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Conserved domains on  [gi|1913184748|ref|NP_001374303|]
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E3 ubiquitin-protein ligase TRIM9 isoform 17 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SPRY_PRY_TRIM67_9 cd12889
PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, ...
456-609 2.73e-107

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: 320.34  E-value: 2.73e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 456 VLQTSEVAWFAFDPGSAHSDIILSNDNLTVTCSSYDDRVVLGKTGFSKGIHYWELTVDRYDNHPDPAFGVARMDVMKDVM 535
Cdd:cd12889     1 CLQTAEVAWFTFDPSTSHPDIILSNDNMTVTCNSYEDRVVLGSVGFSRGVHYWEVTIDRYDGHPDPAFGVARIDVNKDKM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 536 LGKDDKAWAI------------------TEGGITKGATIGVLLDLNRKNLTFFINDEQQGPIAFDNVEGLFFPAVSLNRN 597
Cdd:cd12889    81 LGKDDKGWSMyidnnrswflhnnehsnrTEGGITVGSVVGVLLDLDRHTLSFYVNDEPQGPIAFRNLPGVFYPAVSLNRN 160
                         170
                  ....*....|..
gi 1913184748 598 VQVTLHTGLPVP 609
Cdd:cd12889   161 VQVTLHTGLEPP 172
Bbox2_TRIM9_C-I cd19826
B-box-type 2 zinc finger found in tripartite motif-containing protein 9 (TRIM9) and similar ...
223-271 1.80e-31

B-box-type 2 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 the 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 (DSGXXS) 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 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


:

Pssm-ID: 380884  Cd Length: 49  Bit Score: 115.97  E-value: 1.80e-31
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1913184748 223 PRKVSTCTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKALGAMWK 271
Cdd:cd19826     1 PRKISTCTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKALGAMWK 49
Bbox1_TRIM9_C-I cd19843
B-box-type 1 zinc finger found in tripartite motif-containing protein 9 (TRIM9) and similar ...
166-212 7.80e-31

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: 114.32  E-value: 7.80e-31
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1913184748 166 LKCQLCEKAPKEATVMCEQCDVFYCDPCRLRCHPPRGPLAKHRLVPP 212
Cdd:cd19843     1 LKCQLCEKSPKEATVMCEQCDVFYCDPCRLRCHPPRGPLAKHRLVPP 47
RING_Ubox super family cl17238
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
5-49 2.06e-27

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 cd16755:

Pssm-ID: 473075 [Multi-domain]  Cd Length: 55  Bit Score: 104.73  E-value: 2.06e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1913184748   5 EEELKCPVCGSFYREPIILPCSHNLCQACARNILVQTPESESPQS 49
Cdd:cd16755     1 EEELKCPVCGSFYREPIILPCSHNLCLACARNILVQTPEAESPQS 45
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
380-459 6.35e-15

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: 70.60  E-value: 6.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 380 THNNSATLSWKQPPLSTVPADGYILELDDGNGGQFREVYV--GKETMCTVDGLHFNSTYNARVKAFNKTGVSPYSKTLVL 457
Cdd:cd00063    12 VTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPSESVTV 91

                  ..
gi 1913184748 458 QT 459
Cdd:cd00063    92 TT 93
CC_brat-like super family cl29238
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
271-326 4.70e-10

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: 57.66  E-value: 4.70e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1913184748  271 KLHKVVRDQISHCTVKLRQTTGLMEYCLEVIKENDPSGFLQISDALIRRVHLTEDQ 326
Cdd:smart00502  72 NKLKVLEQQLESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLLKQ 127
 
Name Accession Description Interval E-value
SPRY_PRY_TRIM67_9 cd12889
PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, ...
456-609 2.73e-107

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: 320.34  E-value: 2.73e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 456 VLQTSEVAWFAFDPGSAHSDIILSNDNLTVTCSSYDDRVVLGKTGFSKGIHYWELTVDRYDNHPDPAFGVARMDVMKDVM 535
Cdd:cd12889     1 CLQTAEVAWFTFDPSTSHPDIILSNDNMTVTCNSYEDRVVLGSVGFSRGVHYWEVTIDRYDGHPDPAFGVARIDVNKDKM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 536 LGKDDKAWAI------------------TEGGITKGATIGVLLDLNRKNLTFFINDEQQGPIAFDNVEGLFFPAVSLNRN 597
Cdd:cd12889    81 LGKDDKGWSMyidnnrswflhnnehsnrTEGGITVGSVVGVLLDLDRHTLSFYVNDEPQGPIAFRNLPGVFYPAVSLNRN 160
                         170
                  ....*....|..
gi 1913184748 598 VQVTLHTGLPVP 609
Cdd:cd12889   161 VQVTLHTGLEPP 172
Bbox2_TRIM9_C-I cd19826
B-box-type 2 zinc finger found in tripartite motif-containing protein 9 (TRIM9) and similar ...
223-271 1.80e-31

B-box-type 2 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 the 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 (DSGXXS) 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 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380884  Cd Length: 49  Bit Score: 115.97  E-value: 1.80e-31
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1913184748 223 PRKVSTCTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKALGAMWK 271
Cdd:cd19826     1 PRKISTCTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKALGAMWK 49
Bbox1_TRIM9_C-I cd19843
B-box-type 1 zinc finger found in tripartite motif-containing protein 9 (TRIM9) and similar ...
166-212 7.80e-31

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: 114.32  E-value: 7.80e-31
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1913184748 166 LKCQLCEKAPKEATVMCEQCDVFYCDPCRLRCHPPRGPLAKHRLVPP 212
Cdd:cd19843     1 LKCQLCEKSPKEATVMCEQCDVFYCDPCRLRCHPPRGPLAKHRLVPP 47
RING-HC_TRIM9 cd16755
RING finger, HC subclass, found in tripartite motif-containing protein 9 (TRIM9) and similar ...
5-49 2.06e-27

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: 104.73  E-value: 2.06e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1913184748   5 EEELKCPVCGSFYREPIILPCSHNLCQACARNILVQTPESESPQS 49
Cdd:cd16755     1 EEELKCPVCGSFYREPIILPCSHNLCLACARNILVQTPEAESPQS 45
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
380-459 6.35e-15

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: 70.60  E-value: 6.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 380 THNNSATLSWKQPPLSTVPADGYILELDDGNGGQFREVYV--GKETMCTVDGLHFNSTYNARVKAFNKTGVSPYSKTLVL 457
Cdd:cd00063    12 VTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPSESVTV 91

                  ..
gi 1913184748 458 QT 459
Cdd:cd00063    92 TT 93
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
505-607 5.64e-13

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: 65.83  E-value: 5.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 505 IHYWELTVDRYDNHpDPAFGVARMDVM--KDVMLGKDDKAWAI----------------TEGGITKGATIGVLLDLNRKN 566
Cdd:pfam00622   1 RHYFEVEIFGQDGG-GWRVGWATKSVPrkGERFLGDESGSWGYdgwtgkkywastspltGLPLFEPGDVIGCFLDYEAGT 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1913184748 567 LTFFINDEQQGpIAFDNV--EGLFFPAVSLNRNVQVTLHTGLP 607
Cdd:pfam00622  80 ISFTKNGKSLG-YAFRDVpfAGPLFPAVSLGAGEGLKFNFGLR 121
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
503-595 2.11e-10

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: 58.46  E-value: 2.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748  503 KGIHYWELTVDrydnhpDP---AFGVARMDV--MKDVMLGKDDKAWAI----------------TEGGITKGATIGVLLD 561
Cdd:smart00449   1 SGRHYFEVEIG------DGghwRVGVATKSVprGYFALLGEDKGSWGYdgdggkkyhnstgpeyGLPLQEPGDVIGCFLD 74
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1913184748  562 LNRKNLTFFINDEQQGPIAFDNVE--GLFFPAVSLN 595
Cdd:smart00449  75 LEAGTISFYKNGKYLHGLAFFDVKfsGPLYPAFSLG 110
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
271-326 4.70e-10

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


Pssm-ID: 128778  Cd Length: 127  Bit Score: 57.66  E-value: 4.70e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1913184748  271 KLHKVVRDQISHCTVKLRQTTGLMEYCLEVIKENDPSGFLQISDALIRRVHLTEDQ 326
Cdd:smart00502  72 NKLKVLEQQLESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLLKQ 127
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
380-449 4.58e-09

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: 53.39  E-value: 4.58e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1913184748  380 THNNSATLSWKQPPLSTV--PADGYILELDDGNGGQFREVYVGKETMCTVDGLHFNSTYNARVKAFNKTGVS 449
Cdd:smart00060  12 VTSTSVTLSWEPPPDDGItgYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
382-452 9.30e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 52.80  E-value: 9.30e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1913184748 382 NNSATLSWKQPPLSTVPADGYILEL-DDGNGGQFREVYVGK-ETMCTVDGLHFNSTYNARVKAFNKTGVSPYS 452
Cdd:pfam00041  13 STSLTVSWTPPPDGNGPITGYEVEYrPKNSGEPWNEITVPGtTTSVTLTGLKPGTEYEVRVQAVNGGGEGPPS 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
359-524 5.74e-08

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 55.78  E-value: 5.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 359 VQVKASSPVPATP-ILQLEEccTHNNSATLSWKQPplSTVPADGYILELDDGNGGQFREVY-VGKETMCTVDGLHFNSTY 436
Cdd:COG3401   318 VSVTTDLTPPAAPsGLTATA--VGSSSITLSWTAS--SDADVTGYNVYRSTSGGGTYTKIAeTVTTTSYTDTGLTPGTTY 393
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 437 NARVKAFNKTGV-SPYSKTLVLQTSEVA---WFAFDPGSAHSDIILSNDNLTVTCSSYDDRVVLGKTGFSKGIhYWELTV 512
Cdd:COG3401   394 YYKVTAVDAAGNeSAPSEEVSATTASAAsgeSLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGN-AVPFTT 472
                         170
                  ....*....|..
gi 1913184748 513 DRYDNHPDPAFG 524
Cdd:COG3401   473 TSSTVTATTTDT 484
BBOX smart00336
B-Box-type zinc finger;
224-266 3.99e-07

B-Box-type zinc finger;


Pssm-ID: 197662 [Multi-domain]  Cd Length: 42  Bit Score: 46.56  E-value: 3.99e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1913184748  224 RKVSTCTDHELENHSMYCVQCKMPVCYQClEEGKHSSHEVKAL 266
Cdd:smart00336   1 QRAPKCDSHGDEPAEFFCEECGALLCRTC-DEAEHRGHTVVLL 42
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
359-460 7.25e-07

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 52.31  E-value: 7.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 359 VQVKASSPVPATPI-LQLEEccTHNNSATLSWkqPPLSTVPADGYILELDDGNGGQFREVYVGKETMCTVDGLHFNSTYN 437
Cdd:COG3401   224 VSVTTPTTPPSAPTgLTATA--DTPGSVTLSW--DPVTESDATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYY 299
                          90       100
                  ....*....|....*....|....
gi 1913184748 438 ARVKAFNKTGV-SPYSKTLVLQTS 460
Cdd:COG3401   300 YRVTAVDAAGNeSAPSNVVSVTTD 323
BBOX smart00336
B-Box-type zinc finger;
163-211 4.24e-06

B-Box-type zinc finger;


