PHD finger found in Schizosaccharomyces pombe Set1 complex component ash2 (spAsh2p) and similar proteins; spAsh2p, also termed Set1C component ash2, or COMPASS component ash2, or complex proteins associated with set1 protein ash2, or Lid2 complex component ash2, or Lid2C component ash2, is orthologous to Drosophila melanogaster Ash2 protein. Both spAsh2p and D. melanogaster Ash2 contain a plant homeodomain (PHD) finger and a SPRY domain. In contrast, its counterpart in Saccharomyces cerevisiae, Bre2p, has no PHD finger and is not included in this family. spAsh2p shows histone H3 Lys4 (H3K4) methyltransferase activity through its PHD finger. It also interacts with Lid2p in S. pombe. Human Ash2L contains an atypical PHD finger that lacks part of the Cys4HisCys3 signature characteristic of PHD fingers, it binds to only one zinc ion through the second half of the motif and does not have histone tail binding activity.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 528491263  58 ENGRQLGEVELQCALCMKWFTADTFSIDTATCLPFMTNYVFHCNVC 103
Cdd:cd15583    5 GKDRNLGEVELQCSICLKWFHAKCVSIDNGSCLPFMTNYQFVCKRC 50

PHD finger found in Schizosaccharomyces pombe Set1 complex component ash2 (spAsh2p) and similar proteins; spAsh2p, also termed Set1C component ash2, or COMPASS component ash2, or complex proteins associated with set1 protein ash2, or Lid2 complex component ash2, or Lid2C component ash2, is orthologous to Drosophila melanogaster Ash2 protein. Both spAsh2p and D. melanogaster Ash2 contain a plant homeodomain (PHD) finger and a SPRY domain. In contrast, its counterpart in Saccharomyces cerevisiae, Bre2p, has no PHD finger and is not included in this family. spAsh2p shows histone H3 Lys4 (H3K4) methyltransferase activity through its PHD finger. It also interacts with Lid2p in S. pombe. Human Ash2L contains an atypical PHD finger that lacks part of the Cys4HisCys3 signature characteristic of PHD fingers, it binds to only one zinc ion through the second half of the motif and does not have histone tail binding activity.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 528491263  58 ENGRQLGEVELQCALCMKWFTADTFSIDTATCLPFMTNYVFHCNVC 103
Cdd:cd15583    5 GKDRNLGEVELQCSICLKWFHAKCVSIDNGSCLPFMTNYQFVCKRC 50

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 528491263  377 WFFEVTVDEmPQDAAARLGW---SQPLGNlQAPLGYDKFSYSWRSKKGTRFHQSIGKHYSDG-YGLGDILGFFIelpdet 452
Cdd:pfam00622   2 HYFEVEIFG-QDGGGWRVGWatkSVPRKG-ERFLGDESGSWGYDGWTGKKYWASTSPLTGLPlFEPGDVIGCFL------ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491263  453 etakalpdtykdkalikfksylyfeekDYvdkaeknlkptsTSRMIFF-KNGVNQGVAYEDL-FEGMYYPAISLYKGCTV 530
Cdd:pfam00622  74 ---------------------------DY------------EAGTISFtKNGKSLGYAFRDVpFAGPLFPAVSLGAGEGL 114

                  ....*
gi 528491263  531 SVNFG 535
Cdd:pfam00622 115 KFNFG 119

PHD finger found in Schizosaccharomyces pombe Set1 complex component ash2 (spAsh2p) and similar proteins; spAsh2p, also termed Set1C component ash2, or COMPASS component ash2, or complex proteins associated with set1 protein ash2, or Lid2 complex component ash2, or Lid2C component ash2, is orthologous to Drosophila melanogaster Ash2 protein. Both spAsh2p and D. melanogaster Ash2 contain a plant homeodomain (PHD) finger and a SPRY domain. In contrast, its counterpart in Saccharomyces cerevisiae, Bre2p, has no PHD finger and is not included in this family. spAsh2p shows histone H3 Lys4 (H3K4) methyltransferase activity through its PHD finger. It also interacts with Lid2p in S. pombe. Human Ash2L contains an atypical PHD finger that lacks part of the Cys4HisCys3 signature characteristic of PHD fingers, it binds to only one zinc ion through the second half of the motif and does not have histone tail binding activity.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 528491263  58 ENGRQLGEVELQCALCMKWFTADTFSIDTATCLPFMTNYVFHCNVC 103
Cdd:cd15583    5 GKDRNLGEVELQCSICLKWFHAKCVSIDNGSCLPFMTNYQFVCKRC 50

