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Conserved domains on  [gi|157838004|ref|NP_001103156|]
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histone-lysine N-methyltransferase EHMT1 isoform 3 [Mus musculus]

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 ...
981-1211 2.32e-180

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: 529.50  E-value: 2.32e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  981 TNYKYVSQNCVTSPMNIDRNITHLQYCVCVDDCSSSTCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 1060
Cdd:cd10535     1 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1061 RNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 1140
Cdd:cd10535    81 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157838004 1141 SRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLFSCRCGSSKCRHS 1211
Cdd:cd10535   161 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 231
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
461-591 5.47e-67

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: 221.50  E-value: 5.47e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  461 LQEVPLCSCRMETPKSREISTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCG 539
Cdd:cd20905     1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157838004  540 YFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEEAS-KAKEVTIAK 591
Cdd:cd20905    81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
665-921 2.92e-58

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.88  E-value: 2.92e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  665 LESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQSkrSPLHAAAEAGHVDICHMLVQAGANI 744
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEAGADV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  745 DTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNGQmDVNCQDDGGWTPMIW 824
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHL 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  825 ATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFL 904
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
                         250
                  ....*....|....*..
gi 157838004  905 SRDSDVTLKNKEGETPL 921
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 ...
981-1211 2.32e-180

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: 529.50  E-value: 2.32e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  981 TNYKYVSQNCVTSPMNIDRNITHLQYCVCVDDCSSSTCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 1060
Cdd:cd10535     1 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1061 RNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 1140
Cdd:cd10535    81 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157838004 1141 SRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLFSCRCGSSKCRHS 1211
Cdd:cd10535   161 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 231
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
461-591 5.47e-67

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: 221.50  E-value: 5.47e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  461 LQEVPLCSCRMETPKSREISTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCG 539
Cdd:cd20905     1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157838004  540 YFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEEAS-KAKEVTIAK 591
Cdd:cd20905    81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
665-921 2.92e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.88  E-value: 2.92e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  665 LESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQSkrSPLHAAAEAGHVDICHMLVQAGANI 744
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEAGADV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  745 DTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNGQmDVNCQDDGGWTPMIW 824
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHL 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  825 ATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFL 904
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
                         250
                  ....*....|....*..
gi 157838004  905 SRDSDVTLKNKEGETPL 921
Cdd:COG0666   273 LALLLLAAALLDLLTLL 289
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
1071-1193 2.01e-38

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: 139.39  E-value: 2.01e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004   1071 ARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKdgevYCIDARFYGNVSR 1142
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKaydtdgakAFYLFDIDSD----LCIDARRKGNLAR 76
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 157838004   1143 FINHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGERFWD 1193
Cdd:smart00317   77 FINHSCEPNCELLFVEVNGDD----RIVIFALRDIKPGEELTIDYGSDYAN 123
Pre-SET pfam05033
Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines ...
959-1063 1.09e-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: 113.67  E-value: 1.09e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004   959 IARGYERIPIPCVNAVDSELCPTNYKYVSQNCVTSPMNIDRnithLQYCVCvDDCSSSTCMCGQLSM---RCWYDKDGRL 1035
Cdd:pfam05033    1 ISKGKENVPIPVVNEVDDEPPPPDFTYITSYIYPKEFLLII----PQGCDC-GDCSSEKCSCAQLNGgefRFPYDKDGLL 75
                           90       100
                   ....*....|....*....|....*...
gi 157838004  1036 LPEfnmaEPPLIFECNHACSCWRNCRNR 1063
Cdd:pfam05033   76 VPE----SKPPIYECNPLCGCPPSCPNR 99
Ank_2 pfam12796
Ankyrin repeats (3 copies);
755-848 1.62e-29

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 112.90  E-value: 1.62e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004   755 LMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNgqMDVNCQDDgGWTPMIWATEYKHVELV 834
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDN-GRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 157838004   835 KLLLSKGSDINIRD 848
Cdd:pfam12796   78 KLLLEKGADINVKD 91
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
1081-1210 1.82e-27

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 108.51  E-value: 1.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1081 MGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDS-----YLFDLDnkDGEVycIDARFYGNVSRFINHHCEPNLVPV 1155
Cdd:COG2940    16 HGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKeplhtYLFELD--DDGV--IDGALGGNPARFINHSCDPNCEAD 91
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 157838004 1156 RvfmshqdlRFPRIAFFSTRLIQAGEQLGFDYGERFWDvkgKLFSCRCGssKCRH 1210
Cdd:COG2940    92 E--------EDGRIFIVALRDIAAGEELTYDYGLDYDE---EEYPCRCP--NCRG 133
PHA03100 PHA03100
ankyrin repeat protein; Provisional
695-928 1.15e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 108.60  E-value: 1.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  695 ELQKVLLMLVDGIDPNFKMehqsKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNH-----LDAVKY 769
Cdd:PHA03100   16 KNIKYIIMEDDLNDYSYKK----PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  770 LIKAGAQVDPKDAEGSTCLHLAA--KKGHYDVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVEL--VKLLLSKGSDIN 845
Cdd:PHA03100   92 LLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDIN 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  846 IRDNeeniclhwaafsgcvdiAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCAS 925
Cdd:PHA03100  171 AKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233

