NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|71990534|ref|NP_504786|]
View 

Schlafen-like protein 2 [Caenorhabditis elegans]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 11-167 2.96e-80

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: 244.41  E-value: 2.96e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990534  11 LNKQDQDLHLEIDETGLACKSEVKKRWLGARGTAGLYGNGKYYYEVTITSKGLCRVGWATLGGSLNIGKGLDSFGYGGTG 90
Cdd:cd12873   1 MNPYDRDAALAISPDGLLCQSREEKGWQGCRATKGVKGKGKYYYEVTVTDEGLCRVGWSTEDASLDLGTDKFGFGYGGTG 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71990534  91 MKSTHKKFDDYGLPFTLNDVIGCYLDLDSRTIWWSKNGEQFPAAFSIDVKYKNSntCLFPAVLCQNSSLSVNFGSQP 167
Cdd:cd12873  81 KKSHGRQFDDYGEPFGLGDVIGCYLDLDNGTISFSKNGKDLGKAFDIPPHLRNS--ALFPAVCLKNAEVEFNFGDKP 155
COG2865 COG2865
Predicted transcriptional regulator, contains HTH domain [Transcription];
227-321 2.23e-12

Predicted transcriptional regulator, contains HTH domain [Transcription];


:

Pssm-ID: 442112  Cd Length: 123  Bit Score: 63.75  E-value: 2.23e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990534 227 ELKRTQCKQDKdgsirrtlqpISKTICAFLNTDGGRLFLGVNDDKVIKGISMSKNMIYHFFGSLRHMcenfkpCSPLCRI 306
Cdd:COG2865  16 EFKESLNEPDE----------ILKTVCAFANTEGGTLLIGVDDDGEIVGLDDPDKLLERLENLIADN------ISPPIRP 79

                        90
                ....*....|....*..
gi 71990534 307 KVSILEV--IPVGVIKV 321
Cdd:COG2865  80 DVEEVEIdgKRVLVIEV 96
 
Name Accession Description Interval E-value
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 11-167 2.96e-80

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: 244.41  E-value: 2.96e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990534  11 LNKQDQDLHLEIDETGLACKSEVKKRWLGARGTAGLYGNGKYYYEVTITSKGLCRVGWATLGGSLNIGKGLDSFGYGGTG 90
Cdd:cd12873   1 MNPYDRDAALAISPDGLLCQSREEKGWQGCRATKGVKGKGKYYYEVTVTDEGLCRVGWSTEDASLDLGTDKFGFGYGGTG 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71990534  91 MKSTHKKFDDYGLPFTLNDVIGCYLDLDSRTIWWSKNGEQFPAAFSIDVKYKNSntCLFPAVLCQNSSLSVNFGSQP 167
Cdd:cd12873  81 KKSHGRQFDDYGEPFGLGDVIGCYLDLDNGTISFSKNGKDLGKAFDIPPHLRNS--ALFPAVCLKNAEVEFNFGDKP 155
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 49-166 3.16e-26

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: 102.37  E-value: 3.16e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990534     49 NGKYYYEVTITSKGLCRVGWAT----LGGSLNIGKGLDSFGYGGT-GMKSTHKKFDDYGLPFTL-NDVIGCYLDLDSRTI 122
Cdd:smart00449   1 SGRHYFEVEIGDGGHWRVGVATksvpRGYFALLGEDKGSWGYDGDgGKKYHNSTGPEYGLPLQEpGDVIGCFLDLEAGTI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 71990534    123 WWSKNGEQ--FPAAFSIdvkykNSNTCLFPAVLCQNS-SLSVNFGSQ 166
Cdd:smart00449  81 SFYKNGKYlhGLAFFDV-----KFSGPLYPAFSLGSGnSVRLNFGPL 122
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 51-166 9.46e-26

