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Conserved domains on  [gi|24652121|ref|NP_724802|]
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SET and MYND domain containing, class 4, member 1, isoform B [Drosophila melanogaster]

Protein Classification

SET and MYND domain-containing protein( domain architecture ID 15749148)

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) and MYND (myeloid, Nervy, and DEAF-1) domain-containing protein may function as a protein-lysine N-methyltransferase, catalyzing the S-adenosyl-L-methionine (SAM)-dependent methylation at specific lysine residues of target proteins such as histones

CATH:  2.170.270.10
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 super family cl40432
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 359-549 1.53e-14

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


The actual alignment was detected with superfamily member cd10536:

Pssm-ID: 394802 [Multi-domain]  Cd Length: 218  Bit Score: 73.49  E-value: 1.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652121 359 YLRSLRMVSQLDQAIDEELNYHILCANLLQLYLKEHTDFYDQFHSLPASIEDWQLIISALILRFAGQLLANGHvgdallg 438
Cdd:cd10536  49 YRSVYNLVTHTENRSPEDLFQRALTAVFLAKCLQLSGYFLLWEASTELNGEEPESILGGLLLRHLQQLQCNAH------- 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652121 439 vgmepkEFVMLQPELWQkprhlkrGQLHNlSHSDPI-TAINlPYLSLCNHACEPSIRTKFDGCSVVNYAAKDILEGEEIF 517
Cdd:cd10536 122 ------AITELQTTSSG-------SQVDT-SKQVRIaTAIY-PTLSLLNHSCDPNTIRSFYGNTIVVRATRPIKKGEEIT 186

                       170       180       190
                ....*....|....*....|....*....|..
gi 24652121 518 NCYTMDYRNSLKLQRSHPLKAIYKFECTCAKC 549
Cdd:cd10536 187 ICYGPHFSRMKRSERQRLLKEQYFFDCSCEAC 218
zf-MYND pfam01753
MYND finger;
258-298 2.08e-06

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 44.72  E-value: 2.08e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 24652121   258 CQQCAATLMSaPIPCPNCHQrVVYCSRKCREAHSAIHKFEC 298
Cdd:pfam01753   1 CAVCGKEALK-LLRCSRCKS-VYYCSKECQKADWPYHKKEC 39
SET super family cl40432
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 217-252 2.84e-03

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


The actual alignment was detected with superfamily member cd20071:

Pssm-ID: 394802 [Multi-domain]  Cd Length: 122  Bit Score: 38.51  E-value: 2.84e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 24652121 217 EILTDPGPRGRYMVAKEAISKGNVIFSERASCFVPL 252
Cdd:cd20071   1 EVRESEGSKGRGLVATRDIEPGELILVEKPLVSVPS 36
 
Name Accession Description Interval E-value
SET_SMYD4 cd10536
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
 359-549 1.53e-14

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: 73.49  E-value: 1.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652121 359 YLRSLRMVSQLDQAIDEELNYHILCANLLQLYLKEHTDFYDQFHSLPASIEDWQLIISALILRFAGQLLANGHvgdallg 438
Cdd:cd10536  49 YRSVYNLVTHTENRSPEDLFQRALTAVFLAKCLQLSGYFLLWEASTELNGEEPESILGGLLLRHLQQLQCNAH------- 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652121 439 vgmepkEFVMLQPELWQkprhlkrGQLHNlSHSDPI-TAINlPYLSLCNHACEPSIRTKFDGCSVVNYAAKDILEGEEIF 517
Cdd:cd10536 122 ------AITELQTTSSG-------SQVDT-SKQVRIaTAIY-PTLSLLNHSCDPNTIRSFYGNTIVVRATRPIKKGEEIT 186

                       170       180       190
                ....*....|....*....|....*....|..
gi 24652121 518 NCYTMDYRNSLKLQRSHPLKAIYKFECTCAKC 549
Cdd:cd10536 187 ICYGPHFSRMKRSERQRLLKEQYFFDCSCEAC 218
zf-MYND pfam01753
MYND finger;
258-298 2.08e-06

