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Conserved domains on  [gi|742160569|ref|XP_010847128|]
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PREDICTED: ran-binding protein 9 [Bison bison bison]

Protein Classification

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 ...
 116-256 4.91e-105

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: 314.46  E-value: 4.91e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569 116 GHGKTPKDAASVRATHPIPAACGIYYFEVKIVSKGRDGYMGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQP 195
Cdd:cd12909    3 GPGKTDKDAAAVRANHPIPPQCGIYYFEVKIISKGRDGYIGIGFSTKDVNLNRLPGWEPHSWGYHGDDGHSFCSSGTGKP 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742160569 196 YGPTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTDLPP-NLYPTVGLQTPGEVVDANFGQ 256
Cdd:cd12909   83 YGPTFTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIKKgNLYPTVGLRTPGEHVEANFGQ 144
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 540-632 3.67e-19

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


:

Pssm-ID: 214806  Cd Length: 99  Bit Score: 82.73  E-value: 3.67e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569   540 AIERMIHFGRELQAMSEqlrrecGKNTANKKMLKDAFSLLAYSDP-WNSPVGNQLDPIQREPVCSALNSAILET-HNLPK 617
Cdd:smart00757   2 KIEEALAYARELLAPFA------KEHEKFLKELEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILELlHGKSS 75

                           90
                   ....*....|....*
gi 742160569   618 QPPLALAMGQATQCL 632
Cdd:smart00757  76 ESPLEILLSAGLAAL 90
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
 328-382 2.02e-14

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: 70.68  E-value: 2.02e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 742160569  328 SIKNRQRIQKLVLAGRMGEAIETTQQLYPSLLERNPNLLFTLKVRQFIEMVNGTD 382
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGK 55
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 294-316 4.21e-05

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: 40.76  E-value: 4.21e-05
                          10        20
                  ....*....|....*....|...
gi 742160569  294 IQRMVSSYLVHHGYCATAEAFAR 316
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 ...
 116-256 4.91e-105

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: 314.46  E-value: 4.91e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569 116 GHGKTPKDAASVRATHPIPAACGIYYFEVKIVSKGRDGYMGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQP 195
Cdd:cd12909    3 GPGKTDKDAAAVRANHPIPPQCGIYYFEVKIISKGRDGYIGIGFSTKDVNLNRLPGWEPHSWGYHGDDGHSFCSSGTGKP 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742160569 196 YGPTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTDLPP-NLYPTVGLQTPGEVVDANFGQ 256
Cdd:cd12909   83 YGPTFTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIKKgNLYPTVGLRTPGEHVEANFGQ 144
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 137-256 4.76e-30

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: 114.70  E-value: 4.76e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569   137 CGIYYFEVKIVSKGrdgYMGIGLSAQGVN--MNRLPGWDKHSYGYHGDDGHsFCSSGTGQPYGPTFT-TGDVIGCCVNLI 213
Cdd:smart00449   1 SGRHYFEVEIGDGG---HWRVGVATKSVPrgYFALLGEDKGSWGYDGDGGK-KYHNSTGPEYGLPLQePGDVIGCFLDLE 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 742160569   214 NNTCFYTKNGHSLGI-AFTDLPPN--LYPTVGLQtPGEVVDANFGQ 256
Cdd:smart00449  77 AGTISFYKNGKYLHGlAFFDVKFSgpLYPAFSLG-SGNSVRLNFGP 121
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 139-257 6.80e-27

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: 105.50  E-value: 6.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569  139 IYYFEVKIVSKGrDGYMGIGLSAQGVNM--NRLPGWDKHSYGYHGDDGHSFCSSgTGQPYG-PTFTTGDVIGCCVNLINN 215
Cdd:pfam00622   1 RHYFEVEIFGQD-GGGWRVGWATKSVPRkgERFLGDESGSWGYDGWTGKKYWAS-TSPLTGlPLFEPGDVIGCFLDYEAG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 742160569  216 TCFYTKNGHSLGIAFTDLP--PNLYPTVGLQtPGEVVDANFGQH 257
Cdd:pfam00622  79 TISFTKNGKSLGYAFRDVPfaGPLFPAVSLG-AGEGLKFNFGLR 121
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 540-632 3.67e-19

