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Conserved domains on  [gi|2015520361|ref|XP_029830896|]
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SET and MYND domain-containing protein 4-like [Ixodes scapularis]

Protein Classification

Graphical summary

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List of domain hits

 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 ...
 238-564 2.20e-84

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: 266.86  E-value: 2.20e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 238 VPSCSMAVDMLYSTEKGRFLVANRDLQPGDAIFVERPYASVLLPghtktncqhchkrllnavpcaqcnqvrYCSfacakd 317
Cdd:cd10536     1 IPGASSAVSLRYSEEKGRFLVATRDIKAGEVLIVEKPYASVLLP---------------------------YSS------ 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 318 swnsyhrwecgnlnllysvgiahlavrvllvtglsgladfcrhlaegkvdvdkngGYGSVHELVTHSEKMHVEDLLQYSL 397
Cdd:cd10536    48 -------------------------------------------------------DYRSVYNLVTHTENRSPEDLFQRAL 72

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 398 TAALLSMLLDHVLFFNVDEASwkmselsfgsrngssyrlASTDVAALKTVVGGLLLRHIQQLVCNAHAITSLESKTSQED 477
Cdd:cd10536    73 TAVFLAKCLQLSGYFLLWEAS------------------TELNGEEPESILGGLLLRHLQQLQCNAHAITELQTTSSGSQ 134

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 478 dvVMTTEQVRIATAIYPSASLMNHSCDPNIFSSFrCGSTLVVRAIRRIQEGEEVLNCYGPHHRRMSFAERQQLLQEQYFF 557
Cdd:cd10536   135 --VDTSKQVRIATAIYPTLSLLNHSCDPNTIRSF-YGNTIVVRATRPIKKGEEITICYGPHFSRMKRSERQRLLKEQYFF 211


                  ....*..
gi 2015520361 558 VCSCTAC 564
Cdd:cd10536   212 DCSCEAC 218
PLN03088 super family cl33632
SGT1, suppressor of G2 allele of SKP1; Provisional
 69-231 6.07e-07

SGT1, suppressor of G2 allele of SKP1; Provisional


The actual alignment was detected with superfamily member PLN03088:

Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 52.48  E-value: 6.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361  69 ASELRSEGNLCFNRKQYAKAAELYTQSVLSApfPDTPDAdghseemslgFANRSAAFFHAGKYKQALCDVRYAFELGYPV 148
Cdd:PLN03088    2 AKDLEDKAKEAFVDDDFALAVDLYTQAIDLD--PNNAEL----------YADRAQANIKLGNFTEAVADANKAIELDPSL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 149 HlryKLYLRKGQCYLRLGKPREAlenfdlankslrRAALEG-----------RKLAQQCKE--IDTFKALCSQDCAPTPT 215
Cdd:PLN03088   70 A---KAYLRKGTACMKLEEYQTA------------KAALEKgaslapgdsrfTKLIKECDEkiAEEEKDLVQPVPSDLPS 134

                         170
                  ....*....|....*.
gi 2015520361 216 SEEEDPDDESQVPDVA 231
Cdd:PLN03088  135 SVTAPPVEEADATPVV 150
 
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 ...
 238-564 2.20e-84

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: 266.86  E-value: 2.20e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 238 VPSCSMAVDMLYSTEKGRFLVANRDLQPGDAIFVERPYASVLLPghtktncqhchkrllnavpcaqcnqvrYCSfacakd 317
Cdd:cd10536     1 IPGASSAVSLRYSEEKGRFLVATRDIKAGEVLIVEKPYASVLLP---------------------------YSS------ 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 318 swnsyhrwecgnlnllysvgiahlavrvllvtglsgladfcrhlaegkvdvdkngGYGSVHELVTHSEKMHVEDLLQYSL 397
Cdd:cd10536    48 -------------------------------------------------------DYRSVYNLVTHTENRSPEDLFQRAL 72