Pssm-ID: 197662 [Multi-domain]  Cd Length: 42  Bit Score: 43.87  E-value: 4.24e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1913184748  163 AAALKCQLCEKAPkeATVMCEQCDVFYCDPCRLRCHpprgplAKHRLVP 211
Cdd:smart00336   1 QRAPKCDSHGDEP--AEFFCEECGALLCRTCDEAEH------RGHTVVL 41
zf-B_box pfam00643
B-box zinc finger;
224-266 2.13e-05

B-box zinc finger;


Pssm-ID: 459886 [Multi-domain]  Cd Length: 42  Bit Score: 41.69  E-value: 2.13e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1913184748 224 RKVSTCTDHELENHSMYCVQCKMPVCYQCLeEGKHSSHEVKAL 266
Cdd:pfam00643   1 SKERLCPEHEEEPLTLYCNDCQELLCEECS-VGEHRGHTVVPL 42
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
4-42 8.42e-05

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: 45.38  E-value: 8.42e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1913184748   4 MEEELKCPVCGSFYREPIILPCSHNLCQACARNILVQTP 42
Cdd:TIGR00599  23 LDTSLRCHICKDFFDVPVLTSCSHTFCSLCIRRCLSNQP 61
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
6-43 2.33e-03

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 36.20  E-value: 2.33e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1913184748   6 EELKCPVCGSFYREPIILPCSHN-LCQACARNILVQTPE 43
Cdd:pfam13920   1 EDLLCVICLDRPRNVVLLPCGHLcLCEECAERLLRKKKK 39
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
10-38 3.12e-03

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


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 35.56  E-value: 3.12e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1913184748   10 CPVC-GSFYREPIILPCSHNLCQACARNIL 38
Cdd:smart00184   1 CPIClEEYLKDPVILPCGHTFCRSCIRKWL 30
 
Name Accession Description Interval E-value
SPRY_PRY_TRIM67_9 cd12889
PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, ...
456-609 2.73e-107

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: 320.34  E-value: 2.73e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 456 VLQTSEVAWFAFDPGSAHSDIILSNDNLTVTCSSYDDRVVLGKTGFSKGIHYWELTVDRYDNHPDPAFGVARMDVMKDVM 535
Cdd:cd12889     1 CLQTAEVAWFTFDPSTSHPDIILSNDNMTVTCNSYEDRVVLGSVGFSRGVHYWEVTIDRYDGHPDPAFGVARIDVNKDKM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 536 LGKDDKAWAI------------------TEGGITKGATIGVLLDLNRKNLTFFINDEQQGPIAFDNVEGLFFPAVSLNRN 597
Cdd:cd12889    81 LGKDDKGWSMyidnnrswflhnnehsnrTEGGITVGSVVGVLLDLDRHTLSFYVNDEPQGPIAFRNLPGVFYPAVSLNRN 160
                         170
                  ....*....|..
gi 1913184748 598 VQVTLHTGLPVP 609
Cdd:cd12889   161 VQVTLHTGLEPP 172
SPRY_PRY_C-II cd13734
PRY/SPRY domain in tripartite motif-containing proteins 1, 9, 18, 36, 46, 67,76 (TRIM1, TRIM9, ...
465-603 4.86e-36

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: 132.79  E-value: 4.86e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 465 FAFDPGSAHSDIILSNDNLTVTCSSY--------------DDRVVLGKTGFSKGIHYWELTVDRYdnhPDPAFGVARMDV 530
Cdd:cd13734     1 FKLDPKTAHRKLRLSNDNLTVEYDPEgskdqaavlprrftGSPAVLGDVAISSGRHYWEVSVSRS---TSYRVGVAYKSA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 531 MKDVMLGKDDKAWAITEGGIT----------------KGATIGVLLDLNRKNLTFFINDEQQGPIAFDNV-EGLFFPAVS 593
Cdd:cd13734    78 PRDEDLGKNSTSWCLSRDNNRytarhdgkvvdlrvtgHPARIGVLLDYDNGTLSFYDAESKQHLYTFHVDfEGPVCPAFA 157
                         170
                  ....*....|
gi 1913184748 594 LNrNVQVTLH 603
Cdd:cd13734   158 VW-NGSLTLH 166
Bbox2_TRIM9_C-I cd19826
B-box-type 2 zinc finger found in tripartite motif-containing protein 9 (TRIM9) and similar ...
223-271 1.80e-31

B-box-type 2 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 the 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 (DSGXXS) 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 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380884  Cd Length: 49  Bit Score: 115.97  E-value: 1.80e-31
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1913184748 223 PRKVSTCTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKALGAMWK 271
Cdd:cd19826     1 PRKISTCTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKALGAMWK 49
Bbox1_TRIM9_C-I cd19843
B-box-type 1 zinc finger found in tripartite motif-containing protein 9 (TRIM9) and similar ...
166-212 7.80e-31

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: 114.32  E-value: 7.80e-31
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1913184748 166 LKCQLCEKAPKEATVMCEQCDVFYCDPCRLRCHPPRGPLAKHRLVPP 212
Cdd:cd19843     1 LKCQLCEKSPKEATVMCEQCDVFYCDPCRLRCHPPRGPLAKHRLVPP 47
RING-HC_TRIM9 cd16755
RING finger, HC subclass, found in tripartite motif-containing protein 9 (TRIM9) and similar ...
5-49 2.06e-27

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: 104.73  E-value: 2.06e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1913184748   5 EEELKCPVCGSFYREPIILPCSHNLCQACARNILVQTPESESPQS 49
Cdd:cd16755     1 EEELKCPVCGSFYREPIILPCSHNLCLACARNILVQTPEAESPQS 45
Bbox2_TRIM67_C-I cd19827
B-box-type 2 zinc finger found in tripartite motif-containing protein 67 (TRIM67) and similar ...
228-271 4.99e-25

B-box-type 2 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 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380885  Cd Length: 45  Bit Score: 97.75  E-value: 4.99e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1913184748 228 TCTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKALGAMWK 271
Cdd:cd19827     2 TCAEHELENYSMYCASCRTPVCYQCLEEGKHAKHEVKALGAMWK 45
Bbox1_TRIM9-like_C-I cd19803
B-box-type 1 zinc finger found in tripartite motif-containing proteins, TRIM9, TRIM67 and ...
167-212 4.15e-24

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: 95.06  E-value: 4.15e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1913184748 167 KCQLCEKAP-KEATVMCEQCDVFYCDPCRLRCHPPRGPLAKHRLVPP 212
Cdd:cd19803     1 RCQLCEKSPpKEASVFCEQCEVFYCDSCRESCHPPRGPLAKHTLVSP 47
RING-HC_TRIM67 cd16758
RING finger, HC subclass, found in tripartite motif-containing protein 67 (TRIM67) and similar ...
5-51 3.89e-20

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: 83.98  E-value: 3.89e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1913184748   5 EEELKCPVCGSFYREPIILPCSHNLCQACARNILVQTPESES----------PQSHR 51
Cdd:cd16758     1 EEELKCPVCGSLFREPIILPCSHNVCLPCARTIAVQTPESEQhlphsssitcPQCHR 57
Bbox1_TRIM67_C-I cd19844
B-box-type 1 zinc finger found in tripartite motif-containing protein 67 (TRIM67) and similar ...
165-212 6.94e-20

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: 83.17  E-value: 6.94e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1913184748 165 ALKCQLCEKAP-KEATVMCEQCDVFYCDPCRLRCHPPRGPLAKHRLVPP 212
Cdd:cd19844     1 NARCQLCDRNPpEPAAVLCEQCDVLYCSACQLKCHPTRGPFAKHRLVPP 49
RING-HC_TRIM9-like_C-I cd16576
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM9, TRIM67, and ...
5-42 1.60e-16

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: 73.21  E-value: 1.60e-16
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1913184748   5 EEELKCPVCGSFYREPIILPCSHNLCQACARNILVQTP 42
Cdd:cd16576     1 EEELKCPVCGSLFTEPVILPCSHNLCLGCALNIQLTCP 38
Bbox2_TRIM9-like cd19764
B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM9, TRIM67 and ...
228-266 1.93e-16

B-box-type 2 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 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 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 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: 380822  Cd Length: 39  Bit Score: 73.19  E-value: 1.93e-16
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1913184748 228 TCTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKAL 266
Cdd:cd19764     1 TCSEHPDEALSMYCLSCKVPVCYLCLEDGRHSNHDVQAL 39
SPRY_SOCS3 cd12876
SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY ...
468-593 3.61e-16

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: 76.82  E-value: 3.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 468 DPGSAHSDIILSNDNLTVT---CSSYDDRVVLGKTGFSKGIHYWELTVDrydnhpDPAFGvarMDVM-----KDV----- 534
Cdd:cd12876     5 DERDKSPAVQLSDNNREVYfhpDYSCGTAAVRGTKPLTNGQHYWEIKMS------SPVYG---TDMMvgvgtKKAdlhay 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 535 ------MLGKDDKAW------AITEGGITK---------GATIGVLLDLNRKNLTFFINDEQQGpIAFDNVEGL--FFPA 591
Cdd:cd12876    76 ryefcsLLGEDEESWglsykgLLWHDGQSRpytspfgnqGTIIGVHLDMWRGTLTFYKNGKPLG-VAFTGLNGVkpLYPM 154

                  ..
gi 1913184748 592 VS 593
Cdd:cd12876   155 VS 156
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
380-459 6.35e-15

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: 70.60  E-value: 6.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 380 THNNSATLSWKQPPLSTVPADGYILELDDGNGGQFREVYV--GKETMCTVDGLHFNSTYNARVKAFNKTGVSPYSKTLVL 457
Cdd:cd00063    12 VTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPSESVTV 91

                  ..
gi 1913184748 458 QT 459
Cdd:cd00063    92 TT 93
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
504-603 7.69e-14

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: 68.23  E-value: 7.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 504 GIHYWELTVDRyDNHPDPAFGVARMDV--MKDVMLGKDDKAWAI---------------TEGGITKGATIGVLLDLNRKN 566
Cdd:cd11709     1 GKWYWEVRVDS-GNGGLIQVGWATKSFslDGEGGVGDDEESWGYdgsrlrkghggssgpGGRPWKSGDVVGCLLDLDEGT 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1913184748 567 LTFFINDEQQGpIAFDNV---EGLFFPAVSLNRNVQVTLH 603
Cdd:cd11709    80 LSFSLNGKDLG-VAFTNLflkGGGLYPAVSLGSGQGVTIN 118
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
505-607 5.64e-13

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: 65.83  E-value: 5.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 505 IHYWELTVDRYDNHpDPAFGVARMDVM--KDVMLGKDDKAWAI----------------TEGGITKGATIGVLLDLNRKN 566
Cdd:pfam00622   1 RHYFEVEIFGQDGG-GWRVGWATKSVPrkGERFLGDESGSWGYdgwtgkkywastspltGLPLFEPGDVIGCFLDYEAGT 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1913184748 567 LTFFINDEQQGpIAFDNV--EGLFFPAVSLNRNVQVTLHTGLP 607
Cdd:pfam00622  80 ISFTKNGKSLG-YAFRDVpfAGPLFPAVSLGAGEGLKFNFGLR 121
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
476-612 8.41e-12

