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Conserved domains on  [gi|126723885|gb|ABO26856|]
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RanBPM-like protein, partial [Globodera pallida]

Protein Classification

SPRY domain-containing protein( domain architecture ID 10191422)

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

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

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 ...
 87-225 1.76e-32

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: 115.07  E-value: 1.76e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723885  87 RSVFAVESIPNQeSGIFYYEVKI--SAITASVFIGLATKEMPLDKFVGYVKGTYSYDSR-GYFWGHevagcshlNKHPFV 163
Cdd:cd12885    1 GSVRADHPIPPK-VPVFYFEVTIldLGEKGIVSIGFCTSGFPLNRMPGWEDGSYGYHGDdGRVYLG--------GGEGEN 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126723885 164 KVPKFGEGDVVGCGVNLEKRQIFYTLTGELLEPAGLPIDHDaDLFPCITVYAPGTKIEANFG 225
Cdd:cd12885   72 YGPPFGTGDVVGCGINFKTGEVFFTKNGELLGTAFENVVKG-RLYPTVGLGSPGVKVRVNFG 132
 
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 ...
 87-225 1.76e-32

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: 115.07  E-value: 1.76e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723885  87 RSVFAVESIPNQeSGIFYYEVKI--SAITASVFIGLATKEMPLDKFVGYVKGTYSYDSR-GYFWGHevagcshlNKHPFV 163
Cdd:cd12885    1 GSVRADHPIPPK-VPVFYFEVTIldLGEKGIVSIGFCTSGFPLNRMPGWEDGSYGYHGDdGRVYLG--------GGEGEN 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126723885 164 KVPKFGEGDVVGCGVNLEKRQIFYTLTGELLEPAGLPIDHDaDLFPCITVYAPGTKIEANFG 225
Cdd:cd12885   72 YGPPFGTGDVVGCGINFKTGEVFFTKNGELLGTAFENVVKG-RLYPTVGLGSPGVKVRVNFG 132
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 102-225 3.93e-15

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 69.29  E-value: 3.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723885  102 IFYYEVKISAIT-ASVFIGLATKEMPL--DKFVGYVKGTYSYDSRgyfWGHevagCSHLNKHPFVKVPKFGEGDVVGCGV 178
Cdd:pfam00622   1 RHYFEVEIFGQDgGGWRVGWATKSVPRkgERFLGDESGSWGYDGW---TGK----KYWASTSPLTGLPLFEPGDVIGCFL 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 126723885  179 NLEKRQIFYTLTGELLEPAGLPIDHDADLFPCITVYaPGTKIEANFG 225
Cdd:pfam00622  74 DYEAGTISFTKNGKSLGYAFRDVPFAGPLFPAVSLG-AGEGLKFNFG 119
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 100-227 6.05e-14

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: 66.16  E-value: 6.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723885   100 SGIFYYEVKISAiTASVFIGLATKEMPLDKF--VGYVKGTYSYDSRGyfwGHEvagcSHLNKHPFVKVPKFGEGDVVGCG 177
Cdd:smart00449   1 SGRHYFEVEIGD-GGHWRVGVATKSVPRGYFalLGEDKGSWGYDGDG---GKK----YHNSTGPEYGLPLQEPGDVIGCF 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 126723885   178 VNLEKRQIFYTLTGEllepaGLPIDHDAD------LFPCITVYAPGTkIEANFGPE 227
Cdd:smart00449  73 LDLEAGTISFYKNGK-----YLHGLAFFDvkfsgpLYPAFSLGSGNS-VRLNFGPL 122
 
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 ...
 87-225 1.76e-32

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: 115.07  E-value: 1.76e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723885  87 RSVFAVESIPNQeSGIFYYEVKI--SAITASVFIGLATKEMPLDKFVGYVKGTYSYDSR-GYFWGHevagcshlNKHPFV 163
Cdd:cd12885    1 GSVRADHPIPPK-VPVFYFEVTIldLGEKGIVSIGFCTSGFPLNRMPGWEDGSYGYHGDdGRVYLG--------GGEGEN 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126723885 164 KVPKFGEGDVVGCGVNLEKRQIFYTLTGELLEPAGLPIDHDaDLFPCITVYAPGTKIEANFG 225
Cdd:cd12885   72 YGPPFGTGDVVGCGINFKTGEVFFTKNGELLGTAFENVVKG-RLYPTVGLGSPGVKVRVNFG 132
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 88-225 1.10e-23

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: 92.59  E-value: 1.10e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723885  88 SVFAVESIPNQeSGIFYYEVKIsaITAS----VFIGLATKEMPLDKFVGYVKGTYSY---DsrgyfwGHEVAGCSHLNKH 160
Cdd:cd12909   13 AVRANHPIPPQ-CGIYYFEVKI--ISKGrdgyIGIGFSTKDVNLNRLPGWEPHSWGYhgdD------GHSFCSSGTGKPY 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126723885 161 PfvkvPKFGEGDVVGCGVNLEKRQIFYTLTGELLEPAGLPIDhDADLFPCITVYAPGTKIEANFG 225
Cdd:cd12909   84 G----PTFTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIK-KGNLYPTVGLRTPGEHVEANFG 143
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 85-228 2.03e-15