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 398 TAALLSMLLDHVLFFNVDEASwkmselsfgsrngssyrlASTDVAALKTVVGGLLLRHIQQLVCNAHAITSLESKTSQED 477
Cdd:cd10536    73 TAVFLAKCLQLSGYFLLWEAS------------------TELNGEEPESILGGLLLRHLQQLQCNAHAITELQTTSSGSQ 134

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 478 dvVMTTEQVRIATAIYPSASLMNHSCDPNIFSSFrCGSTLVVRAIRRIQEGEEVLNCYGPHHRRMSFAERQQLLQEQYFF 557
Cdd:cd10536   135 --VDTSKQVRIATAIYPTLSLLNHSCDPNTIRSF-YGNTIVVRATRPIKKGEEITICYGPHFSRMKRSERQRLLKEQYFF 211


                  ....*..
gi 2015520361 558 VCSCTAC 564
Cdd:cd10536   212 DCSCEAC 218
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 496-536 1.62e-10

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: 59.07  E-value: 1.62e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2015520361 496 ASLMNHSCDPN---IFSSFRCGSTLVVRAIRRIQEGEEVLNCYG 536
Cdd:pfam00856  72 ARFINHSCDPNcevRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 489-537 5.58e-09

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: 54.65  E-value: 5.58e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2015520361  489 ATAIYPSASLMNHSCDPNIFSSFRCGST---LVVRAIRRIQEGEEVLNCYGP 537
Cdd:smart00317  68 ARRKGNLARFINHSCEPNCELLFVEVNGddrIVIFALRDIKPGEELTIDYGS 119
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 69-231 6.07e-07

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 52.48  E-value: 6.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361  69 ASELRSEGNLCFNRKQYAKAAELYTQSVLSApfPDTPDAdghseemslgFANRSAAFFHAGKYKQALCDVRYAFELGYPV 148
Cdd:PLN03088    2 AKDLEDKAKEAFVDDDFALAVDLYTQAIDLD--PNNAEL----------YADRAQANIKLGNFTEAVADANKAIELDPSL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 149 HlryKLYLRKGQCYLRLGKPREAlenfdlankslrRAALEG-----------RKLAQQCKE--IDTFKALCSQDCAPTPT 215
Cdd:PLN03088   70 A---KAYLRKGTACMKLEEYQTA------------KAALEKgaslapgdsrfTKLIKECDEkiAEEEKDLVQPVPSDLPS 134

                         170
                  ....*....|....*.
gi 2015520361 216 SEEEDPDDESQVPDVA 231
Cdd:PLN03088  135 SVTAPPVEEADATPVV 150
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
67-178 6.75e-07

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 51.07  E-value: 6.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361  67 EKASELRSEGNLCFNRKQYAKAAELYTQSVlsAPFPDTPDAdghseemslgFANRSAAFFHAGKYKQALCDVRYAFELGy 146
Cdd:COG4785    71 DLAQLYYERGVAYDSLGDYDLAIADFDQAL--ELDPDLAEA----------YNNRGLAYLLLGDYDAALEDFDRALELD- 137

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2015520361 147 PVHLRYklYLRKGQCYLRLGKPREALENFDLA 178
Cdd:COG4785   138 PDYAYA--YLNRGIALYYLGRYELAIADLEKA 167
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
496-564 4.53e-06

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 46.88  E-value: 4.53e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 496 ASLMNHSCDPNIFSSFRCGsTLVVRAIRRIQEGEEvLNC-YGphhrrMSFAERQqllqeqyfFVCSCTAC 564
Cdd:COG2940    77 ARFINHSCDPNCEADEEDG-RIFIVALRDIAAGEE-LTYdYG-----LDYDEEE--------YPCRCPNC 131
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 59-182 1.50e-05

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 48.44  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361  59 SSKHRKfwEKASELRSEGNLCFNRKQYAKAAELYTQSVLSAPFPdtpdadghseemsLGFANRSAAFFHAGKYKQALCDV 138
Cdd:TIGR00990 119 SEEERK--KYAAKLKEKGNKAYRNKDFNKAIKLYSKAIECKPDP-------------VYYSNRAACHNALGDWEKVVEDT 183

