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Conserved domains on  [gi|188035871|ref|NP_064582|]
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N-lysine methyltransferase SMYD2 [Homo sapiens]

Protein Classification

N-lysine methyltransferase SMYD2( domain architecture ID 14443462)

N-lysine methyltransferase SMYD2 acts as a protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1; specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo

CATH:  2.170.270.10
Gene Ontology:  GO:0032259|GO:0042054|GO:0046872|GO:1904047|GO:0000993|GO:0002039|GO:0016279
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_SMYD2 cd19202
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 2 ...
 7-269 5.42e-146

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: 413.84  E-value: 5.42e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871   7 GGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTvnergnhceycftrkeglskcgrckqafycnvecqkedwpmh 86
Cdd:cd19202    1 GGLERFCSPGKGRGLRALRPFQVGDLLFSCPAYAYVLT------------------------------------------ 38

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871  87 klecspmvvfgenwnPSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFYSKHLGF 166
Cdd:cd19202   39 ---------------PSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFYSKHLEF 103

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871 167 PDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYIDLLYP 246
Cdd:cd19202  104 PDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYIDLLYP 183

                        250       260
                 ....*....|....*....|...
gi 188035871 247 TEDRNDRLRDSYFFTCECQECTT 269
Cdd:cd19202  184 TEDRNDRLRDSYFFTCECQECTT 206
zf-MYND pfam01753
MYND finger;
52-90 9.41e-15

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 67.83  E-value: 9.41e-15
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 188035871   52 CEYCFTRKEGLSKCGRCKQAFYCNVECQKEDWPMHKLEC 90
Cdd:pfam01753   1 CAVCGKEALKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
 
Name Accession Description Interval E-value
SET_SMYD2 cd19202
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 2 ...
 7-269 5.42e-146

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: 413.84  E-value: 5.42e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871   7 GGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTvnergnhceycftrkeglskcgrckqafycnvecqkedwpmh 86
Cdd:cd19202    1 GGLERFCSPGKGRGLRALRPFQVGDLLFSCPAYAYVLT------------------------------------------ 38

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871  87 klecspmvvfgenwnPSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFYSKHLGF 166
Cdd:cd19202   39 ---------------PSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFYSKHLEF 103

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871 167 PDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYIDLLYP 246
Cdd:cd19202  104 PDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYIDLLYP 183

                        250       260
                 ....*....|....*....|...
gi 188035871 247 TEDRNDRLRDSYFFTCECQECTT 269
Cdd:cd19202  184 TEDRNDRLRDSYFFTCECQECTT 206
zf-MYND pfam01753
MYND finger;
52-90 9.41e-15

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 67.83  E-value: 9.41e-15
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 188035871   52 CEYCFTRKEGLSKCGRCKQAFYCNVECQKEDWPMHKLEC 90
Cdd:pfam01753   1 CAVCGKEALKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 204-240 8.95e-07

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: 47.52  E-value: 8.95e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 188035871  204 LMNHSCCPNVIVTY----KGTLAEVRAVQEIKPGEEVFTSY 240
Cdd:pfam00856  74 FINHSCDPNCEVRVvyvnGGPRIVIFALRDIKPGEELTIDY 114
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 195-247 9.08e-05

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: 41.94  E-value: 9.08e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 188035871   195 GSAIFPDVALMNHSCCPNVIVTY----KGTLAEVRAVQEIKPGEEVFTSYIDLLYPT 247
Cdd:smart00317  68 ARRKGNLARFINHSCEPNCELLFvevnGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
204-270 3.47e-04

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 40.33  E-value: 3.47e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 188035871 204 LMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFtsyIDllYPTEDRNDRlrdsyfFTCECQECTTK 270
Cdd:COG2940   79 FINHSCDPNCEADEEDGRIFIVALRDIAAGEELT---YD--YGLDYDEEE------YPCRCPNCRGT 134
 
Name Accession Description Interval E-value
SET_SMYD2 cd19202
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 2 ...
 7-269 5.42e-146

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: 413.84  E-value: 5.42e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871   7 GGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTvnergnhceycftrkeglskcgrckqafycnvecqkedwpmh 86
Cdd:cd19202    1 GGLERFCSPGKGRGLRALRPFQVGDLLFSCPAYAYVLT------------------------------------------ 38

