Bit Score: 41.68  E-value: 3.91e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039796541   7 ELTCPICLELFEDPLLLPCAHSLCFNCAHRILvshCATNEPVESINAFQCPTCR 60
Cdd:cd16600     5 EATCSICLQLMTEPVSINCGHSYCKRCIVSFL---ENQSQLEPGLETFSCPQCR 55
zf-RING_2 pfam13639
Ring finger domain;
9-60 4.08e-05

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 41.24  E-value: 4.08e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039796541   9 TCPICLELFEDP---LLLPCAHSLCFNCAHRILVSHCatnepvesinafQCPTCR 60
Cdd:pfam13639   2 ECPICLEEFEEGdkvVVLPCGHHFHRECLDKWLRSSN------------TCPLCR 44
RING-HC_RNF183-like cd16556
RING finger, HC subclass, found in RING finger protein RNF183, RNF223, RNF225 and similar ...
 10-65 4.72e-05

RING finger, HC subclass, found in RING finger protein RNF183, RNF223, RNF225 and similar proteins; RNF183 is an E3 ubiquitin-protein ligase that is upregulated during intestinal inflammation and is negatively regulated by miR-7. It promotes intestinal inflammation by increasing the ubiquitination and degradation of inhibitor of kappa B, thereby resulting in secondary activation of the Nuclear factor-kappaB (NF-kB) pathway. The interaction between RNF183-mediated ubiquitination and miRNA may be an important novel epigenetic mechanism in the pathogenesis of inflammatory bowel disease (IBD). The biological function of RNF223 and RNF225 remains unclear. Members of this family contain an N-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438218 [Multi-domain]  Cd Length: 57  Bit Score: 41.20  E-value: 4.72e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039796541  10 CPICLE----LFEDPLLLPCAHSLCFNCAHRI-LVSHcatnepvESINAFQCPTCRHVITL 65
Cdd:cd16556     3 CSICFSsydnTFKTPKLLDCGHTFCLECLARLsLASP-------PQAERVPCPLCRQPTVL 56
RING-HC_BRCA1 cd16498
RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and ...
 8-87 4.89e-05

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: 42.28  E-value: 4.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541   8 LTCPICLELFEDPLLLPCAHSLCFNCAHRILVShcatnepveSINAFQCPTCRHVITlsQRGL---DGLKRNVT-LQNII 83
Cdd:cd16498    17 LECPICLELLKEPVSTKCDHQFCRFCILKLLQK---------KKKPAPCPLCKKSVT--KRSLqesTRFKQLVEaVKKLI 85


                  ....
gi 1039796541  84 DRFQ 87
Cdd:cd16498    86 DAFE 89
RING-HC_ScPSH1-like cd16568
RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated ...
 4-64 5.07e-05

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: 41.20  E-value: 5.07e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039796541   4 LESELTCPICLELFEDPLLLPCAHSLCFNCahrilvshcaTNEPVESINAFQCPTCRHVIT 64
Cdd:cd16568     1 ILETQECIICHEYLYEPMVTTCGHTYCYTC----------LNTWFKSNRSLSCPDCRTKIT 51
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
6-64 5.36e-05

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 40.82  E-value: 5.36e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541   6 SELTCPICLELFEDPLLLPCAH-SLCFNCAHRILVSHCatnepvesinafQCPTCRHVIT 64
Cdd:pfam13920   1 EDLLCVICLDRPRNVVLLPCGHlCLCEECAERLLRKKK------------KCPICRQPIE 48
Bbox1_TRIM29 cd19840
B-box-type 1 zinc finger found in tripartite motif-containing protein 29 (TRIM29) and similar ...
 117-165 5.36e-05

B-box-type 1 zinc finger found in tripartite motif-containing protein 29 (TRIM29) and similar proteins; TRIM29, also termed ataxia telangiectasia group D-associated protein (ATDC), plays a crucial role in the regulation of macrophage activation in response to viral or bacterial infections within the respiratory tract. TRIM29 belongs to an unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers and thus lack the characteristic tripartite (RING (R), B-box, and coiled coil (CC)) RBCC motif. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


Pssm-ID: 380898  Cd Length: 47  Bit Score: 41.06  E-value: 5.36e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1039796541 117 VLCQFCDQDPAQdAVKTCVTCEVSYCDECLKAtHPNKKPFTGHRLIEPI 165
Cdd:cd19840     1 VLCDSCIDNKQK-AVKSCLVCQASFCELHLKP-HLEGAAFRDHQLLEPI 47
zf-C3HC4_4 pfam15227
zinc finger of C3HC4-type, RING; This is a family of primate-specific Ret finger protein-like ...
 10-33 5.83e-05

zinc finger of C3HC4-type, RING; This is a family of primate-specific Ret finger protein-like (RFPL) zinc-fingers of the C3HC4 type. Ret finger protein-like proteins are primate-specific target genes of Pax6, a key transcription factor for pancreas, eye and neocortex development. This domain is likely to be DNA-binding. This zinc-finger domain together with the RDM domain, pfam11002, forms a large zinc-finger structure of the RING/U-Box superfamily. RING-containing proteins are known to exert an E3 ubiquitin protein ligase activity with the zinc-finger structure being mandatory for binding to the E2 ubiquitin-conjugating enzyme.


Pssm-ID: 464570 [Multi-domain]  Cd Length: 42  Bit Score: 40.50  E-value: 5.83e-05
                          10        20
                  ....*....|....*....|....
gi 1039796541  10 CPICLELFEDPLLLPCAHSLCFNC 33
Cdd:pfam15227   1 CPICLDYLEKPVSIECGHSFCLSC 24
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
 10-59 6.97e-05

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: 40.42  E-value: 6.97e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039796541  10 CPICLELFEDPL-LLPCAHSLCFNCAHRILvshcatnepveSINAFQCPTC 59
Cdd:pfam00097   1 CPICLEEPKDPVtLLPCGHLFCSKCIRSWL-----------ESGNVTCPLC 40
RING-HC_EHV1-like cd23130
RING finger, HC subclass, found in Equid alphaherpesvirus 1 (Equine herpesvirus 1/EHV-1) ...
 10-64 7.13e-05

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: 40.80  E-value: 7.13e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796541  10 CPICLE-LFEDPLLLPCAHSLCFNCAHRILvshcatnepveSINAfQCPTCRHVIT 64
Cdd:cd23130     3 CPICLDdPEDEAITLPCLHQFCYTCILRWL-----------QTSP-TCPLCKTPVT 46
RING-HC_RNF180 cd16554
RING finger, HC subclass, found in RING finger protein 180 (RNF180) and similar proteins; ...
 6-64 8.60e-05

RING finger, HC subclass, found in RING finger protein 180 (RNF180) and similar proteins; RNF180, also known as Rines, is a membrane-bound E3 ubiquitin-protein ligase well conserved among vertebrates. It is a critical regulator of the monoaminergic system, as well as emotional and social behavior. It interacts with brain monoamine oxidase A (MAO-A) and targets it for ubiquitination and degradation. It also functions as a novel tumor suppressor in gastric carcinogenesis. The hypermethylated CpG site count of the RNF180 DNA promoter can be used to predict survival of gastric cancer. RNF180 contains a novel conserved dual specificity protein phosphatase Rines conserved (DSPRC) domain, a basic coiled-coil domain, a C3HC4-type RING-HC finger, and a C-terminal hydrophobic region that is predicted to be a transmembrane domain.