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: 71.01  E-value: 2.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723885  85 GCRSVFAVESIpnqESGIFYYEVKI----SAITASVFIGLATKEMPLDKFVGYvkgtysyDSRGYFWGHEVAGCSHLNKH 160
Cdd:cd12872   15 GYRMARANHGV---REGKWYFEVKIleggGTETGHVRVGWSRREASLQAPVGY-------DKYSYAIRDKDGSKFHQSRG 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126723885 161 PFVKVPKFGEGDVVGCGVNLEKrqIFYTLTGELLEPAGLPIDHDADLFPCITVYAPGTkIEANFGPEF 228
Cdd:cd12872   85 KPYGEPGFKEGDVIGFLITLPK--IEFFKNGKSQGVAFEDIYGTGGYYPAVSLYKGAT-VTINFGPDF 149
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 102-225 3.93e-15

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 69.29  E-value: 3.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723885  102 IFYYEVKISAIT-ASVFIGLATKEMPL--DKFVGYVKGTYSYDSRgyfWGHevagCSHLNKHPFVKVPKFGEGDVVGCGV 178
Cdd:pfam00622   1 RHYFEVEIFGQDgGGWRVGWATKSVPRkgERFLGDESGSWGYDGW---TGK----KYWASTSPLTGLPLFEPGDVIGCFL 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 126723885  179 NLEKRQIFYTLTGELLEPAGLPIDHDADLFPCITVYaPGTKIEANFG 225
Cdd:pfam00622  74 DYEAGTISFTKNGKSLGYAFRDVPFAGPLFPAVSLG-AGEGLKFNFG 119
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 100-227 6.05e-14

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: 66.16  E-value: 6.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723885   100 SGIFYYEVKISAiTASVFIGLATKEMPLDKF--VGYVKGTYSYDSRGyfwGHEvagcSHLNKHPFVKVPKFGEGDVVGCG 177
Cdd:smart00449   1 SGRHYFEVEIGD-GGHWRVGVATKSVPRGYFalLGEDKGSWGYDGDG---GKK----YHNSTGPEYGLPLQEPGDVIGCF 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 126723885   178 VNLEKRQIFYTLTGEllepaGLPIDHDAD------LFPCITVYAPGTkIEANFGPE 227
Cdd:smart00449  73 LDLEAGTISFYKNGK-----YLHGLAFFDvkfsgpLYPAFSLGSGNS-VRLNFGPL 122
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 101-223 1.27e-13

SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L). B30.2 also contains residues in the N-terminus that form a distinct PRY domain structure; i.e. B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil or RBCC core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). TRIM/RBCC proteins are involved in a variety of processes, including apoptosis, cell cycle regulation, cell growth, senescence, viral response, meiosis, cell differentiation, and vesicular transport. Genes belonging to this family are implicated in several human diseases that vary from cancer to rare genetic syndromes. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site. While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Mutations found in the SPRY-containing proteins have shown to cause Mediterranean fever and Opitz syndrome.


Pssm-ID: 293931  Cd Length: 118  Bit Score: 65.53  E-value: 1.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723885 101 GIFYYEVKI-SAITASVFIGLATKEMPLDKFVGYVkgtysydSRGYFWGHEVAGCSHLNK-HPFVKVPKFGEGDVVGCGV 178
Cdd:cd11709    1 GKWYWEVRVdSGNGGLIQVGWATKSFSLDGEGGVG-------DDEESWGYDGSRLRKGHGgSSGPGGRPWKSGDVVGCLL 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 126723885 179 NLEKRQIFYTLTGELLEPAGLPIDHDAD-LFPCITVYaPGTKIEAN 223
Cdd:cd11709   74 DLDEGTLSFSLNGKDLGVAFTNLFLKGGgLYPAVSLG-SGQGVTIN 118
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
 101-200 2.04e-10

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: 56.59  E-value: 2.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723885 101 GIFYYEVKIsaITASVF-IGLATKEMPLDKFVGYVKG----TYSYD-SRGYFWgHEVAGCSHLNkhpfvkvPKFGEGDVV 174
Cdd:cd12883    1 GVWYYEVTV--LTSGVMqIGWATKDSKFLNHEGYGIGddeySCAYDgCRQLIW-YNAKSKPHTH-------PRWKPGDVL 70

                         90       100
                 ....*....|....*....|....*.
gi 126723885 175 GCGVNLEKRQIFYTLTGELLEPAGLP 200
Cdd:cd12883   71 GCLLDLNKKQMIFSLNGNRLPPERQV 96
SPRY_HECT_like cd13735
SPRY domain in HECT E3; This domain consists of the SPRY subdomain similar to those found at ...
 89-225 4.00e-09