                  ...
gi 157838004  926 LSS 928
Cdd:PHA03100  234 LNN 236
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
753-924 5.92e-13

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: 73.12  E-value: 5.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  753 TPLMEAAENNHLDAVKYLIKAgAQVDP--KDAEGSTCLHLAAKKGHYDVVQYLLSNGQMDVN----CQDDGGWTPMIWAT 826
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKC-PSCDLfqRGALGETALHVAALYDNLEAAVVLMEAAPELVNepmtSDLYQGETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  827 EYKHVELVKLLLSKGSDIN--------IRDNEENICL---HWAAFSGCV---DIAEILLAAKCDLHAVNIHGDSPLHIAA 892
Cdd:cd22192    98 VNQNLNLVRELIARGADVVspratgtfFRPGPKNLIYygeHPLSFAACVgneEIVRLLIEHGADIRAQDSLGNTVLHILV 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 157838004  893 RENR-------YDcvvLFLSRDSDV------TLKNKEGETPLQCA 924
Cdd:cd22192   178 LQPNktfacqmYD---LILSYDKEDdlqpldLVPNNQGLTPFKLA 219
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
752-847 8.12e-06

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: 50.08  E-value: 8.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004   752 RTPLMEAA-ENNHLDAVKYLIKAGAQVDpkdaEGSTCLHLAAKKGH---YDVVQYLLSNGQMDVN-------CQDD--GG 818
Cdd:TIGR00870   53 RSALFVAAiENENLELTELLLNLSCRGA----VGDTLLHAISLEYVdavEAILLHLLAAFRKSGPlelandqYTSEftPG 128
                           90       100
                   ....*....|....*....|....*....
gi 157838004   819 WTPMIWATEYKHVELVKLLLSKGSDINIR 847
Cdd:TIGR00870  129 ITALHLAAHRQNYEIVKLLLERGASVPAR 157
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
783-813 1.30e-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: 42.96  E-value: 1.30e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 157838004    783 EGSTCLHLAAKKGHYDVVQYLLSNGQmDVNC 813
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA-DINA 30
 
Name Accession Description Interval E-value
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
981-1211 2.32e-180

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: 529.50  E-value: 2.32e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  981 TNYKYVSQNCVTSPMNIDRNITHLQYCVCVDDCSSSTCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 1060
Cdd:cd10535     1 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1061 RNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 1140
Cdd:cd10535    81 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157838004 1141 SRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLFSCRCGSSKCRHS 1211
Cdd:cd10535   161 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 231
SET_EHMT cd10543
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
981-1211 1.64e-164

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: 488.00  E-value: 1.64e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  981 TNYKYVSQNCVTSPMNIDRNITHLQYCVCVDDCSSSTCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 1060
Cdd:cd10543     1 PDFLYVTENCETSPLNIDRNITSLQTCSCRDDCSSDNCVCGRLSVRCWYDKEGRLLPDFNKLDPPLIFECNRACSCWRNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1061 RNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 1140
Cdd:cd10543    81 RNRVVQNGIRYRLQLFRTRGMGWGVRALQDIPKGTFVCEYIGELISDSEADSREDDSYLFDLDNKDGETYCIDARRYGNI 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157838004 1141 SRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLFSCRCGSSKCRHS 1211
Cdd:cd10543   161 SRFINHLCEPNLIPVRVFVEHQDLRFPRIAFFASRDIKAGEELGFDYGEKFWRIKGKYFTCRCGSPKCKYS 231
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
981-1219 1.15e-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: 1.15e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  981 TNYKYVSQNCVTSPMNIDRNITHLQYCVCVDDCSSSTCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 1060
Cdd:cd10533     1 EDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1061 RNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 1140
Cdd:cd10533    81 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNI 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157838004 1141 SRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLFSCRCGSSKCRHSSAALAQRQ 1219
Cdd:cd10533   161 SRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQ 239
SET_SETDB-like cd10538
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
982-1188 6.19e-103

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: 324.71  E-value: 6.19e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  982 NYKYVSQNCVTSPMNIDRNITHLQYCVCVDDCSSSTCMCGQLS-MRCWYDKDGRLLPefnMAEPPLIFECNHACSCWRNC 1060
Cdd:cd10538     2 SFTYIKDNIVGKNVQPFSNIIDSVGCKCKDDCLDSKCACAAESdGIFAYTKNGLLRL---NNSPPPIFECNSKCSCDDDC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1061 RNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE------DSYLFDLDN-----KDGEV 1129
Cdd:cd10538    79 KNRVVQRGLQARLQVFRTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRGKiydksgGSYLFDLDEfsdsdGDGEE 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 157838004 1130 YCIDARFYGNVSRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDYG 1188
Cdd:cd10538   159 LCVDATFCGNVSRFINHSCDPNLFPFNVVIDHDDLRYPRIALFATRDILPGEELTFDYG 217
SET_SETDB1 cd10517
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
953-1209 1.82e-72