Pssm-ID: 438216 [Multi-domain]  Cd Length: 59  Bit Score: 40.76  E-value: 8.60e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541   6 SELTCPICLELFEDPL-LLPCAHSLCFNCAHRILVSHCaTNEPvesinafqCPTCRHVIT 64
Cdd:cd16554     1 ESLTCPVCLDLYYDPYmCYPCGHIFCEPCLRQLAKSSP-KNTP--------CPLCRTTIR 51
RING-HC_RNF8 cd16535
RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is ...
 7-85 9.68e-05

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: 40.84  E-value: 9.68e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796541   7 ELTCPICLELFEDPLLLPCAHSLCfncahrilvSHCATNEPVESInafQCPTCRHVITlSQrgldglKRNVTLQNIIDR 85
Cdd:cd16535     1 ELQCSICSELFIEAVTLNCSHSFC---------SYCITEWMKRKK---ECPICRKPIT-SK------TRSLVLDNCIDK 60
RING-HC_MEX3B cd16721
RING finger, HC subclass, found in RNA-binding protein MEX3B; MEX3B, also known as RING finger ...
 10-68 9.78e-05

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


Pssm-ID: 438381 [Multi-domain]  Cd Length: 58  Bit Score: 40.43  E-value: 9.78e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541  10 CPICLELFEDPLLLPCAHSL-CFNCAHRIlvshCATNEPvesinafQCPTCRHVITLSQR 68
Cdd:cd16721     7 CSICFESEVIAALVPCGHNLfCMECANRI----CEKNEP-------QCPVCHAAVTQAIR 55
RING-HC_TRIM41-like_C-IV cd16602
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and ...
 5-60 1.17e-04

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and similar proteins; TRIM41 and TRIM52, two closely related tripartite motif-containing proteins, have dramatically expanded RING domains compared with the rest of the TRIM family proteins. TRIM41 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. In contrast, TRIM52 lacks the putative viral recognition SPRY/B30.2 domain, and thus has been classified to the C-V subclass of the TRIM family that contains only RBCC domains. TRIM41, also known as RING finger-interacting protein with C kinase (RINCK), is an E3 ubiquitin-protein ligase that promotes the ubiquitination of protein kinase C (PKC) isozymes in cells. It specifically recognizes the C1 domain of PKC isozymes. It controls the amplitude of PKC signaling by controlling the amount of PKC in the cell. TRIM52, also known as RING finger protein 102 (RNF102), is encoded by a novel, noncanonical antiviral TRIM52 gene in primate genomes with unique specificity determined by the rapidly evolving RING domain.


Pssm-ID: 438264 [Multi-domain]  Cd Length: 53  Bit Score: 40.29  E-value: 1.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796541   5 ESELTCPICLELFEDPLLLPCAHSLCFNCahrilvshcatnepVESINAFQCPTCR 60
Cdd:cd16602     1 QEEAVCAICLDYFKDPVSIGCGHNFCRVC--------------VTQLWGFTCPQCR 42
vRING-HC-C4C4_RBBP6 cd16620
Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) ...
 6-63 1.18e-04

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


Pssm-ID: 438282 [Multi-domain]  Cd Length: 55  Bit Score: 40.08  E-value: 1.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796541   6 SELTCPICLELFEDPLLLPCahslCFNcahrILVSHCATNEPVESinAFQCPTCRHVI 63
Cdd:cd16620     2 DELKCPICKDLMKDAVLTPC----CGN----SFCDECIRTALLEE--DFTCPTCKEPD 49
SPRY_SOCS_Fbox cd12875
SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins; This family ...
 464-592 1.25e-04

SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins; This family consists of the SPRY domain-containing SOCS box protein family (SPSB1-4, also known as SSB-1 to -4) as well as F-box protein 45 (Fbxo45), a novel synaptic E3 and ubiquitin ligase. The SPSB protein is composed of a central SPRY protein interaction domain and a C-terminal SOCS box. SPSB1, SPSB2, and SPSB4 interact with prostate apoptosis response protein 4 (Par-4) and are negative regulators that recruit the ECS E3 ubiquitin ligase complex to polyubiquitinate inducible nitric-oxide synthase (iNOS), resulting in its proteasomal degradation. Fbxo45 is related to this family; it is located N-terminal to the SPRY domain, and known to induce the degradation of a synaptic vesicle-priming factor, Munc13-1, via the SPRY domain, thus playing an important role in the regulation of neurotransmission by modulating Munc13-1 at the synapse. 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: 293935  Cd Length: 169  Bit Score: 43.21  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 464 DPKSAHRKLKVSHDNLTVERdessskkshapeRFAGQGSYGVAGNVFIDSGRHYWEV---VTSGSTWYAIGLAYRSAPKH 540
Cdd:cd12875     4 NPADCSKNIYIKEDGLTFHR------------RPVAQSTDAIRGKKGYTRGLHAWEVkwiSRPRGSHAVVGVATKDAPLQ 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039796541 541 -----EWIGKNAASWALCRCHNHwaVRHDGKET-PIAPAPHLR-----RVGVLLDYDNGSIAF 592
Cdd:cd12875    72 cdgyvTLLGSNSESWGWDLGDNK--LYHNGKKViGSYPAKSENyqvpdRILVILDMEDGTLAF 132
RING-HC_TRIM2 cd16767
RING finger, HC subclass, found in tripartite motif-containing protein 2 (TRIM2); TRIM2, also ...
 8-61 1.48e-04

RING finger, HC subclass, found in tripartite motif-containing protein 2 (TRIM2); TRIM2, also known as RING finger protein 86 (RNF86), is an E3 ubiquitin-protein ligase that ubiquitinates the neurofilament light chain, a component of the intermediate filament in axons. Loss of function of TRIM2 results in early-onset axonal neuropathy. TRIM2 also plays a role in mediating the p42/p44 MAPK-dependent ubiquitination of the cell death-promoting protein Bcl-2-interacting mediator of cell death (Bim) in rapid ischemic tolerance. TRIM2 belongs to the C-VII subclass of the TRIM (tripartite motif)-NHL family that is 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 a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438423 [Multi-domain]  Cd Length: 51  Bit Score: 40.00  E-value: 1.48e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039796541   8 LTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATnepvesinaFQCPTCRH 61
Cdd:cd16767     7 LICSICLDRYKNPKVLPCLHTFCERCLQNYIPAHSLT---------LSCPVCRQ 51
SPRY_PRY_TRIM47 cd15808
PRY/SPRY domain in tripartite motif-containing protein 47 (TRIM47), also known as RING finger ...
 505-593 1.51e-04

PRY/SPRY domain in tripartite motif-containing protein 47 (TRIM47), also known as RING finger protein 100 (RNF100) or Gene overexpressed in astrocytoma protein (GOA); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM47, also known as GOA (Gene overexpressed in astrocytoma protein) or RNF100 (RING finger protein 100). TRIM47 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It is highly expressed in kidney tubular cells, but lowly expressed in most tissue. It is overexpressed in astrocytoma tumor cells and plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis; astrocytoma, also known as cerebral astrocytoma, is a malignant glioma that arises from astrocytes. Genome wide studies on white matter lesions have identified a novel locus on chromosome 17q25 harboring several genes such as TRIM47 and TRIM65 which pinpoints to possible novel mechanisms leading to these lesions.


