NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|18139549|ref|NP_085151|]
View 

histone-lysine N-methyltransferase SETD7 isoform 1 [Homo sapiens]

Protein Classification

SETD7 family SET domain-containing protein( domain architecture ID 15524553)

SETD7 family 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

EC:  2.1.1.-
Gene Ontology:  GO:0005515|GO:1904047|GO:0016279
PubMed:  12372294|17013555

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SET_SETD7 cd10530
SET domain found in SET domain-containing protein 7 (SETD7) and similar proteins; SETD7 (EC 2. ...
 208-337 5.82e-96

SET domain found in SET domain-containing protein 7 (SETD7) and similar proteins; SETD7 (EC 2.1.1.43; also termed histone H3-K4 methyltransferase SETD7, H3-K4-HMTase SETD7, lysine N-methyltransferase 7 (KMT7) or SET7/9) is a histone-lysine N-methyltransferase that specifically monomethylates 'Lys-4' of histone H3. It plays a central role in the transcriptional activation of genes such as collagenase or insulin. Set7/9 also methylates non-histone proteins, including estrogen receptor alpha (ERa), suggesting it has a role in diverse biological processes. ERa methylation by Set7/9 stabilizes ERa and activates its transcriptional activities, which are involved in the carcinogenesis of breast cancer. In a high-throughput screen, treatment of human breast cancer cells (MCF7 cells) with cyproheptadine, a Set7/9 inhibitor, decreased the expression and transcriptional activity of ERa, thereby inhibiting estrogen-dependent cell growth.


:

Pssm-ID: 380928  Cd Length: 130  Bit Score: 281.50  E-value: 5.82e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549 208 PDPYESERVYVAESLISSAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKY 287
Cdd:cd10530   1 PDPYESERVYVAESLIPSAGEGLFAKVAVGPNTVMSFYNGVRITHQEVDSRDWSLNGNTISLDEETVIDVPEPYNSVSKY 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 18139549 288 CASLGHKANHSFTPNCIYDMFVHPRFGPIKCIRTLRAVEADEELTVAYGY 337
Cdd:cd10530  81 CASLGHKANHSFTPNCIYDPFVHPRFGPIKCIRTLRAVEAGEELTVAYGY 130
COG4642 super family cl34799
Uncharacterized conserved protein [Function unknown];
19-132 9.72e-24

Uncharacterized conserved protein [Function unknown];


The actual alignment was detected with superfamily member COG4642:

Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 98.88  E-value: 9.72e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549  19 DGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEY 98
Cdd:COG4642 156 NGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLT 235

                        90       100       110
                ....*....|....*....|....*....|....
gi 18139549  99 DTDGRlIFKGQYKDNIRHGVCWIYYPDGGSLVGE 132
Cdd:COG4642 236 YADGD-RYEGEFKNGKRHGQGTMTYADGSVYEGE 268
 
Name Accession Description Interval E-value
SET_SETD7 cd10530
SET domain found in SET domain-containing protein 7 (SETD7) and similar proteins; SETD7 (EC 2. ...
 208-337 5.82e-96

SET domain found in SET domain-containing protein 7 (SETD7) and similar proteins; SETD7 (EC 2.1.1.43; also termed histone H3-K4 methyltransferase SETD7, H3-K4-HMTase SETD7, lysine N-methyltransferase 7 (KMT7) or SET7/9) is a histone-lysine N-methyltransferase that specifically monomethylates 'Lys-4' of histone H3. It plays a central role in the transcriptional activation of genes such as collagenase or insulin. Set7/9 also methylates non-histone proteins, including estrogen receptor alpha (ERa), suggesting it has a role in diverse biological processes. ERa methylation by Set7/9 stabilizes ERa and activates its transcriptional activities, which are involved in the carcinogenesis of breast cancer. In a high-throughput screen, treatment of human breast cancer cells (MCF7 cells) with cyproheptadine, a Set7/9 inhibitor, decreased the expression and transcriptional activity of ERa, thereby inhibiting estrogen-dependent cell growth.