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: 243.35  E-value: 1.82e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  953 KTVSRDIARGYERIPIPCVNAVDSELcPTNYKYVSQNCVTSPMNIDRNITHLQYCVCVDDCS-SSTCMCGQLS---MRCW 1028
Cdd:cd10517     3 YYYICDISYGKEGVPIPCVNEIDNSS-PPYVEYSKERIPGKGVNINLDPDFLVGCDCTDGCRdKSKCACQQLTieaTAAT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1029 YDKDG--------RLLPEFnmaEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEY 1100
Cdd:cd10517    82 PGGQInpsagyqyRRLMEK---LPTGVYECNSRCKCDKRCYNRVVQNGLQVRLQVFKTEKKGWGIRCLDDIPKGSFVCIY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1101 VGELISDSEADVREE---DSYLFDLD------------NKDGEVYC--IDARFYGNVSRFINHHCEPNLVPVRVFMSHQD 1163
Cdd:cd10517   159 AGQILTEDEANEEGLqygDEYFAELDyievveklkegyESDVEEHCyiIDAKSEGNLGRYLNHSCSPNLFVQNVFVDTHD 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 157838004 1164 LRFPRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLFSCRCGSSKCR 1209
Cdd:cd10517   239 LRFPWVAFFASRYIRAGTELTWDYNYEVGSVPGKVLYCYCGSSNCR 284
SET_SUV39H cd10542
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
982-1209 1.83e-68

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: 230.26  E-value: 1.83e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  982 NYKYVSQNCVTSPMNIDRNIthLQYCVCVDDC--SSSTCmCGQLS-MRCWYDKDGRLLpeFNMAEPplIFECNHACSCWR 1058
Cdd:cd10542     2 NFQYINDYIPGDGVKIPEDF--LVGCECTEDChnNNPTC-CPAESgVKFAYDKQGRLR--LPPGTP--IYECNSRCKCGP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1059 NCRNRVVQNGLRARLQLYRTQD-MGWGVRSLQDIPLGTFVCEYVGELISDSEADVR------EEDSYLFDLD-NKDGEVY 1130
Cdd:cd10542    75 DCPNRVVQRGRKVPLCIFRTSNgRGWGVKTLEDIKKGTFVMEYVGEIITSEEAERRgkiydaNGRTYLFDLDyNDDDCEY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1131 CIDARFYGNVSRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDY------------GERFWDVKGKl 1198
Cdd:cd10542   155 TVDAAYYGNISHFINHSCDPNLAVYAVWINHLDPRLPRIAFFAKRDIKAGEELTFDYlmtgtggssestIPKPKDVRVP- 233
                         250
                  ....*....|.
gi 157838004 1199 fsCRCGSSKCR 1209
Cdd:cd10542   234 --CLCGSKNCR 242
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
461-591 5.47e-67

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: 221.50  E-value: 5.47e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  461 LQEVPLCSCRMETPKSREISTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCG 539
Cdd:cd20905     1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157838004  540 YFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEEAS-KAKEVTIAK 591
Cdd:cd20905    81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
665-921 2.92e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.88  E-value: 2.92e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  665 LESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQSkrSPLHAAAEAGHVDICHMLVQAGANI 744
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEAGADV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  745 DTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNGQmDVNCQDDGGWTPMIW 824
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHL 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  825 ATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFL 904
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
                         250
                  ....*....|....*..
gi 157838004  905 SRDSDVTLKNKEGETPL 921
Cdd:COG0666   273 LALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
668-947 9.38e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 201.34  E-value: 9.38e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  668 ALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQskRSPLHAAAEAGHVDICHMLVQAGANIDTC 747
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALG--ALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  748 SEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNGqMDVNCQDDGGWTPMIWATE 827
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  828 YKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRD 907
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 157838004  908 SDVTLKNKEGETPLQCASLSSQVWSALQMSKALRDSAPDK 947
Cdd:COG0666   243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
981-1209 4.08e-56

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: 195.21  E-value: 4.08e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  981 TNYKYVSQNCVTSPMNIDRNITHLQYCVCVDD-CSSSTCMCgqlsMRCW---YDKDGRLLPEF-NMAEPplIFECNHACS 1055
Cdd:cd10544     1 PDFQYTPENVPGPGADTDPNEITFPGCDCKTSsCEPETCSC----LRKYgpnYDDDGCLLDFDgKYSGP--VFECNSMCK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1056 CWRNCRNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVR------EEDSYLFDLDN--KDG 1127
Cdd:cd10544    75 CSESCQNRVVQNGLQFKLQVFKTPKKGWGLRTLEFIPKGRFVCEYAGEVIGFEEARRRtksqtkGDMNYIIVLREhlSSG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1128 EVY--CIDARFYGNVSRFINHHCEPNL--VPVRVfmshqDLRFPRIAFFSTRLIQAGEQLGFDYGERF-----------W 1192
Cdd:cd10544   155 KVLetFVDPTYIGNIGRFLNHSCEPNLfmVPVRV-----DSMVPKLALFAARDIVAGEELSFDYSGEFsnsvesvtlarQ 229
                         250
                  ....*....|....*..
gi 157838004 1193 DVKGKLFSCRCGSSKCR 1209
Cdd:cd10544   230 DESKSRKPCLCGAENCR 246
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
1007-1188 5.27e-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: 188.38  E-value: 5.27e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1007 CVCVDDC--SSSTCMCGQL-SMRCWYDKDGRLLpefnmAEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTQDMGW 1083
Cdd:cd10545    24 CDCKNRCtdGASDCACVKKnGGEIPYNFNGRLI-----RAKPAIYECGPLCKCPPSCYNRVTQKGLRYRLEVFKTAERGW 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1084 GVRSLQDIPLGTFVCEYVGELISDSEADVR-EEDSYLFDLDNK------DGEV---------------------YCIDAR 1135
Cdd:cd10545    99 GVRSWDSIPAGSFICEYVGELLDTSEADTRsGNDDYLFDIDNRqtnrgwDGGQrldvgmsdgerssaedeesseFTIDAG 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157838004 1136 FYGNVSRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDYG 1188
Cdd:cd10545   179 SFGNVARFINHSCSPNLFVQCVLYDHNDLRLPRVMLFAADNIPPLQELTYDYG 231
SET_SETDB cd10541
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...
1007-1209 7.97e-51

