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Conserved domains on  [gi|193205146|ref|NP_497321|]
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B30.2/SPRY domain-containing protein [Caenorhabditis elegans]

Protein Classification

SPRY domain-containing protein; RING finger and SPRY domain-containing protein( domain architecture ID 10191521)

SPRY (SPla and the RYanodine receptor) domain-containing protein similar to yeast SSH4 (suppressor of SHR3 null mutation protein 4); the SPRY domain is a protein interaction module found in proteins implicated in important biological pathways, including those that regulate innate and adaptive immunity| RING finger and SPRY domain-containing protein similar to Salmo salar tripartite motif-containing protein 39

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); ...
 131-303 5.78e-133

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: 381.20  E-value: 5.78e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205146 131 HSWNPEDRSLNIFVKDEDKFTFHRHPVAQSTDCIRGKMGYSRGFHVWQIEWPERQRGTHAVVGVATKNAPLHAAGYTALI 210
Cdd:cd12906    1 HAWNPDDRSLNIFVKEDDPLTFHRHPVAQSTDCIRGKVGYSRGLHVWEITWPTRQRGTHAVVGVATKDAPLHCVGYTSLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205146 211 GTTDESYGWDITRRECHHDSKHTMTWRYP-FSNSRDVYNVPDKFYCILDMDEGYMAFATDDEFLGVAFRNLKGKTLYPIV 289
Cdd:cd12906   81 GSNEESWGWDIGRNKLYHDSKNQPGWTYPaFLEPDENFVVPDKFLVVLDMDEGTLSFVVDGQYLGVAFRGLKGKKLYPIV 160

                        170
                 ....*....|....
gi 193205146 290 AAVWGHCEISMRYL 303
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); ...
 131-303 5.78e-133

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: 381.20  E-value: 5.78e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205146 131 HSWNPEDRSLNIFVKDEDKFTFHRHPVAQSTDCIRGKMGYSRGFHVWQIEWPERQRGTHAVVGVATKNAPLHAAGYTALI 210
Cdd:cd12906    1 HAWNPDDRSLNIFVKEDDPLTFHRHPVAQSTDCIRGKVGYSRGLHVWEITWPTRQRGTHAVVGVATKDAPLHCVGYTSLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205146 211 GTTDESYGWDITRRECHHDSKHTMTWRYP-FSNSRDVYNVPDKFYCILDMDEGYMAFATDDEFLGVAFRNLKGKTLYPIV 289
Cdd:cd12906   81 GSNEESWGWDIGRNKLYHDSKNQPGWTYPaFLEPDENFVVPDKFLVVLDMDEGTLSFVVDGQYLGVAFRGLKGKKLYPIV 160

                        170
                 ....*....|....
gi 193205146 290 AAVWGHCEISMRYL 303
Cdd:cd12906  161 SAVWGHCEVTMKYI 174
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 175-294 1.61e-15

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: 72.76  E-value: 1.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205146  175 HVWQIEWpERQRGTHAVVGVATKNAPLHAAGYtalIGTTDESYGWDITRRECHHDSKHTMTWRYPFSnsrdvynVPDKFY 254
Cdd:pfam00622   2 HYFEVEI-FGQDGGGWRVGWATKSVPRKGERF---LGDESGSWGYDGWTGKKYWASTSPLTGLPLFE-------PGDVIG 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 193205146  255 CILDMDEGYMAFATDDEFLGVAFRNLKG-KTLYPIVAAVWG 294
Cdd:pfam00622  71 CFLDYEAGTISFTKNGKSLGYAFRDVPFaGPLFPAVSLGAG 111
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 172-302 6.30e-12

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: 62.70  E-value: 6.30e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205146   172 RGFHVWQIEWperQRGTHAVVGVATKNAPLHaagYTALIGTTDESYGWDITRRECHHDSKHTMTwRYPFSNSrdvynvPD 251
Cdd:smart00449   1 SGRHYFEVEI---GDGGHWRVGVATKSVPRG---YFALLGEDKGSWGYDGDGGKKYHNSTGPEY-GLPLQEP------GD 67

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 193205146   252 KFYCILDMDEGYMAF-ATDDEFLGVAFRNLK-GKTLYPIVaAVWGHCEISMRY 302
Cdd:smart00449  68 VIGCFLDLEAGTISFyKNGKYLHGLAFFDVKfSGPLYPAF-SLGSGNSVRLNF 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); ...
 131-303 5.78e-133