Pssm-ID: 293980  Cd Length: 206  Bit Score: 43.33  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 505 VAGNVFIDSGRHYWEV-VTSGstWYAIG-LAYRSAPKHEW----IGKNAASWALCRCHNHWAVRHDGKETPIaPAPHLRR 578
Cdd:cd15808    51 VLGEGALDRGTYYWEVeIIEG--WVSVGvMAEDFSPREPYdrgrLGRNAHSCCLQWNGRNFSVWFHGLEAPL-PHPFSPT 127

                          90
                  ....*....|....*
gi 1039796541 579 VGVLLDYDNGSIAFY 593
Cdd:cd15808   128 VGVCLEYADRALAFY 142
SPRY_PRY_TRIM46 cd12895
PRY/SPRY domain in tripartite motif-containing protein 46 (TRIM46); This domain, consisting of ...
 505-616 1.68e-04

PRY/SPRY domain in tripartite motif-containing protein 46 (TRIM46); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM46 proteins (composed of RING/B-box/coiled-coil core and also known as RBCC proteins). The SPRY/PRY combination is a possible component of immune defense. This protein family has not yet been characterized.


Pssm-ID: 293952  Cd Length: 209  Bit Score: 43.31  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 505 VAGNVFIDSGRHYWEV-VTSGSTWYAIGLAYRS-------------APKHE----------------------WIGKNAA 548
Cdd:cd12895    50 VVGDVAITQGRSYWACsVDPGSYLVKVGVGLESklqewfqlpqdvvSPRYDpdsghdsgaedatvesppfaflTMGMGKI 129

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796541 549 SWALCRCHNHWAVRHDGKET----PIAPaphlrRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQPVCPTF 616
Cdd:cd12895   130 YLPSSVSSGHGLTGRDGPPAgctvPLPP-----RLGICLDYEKGRVSFYDAVSFRPLWECPVDCSGPVCPAF 196
RING-HC_TRIM68_C-IV cd16610
RING finger, HC subclass, found in tripartite motif-containing protein 68 (TRIM68) and similar ...
 7-60 1.95e-04

RING finger, HC subclass, found in tripartite motif-containing protein 68 (TRIM68) and similar proteins; TRIM68, also known as RING finger protein 137 (RNF137) or SSA protein SS-56 (SS-56), is an E3 ubiquitin-protein ligase that negatively regulates Toll-like receptor (TLR)- and RIG-I-like receptor (RLR)-driven type I interferon production by degrading TRK fused gene (TFG), a novel driver of IFN-beta downstream of anti-viral detection systems. It also functions as a cofactor for androgen receptor-mediated transcription by regulating ligand-dependent transcription of androgen receptor in prostate cancer cells. Moreover, TRIM68 is a cellular target of autoantibody responses in Sjogre's syndrome (SS), as well as systemic lupus erythematosus (SLE). It is also an auto-antigen for T cells in SS and SLE. TRIM68 belongs 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, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438272 [Multi-domain]  Cd Length: 49  Bit Score: 39.49  E-value: 1.95e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039796541   7 ELTCPICLELFEDPLLLPCAHSLCFNCAHRILvshcatNEPVESIN-AFQCPTCR 60
Cdd:cd16610     1 EVACPICMTFLREPVSIDCGHSFCHSCLSGLW------EVPGESQNwGYTCPLCR 49
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
342-451 2.04e-04

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 44.61  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 342 TAPNPPAIREELcTASYDT---ITVHWTSEDEFSVVSYELQYTIFTGQANVVnvacdgtcllgsaglcnsadswmIVPNI 418
Cdd:COG3401   322 TDLTPPAAPSGL-TATAVGsssITLSWTASSDADVTGYNVYRSTSGGGTYTK-----------------------IAETV 377

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1039796541 419 KQNHYTVHGLQSGTKYIFTVKAINQAG--SRSSEP 451
Cdd:COG3401   378 TTTSYTDTGLTPGTTYYYKVTAVDAAGneSAPSEE 412
RING-HC_TRIM43-like_C-IV cd16603
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM43, TRIM48, TRIM49, ...
 5-60 2.17e-04

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM43, TRIM48, TRIM49, TRIM51, TRIM64 and similar proteins; The family includes a group of closely related uncharacterized tripartite motif-containing proteins, TRIM43, TRIM43B, TRIM48/RNF101, TRIM49/RNF18, TRIM49B, TRIM49C/TRIM49L2, TRIM49D/TRIM49L, TRIM51/SPRYD5, TRIM64, TRIM64B, and TRIM64C, whose biological function remain unclear. TRIM49, also known as testis-specific RING-finger protein, has moderate similarity with SS-A/Ro52 antigen, suggesting it may be one of the target proteins of autoantibodies in the sera of patients with these autoimmune disorders. All family members belong 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 as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. In RBCC region, they all have a C3HC4-type RING-HC finger.


Pssm-ID: 438265 [Multi-domain]  Cd Length: 59  Bit Score: 39.39  E-value: 2.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796541   5 ESELTCPICLELFEDPLLLPCAHSLCFNCAhrilvshCATNEPVESInaFQCPTCR 60
Cdd:cd16603     2 QRELTCPICMNYFIDPVTIDCGHSFCRPCL-------YLNWQDIPFL--AQCPECR 48
RING-HC_TRIM21_C-IV cd16596
RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar ...
 1-90 2.28e-04

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


Pssm-ID: 438258 [Multi-domain]  Cd Length: 77  Bit Score: 40.27  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541   1 METLESELTCPICLELFEDPLLLPCAHSLCFNCAHRilvshcatnepVESINAFQCPTCRHVITLSQrgldgLKRNVTLQ 80
Cdd:cd16596     3 LTMMWEEVTCPICLDPFVEPVSIECGHSFCQECISQ-----------VGKGGGSVCPVCRQRFLLKN-----LRPNRQLA 66

