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Conserved domains on  [gi|187609184]
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Chain A, SPRY domain-containing protein 3

Protein Classification

SPRY domain-containing protein( domain architecture ID 10191530)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPRYD3 cd12908
SPRY domain-containing protein 3; This family contains SPRY domain-containing protein 3 ...
 8-162 1.64e-89

SPRY domain-containing protein 3; This family contains SPRY domain-containing protein 3 (SPRYD3). In humans, it is highly expressed in most tissues, including brain, kidney, heart, intestine, skeletal muscle, and testis. It also has cross-species conservation, suggesting that it is likely to carry out important cellular processes.


:

Pssm-ID: 293965  Cd Length: 171  Bit Score: 258.77  E-value: 1.64e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187609184   8 FKHILVDGDTLSYHGNS-GEVGCYVASRPLTKDSNYFEVSIVDSGVRGTIAVGLVPQYYSLDHQPGWLPDSVAYHADDGK 86
Cdd:cd12908    4 LNDVRVNGDVLEYHGRGiGDVGLAQARRPLSPDNHYFEVEIVDPGVRCYIAIGLAPQDYPLDRHPGWNPGSVAYHADDGK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187609184  87 LYNGRAKGRQFGSKCNSGDRIGCGIEPVSFD------------VQTAQIFFTKNGKRVGSTI*P*SPDGLFPAVG*HSLG 154
Cdd:cd12908   84 LFKGSGVGDQFGPRCTKGDRMGCGIRFPRDYdtdsedqgdeeeGRTVQVFFTRNGKEVGRTEVPLPPGGFYPAVGMHSEG 163


                 ....*...
gi 187609184 155 EEVRLHLN 162
Cdd:cd12908  164 EKVRVDLH 171
 
Name Accession Description Interval E-value
SPRYD3 cd12908
SPRY domain-containing protein 3; This family contains SPRY domain-containing protein 3 ...
 8-162 1.64e-89

SPRY domain-containing protein 3; This family contains SPRY domain-containing protein 3 (SPRYD3). In humans, it is highly expressed in most tissues, including brain, kidney, heart, intestine, skeletal muscle, and testis. It also has cross-species conservation, suggesting that it is likely to carry out important cellular processes.


Pssm-ID: 293965  Cd Length: 171  Bit Score: 258.77  E-value: 1.64e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187609184   8 FKHILVDGDTLSYHGNS-GEVGCYVASRPLTKDSNYFEVSIVDSGVRGTIAVGLVPQYYSLDHQPGWLPDSVAYHADDGK 86
Cdd:cd12908    4 LNDVRVNGDVLEYHGRGiGDVGLAQARRPLSPDNHYFEVEIVDPGVRCYIAIGLAPQDYPLDRHPGWNPGSVAYHADDGK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187609184  87 LYNGRAKGRQFGSKCNSGDRIGCGIEPVSFD------------VQTAQIFFTKNGKRVGSTI*P*SPDGLFPAVG*HSLG 154
Cdd:cd12908   84 LFKGSGVGDQFGPRCTKGDRMGCGIRFPRDYdtdsedqgdeeeGRTVQVFFTRNGKEVGRTEVPLPPGGFYPAVGMHSEG 163


                 ....*...
gi 187609184 155 EEVRLHLN 162
Cdd:cd12908  164 EKVRVDLH 171
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 42-152 7.29e-11

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: 56.53  E-value: 7.29e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187609184    42 YFEVSIVDSGVrgtIAVGLVPQYYSLDHQ--PGWLPDSVAYHADDGKLYNGRaKGRQFGSKC-NSGDRIGCGIepvsfDV 118
Cdd:smart00449   5 YFEVEIGDGGH---WRVGVATKSVPRGYFalLGEDKGSWGYDGDGGKKYHNS-TGPEYGLPLqEPGDVIGCFL-----DL 75

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 187609184   119 QTAQIFFTKNGKRVGSTI*P*SP--DGLFPAVG*HS 152
Cdd:smart00449  76 EAGTISFYKNGKYLHGLAFFDVKfsGPLYPAFSLGS 111
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 42-161 1.48e-10

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: 55.81  E-value: 1.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187609184   42 YFEVsIVDSGVRGTIAVGLV-PQYYSLDHQ-PGWLPDSVAYHADDGKLYNGRaKGRQFGSKCN-SGDRIGCGIEpvsFDV 118
Cdd:pfam00622   3 YFEV-EIFGQDGGGWRVGWAtKSVPRKGERfLGDESGSWGYDGWTGKKYWAS-TSPLTGLPLFePGDVIGCFLD---YEA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 187609184  119 QTaqIFFTKNGKRVGSTI-*P*SPDGLFPAVG*HSlGEEVRLHL 161
Cdd:pfam00622  78 GT--ISFTKNGKSLGYAFrDVPFAGPLFPAVSLGA-GEGLKFNF 118
 
Name Accession Description Interval E-value
SPRYD3 cd12908
SPRY domain-containing protein 3; This family contains SPRY domain-containing protein 3 ...
 8-162 1.64e-89

SPRY domain-containing protein 3; This family contains SPRY domain-containing protein 3 (SPRYD3). In humans, it is highly expressed in most tissues, including brain, kidney, heart, intestine, skeletal muscle, and testis. It also has cross-species conservation, suggesting that it is likely to carry out important cellular processes.


