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Conserved domains on  [gi|428186471|gb|EKX55321|]
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hypothetical protein GUITHDRAFT_99101 [Guillardia theta CCMP2712]

Protein Classification

SETD7 family SET domain-containing protein( domain architecture ID 14410563)

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

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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. ...
254-394 6.76e-83

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: 249.91  E-value: 6.76e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471 254 PDPYEAERCRVGTSSLCGtkdegvaggneAGEGLFLRTSAQEGELLSFYNGIRYPHAVVDKRAWKMNGNCISLDEEFAID 333
Cdd:cd10530    1 PDPYESERVYVAESLIPS-----------AGEGLFAKVAVGPNTVMSFYNGVRITHQEVDSRDWSLNGNTISLDEETVID 69
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 428186471 334 VPPEHSSIDRYCASLGHKANHSFQPNAEYAPCFHPRFGHIKCIRALRRMEAGEEVLVHYGY 394
Cdd:cd10530   70 VPEPYNSVSKYCASLGHKANHSFTPNCIYDPFVHPRFGPIKCIRTLRAVEAGEELTVAYGY 130
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
69-206 1.08e-29

Uncharacterized conserved protein [Function unknown];


:

Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 116.21  E-value: 1.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471  69 SPYKRGMKEDEDGARYEGRFKDGMLEGRGTIYFPDGGWQQGIWRDGQMEGEGEYVDDEGYRIHGCWKDGLLNGPGQEVAP 148
Cdd:COG4642  135 GRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYA 214
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 428186471 149 GGFlVYQGEFKDGVRNGMGTLNFLDGGRVYGSWVNGELHGQAEYWYPDGKSgLNGVWK 206
Cdd:COG4642  215 DGD-RYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTMTYADGSV-YEGEWK 270
 
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. ...
254-394 6.76e-83

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: 249.91  E-value: 6.76e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471 254 PDPYEAERCRVGTSSLCGtkdegvaggneAGEGLFLRTSAQEGELLSFYNGIRYPHAVVDKRAWKMNGNCISLDEEFAID 333
Cdd:cd10530    1 PDPYESERVYVAESLIPS-----------AGEGLFAKVAVGPNTVMSFYNGVRITHQEVDSRDWSLNGNTISLDEETVID 69
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 428186471 334 VPPEHSSIDRYCASLGHKANHSFQPNAEYAPCFHPRFGHIKCIRALRRMEAGEEVLVHYGY 394
Cdd:cd10530   70 VPEPYNSVSKYCASLGHKANHSFTPNCIYDPFVHPRFGPIKCIRTLRAVEAGEELTVAYGY 130
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
69-206 1.08e-29

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 116.21  E-value: 1.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471  69 SPYKRGMKEDEDGARYEGRFKDGMLEGRGTIYFPDGGWQQGIWRDGQMEGEGEYVDDEGYRIHGCWKDGLLNGPGQEVAP 148
Cdd:COG4642  135 GRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYA 214
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 428186471 149 GGFlVYQGEFKDGVRNGMGTLNFLDGGRVYGSWVNGELHGQAEYWYPDGKSgLNGVWK 206
Cdd:COG4642  215 DGD-RYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTMTYADGSV-YEGEWK 270
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
71-214 3.91e-16

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 80.65  E-value: 3.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471  71 YKRGMKEDE------DGARYEGRFKDGMLEGRGTIYFPDGGWQQGIWRDGQMEGEGEYVDDEGYRIHGCWKDGLLNGPGQ 144
Cdd:PLN03185  38 WRRGMRHGNgkiswpSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQEGPGK 117
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471 145 EVAPGGFlVYQGEFKDGVRNGMGTLNFLDGGRVYGSWVNGELHGQAEYWYPDGKSgLNGVWKHGdMKEAK 214
Cdd:PLN03185 118 YTWANGN-VYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMMHGFGVYTWSDGGC-YVGTWTRG-LKDGK 184
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
284-393 4.46e-13