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2015520361 139 RYAFELGyPVHLryKLYLRKGQCYLRLGKPREALenFDLANKSL 182
Cdd:TIGR00990 184 TAALELD-PDYS--KALNRRANAYDGLGKYADAL--LDLTASCI 222
 
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 ...
 238-564 2.20e-84

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: 266.86  E-value: 2.20e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 238 VPSCSMAVDMLYSTEKGRFLVANRDLQPGDAIFVERPYASVLLPghtktncqhchkrllnavpcaqcnqvrYCSfacakd 317
Cdd:cd10536     1 IPGASSAVSLRYSEEKGRFLVATRDIKAGEVLIVEKPYASVLLP---------------------------YSS------ 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 318 swnsyhrwecgnlnllysvgiahlavrvllvtglsgladfcrhlaegkvdvdkngGYGSVHELVTHSEKMHVEDLLQYSL 397
Cdd:cd10536    48 -------------------------------------------------------DYRSVYNLVTHTENRSPEDLFQRAL 72

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 398 TAALLSMLLDHVLFFNVDEASwkmselsfgsrngssyrlASTDVAALKTVVGGLLLRHIQQLVCNAHAITSLESKTSQED 477
Cdd:cd10536    73 TAVFLAKCLQLSGYFLLWEAS------------------TELNGEEPESILGGLLLRHLQQLQCNAHAITELQTTSSGSQ 134

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 478 dvVMTTEQVRIATAIYPSASLMNHSCDPNIFSSFrCGSTLVVRAIRRIQEGEEVLNCYGPHHRRMSFAERQQLLQEQYFF 557
Cdd:cd10536   135 --VDTSKQVRIATAIYPTLSLLNHSCDPNTIRSF-YGNTIVVRATRPIKKGEEITICYGPHFSRMKRSERQRLLKEQYFF 211


                  ....*..
gi 2015520361 558 VCSCTAC 564
Cdd:cd10536   212 DCSCEAC 218
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
 481-564 2.20e-23

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: 95.91  E-value: 2.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 481 MTTEQVRIATAIYPSASLMNHSCDPNIFSSFRCGSTLVVRAIRRIQEGEEVLNCYGPHHrrMSFAERQQLLQEQYFFVCS 560
Cdd:cd20071    41 LTDGLNEIGVGLFPLASLLNHSCDPNAVVVFDGNGTLRVRALRDIKAGEELTISYIDPL--LPRTERRRELLEKYGFTCS 118


                  ....
gi 2015520361 561 CTAC 564
Cdd:cd20071   119 CPRC 122
SET_SMYD1_2_3-like cd19167
SET domain (including post-SET domain) found in SET and MYND domain-containing proteins, SMYD1, ...
 245-564 1.28e-20

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: 90.56  E-value: 1.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 245 VDMLYSTEKGRFLVANRDLQPGDAIFVERPYASVLLPGHTktncqhchkrllnavpcaqcnqVRycsfacakdswnsyhr 324
Cdd:cd19167     3 VERFCSPGKGRGLRALKPFEPGDLIFSERPYAYVLTPPEH----------------------VR---------------- 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 325 wecgnlnllysvgiahLAVRVLLvtglsgladfcRHLAEGKvdvDKNGGYGSVHELVTHSEKMHVE--DLLQySLTAALL 402
Cdd:cd19167    45 ----------------LTGRILY-----------KQHIRKT---RTSGKLLSVYDLESHVEKLDEEkkDGLR-SDVATLH 93

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 403 SMLLDHVLFFNVDEaswkMSELsFGsrngssyrlastdvaalktvvgglllrhiqQLVCNAHAITSLESKTsqeddvvmt 482
Cdd:cd19167    94 QFMSKDLQLPDAAY----LVEL-FG------------------------------KVNCNGFTISDEELQH--------- 129

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 483 teqvrIATAIYPSASLMNHSCDPNIFSSFRcGSTLVVRAIRRIQEGEEVLNCYGPhhRRMSFAERQQLLQEQYFFVCSCT 562
Cdd:cd19167   130 -----VGVGIYPQAALLNHSCCPNCIVTFN-GPNIEVRAVQEIEPGEEVFHSYID--LLYPTEERRDQLRDQYFFLCQCA 201