                          90
                  ....*....|
gi 1039796541  81 NIIDRFQKAS 90
Cdd:cd16596    67 NMVNNLKEIS 76
RING-HC_HLTF cd16509
RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar ...
 10-67 2.45e-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: 39.21  E-value: 2.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796541  10 CPICLELFEDPLLLPCAHSLCFNCAHRILvshcatnepvESINAfQCPTCRHVITLSQ 67
Cdd:cd16509     6 CAICLDSLTNPVITPCAHVFCRRCICEVI----------QREKA-KCPMCRAPLSASD 52
RING-HC_RAD18 cd16529
RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; ...
 4-67 2.51e-04

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: 39.21  E-value: 2.51e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039796541   4 LESELTCPICLELFE-DPLLLPCAHSLCFNCAHRILvshcaTNEPvesinafQCPTCRHVITLSQ 67
Cdd:cd16529     1 LDDLLRCPICFEYFNtAMMITQCSHNYCSLCIRRFL-----SYKT-------QCPTCRAAVTESD 53
RING-HC_AtRMA-like cd16745
RING finger, HC subclass, found in Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) ...
 10-60 2.83e-04

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


Pssm-ID: 438403 [Multi-domain]  Cd Length: 45  Bit Score: 39.00  E-value: 2.83e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039796541  10 CPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATNEpvesinafqCPTCR 60
Cdd:cd16745     3 CNICLDLAQDPVVTLCGHLFCWPCLHKWLRRQSSQPE---------CPVCK 44
PRY smart00589
associated with SPRY domains;
460-497 3.27e-04

associated with SPRY domains;


Pssm-ID: 128857  Cd Length: 52  Bit Score: 38.71  E-value: 3.27e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1039796541  460 PFRLDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERF 497
Cdd:smart00589   3 DVTLDPDTAHPYLLLSEDRRSVRYGDLKQSLPDNPERF 40
zf-C3HC4_2 pfam13923
Zinc finger, C3HC4 type (RING finger);
10-59 3.37e-04

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 404756 [Multi-domain]  Cd Length: 40  Bit Score: 38.57  E-value: 3.37e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039796541  10 CPICLELFEDPLLL-PCAHSLCFNCAHRILVSHCatnepvesinafQCPTC 59
Cdd:pfam13923   2 CPICMDMLKDPSTTtPCGHVFCQDCILRALRAGN------------ECPLC 40
mRING-HC-C3HC3D_arc-1-like cd23124
Modified RING finger, HC subclass (C3HC3D-type), found in Caenorhabditis elegans putative ...
 7-62 3.68e-04

Modified RING finger, HC subclass (C3HC3D-type), found in Caenorhabditis elegans putative GTP-binding protein trim-23 homolog (arc-1) and similar proteins; arc-1, also called RING-type E3 ubiquitin transferase arc-1, is an E3 ubiquitin-protein ligase that mediates E2-dependent protein ubiquitination. arc-1 contains a modified C3HC3D-type RING-HC finger.


Pssm-ID: 438486 [Multi-domain]  Cd Length: 55  Bit Score: 38.63  E-value: 3.68e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039796541   7 ELTCPICLELF--EDPLLLP-----CAHSLCFNCAHRILvshcatnepVESINAFQCPTCRHV 62
Cdd:cd23124     1 ELECGICQQEYsaDDPLLIPrilteCGHTICTNCAGTIL---------GQSSGSIFCPFDRIV 54
RING-HC_TRIM2_like_C-VII cd16586
RING finger, HC subclass, found in tripartite motif-containing protein TRIM2, TRIM3, and ...
 8-60 3.74e-04

RING finger, HC subclass, found in tripartite motif-containing protein TRIM2, TRIM3, and similar proteins; TRIM2, also known as RING finger protein 86 (RNF86), is an E3 ubiquitin-protein ligase that ubiquitinates the neurofilament light chain, a component of the intermediate filament in axons. Loss of function of TRIM2 results in early-onset axonal neuropathy. TRIM3, also known as brain-expressed RING finger protein (BERP), RING finger protein 97 (RNF97), or RING finger protein 22 (RNF22), is an E3 ubiquitin-protein ligase involved in the pathogenesis of various cancers. It also plays an important role in the central nervous system (CNS). In addition, TRIM3 may be involved in vesicular trafficking via its association with the cytoskeleton-associated-recycling or transport (CART) complex that is necessary for efficient transferrin receptor recycling, but not for epidermal growth factor receptor (EGFR) degradation. Both TRIM2 and TRIM3 belong to the C-VII subclass of the TRIM (tripartite motif)-NHL family that is 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 a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438248 [Multi-domain]  Cd Length: 45  Bit Score: 38.59  E-value: 3.74e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039796541   8 LTCPICLELFEDPLLLPCAHSLCFNCAHRILvshcatnePVESInAFQCPTCR 60
Cdd:cd16586     2 LSCGICLERYKNPKVLPCLHTFCERCLQNYI--------PAESL-SLSCPVCR 45
RING-HC_TRIM60-like_C-IV cd16607
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM60, TRIM61, TRIM75 ...
 7-61 3.94e-04

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM60, TRIM61, TRIM75 and similar proteins; TRIM60, also known as RING finger protein 129 (RNF129) or RING finger protein 33 (RNF33), is a cytoplasmic protein expressed in the testis. It may play an important role in the spermatogenesis process, the development of the preimplantation embryo, and in testicular functions. RNF33 interacts with the cytoplasmic kinesin motor proteins KIF3A and KIF3B suggesting possible contribution to cargo movement along the microtubule in the expressed sites. It is also involved in spermatogenesis in Sertoli cells under the regulation of nuclear factor-kappaB (NF-kappaB). TRIM75 mainly localizes within spindles, suggesting it may function in spindle organization and thereby affect meiosis. Both TRIM60 and TRIM75 belong 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, a B2-box, and two coiled coil domains, as well as a PRY domain and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. In contrast, TRIM61 belongs to the C-V subclass of the TRIM family that contains RBCC domains only. Its biological function remains unclear.


Pssm-ID: 438269 [Multi-domain]  Cd Length: 48  Bit Score: 38.56  E-value: 3.94e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039796541   7 ELTCPICLELFEDPLLLPCAHSLCFNCahrILVSHCATNEpvesinAFQCPTCRH 61
Cdd:cd16607     1 EASCPICLDYLKDPVTINCGHNFCRSC---ISMSWKDLQD------TFPCPVCRF 46
RING-HC_LONFs_rpt1 cd16513
first RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger ...
 7-42 4.87e-04

first 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 first RING-HC finger.