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: 100.88  E-value: 9.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990534    51 KYYYEVTIT--SKGLCRVGWAT----LGGSLNIGKGLDSFGYGG-TGMKSTHKKFDDYGLP-FTLNDVIGCYLDLDSRTI 122
Cdd:pfam00622   1 RHYFEVEIFgqDGGGWRVGWATksvpRKGERFLGDESGSWGYDGwTGKKYWASTSPLTGLPlFEPGDVIGCFLDYEAGTI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 71990534   123 WWSKNGEQFPAAFSIDVKYKnsntCLFPAV-LCQNSSLSVNFGSQ 166
Cdd:pfam00622  81 SFTKNGKSLGYAFRDVPFAG----PLFPAVsLGAGEGLKFNFGLR 121
COG2865 COG2865
Predicted transcriptional regulator, contains HTH domain [Transcription];
227-321 2.23e-12

Predicted transcriptional regulator, contains HTH domain [Transcription];


Pssm-ID: 442112  Cd Length: 123  Bit Score: 63.75  E-value: 2.23e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990534 227 ELKRTQCKQDKdgsirrtlqpISKTICAFLNTDGGRLFLGVNDDKVIKGISMSKNMIYHFFGSLRHMcenfkpCSPLCRI 306
Cdd:COG2865  16 EFKESLNEPDE----------ILKTVCAFANTEGGTLLIGVDDDGEIVGLDDPDKLLERLENLIADN------ISPPIRP 79

                        90
                ....*....|....*..
gi 71990534 307 KVSILEV--IPVGVIKV 321
Cdd:COG2865  80 DVEEVEIdgKRVLVIEV 96
AlbA_2 pfam04326
Putative DNA-binding domain; This family belongs to the AlbA clan of DNA-binding domains.
 231-322 1.72e-11

Putative DNA-binding domain; This family belongs to the AlbA clan of DNA-binding domains.


Pssm-ID: 461263  Cd Length: 116  Bit Score: 60.78  E-value: 1.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990534   231 TQCKQDKDGSIRRTlqpISKTICAFLNTDGGRLFLGVNDDKVIKGIsmSKNMIYHFFGSLRHMCENFKPcsplcRIKVSI 310
Cdd:pfam04326   5 LEFKESLGKSSKKK---IAKTISAFANTEGGTIVIGVDDTGKIVGV--SDDEKDTEDLLKNQILDLIKP-----PIEVDI 74

                          90
                  ....*....|....*.
gi 71990534   311 LEV----IPVGVIKVK 322
Cdd:pfam04326  75 EEIeidgKYVLVVEIP 90
 
Name Accession Description Interval E-value
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 11-167 2.96e-80

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: 244.41  E-value: 2.96e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990534  11 LNKQDQDLHLEIDETGLACKSEVKKRWLGARGTAGLYGNGKYYYEVTITSKGLCRVGWATLGGSLNIGKGLDSFGYGGTG 90
Cdd:cd12873   1 MNPYDRDAALAISPDGLLCQSREEKGWQGCRATKGVKGKGKYYYEVTVTDEGLCRVGWSTEDASLDLGTDKFGFGYGGTG 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71990534  91 MKSTHKKFDDYGLPFTLNDVIGCYLDLDSRTIWWSKNGEQFPAAFSIDVKYKNSntCLFPAVLCQNSSLSVNFGSQP 167
Cdd:cd12873  81 KKSHGRQFDDYGEPFGLGDVIGCYLDLDNGTISFSKNGKDLGKAFDIPPHLRNS--ALFPAVCLKNAEVEFNFGDKP 155
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 11-167 1.68e-36

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: 131.94  E-value: 1.68e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990534  11 LNKQDQDLHLEIDETGLACKSEVKKR----WLGARGTAGLYgNGKYYYEVTITSK-------------GLCRVGWATLGG 73
Cdd:cd12884   3 LDTYNSDLHLKISKDRYSASPLTDEGfaylWAGARATYGVT-KGKVCFEVKVTENlpvkhlpteetdpHVVRVGWSVDSS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990534  74 SLNIGKGLDSFGYGGTGMKSTHKKFDDYGLPFTLNDVIGCYLDLDSR--TIWWSKNGEQFPAAFSIDvKYKNSNTCLFPA 151
Cdd:cd12884  82 SLQLGEEEFSYGYGSTGKKSTNCKFEDYGEPFGENDVIGCYLDFESEpvEISFSKNGKDLGVAFKIS-KEELGGKALFPH 160

