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Conserved domains on  [gi|17570515|ref|NP_508049|]
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SET domain-containing protein [Caenorhabditis elegans]

Protein Classification

SET domain-containing protein( domain architecture ID 1562517)

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain-containing protein may function as a protein-lysine N-methyltransferase, catalyzing the S-adenosyl-L-methionine (SAM)-dependent methylation at specific lysine residues of target proteins such as histones

CATH:  2.170.270.10
EC:  2.1.1.-
Gene Ontology:  GO:0005515|GO:0008168|GO:1904047
PubMed:  12372294|17013555|16086857

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SET super family cl40432
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 52-153 4.49e-17

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, Enhancer-of-zeste, Trithorax (SET) domain superfamily corresponds to SET domain-containing lysine methyltransferases, which catalyze site and state-specific methylation of lysine residues in histones that are fundamental in epigenetic regulation of gene activation and silencing in eukaryotic organisms. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains has been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as N-SET and C-SET. C-SET forms an unusual and conserved knot-like structure of probable functional importance. In addition to N-SET and C-SET, an insert region (I-SET) and flanking regions of high structural variability form part of the overall structure. Some family members contain a pre-SET domain, which is found in a number of histone methyltransferases (HMTase), and a post-SET domain, which harbors a zinc-binding site.


The actual alignment was detected with superfamily member cd10529:

Pssm-ID: 394802  Cd Length: 127  Bit Score: 74.62  E-value: 4.49e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570515  52 TRALRAPRDLKPGESIVMIRG-FC---AFHHEIQPDHRSQRYLFTYG-----PVYLDARAmSKNPGKFVRRSCIPNSYLR 122
Cdd:cd10529  16 RKGLVATEDISPGEPILEYKGeVSlrsEFKEDNGFFKRPSPFVFFYDgfeglPLCVDARK-YGNEARFIRRSCRPNAELR 94

                        90       100       110
                ....*....|....*....|....*....|..
gi 17570515 123 CGR-TDSEFYLIIVAKEFIRNGVEITIDFNAD 153
Cdd:cd10529  95 HVVvSNGELRLFIFALKDIRKGTEITIPFDYD 126
 
Name Accession Description Interval E-value
SET_SETD5-like cd10529
SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...
 52-153 4.49e-17

SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar proteins; SETD5 is a probable transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. KMT2E (also termed inactive lysine N-methyltransferase 2E or myeloid/lymphoid or mixed-lineage leukemia protein 5 (MLL5)) associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription. The family also includes Saccharomyces cerevisiae SET domain-containing proteins, SET3 and SET4, and Schizosaccharomyces pombe SET3. Most of these family members contain a post-SET domain which harbors a zinc-binding site.


Pssm-ID: 380927  Cd Length: 127  Bit Score: 74.62  E-value: 4.49e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570515  52 TRALRAPRDLKPGESIVMIRG-FC---AFHHEIQPDHRSQRYLFTYG-----PVYLDARAmSKNPGKFVRRSCIPNSYLR 122
Cdd:cd10529  16 RKGLVATEDISPGEPILEYKGeVSlrsEFKEDNGFFKRPSPFVFFYDgfeglPLCVDARK-YGNEARFIRRSCRPNAELR 94

                        90       100       110
                ....*....|....*....|....*....|..
gi 17570515 123 CGR-TDSEFYLIIVAKEFIRNGVEITIDFNAD 153
Cdd:cd10529  95 HVVvSNGELRLFIFALKDIRKGTEITIPFDYD 126
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 53-149 3.39e-10

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure.


Pssm-ID: 459965 [Multi-domain]  Cd Length: 115  Bit Score: 55.99  E-value: 3.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570515    53 RALRAPRDLKPGESIVMIRGFCAFHHEIQPDHRSQR-----------YLFTYGPV---YLDARAMSK-NPGKFVRRSCIP 117
Cdd:pfam00856   2 RGLFATEDIPKGEFIGEYVEVLLITKEEADKRELLYydklelrlwgpYLFTLDEDseyCIDARALYYgNWARFINHSCDP 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 17570515   118 NSYLRCGRTDSEFYLIIVAKEFIRNGVEITID 149
Cdd:pfam00856  82 NCEVRVVYVNGGPRIVIFALRDIKPGEELTID 113
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 42-156 1.07e-09