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


Pssm-ID: 293932  Cd Length: 150  Bit Score: 63.31  E-value: 8.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 476 IILSNDNLTVTCSS-YddRVVLGKTGFSKGIHYWELTVDRYDNHPDPA--FGVAR----MDV----------MKDVMLGK 538
Cdd:cd12872     1 LKLSEDRLTVTGEKgY--RMARANHGVREGKWYFEVKILEGGGTETGHvrVGWSRreasLQApvgydkysyaIRDKDGSK 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1913184748 539 DDKAWAI--TEGGITKGATIGVLLDLNRknLTFFINDEQQGPiAFDNV--EGLFFPAVSLNRNVQVTLHTGlpvPDFY 612
Cdd:cd12872    79 FHQSRGKpyGEPGFKEGDVIGFLITLPK--IEFFKNGKSQGV-AFEDIygTGGYYPAVSLYKGATVTINFG---PDFK 150
RING-HC_TRIM46_C-I cd16757
RING finger, HC subclass, found in tripartite motif-containing protein 46 (TRIM46) and similar ...
4-42 8.25e-11

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: 57.13  E-value: 8.25e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1913184748   4 MEEELKCPVCGSFYREPIILPCSHNLCQACARNILVQTP 42
Cdd:cd16757     1 MERELLCPVCKEMYKQPLVLPCMHNVCQVCASEVLFPCP 39
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
503-595 2.11e-10

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: 58.46  E-value: 2.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748  503 KGIHYWELTVDrydnhpDP---AFGVARMDV--MKDVMLGKDDKAWAI----------------TEGGITKGATIGVLLD 561
Cdd:smart00449   1 SGRHYFEVEIG------DGghwRVGVATKSVprGYFALLGEDKGSWGYdgdggkkyhnstgpeyGLPLQEPGDVIGCFLD 74
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1913184748  562 LNRKNLTFFINDEQQGPIAFDNVE--GLFFPAVSLN 595
Cdd:smart00449  75 LEAGTISFYKNGKYLHGLAFFDVKfsGPLYPAFSLG 110
SPRY_PRY_C-I_2 cd12891
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM14-like, ...
467-570 2.54e-10

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: 59.57  E-value: 2.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 467 FDPGSAHSDIILSNDNLTVTCSSYDDRV-----------VLGKTGFSKGIHYWELTVdryDNHPDPAFGVA--RMDVMKD 533
Cdd:cd12891     3 LDPNTAHNNLALSGDLKTVTCSSENQHYpdsperfthsqVLSTQSFSSGRHYWEVEV---SESGGWSVGVAypSIERKGD 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1913184748 534 V-MLGKDDKAWAITEGGITKGA---------------TIGVLLDLNRKNLTFF 570
Cdd:cd12891    80 EsRIGRNDKSWCLEWQDKSFSAwhnneetplpsvssrRLGVYLDYEAGRLSFY 132
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
271-326 4.70e-10

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


Pssm-ID: 128778  Cd Length: 127  Bit Score: 57.66  E-value: 4.70e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1913184748  271 KLHKVVRDQISHCTVKLRQTTGLMEYCLEVIKENDPSGFLQISDALIRRVHLTEDQ 326
Cdd:smart00502  72 NKLKVLEQQLESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLLKQ 127
Bbox1_MID cd19801
B-box-type 1 zinc finger found in the midline (MID) family; The MID family includes MID1 and ...
167-212 7.98e-10

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: 54.69  E-value: 7.98e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1913184748 167 KCQLCEKAPKEATVM-CEQCDVFYCDPCRLRCHPPRGPLAKHRLVPP 212
Cdd:cd19801     3 PCDVCEKEPPRKAVKtCLTCEVSYCKRCLEATHPNRGPFATHRLVEP 49
RING-HC_MID2 cd16754
RING finger, HC subclass, found in midline-2 (MID2) and similar proteins; MID2, also known as ...
1-39 2.24e-09

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: 53.84  E-value: 2.24e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1913184748   1 MEEMEEELKCPVCGSFYREPIILPCSHNLCQACARNILV 39
Cdd:cd16754     1 METLESELTCPICLELFEDPLLLPCAHSLCFSCAHRILT 39
RING-HC_TRIM65_C-IV cd16609
RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar ...
5-53 3.44e-09

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: 53.14  E-value: 3.44e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1913184748   5 EEELKCPVCGSFYREPIILPCSHNLCQACARNILVQTPES--ESPQSHRAA 53
Cdd:cd16609     1 EEELTCSICLGLYQDPVTLPCQHSFCRACIEDHWRQKDEGsfSCPECRAPF 51
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
380-449 4.58e-09

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: 53.39  E-value: 4.58e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1913184748  380 THNNSATLSWKQPPLSTV--PADGYILELDDGNGGQFREVYVGKETMCTVDGLHFNSTYNARVKAFNKTGVS 449
Cdd:smart00060  12 VTSTSVTLSWEPPPDDGItgYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
382-452 9.30e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 52.80  E-value: 9.30e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1913184748 382 NNSATLSWKQPPLSTVPADGYILEL-DDGNGGQFREVYVGK-ETMCTVDGLHFNSTYNARVKAFNKTGVSPYS 452
Cdd:pfam00041  13 STSLTVSWTPPPDGNGPITGYEVEYrPKNSGEPWNEITVPGtTTSVTLTGLKPGTEYEVRVQAVNGGGEGPPS 85
SPRY_PRY_TRIM7_like cd12888
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7)-like, including TRIM7, TRIM10, ...
467-596 1.34e-08

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: 54.49  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 467 FDPGSAHSDIILSNDNLTVTCSS-----------YD-DRVVLGKTGFSKGIHYWELTVDRYDNHpdpAFGVARMDVMK-- 532
Cdd:cd12888     4 LDPDTAHPRLVLSEDRKSVRWGDtrqdlpdnperFDtWPCVLGCEGFTSGRHYWEVEVGDGGGW---AVGVARESVRRkg 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1913184748 533 DVMLGKDDKAWAI-TEGGITKGAT--------------IGVLLDLNRKNLTFFiNDEQQGPIafdnvegLFFPAVSLNR 596
Cdd:cd12888    81 EISFSPEEGIWAVgQWGGQYWALTspetplplsevprrIRVYLDYEGGQVAFF-DADNEAPI-------FTFPPASFAG 151
RING-HC_MID1 cd16753
RING finger, HC subclass, found in midline-1 (MID1) and similar proteins; MID1, also known as ...
4-47 2.13e-08

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: 51.19  E-value: 2.13e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1913184748   4 MEEELKCPVCGSFYREPIILPCSHNLCQACARNILVQTPESESP 47
Cdd:cd16753     2 LESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCASNES 45
RING-HC_TRIM69_C-IV cd16611
RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar ...
6-33 2.28e-08

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: 50.91  E-value: 2.28e-08
                          10        20
                  ....*....|....*....|....*...
gi 1913184748   6 EELKCPVCGSFYREPIILPCSHNLCQAC 33
Cdd:cd16611     3 EELHCPLCLDFFRDPVMLSCGHNFCQSC 30
RING-HC_TRIM59_C-V cd16763
RING finger, HC subclass, found in tripartite motif-containing protein 59 (TRIM59) and similar ...
5-38 3.01e-08

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: 50.29  E-value: 3.01e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1913184748   5 EEELKCPVCGSFYREPIILPCSHNLCQACARNIL 38
Cdd:cd16763     1 EEDLTCSVCYSLFEDPRVLPCSHTFCRNCLENIL 34
Bbox1_MID2_C-I cd19837
B-box-type 1 zinc finger found in midline-2 (MID2) and similar proteins; MID2, also known as ...
166-212 3.59e-08

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: 50.04  E-value: 3.59e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1913184748 166 LKCQLCEK-APKEATVMCEQCDVFYCDPCRLRCHPPRGPLAKHRLVPP 212
Cdd:cd19837     3 IACQFCEQePPRDAVKTCITCEVSYCDRCLRATHPNKKPFTSHRLVEP 50
Bbox1_MID1_C-I cd19836
B-box-type 1 zinc finger found in midline-1 (MID1) and similar proteins; MID1, also termed ...
166-212 3.93e-08

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: 49.67  E-value: 3.93e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1913184748 166 LKCQLCEKAP-KEATVMCEQCDVFYCDPCRLRCHPPRGPLAKHRLVPP 212
Cdd:cd19836     3 VLCQFCDQDPaQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEP 50
SPRY_PRY cd12874
PRY/SPRY domain, also known as B30.2; This domain contains residues in the N-terminus that ...
467-570 5.37e-08

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: 52.69  E-value: 5.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 467 FDPGSAHSDIILSNDNLTVTCSSYDDR------------VVLGKTGFSKGIHYWEltVDRYDNHpDPAFGVA-----RMD 529
Cdd:cd12874     3 FDPDTAHLNLILSDDLRSVRVGDISQHppeppprffecwQVLGSQSFSSGRHYWE--VDVQDDS-SWYVGVTykslpRKG 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1913184748 530 VMkdVMLGKDDKAWAI---------------TEGGITKGATIGVLLDLNRKNLTFF 570
Cdd:cd12874    80 KM--SNLGRNNGSWCLewrenefsawhnnpeTRLPVTPPRRLGVFLDCDGGSLSFY 133
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
359-524 5.74e-08

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 55.78  E-value: 5.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 359 VQVKASSPVPATP-ILQLEEccTHNNSATLSWKQPplSTVPADGYILELDDGNGGQFREVY-VGKETMCTVDGLHFNSTY 436
Cdd:COG3401   318 VSVTTDLTPPAAPsGLTATA--VGSSSITLSWTAS--SDADVTGYNVYRSTSGGGTYTKIAeTVTTTSYTDTGLTPGTTY 393
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 437 NARVKAFNKTGV-SPYSKTLVLQTSEVA---WFAFDPGSAHSDIILSNDNLTVTCSSYDDRVVLGKTGFSKGIhYWELTV 512
Cdd:COG3401   394 YYKVTAVDAAGNeSAPSEEVSATTASAAsgeSLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGN-AVPFTT 472
                         170
                  ....*....|..
gi 1913184748 513 DRYDNHPDPAFG 524
Cdd:COG3401   473 TSSTVTATTTDT 484
RING-HC_TRIM25_C-IV cd16597
RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar ...
3-33 6.16e-08

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: 50.00  E-value: 6.16e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1913184748   3 EMEEELKCPVCGSFYREPIILPCSHNLCQAC 33
Cdd:cd16597     1 DLEEELTCSICLELFKDPVTLPCGHNFCGVC 31
RING-HC_TRIM13_like_C-V cd16581
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and ...
6-38 6.30e-08

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: 49.43  E-value: 6.30e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1913184748   6 EELKCPVCGSFYREPIILPCSHNLCQACARNIL 38
Cdd:cd16581     1 EELTCSICYNIFDDPKILPCSHTFCKNCLEKLL 33
SPRY_PRY_C-I_1 cd13733
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM5, TRIM6, TRIM7, ...
467-570 6.72e-08

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: 52.48  E-value: 6.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 467 FDPGSAHSDIILSNDNLTVTCSS-----------YDDRV-VLGKTGFSKGIHYWELTVdryDNHPDPAFGVARMDVMK-- 532
Cdd:cd13733     4 LDPDTAHPNLILSEDLKSVRYGDkrqnlpdnperFDTCVcVLGSEGFSSGRHYWEVEV---GGKTDWDLGVARESVNRkg 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1913184748 533 DVMLGKDDKAWAI--TEGGITKGAT--------------IGVLLDLNRKNLTFF 570
Cdd:cd13733    81 KITLSPENGYWTVglRNGNEYKALTspstplslrekpqkVGVFLDYEEGQVSFY 134
Bbox1 cd19757
B-box-type 1 zinc finger (Bbox1); The B-box-type zinc finger is a short zinc binding domain of ...
167-211 1.08e-07

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: 48.26  E-value: 1.08e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1913184748 167 KCQLCEKapKEATVMCEQCDVFYCDPCRLRCHPPRGPLAKHRLVP 211
Cdd:cd19757     1 LCDECEE--REATVYCLECEEFLCDDCSDAIHRRGKLTRSHKLVP 43
RING-HC_TRIM13_C-V cd16762
RING finger, HC subclass, found in tripartite motif-containing protein 13 (TRIM13) and similar ...
5-38 1.10e-07

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: 48.76  E-value: 1.10e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1913184748   5 EEELKCPVCGSFYREPIILPCSHNLCQACARNIL 38
Cdd:cd16762     1 EEDLTCPICCCLFDDPRVLPCSHNFCKKCLEGIL 34
RING-HC_TRIM36_C-I cd16756
RING finger, HC subclass, found in tripartite motif-containing protein 36 (TRIM36) and similar ...
5-42 1.11e-07

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: 48.37  E-value: 1.11e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1913184748   5 EEELKCPVCGSFYREPIILPCSHNLCQACARNILVQTP 42
Cdd:cd16756     1 ERELICPSCKELFTHPLILPCQHSVCHKCVKELLTTFP 38
Bbox2 cd19756
B-box-type 2 zinc finger (Bbox2); The B-box-type zinc finger is a short zinc binding domain of ...
229-266 1.50e-07

B-box-type 2 zinc finger (Bbox2); 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 interaction. Based on different consensus sequence 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). The family corresponds to type 2 B-box (Bbox2).