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871  87 klecspmvvfgenwnPSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFYSKHLGF 166
Cdd:cd19202   39 ---------------PSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFYSKHLEF 103

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871 167 PDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYIDLLYP 246
Cdd:cd19202  104 PDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYIDLLYP 183

                        250       260
                 ....*....|....*....|...
gi 188035871 247 TEDRNDRLRDSYFFTCECQECTT 269
Cdd:cd19202  184 TEDRNDRLRDSYFFTCECQECTT 206
SET_SMYD1_2_3-like cd19167
SET domain (including post-SET domain) found in SET and MYND domain-containing proteins, SMYD1, ...
 7-269 4.80e-117

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: 340.17  E-value: 4.80e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871   7 GGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTvnergnhceycftrkeglskcgrckqafycnvecqkedwpmh 86
Cdd:cd19167    1 GQVERFCSPGKGRGLRALKPFEPGDLIFSERPYAYVLT------------------------------------------ 38

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871  87 klecspmvvfgenwnPSETVRLTARILAKQKIHPERTpSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFYSKHLGF 166
Cdd:cd19167   39 ---------------PPEHVRLTGRILYKQHIRKTRT-SGKLLSVYDLESHVEKLDEEKKDGLRSDVATLHQFMSKDLQL 102

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871 167 PDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYIDLLYP 246
Cdd:cd19167  103 PDAAYLVELFGKVNCNGFTISDEELQHVGVGIYPQAALLNHSCCPNCIVTFNGPNIEVRAVQEIEPGEEVFHSYIDLLYP 182

                        250       260
                 ....*....|....*....|...
gi 188035871 247 TEDRNDRLRDSYFFTCECQECTT 269
Cdd:cd19167  183 TEERRDQLRDQYFFLCQCADCQT 205
SET_SMYD3 cd19203
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 ...
 7-269 3.61e-53

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: 176.79  E-value: 3.61e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871   7 GGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTvnergnhceycftrkeglskcgrckqafycnvecqkEDWPMH 86
Cdd:cd19203    1 SKVEKFETAEKGRGLRAVTPLKPGELVLKADPFAYTVC------------------------------------NPPDSV 44

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871  87 KLECspmvvfgenwnpsetvrltaRILAKQKiHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHF----YSK 162
Cdd:cd19203   45 RLEG--------------------RIIFKLL-DKAPSESEKLYSFYDLQSNINKLSEDRKEGLRQLAMVLQHYlreeIQD 103

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871 163 HLGFPDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYID 242
Cdd:cd19203  104 ASQLPPAFDIFELFAKVTCNSFTICDAEMQEVGVGLYPSASLLNHSCDPNCVIVFNGPHLLLRAIREIEVGEELTISYID 183

                        250       260
                 ....*....|....*....|....*..
gi 188035871 243 LLYPTEDRNDRLRDSYFFTCECQECTT 269
Cdd:cd19203  184 MLMPSEERRKQLRDQYCFECDCFRCQD 210
SET_SMYD1 cd10526
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 ...
 8-268 2.60e-49

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: 166.82  E-value: 2.60e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871   8 GLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVltvnergnhceycftrkeglskcgrckqafycnvecqkedwpmhk 87
Cdd:cd10526    2 GVEVFTSEGKGRGLKATKEFWAGDVIFAEPPYAAV--------------------------------------------- 36

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871  88 lecspmvVFGENwnPSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFYSKHlGFP 167
Cdd:cd10526   37 -------VFGKA--PNENIRLAARILWRIEREGGGLKEGELVSIEDLQDHLEDFSEEEKKDLREDVHSFLDYWPYQ-SQQ 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871 168 DNDSLVV-LFAQVNCNGFTIEDEE-LSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYIDLLY 245
Cdd:cd10526  107 FSMEYIShIFGVINCNGFTLSDQRgLQAVGVGIFPNLCLVNHDCWPNCTVIFNNGRIELRALGKISEGDELTVSYIDFLN 186

                        250       260
                 ....*....|....*....|...
gi 188035871 246 PTEDRNDRLRDSYFFTCECQECT 268
Cdd:cd10526  187 TSEDRKEQLKKQYYFDCTCEHCT 209
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
 176-267 1.08e-28