Pssm-ID: 380928  Cd Length: 130  Bit Score: 281.50  E-value: 5.82e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549 208 PDPYESERVYVAESLISSAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKY 287
Cdd:cd10530   1 PDPYESERVYVAESLIPSAGEGLFAKVAVGPNTVMSFYNGVRITHQEVDSRDWSLNGNTISLDEETVIDVPEPYNSVSKY 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 18139549 288 CASLGHKANHSFTPNCIYDMFVHPRFGPIKCIRTLRAVEADEELTVAYGY 337
Cdd:cd10530  81 CASLGHKANHSFTPNCIYDPFVHPRFGPIKCIRTLRAVEAGEELTVAYGY 130
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
19-132 9.72e-24

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 98.88  E-value: 9.72e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549  19 DGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEY 98
Cdd:COG4642 156 NGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLT 235

                        90       100       110
                ....*....|....*....|....*....|....
gi 18139549  99 DTDGRlIFKGQYKDNIRHGVCWIYYPDGGSLVGE 132
Cdd:COG4642 236 YADGD-RYEGEFKNGKRHGQGTMTYADGSVYEGE 268
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
210-339 1.31e-15

SET domain-containing protein (function unknown) [General function prediction only];


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 72.69  E-value: 1.31e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549 210 PYESERVYVAESLIssAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWA---LNGNTLSLDEETVIDvpepynhvSK 286
Cdd:COG2940   2 AMLHPRIEVRPSPI--HGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHkepLHTYLFELDDDGVID--------GA 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 18139549 287 YCASLGHKANHSFTPNCIYDMFVHPRFgpikcIRTLRAVEADEELTVAYGYDH 339
Cdd:COG2940  72 LGGNPARFINHSCDPNCEADEEDGRIF-----IVALRDIAAGEELTYDYGLDY 119
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 226-342 2.07e-11

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: 60.81  E-value: 2.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549    226 AGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNTL------SLDEETVIDvPEPYNHVSKYCaslghkaNHSF 299
Cdd:smart00317  11 KGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkafylfDIDSDLCID-ARRKGNLARFI-------NHSC 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 18139549    300 TPNCIydMFVHPRFGPIK-CIRTLRAVEADEELTVAYGYDHSPP 342
Cdd:smart00317  83 EPNCE--LLFVEVNGDDRiVIFALRDIKPGEELTIDYGSDYANE 124
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 227-336 5.73e-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: 56.38  E-value: 5.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549   227 GEGLFSKVAVGPNT-VMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDV--PEPYNHVSKYCASLGHKA---NHSFT 300
Cdd:pfam00856   1 GRGLFATEDIPKGEfIGEYVEVLLITKEEADKRELLYYDKLELRLWGPYLFTldEDSEYCIDARALYYGNWArfiNHSCD 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 18139549   301 PNCIYDMFVHPRFGPIkCIRTLRAVEADEELTVAYG 336
Cdd:pfam00856  81 PNCEVRVVYVNGGPRI-VIFALRDIKPGEELTIDYG 115
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 20-131 5.03e-07

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 51.76  E-value: 5.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549   20 GLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQ--- 96
Cdd:PLN03185  41 GMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQEGPGKytw 120

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18139549   97 ----EYDTD---------GRLI------FKGQYKDNIRHGVCWIYYPDGGSLVG 131
Cdd:PLN03185 121 angnVYLGDmkggkmsgkGTLTwvsgdsYEGQWLDGMMHGFGVYTWSDGGCYVG 174
 
Name Accession Description Interval E-value
SET_SETD7 cd10530
SET domain found in SET domain-containing protein 7 (SETD7) and similar proteins; SETD7 (EC 2. ...
 208-337 5.82e-96

SET domain found in SET domain-containing protein 7 (SETD7) and similar proteins; SETD7 (EC 2.1.1.43; also termed histone H3-K4 methyltransferase SETD7, H3-K4-HMTase SETD7, lysine N-methyltransferase 7 (KMT7) or SET7/9) is a histone-lysine N-methyltransferase that specifically monomethylates 'Lys-4' of histone H3. It plays a central role in the transcriptional activation of genes such as collagenase or insulin. Set7/9 also methylates non-histone proteins, including estrogen receptor alpha (ERa), suggesting it has a role in diverse biological processes. ERa methylation by Set7/9 stabilizes ERa and activates its transcriptional activities, which are involved in the carcinogenesis of breast cancer. In a high-throughput screen, treatment of human breast cancer cells (MCF7 cells) with cyproheptadine, a Set7/9 inhibitor, decreased the expression and transcriptional activity of ERa, thereby inhibiting estrogen-dependent cell growth.