                       170
                ....*....|....*.
gi 71990534 152 VLCQNSSLSVNFGSQP 167
Cdd:cd12884 161 VLTKNCAVEVNFGQKE 176
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 49-166 3.16e-26

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: 102.37  E-value: 3.16e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990534     49 NGKYYYEVTITSKGLCRVGWAT----LGGSLNIGKGLDSFGYGGT-GMKSTHKKFDDYGLPFTL-NDVIGCYLDLDSRTI 122
Cdd:smart00449   1 SGRHYFEVEIGDGGHWRVGVATksvpRGYFALLGEDKGSWGYDGDgGKKYHNSTGPEYGLPLQEpGDVIGCFLDLEAGTI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 71990534    123 WWSKNGEQ--FPAAFSIdvkykNSNTCLFPAVLCQNS-SLSVNFGSQ 166
Cdd:smart00449  81 SFYKNGKYlhGLAFFDV-----KFSGPLYPAFSLGSGnSVRLNFGPL 122
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 51-166 9.46e-26

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: 100.88  E-value: 9.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990534    51 KYYYEVTIT--SKGLCRVGWAT----LGGSLNIGKGLDSFGYGG-TGMKSTHKKFDDYGLP-FTLNDVIGCYLDLDSRTI 122
Cdd:pfam00622   1 RHYFEVEIFgqDGGGWRVGWATksvpRKGERFLGDESGSWGYDGwTGKKYWASTSPLTGLPlFEPGDVIGCFLDYEAGTI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 71990534   123 WWSKNGEQFPAAFSIDVKYKnsntCLFPAV-LCQNSSLSVNFGSQ 166
Cdd:pfam00622  81 SFTKNGKSLGYAFRDVPFAG----PLFPAVsLGAGEGLKFNFGLR 121
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 50-162 4.44e-22

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: 90.95  E-value: 4.44e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990534  50 GKYYYEVTI--TSKGLCRVGWATLGGSLNIGKGL----DSFGYGGTGMKSTHK-KFDDYGLPFTLNDVIGCYLDLDSRTI 122
Cdd:cd11709   1 GKWYWEVRVdsGNGGLIQVGWATKSFSLDGEGGVgddeESWGYDGSRLRKGHGgSSGPGGRPWKSGDVVGCLLDLDEGTL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 71990534 123 WWSKNGEQFPAAFSIDVKYKNSntcLFPAV-LCQNSSLSVN 162
Cdd:cd11709  81 SFSLNGKDLGVAFTNLFLKGGG---LYPAVsLGSGQGVTIN 118
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 40-164 4.33e-19

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: 82.76  E-value: 4.33e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990534  40 ARGTAGLYGnGKYYYEVTITSKGLCRVGWATLGGSLNIGKGL----DSFGYGGTGMKSTHKKFDDYGLPFTLNDVIGCYL 115
Cdd:cd12882   2 IRANACVYK-GKWMYEVTLGTKGIMQIGWATISCRFTQEEGVgdtrDSYAYDGNRVRKWNVSTQKYGEPWVAGDVIGCCI 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 71990534 116 DLDSRTIWWSKNGEQFPAAFSiDVKyKNSNTCLFPAV-LCQNSSLSVNFG 164
Cdd:cd12882  81 DLDKGTISFYRNGRSLGVAFD-NVR-RGPGLAYFPAVsLSFGERLELNFG 128
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 20-164 1.35e-17

