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Conserved domains on  [gi|24649737|ref|NP_733024|]
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absent, small, or homeotic discs 2, isoform B [Drosophila melanogaster]

Protein Classification

SPRY domain-containing protein( domain architecture ID 10191332)

SPRY (SPla and the RYanodine receptor) domain-containing protein; similar to Saccharomyces cerevisiae COMPASS component BRE2 and Arabidopsis thaliana protein TRAUCO

CATH:  2.60.120.920
Gene Ontology:  GO:0005515
PubMed:  23164942|16313355|23139046
SCOP:  4001665

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 114-304 3.37e-75

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: 228.56  E-value: 3.37e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737 114 LKISEDRLAVTGERGYCMVRATHSVNRGCWYFEVTIEEMP--DGAATRLGWGREYGNLQAPLGYDKFGYSWRSRKGTKFT 191
Cdd:cd12872   1 LKLSEDRLTVTGEKGYRMARANHGVREGKWYFEVKILEGGgtETGHVRVGWSRREASLQAPVGYDKYSYAIRDKDGSKFH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737 192 ESHGKHYSD-AYVEGDTLGFLIELPEeasldylpntfkdrplvkfkshlyyedkdkitetlknlhilqgsrIEFFKNGQS 270
Cdd:cd12872  81 QSRGKPYGEpGFKEGDVIGFLITLPK---------------------------------------------IEFFKNGKS 115

                       170       180       190
                ....*....|....*....|....*....|....*
gi 24649737 271 QGVAFEDI-YAGSYFPAISIHKSATVSVNFGPAFK 304
Cdd:cd12872 116 QGVAFEDIyGTGGYYPAVSLYKGATVTINFGPDFK 150
 
Name Accession Description Interval E-value
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 114-304 3.37e-75

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: 228.56  E-value: 3.37e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737 114 LKISEDRLAVTGERGYCMVRATHSVNRGCWYFEVTIEEMP--DGAATRLGWGREYGNLQAPLGYDKFGYSWRSRKGTKFT 191
Cdd:cd12872   1 LKLSEDRLTVTGEKGYRMARANHGVREGKWYFEVKILEGGgtETGHVRVGWSRREASLQAPVGYDKYSYAIRDKDGSKFH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737 192 ESHGKHYSD-AYVEGDTLGFLIELPEeasldylpntfkdrplvkfkshlyyedkdkitetlknlhilqgsrIEFFKNGQS 270
Cdd:cd12872  81 QSRGKPYGEpGFKEGDVIGFLITLPK---------------------------------------------IEFFKNGKS 115

                       170       180       190
                ....*....|....*....|....*....|....*
gi 24649737 271 QGVAFEDI-YAGSYFPAISIHKSATVSVNFGPAFK 304
Cdd:cd12872 116 QGVAFEDIyGTGGYYPAVSLYKGATVTINFGPDFK 150
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 140-301 9.64e-20

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: 83.50  E-value: 9.64e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737    140 RGCWYFEVTIEempDGAATRLGWGREYGNL--QAPLGYDKFGYSWRSRKGTKFTESHGKHYSDAYVE-GDTLGFLIELPE 216
Cdd:smart00449   1 SGRHYFEVEIG---DGGHWRVGVATKSVPRgyFALLGEDKGSWGYDGDGGKKYHNSTGPEYGLPLQEpGDVIGCFLDLEA 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737    217 EasldylpntfkdrplvkfkshlyyedkdkitetlknlhilqgsRIEFFKNG-QSQGVAFEDIYA-GSYFPAISIHKSAT 294
Cdd:smart00449  78 G-------------------------------------------TISFYKNGkYLHGLAFFDVKFsGPLYPAFSLGSGNS 114


                   ....*..
gi 24649737    295 VSVNFGP 301
Cdd:smart00449 115 VRLNFGP 121
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 143-300 2.35e-14