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: 65.24  E-value: 4.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471  284 GEGLFLRTSAQEGELLSFYNG---IRYPHAVVDKRAWKMNGNCISLDEEFAIDVPPEHSSIDRYCASLGHKA---NHSFQ 357
Cdd:pfam00856   1 GRGLFATEDIPKGEFIGEYVEvllITKEEADKRELLYYDKLELRLWGPYLFTLDEDSEYCIDARALYYGNWArfiNHSCD 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 428186471  358 PNAEYAPCFHPRFGHIkCIRALRRMEAGEEVLVHYG 393
Cdd:pfam00856  81 PNCEVRVVYVNGGPRI-VIFALRDIKPGEELTIDYG 115
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
282-401 5.17e-11

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 59.98  E-value: 5.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471 282 EAGEGLFLRTSAQEGELLSFYNGIRYPHAVVDKRAWKMNGN---CISLDEEFAIDVppehssidRYCASLGHKANHSFQP 358
Cdd:COG2940   15 IHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKEPLhtyLFELDDDGVIDG--------ALGGNPARFINHSCDP 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 428186471 359 NAEYapcfHPRFGHIkCIRALRRMEAGEEVLVHYGYTNQMPRW 401
Cdd:COG2940   87 NCEA----DEEDGRI-FIVALRDIAAGEELTYDYGLDYDEEEY 124
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
281-394 1.10e-10

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: 58.89  E-value: 1.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471   281 NEAGEGLFLRTSAQEGELLSFYNGIRYPHAVVDKRAWKMNGNCI------SLDEEFAIDvPPEHSSIDRYCaslghkaNH 354
Cdd:smart00317   9 PGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkafylfDIDSDLCID-ARRKGNLARFI-------NH 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 428186471   355 SFQPNAEYAPCFHPRFGHIkCIRALRRMEAGEEVLVHYGY 394
Cdd:smart00317  81 SCEPNCELLFVEVNGDDRI-VIFALRDIKPGEELTIDYGS 119
 
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. ...
254-394 6.76e-83

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: 249.91  E-value: 6.76e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471 254 PDPYEAERCRVGTSSLCGtkdegvaggneAGEGLFLRTSAQEGELLSFYNGIRYPHAVVDKRAWKMNGNCISLDEEFAID 333
Cdd:cd10530    1 PDPYESERVYVAESLIPS-----------AGEGLFAKVAVGPNTVMSFYNGVRITHQEVDSRDWSLNGNTISLDEETVID 69
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 428186471 334 VPPEHSSIDRYCASLGHKANHSFQPNAEYAPCFHPRFGHIKCIRALRRMEAGEEVLVHYGY 394
Cdd:cd10530   70 VPEPYNSVSKYCASLGHKANHSFTPNCIYDPFVHPRFGPIKCIRTLRAVEAGEELTVAYGY 130
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
69-206 1.08e-29

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 116.21  E-value: 1.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471  69 SPYKRGMKEDEDGARYEGRFKDGMLEGRGTIYFPDGGWQQGIWRDGQMEGEGEYVDDEGYRIHGCWKDGLLNGPGQEVAP 148
Cdd:COG4642  135 GRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYA 214
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 428186471 149 GGFlVYQGEFKDGVRNGMGTLNFLDGGRVYGSWVNGELHGQAEYWYPDGKSgLNGVWK 206
Cdd:COG4642  215 DGD-RYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTMTYADGSV-YEGEWK 270
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
77-208 6.88e-24

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 100.03  E-value: 6.88e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471  77 EDEDGARYEGRFKDGMLEGRGTIYFPDGGWQQGIWRDGQMEGEGEYVDDEGYRIHGCWKDGLLNGPGQEVAPGGFlVYQG 156
Cdd:COG4642  120 EGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGD-VYEG 198
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 428186471 157 EFKDGVRNGMGTLNFLDGGRVYGSWVNGELHGQAEYWYPDGKSgLNGVWKHG 208
Cdd:COG4642  199 EFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADGDR-YEGEFKNG 249
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
73-183 1.20e-22

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 96.56  E-value: 1.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471  73 RGMKEDEDGARYEGRFKDGMLEGRGTIYFPDGGWQQGIWRDGQMEGEGEYVDDEGYRIHGCWKDGLLNGPGQEVAPGGFl 152
Cdd:COG4642  162 QGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADGD- 240
                         90       100       110
                 ....*....|....*....|....*....|.
gi 428186471 153 VYQGEFKDGVRNGMGTLNFLDGGRVYGSWVN 183
Cdd:COG4642  241 RYEGEFKNGKRHGQGTMTYADGSVYEGEWKN 271
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
71-214 3.91e-16