Pssm-ID: 380814 [Multi-domain]  Cd Length: 39  Bit Score: 47.79  E-value: 1.50e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1913184748 229 CTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKAL 266
Cdd:cd19756     2 CPEHPEEPLKLFCETCQELVCVLCLLSGEHRGHKVVPL 39
RING-HC_TRIM7-like_C-IV cd16594
RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM7, TRIM11 and ...
3-33 2.93e-07

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: 47.68  E-value: 2.93e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1913184748   3 EMEEELKCPVCGSFYREPIILPCSHNLCQAC 33
Cdd:cd16594     1 SLQEELTCPICLDYFTDPVTLDCGHSFCRAC 31
BBOX smart00336
B-Box-type zinc finger;
224-266 3.99e-07

B-Box-type zinc finger;


Pssm-ID: 197662 [Multi-domain]  Cd Length: 42  Bit Score: 46.56  E-value: 3.99e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1913184748  224 RKVSTCTDHELENHSMYCVQCKMPVCYQClEEGKHSSHEVKAL 266
Cdd:smart00336   1 QRAPKCDSHGDEPAEFFCEECGALLCRTC-DEAEHRGHTVVLL 42
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
359-460 7.25e-07

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 52.31  E-value: 7.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 359 VQVKASSPVPATPI-LQLEEccTHNNSATLSWkqPPLSTVPADGYILELDDGNGGQFREVYVGKETMCTVDGLHFNSTYN 437
Cdd:COG3401   224 VSVTTPTTPPSAPTgLTATA--DTPGSVTLSW--DPVTESDATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYY 299
                          90       100
                  ....*....|....*....|....
gi 1913184748 438 ARVKAFNKTGV-SPYSKTLVLQTS 460
Cdd:COG3401   300 YRVTAVDAAGNeSAPSNVVSVTTD 323
Bbox2_TRIM36_C-I cd19778
B-box-type 2 zinc finger found in tripartite motif-containing protein 36 (TRIM36) and similar ...
229-271 7.48e-07

B-box-type 2 zinc finger found in tripartite motif-containing protein 36 (TRIM36) and similar proteins; TRIM36, 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 through 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 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380836  Cd Length: 45  Bit Score: 45.99  E-value: 7.48e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1913184748 229 CTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKALGAMWK 271
Cdd:cd19778     3 CPEHEMEKVNMYCEACRRPVCHLCKLGGSHANHRVTSMSSAYK 45
SPRY_PRY_RNF135 cd12902
PRY/SPRY domain in RING finger protein RNF135; This domain, consisting of the distinct ...
467-576 8.23e-07

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: 49.44  E-value: 8.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 467 FDPGSAHSDIILSNDNLTVTCSS-------YDDRV----VLGKTGFSKGIHYWEltVD-RYDNHpdPAFGVARMDVMKDV 534
Cdd:cd12902     3 FDLRSLSCSLEVSEDSRKVTVSHgpqayawSPDRFsisqVLCSQAFSSGQHYWE--VDtRQCSH--WAVGVASWEMSRDQ 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1913184748 535 MLGKDDKAWAI----------------TEGGITKGATIGVLLDLNRKNLTFFINDEQQ 576
Cdd:cd12902    79 MLGRTMDSWCIewkgtgqlsawhmnkeTVLGSDKPRVVGIWLDLEEGKLAFYSVANQE 136
SPRY_PRY_TRIM18 cd12892
PRY/SPRY domain of TRIM18/MID1, also known as FXY or RNF59; This domain, consisting of the ...
465-610 9.53e-07

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: 49.24  E-value: 9.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 465 FAFDPGSAHSDIILSNDNLTVT--------------CSSYDDRVVLGKTGFSKGIHYWELTVDRYDNHpdpAFGVARMDV 530
Cdd:cd12892     2 FKLDPKSAHRKLKVSHDNLTVErdetsskkshtperFTSQGSYGVAGNVFIDSGRHYWEVVISGSTWY---AIGIAYKSA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 531 MKDVMLGKDDKAWAITEGGITKGA----------------TIGVLLDLNRKNLTFFINDEQQGPIAFDNVEGLFFPAVSL 594
Cdd:cd12892    79 PKHEWIGKNSASWVLCRCNNNWVVrhnskeipiepsphlrRVGILLDYDNGSLSFYDALNSIHLYTFDIAFAQPVCPTFT 158
                         170
                  ....*....|....*.
gi 1913184748 595 NRNVQVTLHTGLPVPD 610
Cdd:cd12892   159 VWNKCLTILTGLPIPD 174
Bbox1_TRIM36-like cd19807
B-box-type 1 zinc finger found in tripartite motif-containing proteins, TRIM36, TRIM46 and ...
165-212 1.20e-06

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: 45.58  E-value: 1.20e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1913184748 165 ALKCQLCEKAPKEATVMCEQCDVFYCDPCRLRCHPPRGPLAKHRLVPP 212
Cdd:cd19807     1 AIKCQLCKPPPQEATKSCADCVASFCNECFKVVHPWGTPKAQHEYVGP 48
RING-HC_TRIM8_C-V cd16580
RING finger, HC subclass, found in tripartite motif-containing protein 8 (TRIM8) and similar ...
5-33 1.20e-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: 46.04  E-value: 1.20e-06
                          10        20
                  ....*....|....*....|....*....
gi 1913184748   5 EEELKCPVCGSFYREPIILPCSHNLCQAC 33
Cdd:cd16580     9 EEELICPICLHVFVEPVQLPCKHNFCRGC 37
SPRY_PRY_A33L cd12905
zinc-binding protein A33-like; This domain, consisting of the distinct N-terminal PRY ...
467-593 1.54e-06

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: 48.95  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 467 FDPGSAHSDIILSNDnLTVTCSSYDDRV-------------VLGKTGFSKGIHYWELTVdryDNHPDPAFGVARMDVMKD 533
Cdd:cd12905     8 FDPETAHPSLILSRD-LTAVTESDEMQPyprspkrflqcvnVLASQGFQSGRHYWEVWV---GSKTKWDLGVASESVDRQ 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1913184748 534 VM-------------LGKDDKAWAITEGGI-----TKGATIGVLLDLNRKNLTFFINDEQQGPIAFDN-VEGLFFPAVS 593
Cdd:cd12905    84 ARvklcpengywtlrLRNGDEYWAGTQPWTrlrvtSRPQRIGVFLDCEERKVSFYNADDMSLLYSFHQgPRGKVFPFFS 162
SPRY_PRY_RFPL cd15821
Ret finger protein-like (RFPL), includes RFP1, 2, 3, 4; This domain, consisting of the ...
467-570 4.21e-06

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: 47.31  E-value: 4.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 467 FDPGSAHSDIILSNDNLTVTCSS-----------YDDRV-VLGKTGFSKGIHYWELTVDR---YDnhpdpaFGVARMDV- 530
Cdd:cd15821     8 LDVDTANNYLIISEDLRSVRCGCfrqnrkelaerFDDALcVLGSPRFTSGRHYWEVDVGTsteWD------LGVCRESVn 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1913184748 531 -MKDVMLGKDDKAWAIT--EGGI----TKGAT----------IGVLLDLNRKNLTFF 570
Cdd:cd15821    82 rQGPIELSPEHGFWTVSlrDGSVffasTVPLTvlwvnprlhrVGIFLDMEMGTISFY 138
BBOX smart00336
B-Box-type zinc finger;
163-211 4.24e-06

B-Box-type zinc finger;


Pssm-ID: 197662 [Multi-domain]  Cd Length: 42  Bit Score: 43.87  E-value: 4.24e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1913184748  163 AAALKCQLCEKAPkeATVMCEQCDVFYCDPCRLRCHpprgplAKHRLVP 211
Cdd:smart00336   1 QRAPKCDSHGDEP--AEFFCEECGALLCRTCDEAEH------RGHTVVL 41
RING-HC_MuRF2 cd16760
RING finger, HC subclass, found in muscle-specific RING finger protein 2 (MuRF-2) and similar ...
5-38 5.49e-06

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: 44.21  E-value: 5.49e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1913184748   5 EEELKCPVCGSFYREPI-ILPCSHNLCQACARNIL 38
Cdd:cd16760     1 EKQLICPICLEMFTKPVvILPCQHNLCRKCANDIF 35
RING-HC_TRIM4_C-IV cd16590
RING finger, HC subclass, found in tripartite motif-containing protein TRIM4 and similar ...
2-33 6.91e-06

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: 43.87  E-value: 6.91e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1913184748   2 EEMEEELKCPVCGSFYREPIILPCSHNLCQAC 33
Cdd:cd16590     1 EDIQEELTCPICLDYFQDPVSIECGHNFCRGC 32
RING-HC_MID_C-I cd16575
RING finger, HC subclass, found in midline-1 (MID1), midline-2 (MID2) and similar proteins; ...
8-39 7.29e-06

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: 43.38  E-value: 7.29e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1913184748   8 LKCPVCGSFYREPIILPCSHNLCQACARNILV 39
Cdd:cd16575     1 LTCPICLELFEDPLLLPCAHSLCFNCAHRILV 32
SPRY_PRY_TRIM62 cd13744
PRY/SPRY domain in tripartite motif-binding protein 62 (TRIM62); This domain, consisting of ...
453-512 7.53e-06

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: 46.92  E-value: 7.53e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1913184748 453 KTLVLQTSEV-AWFAFDPGSAHSDIILSNDNLTVTCSS------------YDDRV-VLGKTGFSKGIHYWELTV 512
Cdd:cd13744     1 KSLFQDIHPVpAALTLDPVTAHQRLILSDDCTIVAYGNlhpqplqdspkrFDVEVsVLGSEGFSGGVHYWEVVV 74
Bbox1_TRIM36_C-I cd19848
B-box-type 1 zinc finger found in tripartite motif-containing protein 36 (TRIM36) and similar ...
163-212 7.99e-06

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: 43.51  E-value: 7.99e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1913184748 163 AAALKCQLCEKAPKEATVMCEQCDVFYCDPCRLRCHPPRGPLAKHRLVPP 212
Cdd:cd19848     2 ATAIMCDLCKPPPQESTKSCMDCKASYCNECFKIHHPWGTPKAQHEYVGP 51
Bbox_SF cd00021
B-box-type zinc finger superfamily; The B-box-type zinc finger is a short zinc binding domain ...
229-266 8.01e-06

