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Conserved domains on  [gi|42571745|ref|NP_973963|]
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SPla/RYanodine receptor (SPRY) domain-containing protein [Arabidopsis thaliana]

Protein Classification

SPRY domain-containing protein( domain architecture ID 10191465)

SPRY (SPla and the RYanodine receptor) domain-containing protein similar to Globodera rostochiensis SPRY domain-containing effector SS15

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 85-215 5.94e-55

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: 179.40  E-value: 5.94e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571745  85 GVVQANKPAPIKCLTYYFEIFVKDSGIKGQIAIGFTKESFKMRRQPGWEVNSCGYHGDDGYLYRGQGKGEPFGPKFTKDD 164
Cdd:cd12885   1 GSVRADHPIPPKVPVFYFEVTILDLGEKGIVSIGFCTSGFPLNRMPGWEDGSYGYHGDDGRVYLGGGEGENYGPPFGTGD 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571745 165 AVGGGINYASQEFFFTKNGTIVGKIPKDI-RGHLFPTVAVHSQNEEVLVNFG 215
Cdd:cd12885  81 VVGCGINFKTGEVFFTKNGELLGTAFENVvKGRLYPTVGLGSPGVKVRVNFG 132
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 349-452 3.43e-21

CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, fungi)


:

Pssm-ID: 214806  Cd Length: 99  Bit Score: 88.12  E-value: 3.43e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571745    349 GKLEEGVNYGRLELAKFVGLTG-FQDIVEDCFALLAYEKP-EESSVWYFLEDSQRELVADAVNAAILSTNPNKkdvqrsc 426
Cdd:smart00757   1 GKIEEALAYARELLAPFAKEHEkFLKELEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILELLHGK------- 73

                           90       100
                   ....*....|....*....|....*.
gi 42571745    427 HLQSHLEKLLRQLTVCCLERRSLNGD 452
Cdd:smart00757  74 SSESPLEILLSAGLAALKTLLEKGGV 99
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 296-353 2.95e-14

C-terminal to LisH motif; Alpha-helical motif of unknown function.


:

Pssm-ID: 128914  Cd Length: 58  Bit Score: 67.21  E-value: 2.95e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 42571745    296 LKQRKNLRQLVRNGEIDTALAELQKLYPQIVQDDKSVvCFLLHCQKFIELVRVGKLEE 353
Cdd:smart00668   2 FDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKL-EFELRKQKFLELVRQGKLEE 58
 
Name Accession Description Interval E-value
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 85-215 5.94e-55

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: 179.40  E-value: 5.94e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571745  85 GVVQANKPAPIKCLTYYFEIFVKDSGIKGQIAIGFTKESFKMRRQPGWEVNSCGYHGDDGYLYRGQGKGEPFGPKFTKDD 164
Cdd:cd12885   1 GSVRADHPIPPKVPVFYFEVTILDLGEKGIVSIGFCTSGFPLNRMPGWEDGSYGYHGDDGRVYLGGGEGENYGPPFGTGD 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571745 165 AVGGGINYASQEFFFTKNGTIVGKIPKDI-RGHLFPTVAVHSQNEEVLVNFG 215
Cdd:cd12885  81 VVGCGINFKTGEVFFTKNGELLGTAFENVvKGRLYPTVGLGSPGVKVRVNFG 132
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 349-452 3.43e-21

CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, fungi)


Pssm-ID: 214806  Cd Length: 99  Bit Score: 88.12  E-value: 3.43e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571745    349 GKLEEGVNYGRLELAKFVGLTG-FQDIVEDCFALLAYEKP-EESSVWYFLEDSQRELVADAVNAAILSTNPNKkdvqrsc 426
Cdd:smart00757   1 GKIEEALAYARELLAPFAKEHEkFLKELEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILELLHGK------- 73

                           90       100
                   ....*....|....*....|....*.
gi 42571745    427 HLQSHLEKLLRQLTVCCLERRSLNGD 452
Cdd:smart00757  74 SSESPLEILLSAGLAALKTLLEKGGV 99
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
 297-414 5.60e-21

CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. This domain is at the C-terminus of the proteins and is the binding domain for the CRA motif (for CT11-RanBPM), which is comprised of approximately 100 amino acids at the C terminal of RanBPM. It was found to be important for the interaction of RanBPM with fragile X mental retardation protein (FMRP), but its functional significance has yet to be determined. This region contains CTLH and CRA domains annotated by SMART; however, these may be a single domain, and it is refereed to as a C-terminal to LisH motif.


