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Conserved domains on  [gi|26350717|dbj|BAC38995|]
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unnamed protein product [Mus musculus]

Protein Classification

SPRY_SOCS1-2-4 domain-containing protein (domain architecture ID 10191521)

SPRY_SOCS1-2-4 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SPRY_SOCS1-2-4 cd12906
SPRY domain in the suppressor of cytokine signaling 1, 2, 4 families (SOCS1, SOCS2, SOCS4); ...
54-227 1.05e-140

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


:

Pssm-ID: 293963  Cd Length: 174  Bit Score: 391.60  E-value: 1.05e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717  54 HAWNPEDRSLNVFVKDDDRLTFHRHPVAQSTDGIRGKVGHARGLHAWQIHWPARQRGTHAVVGVATARAPLHSVGYTALV 133
Cdd:cd12906   1 HAWNPDDRSLNIFVKEDDPLTFHRHPVAQSTDCIRGKVGYSRGLHVWEITWPTRQRGTHAVVGVATKDAPLHCVGYTSLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717 134 GSDSESWGWDLGRSRLYHDGKNRPGVAYPAFLGPDEAFALPDSLLVVLDMDEGTLSFIVDGQYLGVAFRGLKGKKLYPVV 213
Cdd:cd12906  81 GSNEESWGWDIGRNKLYHDSKNQPGWTYPAFLEPDENFVVPDKFLVVLDMDEGTLSFVVDGQYLGVAFRGLKGKKLYPIV 160
                       170
                ....*....|....
gi 26350717 214 SAVWGHCEVTMRYI 227
Cdd:cd12906 161 SAVWGHCEVTMKYI 174
 
Name Accession Description Interval E-value
SPRY_SOCS1-2-4 cd12906
SPRY domain in the suppressor of cytokine signaling 1, 2, 4 families (SOCS1, SOCS2, SOCS4); ...
54-227 1.05e-140

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


Pssm-ID: 293963  Cd Length: 174  Bit Score: 391.60  E-value: 1.05e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717  54 HAWNPEDRSLNVFVKDDDRLTFHRHPVAQSTDGIRGKVGHARGLHAWQIHWPARQRGTHAVVGVATARAPLHSVGYTALV 133
Cdd:cd12906   1 HAWNPDDRSLNIFVKEDDPLTFHRHPVAQSTDCIRGKVGYSRGLHVWEITWPTRQRGTHAVVGVATKDAPLHCVGYTSLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717 134 GSDSESWGWDLGRSRLYHDGKNRPGVAYPAFLGPDEAFALPDSLLVVLDMDEGTLSFIVDGQYLGVAFRGLKGKKLYPVV 213
Cdd:cd12906  81 GSNEESWGWDIGRNKLYHDSKNQPGWTYPAFLEPDENFVVPDKFLVVLDMDEGTLSFVVDGQYLGVAFRGLKGKKLYPIV 160
                       170
                ....*....|....
gi 26350717 214 SAVWGHCEVTMRYI 227
Cdd:cd12906 161 SAVWGHCEVTMKYI 174
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor. Domain of unknown ...
98-224 4.29e-22

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor. Domain of unknown function. Distant homologs are domains in butyrophilin/marenostrin/pyrin homologs.


Pssm-ID: 334177  Cd Length: 121  Bit Score: 88.16  E-value: 4.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717    98 HAWQIHWPaRQRGTHAVVGVATARAPLHSVGYtalVGSDSESWGWDLGRSRLYHDGKNRPgvaYPAFLgpdeaFALPDSL 177
Cdd:pfam00622   2 HYFEVEIF-GQDPGGWRVGWATKDYPRKGERF---LGDDSGSWGYDGWNGKKYWASTSPL---TGLPL-----FEPGDVI 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 26350717   178 LVVLDMDEGTLSFIVDGQYLGVAFRGLKG-KKLYPVVSAVWGHCEVTM 224
Cdd:pfam00622  70 GCFLDYEEGTISFTKNGKSLGYAFRDVPFtGPLFPAVSLGSGEGLQFN 117
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
95-226 1.05e-18