Pssm-ID: 438176 [Multi-domain]  Cd Length: 47  Bit Score: 38.06  E-value: 4.87e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1039796541   7 ELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHC 42
Cdd:cd16513     2 LLSCPLCRGLLFEPVTLPCGHTFCKRCLERDPSSRC 37
RING-HC_TRIM39_C-IV cd16601
RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar ...
 7-36 5.29e-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: 37.85  E-value: 5.29e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1039796541   7 ELTCPICLELFEDPLLLPCAHSLCFNCAHR 36
Cdd:cd16601     1 EASCSLCKEYLKDPVIIECGHNFCRACITR 30
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 176-309 7.38e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.65  E-value: 7.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541  176 LEHEDEKQNLESNLTNLIKRNTELETLLAKLIQtcQHVEVNASRQEAKLTEECDLLIEIIQQrRQIIGTKIKEGKVIRLR 255
Cdd:TIGR00618  249 REAQEEQLKKQQLLKQLRARIEELRAQEAVLEE--TQERINRARKAAPLAAHIKAVTQIEQQ-AQRIHTELQSKMRSRAK 325

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039796541  256 KLAQQIANCKQCLERSASLISQAEHSLKENDHARFLQTAKNITERVSMATASSQ 309
Cdd:TIGR00618  326 LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ 379
RING-HC_TRIM3 cd16768
RING finger, HC subclass, found in tripartite motif-containing protein 3 (TRIM3); TRIM3, also ...
 8-60 7.68e-04

RING finger, HC subclass, found in tripartite motif-containing protein 3 (TRIM3); TRIM3, also known as brain-expressed RING finger protein (BERP), RING finger protein 97 (RNF97), or RING finger protein 22 (RNF22), is an E3 ubiquitin-protein ligase involved in the pathogenesis of various cancers. It functions as a tumor suppressor that regulates asymmetric cell division in glioblastoma. It binds to the cdk inhibitor p21(WAF1/CIP1) and regulates its availability that promotes cyclin D1-cdk4 nuclear accumulation. Moreover, TRIM3 plays an important role in the central nervous system (CNS). It is encoded by the gene BERP (brain-expressed RING finger protein), a unique p53-regulated gene that modulates seizure susceptibility and GABAAR cell surface expression. Furthermore, TRIM3 mediates activity-dependent turnover of postsynaptic density (PSD) scaffold proteins GKAP/SAPAP1 and is a negative regulator of dendritic spine morphology. In addition, TRIM3 may be involved in vesicular trafficking via its association with the cytoskeleton-associated-recycling or transport (CART) complex that is necessary for efficient transferrin receptor recycling, but not for epidermal growth factor receptor (EGFR) degradation. It also regulates the motility of the kinesin superfamily protein KIF21B. TRIM3 belongs to the C-VII subclass of the TRIM (tripartite motif)-NHL family that is 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 a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438424 [Multi-domain]  Cd Length: 48  Bit Score: 37.67  E-value: 7.68e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039796541   8 LTCPICLELFEDPLLLPCAHSLCFNCAHRILvshcatnePVESInAFQCPTCR 60
Cdd:cd16768     5 LVCSICLDRYHNPKVLPCLHTFCERCLQNYI--------PPQSL-TLSCPVCR 48
PRY pfam13765
SPRY-associated domain; PRY is a 50-60 amino acids domain associated with SPRY domains, ...
 463-497 8.13e-04

SPRY-associated domain; PRY is a 50-60 amino acids domain associated with SPRY domains, adjacent to its N-terminal. PRY and SPRY domains are structurally very similar and consist of a beta sandwich fold. Distant homologs are domains in butyrophilin/marenostrin/pyrin, evolutionarily more ancient than SPRY/B30.2 counterpart.


Pssm-ID: 463976  Cd Length: 49  Bit Score: 37.46  E-value: 8.13e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1039796541 463 LDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERF 497
Cdd:pfam13765   3 LDPNTAHPSLVLSEDLKSVRYGDERQNVPDNPERF 37
RING-HC_TRIM56_C-V cd16584
RING finger, HC subclass, found in tripartite motif-containing protein 56 (TRIM56) and similar ...
 8-73 8.31e-04

RING finger, HC subclass, found in tripartite motif-containing protein 56 (TRIM56) and similar proteins; TRIM56, also known as RING finger protein 109 (RNF109), is a virus-inducible E3 ubiquitin ligase that restricts pestivirus infection. It positively regulates the Toll-like receptor 3 (TLR3) antiviral signaling pathway, and possesses antiviral activity against bovine viral diarrhea virus (BVDV), a ruminant pestivirus classified within the family Flaviviridae shared by tick-borne encephalitis virus (TBEV). It also possesses antiviral activity against two classical flaviviruses, yellow fever virus (YFV) and dengue virus (DENV), as well as a human coronavirus, HCoV-OC43, which is responsible for a significant share of common cold cases. It may not act on positive-strand RNA viruses indiscriminately. Moreover, TRIM56 is an interferon-inducible E3 ubiquitin ligase that modulates STING to confer double-stranded DNA-mediated innate immune responses. TRIM56 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: 438246 [Multi-domain]  Cd Length: 56  Bit Score: 38.04  E-value: 8.31e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796541   8 LTCPICLELFEDPLLLPCAHSLCFNCAhRILVSHcatnepvesiNAFQCPTCRHVITLSQRGLDGL 73
Cdd:cd16584     2 LACKICLEQLRAPKTLPCLHTYCQDCL-AQLADG----------GRVRCPECRETVPVPPEGVASF 56
RING-HC_AtBRCA1-like cd23147
RING finger, HC subclass, found in Arabidopsis thaliana protein BREAST CANCER SUSCEPTIBILITY 1 ...
 7-33 1.16e-03

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: 37.45  E-value: 1.16e-03
                          10        20
                  ....*....|....*....|....*..
gi 1039796541   7 ELTCPICLELFEDPLLLPCAHSLCFNC 33
Cdd:cd23147     4 ELKCPICLSLFKSAANLSCNHCFCAGC 30
RING-HC_RNF213 cd16561
RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; ...
 10-60 1.30e-03

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


Pssm-ID: 438223 [Multi-domain]  Cd Length: 50  Bit Score: 37.26  E-value: 1.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039796541  10 CPICLELFEDPLLLPCAHSLCFNCAHRILVSHCatnepvesinafQCPTCR 60
Cdd:cd16561     5 CSICLEDLNDPVKLPCDHVFCEECIRQWLPGQM------------SCPLCR 43
RING-HC_ORTHRUS_rpt1 cd23138
first RING finger, HC subclass, found in Arabidopsis thaliana ORTHRUS and similar proteins; ...
 6-63 1.33e-03

first RING finger, HC subclass, found in Arabidopsis thaliana ORTHRUS and similar proteins; This subfamily includes Arabidopsis thaliana ORTHRUS 1-5. They are E3 ubiquitin-protein ligases that may participate in CpG methylation-dependent transcriptional regulation and/or epigenetic transcriptional silencing. ORTHRUS 1 mediates ubiquitination with the E2 ubiquitin-conjugating enzymes UBC11, UBC8 and UBC8 homologs (e.g. UBC10, UBC11, UBC28 and UBC29) but not with UBC27, UBC30, UBC32, UBC34 and UBC36. ORTHRUS 2 and 5 mediate ubiquitination with the E2 ubiquitin-conjugating enzyme UBC11. ORTHRUS 1 and 2 promote methylation-mediated gene silencing leading, for example, to early flowering. They can bind to CpG, CpNpG, and CpNpN DNA motifs, with a strong preference for methylated forms, and with highest affinity for CpG substrates. Members of this subfamily contain two typical C3HC4-type RING-HC fingers. This model corresponds to the first one.