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 80.65  E-value: 3.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471  71 YKRGMKEDE------DGARYEGRFKDGMLEGRGTIYFPDGGWQQGIWRDGQMEGEGEYVDDEGYRIHGCWKDGLLNGPGQ 144
Cdd:PLN03185  38 WRRGMRHGNgkiswpSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQEGPGK 117
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471 145 EVAPGGFlVYQGEFKDGVRNGMGTLNFLDGGRVYGSWVNGELHGQAEYWYPDGKSgLNGVWKHGdMKEAK 214
Cdd:PLN03185 118 YTWANGN-VYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMMHGFGVYTWSDGGC-YVGTWTRG-LKDGK 184
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
284-393 4.46e-13

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: 65.24  E-value: 4.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471  284 GEGLFLRTSAQEGELLSFYNG---IRYPHAVVDKRAWKMNGNCISLDEEFAIDVPPEHSSIDRYCASLGHKA---NHSFQ 357
Cdd:pfam00856   1 GRGLFATEDIPKGEFIGEYVEvllITKEEADKRELLYYDKLELRLWGPYLFTLDEDSEYCIDARALYYGNWArfiNHSCD 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 428186471  358 PNAEYAPCFHPRFGHIkCIRALRRMEAGEEVLVHYG 393
Cdd:pfam00856  81 PNCEVRVVYVNGGPRI-VIFALRDIKPGEELTIDYG 115
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
282-401 5.17e-11

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 59.98  E-value: 5.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471 282 EAGEGLFLRTSAQEGELLSFYNGIRYPHAVVDKRAWKMNGN---CISLDEEFAIDVppehssidRYCASLGHKANHSFQP 358
Cdd:COG2940   15 IHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKEPLhtyLFELDDDGVIDG--------ALGGNPARFINHSCDP 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 428186471 359 NAEYapcfHPRFGHIkCIRALRRMEAGEEVLVHYGYTNQMPRW 401
Cdd:COG2940   87 NCEA----DEEDGRI-FIVALRDIAAGEELTYDYGLDYDEEEY 124
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
281-394 1.10e-10

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: 58.89  E-value: 1.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471   281 NEAGEGLFLRTSAQEGELLSFYNGIRYPHAVVDKRAWKMNGNCI------SLDEEFAIDvPPEHSSIDRYCaslghkaNH 354
Cdd:smart00317   9 PGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkafylfDIDSDLCID-ARRKGNLARFI-------NH 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 428186471   355 SFQPNAEYAPCFHPRFGHIkCIRALRRMEAGEEVLVHYGY 394
Cdd:smart00317  81 SCEPNCELLFVEVNGDDRI-VIFALRDIKPGEELTIDYGS 119
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
277-394 6.53e-10

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: 56.58  E-value: 6.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471 277 VAGGNEAGEGLFLRTSAQEGELLSFYNGIRYPHAVVDKR---------AWKMNGNCISLDEEfaidvppEHSSIDRYcas 347
Cdd:cd10522    7 IPNLSHNGLGLFAAETIAKGEFVGEYTGEVLDRWEEDRDsvyhydplyPFDLNGDILVIDAG-------KKGNLTRF--- 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 428186471 348 lghkANHSFQPNAEYAPCFHPRFGHIKCiRALRRMEAGEEVLVHYGY 394
Cdd:cd10522   77 ----INHSDQPNLELIVRTLKGEQHIGF-VAIRDIKPGEELFISYGP 118
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
80-197 8.02e-10

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 60.62  E-value: 8.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471  80 DGARYEGRFKDGMLEGRGTIYFPDGGWQQGIWRDGQMEGEGEYVDDEGYRIHGCWKDGLLNGPGQEVAPGGFlVYQGEFK 159
Cdd:PLN03185  76 DGTTYKGRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQEGPGKYTWANGNVYLGDMKGGKMSGKGTLTWVSGD-SYEGQWL 154
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 428186471 160 DGVRNGMGTLNFLDGGRVYGSWVNGELHGQAEYwYPDG 197
Cdd:PLN03185 155 DGMMHGFGVYTWSDGGCYVGTWTRGLKDGKGVF-YPAG 191
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
55-210 2.02e-08