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: 79.26  E-value: 1.05e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717     95 RGLHAWQIHWparQRGTHAVVGVATARAPLHsvgYTALVGSDSESWGWDLGRSRLYHDGKNRPgvaYPAFLGPDeafalP 174
Cdd:smart00449   1 SGRHYFEVEI---GDGGHWRVGVATKSVPRG---YFALLGEDKGSWGYDGDGGKKYHNSTGPE---YGLPLQEP-----G 66
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 26350717    175 DSLLVVLDMDEGTLSFIVDGQYL-GVAFRGLK-GKKLYPVVSaVWGHCEVTMRY 226
Cdd:smart00449  67 DVIGCFLDLEAGTISFYKNGKYLhGLAFFDVKfSGPLYPAFS-LGSGNSVRLNF 119
 
Name Accession Description Interval E-value
SPRY_SOCS1-2-4 cd12906
SPRY domain in the suppressor of cytokine signaling 1, 2, 4 families (SOCS1, SOCS2, SOCS4); ...
54-227 1.05e-140

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


Pssm-ID: 293963  Cd Length: 174  Bit Score: 391.60  E-value: 1.05e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717  54 HAWNPEDRSLNVFVKDDDRLTFHRHPVAQSTDGIRGKVGHARGLHAWQIHWPARQRGTHAVVGVATARAPLHSVGYTALV 133
Cdd:cd12906   1 HAWNPDDRSLNIFVKEDDPLTFHRHPVAQSTDCIRGKVGYSRGLHVWEITWPTRQRGTHAVVGVATKDAPLHCVGYTSLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717 134 GSDSESWGWDLGRSRLYHDGKNRPGVAYPAFLGPDEAFALPDSLLVVLDMDEGTLSFIVDGQYLGVAFRGLKGKKLYPVV 213
Cdd:cd12906  81 GSNEESWGWDIGRNKLYHDSKNQPGWTYPAFLEPDENFVVPDKFLVVLDMDEGTLSFVVDGQYLGVAFRGLKGKKLYPIV 160
                       170
                ....*....|....
gi 26350717 214 SAVWGHCEVTMRYI 227
Cdd:cd12906 161 SAVWGHCEVTMKYI 174
SPRY_SOCS_Fbox cd12875
SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins; This family ...
54-227 1.58e-97

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: 282.42  E-value: 1.58e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717  54 HAWNPEDRSLNVFVKDDdRLTFHRHPVAQSTDGIRGKVGHARGLHAWQIHWPARQRGTHAVVGVATARAPLHSVGYTALV 133
Cdd:cd12875   1 HGWNPADCSKNIYIKED-GLTFHRRPVAQSTDAIRGKKGYTRGLHAWEVKWISRPRGSHAVVGVATKDAPLQCDGYVTLL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717 134 GSDSESWGWDLGRSRLYHDGKnRPGVAYPAFLgpdEAFALPDSLLVVLDMDEGTLSFIVDGQYLGVAFRGLKGKKLYPVV 213
Cdd:cd12875  80 GSNSESWGWDLGDNKLYHNGK-KVIGSYPAKS---ENYQVPDRILVILDMEDGTLAFEANGEYLGVAFRGLPGKLLYPAV 155
                       170
                ....*....|....
gi 26350717 214 SAVWGHCEVTMRYI 227
Cdd:cd12875 156 SAVYGNCEIRLIYL 169
SPRY_Fbox cd12907
SPRY domain in the F-box family Fbxo45; Fbxo45 is a novel synaptic E3 and ubiquitin ligase, ...
54-227 5.24e-65

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


Pssm-ID: 293964  Cd Length: 175  Bit Score: 199.92  E-value: 5.24e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717  54 HAWNPEDRSLNVFVKDDDrLTFHRHPVAQSTDGIRGKVGHARGLHAWQIHWPArQRGTHAVVGVATARAPLHSVGYTALV 133
Cdd:cd12907   1 HAWNPNDCSRNIYIKPNG-FTLHRNPVAQSTDGARGKIGFSSGRHAWEVWWEG-PLGTVAVVGIATKHAPLQCQGYVALL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717 134 GSDSESWGWDLGRSRLYHDGKNRpGVaYPAFLGPDEaFALPDSLLVVLDMDEGTLSFIVDGQYLGVAFRGLKGKKLYPVV 213
Cdd:cd12907  79 GSDDQSWGWNLVDNHLLHNGDSQ-GN-YPQCNNAPK-YQVGERIRVILDCEDNTLAFERGYEFLGVAFRGLPPTKLYPAV 155
                       170
                ....*....|....
gi 26350717 214 SAVWGHCEVTMRYI 227
Cdd:cd12907 156 SAVYGNTEVSMVYL 169
SPRY_SOCS3 cd12876
SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY ...
56-214 3.66e-28