Pssm-ID: 438500 [Multi-domain]  Cd Length: 48  Bit Score: 37.04  E-value: 1.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796541   6 SELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATnepvesinafqCPTCRHVI 63
Cdd:cd23138     1 DELNCSFCMQLPERPVTTPCGHNFCLKCFQKWMGQGKKT-----------CGTCRSPI 47
mRING-HC-C3HC3D_LNX2 cd16780
Modified RING finger, HC subclass (C3HC3D-type), found in ligand of numb protein X 2 (LNX2); ...
 5-41 1.34e-03

Modified RING finger, HC subclass (C3HC3D-type), found in ligand of numb protein X 2 (LNX2); LNX2, also known as numb-binding protein 2, or PDZ domain-containing RING finger protein 1 (PDZRN1), is a PDZ domain-containing RING-type E3 ubiquitin ligase responsible for the ubiquitination and degradation of Numb, a component of the Notch signaling pathway that functions in the specification of cell fates during development and is known to control cell numbers during neurogenesis in vertebrates. It interacts with contactin-associated protein 4 (Caspr4, also known as CNTNAP4) in a PDZ domain-dependent manner, which modulates the proliferation and neuronal differentiation of neural progenitor cells (NPCs). LNX2 contains an N-terminal modified C3HC3D-type RING-HC finger, a NPAF motif for Numb/ Numblike-LNX interaction, and four PDZ domains necessary for the binding of substrates, including ErbB2, RhoC, the presynaptic protein CAST, the melanoma/cancer-testis antigen MAGEB18 and several proteins associated with cell junctions, such as JAM4 and the Coxsackievirus and adenovirus receptor (CAR).


Pssm-ID: 319694 [Multi-domain]  Cd Length: 45  Bit Score: 36.78  E-value: 1.34e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1039796541   5 ESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSH 41
Cdd:cd16780     1 DDDLVCHICLQPLLQPLDTPCGHTFCFKCLRNFLQEK 37
RAD18 COG5432
RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];
4-60 2.46e-03

RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];


Pssm-ID: 227719 [Multi-domain]  Cd Length: 391  Bit Score: 40.84  E-value: 2.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796541   4 LESELTCPICLELFEDPLLLPCAHSLCFNCAHRILvshcaTNEPVesinafqCPTCR 60
Cdd:COG5432    22 LDSMLRCRICDCRISIPCETTCGHTFCSLCIRRHL-----GTQPF-------CPVCR 66
RING-HC_Topors cd16574
RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein ...
 9-36 2.80e-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: 36.11  E-value: 2.80e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1039796541   9 TCPICLELFEDPL--LLPCAHSLCFNCAHR 36
Cdd:cd16574     3 SCPICLDRFENEKafLDGCFHAFCFTCILE 32
RING-HC_RNF5-like cd16534
RING finger, HC subclass, found in RING finger protein RNF5, RNF185 and similar proteins; RNF5 ...
 10-60 3.47e-03

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


Pssm-ID: 438196 [Multi-domain]  Cd Length: 44  Bit Score: 35.74  E-value: 3.47e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039796541  10 CPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATNepvesinafQCPTCR 60
Cdd:cd16534     3 CNICLDTASDPVVTMCGHLFCWPCLYQWLETRPDRQ---------TCPVCK 44
mRING-HC-C3HC3D_LNX1-like cd16637
Modified RING finger, HC subclass (C3HC3D-type), found in ligand of Numb protein LNX1, LNX2, ...
 7-35 3.63e-03

Modified RING finger, HC subclass (C3HC3D-type), found in ligand of Numb protein LNX1, LNX2, and similar proteins; The ligand of Numb protein X (LNX) family, also known as PDZ and RING (PDZRN) family, includes LNX1-5, which can interact with Numb, a key regulator of neurogenesis and neuronal differentiation. LNX5 (also known as PDZK4 or PDZRN4L) shows high sequence homology to LNX3 and LNX4, but it lacks the RING domain. LNX1-4 proteins function as E3 ubiquitin ligases and have a unique domain architecture consisting of an N-terminal RING-HC finger for E3 ubiquitin ligase activity and either two or four PDZ domains necessary for substrate-binding. LNX1/LNX2-like proteins contain a modified C3HC3D-type RING-HC finger and four PDZ domains. This model corresponds to the RING finger.


Pssm-ID: 438299 [Multi-domain]  Cd Length: 42  Bit Score: 35.45  E-value: 3.63e-03
                          10        20
                  ....*....|....*....|....*....
gi 1039796541   7 ELTCPICLELFEDPLLLPCAHSLCFNCAH 35
Cdd:cd16637     1 DLTCHICLQPLVEPLDTPCGHTFCYKCLT 29
SPRY_SOCS3 cd12876
SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY ...
 500-593 3.95e-03

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


Pssm-ID: 293936  Cd Length: 185  Bit Score: 38.68  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796541 500 QGSYGVAGNVFIDSGRHYWEV-VTS---GsTWYAIGLAYRSAPKHEW-------IGKNAASWALcrCHN--HWavrHDGK 566
Cdd:cd12876    30 CGTAAVRGTKPLTNGQHYWEIkMSSpvyG-TDMMVGVGTKKADLHAYryefcslLGEDEESWGL--SYKglLW---HDGQ 103

                          90       100
                  ....*....|....*....|....*....
gi 1039796541 567 ETPIA-PAPHLRR-VGVLLDYDNGSIAFY 593
Cdd:cd12876   104 SRPYTsPFGNQGTiIGVHLDMWRGTLTFY 132
BBOX smart00336
B-Box-type zinc finger;
114-152 4.01e-03

B-Box-type zinc finger;


Pssm-ID: 197662 [Multi-domain]  Cd Length: 42  Bit Score: 35.39  E-value: 4.01e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1039796541  114 AEKVLCQFCDQdpaQDAVKTCVTCEVSYCDECLKATHPN 152
Cdd:smart00336   1 QRAPKCDSHGD---EPAEFFCEECGALLCRTCDEAEHRG 36
RING-HC_SH3RF2 cd16749
RING finger, HC subclass, found in SH3 domain-containing RING finger protein 2 (SH3RF2) and ...
 8-60 4.44e-03

RING finger, HC subclass, found in SH3 domain-containing RING finger protein 2 (SH3RF2) and similar proteins; SH3RF2, also known as heart protein phosphatase 1-binding protein (HEPP1), plenty of SH3s (POSH)-eliminating RING protein (POSHER), protein phosphatase 1 regulatory subunit 39, or RING finger protein 158 (RNF158), is a putative E3 ubiquitin-protein ligase that acts as an anti-apoptotic regulator for the c-Jun N-terminal kinase (JNK) pathway by binding to and promoting the proteasomal degradation of SH3RF1 (or POSH), a scaffold protein that is required for pro-apoptotic JNK activation. It may also play a role in cardiac functions together with protein phosphatase 1. SH3RF2 contains an N-terminal C3HC4-type RING-HC finger responsible for the E3 ligase activity and four Src Homology 3 (SH3) domains, which are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs.


