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Conserved domains on  [gi|998074446|ref|NP_001307167|]
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ran-binding protein 10 isoform 2 [Homo sapiens]

Protein Classification

topless-related protein; WD40 repeat domain-containing protein( domain architecture ID 11596471)

topless-related protein may act as transcription corepressor; WD40 repeat domain-containing protein folds into a beta-propeller structure and functions as a scaffold, providing a platform for the interaction and assembly of several proteins into a signalosome; similar to a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
1-102 4.36e-75

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: 233.95  E-value: 4.36e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074446   1 MGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINGTCFYTKNGHSLGIAFTDLP 80
Cdd:cd12909   42 IGIGFSTKDVNLNRLPGWEPHSWGYHGDDGHSFCSSGTGKPYGPTFTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIK 121
                         90       100
                 ....*....|....*....|...
gi 998074446  81 -ANLYPTVGLQTPGEIVDANFGQ 102
Cdd:cd12909  122 kGNLYPTVGLRTPGEHVEANFGQ 144
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
420-517 1.54e-16

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


:

Pssm-ID: 214806  Cd Length: 99  Bit Score: 75.02  E-value: 1.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074446   420 ATERIILFGRELQAlseQLGREYGKNLahtEMLQDAFSLLAYSDP-WSCPVGQQLDPIQREPVCAALNSAILESQ-NLPK 497
Cdd:smart00757   2 KIEEALAYARELLA---PFAKEHEKFL---KELEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILELLhGKSS 75
                           90       100
                   ....*....|....*....|
gi 998074446   498 QPPLMLALGQASECLRLMAR 517
Cdd:smart00757  76 ESPLEILLSAGLAALKTLLE 95
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
174-228 1.10e-13

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: 68.37  E-value: 1.10e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 998074446  174 SIKNRQKIQKLVLEGRVGEAIETTQRFYPGLLEHNPNLLFMLKCRQFVEMVNGTD 228
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGK 55
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
140-167 2.29e-03

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


:

Pssm-ID: 128913  Cd Length: 34  Bit Score: 35.87  E-value: 2.29e-03
                           10        20
                   ....*....|....*....|....*...
gi 998074446   140 LQNMVSSYLVHHGYCATATAFARMTETP 167
Cdd:smart00667   6 LNRLILEYLLRNGYEETAETLQKESGLS 33
 
Name Accession Description Interval E-value
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
1-102 4.36e-75

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: 233.95  E-value: 4.36e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074446   1 MGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINGTCFYTKNGHSLGIAFTDLP 80
Cdd:cd12909   42 IGIGFSTKDVNLNRLPGWEPHSWGYHGDDGHSFCSSGTGKPYGPTFTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIK 121
                         90       100
                 ....*....|....*....|...
gi 998074446  81 -ANLYPTVGLQTPGEIVDANFGQ 102
Cdd:cd12909  122 kGNLYPTVGLRTPGEHVEANFGQ 144
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
1-103 1.09e-24

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: 98.91  E-value: 1.09e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074446     1 MGIGLSAQGVN--MNRLPGWDKHSYGYHGDDGHsFCSSGTGQPYGPTFT-TGDVIGCCVNLINGTCFYTKNGHSLGI-AF 76
Cdd:smart00449  16 WRVGVATKSVPrgYFALLGEDKGSWGYDGDGGK-KYHNSTGPEYGLPLQePGDVIGCFLDLEAGTISFYKNGKYLHGlAF 94
                           90       100
                   ....*....|....*....|....*....
gi 998074446    77 TDLPAN--LYPTVGLQtPGEIVDANFGQQ 103
Cdd:smart00449  95 FDVKFSgpLYPAFSLG-SGNSVRLNFGPL 122
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
1-103 2.02e-24

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: 98.18  E-value: 2.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074446    1 MGIGLSAQGVNM--NRLPGWDKHSYGYHGDDGHSFCSSgTGQPYG-PTFTTGDVIGCCVNLINGTCFYTKNGHSLGIAFT 77
Cdd:pfam00622  16 WRVGWATKSVPRkgERFLGDESGSWGYDGWTGKKYWAS-TSPLTGlPLFEPGDVIGCFLDYEAGTISFTKNGKSLGYAFR 94
                          90       100
                  ....*....|....*....|....*...
gi 998074446   78 DLPA--NLYPTVGLQtPGEIVDANFGQQ 103
Cdd:pfam00622  95 DVPFagPLFPAVSLG-AGEGLKFNFGLR 121
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
420-517 1.54e-16

