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Conserved domains on  [gi|555290015|ref|NP_001273136|]
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set1/Ash2 histone methyltransferase complex subunit ASH2 isoform b [Mus musculus]

Protein Classification

Set1/Ash2 histone methyltransferase complex subunit ASH2( domain architecture ID 10204188)

Set1/Ash2 histone methyltransferase complex subunit ASH2 acts as a transcriptional regulator that is a component or associated component of some histone methyltransferase complexes which regulates transcription through recruitment of those complexes to gene promoters

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
298-489 7.98e-79

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: 243.96  E-value: 7.98e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555290015 298 LKISDDRLTVVGEKGYSMVRASHGVRKGAWYFEITVDEMP--PDTAARLGWSQPLGNLQAPLGYDKFSYSWRSKKGTKFH 375
Cdd:cd12872    1 LKLSEDRLTVTGEKGYRMARANHGVREGKWYFEVKILEGGgtETGHVRVGWSRREASLQAPVGYDKYSYAIRDKDGSKFH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555290015 376 QSIGKHYS-SGYGQGDVLGFYINLPedtetakslpdtykdkalikfksylyfeekdfvdkaekslkqtphsEIIFYKNGV 454
Cdd:cd12872   81 QSRGKPYGePGFKEGDVIGFLITLP----------------------------------------------KIEFFKNGK 114
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 555290015 455 NQGVAYRDI-FEGVYFPAISLYKSCTVSINFGPSFK 489
Cdd:cd12872  115 SQGVAFEDIyGTGGYYPAVSLYKGATVTINFGPDFK 150
PHD_ash2p_like cd15583
PHD finger found in Schizosaccharomyces pombe Set1 complex component ash2 (spAsh2p) and ...
7-56 4.31e-24

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.


:

Pssm-ID: 277058  Cd Length: 50  Bit Score: 94.72  E-value: 4.31e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 555290015   7 SVDEENGRQLGEVELQCGICTKWFTADTFGIDTSSCLPFMTNYSFHCNVC 56
Cdd:cd15583    1 YCYCGKDRNLGEVELQCSICLKWFHAKCVSIDNGSCLPFMTNYQFVCKRC 50
 
Name Accession Description Interval E-value
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
298-489 7.98e-79

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: 243.96  E-value: 7.98e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555290015 298 LKISDDRLTVVGEKGYSMVRASHGVRKGAWYFEITVDEMP--PDTAARLGWSQPLGNLQAPLGYDKFSYSWRSKKGTKFH 375
Cdd:cd12872    1 LKLSEDRLTVTGEKGYRMARANHGVREGKWYFEVKILEGGgtETGHVRVGWSRREASLQAPVGYDKYSYAIRDKDGSKFH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555290015 376 QSIGKHYS-SGYGQGDVLGFYINLPedtetakslpdtykdkalikfksylyfeekdfvdkaekslkqtphsEIIFYKNGV 454
Cdd:cd12872   81 QSRGKPYGePGFKEGDVIGFLITLP----------------------------------------------KIEFFKNGK 114
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 555290015 455 NQGVAYRDI-FEGVYFPAISLYKSCTVSINFGPSFK 489
Cdd:cd12872  115 SQGVAFEDIyGTGGYYPAVSLYKGATVTINFGPDFK 150
PHD_ash2p_like cd15583
PHD finger found in Schizosaccharomyces pombe Set1 complex component ash2 (spAsh2p) and ...
7-56 4.31e-24

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.


Pssm-ID: 277058  Cd Length: 50  Bit Score: 94.72  E-value: 4.31e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 555290015   7 SVDEENGRQLGEVELQCGICTKWFTADTFGIDTSSCLPFMTNYSFHCNVC 56
Cdd:cd15583    1 YCYCGKDRNLGEVELQCSICLKWFHAKCVSIDNGSCLPFMTNYQFVCKRC 50
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
324-486 7.30e-24