Pssm-ID: 380928  Cd Length: 130  Bit Score: 281.50  E-value: 5.82e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549 208 PDPYESERVYVAESLISSAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKY 287
Cdd:cd10530   1 PDPYESERVYVAESLIPSAGEGLFAKVAVGPNTVMSFYNGVRITHQEVDSRDWSLNGNTISLDEETVIDVPEPYNSVSKY 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 18139549 288 CASLGHKANHSFTPNCIYDMFVHPRFGPIKCIRTLRAVEADEELTVAYGY 337
Cdd:cd10530  81 CASLGHKANHSFTPNCIYDPFVHPRFGPIKCIRTLRAVEAGEELTVAYGY 130
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
19-132 9.72e-24

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 98.88  E-value: 9.72e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549  19 DGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEY 98
Cdd:COG4642 156 NGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLT 235

                        90       100       110
                ....*....|....*....|....*....|....
gi 18139549  99 DTDGRlIFKGQYKDNIRHGVCWIYYPDGGSLVGE 132
Cdd:COG4642 236 YADGD-RYEGEFKNGKRHGQGTMTYADGSVYEGE 268
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
19-112 5.50e-20

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 88.47  E-value: 5.50e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549  19 DGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEY 98
Cdd:COG4642 179 NGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTMT 258

                        90
                ....*....|....
gi 18139549  99 DTDGRlIFKGQYKD 112
Cdd:COG4642 259 YADGS-VYEGEWKN 271
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
6-153 1.53e-19

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 87.32  E-value: 1.53e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549   6 EMVEEAVEGHLDDDGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGT 85
Cdd:COG4642 120 EGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGE 199

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18139549  86 YVDGELNGPAQEYDTDGRlIFKGQYKDNIRHGVCWIYYPDGGSLVGEVnEDGEMTGEKIaYVYPDERT 153
Cdd:COG4642 200 FKNGQRHGQGTYTYADGD-RYEGEFKNGKRHGQGTLTYADGDRYEGEF-KNGKRHGQGT-MTYADGSV 264
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
210-339 1.31e-15

SET domain-containing protein (function unknown) [General function prediction only];


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 72.69  E-value: 1.31e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549 210 PYESERVYVAESLIssAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWA---LNGNTLSLDEETVIDvpepynhvSK 286
Cdd:COG2940   2 AMLHPRIEVRPSPI--HGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHkepLHTYLFELDDDGVID--------GA 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 18139549 287 YCASLGHKANHSFTPNCIYDMFVHPRFgpikcIRTLRAVEADEELTVAYGYDH 339
Cdd:COG2940  72 LGGNPARFINHSCDPNCEADEEDGRIF-----IVALRDIAAGEELTYDYGLDY 119
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
19-169 3.51e-15

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 74.61  E-value: 3.51e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549  19 DGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEY 98
Cdd:COG4642 110 GGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLT 189

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18139549  99 DTDGRlIFKGQYKDNIRHGVCWIYYPDGGSLVGEVnEDGEMTGEKIaYVYPDertalyGKFIDGEMIEGKL 169
Cdd:COG4642 190 YANGD-VYEGEFKNGQRHGQGTYTYADGDRYEGEF-KNGKRHGQGT-LTYAD------GDRYEGEFKNGKR 251
YwqK COG2849
Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];
33-165 9.73e-14

Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];


Pssm-ID: 442097 [Multi-domain]  Cd Length: 163  Bit Score: 68.56  E-value: 9.73e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549  33 TDRFEGNFVHGEKNGRGKFFFFDGSTLEGYYVDDALQGQGVYTYEDGGVL-QGTYVDGELNGPAQEYDTDGRLIFKGQYK 111
Cdd:COG2849  31 GYKSGVKEKTEDSYNEGGKLIKKKLGKGLGKYKKGKLGEWKTYYPNGQLKsEGTYKNGKLEGEWKEYYENGKLKSEGNYK 110