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on outlier plant homologues


Pssm-ID: 214614 [Multi-domain]  Cd Length: 124  Bit Score: 54.65  E-value: 1.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570515     42 SVLISKSPVYTRALRAPRDLKPGESI-----VMIRGFCAFHHEIQPDHRSQ--RYLFT-YGPVYLDARAMSkNPGKFVRR 113
Cdd:smart00317   2 KLEVFKSPGKGWGVRATEDIPKGEFIgeyvgEIITSEEAEERPKAYDTDGAkaFYLFDiDSDLCIDARRKG-NLARFINH 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 17570515    114 SCIPNSYLRCGRTDSEFYLIIVAKEFIRNGVEITIDFNADVFP 156
Cdd:smart00317  81 SCEPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYAN 123
 
Name Accession Description Interval E-value
SET_SETD5-like cd10529
SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...
 52-153 4.49e-17

SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar proteins; SETD5 is a probable transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. KMT2E (also termed inactive lysine N-methyltransferase 2E or myeloid/lymphoid or mixed-lineage leukemia protein 5 (MLL5)) associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription. The family also includes Saccharomyces cerevisiae SET domain-containing proteins, SET3 and SET4, and Schizosaccharomyces pombe SET3. Most of these family members contain a post-SET domain which harbors a zinc-binding site.


Pssm-ID: 380927  Cd Length: 127  Bit Score: 74.62  E-value: 4.49e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570515  52 TRALRAPRDLKPGESIVMIRG-FC---AFHHEIQPDHRSQRYLFTYG-----PVYLDARAmSKNPGKFVRRSCIPNSYLR 122
Cdd:cd10529  16 RKGLVATEDISPGEPILEYKGeVSlrsEFKEDNGFFKRPSPFVFFYDgfeglPLCVDARK-YGNEARFIRRSCRPNAELR 94

                        90       100       110
                ....*....|....*....|....*....|..
gi 17570515 123 CGR-TDSEFYLIIVAKEFIRNGVEITIDFNAD 153
Cdd:cd10529  95 HVVvSNGELRLFIFALKDIRKGTEITIPFDYD 126
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 53-149 3.39e-10

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure.


Pssm-ID: 459965 [Multi-domain]  Cd Length: 115  Bit Score: 55.99  E-value: 3.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570515    53 RALRAPRDLKPGESIVMIRGFCAFHHEIQPDHRSQR-----------YLFTYGPV---YLDARAMSK-NPGKFVRRSCIP 117
Cdd:pfam00856   2 RGLFATEDIPKGEFIGEYVEVLLITKEEADKRELLYydklelrlwgpYLFTLDEDseyCIDARALYYgNWARFINHSCDP 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 17570515   118 NSYLRCGRTDSEFYLIIVAKEFIRNGVEITID 149
Cdd:pfam00856  82 NCEVRVVYVNGGPRIVIFALRDIKPGEELTID 113
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 42-156 1.07e-09

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on outlier plant homologues


Pssm-ID: 214614 [Multi-domain]  Cd Length: 124  Bit Score: 54.65  E-value: 1.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570515     42 SVLISKSPVYTRALRAPRDLKPGESI-----VMIRGFCAFHHEIQPDHRSQ--RYLFT-YGPVYLDARAMSkNPGKFVRR 113
Cdd:smart00317   2 KLEVFKSPGKGWGVRATEDIPKGEFIgeyvgEIITSEEAEERPKAYDTDGAkaFYLFDiDSDLCIDARRKG-NLARFINH 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 17570515    114 SCIPNSYLRCGRTDSEFYLIIVAKEFIRNGVEITIDFNADVFP 156
Cdd:smart00317  81 SCEPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYAN 123
SET_SpSET3-like cd19183
SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...
 55-154 1.03e-08

SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET domain-containing protein 3 (SETD3) and similar proteins; Schizosaccharomyces pombe SETD3 functions as a transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. It is required for both, gene activation and repression.