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: 79.10  E-value: 1.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990534  20 LEIDETGLACKSEvkKRWLGARGTAGLYgNGKYYYEVTITS-----KGLCRVGWATLGGSLNIGKGLDSFGYG---GTGM 91
Cdd:cd12872   1 LKLSEDRLTVTGE--KGYRMARANHGVR-EGKWYFEVKILEgggteTGHVRVGWSRREASLQAPVGYDKYSYAirdKDGS 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71990534  92 KSTHKKFDDYGLP-FTLNDVIGCYLDLDSRTIWwsKNGEQFPAAFsidvkyKNSNTCL--FPAVLC-QNSSLSVNFG 164
Cdd:cd12872  78 KFHQSRGKPYGEPgFKEGDVIGFLITLPKIEFF--KNGKSQGVAF------EDIYGTGgyYPAVSLyKGATVTINFG 146
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 47-164 1.92e-16

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: 75.39  E-value: 1.92e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990534  47 YGNGKYYYEVTITS---KGLCRVGWATLGGSLNIGKGLD--SFGY-GGTGMKSTHKKFD-DYGLPFTLNDVIGCYLDLDS 119
Cdd:cd12885  11 PKVPVFYFEVTILDlgeKGIVSIGFCTSGFPLNRMPGWEdgSYGYhGDDGRVYLGGGEGeNYGPPFGTGDVVGCGINFKT 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 71990534 120 RTIWWSKNGEQFPAAFSIDVKYKnsntcLFPAVLCQNS--SLSVNFG 164
Cdd:cd12885  91 GEVFFTKNGELLGTAFENVVKGR-----LYPTVGLGSPgvKVRVNFG 132
SPRY_like cd12886
SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ...
 50-164 2.00e-13

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: 66.76  E-value: 2.00e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990534  50 GKYYYEVTITSKGL---CRVGWATLGGSLNIGKG---LDSFGYGG---TGMKSTH-KKFDDYGLPFTLNDVIGCYLDLDS 119
Cdd:cd12886   1 GKWYWEVTVVSSAAstyAGIGVANAAATGNNGLNgieLSSIGYSLgvySGNKLSNgSSVATYGAGFTAGDVIGVALDLDA 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 71990534 120 RTIWWSKNGEQF----PAAFSIDVkykNSNTCLFPAVLCQNS---SLSVNFG 164
Cdd:cd12886  81 GKIWFYKNGVWQgggdPAPGTNPA---FAGTAMYPAVTGGSStggSFTANFG 129
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 50-165 2.94e-13

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


Pssm-ID: 293966  Cd Length: 144  Bit Score: 66.78  E-value: 2.94e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990534  50 GKYYYEVTITSK---GLCRVGWATLGGSLNIGKGLD--SFGY----------GGTGMKsthkkfddYGLPFTLNDVIGCY 114
Cdd:cd12909  25 GIYYFEVKIISKgrdGYIGIGFSTKDVNLNRLPGWEphSWGYhgddghsfcsSGTGKP--------YGPTFTTGDVIGCG 96

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 71990534 115 LDLDSRTIWWSKNGEQFPAAFSiDVKYKNsntcLFPAVLCQ--NSSLSVNFGS 165
Cdd:cd12909  97 INFRDNTAFYTKNGVNLGIAFR-DIKKGN----LYPTVGLRtpGEHVEANFGQ 144
COG2865 COG2865
Predicted transcriptional regulator, contains HTH domain [Transcription];
227-321 2.23e-12

Predicted transcriptional regulator, contains HTH domain [Transcription];


Pssm-ID: 442112  Cd Length: 123  Bit Score: 63.75  E-value: 2.23e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990534 227 ELKRTQCKQDKdgsirrtlqpISKTICAFLNTDGGRLFLGVNDDKVIKGISMSKNMIYHFFGSLRHMcenfkpCSPLCRI 306
Cdd:COG2865  16 EFKESLNEPDE----------ILKTVCAFANTEGGTLLIGVDDDGEIVGLDDPDKLLERLENLIADN------ISPPIRP 79

                        90
                ....*....|....*..
gi 71990534 307 KVSILEV--IPVGVIKV 321
Cdd:COG2865  80 DVEEVEIdgKRVLVIEV 96
AlbA_2 pfam04326
Putative DNA-binding domain; This family belongs to the AlbA clan of DNA-binding domains.
 231-322 1.72e-11

Putative DNA-binding domain; This family belongs to the AlbA clan of DNA-binding domains.