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: 105.71  E-value: 3.66e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717  56 WNPEDRSLNVFVKDDDR-LTFHRHpVAQSTDGIRGKVGHARGLHAWQIHWPARQRGTHAVVGVATARAPLHSVGY--TAL 132
Cdd:cd12876   4 WDERDKSPAVQLSDNNReVYFHPD-YSCGTAAVRGTKPLTNGQHYWEIKMSSPVYGTDMMVGVGTKKADLHAYRYefCSL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717 133 VGSDSESWGwdLG-RSRLYHDGKNRPgvaYpaflgpDEAFALPDSLL-VVLDMDEGTLSFIVDGQYLGVAFRGLKG-KKL 209
Cdd:cd12876  83 LGEDEESWG--LSyKGLLWHDGQSRP---Y------TSPFGNQGTIIgVHLDMWRGTLTFYKNGKPLGVAFTGLNGvKPL 151

                ....*
gi 26350717 210 YPVVS 214
Cdd:cd12876 152 YPMVS 156
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor. Domain of unknown ...
98-224 4.29e-22

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor. Domain of unknown function. Distant homologs are domains in butyrophilin/marenostrin/pyrin homologs.


Pssm-ID: 334177  Cd Length: 121  Bit Score: 88.16  E-value: 4.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717    98 HAWQIHWPaRQRGTHAVVGVATARAPLHSVGYtalVGSDSESWGWDLGRSRLYHDGKNRPgvaYPAFLgpdeaFALPDSL 177
Cdd:pfam00622   2 HYFEVEIF-GQDPGGWRVGWATKDYPRKGERF---LGDDSGSWGYDGWNGKKYWASTSPL---TGLPL-----FEPGDVI 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 26350717   178 LVVLDMDEGTLSFIVDGQYLGVAFRGLKG-KKLYPVVSAVWGHCEVTM 224
Cdd:pfam00622  70 GCFLDYEEGTISFTKNGKSLGYAFRDVPFtGPLFPAVSLGSGEGLQFN 117
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
96-225 1.43e-20

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: 84.02  E-value: 1.43e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717  96 GLHAWQIHWPARQRGtHAVVGVATARAPLHSvgyTALVGSDSESWGWDLGRSRLYHDGKNRPGVaypaflgpdEAFALPD 175
Cdd:cd11709   1 GKWYWEVRVDSGNGG-LIQVGWATKSFSLDG---EGGVGDDEESWGYDGSRLRKGHGGSSGPGG---------RPWKSGD 67
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 26350717 176 SLLVVLDMDEGTLSFIVDGQYLGVAFRGLKGKK--LYPVVSAVWGhCEVTMR 225
Cdd:cd11709  68 VVGCLLDLDEGTLSFSLNGKDLGVAFTNLFLKGggLYPAVSLGSG-QGVTIN 118
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
95-226 1.05e-18

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: 79.26  E-value: 1.05e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717     95 RGLHAWQIHWparQRGTHAVVGVATARAPLHsvgYTALVGSDSESWGWDLGRSRLYHDGKNRPgvaYPAFLGPDeafalP 174
Cdd:smart00449   1 SGRHYFEVEI---GDGGHWRVGVATKSVPRG---YFALLGEDKGSWGYDGDGGKKYHNSTGPE---YGLPLQEP-----G 66
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 26350717    175 DSLLVVLDMDEGTLSFIVDGQYL-GVAFRGLK-GKKLYPVVSaVWGHCEVTMRY 226
Cdd:smart00449  67 DVIGCFLDLEAGTISFYKNGKYLhGLAFFDVKfSGPLYPAFS-LGSGNSVRLNF 119
SPRY_HERC1 cd12881
SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to ...
114-214 3.07e-10

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: 57.36  E-value: 3.07e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717 114 VVGVAtaRAPLHSVGYTalvgSDSESWGWDLGRSRLYHDGKNRPGVAypaflgpdEAFALPDSLLVVLDMDEGTLSFIVD 193
Cdd:cd12881  61 CVGVS--RKPVTDFNYR----TSSDMWLYRAYNGNLYHNGEQLLRLS--------SKFHQGDYITVVLDMEEGTLSFGKN 126
                        90       100
                ....*....|....*....|.
gi 26350717 194 GQYLGVAFRGLKGKKLYPVVS 214
Cdd:cd12881 127 GEEPGVAFEDVDATELYPCVM 147
SPRY_PRY_TRIM67_9 cd12889
PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, ...
89-214 8.46e-09