Pssm-ID: 380960  Cd Length: 173  Bit Score: 53.18  E-value: 1.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570515  55 LRAPRDLKPGESIVMIRGFCAFHHEIQPDHRSQ-RYLFT---------YGPVYLDARaMSKNPGKFVRRSCIPNSYLRCG 124
Cdd:cd19183  16 LFADRPIPAGDPIQELLGEIGLQSEYIADPENQyQILGApkphvffhpQSPLYIDTR-RSGSVARFIRRSCRPNAELVTV 94

                        90       100       110
                ....*....|....*....|....*....|..
gi 17570515 125 RTDSEFYL--IIVAKEFIRNGVEITIDFNADV 154
Cdd:cd19183  95 ASDSGSVLkfVLYASRDISPGEEITIGWDWDN 126
SET_KMT2E cd19182
SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...
 42-153 8.51e-08

SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar proteins; KMT2E (also termed inactive lysine N-methyltransferase 2E, myeloid/lymphoid or mixed-lineage leukemia protein 5 (MLL5)) plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. It associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription. Lack of key residues in the SET domain as well as the presence of an unusually large loop in the SET-I subdomain preclude the interaction of MLL5 SET with its cofactor and substrate thus making MLL5 devoid of any in vitro methyltransferase activity on full-length histones and histone H3 peptide.


Pssm-ID: 380959  Cd Length: 129  Bit Score: 49.51  E-value: 8.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570515  42 SVLISKSPVYT------RALRAPRDLKPGESIVMIRGFCAFHHEIQPD----HRSQRYLFTYGPVY-----LDARAMSkN 106
Cdd:cd19182   2 SNLLFKPPVEShvqknkKILKAAKDLPPDTLIIEYRGKFMLREQFEANgyffKRPYPFVLFYSKFHglemcVDARTFG-N 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 17570515 107 PGKFVRRSCIPNSYLRCGRTDSEFYLIIVAKEFIRNGVEITIDFNAD 153
Cdd:cd19182  81 EARFIRRSCTPNAEVRHVIEDGTIHLYIYSIRSIPKGTEITIAFDFD 127
SET_KMT2A cd19206
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...
 42-175 1.93e-07

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) and similar proteins; KMT2A (EC2.1.1.43; also termed lysine N-methyltransferase 2A, ALL-1, CXXC-type zinc finger protein 7 (CXXC7), myeloid/lymphoid or mixed-lineage leukemia (MLL), myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), trithorax-like protein (TRX1), or zinc finger protein HRX) acts as a histone methyltransferase that plays an essential role in early development and hematopoiesis. It is a catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac).


Pssm-ID: 380983 [Multi-domain]  Cd Length: 154  Bit Score: 49.25  E-value: 1.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570515  42 SVLISKSPVYTRALRAPRDLKPGESIVMIRGFCAfhHEIQPDHRSQR--------YLFTYGPVYLDARAMSKNPGKFVRR 113
Cdd:cd19206  15 AVGVYRSPIHGRGLFCKRNIDAGEMVIEYSGNVI--RSILTDKREKYydskgigcYMFRIDDSEVVDATMHGNAARFINH 92

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17570515 114 SCIPNSYLRCGRTDSEFYLIIVAKEFIRNGVEITIDFNadvFPLCSPLECIMHSMDRGNCRK 175
Cdd:cd19206  93 SCEPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYK---FPIEDASNKLPCNCGAKKCRK 151
SET_SETD5 cd19181
SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...
 51-173 3.16e-07

SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and similar proteins; SETD5 is a probable transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. SETD5 loss-of-function mutations are a likely cause of a familial syndromic intellectual disability with variable phenotypic expression.


Pssm-ID: 380958  Cd Length: 150  Bit Score: 48.47  E-value: 3.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570515  51 YTRALRAPRDLKPGESIVMIRGFCAFHHEIQPD----HRSQRYLFTYGP-----VYLDARAMSkNPGKFVRRSCIPNSYL 121
Cdd:cd19181  17 HRKILRAARDLALDTLIIEYRGKVMLRQQFEVNghffKRPYPFVLFYSKfngveMCVDARTFG-NDARFIRRSCTPNAEV 95

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 17570515 122 RCGRTDSEFYLIIVAKEFIRNGVEITIDFNADVFPLCSPLECIMHSMDRgNC 173
Cdd:cd19181  96 RHMIADGMIHLCIYAVAAIAKDAEVTIAFDYEYSNCNYKVDCACHKGNR-NC 146
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
 96-155 3.18e-05

SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), nuclear SETD2 (NSD2), ASH1-like protein (ASH1L) and similar proteins; This family includes SET domain-containing protein 2 (SETD2), nuclear SETD2 (NSD2) and ASH1-like protein (ASH1L), which function as histone-lysine N-methyltransferases. SETD2 specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using demethylated 'Lys-36' (H3K36me2) as substrate. NSD2 shows histone H3 'Lys-27' (H3K27me) methyltransferase activity. ASH1L specifically methylates 'Lys-36' of histone H3 (H3K36me). The family also includes Arabidopsis thaliana ASH1-related protein 3 (ASHR3) and similar proteins.