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: 179.66  E-value: 7.97e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1007 CVCVDDC-SSSTCMCGQLSMRCWYDKDG-----------RLLPEfnmAEPPLIFECNHACSCWRN-CRNRVVQNGLRARL 1073
Cdd:cd10541    18 CDCTDGCrDKSKCACHQLTIQATACTPGgqdnptagyqyKRLEE---CLPTGVYECNKLCKCDPNmCQNRLVQHGLQVRL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1074 QLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEAD---VREEDSYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEP 1150
Cdd:cd10541    95 QLFKTQNKGWGIRCLDDIAKGTFVCIYAGKILTDDFADkegLEMGDEYFANLDHIEESCYIIDAKLEGNLGRYLNHSCSP 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 157838004 1151 NLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLFSCRCGSSKCR 1209
Cdd:cd10541   175 NLFVQNVFVDTHDLRFPWVAFFASKRIKAGTELTWDYNYEVGSVEGKELLCCCGSNECR 233
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
982-1209 2.44e-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: 167.38  E-value: 2.44e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  982 NYKYVSQNCVTSPMNIDRNITHlqyCVCVDDCSSST--CMCGQLSMRCWYDKDGRLLPefnMAEPPlIFECNHACSCWRN 1059
Cdd:cd10525     2 DFVYINEYKVGEGVTLNQVAVG---CECQDCLSQPVggCCPGASKHRFAYNEQGQVKV---RPGLP-IYECNSRCRCGPD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1060 CRNRVVQNGLRARLQLYRTQD-MGWGVRSLQDIPLGTFVCEYVGELISDSEADVR------EEDSYLFDLDNKDgEVYCI 1132
Cdd:cd10525    75 CPNRVVQKGIQYDLCIFRTDNgRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRgqiydrQGATYLFDLDYVE-DVYTV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1133 DARFYGNVSRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDYGERFWDV------------------ 1194
Cdd:cd10525   154 DAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIALFATRTIRAGEELTFDYNMQVDPVdaestkmdsnfglaglpg 233
                         250
                  ....*....|....*...
gi 157838004 1195 ---KGKLFSCRCGSSKCR 1209
Cdd:cd10525   234 spkKRVRIECKCGVRSCR 251
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
1007-1209 6.36e-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: 165.83  E-value: 6.36e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1007 CVCVDdCSSSTCMCGQLSMRCWYDKDGRLlpefnMAEPPL-IFECNHACSCWRNCRNRVVQNGLRARLQLYRTQD-MGWG 1084
Cdd:cd10532    25 CDCSD-CFFGKCCPAEAGVLFAYNEHGQL-----KIPPGTpIYECNSRCKCGPDCPNRVVQKGTQYSLCIFRTSNgRGWG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1085 VRSLQDIPLGTFVCEYVGELISDSEADVREE--DS----YLFDLDNKDGEvYCIDARFYGNVSRFINHHCEPNLVPVRVF 1158
Cdd:cd10532    99 VKTLQKIKKNSFVMEYVGEVITSEEAERRGQfyDSkgitYLFDLDYESDE-FTVDAARYGNVSHFVNHSCDPNLQVFNVF 177
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157838004 1159 MSHQDLRFPRIAFFSTRLIQAGEQLGFDY-----GERFWDV-------KGKLFSCRCGSSKCR 1209
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 ...
1029-1209 1.42e-45