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 44.72  E-value: 2.08e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 24652121   258 CQQCAATLMSaPIPCPNCHQrVVYCSRKCREAHSAIHKFEC 298
Cdd:pfam01753   1 CAVCGKEALK-LLRCSRCKS-VYYCSKECQKADWPYHKKEC 39
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
476-552 9.51e-06

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 45.72  E-value: 9.51e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24652121 476 AINLPYLSLCNHACEPSIRTKFDGCSVVNYAAKDILEGEEIfncyTMDYRNSLklqrshplkAIYKFECTCAKCTRT 552
Cdd:COG2940  71 ALGGNPARFINHSCDPNCEADEEDGRIFIVALRDIAAGEEL----TYDYGLDY---------DEEEYPCRCPNCRGT 134
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 447-526 1.54e-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: 45.02  E-value: 1.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652121    447 VMLQPELWQKPRHLKRGQL--HNLSHSDPITAIN----LPYLSLCNHACEPSIRTKFDGCS----VVNYAAKDILEGEEI 516
Cdd:smart00317  34 IITSEEAEERPKAYDTDGAkaFYLFDIDSDLCIDarrkGNLARFINHSCEPNCELLFVEVNgddrIVIFALRDIKPGEEL 113

                           90
                   ....*....|
gi 24652121    517 FNCYTMDYRN 526
Cdd:smart00317 114 TIDYGSDYAN 123
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 472-520 3.94e-04

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: 40.58  E-value: 3.94e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 24652121   472 DPITAINLPYLSLCNHACEP----SIRTKFDGCSVVNYAAKDILEGEEIFNCY 520
Cdd:pfam00856  62 DARALYYGNWARFINHSCDPncevRVVYVNGGPRIVIFALRDIKPGEELTIDY 114
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
 217-252 2.84e-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: 2.84e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 24652121 217 EILTDPGPRGRYMVAKEAISKGNVIFSERASCFVPL 252
Cdd:cd20071   1 EVRESEGSKGRGLVATRDIEPGELILVEKPLVSVPS 36
 
Name Accession Description Interval E-value
SET_SMYD4 cd10536
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
 359-549 1.53e-14

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: 73.49  E-value: 1.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652121 359 YLRSLRMVSQLDQAIDEELNYHILCANLLQLYLKEHTDFYDQFHSLPASIEDWQLIISALILRFAGQLLANGHvgdallg 438
Cdd:cd10536  49 YRSVYNLVTHTENRSPEDLFQRALTAVFLAKCLQLSGYFLLWEASTELNGEEPESILGGLLLRHLQQLQCNAH------- 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652121 439 vgmepkEFVMLQPELWQkprhlkrGQLHNlSHSDPI-TAINlPYLSLCNHACEPSIRTKFDGCSVVNYAAKDILEGEEIF 517
Cdd:cd10536 122 ------AITELQTTSSG-------SQVDT-SKQVRIaTAIY-PTLSLLNHSCDPNTIRSFYGNTIVVRATRPIKKGEEIT 186

                       170       180       190
                ....*....|....*....|....*....|..
gi 24652121 518 NCYTMDYRNSLKLQRSHPLKAIYKFECTCAKC 549
Cdd:cd10536 187 ICYGPHFSRMKRSERQRLLKEQYFFDCSCEAC 218
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
 480-549 5.40e-14

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: 68.94  E-value: 5.40e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24652121 480 PYLSLCNHACEPSIRTKFDGCSVVN-YAAKDILEGEEIFNCYTMDYRNSLKLQRShpLKAIYKFECTCAKC 549
Cdd:cd20071  54 PLASLLNHSCDPNAVVVFDGNGTLRvRALRDIKAGEELTISYIDPLLPRTERRRE--LLEKYGFTCSCPRC 122
SET_SMYD5 cd10521
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
 483-549 1.56e-06

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: 50.38  E-value: 1.56e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24652121 483 SLCNHACEPSIRTKFDGcsvVNY-----AAKDILEGEEIFNCY-TMDYRNSLKLQRSHPLKAIYKFECTCAKC 549
Cdd:cd10521 210 SCCNHSCVPNAEITFPE---NNFtlslkALRDIQEGEEICISYlDECQRERSRHSRQKILRENYLFICNCPKC 279
zf-MYND pfam01753
MYND finger;
258-298 2.08e-06