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 54.96  E-value: 2.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471  55 NSSIARKSRNAAVMSPYKRGMKEDEDGARYEGRFKDGMLEGRGTIYFPDGGWQQGIWRDGQMEGEGEYVDDEGYRIHGCW 134
Cdd:COG4642   29 AGGEGGGGLGTLPGGGGYGGGADGGGGGGGGTGVAGGGGGEGGVTAAGGGGGGGGGKGDGGDGGGGEGGFGGGGGGGGGK 108
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 428186471 135 KDGLLNGPGQEVAPGGfLVYQGEFKDGVRNGMGTLNFLDGGRVYGSWVNGELHGQAEYWYPDGKSgLNGVWKHGDM 210
Cdd:COG4642  109 KGGGGGGGGVLEGDDG-GGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDR-YEGEFKNGKR 182
YwqK COG2849
Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];
76-208 2.50e-08

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


Pssm-ID: 442097 [Multi-domain]  Cd Length: 163  Bit Score: 53.15  E-value: 2.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471  76 KEDEDGARYEGRFKDGMLEGRGTIYFPDGGWQQGIWRDGQMEGEGEYvddegyrihgcwKDGLLNGPGQEVAPGGFLVYQ 155
Cdd:COG2849   39 KTEDSYNEGGKLIKKKLGKGLGKYKKGKLGEWKTYYPNGQLKSEGTY------------KNGKLEGEWKEYYENGKLKSE 106
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 428186471 156 GEFKDGVRNGMGTLNFLDGGRVY-GSWVNGELHGQAEYWYPDGKSGLNGVWKHG 208
Cdd:COG2849  107 GNYKNGKLHGEWKEYYENGKLKEeGNYKNGKKDGVWKYYDENGKLVKEEEYKNG 160
YwqK COG2849
Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];
78-163 1.54e-07

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


Pssm-ID: 442097 [Multi-domain]  Cd Length: 163  Bit Score: 50.84  E-value: 1.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471  78 DEDGA-RYEGRFKDGMLEGRGTIYFPDGG-WQQGIWRDGQMEGEGEYVDDEGY-RIHGCWKDGLLNGPGQEVAPGGFLVY 154
Cdd:COG2849   74 YPNGQlKSEGTYKNGKLEGEWKEYYENGKlKSEGNYKNGKLHGEWKEYYENGKlKEEGNYKNGKKDGVWKYYDENGKLVK 153

                 ....*....
gi 428186471 155 QGEFKDGVR 163
Cdd:COG2849  154 EEEYKNGKK 162
SET_EZH cd10519
SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...
283-394 2.00e-07

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: 49.16  E-value: 2.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471 283 AGEGLFLRTSAQEGELLSFYNGIRYPHAVVDKRAW---KMNGNCI-SLDEEFAIDVppehssidrycASLGHK---ANHS 355
Cdd:cd10519   11 AGWGLFLKEPIKKDEFIGEYTGELISQDEADRRGKiydKYNSSYLfNLNDQFVVDA-----------TRKGNKirfANHS 79
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 428186471 356 FQPNAeYAPCFHPRFGHIKCIRALRRMEAGEEVLVHYGY 394
Cdd:cd10519   80 SNPNC-YAKVMMVNGDHRIGIFAKRDIEAGEELFFDYGY 117
YwqK COG2849
Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];
91-208 1.12e-06

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


Pssm-ID: 442097 [Multi-domain]  Cd Length: 163  Bit Score: 48.14  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471  91 GMLEGRGTIYFPDGGWQQGIWRDGQMEGEGEYVDDEGYRIHGCWKDGLLNGPGQEVAPGGFLVYQGEFKDGVRNGMGTLn 170
Cdd:COG2849   18 LKYELGDTLLEKNGYKSGVKEKTEDSYNEGGKLIKKKLGKGLGKYKKGKLGEWKTYYPNGQLKSEGTYKNGKLEGEWKE- 96
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 428186471 171 FLDGGRVY--GSWVNGELHGQAEYWYPDGKSGLNGVWKHG 208
Cdd:COG2849   97 YYENGKLKseGNYKNGKLHGEWKEYYENGKLKEEGNYKNG 136
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
348-393 1.53e-06