Pssm-ID: 402305 [Multi-domain]  Cd Length: 143  Bit Score: 88.78  E-value: 5.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571745   297 KQRKNLRQLVRNGEIDTALAELQKLYPQIVQDDKSVVcFLLHCQKFIELVRVGKLEEGVNYGRLELAKFVGltGFQDIVE 376
Cdd:pfam10607   3 KERNRILEAILNGDITEAIEWCNENKPELLKINSNLE-FELRLQQFIELIRSGKILEALEYARENLAPFNE--EHLKELE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 42571745   377 DCFALLAYEKPEESSVwYF--LEDSQRELVADAVNAAILS 414
Cdd:pfam10607  80 KLMGLLAFPDPTDSSP-YKslLSPSRWEKLASEFNRAILK 118
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 99-216 9.11e-19

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: 82.01  E-value: 9.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571745    99 TYYFEIFVkDSGIKGQIAIGFTKES--FKMRRQPGWEVNSCGYHGDDGYLYrGQGKGEPFG-PKFTKDDAVGGGINYASQ 175
Cdd:pfam00622   1 RHYFEVEI-FGQDGGGWRVGWATKSvpRKGERFLGDESGSWGYDGWTGKKY-WASTSPLTGlPLFEPGDVIGCFLDYEAG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 42571745   176 EFFFTKNGTIVGKIPKDIR--GHLFPTVAVhSQNEEVLVNFGK 216
Cdd:pfam00622  79 TISFTKNGKSLGYAFRDVPfaGPLFPAVSL-GAGEGLKFNFGL 120
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 296-353 2.95e-14

C-terminal to LisH motif; Alpha-helical motif of unknown function.


Pssm-ID: 128914  Cd Length: 58  Bit Score: 67.21  E-value: 2.95e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 42571745    296 LKQRKNLRQLVRNGEIDTALAELQKLYPQIVQDDKSVvCFLLHCQKFIELVRVGKLEE 353
Cdd:smart00668   2 FDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKL-EFELRKQKFLELVRQGKLEE 58
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 99-216 4.49e-13

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: 65.78  E-value: 4.49e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571745     99 TYYFEIFVKDsgiKGQIAIGFTKES--FKMRRQPGWEVNSCGYHGDDGYLYRgQGKGEPFGPKFT-KDDAVGGGINYASQ 175
Cdd:smart00449   3 RHYFEVEIGD---GGHWRVGVATKSvpRGYFALLGEDKGSWGYDGDGGKKYH-NSTGPEYGLPLQePGDVIGCFLDLEAG 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 42571745    176 EFFFTKNGTIVGKIPK---DIRGHLFPTVAVHSQNEEVlVNFGK 216
Cdd:smart00449  79 TISFYKNGKYLHGLAFfdvKFSGPLYPAFSLGSGNSVR-LNFGP 121
 
Name Accession Description Interval E-value
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 85-215 5.94e-55

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: 179.40  E-value: 5.94e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571745  85 GVVQANKPAPIKCLTYYFEIFVKDSGIKGQIAIGFTKESFKMRRQPGWEVNSCGYHGDDGYLYRGQGKGEPFGPKFTKDD 164
Cdd:cd12885   1 GSVRADHPIPPKVPVFYFEVTILDLGEKGIVSIGFCTSGFPLNRMPGWEDGSYGYHGDDGRVYLGGGEGENYGPPFGTGD 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571745 165 AVGGGINYASQEFFFTKNGTIVGKIPKDI-RGHLFPTVAVHSQNEEVLVNFG 215
Cdd:cd12885  81 VVGCGINFKTGEVFFTKNGELLGTAFENVvKGRLYPTVGLGSPGVKVRVNFG 132
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 81-215 5.73e-46

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: 156.53  E-value: 5.73e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571745  81 GHDVGVVQANKPAPIKCLTYYFEIFVKDSGIKGQIAIGFTKESFKMRRQPGWEVNSCGYHGDDGYLYRGQGKGEPFGPKF 160
Cdd:cd12909   8 DKDAAAVRANHPIPPQCGIYYFEVKIISKGRDGYIGIGFSTKDVNLNRLPGWEPHSWGYHGDDGHSFCSSGTGKPYGPTF 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42571745 161 TKDDAVGGGINYASQEFFFTKNGTIVGKIPKDI-RGHLFPTVAVHSQNEEVLVNFG 215
Cdd:cd12909  88 TTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIkKGNLYPTVGLRTPGEHVEANFG 143
SPRYD3 cd12908
SPRY domain-containing protein 3; This family contains SPRY domain-containing protein 3 ...
 72-214 7.29e-37