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: 165.05  E-value: 1.42e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1029 YDKDGRLlpefNMAEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDS 1108
Cdd:cd20073    55 YDEYGRV----RANTGSIIYECNENCDCGINCPNRVVQRGRKLPLEIFKTKHKGWGLRCPRFIKAGTFIGVYLGEVITQS 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1109 EADVREED------SYLFDLDNKDGEV---YCIDARFYGNVSRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQA 1179
Cdd:cd20073   131 EAEIRGKKydnvgvTYLFDLDLFEDQVdeyYTVDAQYCGDVTRFINHSCDPNLAIYSVLRDKSDSKIYDLAFFAIKDIPA 210
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 157838004 1180 GEQLGFDYGER----------------FWDVKGKLfSCRCGSSKCR 1209
Cdd:cd20073   211 LEELTFDYSGRnnfdqlgfignrsnskYINLKNKR-PCYCGSANCR 255
SET_SUV39H_DIM5-like cd19473
SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...
1007-1209 3.17e-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: 164.80  E-value: 3.17e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1007 CVCVDD--CSSSTCMCGQ-----------LSMRCWY---DKDGRLLPEFNMAEPPlIFECNHACSCWRNCRNRVVQNGLR 1070
Cdd:cd19473    26 CECTDDedCMYSGCLCLQdvdpdddrdpgKKKNAYHssgAKKGCLRGHMLNSRLP-IYECHEGCACSDDCPNRVVERGRK 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1071 ARLQLYRTQD-MGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDS--------YLFDLDN----------KDGEVYC 1131
Cdd:cd19473   105 VPLQIFRTSDgRGWGVRSTVDIKRGQFVDCYVGEIITPEEAQRRRDAAtiaqrkdvYLFALDKfsdpdsldprLRGDPYE 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1132 IDARFYGNVSRFINHHCEPNLvpvRVFM---SHQDLRFPRIAFFSTRLIQAGEQLGFDY--------GERFWDVKGK-LF 1199
Cdd:cd19473   185 IDGEFMSGPTRFINHSCDPNL---RIFArvgDHADKHIHDLAFFAIKDIPRGTELTFDYvdgvtgldDDAGDEEKEKeMT 261
                         250
                  ....*....|
gi 157838004 1200 SCRCGSSKCR 1209
Cdd:cd19473   262 KCLCGSPKCR 271
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
1007-1209 2.29e-44

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: 161.92  E-value: 2.29e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1007 CVCVDDCSS-STCMCGQLSMR-------------CWYdKDGRLLpefnMAEPPLIFECNHACSCWRN-CRNRVVQNGLRA 1071
Cdd:cd10523    34 CDCTDGCIDiLKCACLQLTARafsksesspskggRGY-KYKRLQ----EPIPSGLYECNVSCKCNRMlCQNRVVQHGLQV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1072 RLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELIS-----------------DSEADVREEDSYLFDLDNKDGEVYCIDA 1134
Cdd:cd10523   109 RLQVFKTEKKGWGVRCLDDIDKGTFVCIYAGRVLSrarspteplppklelpsENEVEVVTSWLILSKKRKLRENVCFLDA 188
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157838004 1135 RFYGNVSRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLFSCRCGSSKCR 1209
Cdd:cd10523   189 SKEGNVGRFLNHSCCPNLFVQNVFVDTHDKNFPWVAFFTNRVVKAGTELTWDYSYDAGTSPEQEIPCLCGVNKCQ 263
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
1071-1193 2.01e-38

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: 139.39  E-value: 2.01e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004   1071 ARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKdgevYCIDARFYGNVSR 1142
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKaydtdgakAFYLFDIDSD----LCIDARRKGNLAR 76
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 157838004   1143 FINHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGERFWD 1193
Cdd:smart00317   77 FINHSCEPNCELLFVEVNGDD----RIVIFALRDIKPGEELTIDYGSDYAN 123
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
1073-1209 2.05e-36

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: 134.30  E-value: 2.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1073 LQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVR--------EEDSYLFDLdnKDGEVycIDARFYGNVSRFI 1144
Cdd:cd10531     2 LELFRTEKKGWGVKAKEDIQKGEFIIEYVGEVIDKKEFKERldeyeelgKSNFYILSL--SDDVV--IDATRKGNLSRFI 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157838004 1145 NHHCEPNLVpVRVFMShqdLRFPRIAFFSTRLIQAGEQLGFDYGerFWDVKGKLFSCRCGSSKCR 1209
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; ...
1073-1209 1.44e-33

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: 126.25  E-value: 1.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1073 LQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDSYLFDLDNkdgevYC--------IDARFYGNVSRFI 1144
Cdd:cd19174     2 LERFRTEDKGWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRMIEQYHNHSHH-----YClnldsgmvIDGYRMGNEARFV 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157838004 1145 NHHCEPNLVPVRVFMSHQdlrfPRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLfSCRCGSSKCR 1209
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), ...
1061-1209 1.00e-32

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: 124.25  E-value: 1.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1061 RNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKdgevYCI 1132
Cdd:cd10518     4 RFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKrydeegggGTYMFRIDED----LVI 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157838004 1133 DARFYGNVSRFINHHCEPNLVpVRVfMSHQDLRfpRIAFFSTRLIQAGEQLGFDYgeRFWDVKGKLFSCRCGSSKCR 1209
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 ...
1071-1209 1.07e-29

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: 115.37  E-value: 1.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1071 ARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDS--------YLFDLDNKDgevyCIDARFYGNVSR 1142
Cdd:cd19172     2 AKVEVFRTEKKGWGLRAAEDLPKGTFVIEYVGEVLDEKEFKRRMKEYaregnrhyYFMALKSDE----IIDATKKGNLSR 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157838004 1143 FINHHCEPNLVpVRVFMSHQDLrfpRIAFFSTRLIQAGEQLGFDYG-ERFWDVKGKlfsCRCGSSKCR 1209
Cdd:cd19172    78 FINHSCEPNCE-TQKWTVNGEL---RVGFFAKRDIPAGEELTFDYQfERYGKEAQK---CYCGSPNCR 138
Pre-SET pfam05033
Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines ...
959-1063 1.09e-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: 113.67  E-value: 1.09e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004   959 IARGYERIPIPCVNAVDSELCPTNYKYVSQNCVTSPMNIDRnithLQYCVCvDDCSSSTCMCGQLSM---RCWYDKDGRL 1035
Cdd:pfam05033    1 ISKGKENVPIPVVNEVDDEPPPPDFTYITSYIYPKEFLLII----PQGCDC-GDCSSEKCSCAQLNGgefRFPYDKDGLL 75
                           90       100
                   ....*....|....*....|....*...
gi 157838004  1036 LPEfnmaEPPLIFECNHACSCWRNCRNR 1063
Cdd:pfam05033   76 VPE----SKPPIYECNPLCGCPPSCPNR 99
Ank_2 pfam12796
Ankyrin repeats (3 copies);
755-848 1.62e-29