Pssm-ID: 438407 [Multi-domain]  Cd Length: 46  Bit Score: 35.68  E-value: 4.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039796541   8 LTCPICLELFE-DPLLLPCAHSLCFNCAHRILVSHcatnepvesiNAFQCPTCR 60
Cdd:cd16749     1 LECPVCFEKLDvTAKVLPCQHTFCKPCLQRIFKAR----------KELRCPECR 44
RING-HC_RNF146 cd16546
RING finger, HC subclass, found in RING finger protein 146 (RNF146) and similar proteins; ...
 8-34 4.60e-03

RING finger, HC subclass, found in RING finger protein 146 (RNF146) and similar proteins; RNF146, also known as dactylidin, or iduna, is a cytoplasmic E3 ubiquitin-protein ligase that is responsible for PARylation-dependent ubiquitination (PARdU). It displays neuroprotective property due to its inhibition of Parthanatos, a PAR dependent cell death, via binding with Poly(ADP-ribose) (PAR). It also modulates PAR polymerase-1 (PARP-1)-mediated oxidative cell injury in cardiac myocytes. Moreover, RNF146 mediates tankyrase-dependent degradation of axin, thereby positively regulating Wnt signaling. It also facilitates DNA repair and protects against cell death induced by DNA damaging agents or gamma-irradiation by translocating to the nucleus after cellular injury and promoting the ubiquitination and degradation of various nuclear proteins involved in DNA damage repair. Furthermore, RNF146 is implicated in neurodegenerative disease and cancer development. It regulates the development and progression of non-small cell lung cancer (NSCLC) by enhancing cell growth, invasion, and survival. RNF146 contains an N-terminal C3HC4-type RING-HC finger followed by a WWE domain with a poly(ADP-ribose) (PAR) binding motif at the tail.


Pssm-ID: 438208 [Multi-domain]  Cd Length: 50  Bit Score: 35.44  E-value: 4.60e-03
                          10        20
                  ....*....|....*....|....*..
gi 1039796541   8 LTCPICLELFEDPLLLPCAHSLCFNCA 34
Cdd:cd16546     1 PECPICLQTCIHPVKLPCGHIFCYLCV 27
RING-HC_RNF170 cd16553
RING finger, HC subclass, found in RING finger protein 170 (RNF170) and similar proteins; ...
 9-65 5.00e-03

RING finger, HC subclass, found in RING finger protein 170 (RNF170) and similar proteins; RNF170, also known as putative LAG1-interacting protein, is an endoplasmic reticulum (ER) membrane-bound E3 ubiquitin-protein ligase that mediates ubiquitination-dependent degradation of type-I inositol 1,4,5-trisphosphate (IP3) receptors (ITPR1) via the endoplasmic-reticulum-associated protein degradation (ERAD) pathway. A point mutation (arginine to cysteine at position 199) in the RNF170 gene is linked with autosomal-dominant sensory ataxia (ADSA), a disease characterized by neurodegeneration in the posterior columns of the spinal cord. RNF170 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438215 [Multi-domain]  Cd Length: 57  Bit Score: 35.73  E-value: 5.00e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796541   9 TCPICLELFEDPLLLPCAHSLCFNCahriLVSHCATNepvESINAFQCPTCRHVITL 65
Cdd:cd16553     3 ECPICLQDARFPVETNCGHLFCGPC----IITYWRHG---SWLGAVSCPVCRQTVTL 52
RING-HC_CHFR cd16503
RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein ...
 7-60 5.38e-03

RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also known as RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22, and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression, and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated (FHA) domain and a C3HC4-type RING-HC finger.


Pssm-ID: 438166 [Multi-domain]  Cd Length: 55  Bit Score: 35.42  E-value: 5.38e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039796541   7 ELTCPICLELFEDPL-LLPCAHSLCFNCAHRILvshcatnEPVESinafQCPTCR 60
Cdd:cd16503     2 NLTCSICQDLLHDCVsLQPCMHNFCAACYSDWM-------ERSNT----ECPTCR 45
RING-HC_LNX3 cd16718
RING finger, HC subclass, found in ligand of numb protein X 3 (LNX3); LNX3, also known as PDZ ...
 4-33 5.50e-03

RING finger, HC subclass, found in ligand of numb protein X 3 (LNX3); LNX3, also known as PDZ domain-containing RING finger protein 3 (PDZRN3), or Semaphorin cytoplasmic domain-associated protein 3 (SEMACAP3), is an E3 ubiquitin-protein ligase that was first identified as a Semaphorin-binding partner. It is also responsible for the ubiquitination and degradation of Numb, a component of the Notch signaling pathway that functions in the specification of cell fates during development and is known to control cell numbers during neurogenesis in vertebrates. LNX3 acts as a negative regulator of osteoblast differentiation by inhibiting Wnt-beta-catenin signaling. LNX3 also plays an important role in neuromuscular junction formation. It interacts with and ubiquitinates the muscle specific tyrosine kinase (MuSK), thus promoting its endocytosis and negatively regulating the cell surface expression of this key regulator of postsynaptic assembly. LNX3 contains an N-terminal C3HC4-type RING-HC finger, two PDZ domains, and a C-terminal LNX3 homology (LNX3H) domain.


Pssm-ID: 438378 [Multi-domain]  Cd Length: 47  Bit Score: 35.35  E-value: 5.50e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1039796541   4 LESELTCPICLELFEDPLLLPCAHSLCFNC 33
Cdd:cd16718     1 VDPDFKCNLCNKVLEDPLTTPCGHVFCAGC 30
Bbox2_TRIM23_C-IX_rpt1 cd19773
first B-box-type 2 zinc finger found in tripartite motif-containing protein 23 (TRIM23) and ...
 122-162 6.60e-03

first B-box-type 2 zinc finger found in tripartite motif-containing protein 23 (TRIM23) and similar proteins; TRIM23, also known as ADP-ribosylation factor domain-containing protein 1, GTP-binding protein ARD-1, or RING finger protein 46 (RNF46), is an E3 ubiquitin-protein ligase belonging to the C-IX subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, two Bbox2, and a coiled coil region, as well as C-terminal ADP ribosylation factor (ARF) domains. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TRIM23 is involved in nuclear factor (NF)-kappaB activation. It mediates atypical lysine 27 (K27)-linked polyubiquitin conjugation to NF-kappaB essential modulator NEMO, also known as IKKgamma, which plays an important role in the NF-kappaB pathway, and this conjugation is essential for TLR3- and RIG-I/MDA5-mediated antiviral innate and inflammatory responses. It also regulates adipocyte differentiation via stabilization of the adipogenic activator peroxisome proliferator-activated receptor gamma (PPARgamma) through atypical ubiquitin conjugation to PPARgamma. Moreover, TRIM23 interacts with and polyubiquitinates yellow fever virus (YFV) NS5 to promote its binding to STAT2 and trigger type I interferon (IFN-I) signaling inhibition.