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: 68.91  E-value: 2.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737   143 WYFEVTIEEmPDGAATRLGWGRE--YGNLQAPLGYDKFGYSWRSRKGTKFTESHGKHYSDA-YVEGDTLGFLIELPEEas 219
Cdd:pfam00622   2 HYFEVEIFG-QDGGGWRVGWATKsvPRKGERFLGDESGSWGYDGWTGKKYWASTSPLTGLPlFEPGDVIGCFLDYEAG-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737   220 ldylpntfkdrplvkfkshlyyedkdkitetlknlhilqgsRIEFFKNGQSQGVAFEDIY-AGSYFPAISIHKSATVSVN 298
Cdd:pfam00622  79 -----------------------------------------TISFTKNGKSLGYAFRDVPfAGPLFPAVSLGAGEGLKFN 117


                  ..
gi 24649737   299 FG 300
Cdd:pfam00622 118 FG 119
 
Name Accession Description Interval E-value
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 114-304 3.37e-75

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: 228.56  E-value: 3.37e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737 114 LKISEDRLAVTGERGYCMVRATHSVNRGCWYFEVTIEEMP--DGAATRLGWGREYGNLQAPLGYDKFGYSWRSRKGTKFT 191
Cdd:cd12872   1 LKLSEDRLTVTGEKGYRMARANHGVREGKWYFEVKILEGGgtETGHVRVGWSRREASLQAPVGYDKYSYAIRDKDGSKFH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737 192 ESHGKHYSD-AYVEGDTLGFLIELPEeasldylpntfkdrplvkfkshlyyedkdkitetlknlhilqgsrIEFFKNGQS 270
Cdd:cd12872  81 QSRGKPYGEpGFKEGDVIGFLITLPK---------------------------------------------IEFFKNGKS 115

                       170       180       190
                ....*....|....*....|....*....|....*
gi 24649737 271 QGVAFEDI-YAGSYFPAISIHKSATVSVNFGPAFK 304
Cdd:cd12872 116 QGVAFEDIyGTGGYYPAVSLYKGATVTINFGPDFK 150
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 140-301 9.64e-20

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: 83.50  E-value: 9.64e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737    140 RGCWYFEVTIEempDGAATRLGWGREYGNL--QAPLGYDKFGYSWRSRKGTKFTESHGKHYSDAYVE-GDTLGFLIELPE 216
Cdd:smart00449   1 SGRHYFEVEIG---DGGHWRVGVATKSVPRgyFALLGEDKGSWGYDGDGGKKYHNSTGPEYGLPLQEpGDVIGCFLDLEA 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737    217 EasldylpntfkdrplvkfkshlyyedkdkitetlknlhilqgsRIEFFKNG-QSQGVAFEDIYA-GSYFPAISIHKSAT 294
Cdd:smart00449  78 G-------------------------------------------TISFYKNGkYLHGLAFFDVKFsGPLYPAFSLGSGNS 114


                   ....*..
gi 24649737    295 VSVNFGP 301
Cdd:smart00449 115 VRLNFGP 121
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 141-298 1.39e-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: 72.08  E-value: 1.39e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737 141 GCWYFEVTIEEMPDGAAtRLGWGREYGNLQAPLGYDKFGYSW-----RSRKGTKFtesHGKHYSDAYVEGDTLGFLIELP 215
Cdd:cd11709   1 GKWYWEVRVDSGNGGLI-QVGWATKSFSLDGEGGVGDDEESWgydgsRLRKGHGG---SSGPGGRPWKSGDVVGCLLDLD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737 216 EeasldylpntfkdrplvkfkshlyyedkdkitetlknlhilqgSRIEFFKNGQSQGVAFEDIY--AGSYFPAISIHKSA 293
Cdd:cd11709  77 E-------------------------------------------GTLSFSLNGKDLGVAFTNLFlkGGGLYPAVSLGSGQ 113


                ....*
gi 24649737 294 TVSVN 298
Cdd:cd11709 114 GVTIN 118
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 103-300 7.28e-15