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


Pssm-ID: 214806  Cd Length: 99  Bit Score: 75.02  E-value: 1.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074446   420 ATERIILFGRELQAlseQLGREYGKNLahtEMLQDAFSLLAYSDP-WSCPVGQQLDPIQREPVCAALNSAILESQ-NLPK 497
Cdd:smart00757   2 KIEEALAYARELLA---PFAKEHEKFL---KELEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILELLhGKSS 75
                           90       100
                   ....*....|....*....|
gi 998074446   498 QPPLMLALGQASECLRLMAR 517
Cdd:smart00757  76 ESPLEILLSAGLAALKTLLE 95
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
174-228 1.10e-13

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: 68.37  E-value: 1.10e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 998074446  174 SIKNRQKIQKLVLEGRVGEAIETTQRFYPGLLEHNPNLLFMLKCRQFVEMVNGTD 228
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGK 55
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
174-230 2.07e-13

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


Pssm-ID: 128914  Cd Length: 58  Bit Score: 64.90  E-value: 2.07e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 998074446   174 SIKNRQKIQKLVLEGRVGEAIETTQRFYPGLLEHNPNLLFMLKCRQFVEMVNGTDSE 230
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLE 57
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
441-512 3.44e-12

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: 64.13  E-value: 3.44e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 998074446  441 EYGK------NLAHTEMLQDAFSLLAYSDPWSC-PVGQQLDPIQREPVCAALNSAILESQNLPKQPPLMLALGQASECL 512
Cdd:pfam10607  61 EYARenlapfNEEHLKELEKLMGLLAFPDPTDSsPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKAGLSAL 139
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
140-167 2.29e-03

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 35.87  E-value: 2.29e-03
                           10        20
                   ....*....|....*....|....*...
gi 998074446   140 LQNMVSSYLVHHGYCATATAFARMTETP 167
Cdd:smart00667   6 LNRLILEYLLRNGYEETAETLQKESGLS 33
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
140-162 3.06e-03

LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex.


Pssm-ID: 462501  Cd Length: 25  Bit Score: 34.99  E-value: 3.06e-03
                          10        20
                  ....*....|....*....|...
gi 998074446  140 LQNMVSSYLVHHGYCATATAFAR 162
Cdd:pfam08513   2 LNRLIYDYLVKEGYEETAEAFEK 24
 
Name Accession Description Interval E-value
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
1-102 4.36e-75

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: 233.95  E-value: 4.36e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074446   1 MGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINGTCFYTKNGHSLGIAFTDLP 80
Cdd:cd12909   42 IGIGFSTKDVNLNRLPGWEPHSWGYHGDDGHSFCSSGTGKPYGPTFTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIK 121
                         90       100
                 ....*....|....*....|...
gi 998074446  81 -ANLYPTVGLQTPGEIVDANFGQ 102
Cdd:cd12909  122 kGNLYPTVGLRTPGEHVEANFGQ 144
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
2-101 2.70e-42

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: 147.43  E-value: 2.70e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074446   2 GIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINGTCFYTKNGHSLGIAFTDL-P 80
Cdd:cd12885   32 SIGFCTSGFPLNRMPGWEDGSYGYHGDDGRVYLGGGEGENYGPPFGTGDVVGCGINFKTGEVFFTKNGELLGTAFENVvK 111
                         90       100
                 ....*....|....*....|.
gi 998074446  81 ANLYPTVGLQTPGEIVDANFG 101
Cdd:cd12885  112 GRLYPTVGLGSPGVKVRVNFG 132
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
1-103 1.09e-24