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


Pssm-ID: 293947  Cd Length: 172  Bit Score: 53.40  E-value: 8.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717  89 GKVGHARGLHAWQIHWPARQRGTHAVVGVATAraplhSVGYTALVGSDSESWGW--DLGRSRLYHDGK--NRP--GVAYP 162
Cdd:cd12889  42 GSVGFSRGVHYWEVTIDRYDGHPDPAFGVARI-----DVNKDKMLGKDDKGWSMyiDNNRSWFLHNNEhsNRTegGITVG 116
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 26350717 163 AFLGpdeafalpdsllVVLDMDEGTLSFIVDGQYLG-VAFRGLKGkKLYPVVS 214
Cdd:cd12889 117 SVVG------------VLLDLDRHTLSFYVNDEPQGpIAFRNLPG-VFYPAVS 156
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
109-223 5.23e-07

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


Pssm-ID: 293943  Cd Length: 132  Bit Score: 47.27  E-value: 5.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717 109 RGTHAVVGVATARAPLHSvgytaLVGSDSESWGW--DLGRsrLYHdGKNRPGVAYPAFLGPDeafalpdsllVV---LDM 183
Cdd:cd12885  27 EKGIVSIGFCTSGFPLNR-----MPGWEDGSYGYhgDDGR--VYL-GGGEGENYGPPFGTGD----------VVgcgINF 88
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 26350717 184 DEGTLSFIVDGQYLGVAFRGLKGKKLYPVVSAVWGHCEVT 223
Cdd:cd12885  89 KTGEVFFTKNGELLGTAFENVVKGRLYPTVGLGSPGVKVR 128
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
115-213 9.25e-06

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


Pssm-ID: 293966  Cd Length: 144  Bit Score: 44.05  E-value: 9.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717 115 VGVATAraplhSVGYTALVGSDSESWGwdlgrsrlYH--DGK----NRPGVAYpaflGPdeAFALPDSLLVVLDMDEGTL 188
Cdd:cd12909  44 IGFSTK-----DVNLNRLPGWEPHSWG--------YHgdDGHsfcsSGTGKPY----GP--TFTTGDVIGCGINFRDNTA 104
                        90       100
                ....*....|....*....|....*
gi 26350717 189 SFIVDGQYLGVAFRGLKGKKLYPVV 213
Cdd:cd12909 105 FYTKNGVNLGIAFRDIKKGNLYPTV 129
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
133-222 5.39e-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: 41.54  E-value: 5.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717 133 VGSDSESWGWDLGRSRLYHDGKNRPGvaypaflgpdEAFALPDSLLVVLDMDEGTLSFIVDGQYLGVAF---RGLKGKKL 209
Cdd:cd12882  42 VGDTRDSYAYDGNRVRKWNVSTQKYG----------EPWVAGDVIGCCIDLDKGTISFYRNGRSLGVAFdnvRRGPGLAY 111
                        90
                ....*....|....
gi 26350717 210 YPVVS-AVWGHCEV 222
Cdd:cd12882 112 FPAVSlSFGERLEL 125
SPRY_PRY_C-II cd13734
PRY/SPRY domain in tripartite motif-containing proteins 1, 9, 18, 36, 46, 67,76 (TRIM1, TRIM9, ...
85-218 7.00e-05

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  Cd Length: 166  Bit Score: 41.88  E-value: 7.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717  85 DGIRGKVGHARGLHAWQIHwpaRQRGTHAVVGVATARAPLHSvgytaLVGSDSESW--GWDLGRSRLYHDGKNRPgvayp 162
Cdd:cd13734  43 PAVLGDVAISSGRHYWEVS---VSRSTSYRVGVAYKSAPRDE-----DLGKNSTSWclSRDNNRYTARHDGKVVD----- 109
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 26350717 163 afLGPDEafaLPDSLLVVLDMDEGTLSFIVDGQYLG-VAFRGLKGKKLYPVVsAVWG 218
Cdd:cd13734 110 --LRVTG---HPARIGVLLDYDNGTLSFYDAESKQHlYTFHVDFEGPVCPAF-AVWN 160
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
169-222 4.19e-04