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18139549 112 DNIRHGVCWIYYPDgGSLVGEVN-EDGEMTGEKIAYvYPDERTALYGKFIDGEMI 165
Cdd:COG2849 111 NGKLHGEWKEYYEN-GKLKEEGNyKNGKKDGVWKYY-DENGKLVKEEEYKNGKKV 163
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 226-342 2.07e-11

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: 60.81  E-value: 2.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549    226 AGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNTL------SLDEETVIDvPEPYNHVSKYCaslghkaNHSF 299
Cdd:smart00317  11 KGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkafylfDIDSDLCID-ARRKGNLARFI-------NHSC 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 18139549    300 TPNCIydMFVHPRFGPIK-CIRTLRAVEADEELTVAYGYDHSPP 342
Cdd:smart00317  83 EPNCE--LLFVEVNGDDRiVIFALRDIKPGEELTIDYGSDYANE 124
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 227-336 5.73e-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: 56.38  E-value: 5.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549   227 GEGLFSKVAVGPNT-VMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDV--PEPYNHVSKYCASLGHKA---NHSFT 300
Cdd:pfam00856   1 GRGLFATEDIPKGEfIGEYVEVLLITKEEADKRELLYYDKLELRLWGPYLFTldEDSEYCIDARALYYGNWArfiNHSCD 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 18139549   301 PNCIYDMFVHPRFGPIkCIRTLRAVEADEELTVAYG 336
Cdd:pfam00856  81 PNCEVRVVYVNGGPRI-VIFALRDIKPGEELTIDYG 115
YwqK COG2849
Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];
43-163 6.92e-10

Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];


Pssm-ID: 442097 [Multi-domain]  Cd Length: 163  Bit Score: 57.39  E-value: 6.92e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549  43 GEKNGRGKFFFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEYDTDGRLIFKGQYKDNIRHGVCWIY 122
Cdd:COG2849  18 LKYELGDTLLEKNGYKSGVKEKTEDSYNEGGKLIKKKLGKGLGKYKKGKLGEWKTYYPNGQLKSEGTYKNGKLEGEWKEY 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 18139549 123 YPDgGSLVGEVN-EDGEMTGEKIAYvYPDERTALYGKFIDGE 163
Cdd:COG2849  98 YEN-GKLKSEGNyKNGKLHGEWKEY-YENGKLKEEGNYKNGK 137
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
13-164 5.13e-09

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 56.50  E-value: 5.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549  13 EGHLDDDGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGELN 92
Cdd:COG4642  81 GGGGKGDGGDGGGGEGGFGGGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPH 160

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18139549  93 GPAQEYDTDGRlIFKGQYKDNIRHGVCWIYYPDGGSLVGEVnEDGEMTGEKIaYVYPDERTalY-GKFIDGEM 164
Cdd:COG4642 161 GQGTLTYADGD-RYEGEFKNGKRHGQGTLTYANGDVYEGEF-KNGQRHGQGT-YTYADGDR--YeGEFKNGKR 228
SET_EZH cd10519
SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...
 214-337 3.85e-08

SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar proteins; The family includes EZH1 and EZH2. EZH1 (EC 2.1.1.43; also termed ENX-2, or histone-lysine N-methyltransferase EZH1) is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. EZH2 (EC 2.1.1.43; also termed lysine N-methyltransferase 6, ENX-1, or histone-lysine N-methyltransferase EZH2) is a catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Both, EZH1 and EZH2, can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively.