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: 71.85  E-value: 7.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737 103 VLLALHDRAPQLKISEDRLAV---TGERGYCM---VRATHSVNRGCWYFEVTI----------EEMPDGAATRLGWGREY 166
Cdd:cd12884   1 VCLDTYNSDLHLKISKDRYSAsplTDEGFAYLwagARATYGVTKGKVCFEVKVtenlpvkhlpTEETDPHVVRVGWSVDS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737 167 GNLQapLGYDKFGYSWRSRkGTKFTESHGKHYSDAYVEGDTLGFLIELpeeasldylpntfkdrplvkfkshlyyeDKDK 246
Cdd:cd12884  81 SSLQ--LGEEEFSYGYGST-GKKSTNCKFEDYGEPFGENDVIGCYLDF----------------------------ESEP 129

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24649737 247 ITetlknlhilqgsrIEFFKNGQSQGVAFE---DIYAG-SYFPAIsIHKSATVSVNFG 300
Cdd:cd12884 130 VE-------------ISFSKNGKDLGVAFKiskEELGGkALFPHV-LTKNCAVEVNFG 173
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 109-300 1.70e-14

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: 69.91  E-value: 1.70e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737 109 DRAPQLKISEDRLAV--TGERGYCMVRATHSV-NRGCWYFEVTIEEmpDGAAtRLGWGREYGNLQapLGYDKFGYSWRSr 185
Cdd:cd12873   5 DRDAALAISPDGLLCqsREEKGWQGCRATKGVkGKGKYYYEVTVTD--EGLC-RVGWSTEDASLD--LGTDKFGFGYGG- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737 186 KGTKfteSHGKH---YSDAYVEGDTLGFLIELpeeasldylpntfkdrplvkfkshlyyedkDKITetlknlhilqgsrI 262
Cdd:cd12873  79 TGKK---SHGRQfddYGEPFGLGDVIGCYLDL------------------------------DNGT-------------I 112

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 24649737 263 EFFKNGQSQGVAFE---DIYAGSYFPAISIhKSATVSVNFG 300
Cdd:cd12873 113 SFSKNGKDLGKAFDippHLRNSALFPAVCL-KNAEVEFNFG 152
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 143-300 2.35e-14

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: 68.91  E-value: 2.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737   143 WYFEVTIEEmPDGAATRLGWGRE--YGNLQAPLGYDKFGYSWRSRKGTKFTESHGKHYSDA-YVEGDTLGFLIELPEEas 219
Cdd:pfam00622   2 HYFEVEIFG-QDGGGWRVGWATKsvPRKGERFLGDESGSWGYDGWTGKKYWASTSPLTGLPlFEPGDVIGCFLDYEAG-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737   220 ldylpntfkdrplvkfkshlyyedkdkitetlknlhilqgsRIEFFKNGQSQGVAFEDIY-AGSYFPAISIHKSATVSVN 298
Cdd:pfam00622  79 -----------------------------------------TISFTKNGKSLGYAFRDVPfAGPLFPAVSLGAGEGLKFN 117


                  ..
gi 24649737   299 FG 300
Cdd:pfam00622 118 FG 119
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 130-300 8.17e-12

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: 61.91  E-value: 8.17e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737 130 CMVRATHSV--NRGCWYFEVTIEEMPDGAATRLGWGREYGNLQAPLGYDKFGYSWRSRKGTKFTES-HGKHYSDAYVEGD 206
Cdd:cd12885   1 GSVRADHPIppKVPVFYFEVTILDLGEKGIVSIGFCTSGFPLNRMPGWEDGSYGYHGDDGRVYLGGgEGENYGPPFGTGD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737 207 TLGFLIelpeeaslDYLPNTFkdrplvkfkshlyyedkdkitetlknlhilqgsrieFF-KNGQSQGVAFEDIYAGSYFP 285
Cdd:cd12885  81 VVGCGI--------NFKTGEV------------------------------------FFtKNGELLGTAFENVVKGRLYP 116

                       170
                ....*....|....*.
gi 24649737 286 AISIHKSAT-VSVNFG 300
Cdd:cd12885 117 TVGLGSPGVkVRVNFG 132
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 132-300 1.80e-09