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: 109.00  E-value: 1.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871 176 FAQVNCNGFTIEDEElSHLGSAIFPDVALMNHSCCPNVIVTYKGTL-AEVRAVQEIKPGEEVFTSYIDLLYPTEDRNDRL 254
Cdd:cd20071   31 LVSVPSNSFSLTDGL-NEIGVGLFPLASLLNHSCDPNAVVVFDGNGtLRVRALRDIKAGEELTISYIDPLLPRTERRREL 109

                         90
                 ....*....|...
gi 188035871 255 RDSYFFTCECQEC 267
Cdd:cd20071  110 LEKYGFTCSCPRC 122
SET_SMYD4 cd10536
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
 172-267 8.84e-25

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: 101.22  E-value: 8.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871 172 LVVLFAQVNCNGFTIED--EELSH----------LGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTS 239
Cdd:cd10536  109 LLRHLQQLQCNAHAITElqTTSSGsqvdtskqvrIATAIYPTLSLLNHSCDPNTIRSFYGNTIVVRATRPIKKGEEITIC 188

                         90       100       110
                 ....*....|....*....|....*....|
gi 188035871 240 Y--IDLLYPTEDRNDRLRDSYFFTCECQEC 267
Cdd:cd10536  189 YgpHFSRMKRSERQRLLKEQYFFDCSCEAC 218
zf-MYND pfam01753
MYND finger;
52-90 9.41e-15

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 67.83  E-value: 9.41e-15
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 188035871   52 CEYCFTRKEGLSKCGRCKQAFYCNVECQKEDWPMHKLEC 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 ...
 11-267 1.29e-12

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: 67.72  E-value: 1.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871  11 RFCSPGKGRGLRALQPFQVGDLLFScpayayvltvnergnhcEYCFTrkeglskcgrCKQaFYCNvecqkedwpmhklEC 90
Cdd:cd10521    5 RFIDAAKGRGLFATRDFKKGDIIFE-----------------EKPLV----------CAQ-FLWN-------------EL 43

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871  91 SPMVVFGENWN----PSET--VRLTARILA--KQKIHPER-----------TPSE------KLLAvKEFESHLDKLDNEK 145
Cdd:cd10521   44 HPLNKLQEAWRnmhyPPETasIMLIARMIAtvKQAKDKDEwlklfsqfcsaTANEeehiahKLLG-KQFQGQLELLRQLF 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871 146 KDLIQSDiaALHHFYSKHlGFPDndslvvLFAQVNCNGFTI--------------------EDEELSHL----------- 194
Cdd:cd10521  123 TEALYEE--RLSQWFTPE-GFRS------LFALVGTNGQGIgtsslsvwvhncdalelpeqEREELDAFidqlyvdieke 193

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871 195 --------GSAIFPDVALMNHSCCPNVIVTYKG---TLAeVRAVQEIKPGEEVFTSYIDLLYPTEDRNDR---LRDSYFF 260
Cdd:cd10521  194 sgeflnceGSGLYLLQSCCNHSCVPNAEITFPEnnfTLS-LKALRDIQEGEEICISYLDECQRERSRHSRqkiLRENYLF 272


                 ....*..
gi 188035871 261 TCECQEC 267
Cdd:cd10521  273 ICNCPKC 279
SET_Suv4-20-like cd10524
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
 194-267 1.51e-08

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: 53.05  E-value: 1.51e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 188035871 194 LGSAifpdvALMNHSCCPNVI-VTYKGTLAEVRAVQEIKPGEEVFTSYidllyptedrndrlRDSYFFT----CECQEC 267
Cdd:cd10524   74 LGPA-----AFINHDCRPNCKfVPTGKSTACVKVLRDIEPGEEITVYY--------------GDNYFGEnneeCECETC 133
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 204-240 8.95e-07

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: 47.52  E-value: 8.95e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 188035871  204 LMNHSCCPNVIVTY----KGTLAEVRAVQEIKPGEEVFTSY 240
Cdd:pfam00856  74 FINHSCDPNCEVRVvyvnGGPRIVIFALRDIKPGEELTIDY 114
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 205-240 3.40e-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: 44.55  E-value: 3.40e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 188035871 205 MNHSCCPNVIVTY----KGTLAEVRAVQEIKPGEEVFTSY 240
Cdd:cd08161   32 INHSCEPNCEFEEvyvgGKPRVFIVALRDIKAGEELTVDY 71
SET_SETD4 cd19177
SET domain found in SET domain-containing protein 4 (SETD4) and similar proteins; SETD4 is a ...
 13-240 3.74e-06

SET domain found in SET domain-containing protein 4 (SETD4) and similar proteins; SETD4 is a cytosolic and nuclear functional lysine methyltransferase that plays a crucial role in breast carcinogenesis. However, its specific substrates and modification sites remain to be disclosed.