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: 54.07  E-value: 4.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723885  89 VFAVESIPNQ-ESgiFYYEVKISAITAS-------VFIGLATKEMPLDKFVGYVKGTYSYDSRGYfwGHEVAGCSHLNKH 160
Cdd:cd13735    5 VYANSPIPAQaPS--FYWEVEVVSLGETddsdgpiISVGFAPPAEDRDGAWTNPVGTCLFHNNGR--AVHYRGSSLTQWK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126723885 161 PFVKVPKFGEGDVVGCGVNLEKRQ-----IFYTLTGELLEPA--GLPidhdADLFPCITVYAPGTKIEANFG 225
Cdd:cd13735   81 SIRTDVTLSIGDVAGCGWERTDTPpakgrVYFTHNGQRLPRSlqDVS----GGLWPVVHVQKKNTRVRANFG 148
SPRY_SSH4_like cd12910
SPRY domain in SSH4 and similar proteins; This family includes SPRY domain in SSH4 (suppressor ...
 88-225 7.31e-09

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: 53.90  E-value: 7.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723885  88 SVFAVESIPNQESGIFYYEVKI----SAITASVFIGLATKEMPLDKFVGYVKGTYSYdsrgyfwgHEVAGCSHLNK---- 159
Cdd:cd12910   42 SVQTNLPLPTGRPKTIYFEVKIfelpRADDTSVAIGFATKPYPPFRLPGWHRGSLAV--------HSDDGHRYINDpfgg 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126723885 160 HPFVkvPKFGEGDVVGCGVNLEKRQIFYTLTGELLEPAGLPIDHDA------------DLFPCITVYAPGTKIEANFG 225
Cdd:cd12910  114 KDFT--PPFREGDTIGIGYRFSSGTIFFTRNGKRLGGWDLGEELDAeddgvtglegfhDLYAAIGVFGGECEVHVNPG 189
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 74-225 2.17e-06

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: 46.03  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723885  74 LMIAEHTKADW-GCRSVFAVesipnQESGIFYYEVKIsaiTAS--VFIGLATKEMPLDKfvgyvkGTysyDSRGYFWGhe 150
Cdd:cd12873   17 LLCQSREEKGWqGCRATKGV-----KGKGKYYYEVTV---TDEglCRVGWSTEDASLDL------GT---DKFGFGYG-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723885 151 vaGC---SHLNKhpFVKVPK-FGEGDVVGCGVNLEKRQIFYTLTGELLEPAGLPIDHDAD--LFPCITVYapGTKIEANF 224
Cdd:cd12873   78 --GTgkkSHGRQ--FDDYGEpFGLGDVIGCYLDLDNGTISFSKNGKDLGKAFDIPPHLRNsaLFPAVCLK--NAEVEFNF 151


                 .
gi 126723885 225 G 225
Cdd:cd12873  152 G 152
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 100-194 9.34e-06

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: 43.83  E-value: 9.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723885 100 SGIFYYEVKIsaITASVF-IGLATKEMPLDKFVGYVKGTYSYD-SRGYFWghevagcsHLNKHPFVKvpKFGEGDVVGCG 177
Cdd:cd12878   13 SGKWYFEFEV--LTSGYMrVGWARPGFRPDLELGSDDLSYAFDgFLARKW--------HQGSESFGK--QWQPGDVVGCM 80

                         90
                 ....*....|....*..
gi 126723885 178 VNLEKRQIFYTLTGELL 194
Cdd:cd12878   81 LDLVDRTISFTLNGELL 97
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 100-225 1.31e-04

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: 40.77  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723885 100 SGIFYYEVKISaiTASVF-IGLATKEMPL--DKFVGYVKGTYSYDsrgyfwGHEVAGCShlnkhpfVKVPKFGE----GD 172
Cdd:cd12882   10 KGKWMYEVTLG--TKGIMqIGWATISCRFtqEEGVGDTRDSYAYD------GNRVRKWN-------VSTQKYGEpwvaGD 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 126723885 173 VVGCGVNLEKRQIFYTLTGELLEPA--GLPIDHDADLFPCITVyAPGTKIEANFG 225
Cdd:cd12882   75 VIGCCIDLDKGTISFYRNGRSLGVAfdNVRRGPGLAYFPAVSL-SFGERLELNFG 128
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 167-225 3.57e-03

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: 37.18  E-value: 3.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126723885 167 KFGEGDVVGCGVNLEKRQ--IFYTLTGELLEPAgLPIDH----DADLFPCITVYapGTKIEANFG 225
Cdd:cd12884  112 PFGENDVIGCYLDFESEPveISFSKNGKDLGVA-FKISKeelgGKALFPHVLTK--NCAVEVNFG 173
 
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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