Pssm-ID: 380831  Cd Length: 50  Bit Score: 35.00  E-value: 6.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1039796541 122 CDQDPAQDAVKTCVTCEVSYCDECLKATHpNKKPFTGHRLI 162
Cdd:cd19773     5 CDENEDHEATLYCTVCSTNLCEECFTSTH-STKTLSKHRRV 44
RING-HC_SH3RFs cd16570
RING finger, HC subclass, found in SH3 domain-containing RING finger proteins SH3RF1, SH3RF2, ...
 8-60 6.84e-03

RING finger, HC subclass, found in SH3 domain-containing RING finger proteins SH3RF1, SH3RF2, SH3RF3, and similar proteins; SH3RF1, also known as plenty of SH3s (POSH), RING finger protein 142 (RNF142), or SH3 multiple domains protein 2 (SH3MD2), is a trans-Golgi network-associated pro-apoptotic scaffold protein with E3 ubiquitin-protein ligase activity. SH3RF2, also known as heart protein phosphatase 1-binding protein (HEPP1), plenty of SH3s (POSH)-eliminating RING protein (POSHER), protein phosphatase 1 regulatory subunit 39, or RING finger protein 158 (RNF158), is a putative E3 ubiquitin-protein ligase that acts as an anti-apoptotic regulator for the c-Jun N-terminal kinase (JNK) pathway by binding to and promoting the proteasomal degradation of SH3RF1 (or POSH) that is required for pro-apoptotic JNK activation. SH3RF3, also known as plenty of SH3s 2 (POSH2) or SH3 multiple domains protein 4 (SH3MD4), is a scaffold protein with E3 ubiquitin-protein ligase activity. It was identified in the screen for interacting partners of p21-activated kinase 2 (PAK2) and may play a role in regulating c-Jun N-terminal kinase (JNK) mediated apoptosis in certain conditions. Members of this subfamily contain an N-terminal C3HC4-type RING-HC finger responsible for the E3 ligase activity and four Src Homology 3 (SH3) domains, which are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs.


Pssm-ID: 438232 [Multi-domain]  Cd Length: 44  Bit Score: 34.71  E-value: 6.84e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039796541   8 LTCPICLE-LFEDPLLLPCAHSLCFNCAHRIlvshcatnepVESINAFQCPTCR 60
Cdd:cd16570     1 LECPVCLErLDVSAKVLPCQHTFCKRCLQII----------VASRGELRCPECR 44
mRING-HC-C4C4_TRIM37_C-VIII cd16619
Modified RING finger, HC subclass (C4C4-type), found in tripartite motif-containing protein 37 ...
 8-60 6.96e-03

Modified RING finger, HC subclass (C4C4-type), found in tripartite motif-containing protein 37 (TRIM37) and similar proteins; TRIM37, also known as mulibrey nanism protein, or MUL, is a peroxisomal E3 ubiquitin-protein ligase that is involved in the tumorigenesis of several cancer types, including pancreatic ductal adenocarcinoma (PDAC), hepatocellular carcinoma (HCC), breast cancer, and sporadic fibrothecoma. It mono-ubiquitinates histone H2A, a chromatin modification associated with transcriptional repression. Moreover, TRIM37 possesses anti-HIV-1 activity, and interferes with viral DNA synthesis. Mutations in the human TRIM37 gene (also known as MUL) cause Mulibrey (muscle-liver-brain-eye) nanism, a rare growth disorder of prenatal onset characterized by dysmorphic features, pericardial constriction, and hepatomegaly. TRIM37 belongs to the C-VIII 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 C4C4-type RING finger, whose overall folding is similar to that of the typical C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a MATH (meprin and TRAF-C homology) domain positioned C-terminal to the RBCC domain. Its MATH domain has been shown to interact with the TRAF (TNF-Receptor-Associated Factor) domain of six known TRAFs in vitro.


Pssm-ID: 438281 [Multi-domain]  Cd Length: 43  Bit Score: 35.03  E-value: 6.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039796541   8 LTCPICLELFEDPLLLPCAHSL-CFNCAHRILVSHCAtnepvesinafQCPTCR 60
Cdd:cd16619     1 FRCFICMEKLRDPRLCPHCSKLfCKGCIRRWLSEQRS-----------SCPHCR 43
RING-HC_RNF166 cd16549
RING finger, HC subclass, found in RING finger protein 166 (RNF166) and similar proteins; ...
 7-60 7.34e-03

RING finger, HC subclass, found in RING finger protein 166 (RNF166) and similar proteins; RNF166 is encoded by the gene RNF166 targeted by thyroid hormone receptor alpha1 (TRalpha1), which is important in brain development. It plays an important role in RNA virus-induced interferon-beta production by enhancing the ubiquitination of TRAF3 and TRAF6. RNF166, together with three closely related proteins: RNF114, RNF125 and RNF138, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM).


Pssm-ID: 438211 [Multi-domain]  Cd Length: 47  Bit Score: 34.79  E-value: 7.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039796541   7 ELTCPICLELFEDPLLL-PCAHSLCFNCAhrilvshcatnEPVESINAFQCPTCR 60
Cdd:cd16549     1 QFSCPICLEVYHKPVVItSCGHTFCGECL-----------QPCLQVASPLCPLCR 44
RING-HC_IRC20-like cd23135
RING finger, HC subclass, found in Saccharomyces cerevisiae increased recombination centers ...
 6-60 8.26e-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: 34.80  E-value: 8.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039796541   6 SELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCAtnepvesinafqCPTCR 60
Cdd:cd23135     2 QKLSCSICFSEIRSGAILKCGHFFCLSCIASWLREKST------------CPLCK 44
RING-H2_SIS3 cd23118
RING finger, H2 subclass, found in Arabidopsis thaliana protein SUGAR INSENSITIVE 3 (SIS3) and ...
 9-63 9.47e-03

RING finger, H2 subclass, found in Arabidopsis thaliana protein SUGAR INSENSITIVE 3 (SIS3) and similar proteins; SIS3 is an E3 ubiquitin-protein ligase that acts as a positive regulator of sugar signaling during early seedling development. SIS3 contains a C3H2C3-type RING-H2 finger.


Pssm-ID: 438480 [Multi-domain]  Cd Length: 47  Bit Score: 34.65  E-value: 9.47e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796541   9 TCPICLELFEDP---LLLPCAHSLCFNCAHRILVSHcatnepvesinaFQCPTCRHVI 63
Cdd:cd23118     2 TCTICLEDFEDGeklRVLPCQHQFHSECVDQWLRRN------------PKCPVCRRDA 47
 
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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