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: 98.91  E-value: 1.09e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074446     1 MGIGLSAQGVN--MNRLPGWDKHSYGYHGDDGHsFCSSGTGQPYGPTFT-TGDVIGCCVNLINGTCFYTKNGHSLGI-AF 76
Cdd:smart00449  16 WRVGVATKSVPrgYFALLGEDKGSWGYDGDGGK-KYHNSTGPEYGLPLQePGDVIGCFLDLEAGTISFYKNGKYLHGlAF 94
                           90       100
                   ....*....|....*....|....*....
gi 998074446    77 TDLPAN--LYPTVGLQtPGEIVDANFGQQ 103
Cdd:smart00449  95 FDVKFSgpLYPAFSLG-SGNSVRLNFGPL 122
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
1-103 2.02e-24

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: 98.18  E-value: 2.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074446    1 MGIGLSAQGVNM--NRLPGWDKHSYGYHGDDGHSFCSSgTGQPYG-PTFTTGDVIGCCVNLINGTCFYTKNGHSLGIAFT 77
Cdd:pfam00622  16 WRVGWATKSVPRkgERFLGDESGSWGYDGWTGKKYWAS-TSPLTGlPLFEPGDVIGCFLDYEAGTISFTKNGKSLGYAFR 94
                          90       100
                  ....*....|....*....|....*...
gi 998074446   78 DLPA--NLYPTVGLQtPGEIVDANFGQQ 103
Cdd:pfam00622  95 DVPFagPLFPAVSLG-AGEGLKFNFGLR 121
SPRYD3 cd12908
SPRY domain-containing protein 3; This family contains SPRY domain-containing protein 3 ...
2-96 9.03e-20

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: 86.58  E-value: 9.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074446   2 GIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLING-----------------TCF 64
Cdd:cd12908   54 AIGLAPQDYPLDRHPGWNPGSVAYHADDGKLFKGSGVGDQFGPRCTKGDRMGCGIRFPRDydtdsedqgdeeegrtvQVF 133
                         90       100       110
                 ....*....|....*....|....*....|...
gi 998074446  65 YTKNGHSLGIAFTDLPAN-LYPTVGLQTPGEIV 96
Cdd:cd12908  134 FTRNGKEVGRTEVPLPPGgFYPAVGMHSEGEKV 166
SPRY_SSH4_like cd12910
SPRY domain in SSH4 and similar proteins; This family includes SPRY domain in SSH4 (suppressor ...
2-102 8.74e-19

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: 84.34  E-value: 8.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074446   2 GIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCS-SGTGQPYGPTFTTGDVIGCCVNLINGTCFYTKNGHSLGIAFTDLP 80
Cdd:cd12910   75 AIGFATKPYPPFRLPGWHRGSLAVHSDDGHRYINdPFGGKDFTPPFREGDTIGIGYRFSSGTIFFTRNGKRLGGWDLGEE 154
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 998074446  81 A--------------NLYPTVGL-QTPGEIVdANFGQ 102
Cdd:cd12910  155 LdaeddgvtglegfhDLYAAIGVfGGECEVH-VNPGQ 190
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
420-517 1.54e-16

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


Pssm-ID: 214806  Cd Length: 99  Bit Score: 75.02  E-value: 1.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074446   420 ATERIILFGRELQAlseQLGREYGKNLahtEMLQDAFSLLAYSDP-WSCPVGQQLDPIQREPVCAALNSAILESQ-NLPK 497
Cdd:smart00757   2 KIEEALAYARELLA---PFAKEHEKFL---KELEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILELLhGKSS 75
                           90       100
                   ....*....|....*....|
gi 998074446   498 QPPLMLALGQASECLRLMAR 517
Cdd:smart00757  76 ESPLEILLSAGLAALKTLLE 95
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
1-99 7.53e-16

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: 73.62  E-value: 7.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074446   1 MGIGLSAQGVNMN--RLPGWDKHSYGYHGDDGHSfCSSGTGQPYGPTFTTGDVIGCCVNLINGTCFYTKNGHSLGIAFTD 78
Cdd:cd11709   17 IQVGWATKSFSLDgeGGVGDDEESWGYDGSRLRK-GHGGSSGPGGRPWKSGDVVGCLLDLDEGTLSFSLNGKDLGVAFTN 95
                         90       100
                 ....*....|....*....|....
gi 998074446  79 LPA---NLYPTVGLqTPGEIVDAN 99
Cdd:cd11709   96 LFLkggGLYPAVSL-GSGQGVTIN 118
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
17-104 3.36e-15