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: 42.97  E-value: 8.01e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1913184748 229 CTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKAL 266
Cdd:cd00021     2 CQEHDEEKANKYCVTCEVLYCALCKKSGAHPDHEVAPL 39
RING-HC_MuRF1 cd16759
RING finger, HC subclass, found in muscle-specific RING finger protein 1 (MuRF-1) and similar ...
5-38 8.11e-06

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: 43.86  E-value: 8.11e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1913184748   5 EEELKCPVCGSFYREPI-ILPCSHNLCQACARNIL 38
Cdd:cd16759     1 EKQLICPICLEMFTKPVvILPCQHNLCRKCANDIF 35
RING-HC_RNF39 cd16592
RING finger, HC subclass, found in RING finger protein 39 (RNF39) and similar proteins; RNF39, ...
4-33 9.80e-06

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: 43.21  E-value: 9.80e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 1913184748   4 MEEELKCPVCGSFYREPIILPCSHNLCQAC 33
Cdd:cd16592     1 LQEETTCPICLGYFKDPVILDCEHSFCRAC 30
SPRY_PRY_BTN1_2 cd15819
butyrophilin subfamily member A1 and A2 (BTN1A and BTN2A); This domain, consisting of the ...
468-545 1.12e-05

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: 46.07  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 468 DPGSAHSDIILSNDNLTVTCSSY------------DDRVVLGKTGFSKGIHYWELTVdryDNHPDPAFGVARMDVMKD-- 533
Cdd:cd15819     7 DPDTAHPALILSEDGRSVTWGETrqdlpenperfdSLPCVLGQEGFTSGRHYWEVEV---GDRTSWDLGVCRDNVMRKgr 83
                          90
                  ....*....|..
gi 1913184748 534 VMLGKDDKAWAI 545
Cdd:cd15819    84 VTLSPENGFWAI 95
RING-HC_TRIM35_C-IV cd16599
RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar ...
5-33 1.17e-05

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


Pssm-ID: 438261 [Multi-domain]  Cd Length: 66  Bit Score: 43.22  E-value: 1.17e-05
                          10        20
                  ....*....|....*....|....*....
gi 1913184748   5 EEELKCPVCGSFYREPIILPCSHNLCQAC 33
Cdd:cd16599     2 KEELLCPICYEPFREAVTLRCGHNFCKGC 30
SPRY_PRY_TRIM15 cd15826
PRY/SPRY domain in tripartite motif-binding protein 15 (TRIM15); This domain, consisting of ...
468-579 1.26e-05

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: 46.01  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 468 DPGSAHSDIILSNDNLTVTCSS-----------YD-DRVVLGKTGFSKGIHYWELTVDRYDNHpDPAFGVARMDVMK--D 533
Cdd:cd15826     5 DPQTASGSLVLSEDRKSVRYTRqkqnlpdsplrFDgLPAVLGSPGFSSGRHRWQVEVQLGDGG-GCTVGVAGESVRRkgE 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1913184748 534 VMLGKDDKAWA--ITEGGI----TKGAT---------IGVLLDLNRKNLTfFINDEQQGPI 579
Cdd:cd15826    84 MGLSAEDGVWAviLSHQQCwastSPGTDlplseiprrVGVALDYEAGTVT-LTNAETQEPI 143
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
8-38 1.30e-05

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


Pssm-ID: 438113 [Multi-domain]  Cd Length: 41  Bit Score: 42.47  E-value: 1.30e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1913184748   8 LKCPVCGSFYREPIILPCSHNLCQACARNIL 38
Cdd:cd16449     1 LECPICLERLKDPVLLPCGHVFCRECIRRLL 31
RING-HC_TRIM45_C-VII cd16588
RING finger, HC subclass, found in tripartite motif-containing protein 45 (TRIM45) and similar ...
10-35 1.43e-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: 42.89  E-value: 1.43e-05
                          10        20
                  ....*....|....*....|....*.
gi 1913184748  10 CPVCGSFYREPIILPCSHNLCQACAR 35
Cdd:cd16588     3 CPVCGKLFQEPRLLPCLHTLCSPCLR 28
SPRY_PRY_TRIM50 cd13743
PRY/SPRY domain in tripartite motif-binding protein 50 (TRIM50); This domain, consisting of ...
467-579 1.54e-05

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: 45.95  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 467 FDPGSAHSDIILSNDNLTVTCSSYDDRV------------VLGKTGFSKGIHYWELTVdryDNHPDPAFGVARMDVMKDV 534
Cdd:cd13743    16 LDPLTAHPMLELSKGNTVVECGLLAQRLpsnperfdysncVLASRGFSSGKHYWEVVV---GSKSKWRLGLIKGTTSRKG 92
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1913184748 535 MLGK--DDKAWAI--TEGGI--------------TKGATIGVLLDLNRKNLTFFINDEQQ--GPI 579
Cdd:cd13743    93 KLNKspENGVWLIglKEGRVyeafanprvplplsTRPQRIGVFLDYEKGELTFYNADSPDelVPI 157
RING-HC_TRIM26_C-IV cd16598
RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar ...
4-47 1.54e-05

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: 42.84  E-value: 1.54e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1913184748   4 MEEELKCPVCGSFYREPIILPCSHNLCQACARNILVQTPESESP 47
Cdd:cd16598     1 LEEEVTCSICLDYLRDPVTIDCGHNFCRSCITDYCPISGGHERP 44
SPRY_PRY_TRIM50_72 cd12897
PRY/SPRY domain in tripartite motif-binding (TRIM) proteins TRIM50 and TRIM72; This domain, ...
467-525 1.67e-05

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: 46.07  E-value: 1.67e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1913184748 467 FDPGSAHSDIILSNDNLTVTCSSYDDRV------------VLGKTGFSKGIHYWELTVdryDNHPDPAFGV 525
Cdd:cd12897    16 FDPATAHPLLVVSSGGTVVECGLQKQRRasqperfdkstcVVASQGFSEGEHYWEVVV---GDKPRWALGV 83
zf-B_box pfam00643
B-box zinc finger;
224-266 2.13e-05

B-box zinc finger;


Pssm-ID: 459886 [Multi-domain]  Cd Length: 42  Bit Score: 41.69  E-value: 2.13e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1913184748 224 RKVSTCTDHELENHSMYCVQCKMPVCYQCLeEGKHSSHEVKAL 266
Cdd:pfam00643   1 SKERLCPEHEEEPLTLYCNDCQELLCEECS-VGEHRGHTVVPL 42
SPRY_PRY_SPRYD4 cd12903
PRY/SPRY domain containing protein 4 (SPRYD4); This domain, consisting of the distinct ...
494-543 2.33e-05

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: 45.13  E-value: 2.33e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1913184748 494 VVLGKTGFSKGIHYWELTVDRYDNHpdpAFGVARMDVMKDVMLGKDDKAW 543
Cdd:cd12903    45 VVLGDTPVTSGRHYWEVTVKRSQEF---RIGVADVDMSRDECIGTNESSW 91
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
523-605 2.45e-05

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


Pssm-ID: 240458  Cd Length: 133  Bit Score: 44.21  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 523 FGVARMDVMKDVMLGKDDKAWAIT--------EGGIT------KGATIGVLLDLNRKNLTFFIN-----DEQQGPIAFDN 583
Cdd:cd12878    30 VGWARPGFRPDLELGSDDLSYAFDgflarkwhQGSESfgkqwqPGDVVGCMLDLVDRTISFTLNgelliDSSGSEVAFKD 109
                          90       100
                  ....*....|....*....|....
gi 1913184748 584 VEGL--FFPAVSLNRNVQVTLHTG 605
Cdd:cd12878   110 IEIGegFVPACSLGVGQKGRLNLG 133
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
553-605 2.50e-05

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


Pssm-ID: 293940  Cd Length: 128  Bit Score: 44.24  E-value: 2.50e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1913184748 553 GATIGVLLDLNRKNLTFFINDEQQGpIAFDNVEGL----FFPAVSLNRNVQVTLHTG 605
Cdd:cd12882    73 GDVIGCCIDLDKGTISFYRNGRSLG-VAFDNVRRGpglaYFPAVSLSFGERLELNFG 128
Bbox1_TRIM46_C-I cd19849
B-box-type 1 zinc finger found in tripartite motif-containing protein 46 (TRIM46) and similar ...
165-212 2.86e-05

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: 41.93  E-value: 2.86e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1913184748 165 ALKCQLCEKAPKEATVMCEQCDVFYCDPCRLRCHPPRGPLAKHRLVPP 212
Cdd:cd19849     1 AIMCQFCKPPQLEATKGCTECRASFCNECFKLYHPWGTQKAQHEPTPP 48
SPRY_PRY_TRIM35 cd12893
PRY/SPRY domain in tripartite motif-containing protein 35 (TRIM35); This PRY/SPRY domain is ...
465-530 4.05e-05

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: 44.54  E-value: 4.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1913184748 465 FAFDPGSAHSDIILSNDNLTVTCSSY-----------DDRV-VLGKTGFSKGIHYWELTVdryDNHPDPAFGVARMDV 530
Cdd:cd12893     2 VTLDPNTAHPWLSLSEDLTSVRYSSEkqqlpdnperfDPYPcVLGSEGFTSGKHSWDVEV---GDNTSWMLGVAKESV 76
SPRY_PRY_TRIM76_like cd12899
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76)-like; This domain is ...
464-606 4.47e-05

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: 44.39  E-value: 4.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 464 WFAFDPGSAHSDIILSNDNLTVTCSS----------YDDR-----VVLGKTGFSKGIHYWELTVdryDNHPDPAFGVARM 528
Cdd:cd12899     1 YFHLNEDTAHPLLSISEDGFTVVYGEeelpardlsfSDNSftrcvAVMGSLIPVRGKHYWEVEV---DEQTEYRVGVAFE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 529 DVMKDVMLGKDDKAWAITEgGIT----------KGAT-----------IGVLLDLNRKNLTFFINDEQQGPIAFD-NVEG 586
Cdd:cd12899    78 DTQRNGYLGANNTSWCMRH-IITpsrhkyeflhNGWTpdiritvppkkIGILLDYDSGRLSFFNVDLAQHLYTFScQFQH 156
                         170       180
                  ....*....|....*....|
gi 1913184748 587 LFFPAVSLNRNVQVTLHTGL 606
Cdd:cd12899   157 FVHPCFSLEKPGALKVHNGI 176
Bbox2_MID cd19758
B-box-type 2 zinc finger found in midline (MID) family; The MID family includes MID1 and MID2. ...
228-266 5.73e-05

B-box-type 2 zinc finger found in 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 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, 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 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380816  Cd Length: 40  Bit Score: 40.53  E-value: 5.73e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1913184748 228 TCTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKAL 266
Cdd:cd19758     2 MCSEHEEEKVNMYCLTDDQLICSLCKLVGKHKDHEVAAL 40
RING-HC_MuRF3 cd16761
RING finger, HC subclass, found in muscle-specific RING finger protein 3 (MuRF-3) and similar ...
8-38 6.92e-05

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: 40.79  E-value: 6.92e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1913184748   8 LKCPVCGSFYREPI-ILPCSHNLCQACARNIL 38
Cdd:cd16761     1 LICPICLEMFTKPVvILPCQHNLCRKCANDVF 32
RING-HC_AtBARD1-like cd23146
RING finger, HC subclass, found in Arabidopsis thaliana BRCA1-associated RING domain protein 1 ...
4-33 7.37e-05