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 44.72  E-value: 2.08e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 24652121   258 CQQCAATLMSaPIPCPNCHQrVVYCSRKCREAHSAIHKFEC 298
Cdd:pfam01753   1 CAVCGKEALK-LLRCSRCKS-VYYCSKECQKADWPYHKKEC 39
SET_SMYD1_2_3-like cd19167
SET domain (including post-SET domain) found in SET and MYND domain-containing proteins, SMYD1, ...
 480-550 2.32e-06

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: 48.96  E-value: 2.32e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24652121 480 PYLSLCNHACEPSIRTKFDGCSVVNYAAKDILEGEEIFNCY------TMDYRNSLKLQrshplkaiYKFECTCAKCT 550
Cdd:cd19167 136 PQAALLNHSCCPNCIVTFNGPNIEVRAVQEIEPGEEVFHSYidllypTEERRDQLRDQ--------YFFLCQCADCQ 204
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
476-552 9.51e-06

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 45.72  E-value: 9.51e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24652121 476 AINLPYLSLCNHACEPSIRTKFDGCSVVNYAAKDILEGEEIfncyTMDYRNSLklqrshplkAIYKFECTCAKCTRT 552
Cdd:COG2940  71 ALGGNPARFINHSCDPNCEADEEDGRIFIVALRDIAAGEEL----TYDYGLDY---------DEEEYPCRCPNCRGT 134
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 447-526 1.54e-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: 45.02  E-value: 1.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652121    447 VMLQPELWQKPRHLKRGQL--HNLSHSDPITAIN----LPYLSLCNHACEPSIRTKFDGCS----VVNYAAKDILEGEEI 516
Cdd:smart00317  34 IITSEEAEERPKAYDTDGAkaFYLFDIDSDLCIDarrkGNLARFINHSCEPNCELLFVEVNgddrIVIFALRDIKPGEEL 113

                           90
                   ....*....|
gi 24652121    517 FNCYTMDYRN 526
Cdd:smart00317 114 TIDYGSDYAN 123
SET_SMYD1 cd10526
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 ...
 480-551 2.90e-05

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: 45.87  E-value: 2.90e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24652121 480 PYLSLCNHACEPSIRTKFDGCSVVNYAAKDILEGEEIFNCYtMDYRNsLKLQRSHPLKAIYKFECTCAKCTR 551
Cdd:cd10526 141 PNLCLVNHDCWPNCTVIFNNGRIELRALGKISEGDELTVSY-IDFLN-TSEDRKEQLKKQYYFDCTCEHCTK 210
SET_SMYD3 cd19203
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 ...
 480-551 1.96e-04

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: 43.51  E-value: 1.96e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24652121 480 PYLSLCNHACEPSIRTKFDGCSVVNYAAKDILEGEEIFNCY------TMDYRNSLKLQrshplkaiYKFECTCAKCTR 551
Cdd:cd19203 141 PSASLLNHSCDPNCVIVFNGPHLLLRAIREIEVGEELTISYidmlmpSEERRKQLRDQ--------YCFECDCFRCQD 210
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 472-520 3.94e-04

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: 40.58  E-value: 3.94e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 24652121   472 DPITAINLPYLSLCNHACEP----SIRTKFDGCSVVNYAAKDILEGEEIFNCY 520
Cdd:pfam00856  62 DARALYYGNWARFINHSCDPncevRVVYVNGGPRIVIFALRDIKPGEELTIDY 114
SET_SMYD2 cd19202
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 2 ...
 480-550 5.93e-04

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: 41.73  E-value: 5.93e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24652121 480 PYLSLCNHACEPSIRTKFDGCSVVNYAAKDILEGEEIFNCYT-MDYRNSLKLQRshpLKAIYKFECTCAKCT 550
Cdd:cd19202 137 PDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYIdLLYPTEDRNDR---LRDSYFFTCECQECT 205
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
 217-252 2.84e-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: 2.84e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 24652121 217 EILTDPGPRGRYMVAKEAISKGNVIFSERASCFVPL 252
Cdd:cd20071   1 EVRESEGSKGRGLVATRDIEPGELILVEKPLVSVPS 36
 
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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