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


Pssm-ID: 293933  Cd Length: 155  Bit Score: 39.48  E-value: 4.19e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 26350717 169 EAFALPDSLLVVLDMDEGTLSFIVDGQYLGVAFR---GLKGKKLYPVVsaVWGHCEV 222
Cdd:cd12873  93 EPFGLGDVIGCYLDLDNGTISFSKNGKDLGKAFDippHLRNSALFPAV--CLKNAEV 147
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
105-214 1.16e-03

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: 38.27  E-value: 1.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717 105 PARQRGTHAVVGVATARAPLHsvgytALVGSDSESWGWdlgRSR---LYHDGKNRPGvaypaflgPDEAFALPDSLLVVL 181
Cdd:cd12872  39 GGGTETGHVRVGWSRREASLQ-----APVGYDKYSYAI---RDKdgsKFHQSRGKPY--------GEPGFKEGDVIGFLI 102
                        90       100       110
                ....*....|....*....|....*....|....
gi 26350717 182 DMDEgtLSFIVDGQYLGVAFRGLKGKKLY-PVVS 214
Cdd:cd12872 103 TLPK--IEFFKNGKSQGVAFEDIYGTGGYyPAVS 134
SPRY_like cd12886
SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ...
96-200 1.23e-03

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


Pssm-ID: 293944  Cd Length: 129  Bit Score: 37.87  E-value: 1.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717  96 GLHAWQIHWPARQRGTHAVVGVATARAPlhsvGYTALVGSDSESWGWDLGRSrlyhdgknrPGVAYPAFLGP---DEAFA 172
Cdd:cd12886   1 GKWYWEVTVVSSAASTYAGIGVANAAAT----GNNGLNGIELSSIGYSLGVY---------SGNKLSNGSSVatyGAGFT 67
                        90       100
                ....*....|....*....|....*...
gi 26350717 173 LPDSLLVVLDMDEGTLSFIVDGQYLGVA 200
Cdd:cd12886  68 AGDVIGVALDLDAGKIWFYKNGVWQGGG 95
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
103-213 1.36e-03

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


Pssm-ID: 293942  Cd Length: 177  Bit Score: 38.34  E-value: 1.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717 103 HWPARQRGTHAV-VGVATARAPLhsvgytaLVGSDSESWGWDlGRSRLYHDGKnrpgvaypaFLGPDEAFALPDSLLVVL 181
Cdd:cd12884  61 HLPTEETDPHVVrVGWSVDSSSL-------QLGEEEFSYGYG-STGKKSTNCK---------FEDYGEPFGENDVIGCYL 123
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 26350717 182 DMD--EGTLSFIVDGQYLGVAFR----GLKGKKLYPVV 213
Cdd:cd12884 124 DFEsePVEISFSKNGKDLGVAFKiskeELGGKALFPHV 161
SPRYD7 cd12880
SPRY domain-containing protein 7; This family contains SPRY domain-containing protein 7 (also ...
115-213 2.51e-03

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


Pssm-ID: 293938  Cd Length: 160  Bit Score: 37.18  E-value: 2.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717 115 VGVATARAPLHSVgytaLVGSDSESWG--WDlgrSRLYHDG--KNRP----------GVAYpaflgpdeafalpdsllvv 180
Cdd:cd12880  45 VGLATRKTDLNRV----PLGNDAESWVlrSD---GTIWHNGevIHKLkqlveegdviGVTY------------------- 98
                        90       100       110
                ....*....|....*....|....*....|...
gi 26350717 181 ldmDEGTLSFIVDGQYLGVAFRGLKGkKLYPVV 213
Cdd:cd12880  99 ---DHVELNFYLNGKPLDCPITGIKG-TVYPVV 127
SPRY_PRY_TRIM35 cd12893
PRY/SPRY domain in tripartite motif-containing protein 35 (TRIM35); This PRY/SPRY domain is ...
87-191 3.00e-03

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  Cd Length: 171  Bit Score: 37.23  E-value: 3.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350717  87 IRGKVGHARGLHAWQIH------WparqrgthaVVGVATAraplhSVGYTALVGSDSESWGWDLGrsrlYHDGKnrpgva 160
Cdd:cd12893  44 VLGSEGFTSGKHSWDVEvgdntsW---------MLGVAKE-----SVQRKGKFTLSPESGFWTIG----FSEGK------ 99
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 26350717 161 YPAFLGPDEAFAL-----PDSLLVVLDMDEGTLSFI 191
Cdd:cd12893 100 YSARTSPEPRTPLrvkqkPQRIRVQLDWDRGKVSFS 135
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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