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: 40.53  E-value: 7.37e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1913184748   4 MEEELKCPVCGSFYREPIILPCSHNLCQAC 33
Cdd:cd23146     1 MELELKCPICLKLLNRPVLLPCDHIFCSSC 30
SPRY_SOCS_Fbox cd12875
SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins; This family ...
466-593 7.46e-05

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: 43.60  E-value: 7.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 466 AFDPGSAHSDIILSNDNLT-----VTCSSYDDRvvlGKTGFSKGIHYWELTVDRYDNHPDPAFGVARMD--VMKD---VM 535
Cdd:cd12875     2 GWNPADCSKNIYIKEDGLTfhrrpVAQSTDAIR---GKKGYTRGLHAWEVKWISRPRGSHAVVGVATKDapLQCDgyvTL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1913184748 536 LGKDDKAWA--ITEGGITKGA------------------TIGVLLDLNRKNLTFFINDEQQGpIAFDNVEG-LFFPAVS 593
Cdd:cd12875    79 LGSNSESWGwdLGDNKLYHNGkkvigsypaksenyqvpdRILVILDMEDGTLAFEANGEYLG-VAFRGLPGkLLYPAVS 156
RING-HC_TRIM39_C-IV cd16601
RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar ...
7-33 7.71e-05

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: 40.16  E-value: 7.71e-05
                          10        20
                  ....*....|....*....|....*..
gi 1913184748   7 ELKCPVCGSFYREPIILPCSHNLCQAC 33
Cdd:cd16601     1 EASCSLCKEYLKDPVIIECGHNFCRAC 27
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
4-42 8.42e-05

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: 45.38  E-value: 8.42e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1913184748   4 MEEELKCPVCGSFYREPIILPCSHNLCQACARNILVQTP 42
Cdd:TIGR00599  23 LDTSLRCHICKDFFDVPVLTSCSHTFCSLCIRRCLSNQP 61
RING-HC_MuRF_C-II cd16577
RING finger, HC subclass, found in muscle-specific RING finger proteins TRIM63/MuRF-1, TRIM55 ...
8-54 9.32e-05

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: 40.65  E-value: 9.32e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1913184748   8 LKCPVCGSFYREPI-ILPCSHNLCQACARNILvQTPESESPQSHRAAG 54
Cdd:cd16577     1 LICPICLEMFTKPVvILPCQHNLCRKCANDIF-QARNPYWPTTTMGSG 47
SPRY_PRY_TRIM7 cd13740
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7); This domain, consisting of the ...
468-549 1.32e-04

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: 43.02  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 468 DPGSAHSDIILSNDNLTV------------TCSSYDDRVVLGKTGFSKGIHYWELTVDRYDNHpdpAFGVARMDVMKDVM 535
Cdd:cd13740     5 DPDSANPRLILSLDLKSVrlgeraqdlpnhPCRFDTNTRVLASCGFSSGRHHWEVEVGSKDGW---AFGVARESVRRKGL 81
                          90
                  ....*....|....*.
gi 1913184748 536 --LGKDDKAWAITEGG 549
Cdd:cd13740    82 tpFTPEEGVWALQLNG 97
SPRY_PRY_TRIM39 cd13745
PRY/SPRY domain in tripartite motif-binding protein 39 (TRIM39) and TRIM39-like; This domain, ...
467-530 1.81e-04

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: 42.61  E-value: 1.81e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1913184748 467 FDPGSAHSDIILSNDNLTVTC-SSYDDR-----------VVLGKTGFSKGIHYWELTVdryDNHPDPAFGVARMDV 530
Cdd:cd13745     7 LDPDTAHPNLVLSEDRKSVRHgDTRQDLpdnperfdtypCVLGAEGFTGGRHYWEVEV---GDKTEWTLGVCRESV 79
SPRY_PRY_TRIM65 cd12896
PRY/SPRY domain in tripartite motif-containing domain 65 (TRIM65); This domain, consisting of ...
467-602 1.95e-04

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: 42.82  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 467 FDPGSAHSDIILSNDNLTVT------------CSSYDDRVVLGKTGFSKGIHYWELTVdrydNHPDPAFGVA-------R 527
Cdd:cd12896    14 FDPRTANKYLELSRQNRRAKhgrsaargvpasPGSFELWQVQCTQSFQHGHHYWEVEV----SSHSVTLGVTypglprhK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 528 MDVMKDvMLGKDDKAWA--ITEGGIT-------------KGATIGVLLDLNRKNLTFFINDEQQGPI-AFDNV--EGLfF 589
Cdd:cd12896    90 QGGHKD-NIGRNPCSWGlqIQEDSLQawhngraqklqgvSYRLLGVDLDLEAGTLTFYGLEPGTQRLhTFHAIftQPL-Y 167
                         170
                  ....*....|...
gi 1913184748 590 PAVSLNRNVQVTL 602
Cdd:cd12896   168 PVFWLLEGRTLTL 180
SPRY_HERC1 cd12881
SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to ...
466-602 2.23e-04

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


Pssm-ID: 293939  Cd Length: 162  Bit Score: 41.95  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 466 AFDPgSAHSDIILSNDNLTVTCSSYDDRVVLGKT--GFSKGIHYWELTVDRyDNHPDPA--FGVARMDVmKDVMLGKDDK 541
Cdd:cd12881     3 SFDP-EKSTNCVVVENGGTLVHSSGGRGYGLAATwiGISSGCYQWKFYLVK-ENRGNEGtcVGVSRKPV-TDFNYRTSSD 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1913184748 542 AWAI----------------TEGGITKGATIGVLLDLNRKNLTFFINDEQQGpIAFDNVEGL-FFPAVSLNRNVQVTL 602
Cdd:cd12881    80 MWLYrayngnlyhngeqllrLSSKFHQGDYITVVLDMEEGTLSFGKNGEEPG-VAFEDVDATeLYPCVMFYSSGPGEK 156
RING-HC_TRIM5-like_C-IV cd16591
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, ...
2-46 2.26e-04

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: 39.73  E-value: 2.26e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1913184748   2 EEMEEELKCPVCGSFYREPIILPCSHNLCQAC--ARNILVQTPESES 46
Cdd:cd16591     1 VNIKEEVTCPICLELLTEPLSLDCGHSFCQACitANHKESVNQEGES 47
RING-HC_TRIM68_C-IV cd16610
RING finger, HC subclass, found in tripartite motif-containing protein 68 (TRIM68) and similar ...
7-33 2.41e-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: 39.11  E-value: 2.41e-04
                          10        20
                  ....*....|....*....|....*..
gi 1913184748   7 ELKCPVCGSFYREPIILPCSHNLCQAC 33
Cdd:cd16610     1 EVACPICMTFLREPVSIDCGHSFCHSC 27
RING-HC_TRIM10_C-IV cd16593
RING finger, HC subclass, found in tripartite motif-containing protein 10 (TRIM10) and similar ...
3-47 2.54e-04

RING finger, HC subclass, found in tripartite motif-containing protein 10 (TRIM10) and similar proteins; TRIM10, also known as B30-RING finger protein (RFB30), RING finger protein 9 (RNF9), or hematopoietic RING finger 1 (HERF1), is a novel hematopoiesis-specific RING finger protein required for terminal differentiation of erythroid cells. TRIM10 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: 438255 [Multi-domain]  Cd Length: 61  Bit Score: 39.51  E-value: 2.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1913184748   3 EMEEELKCPVCGSFYREPIILPCSHNLCQAC-ARNILVQTPESESP 47
Cdd:cd16593     1 SLADEVNCPICQGTLREPVTIDCGHNFCRAClTRYCEIPGPDLEEP 46
SPRY_PRY_TRIM69 cd15818
PRY/SPRY domain in tripartite motif-binding protein 69 (TRIM69), also known as RING finger ...
468-512 2.56e-04

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: 42.48  E-value: 2.56e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 468 DPGSAHSDIILSNDnltVTCSSYDDR---------------VVLGKTGFSKGIHYWELTV 512
Cdd:cd15818    18 DPKTAHPNLILSED---LTCVWHGDTkqmlpdnperfdssvAVLGSEGFTSGKHYWEVEV 74
SPRY_PRY_TRIM14 cd13738
PRY/SPRY domain of tripartite motif-binding protein 14 (TRIM14); This is a TRIM14 domain ...
467-514 2.71e-04

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: 42.08  E-value: 2.71e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 467 FDPGSAHSDIILSNDNLTVTCS-----------SYDD-RVVLGKTGFSKGIHYWELTVDR 514
Cdd:cd13738     3 LEPDTLHPRLRLSDDRLTVSCGwlgtlglcppqRFDKlWQVLSRDSFFSGRHYWEVDLQE 62
RING-HC_TRIM41-like_C-IV cd16602
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and ...
5-33 2.93e-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: 39.14  E-value: 2.93e-04
                          10        20
                  ....*....|....*....|....*....
gi 1913184748   5 EEELKCPVCGSFYREPIILPCSHNLCQAC 33
Cdd:cd16602     1 QEEAVCAICLDYFKDPVSIGCGHNFCRVC 29
RING-HC_TRIM21_C-IV cd16596
RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar ...
1-33 3.09e-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: 39.50  E-value: 3.09e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1913184748   1 MEEMEEELKCPVCGSFYREPIILPCSHNLCQAC 33
Cdd:cd16596     3 LTMMWEEVTCPICLDPFVEPVSIECGHSFCQEC 35
RING-HC_RNF168 cd16550
RING finger, HC subclass, found in RING finger protein 168 (RNF168) and similar proteins; ...
10-33 3.28e-04

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


Pssm-ID: 438212 [Multi-domain]  Cd Length: 48  Bit Score: 38.51  E-value: 3.28e-04
                          10        20
                  ....*....|....*....|....
gi 1913184748  10 CPVCGSFYREPIILPCSHNLCQAC 33
Cdd:cd16550     3 CPICLEILVEPVTLPCNHTLCMPC 26
Bbox2_TRIM37_C-VIII cd19779
B-box-type 2 zinc finger found in tripartite motif-containing protein 37 (TRIM37) and similar ...
227-266 3.31e-04

B-box-type 2 zinc finger found in tripartite motif-containing protein 37 (TRIM37) and similar proteins; TRIM37, also known as Mulibrey nanism protein, 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 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, 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. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380837  Cd Length: 40  Bit Score: 38.46  E-value: 3.31e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1913184748 227 STCTDHElENHSMYCVQCKMPVCYQC-LEEGKHSSHEVKAL 266
Cdd:cd19779     1 DKCETHN-EKLSVYCWTCKKCICHQCaLWGGTHSGHTFKPL 40
PRY pfam13765
SPRY-associated domain; PRY is a 50-60 amino acids domain associated with SPRY domains, ...
467-501 3.56e-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: 38.61  E-value: 3.56e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1913184748 467 FDPGSAHSDIILSNDNLTVTCSS-----------YDDRV-VLGKTGF 501
Cdd:pfam13765   3 LDPNTAHPSLVLSEDLKSVRYGDerqnvpdnperFDSWPcVLGSEGF 49
SPRY_PRY_TRIM72 cd13742
PRY/SPRY domain in tripartite motif-binding protein 72 (TRIM72); This domain, consisting of ...
466-525 4.64e-04