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: 72.99  E-value: 3.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074446  17 GWDKHSYGYHGDDGHSFCSSGTGqpYGPTFTTGDVIGCCVNLINGTCFYTKNGHSLGIAFtDLPAN-----LYPTVGLQt 91
Cdd:cd12873   68 GTDKFGFGYGGTGKKSHGRQFDD--YGEPFGLGDVIGCYLDLDNGTISFSKNGKDLGKAF-DIPPHlrnsaLFPAVCLK- 143
                         90
                 ....*....|...
gi 998074446  92 pGEIVDANFGQQP 104
Cdd:cd12873  144 -NAEVEFNFGDKP 155
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
17-101 3.69e-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: 72.55  E-value: 3.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074446  17 GWDKHSYGYHGDDGHSFcSSGTGQPYG-PTFTTGDVIGCCVNL--INgtcFYtKNGHSLGIAFTDLPANL--YPTVGLQT 91
Cdd:cd12872   63 GYDKYSYAIRDKDGSKF-HQSRGKPYGePGFKEGDVIGFLITLpkIE---FF-KNGKSQGVAFEDIYGTGgyYPAVSLYK 137
                         90
                 ....*....|
gi 998074446  92 PGeIVDANFG 101
Cdd:cd12872  138 GA-TVTINFG 146
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
22-101 6.23e-14

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: 68.51  E-value: 6.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074446  22 SYGYhgdDGHSFCS-SGTGQPYGPTFTTGDVIGCCVNLINGTCFYTKNGHSLGIAFTDLPAN----LYPTVGLQTpGEIV 96
Cdd:cd12882   48 SYAY---DGNRVRKwNVSTQKYGEPWVAGDVIGCCIDLDKGTISFYRNGRSLGVAFDNVRRGpglaYFPAVSLSF-GERL 123

                 ....*
gi 998074446  97 DANFG 101
Cdd:cd12882  124 ELNFG 128
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
174-228 1.10e-13

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: 68.37  E-value: 1.10e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 998074446  174 SIKNRQKIQKLVLEGRVGEAIETTQRFYPGLLEHNPNLLFMLKCRQFVEMVNGTD 228
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGK 55
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
174-230 2.07e-13

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


Pssm-ID: 128914  Cd Length: 58  Bit Score: 64.90  E-value: 2.07e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 998074446   174 SIKNRQKIQKLVLEGRVGEAIETTQRFYPGLLEHNPNLLFMLKCRQFVEMVNGTDSE 230
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLE 57
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
441-512 3.44e-12

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: 64.13  E-value: 3.44e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 998074446  441 EYGK------NLAHTEMLQDAFSLLAYSDPWSC-PVGQQLDPIQREPVCAALNSAILESQNLPKQPPLMLALGQASECL 512
Cdd:pfam10607  61 EYARenlapfNEEHLKELEKLMGLLAFPDPTDSsPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKAGLSAL 139
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
17-104 5.41e-12

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: 64.53  E-value: 5.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074446  17 GWDKHSYGYhGDDGhSFCSSGTGQPYGPTFTTGDVIGCCVNLINGTC--FYTKNGHSLGIAFT----DL-PANLYPTVgl 89
Cdd:cd12884   86 GEEEFSYGY-GSTG-KKSTNCKFEDYGEPFGENDVIGCYLDFESEPVeiSFSKNGKDLGVAFKiskeELgGKALFPHV-- 161
                         90
                 ....*....|....*
gi 998074446  90 QTPGEIVDANFGQQP 104
Cdd:cd12884  162 LTKNCAVEVNFGQKE 176
SPRY_SOCS3 cd12876
SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY ...
17-87 6.68e-10

SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY domain-containing SOCS box protein family (SPSB1-4, also known as SSB-1 to -4) is composed of a central SPRY protein interaction domain and a C-terminal SOCS box. All four SPSB proteins interact with c-Met, the hepatocyte growth factor receptor, but SOCS3 regulates cellular response to a variety of cytokines such as leukemia inhibitory factor (LIF) and interleukin 6. SOCS3, along with SOCS1, are expressed by immune cells and cells of the central nervous system (CNS) and have the potential to impact immune processes within the CNS. In non-small cell lung cancer (NSCLC), SOCS3 is silenced and proline-rich tyrosine kinase 2 (Pyk2) is over-expressed; it has been suggested that SOCS3 could be an effective way to prevent the progression of NSCLC due to its role in regulating Pyk2 expression.


