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        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 555290015   7 SVDEENGRQLGEVELQCGICTKWFTADTFGIDTSSCLPFMTNYSFHCNVC 56
Cdd:cd15583    1 YCYCGKDRNLGEVELQCSICLKWFHAKCVSIDNGSCLPFMTNYQFVCKRC 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        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 555290015   7 SVDEENGRQLGEVELQCGICTKWFTADTFGIDTSSCLPFMTNYSFHCNVC 56
Cdd:cd15583    1 YCYCGKDRNLGEVELQCSICLKWFHAKCVSIDNGSCLPFMTNYQFVCKRC 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 555290015  327 WYFEITVDEmPPDTAARLGW---SQPLGNlQAPLGYDKFSYSWRSKKGTKFHQSIGKHYSSG-YGQGDVLGFYINLPEDT 402
Cdd:pfam00622   2 HYFEVEIFG-QDGGGWRVGWatkSVPRKG-ERFLGDESGSWGYDGWTGKKYWASTSPLTGLPlFEPGDVIGCFLDYEAGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555290015  403 etakslpdtykdkalikfksylyfeekdfvdkaekslkqtphseIIFYKNGVNQGVAYRDI-FEGVYFPAISLYKSCTVS 481
Cdd:pfam00622  80 --------------------------------------------ISFTKNGKSLGYAFRDVpFAGPLFPAVSLGAGEGLK 115

                  ....
gi 555290015  482 INFG 485
Cdd:pfam00622 116 FNFG 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        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 555290015   7 SVDEENGRQLGEVELQCGICTKWFTADTFGIDTSSCLPFMTNYSFHCNVC 56
Cdd:cd15583    1 YCYCGKDRNLGEVELQCSICLKWFHAKCVSIDNGSCLPFMTNYQFVCKRC 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 555290015 287 VLLALHDRAPQLKISDDRLTVV---GEKGYSM---VRASHGVRKGAWYFEITVDEMPPDTAA----------RLGWSQPL 350
Cdd:cd12884    1 VCLDTYNSDLHLKISKDRYSASpltDEGFAYLwagARATYGVTKGKVCFEVKVTENLPVKHLpteetdphvvRVGWSVDS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555290015 351 GNLQapLGYDKFSYSWrSKKGTKFHQSIGKHYSSGYGQGDVLGFYINLpeDTETAkslpdtykdkalikfksylyfeekd 430
Cdd:cd12884   81 SSLQ--LGEEEFSYGY-GSTGKKSTNCKFEDYGEPFGENDVIGCYLDF--ESEPV------------------------- 130

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 555290015 431 fvdkaekslkqtphsEIIFYKNGVNQGVAYRdIFEGVY-----FPAIsLYKSCTVSINFG 485
Cdd:cd12884  131 ---------------EISFSKNGKDLGVAFK-ISKEELggkalFPHV-LTKNCAVEVNFG 173

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 555290015 293 DRAPQLKISDDRLTV--VGEKGYSMVRASHGVR-KGAWYFEITVDEmppDTAARLGWSQPLGNLQapLGYDKFSYSWrSK 369
Cdd:cd12873    5 DRDAALAISPDGLLCqsREEKGWQGCRATKGVKgKGKYYYEVTVTD---EGLCRVGWSTEDASLD--LGTDKFGFGY-GG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555290015 370 KGTKFHQSIGKHYSSGYGQGDVLGFYINLpedtetakslpdtykDKALIKfksylyfeekdfvdkaekslkqtphseiiF 449
Cdd:cd12873   79 TGKKSHGRQFDDYGEPFGLGDVIGCYLDL---------------DNGTIS-----------------------------F 114

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 555290015 450 YKNGVNQGVAYrDI----FEGVYFPAISLyKSCTVSINFG 485
Cdd:cd12873  115 SKNGKDLGKAF-DIpphlRNSALFPAVCL-KNAEVEFNFG 152

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 555290015 314 SMVRASHGV--RKGAWYFEITVDEMPPDTAARLGWSQPLGNLQAPLGYDKFSYSWRSKKGTKFH-QSIGKHYSSGYGQGD 390
Cdd:cd12885    1 GSVRADHPIppKVPVFYFEVTILDLGEKGIVSIGFCTSGFPLNRMPGWEDGSYGYHGDDGRVYLgGGEGENYGPPFGTGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555290015 391 VLGFYINLpedtetakslpdtykdkalikfksylyfeekdfvdkaekslkqtPHSEIIFYKNGVNQGVAYRDIFEGVYFP 470
Cdd:cd12885   81 VVGCGINF--------------------------------------------KTGEVFFTKNGELLGTAFENVVKGRLYP 116

                        170
                 ....*....|....*.
gi 555290015 471 AISL-YKSCTVSINFG 485
Cdd:cd12885  117 TVGLgSPGVKVRVNFG 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 555290015 316 VRASHGVRKGAWYFEITVDEMPpdtAARLGWSQP---------LGNLQAPLGYDkfsySWRSKKGTKFHQSIGKHYSSGy 386
Cdd:cd12882    2 IRANACVYKGKWMYEVTLGTKG---IMQIGWATIscrftqeegVGDTRDSYAYD----GNRVRKWNVSTQKYGEPWVAG- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555290015 387 gqgDVLGFYINLPEDTetakslpdtykdkalikfksylyfeekdfvdkaekslkqtphseIIFYKNGVNQGVAYRDIFEG 466
Cdd:cd12882   74 ---DVIGCCIDLDKGT--------------------------------------------ISFYRNGRSLGVAFDNVRRG 106

                        170       180
                 ....*....|....*....|..
gi 555290015 467 ---VYFPAISLYKSCTVSINFG 485
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 555290015 316 VRASHGVRK--GAWYFEITVDEMPPDTAARLGWSQPLGNLQAPLGYDKFSYSWRSKKGTKFHQS-IGKHYSSGYGQGDVL 392
Cdd:cd12909   14 VRANHPIPPqcGIYYFEVKIISKGRDGYIGIGFSTKDVNLNRLPGWEPHSWGYHGDDGHSFCSSgTGKPYGPTFTTGDVI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555290015 393 GFYINlpedtetakslpdtykdkalikfksylyfeekdFVDKaekslkqtphseIIFY-KNGVNQGVAYRDIFEGVYFPA 471
Cdd:cd12909   94 GCGIN---------------------------------FRDN------------TAFYtKNGVNLGIAFRDIKKGNLYPT 128

                        170
                 ....*....|....*
gi 555290015 472 ISLYKSC-TVSINFG 485
Cdd:cd12909  129 VGLRTPGeHVEANFG 143

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 555290015 439 LKQTPHSEIIFYKNGVNQGVAYRDIFEGVYfPAISLYKSCT-VSI 482
Cdd:cd12887  117 VMRTSDGTLHFYVNGEDQGVAASNVPQPVY-AVVDLYGQCEqVSI 160