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: 133.19  E-value: 7.29e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571745  72 VKYTNTNL--HG---HDVGVVQANKPapIKCLTYYFEIFVKDSGIKGQIAIGFTKESFKMRRQPGWEVNSCGYHGDDGYL 146
Cdd:cd12908   7 VRVNGDVLeyHGrgiGDVGLAQARRP--LSPDNHYFEVEIVDPGVRCYIAIGLAPQDYPLDRHPGWNPGSVAYHADDGKL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571745 147 YRGQGKGEPFGPKFTKDDAVGGGI----NYASQEF-------------FFTKNGTIVGKIPKDIRGH-LFPTVAVHSQNE 208
Cdd:cd12908  85 FKGSGVGDQFGPRCTKGDRMGCGIrfprDYDTDSEdqgdeeegrtvqvFFTRNGKEVGRTEVPLPPGgFYPAVGMHSEGE 164


                ....*.
gi 42571745 209 EVLVNF 214
Cdd:cd12908 165 KVRVDL 170
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 349-452 3.43e-21

CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, fungi)


Pssm-ID: 214806  Cd Length: 99  Bit Score: 88.12  E-value: 3.43e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571745    349 GKLEEGVNYGRLELAKFVGLTG-FQDIVEDCFALLAYEKP-EESSVWYFLEDSQRELVADAVNAAILSTNPNKkdvqrsc 426
Cdd:smart00757   1 GKIEEALAYARELLAPFAKEHEkFLKELEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILELLHGK------- 73

                           90       100
                   ....*....|....*....|....*.
gi 42571745    427 HLQSHLEKLLRQLTVCCLERRSLNGD 452
Cdd:smart00757  74 SSESPLEILLSAGLAALKTLLEKGGV 99
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
 297-414 5.60e-21

CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. This domain is at the C-terminus of the proteins and is the binding domain for the CRA motif (for CT11-RanBPM), which is comprised of approximately 100 amino acids at the C terminal of RanBPM. It was found to be important for the interaction of RanBPM with fragile X mental retardation protein (FMRP), but its functional significance has yet to be determined. This region contains CTLH and CRA domains annotated by SMART; however, these may be a single domain, and it is refereed to as a C-terminal to LisH motif.


Pssm-ID: 402305 [Multi-domain]  Cd Length: 143  Bit Score: 88.78  E-value: 5.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571745   297 KQRKNLRQLVRNGEIDTALAELQKLYPQIVQDDKSVVcFLLHCQKFIELVRVGKLEEGVNYGRLELAKFVGltGFQDIVE 376
Cdd:pfam10607   3 KERNRILEAILNGDITEAIEWCNENKPELLKINSNLE-FELRLQQFIELIRSGKILEALEYARENLAPFNE--EHLKELE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 42571745   377 DCFALLAYEKPEESSVwYF--LEDSQRELVADAVNAAILS 414
Cdd:pfam10607  80 KLMGLLAFPDPTDSSP-YKslLSPSRWEKLASEFNRAILK 118
SPRY_SSH4_like cd12910
SPRY domain in SSH4 and similar proteins; This family includes SPRY domain in SSH4 (suppressor ...
 87-216 8.30e-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: 89.73  E-value: 8.30e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571745  87 VQANKPAPI-KCLTYYFE--IFVKDSGIKGQIAIGFTKESFKMRRQPGWEVNSCGYHGDDGYLYRGQG-KGEPFGPKFTK 162
Cdd:cd12910  43 VQTNLPLPTgRPKTIYFEvkIFELPRADDTSVAIGFATKPYPPFRLPGWHRGSLAVHSDDGHRYINDPfGGKDFTPPFRE 122

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42571745 163 DDAVGGGINYASQEFFFTKNGTIVGKIPKDIRGH--------------LFPTVAVHSQNEEVLVNFGK 216
Cdd:cd12910 123 GDTIGIGYRFSSGTIFFTRNGKRLGGWDLGEELDaeddgvtglegfhdLYAAIGVFGGECEVHVNPGQ 190
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 99-216 9.11e-19

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: 82.01  E-value: 9.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571745    99 TYYFEIFVkDSGIKGQIAIGFTKES--FKMRRQPGWEVNSCGYHGDDGYLYrGQGKGEPFG-PKFTKDDAVGGGINYASQ 175
Cdd:pfam00622   1 RHYFEVEI-FGQDGGGWRVGWATKSvpRKGERFLGDESGSWGYDGWTGKKY-WASTSPLTGlPLFEPGDVIGCFLDYEAG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 42571745   176 EFFFTKNGTIVGKIPKDIR--GHLFPTVAVhSQNEEVLVNFGK 216
Cdd:pfam00622  79 TISFTKNGKSLGYAFRDVPfaGPLFPAVSL-GAGEGLKFNFGL 120
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 296-353 2.95e-14

C-terminal to LisH motif; Alpha-helical motif of unknown function.