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 112.90  E-value: 1.62e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004   755 LMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNgqMDVNCQDDgGWTPMIWATEYKHVELV 834
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDN-GRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 157838004   835 KLLLSKGSDINIRD 848
Cdd:pfam12796   78 KLLLEKGADINVKD 91
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
1082-1188 2.86e-28

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: 110.31  E-value: 2.86e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  1082 GWGVRSLQDIPLGTFVCEYVGE-LISDSEADVREE-----------DSYLFDLDNKDGevYCIDAR--FYGNVSRFINHH 1147
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELlyydklelrlwGPYLFTLDEDSE--YCIDARalYYGNWARFINHS 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 157838004  1148 CEPNLVPVRVFMShqdlRFPRIAFFSTRLIQAGEQLGFDYG 1188
Cdd:pfam00856   79 CDPNCEVRVVYVN----GGPRIVIFALRDIKPGEELTIDYG 115
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
1081-1210 1.82e-27

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 108.51  E-value: 1.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1081 MGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDS-----YLFDLDnkDGEVycIDARFYGNVSRFINHHCEPNLVPV 1155
Cdd:COG2940    16 HGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKeplhtYLFELD--DDGV--IDGALGGNPARFINHSCDPNCEAD 91
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 157838004 1156 RvfmshqdlRFPRIAFFSTRLIQAGEQLGFDYGERFWDvkgKLFSCRCGssKCRH 1210
Cdd:COG2940    92 E--------EDGRIFIVALRDIAAGEELTYDYGLDYDE---EEYPCRCP--NCRG 133
SET_EZH cd10519
SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...
1072-1188 1.79e-26

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: 105.02  E-value: 1.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1072 RLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVRE--ED----SYLFDLDNKdgevYCIDARFYGNVSRFIN 1145
Cdd:cd10519     2 RLLLGKSDVAGWGLFLKEPIKKDEFIGEYTGELISQDEADRRGkiYDkynsSYLFNLNDQ----FVVDATRKGNKIRFAN 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 157838004 1146 HHCEPNLVPvRVFMSHQDlrfPRIAFFSTRLIQAGEQLGFDYG 1188
Cdd:cd10519    78 HSSNPNCYA-KVMMVNGD---HRIGIFAKRDIEAGEELFFDYG 116
SET_ASHR3-like cd19175
SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...
1072-1209 2.31e-25

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: 102.88  E-value: 2.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1072 RLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVR--------EEDSYLFDLDnKDgevYCIDARFYGNVSRF 1143
Cdd:cd19175     1 KMKLVKTEKCGWGLVADEDINAGEFIIEYVGEVIDDKTCEERlwdmkhkgEKNFYMCEID-KD---MVIDATFKGNLSRF 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157838004 1144 INHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYgeRFWDVkGKLFSCRCGSSKCR 1209
Cdd:cd19175    77 INHSCDPNCELQKWQVDGET----RIGVFAIRDIKKGEELTYDY--QFVQF-GADQDCHCGSKNCR 135
SET_NSD cd19173
SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...
1071-1208 2.37e-25

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: 102.78  E-value: 2.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1071 ARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDS--------YLFDLDNKdgevYCIDARFYGNVSR 1142
Cdd:cd19173     2 PPTEPFKTGDRGWGLRTKRDIKKGDFVIEYVGELIDEEECRRRLKKAhennitnfYMLTLDKD----RIIDAGPKGNLSR 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157838004 1143 FINHHCEPNLvPVRVFMSHQDlrfPRIAFFSTRLIQAGEQLGFDYG-ERFWDVKGKlfsCRCGSSKC 1208
Cdd:cd19173    78 FMNHSCQPNC-ETQKWTVNGD---TRVGLFAVRDIPAGEELTFNYNlDCLGNEKKV---CRCGAPNC 137
Ank_2 pfam12796
Ankyrin repeats (3 copies);
722-815 2.83e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 100.96  E-value: 2.83e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004   722 LHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLIKaGAQVDPKDaEGSTCLHLAAKKGHYDVVQ 801
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|....
gi 157838004   802 YLLSNGQmDVNCQD 815
Cdd:pfam12796   79 LLLEKGA-DINVKD 91
PreSET smart00468
N-terminal to some SET domains; A Cys-rich putative Zn2+-binding domain that occurs N-terminal ...
957-1055 4.13e-25

