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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585645734  77 YKGHGKNHKDAASVRATHPIPAACGIYYFEVKIVSKGRDGYMGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTG 156
Cdd:cd12909     1 YKGPGKTDKDAAAVRANHPIPPQCGIYYFEVKIISKGRDGYIGIGFSTKDVNLNRLPGWEPHSWGYHGDDGHSFCSSGTG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1585645734 157 QPYGPTFTTGDVIGCCVNLINGTCFYTKNGHSLGIAFTDLP-ANLYPTVGLQTPGEIVDANFGQ 219
Cdd:cd12909    81 KPYGPTFTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIKkGNLYPTVGLRTPGEHVEANFGQ 144

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1585645734 291 SIKNRQKIQKLVLEGRVGEAIETTQRFYPGLLEHNPNLLFMLKCRQFVEMVNGTD 345
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGK 55

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585645734  77 YKGHGKNHKDAASVRATHPIPAACGIYYFEVKIVSKGRDGYMGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTG 156
Cdd:cd12909     1 YKGPGKTDKDAAAVRANHPIPPQCGIYYFEVKIISKGRDGYIGIGFSTKDVNLNRLPGWEPHSWGYHGDDGHSFCSSGTG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1585645734 157 QPYGPTFTTGDVIGCCVNLINGTCFYTKNGHSLGIAFTDLP-ANLYPTVGLQTPGEIVDANFGQ 219
Cdd:cd12909    81 KPYGPTFTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIKkGNLYPTVGLRTPGEHVEANFGQ 144

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585645734 102 IYYFEVKIVSKGrDGYMGIGLSAQGVNM--NRLPGWDKHSYGYHGDDGHSFCSSgTGQPYG-PTFTTGDVIGCCVNLING 178
Cdd:pfam00622   1 RHYFEVEIFGQD-GGGWRVGWATKSVPRkgERFLGDESGSWGYDGWTGKKYWAS-TSPLTGlPLFEPGDVIGCFLDYEAG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1585645734 179 TCFYTKNGHSLGIAFTDLPA--NLYPTVGLQtPGEIVDANFGQQ 220
Cdd:pfam00622  79 TISFTKNGKSLGYAFRDVPFagPLFPAVSLG-AGEGLKFNFGLR 121

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1585645734 291 SIKNRQKIQKLVLEGRVGEAIETTQRFYPGLLEHNPNLLFMLKCRQFVEMVNGTD 345
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGK 55

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1585645734 528 EYGK------NLAHTEMLQDAFSLLAYSDPWSC-PVGHQLDPIQREPVCAALNSAILESQNLPKQPPLMLALGQASECL 599
Cdd:pfam10607  61 EYARenlapfNEEHLKELEKLMGLLAFPDPTDSsPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKAGLSAL 139

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.

                          10        20
                  ....*....|....*....|...
gi 1585645734 257 LQNMVSSYLVHHGYCSTATAFAR 279
Cdd:pfam08513   2 LNRLIYDYLVKEGYEETAEAFEK 24

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585645734  77 YKGHGKNHKDAASVRATHPIPAACGIYYFEVKIVSKGRDGYMGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTG 156
Cdd:cd12909     1 YKGPGKTDKDAAAVRANHPIPPQCGIYYFEVKIISKGRDGYIGIGFSTKDVNLNRLPGWEPHSWGYHGDDGHSFCSSGTG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1585645734 157 QPYGPTFTTGDVIGCCVNLINGTCFYTKNGHSLGIAFTDLP-ANLYPTVGLQTPGEIVDANFGQ 219
Cdd:cd12909    81 KPYGPTFTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIKkGNLYPTVGLRTPGEHVEANFGQ 144

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585645734  100 CGIYYFEVKIVSKGrdgYMGIGLSAQGVN--MNRLPGWDKHSYGYHGDDGHsFCSSGTGQPYGPTFT-TGDVIGCCVNLI 176
Cdd:smart00449   1 SGRHYFEVEIGDGG---HWRVGVATKSVPrgYFALLGEDKGSWGYDGDGGK-KYHNSTGPEYGLPLQePGDVIGCFLDLE 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1585645734  177 NGTCFYTKNGHSLGI-AFTDLPAN--LYPTVGLQtPGEIVDANFGQQ 220
Cdd:smart00449  77 AGTISFYKNGKYLHGlAFFDVKFSgpLYPAFSLG-SGNSVRLNFGPL 122

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585645734  80 HGKNHKDAASVRATHPI-PAACgiyYFEVKIVSKGRDGYMGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQP 158
Cdd:cd12908    17 HGRGIGDVGLAQARRPLsPDNH---YFEVEIVDPGVRCYIAIGLAPQDYPLDRHPGWNPGSVAYHADDGKLFKGSGVGDQ 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1585645734 159 YGPTFTTGDVIGCCVNLING-----------------TCFYTKNGHSLGIAFTDLPAN-LYPTVGLQTPGEIV 213
Cdd:cd12908    94 FGPRCTKGDRMGCGIRFPRDydtdsedqgdeeegrtvQVFFTRNGKEVGRTEVPLPPGgFYPAVGMHSEGEKV 166

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585645734 101 GIYYFEVKIVSkGRDGYMGIGLSAQGVNMN--RLPGWDKHSYGYHGDDGHSfCSSGTGQPYGPTFTTGDVIGCCVNLING 178
Cdd:cd11709     1 GKWYWEVRVDS-GNGGLIQVGWATKSFSLDgeGGVGDDEESWGYDGSRLRK-GHGGSSGPGGRPWKSGDVVGCLLDLDEG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1585645734 179 TCFYTKNGHSLGIAFTDLPA---NLYPTVGLqTPGEIVDAN 216
Cdd:cd11709    79 TLSFSLNGKDLGVAFTNLFLkggGLYPAVSL-GSGQGVTIN 118