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: 96.59  E-value: 7.30e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555290015   324 KGAWYFEITVDEmppDTAARLGWSQPLGNL--QAPLGYDKFSYSWRSKKGTKFHQSIGKHYSSGYGQ-GDVLGFYINLPE 400
Cdd:smart00449   1 SGRHYFEVEIGD---GGHWRVGVATKSVPRgyFALLGEDKGSWGYDGDGGKKYHNSTGPEYGLPLQEpGDVIGCFLDLEA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555290015   401 DTetakslpdtykdkalikfksylyfeekdfvdkaekslkqtphseIIFYKNGVN-QGVAYRDI-FEGVYFPAISLYKSC 478
Cdd:smart00449  78 GT--------------------------------------------ISFYKNGKYlHGLAFFDVkFSGPLYPAFSLGSGN 113

                   ....*...
gi 555290015   479 TVSINFGP 486
Cdd:smart00449 114 SVRLNFGP 121
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
327-485 5.09e-16

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: 74.30  E-value: 5.09e-16
                          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
 
Name Accession Description Interval E-value
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
298-489 7.98e-79

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: 243.96  E-value: 7.98e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555290015 298 LKISDDRLTVVGEKGYSMVRASHGVRKGAWYFEITVDEMP--PDTAARLGWSQPLGNLQAPLGYDKFSYSWRSKKGTKFH 375
Cdd:cd12872    1 LKLSEDRLTVTGEKGYRMARANHGVREGKWYFEVKILEGGgtETGHVRVGWSRREASLQAPVGYDKYSYAIRDKDGSKFH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555290015 376 QSIGKHYS-SGYGQGDVLGFYINLPedtetakslpdtykdkalikfksylyfeekdfvdkaekslkqtphsEIIFYKNGV 454
Cdd:cd12872   81 QSRGKPYGePGFKEGDVIGFLITLP----------------------------------------------KIEFFKNGK 114
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 555290015 455 NQGVAYRDI-FEGVYFPAISLYKSCTVSINFGPSFK 489
Cdd:cd12872  115 SQGVAFEDIyGTGGYYPAVSLYKGATVTINFGPDFK 150
PHD_ash2p_like cd15583
PHD finger found in Schizosaccharomyces pombe Set1 complex component ash2 (spAsh2p) and ...
7-56 4.31e-24

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.


Pssm-ID: 277058  Cd Length: 50  Bit Score: 94.72  E-value: 4.31e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 555290015   7 SVDEENGRQLGEVELQCGICTKWFTADTFGIDTSSCLPFMTNYSFHCNVC 56
Cdd:cd15583    1 YCYCGKDRNLGEVELQCSICLKWFHAKCVSIDNGSCLPFMTNYQFVCKRC 50
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
324-486 7.30e-24

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: 96.59  E-value: 7.30e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555290015   324 KGAWYFEITVDEmppDTAARLGWSQPLGNL--QAPLGYDKFSYSWRSKKGTKFHQSIGKHYSSGYGQ-GDVLGFYINLPE 400
Cdd:smart00449   1 SGRHYFEVEIGD---GGHWRVGVATKSVPRgyFALLGEDKGSWGYDGDGGKKYHNSTGPEYGLPLQEpGDVIGCFLDLEA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555290015   401 DTetakslpdtykdkalikfksylyfeekdfvdkaekslkqtphseIIFYKNGVN-QGVAYRDI-FEGVYFPAISLYKSC 478
Cdd:smart00449  78 GT--------------------------------------------ISFYKNGKYlHGLAFFDVkFSGPLYPAFSLGSGN 113

                   ....*...
gi 555290015   479 TVSINFGP 486
Cdd:smart00449 114 SVRLNFGP 121
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
287-485 3.34e-20

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: 88.03  E-value: 3.34e-20
                         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 cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
325-483 4.42e-17

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: 77.09  E-value: 4.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555290015 325 GAWYFEITVDEMPPdTAARLGWSQPLGNLQA--PLGYDKFSYSWRSKKGTKFHQSIGKHYSSGYGQGDVLGFYINLPEDT 402
Cdd:cd11709    1 GKWYWEVRVDSGNG-GLIQVGWATKSFSLDGegGVGDDEESWGYDGSRLRKGHGGSSGPGGRPWKSGDVVGCLLDLDEGT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555290015 403 etakslpdtykdkalikfksylyfeekdfvdkaekslkqtphseIIFYKNGVNQGVAYRDIFE--GVYFPAISLYKSCTV 480
Cdd:cd11709   80 --------------------------------------------LSFSLNGKDLGVAFTNLFLkgGGLYPAVSLGSGQGV 115

