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Conserved domains on  [gi|57974582|ref|XP_566179|]
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AGAP000216-PA [Anopheles gambiae str. PEST]

Protein Classification

SET domain-containing protein( domain architecture ID 1562517)

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

CATH:  2.170.270.10
EC:  2.1.1.-
Gene Ontology:  GO:0005515|GO:0008168|GO:1904047
PubMed:  12372294|17013555|16086857

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, ...
 143-458 4.64e-19

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: 85.81  E-value: 4.64e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57974582 143 PRVANCLEMRRSPQYGRYLQTNKALKVGDVVMIDEPYVSVLEPefcyaRCDHcqrpapftlipcerctkamYCSknclrr 222
Cdd:cd10536   2 PGASSAVSLRYSEEKGRFLVATRDIKAGEVLIVEKPYASVLLP-----YSSD-------------------YRS------ 51

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57974582 223 arteyhefecalVHHLtettrdpvvllawravtraistyrynLRHLKQRrnylsrtevnplmlNWVDGQKIAFSAVYILA 302
Cdd:cd10536  52 ------------VYNL--------------------------VTHTENR--------------SPEDLFQRALTAVFLAK 79

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57974582 303 SLarapndpvearvaqisREMHCHLVSENGQTandDSGSVPYPWVGEMCYRFLKVMQCNARP-----AQLTRRDEPEGQY 377
Cdd:cd10536  80 CL----------------QLSGYFLLWEASTE---LNGEEPESILGGLLLRHLQQLQCNAHAitelqTTSSGSQVDTSKQ 140

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57974582 378 RAVPFALrcHPLISLLNHSCAPNV-KCFdlRDGRCSAVVIQPIAAGGQLFANYGYDYLQTGRDERREGLQRVFGFTCNCD 456
Cdd:cd10536 141 VRIATAI--YPTLSLLNHSCDPNTiRSF--YGNTIVVRATRPIKKGEEITICYGPHFSRMKRSERQRLLKEQYFFDCSCE 216


                ..
gi 57974582 457 AC 458
Cdd:cd10536 217 AC 218
 
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 ...
 143-458 4.64e-19

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: 85.81  E-value: 4.64e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57974582 143 PRVANCLEMRRSPQYGRYLQTNKALKVGDVVMIDEPYVSVLEPefcyaRCDHcqrpapftlipcerctkamYCSknclrr 222
Cdd:cd10536   2 PGASSAVSLRYSEEKGRFLVATRDIKAGEVLIVEKPYASVLLP-----YSSD-------------------YRS------ 51

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57974582 223 arteyhefecalVHHLtettrdpvvllawravtraistyrynLRHLKQRrnylsrtevnplmlNWVDGQKIAFSAVYILA 302
Cdd:cd10536  52 ------------VYNL--------------------------VTHTENR--------------SPEDLFQRALTAVFLAK 79

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57974582 303 SLarapndpvearvaqisREMHCHLVSENGQTandDSGSVPYPWVGEMCYRFLKVMQCNARP-----AQLTRRDEPEGQY 377
Cdd:cd10536  80 CL----------------QLSGYFLLWEASTE---LNGEEPESILGGLLLRHLQQLQCNAHAitelqTTSSGSQVDTSKQ 140

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57974582 378 RAVPFALrcHPLISLLNHSCAPNV-KCFdlRDGRCSAVVIQPIAAGGQLFANYGYDYLQTGRDERREGLQRVFGFTCNCD 456
Cdd:cd10536 141 VRIATAI--YPTLSLLNHSCDPNTiRSF--YGNTIVVRATRPIKKGEEITICYGPHFSRMKRSERQRLLKEQYFFDCSCE 216


                ..
gi 57974582 457 AC 458
Cdd:cd10536 217 AC 218
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
383-458 7.00e-08

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 51.50  E-value: 7.00e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57974582 383 ALRCHPLISLLNHSCAPNVKcFDLRDGRCSAVVIQPIAAGGQLFANYGYDYlqtgrDERReglqrvfgFTCNCDAC 458
Cdd:COG2940  70 GALGGNPARFINHSCDPNCE-ADEEDGRIFIVALRDIAAGEELTYDYGLDY-----DEEE--------YPCRCPNC 131
zf-MYND pfam01753
MYND finger;
192-232 3.22e-07

