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 578811309   1 MGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTDLP 80
Cdd:cd12909   42 IGIGFSTKDVNLNRLPGWEPHSWGYHGDDGHSFCSSGTGKPYGPTFTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIK 121

                         90       100
                 ....*....|....*....|...
gi 578811309  81 P-NLYPTVGLQTPGEVVDANFGQ 102
Cdd:cd12909  122 KgNLYPTVGLRTPGEHVEANFGQ 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 578811309  174 SIKNRQRIQKLVLAGRMGEAIETTQQLYPSLLERNPNLLFTLKVRQFIEMVNGTD 228
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 578811309   1 MGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTDLP 80
Cdd:cd12909   42 IGIGFSTKDVNLNRLPGWEPHSWGYHGDDGHSFCSSGTGKPYGPTFTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIK 121

                         90       100
                 ....*....|....*....|...
gi 578811309  81 P-NLYPTVGLQTPGEVVDANFGQ 102
Cdd:cd12909  122 KgNLYPTVGLRTPGEHVEANFGQ 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 578811309    1 MGIGLSAQGVNM--NRLPGWDKHSYGYHGDDGHSFCSSgTGQPYG-PTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFT 77
Cdd:pfam00622  16 WRVGWATKSVPRkgERFLGDESGSWGYDGWTGKKYWAS-TSPLTGlPLFEPGDVIGCFLDYEAGTISFTKNGKSLGYAFR 94

                          90       100
                  ....*....|....*....|....*...
gi 578811309   78 DLP--PNLYPTVGLQtPGEVVDANFGQH 103
Cdd:pfam00622  95 DVPfaGPLFPAVSLG-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 578811309  174 SIKNRQRIQKLVLAGRMGEAIETTQQLYPSLLERNPNLLFTLKVRQFIEMVNGTD 228
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGK 55

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.

                           10        20        30
                   ....*....|....*....|....*....|....
gi 578811309   135 EWQTMIQKMVSSYLVHHGYCATAEAFARSTDQTV 168
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGLSL 34

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 578811309   1 MGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTDLP 80
Cdd:cd12909   42 IGIGFSTKDVNLNRLPGWEPHSWGYHGDDGHSFCSSGTGKPYGPTFTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIK 121

                         90       100
                 ....*....|....*....|...
gi 578811309  81 P-NLYPTVGLQTPGEVVDANFGQ 102
Cdd:cd12909  122 KgNLYPTVGLRTPGEHVEANFGQ 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 578811309     1 MGIGLSAQGVN--MNRLPGWDKHSYGYHGDDGHSFCSSgTGQPYGPTFT-TGDVIGCCVNLINNTCFYTKNGHSLGI-AF 76
Cdd:smart00449  16 WRVGVATKSVPrgYFALLGEDKGSWGYDGDGGKKYHNS-TGPEYGLPLQePGDVIGCFLDLEAGTISFYKNGKYLHGlAF 94

                           90       100
                   ....*....|....*....|....*...
gi 578811309    77 TDLPPN--LYPTVGLQtPGEVVDANFGQ 102
Cdd:smart00449  95 FDVKFSgpLYPAFSLG-SGNSVRLNFGP 121

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 578811309   2 GIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINN-----------------TCF 64
Cdd:cd12908   54 AIGLAPQDYPLDRHPGWNPGSVAYHADDGKLFKGSGVGDQFGPRCTKGDRMGCGIRFPRDydtdsedqgdeeegrtvQVF 133

                         90       100       110
                 ....*....|....*....|....*....|...
gi 578811309  65 YTKNGHSLGIAFTDLPPN-LYPTVGLQTPGEVV 96
Cdd:cd12908  134 FTRNGKEVGRTEVPLPPGgFYPAVGMHSEGEKV 166

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811309   2 GIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCS-SGTGQPYGPTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTDLP 80
Cdd:cd12910   75 AIGFATKPYPPFRLPGWHRGSLAVHSDDGHRYINdPFGGKDFTPPFREGDTIGIGYRFSSGTIFFTRNGKRLGGWDLGEE 154

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 578811309  81 P--------------NLYPTVGL-QTPGEVVdANFGQ 102
Cdd:cd12910  155 LdaeddgvtglegfhDLYAAIGVfGGECEVH-VNPGQ 190

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 578811309  174 SIKNRQRIQKLVLAGRMGEAIETTQQLYPSLLERNPNLLFTLKVRQFIEMVNGTD 228
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGK 55

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

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 578811309   174 SIKNRQRIQKLVLAGRMGEAIETTQQLYPSLLERNPNLLFTLKVRQFIEMVNGTDSE 230
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLE 57

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811309  17 GWDKHSYGYhGDDGhSFCSSGTGQPYGPTFTTGDVIGCCVNLINNTC--FYTKNGHSLGIAFT----DLPPN-LYPTVgl 89
Cdd:cd12884   86 GEEEFSYGY-GSTG-KKSTNCKFEDYGEPFGENDVIGCYLDFESEPVeiSFSKNGKDLGVAFKiskeELGGKaLFPHV-- 161

                         90
                 ....*....|....*
gi 578811309  90 QTPGEVVDANFGQHP 104
Cdd:cd12884  162 LTKNCAVEVNFGQKE 176

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811309   1 MGIGL-SAQGVNMNRLPGWDKHSYGYHG--DDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINNTCFYTKNGHSLG---I 74
Cdd:cd12886   18 AGIGVaNAAATGNNGLNGIELSSIGYSLgvYSGNKLSNGSSVATYGAGFTAGDVIGVALDLDAGKIWFYKNGVWQGggdP 97

                         90       100       110
                 ....*....|....*....|....*....|..
gi 578811309  75 AFTDLPPNL----YPTVGLQ-TPGEVVDANFG 101
Cdd:cd12886   98 APGTNPAFAgtamYPAVTGGsSTGGSFTANFG 129

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.

                           10        20        30
                   ....*....|....*....|....*....|....
gi 578811309   135 EWQTMIQKMVSSYLVHHGYCATAEAFARSTDQTV 168
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGLSL 34

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 578811309  139 MIQKMVSSYLVHHGYCATAEAFAR 162
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAFEK 24

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578811309  45 TFTTGDVIGC-----CVNLINNTCFYTKNGHSLGIAFTDLPPNLYPTVGLQTPGEVVDANFG 101
Cdd:cd13735   87 TLSIGDVAGCgwertDTPPAKGRVYFTHNGQRLPRSLQDVSGGLWPVVHVQKKNTRVRANFG 148