                  ..
gi 2015520361 563 AC 564
Cdd:cd19167   202 DC 203
SET_SMYD3 cd19203
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 ...
 461-565 1.86e-19

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: 87.42  E-value: 1.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 461 CNAHAITSLESKTsqeddvvmtteqvrIATAIYPSASLMNHSCDPNIFSSFRcGSTLVVRAIRRIQEGEEVLNCYgpHHR 540
Cdd:cd19203   122 CNSFTICDAEMQE--------------VGVGLYPSASLLNHSCDPNCVIVFN-GPHLLLRAIREIEVGEELTISY--IDM 184

                          90       100
                  ....*....|....*....|....*
gi 2015520361 541 RMSFAERQQLLQEQYFFVCSCTACS 565
Cdd:cd19203   185 LMPSEERRKQLRDQYCFECDCFRCQ 209
SET_SMYD5 cd10521
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
 491-566 4.95e-13

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: 70.41  E-value: 4.95e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2015520361 491 AIYPSASLMNHSCDPNIFSSF-RCGSTLVVRAIRRIQEGEEVLNCY-GPHHRRMSFAERQQLLQEQYFFVCSCTACSS 566
Cdd:cd10521   204 GLYLLQSCCNHSCVPNAEITFpENNFTLSLKALRDIQEGEEICISYlDECQRERSRHSRQKILRENYLFICNCPKCEA 281
SET_SMYD1 cd10526
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 ...
 245-566 6.29e-13

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: 68.60  E-value: 6.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 245 VDMLYSTEKGRFLVANRDLQPGDAIFVERPYASVLLPGhtktncqhchkrllnavpcAQCNQVRycsfacakdswnsyhr 324
Cdd:cd10526     3 VEVFTSEGKGRGLKATKEFWAGDVIFAEPPYAAVVFGK-------------------APNENIR---------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 325 wecgnlnllysvgiahLAVRVLLvtglsgladfcRHLAEGkvDVDKNGGYGSVHELVTHSEKMHVEDllQYSLTAALLSm 404
Cdd:cd10526    48 ----------------LAARILW-----------RIEREG--GGLKEGELVSIEDLQDHLEDFSEEE--KKDLREDVHS- 95

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 405 LLDhvlFFNVDEASWKMSELSfgsrngssyrlastdvaalktvvgglllrHIQQLV-CNAHAITSLESKTSqeddvvmtt 483
Cdd:cd10526    96 FLD---YWPYQSQQFSMEYIS-----------------------------HIFGVInCNGFTLSDQRGLQA--------- 134

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 484 eqvrIATAIYPSASLMNHSCDPNIFSSFrCGSTLVVRAIRRIQEGEEVLNCYgphhrrMSF----AERQQLLQEQYFFVC 559
Cdd:cd10526   135 ----VGVGIFPNLCLVNHDCWPNCTVIF-NNGRIELRALGKISEGDELTVSY------IDFlntsEDRKEQLKKQYYFDC 203


                  ....*..
gi 2015520361 560 SCTACSS 566
Cdd:cd10526   204 TCEHCTK 210
SET_SMYD2 cd19202
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 2 ...
 484-566 3.63e-11

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: 63.30  E-value: 3.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 484 EQVRIATAIYPSASLMNHSCDPNIFSSFRcGSTLVVRAIRRIQEGEEVLNCYgpHHRRMSFAERQQLLQEQYFFVCSCTA 563
Cdd:cd19202   127 ELSHLGSAIFPDVALMNHSCCPNVIVTYK-GTLAEVRAVQEIKPGEEVFTSY--IDLLYPTEDRNDRLRDSYFFTCECQE 203


                  ...
gi 2015520361 564 CSS 566
Cdd:cd19202   204 CTT 206
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 496-536 1.62e-10

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: 59.07  E-value: 1.62e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2015520361 496 ASLMNHSCDPN---IFSSFRCGSTLVVRAIRRIQEGEEVLNCYG 536
Cdd:pfam00856  72 ARFINHSCDPNcevRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 489-537 5.58e-09

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: 54.65  E-value: 5.58e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2015520361  489 ATAIYPSASLMNHSCDPNIFSSFRCGST---LVVRAIRRIQEGEEVLNCYGP 537
Cdd:smart00317  68 ARRKGNLARFINHSCEPNCELLFVEVNGddrIVIFALRDIKPGEELTIDYGS 119
zf-MYND pfam01753
MYND finger;
288-327 4.79e-08

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 49.34  E-value: 4.79e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2015520361 288 CQHCHKRLLNAVPCAQCNQVRYCSFACAKDSWnSYHRWEC 327
Cdd:pfam01753   1 CAVCGKEALKLLRCSRCKSVYYCSKECQKADW-PYHKKEC 39
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 69-231 6.07e-07

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 52.48  E-value: 6.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361  69 ASELRSEGNLCFNRKQYAKAAELYTQSVLSApfPDTPDAdghseemslgFANRSAAFFHAGKYKQALCDVRYAFELGYPV 148
Cdd:PLN03088    2 AKDLEDKAKEAFVDDDFALAVDLYTQAIDLD--PNNAEL----------YADRAQANIKLGNFTEAVADANKAIELDPSL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 149 HlryKLYLRKGQCYLRLGKPREAlenfdlankslrRAALEG-----------RKLAQQCKE--IDTFKALCSQDCAPTPT 215
Cdd:PLN03088   70 A---KAYLRKGTACMKLEEYQTA------------KAALEKgaslapgdsrfTKLIKECDEkiAEEEKDLVQPVPSDLPS 134

                         170
                  ....*....|....*.
gi 2015520361 216 SEEEDPDDESQVPDVA 231
Cdd:PLN03088  135 SVTAPPVEEADATPVV 150
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
67-178 6.75e-07

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 51.07  E-value: 6.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361  67 EKASELRSEGNLCFNRKQYAKAAELYTQSVlsAPFPDTPDAdghseemslgFANRSAAFFHAGKYKQALCDVRYAFELGy 146
Cdd:COG4785    71 DLAQLYYERGVAYDSLGDYDLAIADFDQAL--ELDPDLAEA----------YNNRGLAYLLLGDYDAALEDFDRALELD- 137

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2015520361 147 PVHLRYklYLRKGQCYLRLGKPREALENFDLA 178
Cdd:COG4785   138 PDYAYA--YLNRGIALYYLGRYELAIADLEKA 167
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
496-564 4.53e-06

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 46.88  E-value: 4.53e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 496 ASLMNHSCDPNIFSSFRCGsTLVVRAIRRIQEGEEvLNC-YGphhrrMSFAERQqllqeqyfFVCSCTAC 564
Cdd:COG2940    77 ARFINHSCDPNCEADEEDG-RIFIVALRDIAAGEE-LTYdYG-----LDYDEEE--------YPCRCPNC 131
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 482-536 5.57e-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: 5.57e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2015520361 482 TTEQVRIATAIYPsASLMNHSCDPN-IFSSFRCGST--LVVRAIRRIQEGEEVLNCYG 536
Cdd:cd08161    16 ATRDIPKGEVIGL-ARFINHSCEPNcEFEEVYVGGKprVFIVALRDIKAGEELTVDYG 72
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 59-182 1.50e-05

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 48.44  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361  59 SSKHRKfwEKASELRSEGNLCFNRKQYAKAAELYTQSVLSAPFPdtpdadghseemsLGFANRSAAFFHAGKYKQALCDV 138
Cdd:TIGR00990 119 SEEERK--KYAAKLKEKGNKAYRNKDFNKAIKLYSKAIECKPDP-------------VYYSNRAACHNALGDWEKVVEDT 183

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2015520361 139 RYAFELGyPVHLryKLYLRKGQCYLRLGKPREALenFDLANKSL 182
Cdd:TIGR00990 184 TAALELD-PDYS--KALNRRANAYDGLGKYADAL--LDLTASCI 222
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
 497-539 3.32e-05

SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces pombe Set7 is a novel histone-lysine N-methyltransferase. The family also includes a viral histone H3 lysine 27 methyltransferase from Paramecium bursaria Chlorella virus 1 (PBCV-1).


Pssm-ID: 380938  Cd Length: 112  Bit Score: 43.78  E-value: 3.32e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2015520361 497 SLMNHSCDPNIfsSFRC---GSTLVVRAIRRIQEGEEVLNCYGPHH 539
Cdd:cd10540    67 SMFNHSYTPNA--EYEIdfeNQTIVFYALRDIEAGEELTINYGDDL 110
SET_Suv4-20-like cd10524
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
 496-538 3.90e-05

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


Pssm-ID: 380922 [Multi-domain]  Cd Length: 141  Bit Score: 44.19  E-value: 3.90e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2015520361 496 ASLMNHSCDPN-IFSSfRCGSTLVVRAIRRIQEGEEVLNCYGPH 538
Cdd:cd10524    77 AAFINHDCRPNcKFVP-TGKSTACVKVLRDIEPGEEITVYYGDN 119
SET_LSMT cd10527
SET domain found in Rubisco large subunit methyltransferase (LSMT) and similar proteins; ...
 498-538 4.22e-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: 45.52  E-value: 4.22e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2015520361 498 LMNHSCD-PNI-FSSFRCGSTLVVRAIRRIQEGEEVLNCYGPH 538
Cdd:cd10527   182 MLNHSPDaPNVrYEYDEDEGSFVLVATRDIAAGEEVFISYGPK 224
SET_KMT5C cd19185
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 5C (KMT5C) ...
 472-570 7.35e-05

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


Pssm-ID: 380962  Cd Length: 142  Bit Score: 43.49  E-value: 7.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 472 KTSQEDDVVMTTEQVRIATAIYPSASLMNHSCDPNIFSSFRCGSTLVVRAIRRIQEGEEVLNCYGPHHrrmsFAERQQLl 551
Cdd:cd19185    53 RAGENDFSIMYSTRKRSAQLWLGPAAFINHDCKPNCKFVPADGNAACVKVLRDIEPGDEVTCFYGEGF----FGEKNEH- 127

                          90       100
                  ....*....|....*....|
gi 2015520361 552 qeqyffvCSCTACS-SGEDA 570
Cdd:cd19185   128 -------CECHTCErKGEGA 140
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 67-178 8.34e-05

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 43.26  E-value: 8.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361  67 EKASELRSEGNLCFNRKQYAKAAELYTQsvLSAPFPDTPDAdghseemslgFANRSAAFFHAGKYKQALCDVRYAFELgY 146
Cdd:COG4783     2 ACAEALYALAQALLLAGDYDEAEALLEK--ALELDPDNPEA----------FALLGEILLQLGDLDEAIVLLHEALEL-D 68

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2015520361 147 PVHLRYKLYLrkGQCYLRLGKPREALENFDLA 178
Cdd:COG4783    69 PDEPEARLNL--GLALLKAGDYDEALALLEKA 98
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
76-178 2.00e-04

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 43.84  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361  76 GNLCFNRKQYAKAAELYTQSVlsAPFPDTPDAdghseemslgFANRSAAFFHAGKYKQALCDVRYAFELGyPVHlrYKLY 155
Cdd:COG0457    15 GLAYRRLGRYEEAIEDYEKAL--ELDPDDAEA----------LYNLGLAYLRLGRYEEALADYEQALELD-PDD--AEAL 79

                          90       100
                  ....*....|....*....|...
gi 2015520361 156 LRKGQCYLRLGKPREALENFDLA 178
Cdd:COG0457    80 NNLGLALQALGRYEEALEDYDKA 102
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
64-178 2.13e-04

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 43.84  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361  64 KFWEKASELRSE--------GNLCFNRKQYAKAAELYTQSVLSAPfpDTPDAdghseemslgFANRSAAFFHAGKYKQAL 135
Cdd:COG0457    29 EDYEKALELDPDdaealynlGLAYLRLGRYEEALADYEQALELDP--DDAEA----------LNNLGLALQALGRYEEAL 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2015520361 136 CDVRYAFELGyPVHlrYKLYLRKGQCYLRLGKPREALENFDLA 178
Cdd:COG0457    97 EDYDKALELD-PDD--AEALYNLGLALLELGRYDEAIEAYERA 136
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
76-195 2.48e-04

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 43.46  E-value: 2.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361  76 GNLCFNRKQYAKAAELYTQSVLSAPfpDTPDAdghseemslgFANRSAAFFHAGKYKQALCDVRYAFELGyPVHlrYKLY 155
Cdd:COG0457    83 GLALQALGRYEEALEDYDKALELDP--DDAEA----------LYNLGLALLELGRYDEAIEAYERALELD-PDD--ADAL 147

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2015520361 156 LRKGQCYLRLGKPREALENFDLANKSLRRAALEGRKLAQQ 195
Cdd:COG0457   148 YNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAA 187
SET_SETD6 cd19178
SET domain found in SET domain-containing protein 6 (SETD6) and similar proteins; SETD6 is a ...
 387-547 1.20e-03

SET domain found in SET domain-containing protein 6 (SETD6) and similar proteins; SETD6 is a lysine N-methyltransferase that monomethylates 'Lys-310' of the RELA subunit of NF-kappa-B complex, leading to down-regulate NF-kappa-B transcription factor activity. It also monomethylates 'Lys-8' of H2AZ (H2AZK8me1).


Pssm-ID: 380955 [Multi-domain]  Cd Length: 250  Bit Score: 41.52  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 387 MHvEDLLQYSLTAALLSML-----LDHVLFFNVDEaswkMSELSFGSRngsSYRLASTDVAALK----TVVGGLLLRHIQ 457
Cdd:cd19178    74 MY-EYTNPSSRWRPYLSLLpdfseLHHPMFWDEEE----REELLGGTG---IAEAVDRDLKEIDeeynSIVLPFIKKHPE 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361 458 QLVCNAH------AITSL-------ESKTSQEDDvvMTTEQVRIATAIYPSASLMNHSCDPNIFSSFrCGSTLVVRAIRR 524
Cdd:cd19178   146 LFSPEKHslelykRMVAFvmaysftEPDEDEDDD--DEDEDDDSPPMMVPMADMLNHIANNNARLEF-DPDCLRMIATRD 222

                         170       180
                  ....*....|....*....|....*...
gi 2015520361 525 IQEGEEVLNCYGPHH-----RRMSFAER 547
Cdd:cd19178   223 IKKGEEIFNTYGELAnwellHMYGFVEP 250
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 76-178 1.53e-03

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 39.40  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361  76 GNLCFNRKQYAKAAELYTQSVlsAPFPDTPDAdghseemslgFANRSAAFFHAGKYKQALCDVRYAFELgYPVHLRYklY 155
Cdd:COG4783    45 GEILLQLGDLDEAIVLLHEAL--ELDPDEPEA----------RLNLGLALLKAGDYDEALALLEKALKL-DPEHPEA--Y 109

                          90       100
                  ....*....|....*....|...
gi 2015520361 156 LRKGQCYLRLGKPREALENFDLA 178
Cdd:COG4783   110 LRLARAYRALGRPDEAIAALEKA 132
SET_SETD4 cd19177
SET domain found in SET domain-containing protein 4 (SETD4) and similar proteins; SETD4 is a ...
 498-559 1.74e-03

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: 40.75  E-value: 1.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2015520361 498 LMNHSCDPN---IFSSFrcGSTLVVRAIRRIQEGEEVLNCYGPHHRRMSFAErqqllqeqYFFVC 559
Cdd:cd19177   191 LLNHSPDVNvkaGFNKS--GKCYEIRTGTDYKKGEEVFISYGPHSNDFLLLE--------YGFVL 245
SET_RBCMT cd19179
SET domain found in chloroplastic ribulose-1,5 bisphosphate carboxylase/oxygenase large ...
 491-537 2.39e-03

SET domain found in chloroplastic ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase (RBCMT) and similar proteins; RBCMT (EC 2.1.1.127; also termed [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase, RuBisCO LSMT, RuBisCO methyltransferase, or rbcMT) methylates 'Lys-14' of the large subunit of RuBisCO.


Pssm-ID: 380956  Cd Length: 237  Bit Score: 40.37  E-value: 2.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2015520361 491 AIYPSASLMNHSCDPNIFSSFR----CGSTLVVRAIRRIQEGEEVLNCYGP 537
Cdd:cd19179   174 ALVPWADLLNHSSGVSSDASYDvrggSSKAVVLTADRNYSAGEQVFISYGP 224
SET_SETD7 cd10530
SET domain found in SET domain-containing protein 7 (SETD7) and similar proteins; SETD7 (EC 2. ...
 468-536 3.03e-03

SET domain found in SET domain-containing protein 7 (SETD7) and similar proteins; SETD7 (EC 2.1.1.43; also termed histone H3-K4 methyltransferase SETD7, H3-K4-HMTase SETD7, lysine N-methyltransferase 7 (KMT7) or SET7/9) is a histone-lysine N-methyltransferase that specifically monomethylates 'Lys-4' of histone H3. It plays a central role in the transcriptional activation of genes such as collagenase or insulin. Set7/9 also methylates non-histone proteins, including estrogen receptor alpha (ERa), suggesting it has a role in diverse biological processes. ERa methylation by Set7/9 stabilizes ERa and activates its transcriptional activities, which are involved in the carcinogenesis of breast cancer. In a high-throughput screen, treatment of human breast cancer cells (MCF7 cells) with cyproheptadine, a Set7/9 inhibitor, decreased the expression and transcriptional activity of ERa, thereby inhibiting estrogen-dependent cell growth.


Pssm-ID: 380928  Cd Length: 130  Bit Score: 38.43  E-value: 3.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2015520361 468 SLESKT-SQEDDVVMTTEQVRIATAIYpSASL---MNHSCDPN-IFSSF---RCGSTLVVRAIRRIQEGEEVLNCYG 536
Cdd:cd10530    54 SLNGNTiSLDEETVIDVPEPYNSVSKY-CASLghkANHSFTPNcIYDPFvhpRFGPIKCIRTLRAVEAGEELTVAYG 129
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 80-176 4.46e-03

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 37.66  E-value: 4.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361  80 FNRKQYAKAAELYTQsvLSAPFPDTPDADghseEMSLGFANrsaAFFHAGKYKQALcdvrYAFEL---GYPVHLRY-KLY 155
Cdd:COG1729     4 LKAGDYDEAIAAFKA--FLKRYPNSPLAP----DALYWLGE---AYYALGDYDEAA----EAFEKllkRYPDSPKApDAL 70

                          90       100
                  ....*....|....*....|.
gi 2015520361 156 LRKGQCYLRLGKPREALENFD 176
Cdd:COG1729    71 LKLGLSYLELGDYDKARATLE 91
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 58-175 7.22e-03

Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443281 [Multi-domain]  Cd Length: 254  Bit Score: 39.09  E-value: 7.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015520361  58 CSSKHRKFWEK-ASELRSEGNLCFNRKQYAKAAELYTQsvLSAPFPDTPdadgHSEEMSLGFANrsaAFFHAGKYKQALc 136
Cdd:COG4105    20 CSSFKKALKSWdAEELYEEAKEALEKGDYEKAIKLFEE--LEPRYPGSP----YAEQAQLMLAY---AYYKQGDYEEAI- 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2015520361 137 dvrYAFE---LGYPVH--LRYKLYLRkGQCYLRLGKP--------REALENF 175
Cdd:COG4105    90 ---AAADrfiKLYPNSpnADYAYYLR-GLSYYEQSPDsdrdqtstRKAIEAF 137
 
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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