Pssm-ID: 293936  Cd Length: 185  Bit Score: 58.33  E-value: 6.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074446  17 GWDKHSYGY-------HGddghsfcssGTGQPYGPTFTT-GDVIGCCVNLINGTCFYTKNGHSLGIAFTDLPA--NLYPT 86
Cdd:cd12876   84 GEDEESWGLsykgllwHD---------GQSRPYTSPFGNqGTIIGVHLDMWRGTLTFYKNGKPLGVAFTGLNGvkPLYPM 154

                 .
gi 998074446  87 V 87
Cdd:cd12876  155 V 155
SPRY_like cd12886
SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ...
1-101 2.63e-09

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: 55.21  E-value: 2.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074446   1 MGIGL-SAQGVNMNRLPGWDKHSYGYHG--DDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINGTCFYTKNGHSLG---I 74
Cdd:cd12886   18 AGIGVaNAAATGNNGLNGIELSSIGYSLgvYSGNKLSNGSSVATYGAGFTAGDVIGVALDLDAGKIWFYKNGVWQGggdP 97
                         90       100       110
                 ....*....|....*....|....*....|..
gi 998074446  75 AFTDLPANL----YPTVGLQTPGEI-VDANFG 101
Cdd:cd12886   98 APGTNPAFAgtamYPAVTGGSSTGGsFTANFG 129
SPRY_HECT_like cd13735
SPRY domain in HECT E3; This domain consists of the SPRY subdomain similar to those found at ...
45-101 1.09e-04

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: 42.51  E-value: 1.09e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 998074446  45 TFTTGDVIGC-----CVNLINGTCFYTKNGHSLGIAFTDLPANLYPTVGLQTPGEIVDANFG 101
Cdd:cd13735   87 TLSIGDVAGCgwertDTPPAKGRVYFTHNGQRLPRSLQDVSGGLWPVVHVQKKNTRVRANFG 148
SPRY_HERC1 cd12881
SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to ...
44-95 1.36e-04

SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to chromosome condensation regulator RCC1. It is widely expressed in many tissues, playing an important role in intracellular membrane trafficking in the cytoplasm as well as Golgi apparatus. HERC1 also interacts with tuberous sclerosis 2 (TSC2, tuberin), which suppresses cell growth, and results in the destabilization of TSC2. However, the biological function of HERC1 has yet to be defined.


Pssm-ID: 293939  Cd Length: 162  Bit Score: 42.34  E-value: 1.36e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 998074446  44 PTFTTGDVIGCCVNLINGTCFYTKNGHSLGIAFTDLPAN-LYPTVGLQTPGEI 95
Cdd:cd12881  102 SKFHQGDYITVVLDMEEGTLSFGKNGEEPGVAFEDVDATeLYPCVMFYSSGPG 154
SPRY_SOCS_Fbox cd12875
SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins; This family ...
15-87 8.79e-04

SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins; This family consists of the SPRY domain-containing SOCS box protein family (SPSB1-4, also known as SSB-1 to -4) as well as F-box protein 45 (Fbxo45), a novel synaptic E3 and ubiquitin ligase. The SPSB protein is composed of a central SPRY protein interaction domain and a C-terminal SOCS box. SPSB1, SPSB2, and SPSB4 interact with prostate apoptosis response protein 4 (Par-4) and are negative regulators that recruit the ECS E3 ubiquitin ligase complex to polyubiquitinate inducible nitric-oxide synthase (iNOS), resulting in its proteasomal degradation. Fbxo45 is related to this family; it is located N-terminal to the SPRY domain, and known to induce the degradation of a synaptic vesicle-priming factor, Munc13-1, via the SPRY domain, thus playing an important role in the regulation of neurotransmission by modulating Munc13-1 at the synapse. Suppressor of cytokine signaling (SOCS) proteins negatively regulate signaling from JAK-associated cytokine receptor complexes, and play key roles in the regulation of immune homeostasis.