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: 41.77  E-value: 4.64e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1913184748 466 AFDPGSAHSDIILSNDNLTVTCS------SYDD-------RVVLGKTGFSKGIHYWELTVdryDNHPDPAFGV 525
Cdd:cd13742    15 TFDPDTAHPYLVVSSDGKRVECAdqkqavSSDDpnrfdkaNCVVSHQSFSEGEHYWEVIV---GDKPRWALGV 84
Bbox2_TRIM23_C-IX_rpt1 cd19773
first B-box-type 2 zinc finger found in tripartite motif-containing protein 23 (TRIM23) and ...
177-211 4.71e-04

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: 38.47  E-value: 4.71e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1913184748 177 EATVMCEQCDVFYCDPCRLRCHPPRgPLAKHRLVP 211
Cdd:cd19773    12 EATLYCTVCSTNLCEECFTSTHSTK-TLSKHRRVP 45
Bbox2_MID2_C-I cd19823
B-box-type 2 zinc finger found in midline-2 (MID2) and similar proteins; MID2, also known as ...
228-266 5.00e-04

B-box-type 2 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 that associate 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. It heterodimerizes in vitro with its paralog MID1. Loss-of-function mutations in MID2 lead to the 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 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380881  Cd Length: 40  Bit Score: 38.03  E-value: 5.00e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1913184748 228 TCTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKAL 266
Cdd:cd19823     2 TCLEHENEKVNMYCVVDDQLICALCKLVGRHRDHQVASL 40
mRING-HC-C3HC3D_TRAF7 cd16644
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
6-34 6.17e-04

Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 7 (TRAF7) and similar proteins; TRAF7, also known as RING finger and WD repeat-containing protein 1 or RING finger protein 119 (RNF119), is an E3 ubiquitin-protein ligase involved in signal transduction pathways that lead either to activation or repression of NF-kappaB transcription factor by promoting K29-linked ubiquitination of several cellular targets, including the NF-kappaB essential modulator (NEMO) and the p65 subunit of NF-kappaB transcription factor. It is also involved in K29-linked polyubiquitination that has been implicated in lysosomal degradation of proteins. Moreover, TRAF7 is required for K48-linked ubiquitination of p53, a key tumor suppressor and a master regulator of various signaling pathways, such as those related to apoptosis, cell cycle and DNA repair. It is also required for tumor necrosis factor alpha (TNFalpha)-induced Jun N-terminal kinase activation and promotes cell death by regulating polyubiquitination and lysosomal degradation of c-FLIP protein. Furthermore, TRAF7 functions as small ubiquitin-like modifier (SUMO) E3 ligase involved in other post-translational modification, such as sumoylation. It binds to and stimulates sumoylation of the proto-oncogene product c-Myb, a transcription factor regulating proliferation and differentiation of hematopoietic cells. It potentiates MEKK3-induced AP1 and CHOP activation and induces apoptosis. Meanwhile, TRAF7 mediates MyoD1 regulation of the pathway and cell-cycle progression in myoblasts. It also plays a role in Toll-like receptors (TLR) signaling. TRAF7 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and an adjacent zinc finger, and a unique C-terminal domain that comprises a coiled coil domain and seven WD40 repeats.


Pssm-ID: 438306 [Multi-domain]  Cd Length: 47  Bit Score: 37.72  E-value: 6.17e-04
                          10        20
                  ....*....|....*....|....*....
gi 1913184748   6 EELKCPVCGSFYREPIILPCSHNLCQACA 34
Cdd:cd16644     4 VKLYCPLCQRVFKDPVITSCGHTFCRRCA 32
SPRY_PRY_TRIM60 cd15828
PRY/SPRY domain of tripartite motif-binding protein 60 (TRIM60) also known as RING finger ...
467-527 6.20e-04

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: 41.12  E-value: 6.20e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1913184748 467 FDPGSAHSDIILSNDNLTVTCSSYDDRV------------VLGKTGFSKGIHYWELTVdryDNHPDPAFGVAR 527
Cdd:cd15828    14 LDPETAHPQLTVSEDRKSVLYGEMKQNVcynprrfylcpaVLGSEGFHSGRQYWEVEV---GDKPEWTLGVCQ 83
SPRY_PRY_TRIM20 cd15813
PRY/SPRY domain in tripartite motif-binding protein 20 (TRIM20), also known as pyrin; This ...
468-512 6.43e-04

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: 41.28  E-value: 6.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1913184748 468 DPGSAHSDIILSNDNLTVTCSSYDDRV------------VLGKTGFSKGIHYWELTV 512
Cdd:cd15813    14 DPETAHPNLIFSDDLKSVRLGNKWDRLpdnperfdsciiVLGSPSFTSGRHYWEVEV 70
SPRY_PRY_TRIM25 cd13736
PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25); This domain, consisting of ...
467-591 7.94e-04

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: 40.64  E-value: 7.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 467 FDPGSAHSDIILSNDNLTVTCS-------SYDDRV-----VLGKTGFSKGIHYWELTVDRyDNHPDPAFGVARMDVM-KD 533
Cdd:cd13736     3 FDYNTAHNKVSLSENYTKASVSddpqnyrEHPQRFtycsqVLGLHCFKQGIHYWEVELQK-NNFCGVGICYGSMDRQgPE 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1913184748 534 VMLGKDDKAWAITEGGI---------------TKGATIGVLLDLNRKNLTFFINDEQQGPI---AFDNVEGLfFPA 591
Cdd:cd13736    82 SRLGRNSESWCVEWFNVkisawhnnvektlpsTKATRVGVLLNCDHGFVIFFAVQDKVHLMykfKVDFTEAL-YPA 156
Bbox2_MuRF3_C-II cd19833
B-box-type 2 zinc finger found in muscle-specific RING finger protein 3 (MuRF-3) and similar ...
229-269 7.94e-04

B-box-type 2 zinc finger 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, and 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 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, 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. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380891  Cd Length: 43  Bit Score: 37.36  E-value: 7.94e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1913184748 229 CTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKALGAM 269
Cdd:cd19833     3 CEEHEEEKINIYCLSCEVPTCSLCKVFGAHKDCEVAPLPTV 43
RING-HC_RAD18 cd16529
RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; ...
4-35 8.37e-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: 37.67  E-value: 8.37e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1913184748   4 MEEELKCPVCGSFYR-EPIILPCSHNLCQACAR 35
Cdd:cd16529     1 LDDLLRCPICFEYFNtAMMITQCSHNYCSLCIR 33
RING-HC_NHL-1-like cd16524
RING finger, HC subclass, found in Caenorhabditis elegans RING finger protein NHL-1 and ...
3-31 8.52e-04

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: 37.79  E-value: 8.52e-04
                          10        20
                  ....*....|....*....|....*....
gi 1913184748   3 EMEEELKCPVCGSFYREPIILPCSHNLCQ 31
Cdd:cd16524     1 QIEQLLTCPICLDRYRRPKLLPCQHTFCL 29
SPRY_PRY_TRIM38 cd15815
PRY/SPRY domain of tripartite motif-binding protein 38 (TRIM38), also known as Ring finger ...
468-545 1.19e-03

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: 40.41  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 468 DPGSAHSDIILSNDNLTVTCSS------------YDDRVVLGKTGFSKGIHYWELTVD---RYDnhpdpaFGVARMDVMK 532
Cdd:cd15815    18 DPDTAHPELTLSKDQRQVTYGRcqenldaspkrfTVLPCVLGCEGFTSGRHYFEVDVGegtGWD------VGVCLENVQR 91
                          90
                  ....*....|....*
gi 1913184748 533 DVMLGKDDKA--WAI 545
Cdd:cd15815    92 GFGMKQEPEFgfWTI 106
Bbox2_MuRF cd19788
B-box-type 2 zinc finger found in muscle-specific RING finger protein (MuRF) family; This ...
228-266 1.25e-03

B-box-type 2 zinc finger found in muscle-specific RING finger protein (MuRF) family; This family 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 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, 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. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380846  Cd Length: 39  Bit Score: 36.67  E-value: 1.25e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1913184748 228 TCTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKAL 266
Cdd:cd19788     1 MCEEHEEEKINIYCLTCEVPTCSMCKVFGAHKDCEVAPL 39
RING-HC_PML_C-V cd16579
RING finger, HC subclass, found in promyelocytic leukemia protein (PML) and similar proteins; ...
8-49 1.31e-03

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: 37.15  E-value: 1.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1913184748   8 LKCPVCGSFYREPIILPCSHNLCQACarnilVQTPESESPQS 49
Cdd:cd16579     5 LRCPGCKAEYKCPKLLPCLHTVCSGC-----LEALAEQASET 41
RING-HC_TRIM72_C-IV cd16612
RING finger, HC subclass, found in tripartite motif-containing protein 72 (TRIM72) and similar ...
4-33 1.40e-03

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: 37.41  E-value: 1.40e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1913184748   4 MEEELKCPVCGSFYREPIILPCSHNLCQAC 33
Cdd:cd16612     1 MHQDLSCPLCLKLFQSPVTTECGHTFCQDC 30
RING-HC_AtBRCA1-like cd23147
RING finger, HC subclass, found in Arabidopsis thaliana protein BREAST CANCER SUSCEPTIBILITY 1 ...
4-33 1.64e-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: 37.06  E-value: 1.64e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1913184748   4 MEEELKCPVCGSFYREPIILPCSHNLCQAC 33
Cdd:cd23147     1 LGKELKCPICLSLFKSAANLSCNHCFCAGC 30
RING-HC_RFPL4B cd16623
RING finger, HC subclass, found in Ret finger protein-like 4B (RFPL4B) and similar proteins; ...
4-33 2.00e-03

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: 37.10  E-value: 2.00e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1913184748   4 MEEELKCPVCGSFYREPIILPCSHNLCQAC 33
Cdd:cd16623     5 LEMEATCPICLDFFSHPISLSCAHIFCFDC 34
RING-HC_TRIM62_C-IV cd16608
RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar ...
4-33 2.18e-03

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: 36.32  E-value: 2.18e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1913184748   4 MEEELKCPVCGSFYREPIILPCSHNLCQAC 33
Cdd:cd16608     3 LKDELLCSICLSIYQDPVSLGCEHYFCRQC 32
Bbox2_TRIM59_C-XI cd19790
B-box-type 2 zinc finger found in tripartite motif-containing protein 59 (TRIM59) and similar ...
228-266 2.18e-03

B-box-type 2 zinc finger found in tripartite motif-containing protein 59 (TRIM59) and similar proteins; TRIM59, also known as TRIM57, or 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-XI 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, Bbox2, and a coiled coil region. In addition, TRIM59 contains a C-terminal transmembrane domain.