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: 100.57  E-value: 4.13e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004    957 RDIARGYERIPIPCVNAVDSELCPTNYKYVSQNCVTSPMNIDRNITHLQYCVCVDDCSSST-CMCGQLSMRCW-YDKDGR 1034
Cdd:smart00468    2 LDISNGKENVPVPLVNEVDEDPPPPDFEYISEYIYGQGVPIDRSPSPLVGCSCSGDCSSSNkCECARKNGGEFaYELNGG 81
                            90       100
                    ....*....|....*....|.
gi 157838004   1035 LLPEfnmaEPPLIFECNHACS 1055
Cdd:smart00468   82 LRLK----RKPLIYECNSRCS 98
PHA03100 PHA03100
ankyrin repeat protein; Provisional
695-928 1.15e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 108.60  E-value: 1.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  695 ELQKVLLMLVDGIDPNFKMehqsKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNH-----LDAVKY 769
Cdd:PHA03100   16 KNIKYIIMEDDLNDYSYKK----PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  770 LIKAGAQVDPKDAEGSTCLHLAA--KKGHYDVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVEL--VKLLLSKGSDIN 845
Cdd:PHA03100   92 LLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDIN 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  846 IRDNeeniclhwaafsgcvdiAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCAS 925
Cdd:PHA03100  171 AKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233

                  ...
gi 157838004  926 LSS 928
Cdd:PHA03100  234 LNN 236
SET_SETD1 cd19169
SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...
1067-1209 1.62e-23

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: 97.79  E-value: 1.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1067 NGLRAR---LQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE--------DSYLFDLDnkdgEVYCIDAR 1135
Cdd:cd19169     6 NQLKFRkkqLKFAKSRIHDWGLFALEPIAADEMVIEYVGQVIRQSVADEREKryeaigigSSYLFRVD----DDTIIDAT 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157838004 1136 FYGNVSRFINHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGERFWDVKgklFSCRCGSSKCR 1209
Cdd:cd19169    82 KCGNLARFINHSCNPNCYAKIITVESQK----KIVIYSKRPIAVNEEITYDYKFPIEDEK---IPCLCGAPQCR 148
SET_KMT2A_2B cd19170
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...
1061-1209 9.20e-23

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: 95.92  E-value: 9.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1061 RNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE--DS-----YLFDLDnkdgEVYCID 1133
Cdd:cd19170     4 RFRHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKyyESkgigcYMFRID----DDEVVD 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157838004 1134 ARFYGNVSRFINHHCEPNLVPvRVFmsHQDLRfPRIAFFSTRLIQAGEQLGFDYGERFWDVKgklFSCRCGSSKCR 1209
Cdd:cd19170    80 ATMHGNAARFINHSCEPNCYS-RVV--NIDGK-KHIVIFALRRILRGEELTYDYKFPIEDVK---IPCTCGSKKCR 148
PHA03095 PHA03095
ankyrin-like protein; Provisional
699-925 1.70e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 102.41  E-value: 1.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  699 VLLMLVDGIDPNFKMEHqsKRSPLHAAAEAGH---VDICHMLVQAGANIDTCSEDQRTPLMEAAEN-NHLDAVKYLIKAG 774
Cdd:PHA03095   30 VRRLLAAGADVNFRGEY--GKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNaTTLDVIKLLIKAG 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  775 AQVDPKDAEGSTCLH--LAAKKGHYDVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKH--VELVKLLLSKGSDINIRDNE 850
Cdd:PHA03095  108 ADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKG-ADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDR 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  851 ENICLHWAAFSgCVDIAEI---LLAAKCDLHAVNIHGDSPLHIAARENRYDCVVL--FLSRDSDVTLKNKEGETPLQCAS 925
Cdd:PHA03095  187 FRSLLHHHLQS-FKPRARIvreLIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAA 265
SET_SETD8 cd10528
SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2. ...
1063-1190 1.82e-22

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: 94.57  E-value: 1.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1063 RVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE----DS------YLFDLDNKDgevYCI 1132
Cdd:cd10528     9 ELILSGKEEGLKVIEIDGKGRGVIATRPFEKGDFVVEYHGDLITITEAKKREAlyakDPstgcymYYFQYKGKT---YCV 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1133 DA-RFYGNVSRFINHHC-EPNLVPVRVFMSHQdlrfPRIAFFSTRLIQAGEQLGFDYGER 1190
Cdd:cd10528    86 DAtKESGRLGRLINHSKkKPNLKTKLLVIDGV----PHLILVAKRDIKPGEELLYDYGDR 141
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
1082-1193 1.19e-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: 1.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1082 GWGVRSLQDIPLGTFVCEYVGELISD--SEADVREEDSYLFDLDNKDGEVYcIDARFYGNVSRFINHHCEPNLVPVrvFM 1159
Cdd:cd10522    14 GLGLFAAETIAKGEFVGEYTGEVLDRweEDRDSVYHYDPLYPFDLNGDILV-IDAGKKGNLTRFINHSDQPNLELI--VR 90
                          90       100       110
                  ....*....|....*....|....*....|....
gi 157838004 1160 SHQDLrfPRIAFFSTRLIQAGEQLGFDYGERFWD 1193
Cdd:cd10522    91 TLKGE--QHIGFVAIRDIKPGEELFISYGPKYWK 122
SET_EZH-like cd19168
SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb ...
1082-1191 1.90e-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: 91.10  E-value: 1.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1082 GWGVRSLQDIPLGTFVCEYVGELISDSEADVRE------EDSYLFDLDNKdgevYCIDARFYGNVSRFINHHCEP----N 1151
Cdd:cd19168    13 GLGLFAAEDIKEGEFVIEYTGELISHDEGVRREhrrgdvSYLYLFEEQEG----IWVDAAIYGNLSRYINHATDKvktgN 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 157838004 1152 LVPVRVFMSHQdlrfPRIAFFSTRLIQAGEQLGFDYGERF 1191
Cdd:cd19168    89 CMPKIMYVNHE----WRIKFTAIKDIKIGEELFFNYGDNF 124
SET_SET1 cd20072
SET domain (including post-SET domain) found in catalytic component of the Saccharomyces ...
1067-1209 7.03e-21