Pssm-ID: 380929  Cd Length: 136  Bit Score: 42.63  E-value: 3.18e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570515  96 VYLDARAMSkNPGKFVRRSCIPNSYLRCGRTDSEFYLIIVAKEFIRNGVEITIDFNADVF 155
Cdd:cd10531  63 VVIDATRKG-NLSRFINHSCEPNCETQKWIVNGEYRIGIFALRDIPAGEELTFDYNFVNY 121
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 107-151 3.46e-04

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, Enhancer-of-zeste, Trithorax (SET) domain superfamily corresponds to SET domain-containing lysine methyltransferases, which catalyze site and state-specific methylation of lysine residues in histones that are fundamental in epigenetic regulation of gene activation and silencing in eukaryotic organisms. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains has been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as N-SET and C-SET. C-SET forms an unusual and conserved knot-like structure of probable functional importance. In addition to N-SET and C-SET, an insert region (I-SET) and flanking regions of high structural variability form part of the overall structure. Some family members contain a pre-SET domain, which is found in a number of histone methyltransferases (HMTase), and a post-SET domain, which harbors a zinc-binding site.


Pssm-ID: 380914 [Multi-domain]  Cd Length: 72  Bit Score: 38.00  E-value: 3.46e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 17570515 107 PGKFVRRSCIPNSYLRCGRTDSEFYLIIVAKEFIRNGVEITIDFN 151
Cdd:cd08161  28 LARFINHSCEPNCEFEEVYVGGKPRVFIVALRDIKAGEELTVDYG 72
SET_KMT2D cd19209
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...
 41-153 1.36e-03

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) and similar proteins; KMT2D (EC2.1.1.43; also termed lysine N-methyltransferase 2D, ALL1-related protein (ALR), or myeloid/lymphoid or mixed-lineage leukemia protein 2 (MLL2)), acts as histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me). It is a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription. KMT2D is a subunit of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation.


Pssm-ID: 380986 [Multi-domain]  Cd Length: 155  Bit Score: 38.14  E-value: 1.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570515  41 HSVLISKSPVYTRALRAPRDLKPGESIV-----MIRGFCAFHHE-IQPDHRSQRYLFTYGPVYLDARAMSKNPGKFVRRS 114
Cdd:cd19209  16 NNVYLARSRIQGLGLYAAKDLEKHTMVIeyigtIIRNEVANRREkIYEEQNRGIYMFRINNEHVIDATLTGGPARYINHS 95

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 17570515 115 CIPNSYLRCGRTDSEFYLIIVAKEFIRNGVEITIDFNAD 153
Cdd:cd19209  96 CAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFD 134
SET_KMT2B cd19207
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...
 42-163 1.89e-03

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) and similar proteins; KMT2B (EC2.1.1.43; also termed lysine N-methyltransferase 2B, myeloid/lymphoid or mixed-lineage leukemia protein 4 (MLL2/MLL4), trithorax homolog 2 (TRX2), or WW domain-binding protein 7 (WBP-7)), acts as a histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me). It is required during the transcriptionally active period of oocyte growth for the establishment and/or maintenance of bulk H3K4 trimethylation (H3K4me3), global transcriptional silencing that precedes resumption of meiosis, oocyte survival and normal zygotic genome activation.


Pssm-ID: 380984 [Multi-domain]  Cd Length: 154  Bit Score: 37.70  E-value: 1.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570515  42 SVLISKSPVYTRALRAPRDLKPGESIVMIRGFCAfhHEIQPDHRSQRY--------LFTYGPVYLDARAMSKNPGKFVRR 113
Cdd:cd19207  15 AVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVI--RSVLTDKREKFYdskgigcyMFRIDDFDVVDATMHGNAARFINH 92

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 17570515 114 SCIPNSYLRCGRTDSEFYLIIVAKEFIRNGVEITIDFNADVFPLCSPLEC 163
Cdd:cd19207  93 SCEPNCYSRVIHVEGQKHIVIFALRKIYRGEELTYDYKFPIEDASNKLPC 142
 
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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