Pssm-ID: 380848 [Multi-domain]  Cd Length: 40  Bit Score: 36.28  E-value: 2.18e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1913184748 228 TCTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKAL 266
Cdd:cd19790     2 TCPEHYRQPLNLFCLLDRKLICGQCLTVGQHQGHPIDDL 40
Bbox2_TRIM65-like cd19793
B-box-type 2 zinc finger found in tripartite motif-containing protein 65 (TRIM65), B box and ...
228-266 2.28e-03

B-box-type 2 zinc finger found in tripartite motif-containing protein 65 (TRIM65), B box and SPRY domain-containing protein (BSPRY) and similar proteins; The family includes TRIM65 and BSPRY. 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 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. BSPRY is a regulatory protein for maintaining calcium homeostasis. It may regulate epithelial calcium transport by inhibiting TRPV5 activity. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380851  Cd Length: 43  Bit Score: 36.13  E-value: 2.28e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1913184748 228 TCTDHELEnHSMYCVQCKMPVCYQCLEEGKHSSHEVKAL 266
Cdd:cd19793     2 LCPEHGRE-LELYCRTEKRCVCAQCASKGECRGHRVTLL 39
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
6-43 2.33e-03

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 36.20  E-value: 2.33e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1913184748   6 EELKCPVCGSFYREPIILPCSHN-LCQACARNILVQTPE 43
Cdd:pfam13920   1 EDLLCVICLDRPRNVVLLPCGHLcLCEECAERLLRKKKK 39
RING-HC_TRIM58_C-IV cd16606
RING finger, HC subclass, found in tripartite motif-containing protein TRIM58 and similar ...
6-33 2.49e-03

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: 36.38  E-value: 2.49e-03
                          10        20
                  ....*....|....*....|....*...
gi 1913184748   6 EELKCPVCGSFYREPIILPCSHNLCQAC 33
Cdd:cd16606     1 EEARCPVCLDFLQEPVSVDCGHSFCLRC 28
RING-HC_TRIM47-like_C-IV cd16604
RING finger, HC subclass, found in tripartite motif-containing protein 47 (TRIM47) and similar ...
8-33 2.50e-03

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: 36.24  E-value: 2.50e-03
                          10        20
                  ....*....|....*....|....*.
gi 1913184748   8 LKCPVCGSFYREPIILPCSHNLCQAC 33
Cdd:cd16604     1 LSCPICLDLLKDPVTLPCGHSFCMGC 26
SPRY_PRY_TRIM75 cd15829
PRY/SPRY domain of tripartite motif-binding protein 75 (TRIM75); This domain, consisting of ...
468-527 2.53e-03

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: 39.19  E-value: 2.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1913184748 468 DPGSAHSDIILSNDNLTVTC-----SSYD-------DRVVLGKTGFSKGIHYWELTVDRydnHPDPAFGVAR 527
Cdd:cd15829    24 DPETAHPNLLVSEDKKCVTFtkkkqRVPDspkrftvNPVVLGFPGFHSGRHFWEVEVGD---KPEWAVGVCK 92
SPRY_PRY_SNTX cd16040
Stonustoxin subunit alpha or SNTX subunit alpha; This domain, consisting of the distinct ...
467-544 2.75e-03

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: 39.01  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184748 467 FDPGSAHSDIILSNDNLTVTCS----SYDD--------RVVLGKTGFSkGIHYWEltVDRYDNHPDPA---FGVARMDVM 531
Cdd:cd16040    13 LDPNTAHRNLSLSEGNRKVTRVkeeqPYPDhperfdywPQVLCREGLS-GRCYWE--VEWSGGGVDIAvayKGISRKGDG 89
                          90
                  ....*....|...
gi 1913184748 532 KDVMLGKDDKAWA 544
Cdd:cd16040    90 DDSRFGYNDKSWS 102
RING-HC_RNF138 cd16544
RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; ...
6-56 3.12e-03

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: 36.23  E-value: 3.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1913184748   6 EELKCPVCGSFYREPIIL-PCSHNLCQACARNILVQTPEsESPQSHRAAGSG 56
Cdd:cd16544     1 AELTCPVCQEVLKDPVELpPCRHIFCKACILLALRSSGA-RCPLCRGPVGKT 51
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
10-38 3.12e-03

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


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 35.56  E-value: 3.12e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1913184748   10 CPVC-GSFYREPIILPCSHNLCQACARNIL 38
Cdd:smart00184   1 CPIClEEYLKDPVILPCGHTFCRSCIRKWL 30
RING-HC_TRIM17_C-IV cd16595
RING finger, HC subclass, found in tripartite motif-containing protein TRIM17 and similar ...
4-35 3.21e-03

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: 36.51  E-value: 3.21e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1913184748   4 MEEELKCPVCGSFYREPIILPCSHNLCQACAR 35
Cdd:cd16595     2 LQEEATCSICLDYFTDPVMTTCGHNFCRACIQ 33
Bbox1_ZBBX cd19818
B-box-type 1 zinc finger found in zinc finger B-box domain-containing protein 1 (ZBBX) and ...
167-211 3.32e-03

B-box-type 1 zinc finger found in zinc finger B-box domain-containing protein 1 (ZBBX) and similar proteins; The family corresponds to a group of uncharacterized zinc finger B-box domain-containing proteins. The B-box motif shows high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


Pssm-ID: 380876  Cd Length: 43  Bit Score: 35.80  E-value: 3.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1913184748 167 KCQLCEKapKEATVMCEQCDVFYCDPCRLRCHpPRGPLAKHRLVP 211
Cdd:cd19818     1 QCGQCEQ--KAALLVCLECGEDYCSSCFAKFH-QKGALKKHRSIP 42
Bbox2_MuRF1_C-II cd19831
B-box-type 2 zinc finger found in muscle-specific RING finger protein 1 (MuRF-1) and similar ...
229-266 4.42e-03

B-box-type 2 zinc finger 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 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, 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. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380889  Cd Length: 43  Bit Score: 35.40  E-value: 4.42e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1913184748 229 CTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKAL 266
Cdd:cd19831     5 CKEHEDEKINIYCLTCEVPTCSMCKVFGIHKACEVAPL 42
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
550-600 5.02e-03

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


Pssm-ID: 240457  Cd Length: 151  Bit Score: 38.06  E-value: 5.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1913184748 550 ITKGATIGVLLDLNRKNLTFFIN-DEQQGPIAFDNVEGLFFPAVSLNRNVQV 600
Cdd:cd12877    95 LKKGDVVGCCLDLSVPSISFRVNgRPVQGMFENFNLDGMFFPVMSFSAGVSC 146
RING-HC_TRIM77_C-IV cd16543
RING finger, HC subclass, found in tripartite motif-containing protein 77 (TRIM77) and similar ...
5-37 5.27e-03

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: 35.45  E-value: 5.27e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1913184748   5 EEELKCPVCGSFYREPIILPCSHNLCQACARNI 37
Cdd:cd16543     1 EDQLTCSICLDLLKDPVTIPCGHSFCMNCITLL 33
zf-RING_UBOX pfam13445
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.
10-33 5.59e-03

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


Pssm-ID: 463881 [Multi-domain]  Cd Length: 38  Bit Score: 35.07  E-value: 5.59e-03
                          10        20
                  ....*....|....*....|....
gi 1913184748  10 CPVCGSFYREPIiLPCSHNLCQAC 33
Cdd:pfam13445   1 CPICLELFTDPV-LPCGHTFCREC 23
Bbox2_TRIM71_C-VII cd19796
B-box-type 2 zinc finger found in tripartite motif-containing protein 71 (TRIM71) and similar ...
226-266 5.94e-03

B-box-type 2 zinc finger found in tripartite motif-containing protein 71 (TRIM71) and similar proteins; TRIM71, also known as protein lineage variant 41 (lin-41), is an E3 ubiquitin-protein ligase that may play essential roles in embryonic stem cells, cellular reprogramming, and the timing of embryonic neurogenesis. It was first identified in the nematode Caenorhabditis elegans as a target of the differentiation-associated microRNA (miRNA) let-7 (lethal 7), and therefore part of a heterochronic gene network that controls larval development. In humans, it regulates let-7 microRNA biogenesis via modulation of Lin28B protein polyubiquitination. TRIM71 localizes to cytoplasmic P-bodies and directly interacts with the miRNA pathway proteins Argonaute 2 (AGO2) and DICER. It represses miRNA activity by promoting degradative ubiquitination of AGO2. Moreover, TRIM71 associates with SHCBP1, a novel component of the fibroblast growth factor (FGF) signaling pathway, and regulates its non-degradative polyubiquitination. It is also involved in the post-transcriptional regulation of the CDKN1A, RBL1 and RBL2 or EGR1 mRNAs through mediating RNA-binding in embryonic stem cells. TRIM71 belongs to the C-VII subclass of 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 RING 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 type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380854 [Multi-domain]  Cd Length: 48  Bit Score: 34.97  E-value: 5.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1913184748 226 VSTCTDHELENHSMYCVQCKMPVCYQCLeEGKHSSHEVKAL 266
Cdd:cd19796     1 PSYCEIHEHEVLRLYCDTCSVPICRECT-MGEHRGHSFIYL 40
Bbox2_MuRF2_C-II cd19832
B-box-type 2 zinc finger found in muscle-specific RING finger protein 2 (MuRF-2) and similar ...
229-271 6.56e-03

B-box-type 2 zinc finger 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 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 signalling 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 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, 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. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380890  Cd Length: 45  Bit Score: 35.04  E-value: 6.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1913184748 229 CTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKALGAMWK 271
Cdd:cd19832     3 CEEHEEERINIYCLNCEVPTCSLCKVFGAHKDCQVAPLTHVFQ 45
SPRY_PRY_TRIM60_75 cd15817
PRY/SPRY domain of tripartite motif-binding protein 60 and 75 (TRIM60 and TRIM75); This domain, ...
468-527 6.89e-03

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: 37.91  E-value: 6.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1913184748 468 DPGSAHSDIILSNDNLTV-------TCSSYDDR-----VVLGKTGFSKGIHYWELTVdryDNHPDPAFGVAR 527
Cdd:cd15817     5 DPETAHPNLIVSEDRKAVryrrmkpNCPYDPRRftvypAVLGSEGFDSGRHFWEVEV---GGKGEWILGVCK 73
Bbox2_BSPRY cd19834
B-box-type 2 zinc finger found in B box and SPRY domain-containing protein (BSPRY) and ...
227-266 7.84e-03

B-box-type 2 zinc finger found in B box and SPRY domain-containing protein (BSPRY) and similar proteins; BSPRY is a regulatory protein for maintaining calcium homeostasis. It may regulate epithelial calcium transport by inhibiting TRPV5 activity. BSPRY is composed of a B-box, an alpha-helical coiled coil and a SPRY domain. The B-box motif shows high sequence similarity with B-Box-type zinc finger 2 found in tripartite motif-containing proteins (TRIMs). The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380892  Cd Length: 43  Bit Score: 34.67  E-value: 7.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1913184748 227 STCTDHELEnHSMYCVQCKMPVCYQCLEEGKHSSHEVKAL 266
Cdd:cd19834     1 DLCPDHELE-LDWFCSTERRLVCAQCASLGTCRGHRVTPL 39
RING-HC_RNFT1-like cd16532
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein ...
10-33 8.12e-03

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein RNFT1, RNFT2, and similar proteins; Both RNFT1 and RNFT2 are multi-pass membrane proteins containing a C3HC4-type RING-HC finger. Their biological roles remain unclear.


Pssm-ID: 438194 [Multi-domain]  Cd Length: 41  Bit Score: 34.59  E-value: 8.12e-03
                          10        20
                  ....*....|....*....|....
gi 1913184748  10 CPVCGSFYREPIILPCSHNLCQAC 33
Cdd:cd16532     3 CPICQDEFKDPVVLRCKHIFCEDC 26
mRING-HC-C3HC5_RNF26 cd16788
Modified RING finger, HC subclass (C3HC5-type), found in RING finger protein 26 (RNF26) and ...
3-43 9.85e-03

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


Pssm-ID: 438442 [Multi-domain]  Cd Length: 60  Bit Score: 34.70  E-value: 9.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1913184748   3 EMEEELKCPVCGSFYREPIILPCSHN-LCQACARNILVQTPE 43
Cdd:cd16788     1 EERDKKKCVICQDQSKTVLILPCRHMcLCRQCANILLQQPVY 42
 
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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