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


Pssm-ID: 214806  Cd Length: 99  Bit Score: 82.73  E-value: 3.67e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569   540 AIERMIHFGRELQAMSEqlrrecGKNTANKKMLKDAFSLLAYSDP-WNSPVGNQLDPIQREPVCSALNSAILET-HNLPK 617
Cdd:smart00757   2 KIEEALAYARELLAPFA------KEHEKFLKELEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILELlHGKSS 75

                           90
                   ....*....|....*
gi 742160569   618 QPPLALAMGQATQCL 632
Cdd:smart00757  76 ESPLEILLSAGLAAL 90
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
 328-382 2.02e-14

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: 70.68  E-value: 2.02e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 742160569  328 SIKNRQRIQKLVLAGRMGEAIETTQQLYPSLLERNPNLLFTLKVRQFIEMVNGTD 382
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGK 55
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 328-384 7.35e-14

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


Pssm-ID: 128914  Cd Length: 58  Bit Score: 66.44  E-value: 7.35e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 742160569   328 SIKNRQRIQKLVLAGRMGEAIETTQQLYPSLLERNPNLLFTLKVRQFIEMVNGTDSE 384
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLE 57
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 294-316 4.21e-05

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: 40.76  E-value: 4.21e-05
                          10        20
                  ....*....|....*....|...
gi 742160569  294 IQRMVSSYLVHHGYCATAEAFAR 316
Cdd:pfam08513   2 LNRLIYDYLVKEGYEETAEAFEK 24
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 294-322 1.38e-04

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: 39.34  E-value: 1.38e-04
                           10        20
                   ....*....|....*....|....*....
gi 742160569   294 IQRMVSSYLVHHGYCATAEAFARSTDQTV 322
Cdd:smart00667   6 LNRLILEYLLRNGYEETAETLQKESGLSL 34
 
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 ...
 116-256 4.91e-105

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: 314.46  E-value: 4.91e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569 116 GHGKTPKDAASVRATHPIPAACGIYYFEVKIVSKGRDGYMGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQP 195
Cdd:cd12909    3 GPGKTDKDAAAVRANHPIPPQCGIYYFEVKIISKGRDGYIGIGFSTKDVNLNRLPGWEPHSWGYHGDDGHSFCSSGTGKP 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742160569 196 YGPTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTDLPP-NLYPTVGLQTPGEVVDANFGQ 256
Cdd:cd12909   83 YGPTFTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIKKgNLYPTVGLRTPGEHVEANFGQ 144
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 125-255 4.10e-56

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: 186.33  E-value: 4.10e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569 125 ASVRATHPIPAACGIYYFEVKIVSKGRDGYMGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGD 204
Cdd:cd12885    1 GSVRADHPIPPKVPVFYFEVTILDLGEKGIVSIGFCTSGFPLNRMPGWEDGSYGYHGDDGRVYLGGGEGENYGPPFGTGD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 742160569 205 VIGCCVNLINNTCFYTKNGHSLGIAFTDLPPN-LYPTVGLQTPGEVVDANFG 255
Cdd:cd12885   81 VVGCGINFKTGEVFFTKNGELLGTAFENVVKGrLYPTVGLGSPGVKVRVNFG 132
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 137-256 4.76e-30

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: 114.70  E-value: 4.76e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569   137 CGIYYFEVKIVSKGrdgYMGIGLSAQGVN--MNRLPGWDKHSYGYHGDDGHsFCSSGTGQPYGPTFT-TGDVIGCCVNLI 213
Cdd:smart00449   1 SGRHYFEVEIGDGG---HWRVGVATKSVPrgYFALLGEDKGSWGYDGDGGK-KYHNSTGPEYGLPLQePGDVIGCFLDLE 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 742160569   214 NNTCFYTKNGHSLGI-AFTDLPPN--LYPTVGLQtPGEVVDANFGQ 256
Cdd:smart00449  77 AGTISFYKNGKYLHGlAFFDVKFSgpLYPAFSLG-SGNSVRLNFGP 121
SPRYD3 cd12908
SPRY domain-containing protein 3; This family contains SPRY domain-containing protein 3 ...
 117-250 1.39e-28