Pssm-ID: 380954 [Multi-domain]  Cd Length: 245  Bit Score: 48.06  E-value: 3.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871  13 CSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTVNERgNHCEYCFTRKEGLSKCGRCKQAFYCNVECQKED---WP----- 84
Cdd:cd19177    9 EFPDTGRGLVATKDIKPGELIISIPESLLINTTTVL-SSLLGSLIKRVKPKLSSLQLLALFLALEKRRGEnsfWApylds 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871  85 MHKLECS-PMvvfgeNWNPSETVRLTARILakqkihpertpsekllavKEFESHLDKLdnekKDLIQSDIAALHHFYSKH 163
Cdd:cd19177   88 LPKSFDThPL-----YWSLEELSLLPPSLL------------------EAVRKLLDKQ----KKRFESDWEIISSVLKSL 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871 164 LGFPDNDS----------LVV----LFAQVNCNGFTIEDEElsHLGSAIFPDvaLMNHSCCPNVIVTYKGTLA--EVRAV 227
Cdd:cd19177  141 PSLFDSEIftleefrwawLCVntrcVYYKLPLSDYLSSSED--NIALAPFLD--LLNHSPDVNVKAGFNKSGKcyEIRTG 216

                        250
                 ....*....|...
gi 188035871 228 QEIKPGEEVFTSY 240
Cdd:cd19177  217 TDYKKGEEVFISY 229
SET_LSMT cd10527
SET domain found in Rubisco large subunit methyltransferase (LSMT) and similar proteins; ...
 14-240 4.47e-05

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: 44.75  E-value: 4.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871  14 SPGKGRGLRALQPFQVGDLLFSCPAyAYVLTVnergnhceycftrkEGLSKCGRCKQAFYCNVECQKEDWPM-------- 85
Cdd:cd10527    7 SPDGGRGLFATRDIAAGEVLLSVPR-SLLLTV--------------ETARESPLGGAALALLELDPELSWDValalflly 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871  86 --HKLECSPmvvfgenWNPsetvrlTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLiQSDIAALHHFYSKH 163
Cdd:cd10527   72 erARGPDSF-------WAP------YLDSLPRPFEDTPLFWSEEELDALQGTPLLEAAAAQRRRL-REEYEALVEALPEA 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035871 164 LGFPDNDSLVV-LFAQVNCN----GFTIEDEELSHlGSAIFP--DvaLMNHS-CCPNVIVTYKGTLA--EVRAVQEIKPG 233
Cdd:cd10527  138 LPAEPGEAFTLeEFLWALALvlsrAFSLPVPDGGG-GLALVPlaD--MLNHSpDAPNVRYEYDEDEGsfVLVATRDIAAG 214


                 ....*..
gi 188035871 234 EEVFTSY 240
Cdd:cd10527  215 EEVFISY 221
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 195-247 9.08e-05

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: 41.94  E-value: 9.08e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 188035871   195 GSAIFPDVALMNHSCCPNVIVTY----KGTLAEVRAVQEIKPGEEVFTSYIDLLYPT 247
Cdd:smart00317  68 ARRKGNLARFINHSCEPNCELLFvevnGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
204-270 3.47e-04

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 40.33  E-value: 3.47e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 188035871 204 LMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFtsyIDllYPTEDRNDRlrdsyfFTCECQECTTK 270
Cdd:COG2940   79 FINHSCDPNCEADEEDGRIFIVALRDIAAGEELT---YD--YGLDYDEEE------YPCRCPNCRGT 134
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
 206-240 5.94e-03

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: 36.55  E-value: 5.94e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 188035871 206 NHSCCPN---VIVTYKGTL-AEVRAVQEIKPGEEVFTSY 240
Cdd:cd10522   78 NHSDQPNlelIVRTLKGEQhIGFVAIRDIKPGEELFISY 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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