Pssm-ID: 380917  Cd Length: 117  Bit Score: 51.09  E-value: 3.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549 214 ERVYVAESLIssAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNTLS----LDEETVIDVPEPYNhVSKYca 289
Cdd:cd10519   1 KRLLLGKSDV--AGWGLFLKEPIKKDEFIGEYTGELISQDEADRRGKIYDKYNSSylfnLNDQFVVDATRKGN-KIRF-- 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 18139549 290 slghkANHSFTPNCI-YDMFV---HpRFGpikcIRTLRAVEADEELTVAYGY 337
Cdd:cd10519  76 -----ANHSSNPNCYaKVMMVngdH-RIG----IFAKRDIEAGEELFFDYGY 117
SET_SETD1-like cd10518
SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...
 212-338 1.85e-07

SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), histone-lysine N-methyltransferases (KMT2A/KMT2B/KMT2C/KMT2D) and similar proteins; This family includes SET domain-containing protein 1A (SETD1A), 1B (SETD1B), as well as histone-lysine N-methyltransferase 2A (KMT2A), 2B (KMT2B), 2C (KMT2C), 2D (KMT2D). These proteins are histone-lysine N-methyltransferases (EC 2.1.1.43) that specifically methylate 'Lys-4' of histone H3 (H3K4me).


Pssm-ID: 380916  Cd Length: 150  Bit Score: 49.90  E-value: 1.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549 212 ESERVYVAESLIssAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSR----DWALNGNT--LSLDEETVIDvpepynhvS 285
Cdd:cd10518  12 LKERLRVGKSGI--HGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKRekryDEEGGGGTymFRIDEDLVID--------A 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 18139549 286 KYCASLGHKANHSFTPNCIYDMFVHPRFGPIkCIRTLRAVEADEELTvaygYD 338
Cdd:cd10518  82 TKKGNIARFINHSCDPNCYAKIITVDGEKHI-VIFAKRDIAPGEELT----YD 129
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 291-336 2.16e-07

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: 47.63  E-value: 2.16e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 18139549 291 LGHKANHSFTPNCIYDMFVHPRFGPIkCIRTLRAVEADEELTVAYG 336
Cdd:cd08161  28 LARFINHSCEPNCEFEEVYVGGKPRV-FIVALRDIKAGEELTVDYG 72
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 20-131 5.03e-07

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 51.76  E-value: 5.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549   20 GLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQ--- 96
Cdd:PLN03185  41 GMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQEGPGKytw 120

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18139549   97 ----EYDTD---------GRLI------FKGQYKDNIRHGVCWIYYPDGGSLVG 131
Cdd:PLN03185 121 angnVYLGDmkggkmsgkGTLTwvsgdsYEGQWLDGMMHGFGVYTWSDGGCYVG 174
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 19-104 2.00e-06

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 49.83  E-value: 2.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549   19 DGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEY 98
Cdd:PLN03185 109 QGLQEGPGKYTWANGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTWTRGLKDGKGVFY 188


                 ....*.
gi 18139549   99 DTDGRL 104
Cdd:PLN03185 189 PAGSRV 194
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 31-126 5.19e-06

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 48.29  E-value: 5.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549   31 SSTDRFEGNFVHGEKNGRGKFFFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEYDTDGrLIFKGQY 110
Cdd:PLN03185   6 SNGDFYSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDG-TTYKGRW 84

                         90
                 ....*....|....*.
gi 18139549  111 KDNIRHGVCWIYYPDG 126
Cdd:PLN03185  85 RLNLKHGLGYQRYPNG 100
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
 294-342 2.72e-05

SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing protein, and similar proteins; The family includes SET and MYND domain-containing proteins, SMYD1-SYMD5. SMYD1 (EC 2.1.1.43; also termed BOP) is a heart and muscle specific SET-MYND domain containing protein, which functions as a histone methyltransferase and regulates downstream gene transcription. It methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. SMYD2 (also termed HSKM-B, or lysine N-methyltransferase 3C (KMT3C)) functions as a histone methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. It specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). SMYD3 (also termed zinc finger MYND domain-containing protein 1) functions as a histone methyltransferase that specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. It also methylates 'Lys-5' of histone H4. SMYD3 plays an important role in transcriptional activation as a member of an RNA polymerase complex. SMYD4 functions as a potential tumor suppressor that plays a critical role in breast carcinogenesis at least partly through inhibiting the expression of PDGFR-alpha. SMYD5 (also termed protein NN8-4AG, or retinoic acid-induced protein 15) functions as histone lysine methyltransferase that mediates H4K20me3 at heterochromatin regions.