Pssm-ID: 293935  Cd Length: 169  Bit Score: 40.13  E-value: 8.79e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 998074446  15 LPGWDKHSYGYHGDDG---HSF-CSSGTGQPYGPTFTTGDVIGCCVNLINGTCFYTKNGHSLGIAFTDLPAN-LYPTV 87
Cdd:cd12875   78 LLGSNSESWGWDLGDNklyHNGkKVIGSYPAKSENYQVPDRILVILDMEDGTLAFEANGEYLGVAFRGLPGKlLYPAV 155
SPRY_Fbox cd12907
SPRY domain in the F-box family Fbxo45; Fbxo45 is a novel synaptic E3 and ubiquitin ligase, ...
15-87 1.32e-03

SPRY domain in the F-box family Fbxo45; Fbxo45 is a novel synaptic E3 and ubiquitin ligase, related to the suppressor of cytokine signaling (SOCS) proteins and located N-terminal to a SPRY (SPla and the ryanodine receptor) domain. Fbxo45 induces the degradation of a synaptic vesicle-priming factor, Munc13-1, via the SPRY domain, thus playing an important role in the regulation of neurotransmission by modulating Munc13-1 at the synapse. F-box motifs are found in proteins that function as the substrate recognition component of SCF E3 complexes.


Pssm-ID: 293964  Cd Length: 175  Bit Score: 39.68  E-value: 1.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 998074446  15 LPGWDKHSYGYHGDDGHSFCSSGTGQPY-----GPTFTTGDVIGCCVNLINGTCFYTKNGHSLGIAFTDLP-ANLYPTV 87
Cdd:cd12907   77 LLGSDDQSWGWNLVDNHLLHNGDSQGNYpqcnnAPKYQVGERIRVILDCEDNTLAFERGYEFLGVAFRGLPpTKLYPAV 155
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
15-87 1.52e-03

SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, but no specific function has been found for this first SPRY domain of the RyRs.


Pssm-ID: 240457  Cd Length: 151  Bit Score: 39.22  E-value: 1.52e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 998074446  15 LPGWDKHSYGYhgdDGHSFCSSG----TGQPYGPTFTTGDVIGCCVNLINGTCFYTKNGHSLGIAFTD--LPANLYPTV 87
Cdd:cd12877   63 GVGDDLYSYGF---DGLHLWTGGrsrrVTSGTQHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENfnLDGMFFPVM 138
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
140-167 2.29e-03

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 35.87  E-value: 2.29e-03
                           10        20
                   ....*....|....*....|....*...
gi 998074446   140 LQNMVSSYLVHHGYCATATAFARMTETP 167
Cdd:smart00667   6 LNRLILEYLLRNGYEETAETLQKESGLS 33
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
1-101 2.89e-03

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: 38.05  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074446   1 MGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFcsSGTGQPYGPTFTTGDVIGCCVNLINGTCFYTKNGH----SLG--I 74
Cdd:cd12878   28 MRVGWARPGFRPDLELGSDDLSYAFDGFLARKW--HQGSESFGKQWQPGDVVGCMLDLVDRTISFTLNGEllidSSGseV 105
                         90       100
                 ....*....|....*....|....*....
gi 998074446  75 AFTDLPAN--LYPTVGLQTpGEIVDANFG 101
Cdd:cd12878  106 AFKDIEIGegFVPACSLGV-GQKGRLNLG 133
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
140-162 3.06e-03

LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex.


Pssm-ID: 462501  Cd Length: 25  Bit Score: 34.99  E-value: 3.06e-03
                          10        20
                  ....*....|....*....|...
gi 998074446  140 LQNMVSSYLVHHGYCATATAFAR 162
Cdd:pfam08513   2 LNRLIYDYLVKEGYEETAEAFEK 24
 
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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