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 528491263 337 VLLALHDRAPQLKISDDRLTV---TGEKGYSM---VRASHGVRKGSWFFEVTV----------DEMPQDAAARLGWSQPL 400
Cdd:cd12884    1 VCLDTYNSDLHLKISKDRYSAsplTDEGFAYLwagARATYGVTKGKVCFEVKVtenlpvkhlpTEETDPHVVRVGWSVDS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491263 401 GNLQapLGYDKFSYSWrSKKGTRFHQSIGKHYSDGYGLGDILGFFIELpdETETAKalpdtykdkalikfksylyfeekd 480
Cdd:cd12884   81 SSLQ--LGEEEFSYGY-GSTGKKSTNCKFEDYGEPFGENDVIGCYLDF--ESEPVE------------------------ 131

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491263 481 yvdkaeknlkptstsrmIFF-KNGVNQGVAY----EDLFEGMYYPAIsLYKGCTVSVNFG 535
Cdd:cd12884  132 -----------------ISFsKNGKDLGVAFkiskEELGGKALFPHV-LTKNCAVEVNFG 173

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 528491263 375 GSWFFEVTVDEMPQDAAaRLGWSQPLGNLQA--PLGYDKFSYSWRSKKGTRFHQSIGKHYSDGYGLGDILGFFIELpdet 452
Cdd:cd11709    1 GKWYWEVRVDSGNGGLI-QVGWATKSFSLDGegGVGDDEESWGYDGSRLRKGHGGSSGPGGRPWKSGDVVGCLLDL---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491263 453 etakalpdtykdkalikfksylyfeekdyvdkaeknlkptSTSRMIFFKNGVNQGVAYEDLFEGM--YYPAISLYKGCTV 530
Cdd:cd11709   76 ----------------------------------------DEGTLSFSLNGKDLGVAFTNLFLKGggLYPAVSLGSGQGV 115

                 ...
gi 528491263 531 SVN 533
Cdd:cd11709  116 TIN 118

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491263 364 SMVRASHGV--RKGSWFFEVTVDEMPQDAAARLGWSQPLGNLQAPLGYDKFSYSWRSKKGTRFH-QSIGKHYSDGYGLGD 440
Cdd:cd12885    1 GSVRADHPIppKVPVFYFEVTILDLGEKGIVSIGFCTSGFPLNRMPGWEDGSYGYHGDDGRVYLgGGEGENYGPPFGTGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491263 441 ILGFFIelpdetetakalpdtykdkalikfksylyfeekDYVDKAeknlkptstsrmIFF-KNGVNQGVAYEDLFEGMYY 519
Cdd:cd12885   81 VVGCGI---------------------------------NFKTGE------------VFFtKNGELLGTAFENVVKGRLY 115

                        170
                 ....*....|....*..
gi 528491263 520 PAISL-YKGCTVSVNFG 535
Cdd:cd12885  116 PTVGLgSPGVKVRVNFG 132

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 528491263 366 VRASHGVRKGSWFFEVTVDEMPqdaAARLGWSQP---------LGNLQAPLGYDkfsySWRSKKGTRFHQSIGKHYSdgy 436
Cdd:cd12882    2 IRANACVYKGKWMYEVTLGTKG---IMQIGWATIscrftqeegVGDTRDSYAYD----GNRVRKWNVSTQKYGEPWV--- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491263 437 gLGDILGFFIELPDETetakalpdtykdkalikfksylyfeekdyvdkaeknlkptstsrMIFFKNGVNQGVAYEDL--F 514
Cdd:cd12882   72 -AGDVIGCCIDLDKGT--------------------------------------------ISFYRNGRSLGVAFDNVrrG 106

                        170       180
                 ....*....|....*....|..
gi 528491263 515 EGM-YYPAISLYKGCTVSVNFG 535
Cdd:cd12882  107 PGLaYFPAVSLSFGERLELNFG 128

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 528491263 366 VRASHGVRK--GSWFFEVTVDEMPQDAAARLGWSQPLGNLQAPLGYDKFSYSWRSKKGTRFHQS-IGKHYSDGYGLGDIL 442
Cdd:cd12909   14 VRANHPIPPqcGIYYFEVKIISKGRDGYIGIGFSTKDVNLNRLPGWEPHSWGYHGDDGHSFCSSgTGKPYGPTFTTGDVI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491263 443 GFFIELPDETetakalpdtykdkalikfksylyfeekdyvdkaeknlkptstsrmIFF-KNGVNQGVAYEDLFEGMYYPA 521
Cdd:cd12909   94 GCGINFRDNT---------------------------------------------AFYtKNGVNLGIAFRDIKKGNLYPT 128

                        170
                 ....*....|....*
gi 528491263 522 ISLYK-GCTVSVNFG 535
Cdd:cd12909  129 VGLRTpGEHVEANFG 143