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: 112.01  E-value: 1.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569 117 HGKTPKDAASVRATHPI-PAACgiyYFEVKIVSKGRDGYMGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQP 195
Cdd:cd12908   17 HGRGIGDVGLAQARRPLsPDNH---YFEVEIVDPGVRCYIAIGLAPQDYPLDRHPGWNPGSVAYHADDGKLFKGSGVGDQ 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742160569 196 YGPTFTTGDVIGCCVNLINN-----------------TCFYTKNGHSLGIAFTDLPPN-LYPTVGLQTPGEVV 250
Cdd:cd12908   94 FGPRCTKGDRMGCGIRFPRDydtdsedqgdeeegrtvQVFFTRNGKEVGRTEVPLPPGgFYPAVGMHSEGEKV 166
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 139-257 6.80e-27

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: 105.50  E-value: 6.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569  139 IYYFEVKIVSKGrDGYMGIGLSAQGVNM--NRLPGWDKHSYGYHGDDGHSFCSSgTGQPYG-PTFTTGDVIGCCVNLINN 215
Cdd:pfam00622   1 RHYFEVEIFGQD-GGGWRVGWATKSVPRkgERFLGDESGSWGYDGWTGKKYWAS-TSPLTGlPLFEPGDVIGCFLDYEAG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 742160569  216 TCFYTKNGHSLGIAFTDLP--PNLYPTVGLQtPGEVVDANFGQH 257
Cdd:pfam00622  79 TISFTKNGKSLGYAFRDVPfaGPLFPAVSLG-AGEGLKFNFGLR 121
SPRY_SSH4_like cd12910
SPRY domain in SSH4 and similar proteins; This family includes SPRY domain in SSH4 (suppressor ...
 126-256 2.22e-23

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: 97.82  E-value: 2.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569 126 SVRATHPIPaaCGI---YYFEVKIVSKGR--DGYMGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCS-SGTGQPYGPT 199
Cdd:cd12910   42 SVQTNLPLP--TGRpktIYFEVKIFELPRadDTSVAIGFATKPYPPFRLPGWHRGSLAVHSDDGHRYINdPFGGKDFTPP 119

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742160569 200 FTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTDLPP--------------NLYPTVGL-QTPGEVVdANFGQ 256
Cdd:cd12910  120 FREGDTIGIGYRFSSGTIFFTRNGKRLGGWDLGEELdaeddgvtglegfhDLYAAIGVfGGECEVH-VNPGQ 190
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 126-259 7.92e-22

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: 92.20  E-value: 7.92e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569 126 SVRATHPIpaACGIYYFEVKIVSKG--RDGYMGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFcSSGTGQPYG-PTFTT 202
Cdd:cd12872   18 MARANHGV--REGKWYFEVKILEGGgtETGHVRVGWSRREASLQAPVGYDKYSYAIRDKDGSKF-HQSRGKPYGePGFKE 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 742160569 203 GDVIGCCVNL--INntcFYtKNGHSLGIAFTDLPPNL--YPTVGLQTPGeVVDANFGQHPF 259
Cdd:cd12872   95 GDVIGFLITLpkIE---FF-KNGKSQGVAFEDIYGTGgyYPAVSLYKGA-TVTINFGPDFK 150
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 138-253 1.71e-20

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: 87.10  E-value: 1.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569 138 GIYYFEVKIVSkGRDGYMGIGLSAQGVNMN--RLPGWDKHSYGYHGDDGHSfCSSGTGQPYGPTFTTGDVIGCCVNLINN 215
Cdd:cd11709    1 GKWYWEVRVDS-GNGGLIQVGWATKSFSLDgeGGVGDDEESWGYDGSRLRK-GHGGSSGPGGRPWKSGDVVGCLLDLDEG 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 742160569 216 TCFYTKNGHSLGIAFTDL---PPNLYPTVGLqTPGEVVDAN 253
Cdd:cd11709   79 TLSFSLNGKDLGVAFTNLflkGGGLYPAVSL-GSGQGVTIN 118
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 540-632 3.67e-19

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


Pssm-ID: 214806  Cd Length: 99  Bit Score: 82.73  E-value: 3.67e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569   540 AIERMIHFGRELQAMSEqlrrecGKNTANKKMLKDAFSLLAYSDP-WNSPVGNQLDPIQREPVCSALNSAILET-HNLPK 617
Cdd:smart00757   2 KIEEALAYARELLAPFA------KEHEKFLKELEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILELlHGKSS 75

                           90
                   ....*....|....*
gi 742160569   618 QPPLALAMGQATQCL 632
Cdd:smart00757  76 ESPLEILLSAGLAAL 90
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 127-258 4.57e-18