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: 381.20  E-value: 5.78e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205146 131 HSWNPEDRSLNIFVKDEDKFTFHRHPVAQSTDCIRGKMGYSRGFHVWQIEWPERQRGTHAVVGVATKNAPLHAAGYTALI 210
Cdd:cd12906    1 HAWNPDDRSLNIFVKEDDPLTFHRHPVAQSTDCIRGKVGYSRGLHVWEITWPTRQRGTHAVVGVATKDAPLHCVGYTSLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205146 211 GTTDESYGWDITRRECHHDSKHTMTWRYP-FSNSRDVYNVPDKFYCILDMDEGYMAFATDDEFLGVAFRNLKGKTLYPIV 289
Cdd:cd12906   81 GSNEESWGWDIGRNKLYHDSKNQPGWTYPaFLEPDENFVVPDKFLVVLDMDEGTLSFVVDGQYLGVAFRGLKGKKLYPIV 160

                        170
                 ....*....|....
gi 193205146 290 AAVWGHCEISMRYL 303
Cdd:cd12906  161 SAVWGHCEVTMKYI 174
SPRY_SOCS_Fbox cd12875
SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins; This family ...
 131-303 6.21e-87

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: 263.93  E-value: 6.21e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205146 131 HSWNPEDRSLNIFVKdEDKFTFHRHPVAQSTDCIRGKMGYSRGFHVWQIEWPERQRGTHAVVGVATKNAPLHAAGYTALI 210
Cdd:cd12875    1 HGWNPADCSKNIYIK-EDGLTFHRRPVAQSTDAIRGKKGYTRGLHAWEVKWISRPRGSHAVVGVATKDAPLQCDGYVTLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205146 211 GTTDESYGWDITRRECHHDSKHTMTwRYPFSNSRdvYNVPDKFYCILDMDEGYMAFATDDEFLGVAFRNLKGKTLYPIVA 290
Cdd:cd12875   80 GSNSESWGWDLGDNKLYHNGKKVIG-SYPAKSEN--YQVPDRILVILDMEDGTLAFEANGEYLGVAFRGLPGKLLYPAVS 156

                        170
                 ....*....|...
gi 193205146 291 AVWGHCEISMRYL 303
Cdd:cd12875  157 AVYGNCEIRLIYL 169
SPRY_Fbox cd12907
SPRY domain in the F-box family Fbxo45; Fbxo45 is a novel synaptic E3 and ubiquitin ligase, ...
 131-305 4.64e-64

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: 205.32  E-value: 4.64e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205146 131 HSWNPEDRSLNIFVKdEDKFTFHRHPVAQSTDCIRGKMGYSRGFHVWQIEWpERQRGTHAVVGVATKNAPLHAAGYTALI 210
Cdd:cd12907    1 HAWNPNDCSRNIYIK-PNGFTLHRNPVAQSTDGARGKIGFSSGRHAWEVWW-EGPLGTVAVVGIATKHAPLQCQGYVALL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205146 211 GTTDESYGWDITRRECHHDSKHTMTwrYPFSNSRDVYNVPDKFYCILDMDEGYMAFATDDEFLGVAFRNLKGKTLYPIVA 290
Cdd:cd12907   79 GSDDQSWGWNLVDNHLLHNGDSQGN--YPQCNNAPKYQVGERIRVILDCEDNTLAFERGYEFLGVAFRGLPPTKLYPAVS 156

                        170
                 ....*....|....*
gi 193205146 291 AVWGHCEISMRYLGS 305
Cdd:cd12907  157 AVYGNTEVSMVYLGP 171
SPRY_SOCS3 cd12876
SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY ...
 132-290 2.90e-20

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: 88.37  E-value: 2.90e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205146 132 SWNPEDRSLNI-FVKDEDKFTFHRHpVAQSTDCIRGKMGYSRGFHVWQIEWPERQRGTHAVVGVATKNAPLHAAGY--TA 208
Cdd:cd12876    3 TWDERDKSPAVqLSDNNREVYFHPD-YSCGTAAVRGTKPLTNGQHYWEIKMSSPVYGTDMMVGVGTKKADLHAYRYefCS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205146 209 LIGTTDESYGWDITRReCHHDSKhtmTWRY--PFSNSRDVYNVpdkfycILDMDEGYMAFATDDEFLGVAFRNLKG-KTL 285
Cdd:cd12876   82 LLGEDEESWGLSYKGL-LWHDGQ---SRPYtsPFGNQGTIIGV------HLDMWRGTLTFYKNGKPLGVAFTGLNGvKPL 151


                 ....*
gi 193205146 286 YPIVA 290
Cdd:cd12876  152 YPMVS 156
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 175-294 1.61e-15