Pssm-ID: 128914  Cd Length: 58  Bit Score: 67.21  E-value: 2.95e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 42571745    296 LKQRKNLRQLVRNGEIDTALAELQKLYPQIVQDDKSVvCFLLHCQKFIELVRVGKLEE 353
Cdd:smart00668   2 FDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKL-EFELRKQKFLELVRQGKLEE 58
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 99-216 4.49e-13

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: 65.78  E-value: 4.49e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571745     99 TYYFEIFVKDsgiKGQIAIGFTKES--FKMRRQPGWEVNSCGYHGDDGYLYRgQGKGEPFGPKFT-KDDAVGGGINYASQ 175
Cdd:smart00449   3 RHYFEVEIGD---GGHWRVGVATKSvpRGYFALLGEDKGSWGYDGDGGKKYH-NSTGPEYGLPLQePGDVIGCFLDLEAG 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 42571745    176 EFFFTKNGTIVGKIPK---DIRGHLFPTVAVHSQNEEVlVNFGK 216
Cdd:smart00449  79 TISFYKNGKYLHGLAFfdvKFSGPLYPAFSLGSGNSVR-LNFGP 121
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 100-213 1.28e-08

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: 52.82  E-value: 1.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571745 100 YYFEIFVkDSGIKGQIAIGFTKESFKMR--RQPGWEVNSCGYHGDdgYLYRG-QGKGEPFGPKFTKDDAVGGGINYASQE 176
Cdd:cd11709   3 WYWEVRV-DSGNGGLIQVGWATKSFSLDgeGGVGDDEESWGYDGS--RLRKGhGGSSGPGGRPWKSGDVVGCLLDLDEGT 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 42571745 177 FFFTKNGTIVG---KIPKDIRGHLFPTVAVHSqNEEVLVN 213
Cdd:cd11709  80 LSFSLNGKDLGvafTNLFLKGGGLYPAVSLGS-GQGVTIN 118
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 59-218 1.70e-08

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: 53.35  E-value: 1.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571745  59 AGGFLVVSPDKLSVK-YTNTNLHGhdvgvVQANKPAPIKClTYYFEIFVKDSGIkgqIAIgftkesfkmrrqpGWEVNSC 137
Cdd:cd12873   6 RDAALAISPDGLLCQsREEKGWQG-----CRATKGVKGKG-KYYYEVTVTDEGL---CRV-------------GWSTEDA 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571745 138 GYH-GDD--GYLYRGQGK----------GEPFGpkftKDDAVGGGINYASQEFFFTKNGTIVGK---IPKDIRG-HLFPT 200
Cdd:cd12873  64 SLDlGTDkfGFGYGGTGKkshgrqfddyGEPFG----LGDVIGCYLDLDNGTISFSKNGKDLGKafdIPPHLRNsALFPA 139

                       170
                ....*....|....*...
gi 42571745 201 VAVhsQNEEVLVNFGKKK 218
Cdd:cd12873 140 VCL--KNAEVEFNFGDKP 155
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 99-219 1.14e-07

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: 50.98  E-value: 1.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571745  99 TYYFEIFVKDSGI--KGQIAIGFTkesfkmRRQPGWEVNsCGYHGDdGYLYRG-------QGKGEPFGPK-FTKDDAVGG 168
Cdd:cd12872  29 KWYFEVKILEGGGteTGHVRVGWS------RREASLQAP-VGYDKY-SYAIRDkdgskfhQSRGKPYGEPgFKEGDVIGF 100

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 42571745 169 GINYASQEFFftKNGTIVGKIPKDIRGHL--FPTVAVHsQNEEVLVNFGKKKF 219
Cdd:cd12872 101 LITLPKIEFF--KNGKSQGVAFEDIYGTGgyYPAVSLY-KGATVTINFGPDFK 150
SPRY_HECT_like cd13735
SPRY domain in HECT E3; This domain consists of the SPRY subdomain similar to those found at ...
 87-215 1.06e-06

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: 48.29  E-value: 1.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571745  87 VQANKPAPIKCLTYYFEIFVKDSGIKGQ-----IAIGFTKESFKMRRQPGWEVNSCGYHGDD-GYLYRGQG--------- 151
Cdd:cd13735   5 VYANSPIPAQAPSFYWEVEVVSLGETDDsdgpiISVGFAPPAEDRDGAWTNPVGTCLFHNNGrAVHYRGSSltqwksirt 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42571745 152 -----KGEPFGPKFTKDDA--VGGGInyasqefFFTKNGTIVGKIPKDIRGHLFPTVAVHSQNEEVLVNFG 215
Cdd:cd13735  85 dvtlsIGDVAGCGWERTDTppAKGRV-------YFTHNGQRLPRSLQDVSGGLWPVVHVQKKNTRVRANFG 148
 
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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