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: 81.47  E-value: 4.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569 127 VRATHPIPAAcGIYYFEVKIVSKG--RdgymgIGLSAQGVNMNRlpGWDKHSYGYHGDDGHSFCSSGTGqpYGPTFTTGD 204
Cdd:cd12873   30 CRATKGVKGK-GKYYYEVTVTDEGlcR-----VGWSTEDASLDL--GTDKFGFGYGGTGKKSHGRQFDD--YGEPFGLGD 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 742160569 205 VIGCCVNLINNTCFYTKNGHSLGIAFtDLPPN-----LYPTVGLQTpGEVVdANFGQHP 258
Cdd:cd12873  100 VIGCYLDLDNGTISFSKNGKDLGKAF-DIPPHlrnsaLFPAVCLKN-AEVE-FNFGDKP 155
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 125-258 9.38e-17

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: 78.40  E-value: 9.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569 125 ASVRATHPIPAacGIYYFEVKIV---------SKGRDGYMG-IGLSAQGVNMnrLPGWDKHSYGYhGDDGhSFCSSGTGQ 194
Cdd:cd12884   34 AGARATYGVTK--GKVCFEVKVTenlpvkhlpTEETDPHVVrVGWSVDSSSL--QLGEEEFSYGY-GSTG-KKSTNCKFE 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 742160569 195 PYGPTFTTGDVIGCCVNLINNTC--FYTKNGHSLGIAFT----DLPPN-LYPTVglQTPGEVVDANFGQHP 258
Cdd:cd12884  108 DYGEPFGENDVIGCYLDFESEPVeiSFSKNGKDLGVAFKiskeELGGKaLFPHV--LTKNCAVEVNFGQKE 176
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
 328-382 2.02e-14

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: 70.68  E-value: 2.02e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 742160569  328 SIKNRQRIQKLVLAGRMGEAIETTQQLYPSLLERNPNLLFTLKVRQFIEMVNGTD 382
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGK 55
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 328-384 7.35e-14

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


Pssm-ID: 128914  Cd Length: 58  Bit Score: 66.44  E-value: 7.35e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 742160569   328 SIKNRQRIQKLVLAGRMGEAIETTQQLYPSLLERNPNLLFTLKVRQFIEMVNGTDSE 384
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLE 57
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 126-255 8.48e-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: 8.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569 126 SVRAThpipaAC---GIYYFEVKIVSKGrdgYMGIGLSAQGVNMNRLPG-WDKH-SYGYhgdDGHSFCS-SGTGQPYGPT 199
Cdd:cd12882    1 SIRAN-----ACvykGKWMYEVTLGTKG---IMQIGWATISCRFTQEEGvGDTRdSYAY---DGNRVRKwNVSTQKYGEP 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569 200 FTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTDLP--PNL--YPTVGLqTPGEVVDANFG 255
Cdd:cd12882   70 WVAGDVIGCCIDLDKGTISFYRNGRSLGVAFDNVRrgPGLayFPAVSL-SFGERLELNFG 128
SPRY_like cd12886
SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ...
 138-255 9.14e-14

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: 68.30  E-value: 9.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569 138 GIYYFEVKIVSKGRDGYMGIGL-SAQGVNMNRLPGWDKHSYGYHG--DDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLIN 214
Cdd:cd12886    1 GKWYWEVTVVSSAASTYAGIGVaNAAATGNNGLNGIELSSIGYSLgvYSGNKLSNGSSVATYGAGFTAGDVIGVALDLDA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 742160569 215 NTCFYTKNGHSLG---IAFTDLPPNL----YPTVGLQ-TPGEVVDANFG 255
Cdd:cd12886   81 GKIWFYKNGVWQGggdPAPGTNPAFAgtamYPAVTGGsSTGGSFTANFG 129
SPRY_SOCS3 cd12876
SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY ...
 125-241 8.09e-13

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: 67.19  E-value: 8.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569 125 ASVRATHPIPAacGIYYFEVKIVSK--GRDgyMGIGLSAQGVNMNR-------LPGWDKHSYGY-------HGddghsfc 188
Cdd:cd12876   33 AAVRGTKPLTN--GQHYWEIKMSSPvyGTD--MMVGVGTKKADLHAyryefcsLLGEDEESWGLsykgllwHD------- 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 742160569 189 ssGTGQPYGPTFTT-GDVIGCCVNLINNTCFYTKNGHSLGIAFTDLP--PNLYPTV 241
Cdd:cd12876  102 --GQSRPYTSPFGNqGTIIGVHLDMWRGTLTFYKNGKPLGVAFTGLNgvKPLYPMV 155
SPRY_HECT_like cd13735
SPRY domain in HECT E3; This domain consists of the SPRY subdomain similar to those found at ...
 125-255 1.36e-08

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: 1.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569 125 ASVRATHPIPAACGIYYFEVKIVSKGRDG-----YMGIGLSAQGVNMNRLPGWDKHSYGYHgDDGHSFCSSGTGQPYGPT 199
Cdd:cd13735    3 VFVYANSPIPAQAPSFYWEVEVVSLGETDdsdgpIISVGFAPPAEDRDGAWTNPVGTCLFH-NNGRAVHYRGSSLTQWKS 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742160569 200 FTT------GDVIGC-----CVNLINNTCFYTKNGHSLGIAFTDLPPNLYPTVGLQTPGEVVDANFG 255
Cdd:cd13735   82 IRTdvtlsiGDVAGCgwertDTPPAKGRVYFTHNGQRLPRSLQDVSGGLWPVVHVQKKNTRVRANFG 148
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 138-234 1.16e-07

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: 51.15  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569 138 GIYYFEVKIVSkgrDGYMGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFcsSGTGQPYGPTFTTGDVIGCCVNLINNTC 217
Cdd:cd12878   14 GKWYFEFEVLT---SGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKW--HQGSESFGKQWQPGDVVGCMLDLVDRTI 88

                         90       100
                 ....*....|....*....|...
gi 742160569 218 FYTKNGH----SLG--IAFTDLP 234
Cdd:cd12878   89 SFTLNGEllidSSGseVAFKDIE 111
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 294-316 4.21e-05

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: 40.76  E-value: 4.21e-05
                          10        20
                  ....*....|....*....|...
gi 742160569  294 IQRMVSSYLVHHGYCATAEAFAR 316
Cdd:pfam08513   2 LNRLIYDYLVKEGYEETAEAFEK 24
SPRY_Fbox cd12907
SPRY domain in the F-box family Fbxo45; Fbxo45 is a novel synaptic E3 and ubiquitin ligase, ...
 169-241 9.28e-05

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: 43.53  E-value: 9.28e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742160569 169 LPGWDKHSYGYHGDDGHSFCSSGTGQPY-----GPTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTDLPP-NLYPTV 241
Cdd:cd12907   77 LLGSDDQSWGWNLVDNHLLHNGDSQGNYpqcnnAPKYQVGERIRVILDCEDNTLAFERGYEFLGVAFRGLPPtKLYPAV 155
SPRYD7 cd12880
SPRY domain-containing protein 7; This family contains SPRY domain-containing protein 7 (also ...
 141-254 1.08e-04

SPRY domain-containing protein 7; This family contains SPRY domain-containing protein 7 (also known as SPRY domain-containing protein 7 or CLL deletion region gene 6 protein homolog or CLLD6 or chronic lymphocytic leukemia deletion region gene 6 protein homolog). In humans, CLLD6 is highly expressed in heart, skeletal muscle, and testis as well as cancer cell lines. It also has cross-species conservation, suggesting that it is likely to carry out important cellular processes.


Pssm-ID: 293938  Cd Length: 160  Bit Score: 42.96  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569 141 YFEVKIVSKGRdgyMGIGLSAQGVNMNRLPGwdkhsygyhGDDGHSF--CSSGT----GQPYG---PTFTTGDVIGCC-- 209
Cdd:cd12880   32 YFEVKIQSTGV---WGVGLATRKTDLNRVPL---------GNDAESWvlRSDGTiwhnGEVIHklkQLVEEGDVIGVTyd 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 742160569 210 -VNLiNntcFYtKNGHSLGIAFTDLPPNLYPTVGLQTpGEVVDANF 254
Cdd:cd12880  100 hVEL-N---FY-LNGKPLDCPITGIKGTVYPVVYVDD-GAILDVQF 139
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 294-322 1.38e-04

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: 39.34  E-value: 1.38e-04
                           10        20
                   ....*....|....*....|....*....
gi 742160569   294 IQRMVSSYLVHHGYCATAEAFARSTDQTV 322
Cdd:smart00667   6 LNRLILEYLLRNGYEETAETLQKESGLSL 34
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
 138-255 2.74e-04