Pssm-ID: 293965  Cd Length: 171  Bit Score: 258.77  E-value: 1.64e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187609184   8 FKHILVDGDTLSYHGNS-GEVGCYVASRPLTKDSNYFEVSIVDSGVRGTIAVGLVPQYYSLDHQPGWLPDSVAYHADDGK 86
Cdd:cd12908    4 LNDVRVNGDVLEYHGRGiGDVGLAQARRPLSPDNHYFEVEIVDPGVRCYIAIGLAPQDYPLDRHPGWNPGSVAYHADDGK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187609184  87 LYNGRAKGRQFGSKCNSGDRIGCGIEPVSFD------------VQTAQIFFTKNGKRVGSTI*P*SPDGLFPAVG*HSLG 154
Cdd:cd12908   84 LFKGSGVGDQFGPRCTKGDRMGCGIRFPRDYdtdsedqgdeeeGRTVQVFFTRNGKEVGRTEVPLPPGGFYPAVGMHSEG 163


                 ....*...
gi 187609184 155 EEVRLHLN 162
Cdd:cd12908  164 EKVRVDLH 171
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 28-161 2.12e-37

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: 125.08  E-value: 2.12e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187609184  28 GCYVASRPL--TKDSNYFEVSIVDSGVRGTIAVGLVPQYYSLDHQPGWLPDSVAYHADDGKLYNGRAKGRQFGSKCNSGD 105
Cdd:cd12885    1 GSVRADHPIppKVPVFYFEVTILDLGEKGIVSIGFCTSGFPLNRMPGWEDGSYGYHGDDGRVYLGGGEGENYGPPFGTGD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 187609184 106 RIGCGIepvsfDVQTAQIFFTKNGKRVGSTI*P*SPDGLFPAVG*HSLGEEVRLHL 161
Cdd:cd12885   81 VVGCGI-----NFKTGEVFFTKNGELLGTAFENVVKGRLYPTVGLGSPGVKVRVNF 131
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 42-158 2.46e-29

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: 104.91  E-value: 2.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187609184  42 YFEVSIVDSGVRGTIAVGLVPQYYSLDHQPGWLPDSVAYHADDGKLYNGRAKGRQFGSKCNSGDRIGCGIepvsfDVQTA 121
Cdd:cd12909   28 YFEVKIISKGRDGYIGIGFSTKDVNLNRLPGWEPHSWGYHGDDGHSFCSSGTGKPYGPTFTTGDVIGCGI-----NFRDN 102

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 187609184 122 QIFFTKNGKRVGSTI*P*SPDGLFPAVG*HSLGEEVR 158
Cdd:cd12909  103 TAFYTKNGVNLGIAFRDIKKGNLYPTVGLRTPGEHVE 139
SPRY_SSH4_like cd12910
SPRY domain in SSH4 and similar proteins; This family includes SPRY domain in SSH4 (suppressor ...
 24-162 6.72e-21

SPRY domain in SSH4 and similar proteins; This family includes SPRY domain in SSH4 (suppressor of SHR3 null mutation protein 4) and similar proteins. SSH4 is a component of the endosome-vacuole trafficking pathway that regulates nutrient transport and may be involved in processes determining whether plasma membrane proteins are degraded or routed to the plasma membrane. 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. In yeast, SSH4 and the homologous protein EAR1 (endosomal adapter of RSP5) recruit Rsp5p, an essential ubiquitin ligase of the Nedd4 family, and assist it in its function at multivesicular bodies by directing the ubiquitylation of specific cargoes.


Pssm-ID: 293967  Cd Length: 192  Bit Score: 84.72  E-value: 6.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187609184  24 SGEVGCYVASRPLTKDSN---YFEVSIVDSGVR--GTIAVGLVPQYYSLDHQPGWLPDSVAYHADDGKLY-NGRAKGRQF 97
Cdd:cd12910   37 SLPLYSVQTNLPLPTGRPktiYFEVKIFELPRAddTSVAIGFATKPYPPFRLPGWHRGSLAVHSDDGHRYiNDPFGGKDF 116

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187609184  98 GSKCNSGDRIGCGIEPvsfdvQTAQIFFTKNGKRVGS----------TI*P*SPDG---LFPAVG*hSLGEEVRLHLN 162
Cdd:cd12910  117 TPPFREGDTIGIGYRF-----SSGTIFFTRNGKRLGGwdlgeeldaeDDGVTGLEGfhdLYAAIG--VFGGECEVHVN 187
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 41-160 8.05e-15