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 46.64  E-value: 3.22e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 57974582   192 CDHCQRPApFTLIPCERCTKAMYCSKNCLRRARtEYHEFEC 232
Cdd:pfam01753   1 CAVCGKEA-LKLLRCSRCKSVYYCSKECQKADW-PYHKKEC 39
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 388-433 2.84e-04

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: 40.78  E-value: 2.84e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 57974582    388 PLISLLNHSCAPNVKC-FDLRDGRCSAVV--IQPIAAGGQLFANYGYDY 433
Cdd:smart00317  73 NLARFINHSCEPNCELlFVEVNGDDRIVIfaLRDIKPGEELTIDYGSDY 121
 
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 ...
 143-458 4.64e-19

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: 85.81  E-value: 4.64e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57974582 143 PRVANCLEMRRSPQYGRYLQTNKALKVGDVVMIDEPYVSVLEPefcyaRCDHcqrpapftlipcerctkamYCSknclrr 222
Cdd:cd10536   2 PGASSAVSLRYSEEKGRFLVATRDIKAGEVLIVEKPYASVLLP-----YSSD-------------------YRS------ 51

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57974582 223 arteyhefecalVHHLtettrdpvvllawravtraistyrynLRHLKQRrnylsrtevnplmlNWVDGQKIAFSAVYILA 302
Cdd:cd10536  52 ------------VYNL--------------------------VTHTENR--------------SPEDLFQRALTAVFLAK 79

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57974582 303 SLarapndpvearvaqisREMHCHLVSENGQTandDSGSVPYPWVGEMCYRFLKVMQCNARP-----AQLTRRDEPEGQY 377
Cdd:cd10536  80 CL----------------QLSGYFLLWEASTE---LNGEEPESILGGLLLRHLQQLQCNAHAitelqTTSSGSQVDTSKQ 140

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57974582 378 RAVPFALrcHPLISLLNHSCAPNV-KCFdlRDGRCSAVVIQPIAAGGQLFANYGYDYLQTGRDERREGLQRVFGFTCNCD 456
Cdd:cd10536 141 VRIATAI--YPTLSLLNHSCDPNTiRSF--YGNTIVVRATRPIKKGEEITICYGPHFSRMKRSERQRLLKEQYFFDCSCE 216


                ..
gi 57974582 457 AC 458
Cdd:cd10536 217 AC 218
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
 388-458 1.40e-15

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: 73.18  E-value: 1.40e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57974582 388 PLISLLNHSCAPNVKCFDLRDGRCSAVVIQPIAAGGQLFANYGYDYLqtGRDERREGLQRVFGFTCNCDAC 458
Cdd:cd20071  54 PLASLLNHSCDPNAVVVFDGNGTLRVRALRDIKAGEELTISYIDPLL--PRTERRRELLEKYGFTCSCPRC 122
SET_SMYD3 cd19203
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 ...
 388-460 8.04e-11

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: 61.61  E-value: 8.04e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57974582 388 PLISLLNHSCAPNvkCFDLRDGRC-SAVVIQPIAAGGQLFANYgYDYLQTgRDERREGLQRVFGFTCNCDACEN 460
Cdd:cd19203 141 PSASLLNHSCDPN--CVIVFNGPHlLLRAIREIEVGEELTISY-IDMLMP-SEERRKQLRDQYCFECDCFRCQD 210
SET_SMYD1 cd10526
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 ...
 387-460 2.58e-08

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: 54.34  E-value: 2.58e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57974582 387 HPLISLLNHSCAPNVKCFdLRDGRCSAVVIQPIAAGGQLFANYgYDYLQTGRDeRREGLQRVFGFTCNCDACEN 460
Cdd:cd10526 140 FPNLCLVNHDCWPNCTVI-FNNGRIELRALGKISEGDELTVSY-IDFLNTSED-RKEQLKKQYYFDCTCEHCTK 210
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
383-458 7.00e-08

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 51.50  E-value: 7.00e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57974582 383 ALRCHPLISLLNHSCAPNVKcFDLRDGRCSAVVIQPIAAGGQLFANYGYDYlqtgrDERReglqrvfgFTCNCDAC 458
Cdd:COG2940  70 GALGGNPARFINHSCDPNCE-ADEEDGRIFIVALRDIAAGEELTYDYGLDY-----DEEE--------YPCRCPNC 131
zf-MYND pfam01753
MYND finger;
192-232 3.22e-07

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 46.64  E-value: 3.22e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 57974582   192 CDHCQRPApFTLIPCERCTKAMYCSKNCLRRARtEYHEFEC 232
Cdd:pfam01753   1 CAVCGKEA-LKLLRCSRCKSVYYCSKECQKADW-PYHKKEC 39
SET_SMYD1_2_3-like cd19167
SET domain (including post-SET domain) found in SET and MYND domain-containing proteins, SMYD1, ...
 388-460 2.39e-05

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: 45.49  E-value: 2.39e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57974582 388 PLISLLNHSCAPNvkCFDLRDGRCSAV-VIQPIAAGGQLFANYgYDYLQTgRDERREGLQRVFGFTCNCDACEN 460
Cdd:cd19167 136 PQAALLNHSCCPN--CIVTFNGPNIEVrAVQEIEPGEEVFHSY-IDLLYP-TEERRDQLRDQYFFLCQCADCQT 205
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 374-430 4.03e-05

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: 42.90  E-value: 4.03e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 57974582   374 EGQYRAVPFALRCHPLISLLNHSCAPNVKC-FDLRDGRCSAVV--IQPIAAGGQLFANYG 430
Cdd:pfam00856  56 DSEYCIDARALYYGNWARFINHSCDPNCEVrVVYVNGGPRIVIfaLRDIKPGEELTIDYG 115
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 382-430 1.16e-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: 1.16e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 57974582 382 FALRCHP---LISL---LNHSCAPNVKC---FDLRDGRCSAVVIQPIAAGGQLFANYG 430
Cdd:cd08161  15 FATRDIPkgeVIGLarfINHSCEPNCEFeevYVGGKPRVFIVALRDIKAGEELTVDYG 72
SET_SMYD2 cd19202
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 2 ...
 388-458 1.76e-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: 42.89  E-value: 1.76e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57974582 388 PLISLLNHSCAPNVkcFDLRDGRCSAV-VIQPIAAGGQLFANYgYDYLQTGRDeRREGLQRVFGFTCNCDAC 458
Cdd:cd19202 137 PDVALMNHSCCPNV--IVTYKGTLAEVrAVQEIKPGEEVFTSY-IDLLYPTED-RNDRLRDSYFFTCECQEC 204
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 388-433 2.84e-04

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: 40.78  E-value: 2.84e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 57974582    388 PLISLLNHSCAPNVKC-FDLRDGRCSAVV--IQPIAAGGQLFANYGYDY 433
Cdd:smart00317  73 NLARFINHSCEPNCELlFVEVNGDDRIVIfaLRDIKPGEELTIDYGSDY 121
SET_Suv4-20-like cd10524
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
 390-459 3.08e-04

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


Pssm-ID: 380922 [Multi-domain]  Cd Length: 141  Bit Score: 41.11  E-value: 3.08e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57974582 390 ISLLNHSCAPNVKCFDLRDGRCSAVVIQPIAAGGQLFANYGYDYLqtgRDERREglqrvfgftCNCDACE 459
Cdd:cd10524  77 AAFINHDCRPNCKFVPTGKSTACVKVLRDIEPGEEITVYYGDNYF---GENNEE---------CECETCE 134
SET_SMYD5 cd10521
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
 387-459 6.56e-04

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: 41.91  E-value: 6.56e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57974582 387 HPLISLLNHSCAPNVK-CFDLRDGRCSAVVIQPIAAGGQLFANY-GYDYLQTGRDERREGLQRVFGFTCNCDACE 459
Cdd:cd10521 206 YLLQSCCNHSCVPNAEiTFPENNFTLSLKALRDIQEGEEICISYlDECQRERSRHSRQKILRENYLFICNCPKCE 280
SET_LSMT cd10527
SET domain found in Rubisco large subunit methyltransferase (LSMT) and similar proteins; ...
 388-430 1.73e-03

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


Pssm-ID: 380925 [Multi-domain]  Cd Length: 236  Bit Score: 40.13  E-value: 1.73e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 57974582 388 PLISLLNHS-CAPNVKC-FDLRDGRCSAVVIQPIAAGGQLFANYG 430
Cdd:cd10527 178 PLADMLNHSpDAPNVRYeYDEDEGSFVLVATRDIAAGEEVFISYG 222
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
 394-435 4.37e-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: 37.32  E-value: 4.37e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 57974582 394 NHSCAPNVKC---FDLRDGRCSAVVIQPIAAGGQLFANYGYDYLQ 435
Cdd:cd10522  78 NHSDQPNLELivrTLKGEQHIGFVAIRDIKPGEELFISYGPKYWK 122
 
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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