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: 72.76  E-value: 1.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205146  175 HVWQIEWpERQRGTHAVVGVATKNAPLHAAGYtalIGTTDESYGWDITRRECHHDSKHTMTWRYPFSnsrdvynVPDKFY 254
Cdd:pfam00622   2 HYFEVEI-FGQDGGGWRVGWATKSVPRKGERF---LGDESGSWGYDGWTGKKYWASTSPLTGLPLFE-------PGDVIG 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 193205146  255 CILDMDEGYMAFATDDEFLGVAFRNLKG-KTLYPIVAAVWG 294
Cdd:pfam00622  71 CFLDYEAGTISFTKNGKSLGYAFRDVPFaGPLFPAVSLGAG 111
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 173-295 2.01e-13

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: 66.69  E-value: 2.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205146 173 GFHVWQIEWpERQRGTHAVVGVATKNAPLHAagyTALIGTTDESYGWDITRRECHHDSKHTMTWRYpfsnsrdvYNVPDK 252
Cdd:cd11709    1 GKWYWEVRV-DSGNGGLIQVGWATKSFSLDG---EGGVGDDEESWGYDGSRLRKGHGGSSGPGGRP--------WKSGDV 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 193205146 253 FYCILDMDEGYMAFATDDEFLGVAFRNL--KGKTLYPIVAAVWGH 295
Cdd:cd11709   69 VGCLLDLDEGTLSFSLNGKDLGVAFTNLflKGGGLYPAVSLGSGQ 113
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 172-302 6.30e-12

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: 62.70  E-value: 6.30e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205146   172 RGFHVWQIEWperQRGTHAVVGVATKNAPLHaagYTALIGTTDESYGWDITRRECHHDSKHTMTwRYPFSNSrdvynvPD 251
Cdd:smart00449   1 SGRHYFEVEI---GDGGHWRVGVATKSVPRG---YFALLGEDKGSWGYDGDGGKKYHNSTGPEY-GLPLQEP------GD 67

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 193205146   252 KFYCILDMDEGYMAF-ATDDEFLGVAFRNLK-GKTLYPIVaAVWGHCEISMRY 302
Cdd:smart00449  68 VIGCFLDLEAGTISFyKNGKYLHGLAFFDVKfSGPLYPAF-SLGSGNSVRLNF 119
SPRY_HERC1 cd12881
SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to ...
 255-289 2.54e-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: 41.56  E-value: 2.54e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 193205146 255 CILDMDEGYMAFATDDEFLGVAFRNLKGKTLYPIV 289
Cdd:cd12881  112 VVLDMEEGTLSFGKNGEEPGVAFEDVDATELYPCV 146
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 179-289 3.17e-04

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: 40.96  E-value: 3.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205146 179 IEWPERQRGTHAVVGVATKNAPLHAAgytalIGTTDESYGWDITRRECHHDSKhtmtwRYPFSNSRdvYNVPDKFYCILD 258
Cdd:cd12872   36 ILEGGGTETGHVRVGWSRREASLQAP-----VGYDKYSYAIRDKDGSKFHQSR-----GKPYGEPG--FKEGDVIGFLIT 103

                         90       100       110
                 ....*....|....*....|....*....|..
gi 193205146 259 MdeGYMAFATDDEFLGVAFRNLKG-KTLYPIV 289
Cdd:cd12872  104 L--PKIEFFKNGKSQGVAFEDIYGtGGYYPAV 133
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 183-299 6.28e-03

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: 36.87  E-value: 6.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205146 183 ERQRGTHAVVGVATKNAPLHAagytaLIGTTDESYGWditrrecHHDSKHTMTWRYPFSNSRDVYNVPDKFYCILDMDEG 262
Cdd:cd12885   24 DLGEKGIVSIGFCTSGFPLNR-----MPGWEDGSYGY-------HGDDGRVYLGGGEGENYGPPFGTGDVVGCGINFKTG 91

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 193205146 263 YMAFATDDEFLGVAFRNLKGKTLYPIVAAVWGHCEIS 299
Cdd:cd12885   92 EVFFTKNGELLGTAFENVVKGRLYPTVGLGSPGVKVR 128
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 192-289 7.48e-03

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


Pssm-ID: 293966  Cd Length: 144  Bit Score: 37.12  E-value: 7.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205146 192 VGVATKNAPLhaagyTALIGTTDESYGWditrrecHHDSKHTmtwrypFSNSRD------VYNVPDKFYCILDMDEGYMA 265
Cdd:cd12909   44 IGFSTKDVNL-----NRLPGWEPHSWGY-------HGDDGHS------FCSSGTgkpygpTFTTGDVIGCGINFRDNTAF 105

                         90       100
                 ....*....|....*....|....
gi 193205146 266 FATDDEFLGVAFRNLKGKTLYPIV 289
Cdd:cd12909  106 YTKNGVNLGIAFRDIKKGNLYPTV 129
 
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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