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: 45.32  E-value: 1.53e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 428186471 348 LGHKANHSFQPNAEYAPCFHPRFGHIkCIRALRRMEAGEEVLVHYG 393
Cdd:cd08161   28 LARFINHSCEPNCEFEEVYVGGKPRV-FIVALRDIKAGEELTVDYG 72
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
283-393 1.83e-06

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: 46.48  E-value: 1.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471 283 AGEGLFLRTSAQEGELLSfyngiRYPHAVVDKRAWKmnGNCISLDEEFAIDVPPEHSSIDRYCASLghkANHSFQPNAEY 362
Cdd:cd10540   10 KGRGVFATRPIKKGEVIE-----EAPVIVLPKEEYQ--HLCKTVLDHYVFSWGDGCLALALGYGSM---FNHSYTPNAEY 79
                         90       100       110
                 ....*....|....*....|....*....|.
gi 428186471 363 APCFHprfGHIKCIRALRRMEAGEEVLVHYG 393
Cdd:cd10540   80 EIDFE---NQTIVFYALRDIEAGEELTINYG 107
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
284-396 2.98e-06

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: 46.48  E-value: 2.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471 284 GEGLFLRTSAQEGELLSFYNGIRYPHAVVDKRAWKMNGN------CISLDEEFAIDvPPEHSSIDRYcaslghkANHSFQ 357
Cdd:cd10531   11 GWGVKAKEDIQKGEFIIEYVGEVIDKKEFKERLDEYEELgksnfyILSLSDDVVID-ATRKGNLSRF-------INHSCE 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 428186471 358 PNAE---YAPCFHPRFGhikcIRALRRMEAGEEVLVHYGYTN 396
Cdd:cd10531   83 PNCEtqkWIVNGEYRIG----IFALRDIPAGEELTFDYNFVN 120
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
74-168 1.63e-05

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 47.14  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471  74 GMKEDEDGARYEGRFKDGMLEGRGTIYFPDGGWQQGIWRDGQMEGEGEYVDDEGYRIHGCWKDGLLNGPGQEV-APGGfl 152
Cdd:PLN03185  93 GYQRYPNGDVFEGSWIQGLQEGPGKYTWANGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMMHGFGVYTwSDGG-- 170
                         90
                 ....*....|....*.
gi 428186471 153 VYQGEFKDGVRNGMGT 168
Cdd:PLN03185 171 CYVGTWTRGLKDGKGV 186
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
80-169 1.73e-05

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 47.14  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471  80 DGARYEGRFKDGMLEGRGTIYFPDGGWQQGIWRDGQMEGEGEYVDDEGYRIHGCWKDGLLNGPGQEVAPGGFLVYQGEFK 159
Cdd:PLN03185 122 NGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTWTRGLKDGKGVFYPAGSRVPAVQEFY 201
                         90
                 ....*....|
gi 428186471 160 DGVRNGMGTL 169
Cdd:PLN03185 202 LNALRKRGVL 211
SET_Suv4-20-like cd10524
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
311-393 5.13e-05

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: 43.04  E-value: 5.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471 311 VVDKRAWKMN------GNCIS-LDEEFAIDVPPE-------HSSIDRyCAS--LGHKA--NHSFQPNAEYAPCFHPRFgh 372
Cdd:cd10524   22 IIATKPIKKGekihelCGCIAeLSEEEEALLRPGgndfsvmYSSRKK-CSQlwLGPAAfiNHDCRPNCKFVPTGKSTA-- 98
                         90       100
                 ....*....|....*....|.
gi 428186471 373 ikCIRALRRMEAGEEVLVHYG 393
Cdd:cd10524   99 --CVKVLRDIEPGEEITVYYG 117
SET_EZH2 cd19218
SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...
277-394 2.12e-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: 40.67  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471 277 VAGGNEAGEGLFLRTSAQEGELLSFYNGIRYPHAVVDKRA----WKMNGNCISLDEEFAIDVPPEHSSIdRYcaslghkA 352
Cdd:cd19218    8 LAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGkvydKYMCSFLFNLNNDFVVDATRKGNKI-RF-------A 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 428186471 353 NHSFQPNAeYAPCFHPRFGHIKCIRALRRMEAGEEVLVHYGY 394
Cdd:cd19218   80 NHSVNPNC-YAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRY 120
SET_SETD1-like cd10518
SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...
284-392 2.58e-04

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: 41.04  E-value: 2.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471 284 GEGLFLRTSAQEGELLSFYNG--IRypHAVVDKRAWKMNGNCISLDEEFAIDvppEHSSID-RYCASLGHKANHSFQPNa 360
Cdd:cd10518   25 GWGLFAKRPIAAGEMVIEYVGevIR--PIVADKREKRYDEEGGGGTYMFRID---EDLVIDaTKKGNIARFINHSCDPN- 98
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 428186471 361 eyapCF-----HPRFGHIkCIRALRRMEAGEEVLVHY 392
Cdd:cd10518   99 ----CYakiitVDGEKHI-VIFAKRDIAPGEELTYDY 130
SET_KMT5C cd19185
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 5C (KMT5C) ...
311-393 4.63e-04

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 5C (KMT5C) and similar proteins; KMT5C (also termed lysine N-methyltransferase 5C, lysine-specific methyltransferase 5C, suppressor of variegation 4-20 homolog 2, Su(var)4-20 homolog 2 or Suv4-20h2) is a histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4 (H4K20me3). It plays a central role in the establishment of constitutive heterochromatin in pericentric heterochromatin regions.


Pssm-ID: 380962  Cd Length: 142  Bit Score: 40.41  E-value: 4.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428186471 311 VVDKRAWKMNGN------CIS--LDEEFAIDVPPEHS-----SIDRYCASL--GHKA--NHSFQPNAEyapcFHPRFGHI 373
Cdd:cd19185   22 IVSTRAWKKNEKlellvgCIAelREEDEGLLRAGENDfsimySTRKRSAQLwlGPAAfiNHDCKPNCK----FVPADGNA 97
                         90       100
                 ....*....|....*....|
gi 428186471 374 KCIRALRRMEAGEEVLVHYG 393
Cdd:cd19185   98 ACVKVLRDIEPGDEVTCFYG 117
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
351-397 1.27e-03

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: 38.51  E-value: 1.27e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 428186471 351 KANHSFQPNAEYapcfHPRFGHIKCIRALRRMEAGEEVLVHYGYTNQ 397
Cdd:cd20071   58 LLNHSCDPNAVV----VFDGNGTLRVRALRDIKAGEELTISYIDPLL 100
SET_LSMT cd10527
SET domain found in Rubisco large subunit methyltransferase (LSMT) and similar proteins; ...
352-393 2.80e-03

SET domain found in Rubisco large subunit methyltransferase (LSMT) and similar proteins; Rubisco LSMT is a non-histone protein methyl transferase responsible for the trimethylation of lysine14 in the large subunit of Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase). The family also includes SET domain-containing proteins, SETD3, SETD4 and SETD6, which belong to methyltransferase class VII that represents classical non-histone SET domain methyltransferases. Members in this family contain a SET domain and a C-terminal RubisCO LSMT substrate-binding (Rubis-subs-bind) domain.


Pssm-ID: 380925 [Multi-domain]  Cd Length: 236  Bit Score: 38.97  E-value: 2.80e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 428186471 352 ANHSF-QPNAEYApcFHPRFGHIkCIRALRRMEAGEEVLVHYG 393
Cdd:cd10527  183 LNHSPdAPNVRYE--YDEDEGSF-VLVATRDIAAGEEVFISYG 222
SET_SMYD4 cd10536
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
353-400 9.74e-03

SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing protein 4 (SMYD4) and similar proteins; 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. In zebrafish, SMYD4 is ubiquitously expressed in early embryos and becomes enriched in the developing heart; mutants show a strong defect in cardiomyocyte proliferation, which lead to a severe cardiac malformation.


Pssm-ID: 380934 [Multi-domain]  Cd Length: 218  Bit Score: 37.28  E-value: 9.74e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 428186471 353 NHSFQPNAEYapCFHPRFGHIkciRALRRMEAGEEVLVHYGYT-NQMPR 400
Cdd:cd10536  155 NHSCDPNTIR--SFYGNTIVV---RATRPIKKGEEITICYGPHfSRMKR 198
 
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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