Pssm-ID: 380997 [Multi-domain]  Cd Length: 122  Bit Score: 43.14  E-value: 2.72e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 18139549 294 KANHSFTPNCiydmFVHPRFGPIKCIRTLRAVEADEELTVAYGYDHSPP 342
Cdd:cd20071  58 LLNHSCDPNA----VVVFDGNGTLRVRALRDIKAGEELTISYIDPLLPR 102
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
 296-339 1.22e-04

SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces pombe Set7 is a novel histone-lysine N-methyltransferase. The family also includes a viral histone H3 lysine 27 methyltransferase from Paramecium bursaria Chlorella virus 1 (PBCV-1).


Pssm-ID: 380938  Cd Length: 112  Bit Score: 41.08  E-value: 1.22e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 18139549 296 NHSFTPNCIYDM-FVHPRFGpikcIRTLRAVEADEELTVAYGYDH 339
Cdd:cd10540  70 NHSYTPNAEYEIdFENQTIV----FYALRDIEAGEELTINYGDDL 110
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
 215-338 2.77e-04

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), 2D (KMT2D) and similar proteins; This family includes KMT2C and KMT2D. Both, KMT2C (also termed HALR or MLL3) and KMT2D (also termed ALR or MLL2), act as histone methyltransferases that methylate 'Lys-4' of histone H3 (H3K4me). They are subunits of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation.


Pssm-ID: 380948 [Multi-domain]  Cd Length: 153  Bit Score: 40.88  E-value: 2.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549 215 RVYVAESLIssAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNT-----LSLDEETVIDVPEpynhvskyCA 289
Cdd:cd19171  15 NVYLARSRI--QGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNrgiymFRIDNDWVIDATM--------TG 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 18139549 290 SLGHKANHSFTPNCIYDMfVHprFGPIK--CIRTLRAVEADEELTVAYGYD 338
Cdd:cd19171  85 GPARYINHSCNPNCVAEV-VT--FDKEKkiIIISNRRIAKGEELTYDYKFD 132
SET_Suv4-20-like cd10524
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
 295-336 3.14e-04

SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of variegation 4-20 (Suv4-20) and similar proteins; Suv4-20 (also termed Su(var)4-20) is a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-20' of histone H4. It acts as a dominant suppressor of position-effect variegation. The family also includes Suv4-20 homologs, lysine N-methyltransferase 5B (KMT5B) and lysine N-methyltransferase 5C (KMT5C). Both KMT5B (also termed lysine-specific methyltransferase 5B, or suppressor of variegation 4-20 homolog 1, or Su(var)4-20 homolog 1, or Suv4-20h1) and KMT5C (also termed lysine-specific methyltransferase 5C, or suppressor of variegation 4-20 homolog 2, or Su(var)4-20 homolog 2, or Suv4-20h2) are histone methyltransferases that specifically trimethylate 'Lys-20' of histone H4 (H4K20me3). They play central roles in the establishment of constitutive heterochromatin in pericentric heterochromatin regions.


Pssm-ID: 380922 [Multi-domain]  Cd Length: 141  Bit Score: 40.34  E-value: 3.14e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 18139549 295 ANHSFTPNCIYDmfvhPRFGPIKCIRTLRAVEADEELTVAYG 336
Cdd:cd10524  80 INHDCRPNCKFV----PTGKSTACVKVLRDIEPGEEITVYYG 117
SET_EZH2 cd19218
SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...
 226-337 3.32e-04

SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43), also termed lysine N-methyltransferase 6, or ENX-1, or histone-lysine N-methyltransferase EZH2, is a catalytic subunit of the polycomb repressive complex 2 (PRC2)/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. It can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. PRC2 is involved in several cancers; EZH2 is overexpressed in breast, liver and prostate cancer, while point mutations in EZH2 alter the substrate preference and product specificity of PRC2 in Non-Hodgkin lymphomas (NHLs). Thus, PRC2 is a popular target for cancer therapeutics.