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: 41.18  E-value: 2.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569 138 GIYYFEVKIVSkgrDGYMGIGLSAQGVNMNRLPGwdkhsYGYhGDDGHSFCSSGTGQPY----------GPTFTTGDVIG 207
Cdd:cd12883    1 GVWYYEVTVLT---SGVMQIGWATKDSKFLNHEG-----YGI-GDDEYSCAYDGCRQLIwynakskphtHPRWKPGDVLG 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 742160569 208 CCVNLINNTCFYTKNGHSLG---IAFTDLPPNLYPTVGLQTpGEVVDANFG 255
Cdd:cd12883   72 CLLDLNKKQMIFSLNGNRLPperQVFTSAKSGFFAAASFMS-FQQCEFNFG 121
SPRY_HERC1 cd12881
SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to ...
 198-247 9.70e-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: 40.41  E-value: 9.70e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 742160569 198 PTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTDLPPN-LYPTVGLQTPG 247
Cdd:cd12881  102 SKFHQGDYITVVLDMEEGTLSFGKNGEEPGVAFEDVDATeLYPCVMFYSSG 152
SPRY_SOCS_Fbox cd12875
SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins; This family ...
 138-241 3.07e-03

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: 38.98  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569 138 GIYYFEVKIVSKGRDGYMGIGLSA-----QGVNMNRLPGWDKHSYGYHGDDGH----SFCSSGTGQPYGPTFTTGDVIGC 208
Cdd:cd12875   42 GLHAWEVKWISRPRGSHAVVGVATkdaplQCDGYVTLLGSNSESWGWDLGDNKlyhnGKKVIGSYPAKSENYQVPDRILV 121

                         90       100       110
                 ....*....|....*....|....*....|....
gi 742160569 209 CVNLINNTCFYTKNGHSLGIAFTDLPPN-LYPTV 241
Cdd:cd12875  122 ILDMEDGTLAFEANGEYLGVAFRGLPGKlLYPAV 155
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 140-224 3.26e-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: 38.45  E-value: 3.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569 140 YYFEVKI------------------VSKGRDGYMGIGLSAQGVnmnrLPGWDKHSYGYhgdDGHSFCSSG----TGQPYG 197
Cdd:cd12877   20 WYFEVEVdhveqfthqpahlrvgwaNTSGYVPYPGGGEGWGGN----GVGDDLYSYGF---DGLHLWTGGrsrrVTSGTQ 92

                         90       100
                 ....*....|....*....|....*..
gi 742160569 198 PTFTTGDVIGCCVNLINNTCFYTKNGH 224
Cdd:cd12877   93 HLLKKGDVVGCCLDLSVPSISFRVNGR 119
SPRY_NHR_like cd12887
SPRY domain in neuralized homology repeat; This family contains the neuralized homology repeat ...
 142-243 5.49e-03

SPRY domain in neuralized homology repeat; This family contains the neuralized homology repeat 1 (NHR1) domain similar to the SPRY domain (known to mediate specific protein-protein interactions) at the C-terminus of a conserved region within eukaryotic neuralized and neuralized-like proteins. In Drosophila, the neuralized protein (Neur) belongs to a group of ubiquitin ligases and is required in a subset of Notch pathway-mediated cell fate decisions during development of the nervous system. Neur binds to the Notch receptor ligand Delta through its first NHR1 domain and mediates its ubiquitination for endocytosis. Multiple copies of this region are found in some members of the family.


Pssm-ID: 293945  Cd Length: 161  Bit Score: 37.87  E-value: 5.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742160569 142 FEVKIVSKGRD--GYMGIGLSAQGVNMNRLP----GWDKHSYGYHGD----DGHSFCSSgtgqpYGPTF---TTGDVIGc 208
Cdd:cd12887   43 FEVRIDKLVDRwsGSLEIGVTTLNPETLDLPpsatDLKSGTWILSGSsvfkNGNKIREN-----YGPDLdrlRVGDRVG- 116

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 742160569 209 cVNLINNTC--FYTkNGHSLGIAFTDLPPNLYPTVGL 243
Cdd:cd12887  117 -VMRTSDGTlhFYV-NGEDQGVAASNVPQPVYAVVDL 151
 
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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