                 ...
gi 555290015 481 SIN 483
Cdd:cd11709  116 TIN 118
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
293-485 4.57e-17

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: 78.38  E-value: 4.57e-17
                         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 pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
327-485 5.09e-16

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: 74.30  E-value: 5.09e-16
                          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
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
314-485 1.05e-12

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: 64.99  E-value: 1.05e-12
                         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
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
316-485 2.51e-10

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: 58.47  E-value: 2.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555290015 316 VRASHGVRKGAWYFE---ITVDEMppdtaaRLGWSQPLGNLQAPLGYDKFSYSWRSKKGTKFHQSiGKHYSSGYGQGDVL 392
Cdd:cd12878    5 AEKTYAVTSGKWYFEfevLTSGYM------RVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQG-SESFGKQWQPGDVV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555290015 393 GFYINLPEDTetakslpdtykdkalikfksylyfeekdfvdkaekslkqtphseIIFYKNGV----NQG--VAYRDIFEG 466
Cdd:cd12878   78 GCMLDLVDRT--------------------------------------------ISFTLNGEllidSSGseVAFKDIEIG 113
                        170       180
                 ....*....|....*....|
gi 555290015 467 V-YFPAISLYKSCTVSINFG 485
Cdd:cd12878  114 EgFVPACSLGVGQKGRLNLG 133
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
316-485 1.51e-07

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: 50.40  E-value: 1.51e-07
                         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
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
11-56 1.65e-07

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) finger typically characterized as Cys4HisCys3, and a non-canonical extended PHD finger, characterized as Cys2HisCys5HisCys2His. Variations include the RAG2 PHD finger characterized by Cys3His2Cys2His and the PHD finger 5 found in nuclear receptor-binding SET domain-containing proteins characterized by Cys4HisCys2His. The PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. Single or multiple copies of PHD fingers have been found in a variety of eukaryotic proteins involved in the control of gene transcription and chromatin dynamics. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. They also function as epigenome readers controlling gene expression through molecular recruitment of multi-protein complexes of chromatin regulators and transcription factors. The PHD finger domain SF is structurally similar to the RING and FYVE_like superfamilies.


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 47.70  E-value: 1.65e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 555290015  11 ENGRQLGEVELQCGICTKWFTADTFGIDTSSclpFMTNYSFHCNVC 56
Cdd:cd15489    6 GKGGDLGGELLQCDGCGKWFHADCLGPPLSS---FVPNGKWICPVC 48
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
316-485 3.06e-05

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: 44.05  E-value: 3.06e-05
                         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_like cd12886
SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ...
325-485 3.44e-04

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: 40.57  E-value: 3.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555290015 325 GAWYFEITVDEMPPDTAARLGW---SQPLGNLQAPLGYDKFSYSWRSKKGTK-FHQSIGKHYSSGYGQGDVLGFYINLPE 400
Cdd:cd12886    1 GKWYWEVTVVSSAASTYAGIGVanaAATGNNGLNGIELSSIGYSLGVYSGNKlSNGSSVATYGAGFTAGDVIGVALDLDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555290015 401 DTetakslpdtykdkalikfksylyfeekdfvdkaekslkqtphseIIFYKNGVNQGV------AYRDIFEGVYFPAISL 474
Cdd:cd12886   81 GK--------------------------------------------IWFYKNGVWQGGgdpapgTNPAFAGTAMYPAVTG 116
                        170
                 ....*....|...
gi 555290015 475 YKSC--TVSINFG 485
Cdd:cd12886  117 GSSTggSFTANFG 129
SPRY_NHR_like cd12887
SPRY domain in neuralized homology repeat; This family contains the neuralized homology repeat ...
439-482 4.51e-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: 4.51e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 555290015 439 LKQTPHSEIIFYKNGVNQGVAYRDIFEGVYfPAISLYKSCT-VSI 482
Cdd:cd12887  117 VMRTSDGTLHFYVNGEDQGVAASNVPQPVY-AVVDLYGQCEqVSI 160
 
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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