Pssm-ID: 380995  Cd Length: 120  Bit Score: 39.90  E-value: 3.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549 226 AGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSR----DWALNGNTLSLDEETVIDVPEPYNHVskycaslgHKANHSFTP 301
Cdd:cd19218  14 AGWGIFIKDPVQKNEFISEYCGEIISQDEADRRgkvyDKYMCSFLFNLNNDFVVDATRKGNKI--------RFANHSVNP 85

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 18139549 302 NCIYD-MFVHP--RFGpikcIRTLRAVEADEELTVAYGY 337
Cdd:cd19218  86 NCYAKvMMVNGdhRIG----IFAKRAIQTGEELFFDYRY 120
SET_EZH1 cd19217
SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43) ...
 226-340 5.17e-04

SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43), also termed ENX-2, or histone-lysine N-methyltransferase EZH1, is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. It can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively.


Pssm-ID: 380994  Cd Length: 136  Bit Score: 39.67  E-value: 5.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549 226 AGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSR----DWALNGNTLSLDEETVIDVPEPYNHVskycaslgHKANHSFTP 301
Cdd:cd19217  16 AGWGTFIKESVQKNEFISEYCGELISQDEADRRgkvyDKYMSSFLFNLNNDFVVDATRKGNKI--------RFANHSVNP 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 18139549 302 NCIYDMFV---HPRFGpikcIRTLRAVEADEELTVAYGYDHS 340
Cdd:cd19217  88 NCYAKVVMvngDHRIG----IFAKRAIQQGEELFFDYRYSQA 125
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
 215-338 5.68e-04

SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and similar proteins; LegAS4 is a type IV secretion system effector of Legionella pneumophila. It contains a SET domain that is involved in the modification of Lys4 of histone H3 (H3K4) in the nucleolus of the host cell, thereby enhancing heterochromatic rDNA transcription. It also contains an ankyrin repeat domain of unknown function at its C-terminal region.


Pssm-ID: 380920 [Multi-domain]  Cd Length: 122  Bit Score: 39.25  E-value: 5.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549 215 RVYVAE-SLISSAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSR---------DWALNGNTLSLDEEtvidvpePYNHV 284
Cdd:cd10522   1 KVDISMiPNLSHNGLGLFAAETIAKGEFVGEYTGEVLDRWEEDRDsvyhydplyPFDLNGDILVIDAG-------KKGNL 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18139549 285 SKYcaslghkANHSFTPNCiyDMFVHPRFGPIKC-IRTLRAVEADEELTVAYGYD 338
Cdd:cd10522  74 TRF-------INHSDQPNL--ELIVRTLKGEQHIgFVAIRDIKPGEELFISYGPK 119
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
 267-338 1.22e-03

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: 38.78  E-value: 1.22e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18139549 267 LSLDEETVIDvPEPYNHVSKYcaslghkANHSFTPNCI---YDMFVHPRFGpikcIRTLRAVEADEELTVAYGYD 338
Cdd:cd10531  57 LSLSDDVVID-ATRKGNLSRF-------INHSCEPNCEtqkWIVNGEYRIG----IFALRDIPAGEELTFDYNFV 119
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
 227-338 1.44e-03

SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ASH1L (EC 2.1.1.43; also termed absent small and homeotic disks protein 1 homolog, KMT2H, or lysine N-methyltransferase 2H) acts as histone-lysine N-methyltransferase that specifically methylates 'Lys-36' of histone H3 (H3K36me). It plays important roles in development; heterozygous mutation of ASH1L is associated with severe intellectual disability (ID) and multiple congenital anomaly (MCA).


Pssm-ID: 380951 [Multi-domain]  Cd Length: 141  Bit Score: 38.43  E-value: 1.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18139549 227 GEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNT-----LSLDEETVIDvpepynhvSKYCASLGHKANHSFTP 301
Cdd:cd19174  11 GWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRMIEQYHNHshhycLNLDSGMVID--------GYRMGNEARFVNHSCDP 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 18139549 302 NC---IYDMFVHPRFGpikcIRTLRAVEADEELTVAYGYD 338
Cdd:cd19174  83 NCemqKWSVNGVYRIG----LFALKDIPAGEELTYDYNFH 118
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH