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Conserved domains on  [gi|156717252|ref|NP_001096168|]
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histone-lysine N-methyltransferase EHMT1 [Xenopus tropicalis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
970-1200 0e+00

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine N-methyltransferase 1 (EHMT1) and similar proteins; EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, or lysine N-methyltransferase 1D (KMT1D)) acts as a histone-lysine N-methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin.


:

Pssm-ID: 380933 [Multi-domain]  Cd Length: 231  Bit Score: 535.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  970 VNYKYVSQNCVTSPLNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKNGRLLPEFNMLEPPLIFECNHACSCWRNC 1049
Cdd:cd10535     1 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1050 RNRVVQNGLKIRLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVREDDTYLFDLDNKDREVYCIDARFYGNI 1129
Cdd:cd10535    81 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156717252 1130 SRFINHLCEPNLLPVRVFMSHQDLRFPRIGFFSSRHIGAGEEIGFDYGDRFWDVKGKLFSCQCGSPKCKHP 1200
Cdd:cd10535   161 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 231
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
455-581 9.83e-61

Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 (also known as GLP) and EHMT2 (also known as NG36 and G9a) are histone methyltransferases that methylate the K9 position of histone H3, marking genomic regions for transcriptional repression. They may play a role in the G0/G1 cell cycle transition and are associated with promoting various types of cancer. Mutations in EHMT1 are associated with the genetic disorder Kleefstra syndrome. A functional role for the zinc-binding domain has not been established.


:

Pssm-ID: 411018  Cd Length: 133  Bit Score: 203.78  E-value: 9.83e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  455 PLCSCRMETPKEEEVSAKAGEHCMAIESTGQELGRCTN-RVAKYELMRPSNKVRHLVLCEDHRGKMVKHQCCPGCGYFCT 533
Cdd:cd20905     5 PLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCGLFCT 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 156717252  534 AGTFMECQPDSTISHRFHKDCATRVNNSSYCPHCGEEAS-KAKEVTIAK 581
Cdd:cd20905    85 QGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
658-914 6.93e-53

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 187.47  E-value: 6.93e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  658 LESALLALDSEKPKKLRFHPKQLYFSARQGELQKVLMMLVDGIDPNYKMEQhsRRTPLHAAAEMGYTDICHMLIQAGANL 737
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG--GNTLLHAAARNGDLEIVKLLLEAGADV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  738 DSCSEDQRTPLMEAAENNHLDTVKYLVKGGALIDPKDSEGSTCLHLAAKKGHYEVVKYLLSSeRTDVNCQDDGGWTPMIW 817
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHL 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  818 ATEYKHVEIVKLLHSSRADVNIRDNEENICLHWAAFAGSVEIAEILLASKCDLRAVNIHGDSPLHIAARENRHECVMLFL 897
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
                         250
                  ....*....|....*..
gi 156717252  898 GHGSEVGLKNKEGETPL 914
Cdd:COG0666   273 LALLLLAAALLDLLTLL 289
 
Name Accession Description Interval E-value
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
970-1200 0e+00

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine N-methyltransferase 1 (EHMT1) and similar proteins; EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, or lysine N-methyltransferase 1D (KMT1D)) acts as a histone-lysine N-methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin.


Pssm-ID: 380933 [Multi-domain]  Cd Length: 231  Bit Score: 535.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  970 VNYKYVSQNCVTSPLNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKNGRLLPEFNMLEPPLIFECNHACSCWRNC 1049
Cdd:cd10535     1 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1050 RNRVVQNGLKIRLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVREDDTYLFDLDNKDREVYCIDARFYGNI 1129
Cdd:cd10535    81 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156717252 1130 SRFINHLCEPNLLPVRVFMSHQDLRFPRIGFFSSRHIGAGEEIGFDYGDRFWDVKGKLFSCQCGSPKCKHP 1200
Cdd:cd10535   161 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 231
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
455-581 9.83e-61

Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 (also known as GLP) and EHMT2 (also known as NG36 and G9a) are histone methyltransferases that methylate the K9 position of histone H3, marking genomic regions for transcriptional repression. They may play a role in the G0/G1 cell cycle transition and are associated with promoting various types of cancer. Mutations in EHMT1 are associated with the genetic disorder Kleefstra syndrome. A functional role for the zinc-binding domain has not been established.


Pssm-ID: 411018  Cd Length: 133  Bit Score: 203.78  E-value: 9.83e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  455 PLCSCRMETPKEEEVSAKAGEHCMAIESTGQELGRCTN-RVAKYELMRPSNKVRHLVLCEDHRGKMVKHQCCPGCGYFCT 533
Cdd:cd20905     5 PLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCGLFCT 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 156717252  534 AGTFMECQPDSTISHRFHKDCATRVNNSSYCPHCGEEAS-KAKEVTIAK 581
Cdd:cd20905    85 QGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
658-914 6.93e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 187.47  E-value: 6.93e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  658 LESALLALDSEKPKKLRFHPKQLYFSARQGELQKVLMMLVDGIDPNYKMEQhsRRTPLHAAAEMGYTDICHMLIQAGANL 737
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG--GNTLLHAAARNGDLEIVKLLLEAGADV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  738 DSCSEDQRTPLMEAAENNHLDTVKYLVKGGALIDPKDSEGSTCLHLAAKKGHYEVVKYLLSSeRTDVNCQDDGGWTPMIW 817
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHL 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  818 ATEYKHVEIVKLLHSSRADVNIRDNEENICLHWAAFAGSVEIAEILLASKCDLRAVNIHGDSPLHIAARENRHECVMLFL 897
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
                         250
                  ....*....|....*..
gi 156717252  898 GHGSEVGLKNKEGETPL 914
Cdd:COG0666   273 LALLLLAAALLDLLTLL 289
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
1060-1182 2.78e-41

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: 147.87  E-value: 2.78e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252   1060 IRLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVRE--------DDTYLFDLDNKdrevYCIDARFYGNISR 1131
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPkaydtdgaKAFYLFDIDSD----LCIDARRKGNLAR 76
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 156717252   1132 FINHLCEPNLLPVRVFMSHQDlrfpRIGFFSSRHIGAGEEIGFDYGDRFWD 1182
Cdd:smart00317   77 FINHSCEPNCELLFVEVNGDD----RIVIFALRDIKPGEELTIDYGSDYAN 123
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
1071-1177 7.26e-30

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: 114.93  E-value: 7.26e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  1071 GWGVRSLQDIPQGTFVCEYVGE-LISDAEADVRED-----------DTYLFDLDNKDRevYCIDAR--FYGNISRFINHL 1136
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELlyydklelrlwGPYLFTLDEDSE--YCIDARalYYGNWARFINHS 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 156717252  1137 CEPNLLPVRVFMShqdlRFPRIGFFSSRHIGAGEEIGFDYG 1177
Cdd:pfam00856   79 CDPNCEVRVVYVN----GGPRIVIFALRDIKPGEELTIDYG 115
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
1058-1199 1.37e-27

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 108.90  E-value: 1.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1058 LKIRLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVRED-----DTYLFDLDNKDRevycIDARFYGNISRF 1132
Cdd:COG2940     4 LHPRIEVRPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPhkeplHTYLFELDDDGV----IDGALGGNPARF 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156717252 1133 INHLCEPNLLPVRvfmshqdlRFPRIGFFSSRHIGAGEEIGFDYGDRFWDvkgKLFSCQCgsPKCKH 1199
Cdd:COG2940    80 INHSCDPNCEADE--------EDGRIFIVALRDIAAGEELTYDYGLDYDE---EEYPCRC--PNCRG 133
Ank_2 pfam12796
Ankyrin repeats (3 copies);
748-841 2.02e-26

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 104.04  E-value: 2.02e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252   748 LMEAAENNHLDTVKYLVKGGALIDPKDSEGSTCLHLAAKKGHYEVVKYLLssERTDVNCQDDgGWTPMIWATEYKHVEIV 827
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL--EHADVNLKDN-GRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 156717252   828 KLLHSSRADVNIRD 841
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
688-922 3.87e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 103.98  E-value: 3.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  688 ELQKVLMMLVDGIDPNYKMeqhsRRTPLHAAAEMGYTDICHMLIQAGANLDSCSEDQRTPLMEAAENNH-----LDTVKY 762
Cdd:PHA03100   16 KNIKYIIMEDDLNDYSYKK----PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  763 LVKGGALIDPKDSEGSTCLHLAA--KKGHYEVVKYLLSsERTDVNCQDDGGWTPMIWATEYKHV--EIVKLLHSSRADVN 838
Cdd:PHA03100   92 LLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLD-NGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDIN 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  839 IRDNeeniclhwaafagsveiAEILLASKCDLRAVNIHGDSPLHIAARENRHECVMLFLGHGSEVGLKNKEGETPLECSA 918
Cdd:PHA03100  171 AKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233

                  ....
gi 156717252  919 PNSD 922
Cdd:PHA03100  234 LNNN 237
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
746-918 4.34e-11

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 67.35  E-value: 4.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  746 TPLMEAAENNHLDTVKYLVKGGAlIDP--KDSEGSTCLHLAAKKGHYEVVKYLLSSERTDVN----CQDDGGWTPMIWAT 819
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPS-CDLfqRGALGETALHVAALYDNLEAAVVLMEAAPELVNepmtSDLYQGETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  820 EYKHVEIVKLLHSSRADVN--------IRDNEENIC------LHWAAFAGSVEIAEILLASKCDLRAVNIHGDSPLHIAA 885
Cdd:cd22192    98 VNQNLNLVRELIARGADVVspratgtfFRPGPKNLIyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILV 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 156717252  886 RENRHE--CVM--LFL---GHGSEVGL---KNKEGETPLECSA 918
Cdd:cd22192   178 LQPNKTfaCQMydLILsydKEDDLQPLdlvPNNQGLTPFKLAA 220
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
776-806 3.98e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 3.98e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 156717252    776 EGSTCLHLAAKKGHYEVVKYLLsSERTDVNC 806
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLL-DKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
745-840 7.00e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.00  E-value: 7.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252   745 RTPLMEAA-ENNHLDTVKYLVKGGALIDpkdsEGSTCLHLAAKKGH---YEVVKYLLSSERTDVN-------CQDD--GG 811
Cdd:TIGR00870   53 RSALFVAAiENENLELTELLLNLSCRGA----VGDTLLHAISLEYVdavEAILLHLLAAFRKSGPlelandqYTSEftPG 128
                           90       100
                   ....*....|....*....|....*....
gi 156717252   812 WTPMIWATEYKHVEIVKLLHSSRADVNIR 840
Cdd:TIGR00870  129 ITALHLAAHRQNYEIVKLLLERGASVPAR 157
 
Name Accession Description Interval E-value
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
970-1200 0e+00

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine N-methyltransferase 1 (EHMT1) and similar proteins; EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, or lysine N-methyltransferase 1D (KMT1D)) acts as a histone-lysine N-methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin.


Pssm-ID: 380933 [Multi-domain]  Cd Length: 231  Bit Score: 535.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  970 VNYKYVSQNCVTSPLNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKNGRLLPEFNMLEPPLIFECNHACSCWRNC 1049
Cdd:cd10535     1 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1050 RNRVVQNGLKIRLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVREDDTYLFDLDNKDREVYCIDARFYGNI 1129
Cdd:cd10535    81 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156717252 1130 SRFINHLCEPNLLPVRVFMSHQDLRFPRIGFFSSRHIGAGEEIGFDYGDRFWDVKGKLFSCQCGSPKCKHP 1200
Cdd:cd10535   161 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 231
SET_EHMT cd10543
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
971-1199 2.33e-163

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine N-methyltransferase EHMT1, EHMT2 and similar proteins; This family includes EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, lysine N-methyltransferase 1D, or KMT1D) and EHMT2 (also termed Eu-HMTase2, HLA-B-associated transcript 8, histone H3-K9 methyltransferase 3, H3-K9-HMTase 3, lysine N-methyltransferase 1C, KMT1C, or protein G9a), both act as histone-lysine N-methyltransferases that specifically mono- and dimethylate 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin.


Pssm-ID: 380941 [Multi-domain]  Cd Length: 231  Bit Score: 484.92  E-value: 2.33e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  971 NYKYVSQNCVTSPLNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKNGRLLPEFNMLEPPLIFECNHACSCWRNCR 1050
Cdd:cd10543     2 DFLYVTENCETSPLNIDRNITSLQTCSCRDDCSSDNCVCGRLSVRCWYDKEGRLLPDFNKLDPPLIFECNRACSCWRNCR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1051 NRVVQNGLKIRLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVREDDTYLFDLDNKDREVYCIDARFYGNIS 1130
Cdd:cd10543    82 NRVVQNGIRYRLQLFRTRGMGWGVRALQDIPKGTFVCEYIGELISDSEADSREDDSYLFDLDNKDGETYCIDARRYGNIS 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156717252 1131 RFINHLCEPNLLPVRVFMSHQDLRFPRIGFFSSRHIGAGEEIGFDYGDRFWDVKGKLFSCQCGSPKCKH 1199
Cdd:cd10543   162 RFINHLCEPNLIPVRVFVEHQDLRFPRIAFFASRDIKAGEELGFDYGEKFWRIKGKYFTCRCGSPKCKY 230
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
971-1208 1.09e-152

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine N-methyltransferase 2 (EHMT2) and similar proteins; EHMT2 (also termed Eu-HMTase2, HLA-B-associated transcript 8, histone H3-K9 methyltransferase 3, H3-K9-HMTase 3, lysine N-methyltransferase 1C (KMT1C), or protein G9a) acts as a histone-lysine N-methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin.


Pssm-ID: 380931 [Multi-domain]  Cd Length: 239  Bit Score: 457.56  E-value: 1.09e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  971 NYKYVSQNCVTSPLNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKNGRLLPEFNMLEPPLIFECNHACSCWRNCR 1050
Cdd:cd10533     2 DYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRNCK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1051 NRVVQNGLKIRLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVREDDTYLFDLDNKDREVYCIDARFYGNIS 1130
Cdd:cd10533    82 NRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNIS 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156717252 1131 RFINHLCEPNLLPVRVFMSHQDLRFPRIGFFSSRHIGAGEEIGFDYGDRFWDVKGKLFSCQCGSPKCKHPIKVLSPSQ 1208
Cdd:cd10533   162 RFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQ 239
SET_SETDB-like cd10538
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
971-1177 3.36e-99

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) and 2 (SETDB2), suppressor of variegation 3-9 homologs, SUV39H1 and SUV39H2, euchromatic histone-lysine N-methyltransferase EHMT1 and EHMT2, and similar proteins; The family includes SET domain bifurcated 1 (SETDB1) and 2 (SETDB2), suppressor of variegation 3-9 homologs, SUV39H1 and SUV39H2, euchromatic histone-lysine N-methyltransferase EHMT1 and EHMT2. SETDB1 (EC 2.1.1.43; also termed ERG-associated protein with SET domain (ESET), histone H3-K9 methyltransferase 4, H3-K9-HMTase 4, or lysine N-methyltransferase 1E (KMT1E)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. SETDB2 (EC 2.1.1.43; also termed chronic lymphocytic leukemia deletion region gene 8 protein (CLLD8), or lysine N-methyltransferase 1F (KMT1F)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It is involved in left-right axis specification in early development and mitosis. SUV39H1 (also termed histone H3-K9 methyltransferase 1, H3-K9-HMTase 1, lysine N-methyltransferase 1A, KMT1A, position-effect variegation 3-9 homolog, SUV39H, or Su(var)3-9 homolog 1) and SUV39H2 (also termed histone H3-K9 methyltransferase 2, H3-K9-HMTase 2, lysine N-methyltransferase 1B, KMT1B, or Su(var)3-9 homolog 2), both act as histone-lysine N-methyltransferases that specifically trimethylate 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. They mainly function in heterochromatin regions, thereby playing central roles in the establishment of constitutive heterochromatin at pericentric and telomere regions. EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, lysine N-methyltransferase 1D, or KMT1D) and EHMT2 (also termed Eu-HMTase2, HLA-B-associated transcript 8, histone H3-K9 methyltransferase 3, H3-K9-HMTase 3, lysine N-methyltransferase 1C, KMT1C, or protein G9a), both act as histone-lysine N-methyltransferases that specifically mono- and dimethylate 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. This family also includes the pre-SET domain, which is found in a number of histone methyltransferases (HMTase), N-terminal to the SET domain. Pre-SET domain is a zinc binding motif which contains 9 conserved cysteines that coordinate three zinc ions. It is thought that this region plays a structural role in stabilizing SET domains. Most family members, except for Arabidopsis thaliana SUVH9, contain a post-SET domain which harbors a zinc-binding site.


Pssm-ID: 380936 [Multi-domain]  Cd Length: 217  Bit Score: 314.31  E-value: 3.36e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  971 NYKYVSQNCVTSPLNIDRNITHLQYCVCIDDCSSSNCMCGQLS-MRCWYDKNGRLLPefnMLEPPLIFECNHACSCWRNC 1049
Cdd:cd10538     2 SFTYIKDNIVGKNVQPFSNIIDSVGCKCKDDCLDSKCACAAESdGIFAYTKNGLLRL---NNSPPPIFECNSKCSCDDDC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1050 RNRVVQNGLKIRLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVR------EDDTYLFDLDN-----KDREV 1118
Cdd:cd10538    79 KNRVVQRGLQARLQVFRTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRgkiydkSGGSYLFDLDEfsdsdGDGEE 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 156717252 1119 YCIDARFYGNISRFINHLCEPNLLPVRVFMSHQDLRFPRIGFFSSRHIGAGEEIGFDYG 1177
Cdd:cd10538   159 LCVDATFCGNVSRFINHSCDPNLFPFNVVIDHDDLRYPRIALFATRDILPGEELTFDYG 217
SET_SETDB1 cd10517
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
947-1198 1.31e-76

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) and similar proteins; SETDB1 (EC 2.1.1.43; also termed ERG-associated protein with SET domain (ESET), histone H3-K9 methyltransferase 4, H3-K9-HMTase 4, or lysine N-methyltransferase 1E (KMT1E)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes.


Pssm-ID: 380915 [Multi-domain]  Cd Length: 288  Bit Score: 254.91  E-value: 1.31e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  947 DISRGYENIPIPCVNAEDSELcPVNYKYVSQNCVTSPLNIDRNITHLQYCVCIDDCS-SSNCMCGQLS---MRCWydKNG 1022
Cdd:cd10517     8 DISYGKEGVPIPCVNEIDNSS-PPYVEYSKERIPGKGVNINLDPDFLVGCDCTDGCRdKSKCACQQLTieaTAAT--PGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1023 RLLP----EFNMLEPPL---IFECNHACSCWRNCRNRVVQNGLKIRLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELIS 1095
Cdd:cd10517    85 QINPsagyQYRRLMEKLptgVYECNSRCKCDKRCYNRVVQNGLQVRLQVFKTEKKGWGIRCLDDIPKGSFVCIYAGQILT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1096 DAEADVRE---DDTYLFDLD--------------NKDREVYCIDARFYGNISRFINHLCEPNLLPVRVFMSHQDLRFPRI 1158
Cdd:cd10517   165 EDEANEEGlqyGDEYFAELDyievveklkegyesDVEEHCYIIDAKSEGNLGRYLNHSCSPNLFVQNVFVDTHDLRFPWV 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 156717252 1159 GFFSSRHIGAGEEIGFDYGDRFWDVKGKLFSCQCGSPKCK 1198
Cdd:cd10517   245 AFFASRYIRAGTELTWDYNYEVGSVPGKVLYCYCGSSNCR 284
SET_SUV39H cd10542
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
970-1198 3.60e-69

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 homologs, SUV39H1, SUV39H2 and similar proteins; This family includes SUV39H1 (also termed histone H3-K9 methyltransferase 1, H3-K9-HMTase 1, lysine N-methyltransferase 1A, KMT1A, position-effect variegation 3-9 homolog, SUV39H, or Su(var)3-9 homolog 1) and SUV39H2 (also termed histone H3-K9 methyltransferase 2, H3-K9-HMTase 2, lysine N-methyltransferase 1B, KMT1B, or Su(var)3-9 homolog 2), both act as histone-lysine N-methyltransferases that specifically trimethylate 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. They mainly function in heterochromatin regions, thereby playing central roles in the establishment of constitutive heterochromatin at pericentric and telomere regions. Also included are Schizosaccharomyces pombe H3K9 methyltransferase Clr4 (SUV39H homolog) and Neurospora crassa DIM-5, both of which also methylate 'Lys-9' of histone H3.


Pssm-ID: 380940 [Multi-domain]  Cd Length: 245  Bit Score: 232.18  E-value: 3.60e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  970 VNYKYVSQNCVTSPLNIDRNIthLQYCVCIDDC--SSSNCmCGQLS-MRCWYDKNGRLLpefnmLEPPL-IFECNHACSC 1045
Cdd:cd10542     1 PNFQYINDYIPGDGVKIPEDF--LVGCECTEDChnNNPTC-CPAESgVKFAYDKQGRLR-----LPPGTpIYECNSRCKC 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1046 WRNCRNRVVQNGLKIRLQLFRTKS-KGWGVRSLQDIPQGTFVCEYVGELISDAEADVR------EDDTYLFDLD-NKDRE 1117
Cdd:cd10542    73 GPDCPNRVVQRGRKVPLCIFRTSNgRGWGVKTLEDIKKGTFVMEYVGEIITSEEAERRgkiydaNGRTYLFDLDyNDDDC 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1118 VYCIDARFYGNISRFINHLCEPNLLPVRVFMSHQDLRFPRIGFFSSRHIGAGEEIGFDYgDRFWDV----------KGKL 1187
Cdd:cd10542   153 EYTVDAAYYGNISHFINHSCDPNLAVYAVWINHLDPRLPRIAFFAKRDIKAGEELTFDY-LMTGTGgssestipkpKDVR 231
                         250
                  ....*....|.
gi 156717252 1188 FSCQCGSPKCK 1198
Cdd:cd10542   232 VPCLCGSKNCR 242
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
455-581 9.83e-61

Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 (also known as GLP) and EHMT2 (also known as NG36 and G9a) are histone methyltransferases that methylate the K9 position of histone H3, marking genomic regions for transcriptional repression. They may play a role in the G0/G1 cell cycle transition and are associated with promoting various types of cancer. Mutations in EHMT1 are associated with the genetic disorder Kleefstra syndrome. A functional role for the zinc-binding domain has not been established.


Pssm-ID: 411018  Cd Length: 133  Bit Score: 203.78  E-value: 9.83e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  455 PLCSCRMETPKEEEVSAKAGEHCMAIESTGQELGRCTN-RVAKYELMRPSNKVRHLVLCEDHRGKMVKHQCCPGCGYFCT 533
Cdd:cd20905     5 PLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCGLFCT 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 156717252  534 AGTFMECQPDSTISHRFHKDCATRVNNSSYCPHCGEEAS-KAKEVTIAK 581
Cdd:cd20905    85 QGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
971-1197 3.70e-55

SET domain (including pre-SET and post-SET domains) found in SET domain and mariner transposase fusion protein (SETMAR) and similar proteins; SETMAR (also termed metnase) is a DNA-binding protein that is indirectly recruited to sites of DNA damage through protein-protein interactions. It has a sequence-specific DNA-binding activity recognizing the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element and displays a DNA nicking and end joining activity. SETMAR also acts as a histone-lysine N-methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3. It specifically mediates dimethylation of H3 'Lys-36' at sites of DNA double-strand break and may recruit proteins required for efficient DSB repair through non-homologous end-joining.


Pssm-ID: 380942 [Multi-domain]  Cd Length: 254  Bit Score: 192.51  E-value: 3.70e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  971 NYKYVSQNCVTSPLNIDRNITHLQYCVCIDD-CSSSNCMCgqlsMRCW---YDKNGRLLPEFNMLEPPlIFECNHACSCW 1046
Cdd:cd10544     2 DFQYTPENVPGPGADTDPNEITFPGCDCKTSsCEPETCSC----LRKYgpnYDDDGCLLDFDGKYSGP-VFECNSMCKCS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1047 RNCRNRVVQNGLKIRLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVR------EDDTYLFDLdnkdRE--- 1117
Cdd:cd10544    77 ESCQNRVVQNGLQFKLQVFKTPKKGWGLRTLEFIPKGRFVCEYAGEVIGFEEARRRtksqtkGDMNYIIVL----REhls 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1118 -----VYCIDARFYGNISRFINHLCEPNL--LPVRVfmshqDLRFPRIGFFSSRHIGAGEEIGFDYGDRF---------- 1180
Cdd:cd10544   153 sgkvlETFVDPTYIGNIGRFLNHSCEPNLfmVPVRV-----DSMVPKLALFAARDIVAGEELSFDYSGEFsnsvesvtla 227
                         250
                  ....*....|....*...
gi 156717252 1181 -WDVKGKLFSCQCGSPKC 1197
Cdd:cd10544   228 rQDESKSRKPCLCGAENC 245
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
996-1177 1.92e-54

SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar proteins; Arabidopsis thaliana SUVH protein (also termed suppressor of variegation 3-9 homolog protein) is a histone-lysine N-methyltransferase that methylates 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression. Some family members contain a post-SET domain which binds a Zn2+ ion. Most family members, except for Arabidopsis thaliana SUVH9, contain a post-SET domain which harbors a zinc-binding site.


Pssm-ID: 380943 [Multi-domain]  Cd Length: 232  Bit Score: 189.54  E-value: 1.92e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  996 CVCIDDC--SSSNCMCGQL-SMRCWYDKNGRLLPEFnmlepPLIFECNHACSCWRNCRNRVVQNGLKIRLQLFRTKSKGW 1072
Cdd:cd10545    24 CDCKNRCtdGASDCACVKKnGGEIPYNFNGRLIRAK-----PAIYECGPLCKCPPSCYNRVTQKGLRYRLEVFKTAERGW 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1073 GVRSLQDIPQGTFVCEYVGELISDAEADVR-EDDTYLFDLDNK------------DREV---------------YCIDAR 1124
Cdd:cd10545    99 GVRSWDSIPAGSFICEYVGELLDTSEADTRsGNDDYLFDIDNRqtnrgwdggqrlDVGMsdgerssaedeesseFTIDAG 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 156717252 1125 FYGNISRFINHLCEPNLLPVRVFMSHQDLRFPRIGFFSSRHIGAGEEIGFDYG 1177
Cdd:cd10545   179 SFGNVARFINHSCSPNLFVQCVLYDHNDLRLPRVMLFAADNIPPLQELTYDYG 231
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
658-914 6.93e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 187.47  E-value: 6.93e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  658 LESALLALDSEKPKKLRFHPKQLYFSARQGELQKVLMMLVDGIDPNYKMEQhsRRTPLHAAAEMGYTDICHMLIQAGANL 737
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG--GNTLLHAAARNGDLEIVKLLLEAGADV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  738 DSCSEDQRTPLMEAAENNHLDTVKYLVKGGALIDPKDSEGSTCLHLAAKKGHYEVVKYLLSSeRTDVNCQDDGGWTPMIW 817
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHL 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  818 ATEYKHVEIVKLLHSSRADVNIRDNEENICLHWAAFAGSVEIAEILLASKCDLRAVNIHGDSPLHIAARENRHECVMLFL 897
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
                         250
                  ....*....|....*..
gi 156717252  898 GHGSEVGLKNKEGETPL 914
Cdd:COG0666   273 LALLLLAAALLDLLTLL 289
SET_SETDB cd10541
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...
996-1198 3.09e-52

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), SET domain bifurcated 2 (SETDB2), and similar proteins; SETDB1 (EC 2.1.1.43; also termed ERG-associated protein with SET domain (ESET), histone H3-K9 methyltransferase 4, H3-K9-HMTase 4, or lysine N-methyltransferase 1E (KMT1E)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. SETDB2 (EC 2.1.1.43; also termed chronic lymphocytic leukemia deletion region gene 8 protein (CLLD8), or lysine N-methyltransferase 1F (KMT1F)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It is involved in left-right axis specification in early development and mitosis.


Pssm-ID: 380939 [Multi-domain]  Cd Length: 236  Bit Score: 183.51  E-value: 3.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  996 CVCIDDC-SSSNCMCGQLSMRcwydkNGRLLP----------EFNMLE---PPLIFECNHACSCWRN-CRNRVVQNGLKI 1060
Cdd:cd10541    18 CDCTDGCrDKSKCACHQLTIQ-----ATACTPggqdnptagyQYKRLEeclPTGVYECNKLCKCDPNmCQNRLVQHGLQV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1061 RLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADvRED----DTYLFDLDNKDREVYCIDARFYGNISRFINHL 1136
Cdd:cd10541    93 RLQLFKTQNKGWGIRCLDDIAKGTFVCIYAGKILTDDFAD-KEGlemgDEYFANLDHIEESCYIIDAKLEGNLGRYLNHS 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156717252 1137 CEPNLLPVRVFMSHQDLRFPRIGFFSSRHIGAGEEIGFDYGDRFWDVKGKLFSCQCGSPKCK 1198
Cdd:cd10541   172 CSPNLFVQNVFVDTHDLRFPWVAFFASKRIKAGTELTWDYNYEVGSVEGKELLCCCGSNECR 233
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
661-914 2.70e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 182.85  E-value: 2.70e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  661 ALLALDSEKPKKLRFHPKQLYFSARQGELQKVLMMLVDGIDPNYKMEQhsRRTPLHAAAEMGYTDICHMLIQAGANLDSC 740
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADAL--GALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  741 SEDQRTPLMEAAENNHLDTVKYLVKGGALIDPKDSEGSTCLHLAAKKGHYEVVKYLLSSErTDVNCQDDGGWTPMIWATE 820
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  821 YKHVEIVKLLHSSRADVNIRDNEENICLHWAAFAGSVEIAEILLASKCDLRAVNIHGDSPLHIAARENRHECVMLFLGHG 900
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
                         250
                  ....*....|....
gi 156717252  901 SEVGLKNKEGETPL 914
Cdd:COG0666   243 ADLNAKDKDGLTAL 256
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
971-1176 3.11e-46

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 homolog 1 (SUV39H1) and similar proteins; SUV39H1 (EC 2.1.1.43; also termed histone H3-K9 methyltransferase 1, H3-K9-HMTase 1, lysine N-methyltransferase 1A (KMT1A), position-effect variegation 3-9 homolog (SUV39H), or Su(var)3-9 homolog 1) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. It mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions.


Pssm-ID: 380923 [Multi-domain]  Cd Length: 255  Bit Score: 166.99  E-value: 3.11e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  971 NYKYVSQNCVTSPLNIDRNITHlqyCVCiDDCSSS---NCMCGQLSMRCWYDKNGRLlpefnMLEPPL-IFECNHACSCW 1046
Cdd:cd10525     2 DFVYINEYKVGEGVTLNQVAVG---CEC-QDCLSQpvgGCCPGASKHRFAYNEQGQV-----KVRPGLpIYECNSRCRCG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1047 RNCRNRVVQNGLKIRLQLFRTKS-KGWGVRSLQDIPQGTFVCEYVGELISDAEADVR------EDDTYLFDLDNKDrEVY 1119
Cdd:cd10525    73 PDCPNRVVQKGIQYDLCIFRTDNgRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRgqiydrQGATYLFDLDYVE-DVY 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 156717252 1120 CIDARFYGNISRFINHLCEPNLLPVRVFMSHQDLRFPRIGFFSSRHIGAGEEIGFDY 1176
Cdd:cd10525   152 TVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIALFATRTIRAGEELTFDY 208
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
996-1198 4.64e-46

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 homolog 2 (SUV39H2) and similar proteins; SUV39H2 (EC 2.1.1.43; also termed histone H3-K9 methyltransferase 2, H3-K9-HMTase 2, lysine N-methyltransferase 1B (KMT1B), or Su(var)3-9 homolog 2) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. It mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions.


Pssm-ID: 380930 [Multi-domain]  Cd Length: 243  Bit Score: 166.22  E-value: 4.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  996 CVCIDdCSSSNCMCGQLSMRCWYDKNGRLlpefnMLEPPL-IFECNHACSCWRNCRNRVVQNGLKIRLQLFRTKS-KGWG 1073
Cdd:cd10532    25 CDCSD-CFFGKCCPAEAGVLFAYNEHGQL-----KIPPGTpIYECNSRCKCGPDCPNRVVQKGTQYSLCIFRTSNgRGWG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1074 VRSLQDIPQGTFVCEYVGELISDAEADVR------EDDTYLFDLDNKDREvYCIDARFYGNISRFINHLCEPNLLPVRVF 1147
Cdd:cd10532    99 VKTLQKIKKNSFVMEYVGEVITSEEAERRgqfydsKGITYLFDLDYESDE-FTVDAARYGNVSHFVNHSCDPNLQVFNVF 177
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156717252 1148 MSHQDLRFPRIGFFSSRHIGAGEEIGFDY-----GDRFWDV-------KGKLFSCQCGSPKCK 1198
Cdd:cd10532   178 IDNLDTRLPRIALFSTRTIKAGEELTFDYqmkgsGDLSSDSidnspakKRVRTVCKCGAVTCR 240
SET_SUV39H_Clr4-like cd20073
SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 ...
996-1198 5.53e-46

SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 methyltransferase Clr4, and similar proteins; This subfamily contains fission yeast Schizosaccharomyces pombe H3K9 methyltransferase Clr4 (also known as Suv39h), the sole homolog of the mammalian SUV39H1 and SUV39H2 enzymes, that has a critical role in preventing aberrant heterochromatin formation. It is known to di- and tri-methylate Lys-9 of histone H3, a central heterochromatic histone modification, with its specificity profile most similar to that of the human SUV39H2 homolog.


Pssm-ID: 380999 [Multi-domain]  Cd Length: 259  Bit Score: 166.21  E-value: 5.53e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  996 CVCIDDCSSSNCMcgqlsmrcwYDKNGRLLPEFNMLepplIFECNHACSCWRNCRNRVVQNGLKIRLQLFRTKSKGWGVR 1075
Cdd:cd20073    42 CQCLEDSNEKSFA---------YDEYGRVRANTGSI----IYECNENCDCGINCPNRVVQRGRKLPLEIFKTKHKGWGLR 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1076 SLQDIPQGTFVCEYVGELISDAEADVRE---DD---TYLFDLDNKDREV---YCIDARFYGNISRFINHLCEPNLLPVRV 1146
Cdd:cd20073   109 CPRFIKAGTFIGVYLGEVITQSEAEIRGkkyDNvgvTYLFDLDLFEDQVdeyYTVDAQYCGDVTRFINHSCDPNLAIYSV 188
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156717252 1147 FMSHQDLRFPRIGFFSSRHIGAGEEIGFDYGDR----------------FWDVKGKLfSCQCGSPKCK 1198
Cdd:cd20073   189 LRDKSDSKIYDLAFFAIKDIPALEELTFDYSGRnnfdqlgfignrsnskYINLKNKR-PCYCGSANCR 255
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
996-1201 6.17e-46

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) and similar proteins; SETDB2 (EC 2.1.1.43; also termed chronic lymphocytic leukemia deletion region gene 8 protein (CLLD8), or lysine N-methyltransferase 1F (KMT1F)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It is involved in left-right axis specification in early development and mitosis.


Pssm-ID: 380921 [Multi-domain]  Cd Length: 266  Bit Score: 166.55  E-value: 6.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  996 CVCIDDCSS-SNCMCGQLSMR----CWYDKN-GRLLPEFNMLEPPL---IFECNHACSCWRN-CRNRVVQNGLKIRLQLF 1065
Cdd:cd10523    34 CDCTDGCIDiLKCACLQLTARafskSESSPSkGGRGYKYKRLQEPIpsgLYECNVSCKCNRMlCQNRVVQHGLQVRLQVF 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1066 RTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVREDDTYLFDLDNKDRE-----------------VYCIDARFYGN 1128
Cdd:cd10523   114 KTEKKGWGVRCLDDIDKGTFVCIYAGRVLSRARSPTEPLPPKLELPSENEVEvvtswlilskkrklrenVCFLDASKEGN 193
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156717252 1129 ISRFINHLCEPNLLPVRVFMSHQDLRFPRIGFFSSRHIGAGEEIGFDYGDRFWDVKGKLFSCQCGSPKCKHPI 1201
Cdd:cd10523   194 VGRFLNHSCCPNLFVQNVFVDTHDKNFPWVAFFTNRVVKAGTELTWDYSYDAGTSPEQEIPCLCGVNKCQKKI 266
SET_SUV39H_DIM5-like cd19473
SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...
996-1198 5.19e-45

SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; This subfamily contains Neurospora crassa DIM-5 (also termed H3-K9-HMTase dim-5, or HKMT) which functions as histone-lysine N-methyltransferase that specifically trimethylates histone H3 to form H3K9me3.


Pssm-ID: 380996 [Multi-domain]  Cd Length: 274  Bit Score: 164.03  E-value: 5.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  996 CVCIDDCSSSNCMCGQLSMRCWY---DKNGRLLPEFNMLEPPlIFECNHACSCWRNCRNRVVQNGLKIRLQLFRTKS-KG 1071
Cdd:cd19473    39 CLCLQDVDPDDDRDPGKKKNAYHssgAKKGCLRGHMLNSRLP-IYECHEGCACSDDCPNRVVERGRKVPLQIFRTSDgRG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1072 WGVRSLQDIPQGTFVCEYVGELISDAEADVRED--------DTYLFDLDN-------KDR---EVYCIDARFYGNISRFI 1133
Cdd:cd19473   118 WGVRSTVDIKRGQFVDCYVGEIITPEEAQRRRDaatiaqrkDVYLFALDKfsdpdslDPRlrgDPYEIDGEFMSGPTRFI 197
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156717252 1134 NHLCEPNLlpvRVFM---SHQDLRFPRIGFFSSRHIGAGEEIGFDY--------GDRFWDVKGK-LFSCQCGSPKCK 1198
Cdd:cd19473   198 NHSCDPNL---RIFArvgDHADKHIHDLAFFAIKDIPRGTELTFDYvdgvtgldDDAGDEEKEKeMTKCLCGSPKCR 271
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
1060-1182 2.78e-41

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: 147.87  E-value: 2.78e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252   1060 IRLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVRE--------DDTYLFDLDNKdrevYCIDARFYGNISR 1131
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPkaydtdgaKAFYLFDIDSD----LCIDARRKGNLAR 76
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 156717252   1132 FINHLCEPNLLPVRVFMSHQDlrfpRIGFFSSRHIGAGEEIGFDYGDRFWD 1182
Cdd:smart00317   77 FINHSCEPNCELLFVEVNGDD----RIVIFALRDIKPGEELTIDYGSDYAN 123
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
1062-1198 2.22e-39

SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), nuclear SETD2 (NSD2), ASH1-like protein (ASH1L) and similar proteins; This family includes SET domain-containing protein 2 (SETD2), nuclear SETD2 (NSD2) and ASH1-like protein (ASH1L), which function as histone-lysine N-methyltransferases. SETD2 specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using demethylated 'Lys-36' (H3K36me2) as substrate. NSD2 shows histone H3 'Lys-27' (H3K27me) methyltransferase activity. ASH1L specifically methylates 'Lys-36' of histone H3 (H3K36me). The family also includes Arabidopsis thaliana ASH1-related protein 3 (ASHR3) and similar proteins.


Pssm-ID: 380929  Cd Length: 136  Bit Score: 142.78  E-value: 2.22e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1062 LQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVRED--------DTYLFDLdnKDREVycIDARFYGNISRFI 1133
Cdd:cd10531     2 LELFRTEKKGWGVKAKEDIQKGEFIIEYVGEVIDKKEFKERLDeyeelgksNFYILSL--SDDVV--IDATRKGNLSRFI 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156717252 1134 NHLCEPNLLpVRVFMShqdLRFPRIGFFSSRHIGAGEEIGFDYGdrFWDVKGKLFSCQCGSPKCK 1198
Cdd:cd10531    78 NHSCEPNCE-TQKWIV---NGEYRIGIFALRDIPAGEELTFDYN--FVNYNEAKQVCLCGAQNCR 136
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
1062-1198 7.17e-35

SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ASH1L (EC 2.1.1.43; also termed absent small and homeotic disks protein 1 homolog, KMT2H, or lysine N-methyltransferase 2H) acts as histone-lysine N-methyltransferase that specifically methylates 'Lys-36' of histone H3 (H3K36me). It plays important roles in development; heterozygous mutation of ASH1L is associated with severe intellectual disability (ID) and multiple congenital anomaly (MCA).


Pssm-ID: 380951 [Multi-domain]  Cd Length: 141  Bit Score: 130.10  E-value: 7.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1062 LQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVREDDTYlfdldNKDREVYC--------IDARFYGNISRFI 1133
Cdd:cd19174     2 LERFRTEDKGWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRMIEQY-----HNHSHHYClnldsgmvIDGYRMGNEARFV 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156717252 1134 NHLCEPNLLPVRVFMSHQdlrfPRIGFFSSRHIGAGEEIGFDYGDRFWDVKGKLfSCQCGSPKCK 1198
Cdd:cd19174    77 NHSCDPNCEMQKWSVNGV----YRIGLFALKDIPAGEELTYDYNFHSFNVEKQQ-PCKCGSPNCR 136
SET_SETD1-like cd10518
SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...
1050-1198 5.30e-33

SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), histone-lysine N-methyltransferases (KMT2A/KMT2B/KMT2C/KMT2D) and similar proteins; This family includes SET domain-containing protein 1A (SETD1A), 1B (SETD1B), as well as histone-lysine N-methyltransferase 2A (KMT2A), 2B (KMT2B), 2C (KMT2C), 2D (KMT2D). These proteins are histone-lysine N-methyltransferases (EC 2.1.1.43) that specifically methylate 'Lys-4' of histone H3 (H3K4me).


Pssm-ID: 380916  Cd Length: 150  Bit Score: 125.02  E-value: 5.30e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1050 RNRVVQNGLKIRLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVRED--------DTYLFDLDNKdrevYCI 1121
Cdd:cd10518     4 RFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKrydeegggGTYMFRIDED----LVI 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156717252 1122 DARFYGNISRFINHLCEPNLLpVRVfMSHQDLRfpRIGFFSSRHIGAGEEIGFDYgdRFWDVKGKLFSCQCGSPKCK 1198
Cdd:cd10518    80 DATKKGNIARFINHSCDPNCY-AKI-ITVDGEK--HIVIFAKRDIAPGEELTYDY--KFPIEDEEKIPCLCGAPNCR 150
SET_SETD2 cd19172
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...
1061-1198 1.89e-31

SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and similar proteins; SETD2 (also termed HIF-1, huntingtin yeast partner B, huntingtin-interacting protein 1 (HIP-1), huntingtin-interacting protein B, lysine N-methyltransferase 3A or protein-lysine N-methyltransferase SETD2) acts as histone-lysine N-methyltransferase that specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using demethylated 'Lys-36' (H3K36me2) as substrate. It has been shown that methylation is a posttranslational modification of dynamic microtubules and that SETD2 methylates alpha-tubulin at lysine 40, the same lysine that is marked by acetylation on microtubules. Methylation of microtubules occurs during mitosis and cytokinesis and can be ablated by SETD2 deletion, which causes mitotic spindle and cytokinesis defects, micronuclei, and polyploidy.


Pssm-ID: 380949 [Multi-domain]  Cd Length: 142  Bit Score: 120.38  E-value: 1.89e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1061 RLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAE--------ADVREDDTYLFDLDNKDrevyCIDARFYGNISRF 1132
Cdd:cd19172     3 KVEVFRTEKKGWGLRAAEDLPKGTFVIEYVGEVLDEKEfkrrmkeyAREGNRHYYFMALKSDE----IIDATKKGNLSRF 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156717252 1133 INHLCEPNlLPVRVFMSHQDLrfpRIGFFSSRHIGAGEEIGFDYG-DRFWDVKGKlfsCQCGSPKCK 1198
Cdd:cd19172    79 INHSCEPN-CETQKWTVNGEL---RVGFFAKRDIPAGEELTFDYQfERYGKEAQK---CYCGSPNCR 138
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
1071-1177 7.26e-30

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: 114.93  E-value: 7.26e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  1071 GWGVRSLQDIPQGTFVCEYVGE-LISDAEADVRED-----------DTYLFDLDNKDRevYCIDAR--FYGNISRFINHL 1136
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELlyydklelrlwGPYLFTLDEDSE--YCIDARalYYGNWARFINHS 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 156717252  1137 CEPNLLPVRVFMShqdlRFPRIGFFSSRHIGAGEEIGFDYG 1177
Cdd:pfam00856   79 CDPNCEVRVVYVN----GGPRIVIFALRDIKPGEELTIDYG 115
SET_NSD cd19173
SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...
1061-1197 5.04e-29

SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, NSD2, NSD3 and similar proteins; The nuclear receptor-binding SET Domain (NSD) family of histone H3 lysine 36 methyltransferases is comprised of NSD1, NSD2, and NSD3, which are primarily known to be involved in chromatin integrity and gene expression through mono-, di-, or tri-methylating lysine 36 of histone H3 (H3K36), respectively. NSD1 (EC 2.1.1.43; also termed histone-lysine N-methyltransferase H3 lysine-36 and H4 lysine-20 specific, androgen receptor coactivator 267 kDa protein (ARA267), androgen receptor-associated protein of 267 kDa, H3-K36-HMTase, H4-K20-HMTase, lysine N-methyltransferase 3B (KMT3B) or NR-binding SET domain-containing protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-36' of histone H3 and 'Lys-20' of histone H4. NSD2 (EC 2.1.1.43; also termed multiple myeloma SET domain-containing protein (MMSET), protein trithorax-5 (TRX5), or wolf-Hirschhorn syndrome candidate 1 protein (WHSC1)) acts as histone-lysine N-methyltransferase with histone H3 'Lys-27' (H3K27me) methyltransferase activity. NSD3 (EC 2.1.1.43; also termed protein whistle, WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1L1), or WHSC1-like protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-4' and 'Lys-27' of histone H3.


Pssm-ID: 380950 [Multi-domain]  Cd Length: 142  Bit Score: 113.56  E-value: 5.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1061 RLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVR------EDDT--YLFDLDnKDRevyCIDARFYGNISRF 1132
Cdd:cd19173     3 PTEPFKTGDRGWGLRTKRDIKKGDFVIEYVGELIDEEECRRRlkkaheNNITnfYMLTLD-KDR---IIDAGPKGNLSRF 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156717252 1133 INHLCEPNlLPVRVFMSHQDlrfPRIGFFSSRHIGAGEEIGFDYG-DRFWDVKGKlfsCQCGSPKC 1197
Cdd:cd19173    79 MNHSCQPN-CETQKWTVNGD---TRVGLFAVRDIPAGEELTFNYNlDCLGNEKKV---CRCGAPNC 137
Pre-SET pfam05033
Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines ...
948-1052 8.50e-29

Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines that coordinate three zinc ions. It is thought that this region plays a structural role in stabilising SET domains.


Pssm-ID: 461530 [Multi-domain]  Cd Length: 99  Bit Score: 110.97  E-value: 8.50e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252   948 ISRGYENIPIPCVNAEDSELCPVNYKYVSQNCVTSPLNIDRnithLQYCVCiDDCSSSNCMCGQLSM---RCWYDKNGRL 1024
Cdd:pfam05033    1 ISKGKENVPIPVVNEVDDEPPPPDFTYITSYIYPKEFLLII----PQGCDC-GDCSSEKCSCAQLNGgefRFPYDKDGLL 75
                           90       100
                   ....*....|....*....|....*...
gi 156717252  1025 LPEfnmlEPPLIFECNHACSCWRNCRNR 1052
Cdd:pfam05033   76 VPE----SKPPIYECNPLCGCPPSCPNR 99
SET_EZH cd10519
SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...
1061-1178 1.99e-28

SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar proteins; The family includes EZH1 and EZH2. EZH1 (EC 2.1.1.43; also termed ENX-2, or histone-lysine N-methyltransferase EZH1) is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. EZH2 (EC 2.1.1.43; also termed lysine N-methyltransferase 6, ENX-1, or histone-lysine N-methyltransferase EZH2) is a catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Both, EZH1 and EZH2, can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively.


Pssm-ID: 380917  Cd Length: 117  Bit Score: 110.80  E-value: 1.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1061 RLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVRE---DD---TYLFDLDNKdrevYCIDARFYGNISRFIN 1134
Cdd:cd10519     2 RLLLGKSDVAGWGLFLKEPIKKDEFIGEYTGELISQDEADRRGkiyDKynsSYLFNLNDQ----FVVDATRKGNKIRFAN 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 156717252 1135 HLCEPNLLPvRVFMSHQDlrfPRIGFFSSRHIGAGEEIGFDYGD 1178
Cdd:cd10519    78 HSSNPNCYA-KVMMVNGD---HRIGIFAKRDIEAGEELFFDYGY 117
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
1058-1199 1.37e-27

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 108.90  E-value: 1.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1058 LKIRLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVRED-----DTYLFDLDNKDRevycIDARFYGNISRF 1132
Cdd:COG2940     4 LHPRIEVRPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPhkeplHTYLFELDDDGV----IDGALGGNPARF 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156717252 1133 INHLCEPNLLPVRvfmshqdlRFPRIGFFSSRHIGAGEEIGFDYGDRFWDvkgKLFSCQCgsPKCKH 1199
Cdd:COG2940    80 INHSCDPNCEADE--------EDGRIFIVALRDIAAGEELTYDYGLDYDE---EEYPCRC--PNCRG 133
Ank_2 pfam12796
Ankyrin repeats (3 copies);
748-841 2.02e-26

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 104.04  E-value: 2.02e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252   748 LMEAAENNHLDTVKYLVKGGALIDPKDSEGSTCLHLAAKKGHYEVVKYLLssERTDVNCQDDgGWTPMIWATEYKHVEIV 827
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL--EHADVNLKDN-GRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 156717252   828 KLLHSSRADVNIRD 841
Cdd:pfam12796   78 KLLLEKGADINVKD 91
SET_ASHR3-like cd19175
SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...
1061-1198 6.16e-26

SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 (ASHR3) and similar proteins; This family includes Arabidopsis thaliana ASH1-related protein 3 (ASHR3, also termed protein SET DOMAIN GROUP 4 or protein stamen loss), ASH1 homolog 3 (ASHH3, also termed protein SET DOMAIN GROUP 7) and homolog 4 (ASHH4, also termed protein SET DOMAIN GROUP 24). They all function as histone-lysine N-methyltransferases (EC 2.1.1.43).


Pssm-ID: 380952 [Multi-domain]  Cd Length: 139  Bit Score: 104.42  E-value: 6.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1061 RLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVR--------EDDTYLFDLDnKDrevYCIDARFYGNISRF 1132
Cdd:cd19175     1 KMKLVKTEKCGWGLVADEDINAGEFIIEYVGEVIDDKTCEERlwdmkhkgEKNFYMCEID-KD---MVIDATFKGNLSRF 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156717252 1133 INHLCEPNllpvRVFMSHQDLRFPRIGFFSSRHIGAGEEIGFDYgdRFWDVkGKLFSCQCGSPKCK 1198
Cdd:cd19175    77 INHSCDPN----CELQKWQVDGETRIGVFAIRDIKKGEELTYDY--QFVQF-GADQDCHCGSKNCR 135
SET_SETD1 cd19169
SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...
1056-1198 3.98e-25

SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and similar proteins; This family includes SET domain-containing protein 1A (SETD1A) and SET domain-containing protein 1B (SETD1B). These proteins are histone-lysine N-methyltransferases that specifically methylate 'Lys-4' of histone H3 (H3K4me) when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated.


Pssm-ID: 380946  Cd Length: 148  Bit Score: 102.42  E-value: 3.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1056 NGLKIR---LQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVRED--------DTYLFDLDnkdrEVYCIDAR 1124
Cdd:cd19169     6 NQLKFRkkqLKFAKSRIHDWGLFALEPIAADEMVIEYVGQVIRQSVADEREKryeaigigSSYLFRVD----DDTIIDAT 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156717252 1125 FYGNISRFINHLCEPNLLPVRVFMSHQDlrfpRIGFFSSRHIGAGEEIGFDYGDRFWDVKgklFSCQCGSPKCK 1198
Cdd:cd19169    82 KCGNLARFINHSCNPNCYAKIITVESQK----KIVIYSKRPIAVNEEITYDYKFPIEDEK---IPCLCGAPQCR 148
PreSET smart00468
N-terminal to some SET domains; A Cys-rich putative Zn2+-binding domain that occurs N-terminal ...
946-1044 2.96e-24

N-terminal to some SET domains; A Cys-rich putative Zn2+-binding domain that occurs N-terminal to some SET domains. Function is unknown. Unpublished.


Pssm-ID: 128744 [Multi-domain]  Cd Length: 98  Bit Score: 98.26  E-value: 2.96e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252    946 RDISRGYENIPIPCVNAEDSELCPVNYKYVSQNCVTSPLNIDRNITHLQYCVCIDDCSSSN-CMCGQLSMRCW-YDKNGR 1023
Cdd:smart00468    2 LDISNGKENVPVPLVNEVDEDPPPPDFEYISEYIYGQGVPIDRSPSPLVGCSCSGDCSSSNkCECARKNGGEFaYELNGG 81
                            90       100
                    ....*....|....*....|.
gi 156717252   1024 llpeFNMLEPPLIFECNHACS 1044
Cdd:smart00468   82 ----LRLKRKPLIYECNSRCS 98
SET_SETD8 cd10528
SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2. ...
1057-1179 7.04e-24

SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2.1.1.43; also termed N-lysine methyltransferase KMT5A, H4-K20-HMTase KMT5A, lysine N-methyltransferase 5A, lysine-specific methylase 5A, PR/SET domain-containing protein 07, PR-Set7 or PR/SET07) is a nucleosomal histone-lysine N-methyltransferase that specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). It plays a central role in the silencing of euchromatic genes.


Pssm-ID: 380926 [Multi-domain]  Cd Length: 141  Bit Score: 98.42  E-value: 7.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1057 GLKIRLqlfrTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVRE----DDT------YLFDLDNKDrevYCIDA-RF 1125
Cdd:cd10528    18 GLKVIE----IDGKGRGVIATRPFEKGDFVVEYHGDLITITEAKKREalyaKDPstgcymYYFQYKGKT---YCVDAtKE 90
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 156717252 1126 YGNISRFINHLC-EPNLLPVRVFMSHQdlrfPRIGFFSSRHIGAGEEIGFDYGDR 1179
Cdd:cd10528    91 SGRLGRLINHSKkKPNLKTKLLVIDGV----PHLILVAKRDIKPGEELLYDYGDR 141
Ank_2 pfam12796
Ankyrin repeats (3 copies);
715-808 3.21e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.80  E-value: 3.21e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252   715 LHAAAEMGYTDICHMLIQAGANLDSCSEDQRTPLMEAAENNHLDTVKYLVKgGALIDPKDsEGSTCLHLAAKKGHYEVVK 794
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|....
gi 156717252   795 YLLSSErTDVNCQD 808
Cdd:pfam12796   79 LLLEKG-ADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
688-922 3.87e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 103.98  E-value: 3.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  688 ELQKVLMMLVDGIDPNYKMeqhsRRTPLHAAAEMGYTDICHMLIQAGANLDSCSEDQRTPLMEAAENNH-----LDTVKY 762
Cdd:PHA03100   16 KNIKYIIMEDDLNDYSYKK----PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  763 LVKGGALIDPKDSEGSTCLHLAA--KKGHYEVVKYLLSsERTDVNCQDDGGWTPMIWATEYKHV--EIVKLLHSSRADVN 838
Cdd:PHA03100   92 LLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLD-NGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDIN 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  839 IRDNeeniclhwaafagsveiAEILLASKCDLRAVNIHGDSPLHIAARENRHECVMLFLGHGSEVGLKNKEGETPLECSA 918
Cdd:PHA03100  171 AKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233

                  ....
gi 156717252  919 PNSD 922
Cdd:PHA03100  234 LNNN 237
SET_NSD2 cd19211
SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...
1063-1197 9.15e-23

SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) and similar proteins; NSD2 (EC 2.1.1.43; also termed multiple myeloma SET domain-containing protein (MMSET), protein trithorax-5 (TRX5), or wolf-Hirschhorn syndrome candidate 1 protein (WHSC1)) acts as histone-lysine N-methyltransferase with histone H3 'Lys-36' (H3K36me) methyltransferase activity. NSD2 has been shown to mediate di- and trimethylation of H3K36 and dimethylation of H4K20 in different systems, and has been characterized as a transcriptional repressor interacting with histone deacetylase HDAC1 and histone demethylase LSD1. NSD2 mediates constitutive NF-kappaB signaling for cancer cell proliferation, survival and tumor growth. It is highly overexpressed in several types of human cancers, including small-cell lung cancers, neuroblastoma, carcinomas of stomach and colon, and bladder cancers, and its overexpression tends to be associated with tumor aggressiveness. WHSC1 is frequently deleted in Wolf-Hirschhorn syndrome (WHS).


Pssm-ID: 380988 [Multi-domain]  Cd Length: 142  Bit Score: 95.44  E-value: 9.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1063 QLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVR-----EDDT---YLFDLDnKDRevyCIDARFYGNISRFIN 1134
Cdd:cd19211     5 KIIKTEGKGWGLIAKRDIKKGEFVNEYVGELIDEEECMARikhahENDIthfYMLTID-KDR---IIDAGPKGNYSRFMN 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156717252 1135 HLCEPNLLPVRVFMSHQDlrfpRIGFFSSRHIGAGEEIGFDYGdrfWDVKGKLFS-CQCGSPKC 1197
Cdd:cd19211    81 HSCQPNCETQKWTVNGDT----RVGLFAVCDIPAGTELTFNYN---LDCLGNEKTvCRCGAPNC 137
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
1062-1197 2.94e-22

SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) and similar proteins; NSD1 (EC 2.1.1.43; also termed Histone-lysine N-methyltransferase H3 lysine-36 and H4 lysine-20 specific, androgen receptor coactivator 267 kDa protein (ARA267), androgen receptor-associated protein of 267 kDa, H3-K36-HMTase, H4-K20-HMTase, lysine N-methyltransferase 3B (KMT3B), or NR-binding SET domain-containing protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-36' of histone H3 and 'Lys-20' of histone H4. NSD1 is altered in approximately 10% of head and neck cancer patients with 55% decrease in risk of death in NSD1-mutated versus non-mutated patients; its disruption promotes favorable chemotherapeutic responses linked to hypomethylation.


Pssm-ID: 380987 [Multi-domain]  Cd Length: 142  Bit Score: 94.22  E-value: 2.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1062 LQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVR-----EDDT---YLFDLDnKDRevyCIDARFYGNISRFI 1133
Cdd:cd19210     4 VEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIDEEECRARiryaqEHDItnfYMLTLD-KDR---IIDAGPKGNYARFM 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156717252 1134 NHLCEPNLLPVRVFMSHQDlrfpRIGFFSSRHIGAGEEIGFDYGDRFWDvKGKLfSCQCGSPKC 1197
Cdd:cd19210    80 NHCCQPNCETQKWTVNGDT----RVGLFALCDIKAGTELTFNYNLECLG-NGKT-VCKCGAPNC 137
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
1059-1198 4.03e-22

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), 2D (KMT2D) and similar proteins; This family includes KMT2C and KMT2D. Both, KMT2C (also termed HALR or MLL3) and KMT2D (also termed ALR or MLL2), act as histone methyltransferases that methylate 'Lys-4' of histone H3 (H3K4me). They are subunits of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation.


Pssm-ID: 380948 [Multi-domain]  Cd Length: 153  Bit Score: 94.03  E-value: 4.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1059 KIRLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVRED-------DTYLFDLDNKdrevYCIDARFYGNISR 1131
Cdd:cd19171    13 RSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKiyesqnrGIYMFRIDND----WVIDATMTGGPAR 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156717252 1132 FINHLCEPNLLP-VRVFMSHQdlrfpRIGFFSSRHIGAGEEIGFDYGDRFWDVKGKLfSCQCGSPKCK 1198
Cdd:cd19171    89 YINHSCNPNCVAeVVTFDKEK-----KIIIISNRRIAKGEELTYDYKFDFEDDQHKI-PCLCGAPNCR 150
SET_SET1 cd20072
SET domain (including post-SET domain) found in catalytic component of the Saccharomyces ...
1056-1198 8.56e-22

SET domain (including post-SET domain) found in catalytic component of the Saccharomyces cerevisiae COMPASS complex and similar proteins; The family contains mostly fungal SET domains, including SET1 found in the catalytic component of the Saccharomyces cerevisiae COMPASS (complex of proteins associated with Set1). SET1 is a histone-lysine N-methyltransferase that specifically methylates 'Lys-4' of histone H3 (H3K4me), when part of the SET1 histone methyltransferase (HMT) complex. The activity of this catalytic domain is established through forming a complex with a set of core proteins; it is extensively contacted by Cps60 (Bre2), Cps50 (Swd1), and Cps30 (Swd3).


Pssm-ID: 380998  Cd Length: 148  Bit Score: 92.87  E-value: 8.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1056 NGLKIR---LQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVRED--------DTYLFDLDnkdrEVYCIDAR 1124
Cdd:cd20072     6 NQLKKRkkqLKFARSAIHNWGLYAMENISAKDMVIEYVGEVIRQQVADEREKrylrqgigSSYLFRID----DDTVVDAT 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156717252 1125 FYGNISRFINHLCEPNLLPVRVFMSHQDlrfpRIGFFSSRHIGAGEEIGFDYGDRFWDVKgklFSCQCGSPKCK 1198
Cdd:cd20072    82 KKGNIARFINHCCDPNCTAKIIKVEGEK----RIVIYAKRDIAAGEELTYDYKFPREEDK---IPCLCGAPNCR 148
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
1069-1182 1.29e-21

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: 91.63  E-value: 1.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1069 SKGWGVRSLQDIPQGTFVCEYVGELISDAEADVR----EDDTYLFDLDnkDREVYcIDARFYGNISRFINHLCEPNLLPV 1144
Cdd:cd10522    12 HNGLGLFAAETIAKGEFVGEYTGEVLDRWEEDRDsvyhYDPLYPFDLN--GDILV-IDAGKKGNLTRFINHSDQPNLELI 88
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 156717252 1145 rvFMSHQDLrfPRIGFFSSRHIGAGEEIGFDYGDRFWD 1182
Cdd:cd10522    89 --VRTLKGE--QHIGFVAIRDIKPGEELFISYGPKYWK 122
SET_EZH-like cd19168
SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb ...
1071-1180 1.30e-21

SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb repressive complex 2 (PRC2), and similar proteins; The family includes EZH1 and EZH2. EZH1 (EC 2.1.1.43; also termed ENX-2, or histone-lysine N-methyltransferase EZH1) is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. EZH2 (EC 2.1.1.43; also termed lysine N-methyltransferase 6, ENX-1, or histone-lysine N-methyltransferase EZH2) is a catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Both EZH1 and EZH2 can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. PRC2 is involved in several cancers; EZH2 is overexpressed in breast, liver and prostate cancer, while point mutations in EZH2 alter the substrate preference and product specificity of PRC2 in Non-Hodgkin lymphomas (NHLs). Thus, PRC2 is a popular target for cancer therapeutics.


Pssm-ID: 380945  Cd Length: 124  Bit Score: 91.48  E-value: 1.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1071 GWGVRSLQDIPQGTFVCEYVGELISDAEADVRE---DDT---YLFDLDNKdrevYCIDARFYGNISRFINHLCEP----N 1140
Cdd:cd19168    13 GLGLFAAEDIKEGEFVIEYTGELISHDEGVRREhrrGDVsylYLFEEQEG----IWVDAAIYGNLSRYINHATDKvktgN 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 156717252 1141 LLPVRVFMSHQdlrfPRIGFFSSRHIGAGEEIGFDYGDRF 1180
Cdd:cd19168    89 CMPKIMYVNHE----WRIKFTAIKDIKIGEELFFNYGDNF 124
SET_KMT2A_2B cd19170
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...
1050-1198 1.27e-20

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), 2B (KMT2B) and similar proteins; This family includes KMT2A and KMT2B. Both KMT2A (also termed ALL-1 or CXXC7 or MLL or MLL1 or TRX1 or HRX) and KMT2B (also termed MLL4 or TRX2) act as histone methyltransferases that methylate 'Lys-4' of histone H3 (H3K4me).


Pssm-ID: 380947 [Multi-domain]  Cd Length: 152  Bit Score: 89.76  E-value: 1.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1050 RNRVVQNGLKIRLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVRED-------DTYLFDLDnkDREVycID 1122
Cdd:cd19170     4 RFRHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKyyeskgiGCYMFRID--DDEV--VD 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156717252 1123 ARFYGNISRFINHLCEPNLLPvRVFmsHQDLRfPRIGFFSSRHIGAGEEIGFDYGDRFWDVKgklFSCQCGSPKCK 1198
Cdd:cd19170    80 ATMHGNAARFINHSCEPNCYS-RVV--NIDGK-KHIVIFALRRILRGEELTYDYKFPIEDVK---IPCTCGSKKCR 148
PHA03100 PHA03100
ankyrin repeat protein; Provisional
682-874 3.56e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 91.65  E-value: 3.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  682 FSARQGELQKVLMMLVD-GIDPNYKMEQHSRRTPLHAAAEMGYTD---ICHMLIQAGANLDSCSEDQRTPLMEAAEN--N 755
Cdd:PHA03100   40 YLAKEARNIDVVKILLDnGADINSSTKNNSTPLHYLSNIKYNLTDvkeIVKLLLEYGANVNAPDNNGITPLLYAISKksN 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  756 HLDTVKYLVKGGALIDPKDSEGSTCLHLAAKKGHYEV------------------VKYLLSSErTDVNCQDDGGWTPMIW 817
Cdd:PHA03100  120 SYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYG-VPINIKDVYGFTPLHY 198
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 156717252  818 ATEYKHVEIVKLLHSSRADVNIRDNEENICLHWAAFAGSVEIAEILLASKCDLRAVN 874
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
SET_NSD3 cd19212
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
1063-1197 1.03e-18

SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing protein 3 (NSD3) and similar proteins; NSD3 (EC 2.1.1.43; also termed protein whistle, WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1L1), or WHSC1-like protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-4' and 'Lys-27' of histone H3. NSD3 is amplified and overexpressed in multiple cancer types, including acute myeloid leukemia (AML), breast, lung, pancreatic and bladder cancers, as well as squamous cell carcinoma of the head and neck (SCCHN). NSD3 contributes to tumorigenesis by interacting with bromodomain-containing protein 4 (BRD4), the bromodomain and extraterminal (BET) protein, which is a potential therapeutic target in acute myeloid leukemia (AML). NSD3 is amplified in primary tumors and cell lines from breast carcinoma, and can promote the cell viability of small-cell lung cancer and pancreatic ductal adenocarcinoma. High NSD3 expression is implicated in poor grade and heavy smoking history in SCCHN. Thus, NSD3 may serve as a potential druggable target for selective cancer therapy.


Pssm-ID: 380989 [Multi-domain]  Cd Length: 142  Bit Score: 83.82  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1063 QLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVR-----EDDT---YLFDLdNKDRevyCIDARFYGNISRFIN 1134
Cdd:cd19212     5 EIIKTERRGWGLRTKRSIKKGEFVNEYVGELIDEEECRLRikrahENSVtnfYMLTV-TKDR---IIDAGPKGNYSRFMN 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156717252 1135 HLCEPNlLPVRVFMSHQDLrfpRIGFFSSRHIGAGEEIGFDYGdrfWDVKGK-LFSCQCGSPKC 1197
Cdd:cd19212    81 HSCNPN-CETQKWTVNGDV---RVGLFALCDIPAGMELTFNYN---LDCLGNgRTECHCGADNC 137
Ank_2 pfam12796
Ankyrin repeats (3 copies);
815-907 3.01e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 3.01e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252   815 MIWATEYKHVEIVKLLHSSRADVNIRDNEENICLHWAAFAGSVEIAEILLaSKCDLRAVNiHGDSPLHIAARENRHECVM 894
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 156717252   895 LFLGHGSEVGLKN 907
Cdd:pfam12796   79 LLLEKGADINVKD 91
SET_KMT2A cd19206
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...
1050-1198 3.70e-17

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) and similar proteins; KMT2A (EC2.1.1.43; also termed lysine N-methyltransferase 2A, ALL-1, CXXC-type zinc finger protein 7 (CXXC7), myeloid/lymphoid or mixed-lineage leukemia (MLL), myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), trithorax-like protein (TRX1), or zinc finger protein HRX) acts as a histone methyltransferase that plays an essential role in early development and hematopoiesis. It is a catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac).


Pssm-ID: 380983 [Multi-domain]  Cd Length: 154  Bit Score: 79.68  E-value: 3.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1050 RNRVVQNGLKIRLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVRE---DDT----YLFDLDnkDREVycID 1122
Cdd:cd19206     4 RFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREkyyDSKgigcYMFRID--DSEV--VD 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156717252 1123 ARFYGNISRFINHLCEPNLLPVRVFMSHQDlrfpRIGFFSSRHIGAGEEIGFDYGDRFWDVKGKLfSCQCGSPKCK 1198
Cdd:cd19206    80 ATMHGNAARFINHSCEPNCYSRVINIDGQK----HIVIFAMRKIYRGEELTYDYKFPIEDASNKL-PCNCGAKKCR 150
SET_EZH1 cd19217
SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43) ...
1055-1176 6.32e-17

SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43), also termed ENX-2, or histone-lysine N-methyltransferase EZH1, is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. It can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively.


Pssm-ID: 380994  Cd Length: 136  Bit Score: 78.57  E-value: 6.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1055 QNGLKIRLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVRED------DTYLFDLDNKdrevYCIDARFYGN 1128
Cdd:cd19217     1 QRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKvydkymSSFLFNLNND----FVVDATRKGN 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 156717252 1129 ISRFINHLCEPNLLpVRVFMSHQDlrfPRIGFFSSRHIGAGEEIGFDY 1176
Cdd:cd19217    77 KIRFANHSVNPNCY-AKVVMVNGD---HRIGIFAKRAIQQGEELFFDY 120
SET_SETD5-like cd10529
SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...
1073-1176 1.02e-16

SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar proteins; SETD5 is a probable transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. KMT2E (also termed inactive lysine N-methyltransferase 2E or myeloid/lymphoid or mixed-lineage leukemia protein 5 (MLL5)) associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription. The family also includes Saccharomyces cerevisiae SET domain-containing proteins, SET3 and SET4, and Schizosaccharomyces pombe SET3. Most of these family members contain a post-SET domain which harbors a zinc-binding site.


Pssm-ID: 380927  Cd Length: 127  Bit Score: 77.70  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1073 GVRSLQDIPQGTFVCEYVGE--LISDAEADVREDDTY----LFDLDNKDREVyCIDARFYGNISRFINHLCEPN--LLPV 1144
Cdd:cd10529    18 GLVATEDISPGEPILEYKGEvsLRSEFKEDNGFFKRPspfvFFYDGFEGLPL-CVDARKYGNEARFIRRSCRPNaeLRHV 96
                          90       100       110
                  ....*....|....*....|....*....|....
gi 156717252 1145 RVFMShqdlrFPRIGFFSSRHIGAGEEI--GFDY 1176
Cdd:cd10529    97 VVSNG-----ELRLFIFALKDIRKGTEItiPFDY 125
SET_SETD1A cd19204
SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...
1059-1198 1.21e-16

SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and similar proteins; SETD1A (EC2.1.1.43), also termed lysine N-methyltransferase 2F, or Set1/Ash2 histone methyltransferase complex subunit SET1, is a histone-lysine N-methyltransferase that specifically methylates 'Lys-4' of histone H3 (H3K4me), when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. Human SET domain containing protein 1A (hSETD1A) expression occurs at a high rate in hepatocellular carcinoma patients and controls tumor metastasis in breast cancer by activating MMP expression.


Pssm-ID: 380981 [Multi-domain]  Cd Length: 153  Bit Score: 78.53  E-value: 1.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1059 KIRLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVRED--------DTYLFDLDNKDrevyCIDARFYGNIS 1130
Cdd:cd19204    13 KKKLRFGRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQVVADMREKryvqegigSSYLFRVDHDT----IIDATKCGNLA 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156717252 1131 RFINHLCEPNLLPVRVFMSHQDlrfpRIGFFSSRHIGAGEEIGFDYGDRFWDVKgklFSCQCGSPKCK 1198
Cdd:cd19204    89 RFINHCCTPNCYAKVITIESQK----KIVIYSKQPIGVNEEITYDYKFPIEDNK---IPCLCGTENCR 149
PHA02874 PHA02874
ankyrin repeat protein; Provisional
713-914 1.40e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 83.86  E-value: 1.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  713 TPLHAAAEMGYTDICHMLIQAGANLDSCSEDQRTPLMEAAE-----------NNHLDT------------VKYLVKGGAL 769
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKigahdiiklliDNGVDTsilpipciekdmIKTILDCGID 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  770 IDPKDSEGSTCLHLAAKKGHYEVVKYLLSSeRTDVNCQDDGGWTPMIWATEYKHVEIVKLLHSSRADVNIRDNEENICLH 849
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEY-GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156717252  850 WAAFAGSVEIAEILLASKCDLRAVNIHGDSPLHIAARENRheCVMLFLGHGSEVGLKNKEGETPL 914
Cdd:PHA02874  196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR--SAIELLINNASINDQDIDGSTPL 258
SET_EZH2 cd19218
SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...
1057-1176 5.88e-16

SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43), also termed lysine N-methyltransferase 6, or ENX-1, or histone-lysine N-methyltransferase EZH2, is a catalytic subunit of the polycomb repressive complex 2 (PRC2)/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. It can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. PRC2 is involved in several cancers; EZH2 is overexpressed in breast, liver and prostate cancer, while point mutations in EZH2 alter the substrate preference and product specificity of PRC2 in Non-Hodgkin lymphomas (NHLs). Thus, PRC2 is a popular target for cancer therapeutics.


Pssm-ID: 380995  Cd Length: 120  Bit Score: 75.33  E-value: 5.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1057 GLKIRLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVRED--DTY----LFDLDNKdrevYCIDARFYGNIS 1130
Cdd:cd19218     1 GSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKvyDKYmcsfLFNLNND----FVVDATRKGNKI 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 156717252 1131 RFINHLCEPNLLpVRVFMSHQDlrfPRIGFFSSRHIGAGEEIGFDY 1176
Cdd:cd19218    77 RFANHSVNPNCY-AKVMMVNGD---HRIGIFAKRAIQTGEELFFDY 118
PHA03100 PHA03100
ankyrin repeat protein; Provisional
688-842 1.55e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.48  E-value: 1.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  688 ELQKVLmmLVDGIDPNYKMEQHSrrTPLHAAA--EMGYTDICHMLIQAGANLDSCSEDQRTPLMEAAENNHLDT------ 759
Cdd:PHA03100   87 EIVKLL--LEYGANVNAPDNNGI--TPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkll 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  760 ------------VKYLVKGGALIDPKDSEGSTCLHLAAKKGHYEVVKYLLSsERTDVNCQDDGGWTPMIWATEYKHVEIV 827
Cdd:PHA03100  163 idkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLD-LGANPNLVNKYGDTPLHIAILNNNKEIF 241
                         170
                  ....*....|....*
gi 156717252  828 KLLHSSRADVNIRDN 842
Cdd:PHA03100  242 KLLLNNGPSIKTIIE 256
Ank_2 pfam12796
Ankyrin repeats (3 copies);
680-774 1.79e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.79e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252   680 LYFSARQGELQKVLMMLVDGIDPNykMEQHSRRTPLHAAAEMGYTDICHMLIQaGANLDSCsEDQRTPLMEAAENNHLDT 759
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADAN--LQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLK-DNGRTALHYAARSGHLEI 76
                           90
                   ....*....|....*
gi 156717252   760 VKYLVKGGALIDPKD 774
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
SET_KMT2D cd19209
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...
1047-1198 5.72e-15

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) and similar proteins; KMT2D (EC2.1.1.43; also termed lysine N-methyltransferase 2D, ALL1-related protein (ALR), or myeloid/lymphoid or mixed-lineage leukemia protein 2 (MLL2)), acts as histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me). It is a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription. KMT2D is a subunit of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation.


Pssm-ID: 380986 [Multi-domain]  Cd Length: 155  Bit Score: 73.58  E-value: 5.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1047 RNCRNRVVQNGLKIRLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVRED-------DTYLFDLDNKdrevY 1119
Cdd:cd19209     3 KSSQYRRLKTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKiyeeqnrGIYMFRINNE----H 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156717252 1120 CIDARFYGNISRFINHLCEPNLLPVRVFMSHQDlrfpRIGFFSSRHIGAGEEIGFDYGDRFWDVKGKLfSCQCGSPKCK 1198
Cdd:cd19209    79 VIDATLTGGPARYINHSCAPNCVAEVVTFDKED----KIIIISSRRIPKGEELTYDYQFDFEDDQHKI-PCHCGAWNCR 152
SET_KMT2C cd19208
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) ...
1047-1198 9.12e-15

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) and similar proteins; KMT2C (EC2.1.1.43; also termed lysine N-methyltransferase 2C, homologous to ALR protein (HALR) myeloid/lymphoid, or mixed-lineage leukemia protein 3 (MLL3)), acts as a histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me) and may be involved in leukemogenesis and developmental disorder. KMT2C is a catalytic subunit of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation. Overexpression of KMT2C is associated with estrogen receptor-positive breast cancer; KMT2C mediates the estrogen dependence of breast cancer through regulation of estrogen receptor alpha (ERalpha) enhancer function. KMT2C is frequently mutated in certain populations with diffuse-type gastric adenocarcinomas (DGA); its loss promotes epithelial-to-mesenchymal transition (EMT) and is associated with worse overall survival.


Pssm-ID: 380985 [Multi-domain]  Cd Length: 154  Bit Score: 73.12  E-value: 9.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1047 RNCRNRVVQNGLKIRLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVRED-------DTYLFDLDNKdrevY 1119
Cdd:cd19208     2 KSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKlyesqnrGVYMFRIDND----H 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156717252 1120 CIDARFYGNISRFINHLCEPNLLPVRVFMSHQDlrfpRIGFFSSRHIGAGEEIGFDYGDRFWDVKGKLfSCQCGSPKCK 1198
Cdd:cd19208    78 VIDATLTGGPARYINHSCAPNCVAEVVTFEKGH----KIIISSSRRIQKGEELCYDYKFDFEDDQHKI-PCHCGAVNCR 151
PHA02874 PHA02874
ankyrin repeat protein; Provisional
742-922 1.64e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 77.31  E-value: 1.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  742 EDQRTPLMEAAENNHLDTVKYLVKGGALIDPKDSEGSTCLHLAAKKGHYEVVKYLLssertdvncqdDGGWTPMIWATEY 821
Cdd:PHA02874   33 DETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI-----------DNGVDTSILPIPC 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  822 KHVEIVKLLHSSRADVNIRDNEENICLHWAAFAGSVEIAEILLASKCDLRAVNIHGDSPLHIAARENRHECVMLFLGHGS 901
Cdd:PHA02874  102 IEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181
                         170       180
                  ....*....|....*....|.
gi 156717252  902 EVGLKNKEGETPLECSAPNSD 922
Cdd:PHA02874  182 YANVKDNNGESPLHNAAEYGD 202
SET_KMT2B cd19207
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...
1050-1198 3.77e-14

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) and similar proteins; KMT2B (EC2.1.1.43; also termed lysine N-methyltransferase 2B, myeloid/lymphoid or mixed-lineage leukemia protein 4 (MLL2/MLL4), trithorax homolog 2 (TRX2), or WW domain-binding protein 7 (WBP-7)), acts as a histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me). It is required during the transcriptionally active period of oocyte growth for the establishment and/or maintenance of bulk H3K4 trimethylation (H3K4me3), global transcriptional silencing that precedes resumption of meiosis, oocyte survival and normal zygotic genome activation.


Pssm-ID: 380984 [Multi-domain]  Cd Length: 154  Bit Score: 71.21  E-value: 3.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1050 RNRVVQNGLKIRLQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVRED-------DTYLFDLDNKDrevyCID 1122
Cdd:cd19207     4 RFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKfydskgiGCYMFRIDDFD----VVD 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156717252 1123 ARFYGNISRFINHLCEPNLLPVRVFMSHQDlrfpRIGFFSSRHIGAGEEIGFDYGDRFWDVKGKLfSCQCGSPKCK 1198
Cdd:cd19207    80 ATMHGNAARFINHSCEPNCYSRVIHVEGQK----HIVIFALRKIYRGEELTYDYKFPIEDASNKL-PCNCGAKRCR 150
SET_SpSET3-like cd19183
SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...
1073-1184 4.30e-14

SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET domain-containing protein 3 (SETD3) and similar proteins; Schizosaccharomyces pombe SETD3 functions as a transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. It is required for both, gene activation and repression.


Pssm-ID: 380960  Cd Length: 173  Bit Score: 71.67  E-value: 4.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1073 GVRSLQDIPQGTFVCEYVGELISDAEADVREDDTYLFDLDNKDREVY------CIDARFYGNISRFINHLCEPN--LLPV 1144
Cdd:cd19183    15 GLFADRPIPAGDPIQELLGEIGLQSEYIADPENQYQILGAPKPHVFFhpqsplYIDTRRSGSVARFIRRSCRPNaeLVTV 94
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 156717252 1145 RVfmshQDLRFPRIGFFSSRHIGAGEEIGFDYGdrfWDVK 1184
Cdd:cd19183    95 AS----DSGSVLKFVLYASRDISPGEEITIGWD---WDNP 127
PHA02874 PHA02874
ankyrin repeat protein; Provisional
647-843 6.59e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 75.39  E-value: 6.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  647 PSLSQGPVKETLESALlALDSEKPKKLRFhpkqLYFSARQGELQKVLMMLVDGIDPNykMEQHSRRTPLHAAAEMGYTDI 726
Cdd:PHA02874  100 PCIEKDMIKTILDCGI-DVNIKDAELKTF----LHYAIKKGDLESIKMLFEYGADVN--IEDDNGCYPIHIAIKHNFFDI 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  727 CHMLIQAGANLDSCSEDQRTPLMEAAENNHLDTVKYLVKGGALIDPKDSEGSTCLHLAAKkgHYEVVKYLLSSERTdVNC 806
Cdd:PHA02874  173 IKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNAS-IND 249
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 156717252  807 QDDGGWTPMIWATEYK-HVEIVKLLHSSRADVNIRDNE 843
Cdd:PHA02874  250 QDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNK 287
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
1061-1177 1.13e-13

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: 66.89  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1061 RLQLFRTKSKGWGVRSLQDIPQGTFVCeyvgelisdaeadvreddtylfdldnkdrevycidarfygnISRFINHLCEPN 1140
Cdd:cd08161     1 EIRPSTIPGAGFGLFATRDIPKGEVIG-----------------------------------------LARFINHSCEPN 39
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 156717252 1141 LLPVRVFmshqDLRFPRIGFFSSRHIGAGEEIGFDYG 1177
Cdd:cd08161    40 CEFEEVY----VGGKPRVFIVALRDIKAGEELTVDYG 72
PHA02874 PHA02874
ankyrin repeat protein; Provisional
695-886 2.98e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.46  E-value: 2.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  695 MLVDGIDPNYKmeQHSRRTPLHAAAEMGYTDICHMLIQAGANLDSCSEDQRTPLMEAAENNHLDTVKYLVKGGALIDPKD 774
Cdd:PHA02874  110 ILDCGIDVNIK--DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  775 SEGSTCLHLAAKKGHYEVVKYLLS-SERTDVNCQDdgGWTPMIWATEYKHvEIVKLLHSSRAdVNIRDNEENICLHWA-A 852
Cdd:PHA02874  188 NNGESPLHNAAEYGDYACIKLLIDhGNHIMNKCKN--GFTPLHNAIIHNR-SAIELLINNAS-INDQDIDGSTPLHHAiN 263
                         170       180       190
                  ....*....|....*....|....*....|....
gi 156717252  853 FAGSVEIAEILLASKCDLRAVNIHGDSPLHIAAR 886
Cdd:PHA02874  264 PPCDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
PHA02876 PHA02876
ankyrin repeat protein; Provisional
685-921 4.74e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.56  E-value: 4.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  685 RQGELQKVLMMLVDGIDPNYKmEQHSRrTPLHAAAEMGYTDICHMLIQAGANLDSCSEDQRTPLMEAAENNHLDTVKY-- 762
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAK-DIYCI-TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAii 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  763 -------------------------------------------------------------LVKGGALIDPKDSEGSTCL 781
Cdd:PHA02876  232 dnrsninkndlsllkairnedletslllydagfsvnsiddckntplhhasqapslsrlvpkLLERGADVNAKNIKGETPL 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  782 HLAAKKGH-YEVVKYLLsSERTDVNCQDDGGWTPMIWATEY-KHVEIVKLLHSSRADVNIRDNEENICLHWAAFAGSVEI 859
Cdd:PHA02876  312 YLMAKNGYdTENIRTLI-MLGADVNAADRLYITPLHQASTLdRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156717252  860 AEILLASKCDLRAVNIHGDSPLHIA-ARENRHECVMLFLGHGSEVGLKNKEGETPLECSAPNS 921
Cdd:PHA02876  391 INTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKN 453
Ank_4 pfam13637
Ankyrin repeats (many copies);
744-797 7.02e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 64.22  E-value: 7.02e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 156717252   744 QRTPLMEAAENNHLDTVKYLVKGGALIDPKDSEGSTCLHLAAKKGHYEVVKYLL 797
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SET_SETD1B cd19205
SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...
1056-1198 1.32e-12

SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and similar proteins; SETD1B (EC2.1.1.43), also termed lysine N-methyltransferase 2G, is a histone-lysine N-methyltransferase that specifically methylates 'Lys-4' of histone H3 (H3K4me) when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. Loss of SETD1B occurs in up to half the gastric and colorectal cancers, most commonly via SETD1B mutations, while de novo variants in SETD1B are associated with intellectual disability, epilepsy and autism.


Pssm-ID: 380982 [Multi-domain]  Cd Length: 153  Bit Score: 66.62  E-value: 1.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1056 NGLKIR---LQLFRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVRED--------DTYLFDLDNKDrevyCIDAR 1124
Cdd:cd19205     7 NQLKFRkkkLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKryedegigSSYMFRVDHDT----IIDAT 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156717252 1125 FYGNISRFINHLCEPNLLPVRVFMSHQDlrfpRIGFFSSRHIGAGEEIGFDYGdrfWDVKGKLFSCQCGSPKCK 1198
Cdd:cd19205    83 KCGNFARFINHSCNPNCYAKVITVESQK----KIVIYSKQHINVNEEITYDYK---FPIEDVKIPCLCGSENCR 149
Ank_2 pfam12796
Ankyrin repeats (3 copies);
848-926 3.00e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.60  E-value: 3.00e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156717252   848 LHWAAFAGSVEIAEILLASKCDLRAVNIHGDSPLHIAARENRHECVMLFLGHGSevGLKNKEGETPLECSAPNSDVWAA 926
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIV 77
PHA02878 PHA02878
ankyrin repeat protein; Provisional
688-874 6.65e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.52  E-value: 6.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  688 ELQKVLMMLVDGIDPNYKmEQHSRRTPLHAAAEMGYTDICHMLIQAGANLDSCSEDQRTPLMEAAENNHLDTVKYLVKGG 767
Cdd:PHA02878  146 EAEITKLLLSYGADINMK-DRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  768 ALIDPKDSEGSTCLHLAAKK-GHYEVVKYLLssER-TDVNCQDD-GGWTPMiwATEYKHVEIVKLLHSSRADVNIRDNEE 844
Cdd:PHA02878  225 ASTDARDKCGNTPLHISVGYcKDYDILKLLL--EHgVDVNAKSYiLGLTAL--HSSIKSERKLKLLLEYGADINSLNSYK 300
                         170       180       190
                  ....*....|....*....|....*....|.
gi 156717252  845 NICLHWAAFAGS-VEIAEILLASKCDLRAVN 874
Cdd:PHA02878  301 LTPLSSAVKQYLcINIGRILISNICLLKRIK 331
PHA02875 PHA02875
ankyrin repeat protein; Provisional
712-918 7.46e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 68.86  E-value: 7.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  712 RTPLHAAAEMGYTDICHMLIQAGANLDSCSEDQRTPLMEAAENNHLDTVKYLVKGGALIDPKDSEGSTCLHLAAKKGHYE 791
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  792 VVKYLLSSER--TDVNCQDdgGWTPMIWATEYKHVEIVKLLHSSRADVNIRDNEENICLHWAAFAGSVEIAEILLASKCD 869
Cdd:PHA02875   83 AVEELLDLGKfaDDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 156717252  870 LRAVNIHGDSPLHIA-ARENRHECVMLfLGHGSEVGLKNKEGETPLECSA 918
Cdd:PHA02875  161 LDIEDCCGCTPLIIAmAKGDIAICKML-LDSGANIDYFGKNGCVAALCYA 209
PHA02875 PHA02875
ankyrin repeat protein; Provisional
687-902 1.26e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 68.09  E-value: 1.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  687 GELQKVLMMLVDGIDPNYKMeqHSRRTPLHAAAEMGYTDICHMLIQAGANLDSCSEDQRTPLMEAAENNHLDTVKYLVKG 766
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEI--YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  767 GALIDP---KDseGSTCLHLAAKKGHYEVVKYLLS-SERTDVNCQDDggWTPMIWATEYKHVEIVKLLHSSRADVNIRDN 842
Cdd:PHA02875   91 GKFADDvfyKD--GMTPLHLATILKKLDIMKLLIArGADPDIPNTDK--FSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156717252  843 EENICLHWAAFAGSVEIAEILLASKCDLRAVNIHGD-SPLHIAARENRHECVMLFLGHGSE 902
Cdd:PHA02875  167 CGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
Ank_4 pfam13637
Ankyrin repeats (many copies);
711-764 1.75e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 1.75e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 156717252   711 RRTPLHAAAEMGYTDICHMLIQAGANLDSCSEDQRTPLMEAAENNHLDTVKYLV 764
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
747-917 1.87e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.98  E-value: 1.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  747 PLMEAAENNHLDTVKYLVKGGALIDPKDSEGSTCLHLAAKKGHYEVVKYLLSSERtdvncQDDGGWT------------- 813
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSIN-----KCSVFYTlvaikdafnnrnv 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  814 ---PMIWATEYKHV-------------------EIVKLLHSSRADVNIRD-NEENICLHWAAFAGSVEIAEILLASKCDL 870
Cdd:PHA02878  115 eifKIILTNRYKNIqtidlvyidkkskddiieaEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANV 194
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 156717252  871 RAVNIHGDSPLHIAARENRHECVMLFLGHGSEVGLKNKEGETPLECS 917
Cdd:PHA02878  195 NIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
PHA03095 PHA03095
ankyrin-like protein; Provisional
692-914 1.96e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.74  E-value: 1.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  692 VLMMLVDGIDPNYKMEQHsrRTPLHAAAEMG---YTDICHMLIQAGANLDSCSEDQRTPLMEAAEN-NHLDTVKYLVKGG 767
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYG--KTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNaTTLDVIKLLIKAG 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  768 ALIDPKDSEGSTCLH--LAAKKGHYEVVKYLLSsERTDVNCQDDGGWTPMIWATEYKH--VEIVKLLHSSRADVNIRDNE 843
Cdd:PHA03095  108 ADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLR-KGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDR 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  844 ENICLHwaAFAGSV----EIAEILLASKCDLRAVNIHGD-----------------------------------SPLHIA 884
Cdd:PHA03095  187 FRSLLH--HHLQSFkpraRIVRELIRAGCDPAATDMLGNtplhsmatgssckrslvlplliagisinarnrygqTPLHYA 264
                         250       260       270
                  ....*....|....*....|....*....|
gi 156717252  885 ARENRHECVMLFLGHGSEVGLKNKEGETPL 914
Cdd:PHA03095  265 AVFNNPRACRRLIALGADINAVSSDGNTPL 294
Ank_4 pfam13637
Ankyrin repeats (many copies);
777-831 2.69e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.60  E-value: 2.69e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 156717252   777 GSTCLHLAAKKGHYEVVKYLLSSeRTDVNCQDDGGWTPMIWATEYKHVEIVKLLH 831
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
750-1043 3.11e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.78  E-value: 3.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  750 EAAENNHLDTVKYLVKGGALIDPKDSEGSTCLHLAAKKGHYEVVKYLLSSErTDVNCQDDGGWTPMIWATEYKHVEIVKL 829
Cdd:PHA02876  151 ERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYG-ADVNIIALDDLSVLECAVDSKNIDTIKA 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  830 LHSSRADVNIRDneenICLHWAAFAGSVEIAEILLASKCDLRAVNIHGDSPLHIAARE-NRHECVMLFLGHGSEVGLKNK 908
Cdd:PHA02876  230 IIDNRSNINKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNI 305
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  909 EGETPLECSAPNS----------DVWAALSKCQALPEKPTLQEKVVDRdisrgYENIPIPC------VNAED-SELCPVN 971
Cdd:PHA02876  306 KGETPLYLMAKNGydtenirtliMLGADVNAADRLYITPLHQASTLDR-----NKDIVITLlelganVNARDyCDKTPIH 380
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  972 YKYVSQNCVTspLNidrniTHLQYCVCIDDCSSS------NCMCGQ---LSMRCWYDKNGRLLPEFNMLEPPLIFECNHA 1042
Cdd:PHA02876  381 YAAVRNNVVI--IN-----TLLDYGADIEALSQKigtalhFALCGTnpyMSVKTLIDRGANVNSKNKDLSTPLHYACKKN 453

                  .
gi 156717252 1043 C 1043
Cdd:PHA02876  454 C 454
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
746-918 4.34e-11

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 67.35  E-value: 4.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  746 TPLMEAAENNHLDTVKYLVKGGAlIDP--KDSEGSTCLHLAAKKGHYEVVKYLLSSERTDVN----CQDDGGWTPMIWAT 819
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPS-CDLfqRGALGETALHVAALYDNLEAAVVLMEAAPELVNepmtSDLYQGETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  820 EYKHVEIVKLLHSSRADVN--------IRDNEENIC------LHWAAFAGSVEIAEILLASKCDLRAVNIHGDSPLHIAA 885
Cdd:cd22192    98 VNQNLNLVRELIARGADVVspratgtfFRPGPKNLIyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILV 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 156717252  886 RENRHE--CVM--LFL---GHGSEVGL---KNKEGETPLECSA 918
Cdd:cd22192   178 LQPNKTfaCQMydLILsydKEDDLQPLdlvPNNQGLTPFKLAA 220
PHA03095 PHA03095
ankyrin-like protein; Provisional
749-915 2.18e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.66  E-value: 2.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  749 MEAAENNHLDTVKYLVKGGALIDPKDSEGSTCLHLAAKKGHYEVVK--YLLSSERTDVNCQDDGGWTPMIWATEYKHVE- 825
Cdd:PHA03095   19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDivRLLLEAGADVNAPERCGFTPLHLYLYNATTLd 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  826 IVKLLHSSRADVNIRDNEENICLH--WAAFAGSVEIAEILLASKCDLRAVNIHGDSPLHIAARENRH--ECVMLFLGHGS 901
Cdd:PHA03095   99 VIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNAnvELLRLLIDAGA 178
                         170
                  ....*....|....
gi 156717252  902 EVGLKNKEGETPLE 915
Cdd:PHA03095  179 DVYAVDDRFRSLLH 192
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
796-923 1.82e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.35  E-value: 1.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  796 LLSSERTDVNCQDDGGWTPMIWATEYKHVEIVKLLHSSRADVNIRDNEENICLHWAAFAGSVEIAEILLASKCDLRAVNI 875
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 156717252  876 HGDSPLHIAARENRHECVMLFLGHGSEVGLKNKEGETPLECSAPNSDV 923
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133
Ank_4 pfam13637
Ankyrin repeats (many copies);
811-864 5.03e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 5.03e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 156717252   811 GWTPMIWATEYKHVEIVKLLHSSRADVNIRDNEENICLHWAAFAGSVEIAEILL 864
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
1068-1197 3.74e-08

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: 53.15  E-value: 3.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1068 KSKGWGVRSLQDIPQGTFVCEyvgelisdaEADVREDDTYLFDLDNKDREVYCidaRFYGNISRFiNHLCEPNllpVRVF 1147
Cdd:cd20071     7 GSKGRGLVATRDIEPGELILV---------EKPLVSVPSNSFSLTDGLNEIGV---GLFPLASLL-NHSCDPN---AVVV 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 156717252 1148 MSHQDlrfpRIGFFSSRHIGAGEEIGFDYGDRFWDV--------KGKLFSCQCgsPKC 1197
Cdd:cd20071    71 FDGNG----TLRVRALRDIKAGEELTISYIDPLLPRterrrellEKYGFTCSC--PRC 122
PHA02876 PHA02876
ankyrin repeat protein; Provisional
680-903 1.20e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 56.23  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  680 LYFSARQG-ELQKVLMMLVDGIDPNYKMEQHSrrTPLHAAAEMG-YTDICHMLIQAGANLDSCSEDQRTPLMEAAENNHL 757
Cdd:PHA02876  311 LYLMAKNGyDTENIRTLIMLGADVNAADRLYI--TPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNV 388
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  758 DTVKYLVKGGALIDPKDSEGSTCLHLA-AKKGHYEVVKYLLssertdvncqDDGgwtpmiwateykhveivkllhssrAD 836
Cdd:PHA02876  389 VIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLI----------DRG------------------------AN 434
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156717252  837 VNIRDNEENICLHWAAFAG-SVEIAEILLASKCDLRAVNIHGDSPLHIAAreNRHECVMLFLGHGSEV 903
Cdd:PHA02876  435 VNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
Ank_5 pfam13857
Ankyrin repeats (many copies);
762-818 1.82e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 1.82e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 156717252   762 YLVKGGALIDPKDSEGSTCLHLAAKKGHYEVVKYLLsSERTDVNCQDDGGWTPMIWA 818
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
847-897 2.61e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 2.61e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 156717252   847 CLHWAAFAGSVEIAEILLASKCDLRAVNIHGDSPLHIAARENRHECVMLFL 897
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
829-884 2.83e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 2.83e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 156717252   829 LLHSSRADVNIRDNEENICLHWAAFAGSVEIAEILLASKCDLRAVNIHGDSPLHIA 884
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
631-945 4.29e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 54.38  E-value: 4.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  631 PGGTPEPIETPSlgkpPSLSQGPVKETLESALLALDSEKPKKLRFHPKQLYFSARQGELQKVL----MMLVDGIDPNYKM 706
Cdd:cd22194    10 PSGNCDDMDSPQ----SPQDDTPSNPNSPSAELAKEEQRDKKKRLKKVSEAAVEELGELLKELkdlsRRRRKTDVPDFLM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  707 EQHSrrtplhaAAEMGYTdiChmLIQAGANLDSCSEDQRTPLMEAAENNhlDTVKYLVKggALIDPKDSEGSTCLHLAAK 786
Cdd:cd22194    86 HKLT-------ASDTGKT--C--LMKALLNINENTKEIVRILLAFAEEN--GILDRFIN--AEYTEEAYEGQTALNIAIE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  787 KGHYEVVKYLLSSErTDVNCQ-----------DDG---GWTPMIWATEYKHVEIVKLLHS-SRADVNIRDNEENICLHwa 851
Cdd:cd22194   151 RRQGDIVKLLIAKG-ADVNAHakgvffnpkykHEGfyfGETPLALAACTNQPEIVQLLMEkESTDITSQDSRGNTVLH-- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  852 afaGSVEIAEillaskcdlravnihgDSPLHIAARENRHECVMLFLGHGSEVGLKNKEGETPLECSAPNSDVW---AALS 928
Cdd:cd22194   228 ---ALVTVAE----------------DSKTQNDFVKRMYDMILLKSENKNLETIRNNEGLTPLQLAAKMGKAEilkYILS 288
                         330
                  ....*....|....*....
gi 156717252  929 KcqALPEKPT--LQEKVVD 945
Cdd:cd22194   289 R--EIKEKPNrsLSRKFTD 305
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
712-837 4.68e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 4.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  712 RTPLHAAAEMGYTDICHMLIQAGANLDSCSEDQRTPLMEAAENNHLDTVKYLVKGGALIDPKDSEGSTClhLAAKKGHYE 791
Cdd:PLN03192  559 RTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLC--TAAKRNDLT 636
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 156717252  792 VVKYLLsSERTDVNCQDDGGWTPMIWATEYKHVEIVKLLHSSRADV 837
Cdd:PLN03192  637 AMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
1061-1182 1.78e-06

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: 48.02  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1061 RLQLFRTKSKGWGVRSLQDIPQGTFVcEYVGELISDAEADVREDDTYLFD-LDNKDREVYCIdARFYGniSRFiNHLCEP 1139
Cdd:cd10540     1 RLEVKPSTLKGRGVFATRPIKKGEVI-EEAPVIVLPKEEYQHLCKTVLDHyVFSWGDGCLAL-ALGYG--SMF-NHSYTP 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 156717252 1140 NLLPVRVFMSHqdlrfpRIGFFSSRHIGAGEEIGFDYGDRFWD 1182
Cdd:cd10540    76 NAEYEIDFENQ------TIVFYALRDIEAGEELTINYGDDLWD 112
PHA02798 PHA02798
ankyrin-like protein; Provisional
724-844 2.76e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 51.37  E-value: 2.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  724 TDICHMLIQAGANLDSCSEDQRTPLMEAAEN----NH-LDTVKYLVKGGALIDPKDSEGST---CLHLAAKKGHYEVVKY 795
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHmLDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLF 130
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 156717252  796 LLSSErTDVNCQDDGGWTPM-IWATEYKHV--EIVKLLHSSRADVNIRDNEE 844
Cdd:PHA02798  131 MIENG-ADTTLLDKDGFTMLqVYLQSNHHIdiEIIKLLLEKGVDINTHNNKE 181
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
717-922 5.10e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.02  E-value: 5.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  717 AAAEMGYTDICHMLIQAGANLDSCSEDQRTPLMEAAENNHLDTVKYLVKGGALIDPKDSEGSTCLHLAAKKGHYEVVKYL 796
Cdd:PLN03192  531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  797 -----LSSERT--DVNCQddggwtpmiwATEYKHVEIVKLLHSSRADVNIRDNEENICLHWAAFAGSVEIAEILLASKCD 869
Cdd:PLN03192  611 yhfasISDPHAagDLLCT----------AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 156717252  870 LRAVNIHGD-SPLH----IAARENRHECVMLFLGHGSEVGLKNKEGETPLECSAPNSD 922
Cdd:PLN03192  681 VDKANTDDDfSPTElrelLQKRELGHSITIVDSVPADEPDLGRDGGSRPGRLQGTSSD 738
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
827-921 7.18e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 7.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  827 VKLLHSSRADVNIRDNEENICLHWAAFAGSVEIAEILLASKCDLRAVNIHGDSPLHIAARENRHECVMLFLGHGSEvglk 906
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC---- 173
                          90
                  ....*....|....*
gi 156717252  907 NKEGETpleCSAPNS 921
Cdd:PTZ00322  174 HFELGA---NAKPDS 185
PHA02875 PHA02875
ankyrin repeat protein; Provisional
788-981 8.19e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.60  E-value: 8.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  788 GHYEVVKYLLSSeRTDVNCQDDGGWTPMIWATEYKHVEIVKLL--HSSRADVNIRDNEENicLHWAAFAGSVEIAEILLA 865
Cdd:PHA02875   13 GELDIARRLLDI-GINPNFEIYDGISPIKLAMKFRDSEAIKLLmkHGAIPDVKYPDIESE--LHDAVEEGDVKAVEELLD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  866 SKCDLRAVNIH-GDSPLHIAARENRHECVMLFLGHGSEVGLKNKEGETPLECSAPNSDVwaALSKCqALPEKPTLqekvv 944
Cdd:PHA02875   90 LGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI--KGIEL-LIDHKACL----- 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 156717252  945 drDISRGYENIP-IPCVNAEDSELCPV------NYKYVSQN-CVT 981
Cdd:PHA02875  162 --DIEDCCGCTPlIIAMAKGDIAICKMlldsgaNIDYFGKNgCVA 204
Ank_5 pfam13857
Ankyrin repeats (many copies);
868-915 1.40e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.40e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 156717252   868 CDLRAVNIHGDSPLHIAARENRHECVMLFLGHGSEVGLKNKEGETPLE 915
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
SET_ATXR5_6-like cd10539
SET domain found in fungal protein lysine methyltransferase SET5 and similar protein; The ...
1071-1176 1.92e-05

SET domain found in fungal protein lysine methyltransferase SET5 and similar protein; The family includes Arabidopsis thaliana ATXR5 and ATXR6. Both ATXR5 (also termed protein SET DOMAIN GROUP 15, or TRX-related protein 5) and ATXR6 (also termed protein SET DOMAIN GROUP 34, or TRX-related protein 6) function as histone methyltransferase that specifically monomethylates 'Lys-37' of histone H3 (H3K27me1). They are required for chromatin structure and gene silencing.


Pssm-ID: 380937  Cd Length: 138  Bit Score: 45.48  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1071 GWGVRSLQDIPQGTFVCEYVGEL--ISDAEADVREDDTYLFDLDNKDREVYCIDARfYGNISRFI----NHLCE----PN 1140
Cdd:cd10539    15 GFTVEADGFIKDLTIIAEYTGDVdyIRNREFDDNDSIMTLLLAGDPSKSLVICPDK-RGNIARFIsginNHTKDgkkkQN 93
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 156717252 1141 LLPVRVFMSHQdlrfPRIGFFSSRHIGAGEEIGFDY 1176
Cdd:cd10539    94 CKCVRYSINGE----ARVLLVATRDIAKGERLYYDY 125
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
776-809 3.91e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.89  E-value: 3.91e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 156717252   776 EGSTCLHLAAKK-GHYEVVKYLLSSeRTDVNCQDD 809
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSK-GADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
776-806 3.98e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 3.98e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 156717252    776 EGSTCLHLAAKKGHYEVVKYLLsSERTDVNC 806
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLL-DKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
811-842 5.57e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.12  E-value: 5.57e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 156717252   811 GWTPMIWA-TEYKHVEIVKLLHSSRADVNIRDN 842
Cdd:pfam00023    2 GNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
743-832 6.47e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 6.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  743 DQRTPLMEAAENNHL----DTV--KYLVKGGALIDPKDSEGSTCLHLAAKKGHYEVVKYLLSSErTDVNCQDDGGWTPMI 816
Cdd:PTZ00322   75 DPVVAHMLTVELCQLaasgDAVgaRILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLE 153
                          90
                  ....*....|....*.
gi 156717252  817 WATEYKHVEIVKLLHS 832
Cdd:PTZ00322  154 LAEENGFREVVQLLSR 169
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
717-805 6.99e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 6.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  717 AAAEMGYTDICHM-----------LIQAGANLDSCSEDQRTPLMEAAENNHLDTVKYLVKGGALIDPKDSEGSTCLHLAA 785
Cdd:PTZ00322   77 VVAHMLTVELCQLaasgdavgariLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAE 156
                          90       100
                  ....*....|....*....|
gi 156717252  786 KKGHYEVVKYLLSSERTDVN 805
Cdd:PTZ00322  157 ENGFREVVQLLSRHSQCHFE 176
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
745-840 7.00e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.00  E-value: 7.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252   745 RTPLMEAA-ENNHLDTVKYLVKGGALIDpkdsEGSTCLHLAAKKGH---YEVVKYLLSSERTDVN-------CQDD--GG 811
Cdd:TIGR00870   53 RSALFVAAiENENLELTELLLNLSCRGA----VGDTLLHAISLEYVdavEAILLHLLAAFRKSGPlelandqYTSEftPG 128
                           90       100
                   ....*....|....*....|....*....
gi 156717252   812 WTPMIWATEYKHVEIVKLLHSSRADVNIR 840
Cdd:TIGR00870  129 ITALHLAAHRQNYEIVKLLLERGASVPAR 157
Ank_5 pfam13857
Ankyrin repeats (many copies);
803-843 7.46e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 7.46e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 156717252   803 DVNCQDDGGWTPMIWATEYKHVEIVKLLHSSRADVNIRDNE 843
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE 48
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
752-881 7.71e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 47.21  E-value: 7.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  752 AENNHLDTVKYLVKGGALIDPKDSEGSTCLHlaakkghyevvKYLLsseRTDVNcqddggwtpmiwateykhVEIVKLLH 831
Cdd:PHA02716  292 ARNIDISVVYSFLQPGVKLHYKDSAGRTCLH-----------QYIL---RHNIS------------------TDIIKLLH 339
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156717252  832 SSRADVNIRDNEENICLHWAAFAGSV--------------EIAEILLASKCDLRAVNIHGDSPL 881
Cdd:PHA02716  340 EYGNDLNEPDNIGNTVLHTYLSMLSVvnildpetdndirlDVIQCLISLGADITAVNCLGYTPL 403
Ank_5 pfam13857
Ankyrin repeats (many copies);
730-784 1.13e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 1.13e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 156717252   730 LIQAG-ANLDSCSEDQRTPLMEAAENNHLDTVKYLVKGGALIDPKDSEGSTCLHLA 784
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
712-740 1.25e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 1.25e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 156717252   712 RTPLHAAAEM-GYTDICHMLIQAGANLDSC 740
Cdd:pfam00023    3 NTPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
684-763 2.26e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  684 ARQGELQKVLMMLVDGIDPNYKmeQHSRRTPLHAAAEMGYTDICHMLIQAGANLDSCSEDQRTPLMEAAENNHLDTVKYL 763
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCR--DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
712-738 3.19e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 3.19e-04
                            10        20
                    ....*....|....*....|....*..
gi 156717252    712 RTPLHAAAEMGYTDICHMLIQAGANLD 738
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
743-771 3.92e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 3.92e-04
                            10        20
                    ....*....|....*....|....*....
gi 156717252    743 DQRTPLMEAAENNHLDTVKYLVKGGALID 771
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
851-928 3.97e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.86  E-value: 3.97e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156717252  851 AAFAGSVEIAEILLASKCDLRAVNIHGDSPLHIAARENRHECVMLFLGHGSEVGLKNKEGetplecsapNSDVWAALS 928
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANG---------NTALWNAIS 600
Ank_4 pfam13637
Ankyrin repeats (many copies);
877-923 4.12e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 4.12e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 156717252   877 GDSPLHIAARENRHECVMLFLGHGSEVGLKNKEGETPLECSAPNSDV 923
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNV 47
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
876-908 5.39e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 5.39e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 156717252   876 HGDSPLHIAARENRH-ECVMLFLGHGSEVGLKNK 908
Cdd:pfam00023    1 DGNTPLHLAAGRRGNlEIVKLLLSKGADVNARDK 34
RING-HC_PCGF2 cd16734
RING finger found in polycomb group RING finger protein 2 (PCGF2) and similar proteins; PCGF2, ...
515-585 7.43e-04

RING finger found in polycomb group RING finger protein 2 (PCGF2) and similar proteins; PCGF2, also known as DNA-binding protein Mel-18, RING finger protein 110 (RNF110), or zinc finger protein 144 (ZNF144), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR). It serves as the core component of a canonical Polycomb repressive complex 1 (PRC1), which is composed of a chromodomain-containing protein (CBX2, CBX4, CBX6, CBX7 or CBX8) and a Polyhomeotic protein (PHC1, PHC2, or PHC3). Like other PCGF homologs, PCGF2 associates with ring finger protein 2 (RNF2) to form a RNF2-PCGF heterodimer, which is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. Moreover, PCGF2 uniquely regulates PRC1 to specify mesoderm cell fate in embryonic stem cells. It is required for PRC1 stability and maintenance of gene repression in embryonic stem cells (ESCs) and essential for ESC differentiation into early cardiac-mesoderm precursors. PCGF2 also plays a significant role in the angiogenic function of endothelial cells (ECs) by regulating endothelial gene expression. Furthermore, PCGF2 is a SUMO-dependent regulator of hormone receptors. It facilitates the deSUMOylation process by inhibiting PCGF4/BMI1-mediated ubiquitin-proteasomal degradation of SUMO1/sentrin-specific protease 1 (SENP1). It is also a novel negative regulator of breast cancer stem cells (CSCs) that inhibits the stem cell population and in vitro and in vivo self-renewal through the inactivation of Wnt-mediated Notch signaling. PCGF2 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438392 [Multi-domain]  Cd Length: 80  Bit Score: 39.58  E-value: 7.43e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156717252  515 HRGKMVK------HQCCPGCG-YFCTAGTFMECQpdstisHRFHKDCATR-VNNSSYCPHCGEEASKAKEVTIAKADTT 585
Cdd:cd16734     1 HRTTRIKitelnpHLMCALCGgYFIDAATIVECL------HSFCKTCIVRyLETNKYCPMCDVQVHKTRPLLSIRSDKT 73
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
876-903 1.52e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 1.52e-03
                            10        20
                    ....*....|....*....|....*...
gi 156717252    876 HGDSPLHIAARENRHECVMLFLGHGSEV 903
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
SET_KMT2E cd19182
SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...
1074-1177 1.81e-03

SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar proteins; KMT2E (also termed inactive lysine N-methyltransferase 2E, myeloid/lymphoid or mixed-lineage leukemia protein 5 (MLL5)) plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. It associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription. Lack of key residues in the SET domain as well as the presence of an unusually large loop in the SET-I subdomain preclude the interaction of MLL5 SET with its cofactor and substrate thus making MLL5 devoid of any in vitro methyltransferase activity on full-length histones and histone H3 peptide.


Pssm-ID: 380959  Cd Length: 129  Bit Score: 39.88  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1074 VRSLQDIPQGTFVCEYVGE--LISDAEAD----VREDDTYLFDLDNKDREVyCIDARFYGNISRFINHLCEPNlLPVRVF 1147
Cdd:cd19182    21 LKAAKDLPPDTLIIEYRGKfmLREQFEANgyffKRPYPFVLFYSKFHGLEM-CVDARTFGNEARFIRRSCTPN-AEVRHV 98
                          90       100       110
                  ....*....|....*....|....*....|....
gi 156717252 1148 MSHQDLrfpRIGFFSSRHIGAGEEI----GFDYG 1177
Cdd:cd19182    99 IEDGTI---HLYIYSIRSIPKGTEItiafDFDYG 129
SET_SETD5 cd19181
SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...
1057-1140 2.17e-03

SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and similar proteins; SETD5 is a probable transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. SETD5 loss-of-function mutations are a likely cause of a familial syndromic intellectual disability with variable phenotypic expression.


Pssm-ID: 380958  Cd Length: 150  Bit Score: 39.99  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1057 GLKIRLQL---FRTKSKGWGVRSLQDIPQGTFVCEYVGELISDAEADVRE---DDTYLFDL-DNKDREV-YCIDARFYGN 1128
Cdd:cd19181     1 GSQMQLQLgrvTRVQKHRKILRAARDLALDTLIIEYRGKVMLRQQFEVNGhffKRPYPFVLfYSKFNGVeMCVDARTFGN 80
                          90
                  ....*....|..
gi 156717252 1129 ISRFINHLCEPN 1140
Cdd:cd19181    81 DARFIRRSCTPN 92
PHA03095 PHA03095
ankyrin-like protein; Provisional
691-761 2.68e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.93  E-value: 2.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156717252  691 KVLMMLVDGIDPNYkmEQHSRRTPLHAAAEMGYTDICHMLIQAGANLDSCSEDQRTPLMEAAENNHLDTVK 761
Cdd:PHA03095  239 LVLPLLIAGISINA--RNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
811-839 3.03e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 3.03e-03
                            10        20
                    ....*....|....*....|....*....
gi 156717252    811 GWTPMIWATEYKHVEIVKLLHSSRADVNI 839
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
1071-1180 4.88e-03

PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar proteins; PRDM7 (also termed PR domain-containing protein 7) is a primate-specific histone methyltransferase that is the result of a recent gene duplication of PRDM9. It selectively catalyzes the trimethylation of H3 lysine 4 (H3K4me3). PRDM9 (also termed PR domain-containing protein 9) is a histone methyltransferase that specifically trimethylates 'Lys-4' of histone H3 (H3K4me3) during meiotic prophase and is essential for proper meiotic progression. It also efficiently mono-, di-, and trimethylates H3K36. Aberrant PRDM9 expression is assciated with with genome instability in cancer.


Pssm-ID: 380970 [Multi-domain]  Cd Length: 129  Bit Score: 38.37  E-value: 4.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1071 GWGVRSLQDIPQGTFVCEYVGELISDAEAdvrEDDTYLFDLDNKDREVYCIDAR--FYGNISRFIN---HLCEPNLlpvr 1145
Cdd:cd19193    19 GLGVWAEAPIPKGMVFGPYEGEIVEDEEA---ADSGYSWQIYKGGKLSHYIDAKdeSKSNWMRYVNcarNEEEQNL---- 91
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 156717252 1146 VFMSHQDlrfpRIGFFSSRHIGAGEEIGFDYGDRF 1180
Cdd:cd19193    92 VAFQYRG----KIYYRTCKDIAPGTELLVWYGDEY 122
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
743-771 5.58e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.70  E-value: 5.58e-03
                           10        20
                   ....*....|....*....|....*....
gi 156717252   743 DQRTPLMEAAENNHLDTVKYLVKGGALID 771
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA03095 PHA03095
ankyrin-like protein; Provisional
675-799 6.21e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.78  E-value: 6.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252  675 FHPKQLYFSARQGelqKVLMMLVDGIDPNYKMEQHsrRTPLHAAAEMGYTDICHM--LIQAGANLDSCSEDQRTPLMEAA 752
Cdd:PHA03095  191 LHHHLQSFKPRAR---IVRELIRAGCDPAATDMLG--NTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAA 265
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 156717252  753 ENNHLDTVKYLVKGGALIDPKDSEGSTCLHLAAKKGHYEVVKYLLSS 799
Cdd:PHA03095  266 VFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
RING-HC_PCGF4 cd16736
RING finger found in polycomb group RING finger protein 4 (PCGF4) and similar proteins; PCGF4, ...
522-585 7.53e-03

RING finger found in polycomb group RING finger protein 4 (PCGF4) and similar proteins; PCGF4, also known as polycomb complex protein BMI-1 (B cell-specific Moloney murine leukemia virus integration site 1) or RING finger protein 51 (RNF51), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR). It serves as the core component of a canonical Polycomb repressive complex 1 (PRC1), which is composed of a chromodomain-containing protein (CBX2, CBX4, CBX6, CBX7 or CBX8) and a Polyhomeotic protein (PHC1, PHC2, or PHC3), and plays important roles in chromatin compaction and H2AK119 monoubiquitination. PCGF4 associates with the Runx1/CBFbeta transcription factor complex to silence target genes in a PRC2-independent manner. Moreover, PCGF4 is expressed in the hair cells and supporting cells. It can regulate cell survival by controlling mitochondrial function and reactive oxygen species (ROS) level in thymocytes and neurons, thus having an important role in the survival and sensitivity to ototoxic drug of auditory hair cells. Furthermore, PCGF4 controls memory CD4 T-cell survival through direct repression of Noxa gene in an Ink4a- and Arf-independent manner. It is required in neurons to suppress p53-induced apoptosis via regulating the antioxidant defensive response, and also involved in the tumorigenesis of various cancer types. PCGF4 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438394 [Multi-domain]  Cd Length: 97  Bit Score: 37.30  E-value: 7.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156717252  522 HQCCPGCG-YFCTAGTFMECQpdstisHRFHKDCATR-VNNSSYCPHCGEEASKAKEVTIAKADTT 585
Cdd:cd16736    11 HLMCVLCGgYFIDATTIIECL------HSFCKTCIVRyLETSKYCPICDVQVHKTRPLLNIRSDKT 70
SET_Suv4-20-like cd10524
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
1069-1192 7.58e-03

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: 38.03  E-value: 7.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156717252 1069 SKGWGVRSLQDIPQGTFVCEYVGELISDAEADVREDDTYLFDLDNKDREVYCIDARFYGNIsRFINHLCEPN--LLPVRV 1146
Cdd:cd10524    17 HYGAKIIATKPIKKGEKIHELCGCIAELSEEEEALLRPGGNDFSVMYSSRKKCSQLWLGPA-AFINHDCRPNckFVPTGK 95
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 156717252 1147 -FMSHQDLrfprigffssRHIGAGEEIGFDYGDRFWDVKGKlfSCQC 1192
Cdd:cd10524    96 sTACVKVL----------RDIEPGEEITVYYGDNYFGENNE--ECEC 130
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
712-738 8.85e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 8.85e-03
                           10        20
                   ....*....|....*....|....*..
gi 156717252   712 RTPLHAAAEMGYTDICHMLIQAGANLD 738
Cdd:pfam13606    3 NTPLHLAARNGRLEIVKLLLENGADIN 29
RING-HC_PCGF1 cd16733
RING finger, HC subclass, found in polycomb group RING finger protein 1 (PCGF1) and similar ...
524-585 9.75e-03

RING finger, HC subclass, found in polycomb group RING finger protein 1 (PCGF1) and similar proteins; PCGF1, also known as nervous system Polycomb-1 (NSPc1) or RING finger protein 68 (RNF68), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR). It serves as the core component of a noncanonical Polycomb repressive complex 1 (PRC1)-like BCOR complex that also contains RING1, RNF2, RYBP, SKP1, as well as the BCL6 co-repressor BCOR and the histone demethylase KDM2B, and is required to maintain the transcriptionally repressive state of some genes, such as Hox genes, BCL6 and the cyclin-dependent kinase inhibitor, CDKN1A. PCGF1 promotes cell cycle progression and enhances cell proliferation as well. It is a cell growth regulator that acts as a transcriptional repressor of p21Waf1/Cip1 via the retinoid acid response element (RARE element). Moreover, PCGF1 functions as an epigenetic regulator involved in hematopoietic cell differentiation. It cooperates with the transcription factor runt-related transcription factor 1 (Runx1) in regulating differentiation and self-renewal of hematopoietic cells. Furthermore, PCGF1 represents a physical and functional link between Polycomb function and pluripotency. PCGF1 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438391 [Multi-domain]  Cd Length: 71  Bit Score: 36.09  E-value: 9.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156717252  524 CCPGCGYFCTAGTFMECQpdstisHRFHKDCATR-VNNSSYCPHCGEEASKAKEVTIAKADTT 585
Cdd:cd16733    12 CYLCAGYFIDATTITECL------HTFCKSCIVKyLQTSKYCPMCNIKIHETQPLLNLKLDRV 68
 
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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