Pssm-ID: 461263  Cd Length: 116  Bit Score: 60.78  E-value: 1.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990534   231 TQCKQDKDGSIRRTlqpISKTICAFLNTDGGRLFLGVNDDKVIKGIsmSKNMIYHFFGSLRHMCENFKPcsplcRIKVSI 310
Cdd:pfam04326   5 LEFKESLGKSSKKK---IAKTISAFANTEGGTIVIGVDDTGKIVGV--SDDEKDTEDLLKNQILDLIKP-----PIEVDI 74

                          90
                  ....*....|....*.
gi 71990534   311 LEV----IPVGVIKVK 322
Cdd:pfam04326  75 EEIeidgKYVLVVEIP 90
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 50-129 2.97e-11

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: 60.78  E-value: 2.97e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990534  50 GKYYYEVTITSKGLCRVGWATLGGSLNIGKGLDSFGYGGTGMKST--HKKFDDYGLPFTLNDVIGCYLDLDSRTIWWSKN 127
Cdd:cd12878  14 GKWYFEFEVLTSGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARkwHQGSESFGKQWQPGDVVGCMLDLVDRTISFTLN 93


                ..
gi 71990534 128 GE 129
Cdd:cd12878  94 GE 95
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
 50-132 1.53e-08

SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY domain is found at the N-terminus of RING finger domains which are present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RING-finger domain is a type of Zn-finger that binds two Zn atoms and is identified in proteins with a wide range of functions such as viral replication, signal transduction, and development.


Pssm-ID: 293941  Cd Length: 121  Bit Score: 52.74  E-value: 1.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990534  50 GKYYYEVTITSKGLCRVGWATLGGS-LN-----IGKGLDSFGYGGT---------GMKSTHKKFddyglpfTLNDVIGCY 114
Cdd:cd12883   1 GVWYYEVTVLTSGVMQIGWATKDSKfLNhegygIGDDEYSCAYDGCrqliwynakSKPHTHPRW-------KPGDVLGCL 73

                        90
                ....*....|....*...
gi 71990534 115 LDLDSRTIWWSKNGEQFP 132
Cdd:cd12883  74 LDLNKKQMIFSLNGNRLP 91
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 51-163 5.69e-07

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: 48.85  E-value: 5.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990534  51 KYYYEVTITSKGLC-------RVGWATL-------------GGSLnIGKGLDSFGYGGTGMKSTHKKF--DDYGLPF-TL 107
Cdd:cd12877  19 KWYFEVEVDHVEQFthqpahlRVGWANTsgyvpypgggegwGGNG-VGDDLYSYGFDGLHLWTGGRSRrvTSGTQHLlKK 97

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 71990534 108 NDVIGCYLDLDSRTIWWSKNGEQFPAAFsidvKYKNSNTCLFPaVLCQNSSLSVNF 163
Cdd:cd12877  98 GDVVGCCLDLSVPSISFRVNGRPVQGMF----ENFNLDGMFFP-VMSFSAGVSCRF 148
SPRY_HERC1 cd12881
SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to ...
 105-158 4.64e-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: 40.79  E-value: 4.64e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 71990534 105 FTLNDVIGCYLDLDSRTIWWSKNGEQFPAAFSiDVkyknSNTCLFPAVLCQNSS 158
Cdd:cd12881 104 FHQGDYITVVLDMEEGTLSFGKNGEEPGVAFE-DV----DATELYPCVMFYSSG 152
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH