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Conserved domains on  [gi|157819445|ref|NP_001100065|]
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histone-lysine N-methyltransferase SMYD1 [Rattus norvegicus]

Protein Classification

histone-lysine N-methyltransferase SMYD1( domain architecture ID 14410430)

histone-lysine N-methyltransferase SMYD1 methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation

CATH:  2.170.270.10
EC:  2.1.1.354
Gene Ontology:  GO:0032259|GO:0042054|GO:0046872|GO:1904047
PubMed:  16086857|25580534|25125178|34555372|24710145
SCOP:  4000530

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SET_SMYD1 cd10526
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 ...
 7-281 9.46e-140

SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 (SMYD1) and similar proteins; 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. SMYD1 plays a critical role in cardiomyocyte differentiation, cardiac morphogenesis and myofibril organization, as well as in the regulation of endothelial cells (ECs). It is expressed in vascular endothelial cells, it has beenshown that knockdown of SMYD1 in endothelial cells impairs EC migration and tube formation.


:

Pssm-ID: 380924 [Multi-domain]  Cd Length: 210  Bit Score: 400.25  E-value: 9.46e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445   7 ENVEVFTSEGKGRGLKATKEFWAADVIFAERAYSAVVFdslinfvchtcfkrqerlhrcgqckfahycdrtcqkdawlnh 86
Cdd:cd10526    1 EGVEVFTSEGKGRGLKATKEFWAGDVIFAEPPYAAVVF------------------------------------------ 38

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445  87 knecsaikryGKVPNENIRLAARIMWRVEREGTGLTEGCLVSVDDLQNHVEHFGEEEQKELRVDVDTFLQYWPPQSQQFS 166
Cdd:cd10526   39 ----------GKAPNENIRLAARILWRIEREGGGLKEGELVSIEDLQDHLEDFSEEEKKDLREDVHSFLDYWPYQSQQFS 108

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445 167 MQYISHIFGVINCNGFTLSDQRGLQAVGVGIFPNLGLVNHDCWPNCTVIFNNGnheavksmfhtqmRIELRALGKISEGE 246
Cdd:cd10526  109 MEYISHIFGVINCNGFTLSDQRGLQAVGVGIFPNLCLVNHDCWPNCTVIFNNG-------------RIELRALGKISEGD 175

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 157819445 247 ELTVSYIDFLHLSEERRQQLKKQYYFDCSCEHCQK 281
Cdd:cd10526  176 ELTVSYIDFLNTSEDRKEQLKKQYYFDCTCEHCTK 210
zf-MYND pfam01753
MYND finger;
52-90 1.98e-13

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 64.36  E-value: 1.98e-13
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 157819445   52 CHTCFKRQERLHRCGQCKFAHYCDRTCQKDAWLNHKNEC 90
Cdd:pfam01753   1 CAVCGKEALKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
 
Name Accession Description Interval E-value
SET_SMYD1 cd10526
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 ...
 7-281 9.46e-140

SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 (SMYD1) and similar proteins; 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. SMYD1 plays a critical role in cardiomyocyte differentiation, cardiac morphogenesis and myofibril organization, as well as in the regulation of endothelial cells (ECs). It is expressed in vascular endothelial cells, it has beenshown that knockdown of SMYD1 in endothelial cells impairs EC migration and tube formation.


Pssm-ID: 380924 [Multi-domain]  Cd Length: 210  Bit Score: 400.25  E-value: 9.46e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445   7 ENVEVFTSEGKGRGLKATKEFWAADVIFAERAYSAVVFdslinfvchtcfkrqerlhrcgqckfahycdrtcqkdawlnh 86
Cdd:cd10526    1 EGVEVFTSEGKGRGLKATKEFWAGDVIFAEPPYAAVVF------------------------------------------ 38

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445  87 knecsaikryGKVPNENIRLAARIMWRVEREGTGLTEGCLVSVDDLQNHVEHFGEEEQKELRVDVDTFLQYWPPQSQQFS 166
Cdd:cd10526   39 ----------GKAPNENIRLAARILWRIEREGGGLKEGELVSIEDLQDHLEDFSEEEKKDLREDVHSFLDYWPYQSQQFS 108

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445 167 MQYISHIFGVINCNGFTLSDQRGLQAVGVGIFPNLGLVNHDCWPNCTVIFNNGnheavksmfhtqmRIELRALGKISEGE 246
Cdd:cd10526  109 MEYISHIFGVINCNGFTLSDQRGLQAVGVGIFPNLCLVNHDCWPNCTVIFNNG-------------RIELRALGKISEGD 175

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 157819445 247 ELTVSYIDFLHLSEERRQQLKKQYYFDCSCEHCQK 281
Cdd:cd10526  176 ELTVSYIDFLNTSEDRKEQLKKQYYFDCTCEHCTK 210
zf-MYND pfam01753
MYND finger;
52-90 1.98e-13

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 64.36  E-value: 1.98e-13
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 157819445   52 CHTCFKRQERLHRCGQCKFAHYCDRTCQKDAWLNHKNEC 90
Cdd:pfam01753   1 CAVCGKEALKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 194-257 8.83e-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: 56.57  E-value: 8.83e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157819445   194 GVGIFPNLGLVNHDCWPNCTVIFNNGNHEavksmfhtqMRIELRALGKISEGEELTVSYIDFLH 257
Cdd:smart00317  68 ARRKGNLARFINHSCEPNCELLFVEVNGD---------DRIVIFALRDIKPGEELTIDYGSDYA 122
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 203-252 6.43e-08

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: 50.98  E-value: 6.43e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 157819445  203 LVNHDCWPNCTVIFNNGNHEavksmfhtqMRIELRALGKISEGEELTVSY 252
Cdd:pfam00856  74 FINHSCDPNCEVRVVYVNGG---------PRIVIFALRDIKPGEELTIDY 114
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
182-279 6.52e-07

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 48.42  E-value: 6.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445 182 FTLSDQRGLQAVGVGifpNLG-LVNHDCWPNCTVIFNNGnheavksmfhtqmRIELRALGKISEGEELTVSYIDFLHlsE 260
Cdd:COG2940   60 FELDDDGVIDGALGG---NPArFINHSCDPNCEADEEDG-------------RIFIVALRDIAAGEELTYDYGLDYD--E 121

                         90
                 ....*....|....*....
gi 157819445 261 ERrqqlkkqyyFDCSCEHC 279
Cdd:COG2940  122 EE---------YPCRCPNC 131
 
Name Accession Description Interval E-value
SET_SMYD1 cd10526
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 ...
 7-281 9.46e-140

SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 (SMYD1) and similar proteins; 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. SMYD1 plays a critical role in cardiomyocyte differentiation, cardiac morphogenesis and myofibril organization, as well as in the regulation of endothelial cells (ECs). It is expressed in vascular endothelial cells, it has beenshown that knockdown of SMYD1 in endothelial cells impairs EC migration and tube formation.


Pssm-ID: 380924 [Multi-domain]  Cd Length: 210  Bit Score: 400.25  E-value: 9.46e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445   7 ENVEVFTSEGKGRGLKATKEFWAADVIFAERAYSAVVFdslinfvchtcfkrqerlhrcgqckfahycdrtcqkdawlnh 86
Cdd:cd10526    1 EGVEVFTSEGKGRGLKATKEFWAGDVIFAEPPYAAVVF------------------------------------------ 38

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445  87 knecsaikryGKVPNENIRLAARIMWRVEREGTGLTEGCLVSVDDLQNHVEHFGEEEQKELRVDVDTFLQYWPPQSQQFS 166
Cdd:cd10526   39 ----------GKAPNENIRLAARILWRIEREGGGLKEGELVSIEDLQDHLEDFSEEEKKDLREDVHSFLDYWPYQSQQFS 108

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445 167 MQYISHIFGVINCNGFTLSDQRGLQAVGVGIFPNLGLVNHDCWPNCTVIFNNGnheavksmfhtqmRIELRALGKISEGE 246
Cdd:cd10526  109 MEYISHIFGVINCNGFTLSDQRGLQAVGVGIFPNLCLVNHDCWPNCTVIFNNG-------------RIELRALGKISEGD 175

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 157819445 247 ELTVSYIDFLHLSEERRQQLKKQYYFDCSCEHCQK 281
Cdd:cd10526  176 ELTVSYIDFLNTSEDRKEQLKKQYYFDCTCEHCTK 210
SET_SMYD1_2_3-like cd19167
SET domain (including post-SET domain) found in SET and MYND domain-containing proteins, SMYD1, ...
 7-281 1.71e-103

SET domain (including post-SET domain) found in SET and MYND domain-containing proteins, SMYD1, SMYD2, SMYD3 and similar proteins; The family includes SET and MYND domain-containing proteins, SMYD1, SMYD2 and SMYD3. 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.


Pssm-ID: 380944 [Multi-domain]  Cd Length: 205  Bit Score: 307.82  E-value: 1.71e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445   7 ENVEVFTSEGKGRGLKATKEFWAADVIFAERAYSAVVFdslinfvchtcfkrqerlhrcgqckfahycdrtcqkdawlnh 86
Cdd:cd19167    1 GQVERFCSPGKGRGLRALKPFEPGDLIFSERPYAYVLT------------------------------------------ 38

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445  87 knecsaikrygkvPNENIRLAARIMWRVEREGTGlTEGCLVSVDDLQNHVEHFGEEEQKELRVDVDTFLQYWPPQSQQFS 166
Cdd:cd19167   39 -------------PPEHVRLTGRILYKQHIRKTR-TSGKLLSVYDLESHVEKLDEEKKDGLRSDVATLHQFMSKDLQLPD 104

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445 167 MQYISHIFGVINCNGFTLSDQrGLQAVGVGIFPNLGLVNHDCWPNCTVIFNNGNheavksmfhtqmrIELRALGKISEGE 246
Cdd:cd19167  105 AAYLVELFGKVNCNGFTISDE-ELQHVGVGIYPQAALLNHSCCPNCIVTFNGPN-------------IEVRAVQEIEPGE 170

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 157819445 247 ELTVSYIDFLHLSEERRQQLKKQYYFDCSCEHCQK 281
Cdd:cd19167  171 EVFHSYIDLLYPTEERRDQLRDQYFFLCQCADCQT 205
SET_SMYD3 cd19203
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 ...
 8-280 4.38e-48

SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 (SMYD3) and similar proteins; 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. It is overexpressed in colorectal, breast, prostate, and hepatocellular tumors, and has been implicated as an oncogene in human malignancies. Methylation of MEKK2 by SMYD3 is important for regulation of the MEK/ERK pathway, suggesting the possibility of selectively targeting SMYD3 in RAS-driven cancers.


Pssm-ID: 380980 [Multi-domain]  Cd Length: 210  Bit Score: 164.85  E-value: 4.38e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445   8 NVEVFTSEGKGRGLKATKEFWAADVIFAERAYSAVVfdslinfvchtcfkrqerlhrcgqCKfahycdrtcqkdAWLNHK 87
Cdd:cd19203    2 KVEKFETAEKGRGLRAVTPLKPGELVLKADPFAYTV------------------------CN------------PPDSVR 45

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445  88 NECSAIKRYGKVPNEnirlaarimwrveregtgLTEGcLVSVDDLQNHVEHFGEEEQKELRVDVDTFLQYWPPQSQQFSm 167
Cdd:cd19203   46 LEGRIIFKLLDKAPS------------------ESEK-LYSFYDLQSNINKLSEDRKEGLRQLAMVLQHYLREEIQDAS- 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445 168 QYIS-----HIFGVINCNGFTLSDQRgLQAVGVGIFPNLGLVNHDCWPNCTVIFNNgnheavksmfhtqMRIELRALGKI 242
Cdd:cd19203  106 QLPPafdifELFAKVTCNSFTICDAE-MQEVGVGLYPSASLLNHSCDPNCVIVFNG-------------PHLLLRAIREI 171

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 157819445 243 SEGEELTVSYIDFLHLSEERRQQLKKQYYFDCSCEHCQ 280
Cdd:cd19203  172 EVGEELTISYIDMLMPSEERRKQLRDQYCFECDCFRCQ 209
SET_SMYD2 cd19202
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 2 ...
 7-279 9.27e-30

SET domain (including post-SET domain) found in SET and MYND domain-containing protein 2 (SMYD2) and similar proteins; SMYD2 (also termed HSKM-B, 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). It plays a role in myofilament organization in both skeletal and cardiac muscles via Hsp90 methylation. SMYD2 overexpression is associated with tumor cell proliferation and a worse outcome in human papillomavirus-unrelated nonmultiple head and neck carcinomas. It regulates leukemia cell growth such that diminished SMYD2 expression upregulates SET7/9, thereby possibly shifting leukemia cells from growth to quiescence state associated with resistance to DNA damage associated with Acute Myeloid Leukemia (AML).


Pssm-ID: 380979 [Multi-domain]  Cd Length: 206  Bit Score: 115.31  E-value: 9.27e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445   7 ENVEVFTSEGKGRGLKATKEFWAADVIFAERAYSAVVfdslinfvchtcfkrqerlhrcgqckfahycdrtcqkdawlnh 86
Cdd:cd19202    1 GGLERFCSPGKGRGLRALRPFQVGDLLFSCPAYAYVL------------------------------------------- 37

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445  87 knecsaikrygkVPNENIRLAARIMWRVEREGTGLTEGCLVSVDDLQNHVEHFGEEEQKELRVDVDTFLQYWPPQSQQFS 166
Cdd:cd19202   38 ------------TPSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFYSKHLEFPD 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445 167 MQYISHIFGVINCNGFTLSDQRgLQAVGVGIFPNLGLVNHDCWPNCTVIFNNGNheavksmfhtqmrIELRALGKISEGE 246
Cdd:cd19202  106 NDSLVVLFAQVNCNGFTIEDEE-LSHLGSAIFPDVALMNHSCCPNVIVTYKGTL-------------AEVRAVQEIKPGE 171

                        250       260       270
                 ....*....|....*....|....*....|...
gi 157819445 247 ELTVSYIDFLHLSEERRQQLKKQYYFDCSCEHC 279
Cdd:cd19202  172 EVFTSYIDLLYPTEDRNDRLRDSYFFTCECQEC 204
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
 180-279 1.15e-27

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: 107.08  E-value: 1.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445 180 NGFTLSDQRGlqAVGVGIFPNLGLVNHDCWPNCTVIFNNGNheavksmfhtqmRIELRALGKISEGEELTVSYIDFLHLS 259
Cdd:cd20071   37 NSFSLTDGLN--EIGVGLFPLASLLNHSCDPNAVVVFDGNG------------TLRVRALRDIKAGEELTISYIDPLLPR 102

                         90       100
                 ....*....|....*....|
gi 157819445 260 EERRQQLKKQYYFDCSCEHC 279
Cdd:cd20071  103 TERRRELLEKYGFTCSCPRC 122
SET_SMYD4 cd10536
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
 193-279 2.87e-20

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: 89.28  E-value: 2.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445 193 VGVGIFPNLGLVNHDCWPNCTVIFNNGNheavksmfhtqmrIELRALGKISEGEELTVSY-IDFLHLS-EERRQQLKKQY 270
Cdd:cd10536  143 IATAIYPTLSLLNHSCDPNTIRSFYGNT-------------IVVRATRPIKKGEEITICYgPHFSRMKrSERQRLLKEQY 209


                 ....*....
gi 157819445 271 YFDCSCEHC 279
Cdd:cd10536  210 FFDCSCEAC 218
zf-MYND pfam01753
MYND finger;
52-90 1.98e-13

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 64.36  E-value: 1.98e-13
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 157819445   52 CHTCFKRQERLHRCGQCKFAHYCDRTCQKDAWLNHKNEC 90
Cdd:pfam01753   1 CAVCGKEALKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
SET_SMYD5 cd10521
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
 8-280 5.52e-11

SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing protein 5 (SMYD5) and similar proteins; SMYD5 (also termed protein NN8-4AG, or retinoic acid-induced protein 15) functions as histone lysine methyltransferase that mediates H4K20me3 at heterochromatin regions. It plays an important role in chromosome integrity by regulating heterochromatin and repressing endogenous repetitive DNA elements during differentiation. In zebrafish embryogenesis, it plays pivotal roles in both primitive and definitive hematopoiesis.


Pssm-ID: 380919 [Multi-domain]  Cd Length: 282  Bit Score: 63.10  E-value: 5.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445   8 NVEV-FTSEGKGRGLKATKEFWAADVIFAERAYSAVVFdsLINfVCHTCFKRQErlhrcgqckfahycdrtcqkdAWLN- 85
Cdd:cd10521    1 HVEVrFIDAAKGRGLFATRDFKKGDIIFEEKPLVCAQF--LWN-ELHPLNKLQE---------------------AWRNm 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445  86 HknecsaikrYgkvPNE--NIRLAARIMWRV------EREGTGLTEGCLVSVDDlQNHVEH--FGEEEQKELRVDVDTFL 155
Cdd:cd10521   57 H---------Y---PPEtaSIMLIARMIATVkqakdkDEWLKLFSQFCSATANE-EEHIAHklLGKQFQGQLELLRQLFT 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445 156 Q--YWPPQSQQFSMQYISHIFGVI-----------------NCNGFTLSDQRG---------------------LQAVGV 195
Cdd:cd10521  124 EalYEERLSQWFTPEGFRSLFALVgtngqgigtsslsvwvhNCDALELPEQEReeldafidqlyvdiekesgefLNCEGS 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445 196 GIFPNLGLVNHDCWPNCTVIFNNGNHeavksmfhtqmRIELRALGKISEGEELTVSYID--FLHLSEERRQQ-LKKQYYF 272
Cdd:cd10521  204 GLYLLQSCCNHSCVPNAEITFPENNF-----------TLSLKALRDIQEGEEICISYLDecQRERSRHSRQKiLRENYLF 272


                 ....*...
gi 157819445 273 DCSCEHCQ 280
Cdd:cd10521  273 ICNCPKCE 280
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 194-257 8.83e-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: 56.57  E-value: 8.83e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157819445   194 GVGIFPNLGLVNHDCWPNCTVIFNNGNHEavksmfhtqMRIELRALGKISEGEELTVSYIDFLH 257
Cdd:smart00317  68 ARRKGNLARFINHSCEPNCELLFVEVNGD---------DRIVIFALRDIKPGEELTIDYGSDYA 122
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 203-252 6.43e-08

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: 50.98  E-value: 6.43e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 157819445  203 LVNHDCWPNCTVIFNNGNHEavksmfhtqMRIELRALGKISEGEELTVSY 252
Cdd:pfam00856  74 FINHSCDPNCEVRVVYVNGG---------PRIVIFALRDIKPGEELTIDY 114
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
182-279 6.52e-07

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 48.42  E-value: 6.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445 182 FTLSDQRGLQAVGVGifpNLG-LVNHDCWPNCTVIFNNGnheavksmfhtqmRIELRALGKISEGEELTVSYIDFLHlsE 260
Cdd:COG2940   60 FELDDDGVIDGALGG---NPArFINHSCDPNCEADEEDG-------------RIFIVALRDIAAGEELTYDYGLDYD--E 121

                         90
                 ....*....|....*....
gi 157819445 261 ERrqqlkkqyyFDCSCEHC 279
Cdd:COG2940  122 EE---------YPCRCPNC 131
SET_Suv4-20-like cd10524
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
 203-281 4.83e-06

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: 46.12  E-value: 4.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445 203 LVNHDCWPNCtvIFNNgnheavksmfHTQMRIELRALGKISEGEELTVSYidflhlSEErrqqlkkqyYF-----DCSCE 277
Cdd:cd10524   79 FINHDCRPNC--KFVP----------TGKSTACVKVLRDIEPGEEITVYY------GDN---------YFgenneECECE 131


                 ....
gi 157819445 278 HCQK 281
Cdd:cd10524  132 TCER 135
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
 203-281 5.47e-05

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: 43.05  E-value: 5.47e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157819445 203 LVNHDCWPNCtvifnngnhEAVKSMFHTQMRIELRALGKISEGEELTVSYiDFLHLSEERRQQLKkqyyfdCSCEHCQK 281
Cdd:cd19174   75 FVNHSCDPNC---------EMQKWSVNGVYRIGLFALKDIPAGEELTYDY-NFHSFNVEKQQPCK------CGSPNCRG 137
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 182-252 1.20e-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: 40.31  E-value: 1.20e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157819445 182 FTLSD-QRGlQAVGVGIFpnlglVNHDCWPNCtvifnngnhEAVKSMFHTQMRIELRALGKISEGEELTVSY 252
Cdd:cd08161   15 FATRDiPKG-EVIGLARF-----INHSCEPNC---------EFEEVYVGGKPRVFIVALRDIKAGEELTVDY 71
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
 159-252 7.15e-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: 39.16  E-value: 7.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819445 159 PPQSQQFSMQYishifGVINCNGFTLSDQRGLQAVGVGifpnlGLVNHDCWPNCTVIFNNGNHeavksmfhtqmRIELRA 238
Cdd:cd10540   34 LPKEEYQHLCK-----TVLDHYVFSWGDGCLALALGYG-----SMFNHSYTPNAEYEIDFENQ-----------TIVFYA 92

                         90
                 ....*....|....
gi 157819445 239 LGKISEGEELTVSY 252
Cdd:cd10540   93 LRDIEAGEELTINY 106
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
 204-252 3.58e-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: 37.62  E-value: 3.58e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 157819445 204 VNHDCWPNCtvifnngnhEAVKSMFHTQMRIELRALGKISEGEELTVSY 252
Cdd:cd10531   77 INHSCEPNC---------ETQKWIVNGEYRIGIFALRDIPAGEELTFDY 116
 
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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