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: 8.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187609184  41 NYFEVsIVDSGVRGTIAVGLVPQYYSLDHQPGWLPDSVAYHADDGKLYNG-RAKGRQFGSKCNSGDRIGCGIepvsfDVQ 119
Cdd:cd11709    3 WYWEV-RVDSGNGGLIQVGWATKSFSLDGEGGVGDDEESWGYDGSRLRKGhGGSSGPGGRPWKSGDVVGCLL-----DLD 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 187609184 120 TAQIFFTKNGKRVG--STI*P*SPDGLFPAVG*HSlGEEVRLH 160
Cdd:cd11709   77 EGTLSFSLNGKDLGvaFTNLFLKGGGLYPAVSLGS-GQGVTIN 118
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 42-152 7.29e-11

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: 56.53  E-value: 7.29e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187609184    42 YFEVSIVDSGVrgtIAVGLVPQYYSLDHQ--PGWLPDSVAYHADDGKLYNGRaKGRQFGSKC-NSGDRIGCGIepvsfDV 118
Cdd:smart00449   5 YFEVEIGDGGH---WRVGVATKSVPRGYFalLGEDKGSWGYDGDGGKKYHNS-TGPEYGLPLqEPGDVIGCFL-----DL 75

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 187609184   119 QTAQIFFTKNGKRVGSTI*P*SP--DGLFPAVG*HS 152
Cdd:smart00449  76 EAGTISFYKNGKYLHGLAFFDVKfsGPLYPAFSLGS 111
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 42-161 1.48e-10

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: 55.81  E-value: 1.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187609184   42 YFEVsIVDSGVRGTIAVGLV-PQYYSLDHQ-PGWLPDSVAYHADDGKLYNGRaKGRQFGSKCN-SGDRIGCGIEpvsFDV 118
Cdd:pfam00622   3 YFEV-EIFGQDGGGWRVGWAtKSVPRKGERfLGDESGSWGYDGWTGKKYWAS-TSPLTGLPLFePGDVIGCFLD---YEA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 187609184  119 QTaqIFFTKNGKRVGSTI-*P*SPDGLFPAVG*HSlGEEVRLHL 161
Cdd:pfam00622  78 GT--ISFTKNGKSLGYAFrDVPFAGPLFPAVSLGA-GEGLKFNF 118
SPRY_HECT_like cd13735
SPRY domain in HECT E3; This domain consists of the SPRY subdomain similar to those found at ...
 35-162 4.24e-05

SPRY domain in HECT E3; This domain consists of the SPRY subdomain similar to those found at the N-terminus of the HECT (homologous to the E6AP carboxyl terminus) protein, a C-terminal catalytic domain of a subclass of ubiquitin-protein ligase (E3). HECT E3 binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains. It has a prominent role in protein trafficking and immune response, and is involved in crucial signaling pathways implicated in tumorigenesis.


Pssm-ID: 293970 [Multi-domain]  Cd Length: 150  Bit Score: 41.36  E-value: 4.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187609184  35 PLTKDSNYFEVSIVDSGVRGT-----IAVGLVPQYYSLDHQPGWLPDSVAYHaDDGKLYNGRAKGRQFGSKCNS------ 103
Cdd:cd13735   12 PAQAPSFYWEVEVVSLGETDDsdgpiISVGFAPPAEDRDGAWTNPVGTCLFH-NNGRAVHYRGSSLTQWKSIRTdvtlsi 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 187609184 104 GDRIGCGIEPVSFDVQTAQIFFTKNGKRVGSTI*p*SPDGLFPAVg*HSLGEEVRLHLN 162
Cdd:cd13735   91 GDVAGCGWERTDTPPAKGRVYFTHNGQRLPRSLQ-DVSGGLWPVV--HVQKKNTRVRAN 146
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 32-133 3.89e-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: 35.96  E-value: 3.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187609184  32 ASRPLTKDSNYFEVSIVDSGVRGT--IAVGLVPQYYSLDHQPGWLPDSVAYHADDGKLYNgRAKGRQFGSKC-NSGDRIG 108
Cdd:cd12872   21 ANHGVREGKWYFEVKILEGGGTETghVRVGWSRREASLQAPVGYDKYSYAIRDKDGSKFH-QSRGKPYGEPGfKEGDVIG 99

                         90       100
                 ....*....|....*....|....*
gi 187609184 109 CGIEpvsfdvqTAQIFFTKNGKRVG 133
Cdd:cd12872  100 FLIT-------LPKIEFFKNGKSQG 117
SPRY_like cd12886
SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ...
 42-154 5.39e-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: 35.18  E-value: 5.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187609184  42 YFEVSIVDSGVRGTIAVGLVPQYYSLDHQPGWLPDS---VAYHADDGKLYNGRAKGRQFGSKCNSGDRIGcgiepVSFDV 118
Cdd:cd12886    4 YWEVTVVSSAASTYAGIGVANAAATGNNGLNGIELSsigYSLGVYSGNKLSNGSSVATYGAGFTAGDVIG-----VALDL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 187609184 119 QTAQIFFTKNGKRVGS------TI*P*SPDGLFPAVG*HSLG 154
Cdd:cd12886   79 DAGKIWFYKNGVWQGGgdpapgTNPAFAGTAMYPAVTGGSST 120
 
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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