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: 55.03  E-value: 1.80e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737 132 VRATHSVNRGCWYFEVTIEEMPdgaATRLGWG---------REYGNLQAPLGYDkfgySWRSRKGTKFTESHGKHYsday 202
Cdd:cd12882   2 IRANACVYKGKWMYEVTLGTKG---IMQIGWAtiscrftqeEGVGDTRDSYAYD----GNRVRKWNVSTQKYGEPW---- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737 203 VEGDTLGFLIELPEEasldylpntfkdrplvkfkshlyyedkdkitetlknlhilqgsRIEFFKNGQSQGVAFEDIYAG- 281
Cdd:cd12882  71 VAGDVIGCCIDLDKG-------------------------------------------TISFYRNGRSLGVAFDNVRRGp 107

                       170       180
                ....*....|....*....|.
gi 24649737 282 --SYFPAISIHKSATVSVNFG 300
Cdd:cd12882 108 glAYFPAVSLSFGERLELNFG 128
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 132-300 9.63e-08

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: 50.38  E-value: 9.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737 132 VRATHSVNRGCWYFE---VTIEEMpdgaatRLGWGREYGNLQAPLGYDKFGYSWRSRKGTKF---TESHGKHYSdayvEG 205
Cdd:cd12878   5 AEKTYAVTSGKWYFEfevLTSGYM------RVGWARPGFRPDLELGSDDLSYAFDGFLARKWhqgSESFGKQWQ----PG 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737 206 DTLGFLIELpeeasldylpntfKDRplvkfkshlyyedkdKITETLkNLHILQGSrieffkngQSQGVAFEDIYAG-SYF 284
Cdd:cd12878  75 DVVGCMLDL-------------VDR---------------TISFTL-NGELLIDS--------SGSEVAFKDIEIGeGFV 117

                       170
                ....*....|....*.
gi 24649737 285 PAISIHKSATVSVNFG 300
Cdd:cd12878 118 PACSLGVGQKGRLNLG 133
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 132-300 6.09e-04

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: 39.43  E-value: 6.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737 132 VRATHSVNRGC--WYFEVTIeempdgaatrLGWGRE------YGNLQAPL----GYDKFGYSWRSRKGTKFTESH-GKHY 198
Cdd:cd12909  14 VRANHPIPPQCgiYYFEVKI----------ISKGRDgyigigFSTKDVNLnrlpGWEPHSWGYHGDDGHSFCSSGtGKPY 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737 199 SDAYVEGDTLGFLIelpeeasldylpntfkdrplvkfkshlyyedkDKITETLknlhilqgsrieFF-KNGQSQGVAFED 277
Cdd:cd12909  84 GPTFTTGDVIGCGI--------------------------------NFRDNTA------------FYtKNGVNLGIAFRD 119

                       170       180
                ....*....|....*....|....
gi 24649737 278 IYAGSYFPAISIHKSA-TVSVNFG 300
Cdd:cd12909 120 IKKGNLYPTVGLRTPGeHVEANFG 143
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
 141-217 4.27e-03

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: 36.56  E-value: 4.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649737 141 GCWYFEVTIeeMPDGaATRLGWGREYGNLQAPLGY----DKFGYSWR-SRKGTKFTESHGKHYSDAYVEGDTLGFLIELP 215
Cdd:cd12883   1 GVWYYEVTV--LTSG-VMQIGWATKDSKFLNHEGYgigdDEYSCAYDgCRQLIWYNAKSKPHTHPRWKPGDVLGCLLDLN 77


                ..
gi 24649737 216 EE 217
Cdd:cd12883  78 KK 79
SPRY_PRY_TRIM67_9 cd12889
PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, ...
 264-300 9.03e-03

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


Pssm-ID: 293947  Cd Length: 172  Bit Score: 36.45  E-value: 9.03e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 24649737 264 FFKNGQSQG-VAFEDIYaGSYFPAISIHKSATVSVNFG 300
Cdd:cd12889 132 FYVNDEPQGpIAFRNLP-GVFYPAVSLNRNVQVTLHTG 168
 
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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