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585645734  90 VRATHPIPAAcGIYYFEVKIVSKG--RdgymgIGLSAQGVNMNRlpGWDKHSYGYHGDDGHSFCSSGTGqpYGPTFTTGD 167
Cdd:cd12873    30 CRATKGVKGK-GKYYYEVTVTDEGlcR-----VGWSTEDASLDL--GTDKFGFGYGGTGKKSHGRQFDD--YGEPFGLGD 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1585645734 168 VIGCCVNLINGTCFYTKNGHSLGIAFtDLPAN-----LYPTVGLQtpGEIVDANFGQQP 221
Cdd:cd12873   100 VIGCYLDLDNGTISFSKNGKDLGKAF-DIPPHlrnsaLFPAVCLK--NAEVEFNFGDKP 155

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585645734  56 SWSPKDKYNYIGLSQGNLRVHYkghgknHKD----AASVRATHPIPAacGIYYFEVKIVSK--GRDgyMGIGLSAQGVNM 129
Cdd:cd12876     3 TWDERDKSPAVQLSDNNREVYF------HPDyscgTAAVRGTKPLTN--GQHYWEIKMSSPvyGTD--MMVGVGTKKADL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585645734 130 NR-------LPGWDKHSYGY-------HGddghsfcssGTGQPYGPTFTT-GDVIGCCVNLINGTCFYTKNGHSLGIAFT 194
Cdd:cd12876    73 HAyryefcsLLGEDEESWGLsykgllwHD---------GQSRPYTSPFGNqGTIIGVHLDMWRGTLTFYKNGKPLGVAFT 143

                         170
                  ....*....|..
gi 1585645734 195 DLPA--NLYPTV 204
Cdd:cd12876   144 GLNGvkPLYPMV 155

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585645734  89 SVRAThpipaAC---GIYYFEVKIVSKGrdgYMGIGLSAQGVNMNRLPG-WDKH-SYGYhgdDGHSFCS-SGTGQPYGPT 162
Cdd:cd12882     1 SIRAN-----ACvykGKWMYEVTLGTKG---IMQIGWATISCRFTQEEGvGDTRdSYAY---DGNRVRKwNVSTQKYGEP 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585645734 163 FTTGDVIGCCVNLINGTCFYTKNGHSLGIAFTDLPAN----LYPTVGLQTpGEIVDANFG 218
Cdd:cd12882    70 WVAGDVIGCCIDLDKGTISFYRNGRSLGVAFDNVRRGpglaYFPAVSLSF-GERLELNFG 128

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1585645734 291 SIKNRQKIQKLVLEGRVGEAIETTQRFYPGLLEHNPNLLFMLKCRQFVEMVNGTD 345
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGK 55

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1585645734 528 EYGK------NLAHTEMLQDAFSLLAYSDPWSC-PVGHQLDPIQREPVCAALNSAILESQNLPKQPPLMLALGQASECL 599
Cdd:pfam10607  61 EYARenlapfNEEHLKELEKLMGLLAFPDPTDSsPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKAGLSAL 139

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585645734 101 GIYYFEVKIVSkgrDGYMGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFcsSGTGQPYGPTFTTGDVIGCCVNLINGTC 180
Cdd:cd12878    14 GKWYFEFEVLT---SGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKW--HQGSESFGKQWQPGDVVGCMLDLVDRTI 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1585645734 181 FYTKNGH----SLG--IAFTDLPAN--LYPTVGLQTpGEIVDANFG 218
Cdd:cd12878    89 SFTLNGEllidSSGseVAFKDIEIGegFVPACSLGV-GQKGRLNLG 133

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585645734 101 GIYYFEVKIVSkgrDGYMGIGLSAQGVNMNRLPGwdkhsYGYhGDDGHSFCSSGTGQPY----------GPTFTTGDVIG 170
Cdd:cd12883     1 GVWYYEVTVLT---SGVMQIGWATKDSKFLNHEG-----YGI-GDDEYSCAYDGCRQLIwynakskphtHPRWKPGDVLG 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1585645734 171 CCVNLINGTCFYTKNGHSLG---IAFTDLPANLYPTVGLQTPGEiVDANFG 218
Cdd:cd12883    72 CLLDLNKKQMIFSLNGNRLPperQVFTSAKSGFFAAASFMSFQQ-CEFNFG 121

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585645734 103 YYFEVKI------------------VSKGRDGYMGIGLSAQGVnmnrLPGWDKHSYGYhgdDGHSFCSSG----TGQPYG 160
Cdd:cd12877    20 WYFEVEVdhveqfthqpahlrvgwaNTSGYVPYPGGGEGWGGN----GVGDDLYSYGF---DGLHLWTGGrsrrVTSGTQ 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1585645734 161 PTFTTGDVIGCCVNLINGTCFYTKNGHSLGIAFTD--LPANLYPTV 204
Cdd:cd12877    93 HLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENfnLDGMFFPVM 138

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1585645734 132 LPGWDKHSYGYHGDDGHSFCSSGTGQPY-----GPTFTTGDVIGCCVNLINGTCFYTKNGHSLGIAFTDLP-ANLYPTV 204
Cdd:cd12907    77 LLGSDDQSWGWNLVDNHLLHNGDSQGNYpqcnnAPKYQVGERIRVILDCEDNTLAFERGYEFLGVAFRGLPpTKLYPAV 155

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.

                          10        20
                  ....*....|....*....|...
gi 1585645734 257 LQNMVSSYLVHHGYCSTATAFAR 279
Cdd:pfam08513   2 LNRLIYDYLVKEGYEETAEAFEK 24