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: 90.18  E-value: 7.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1067 NGLRAR---LQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE--------DSYLFDLDnkdgEVYCIDAR 1135
Cdd:cd20072     6 NQLKKRkkqLKFARSAIHNWGLYAMENISAKDMVIEYVGEVIRQQVADEREKrylrqgigSSYLFRID----DDTVVDAT 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157838004 1136 FYGNVSRFINHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGERFWDVKgklFSCRCGSSKCR 1209
Cdd:cd20072    82 KKGNIARFINHCCDPNCTAKIIKVEGEK----RIVIYAKRDIAAGEELTYDYKFPREEDK---IPCLCGAPNCR 148
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
1070-1209 1.00e-20

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: 90.18  E-value: 1.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1070 RARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVRE---EDS----YLFDLDNKdgevYCIDARFYGNVSR 1142
Cdd:cd19171    13 RSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREkiyESQnrgiYMFRIDND----WVIDATMTGGPAR 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157838004 1143 FINHHCEPNLVP-VRVFMSHQdlrfpRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLfSCRCGSSKCR 1209
Cdd:cd19171    89 YINHSCNPNCVAeVVTFDKEK-----KIIIISNRRIAKGEELTYDYKFDFEDDQHKI-PCLCGAPNCR 150
PHA03100 PHA03100
ankyrin repeat protein; Provisional
689-881 1.67e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 95.89  E-value: 1.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  689 FSARQGELQKVLLMLVD-GIDPNFKMEHQSkrSPLHAAAEAGHV-----DICHMLVQAGANIDTCSEDQRTPLMEAAEN- 761
Cdd:PHA03100   40 YLAKEARNIDVVKILLDnGADINSSTKNNS--TPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKk 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  762 -NHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDV------------------VQYLLSNGqMDVNCQDDGGWTPM 822
Cdd:PHA03100  118 sNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYG-VPINIKDVYGFTPL 196
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 157838004  823 IWATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVN 881
Cdd:PHA03100  197 HYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
SET_KMT2A cd19206
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...
1061-1209 2.94e-19

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: 85.84  E-value: 2.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1061 RNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE--DS-----YLFDLDnkDGEVycID 1133
Cdd:cd19206     4 RFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREKyyDSkgigcYMFRID--DSEV--VD 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157838004 1134 ARFYGNVSRFINHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLfSCRCGSSKCR 1209
Cdd:cd19206    80 ATMHGNAARFINHSCEPNCYSRVINIDGQK----HIVIFAMRKIYRGEELTYDYKFPIEDASNKL-PCNCGAKKCR 150
Ank_2 pfam12796
Ankyrin repeats (3 copies);
822-914 5.73e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 5.73e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004   822 MIWATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLaAKCDLHAVNiHGDSPLHIAARENRYDCVV 901
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 157838004   902 LFLSRDSDVTLKN 914
Cdd:pfam12796   79 LLLEKGADINVKD 91
SET_NSD2 cd19211
SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...
1074-1208 6.06e-19

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: 84.66  E-value: 6.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1074 QLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVR-----EEDS---YLFDLDnKDgevYCIDARFYGNVSRFIN 1145
Cdd:cd19211     5 KIIKTEGKGWGLIAKRDIKKGEFVNEYVGELIDEEECMARikhahENDIthfYMLTID-KD---RIIDAGPKGNYSRFMN 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157838004 1146 HHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGerfWDVKGKLFS-CRCGSSKC 1208
Cdd:cd19211    81 HSCQPNCETQKWTVNGDT----RVGLFAVCDIPAGTELTFNYN---LDCLGNEKTvCRCGAPNC 137
PHA02874 PHA02874
ankyrin repeat protein; Provisional
728-926 4.03e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 88.48  E-value: 4.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  728 AGHVDICHMLVQAGAN-IDTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSN 806
Cdd:PHA02874   11 SGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  807 G----------------------QMDVNCQDDGGWTPMIWATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCV 864
Cdd:PHA02874   91 GvdtsilpipciekdmiktildcGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFF 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157838004  865 DIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASL 926
Cdd:PHA02874  171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
687-781 1.62e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 1.62e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004   687 LYFSARQGELQKVLLMLVDGIDPNFKmeHQSKRSPLHAAAEAGHVDICHMLVQaGANIDtCSEDQRTPLMEAAENNHLDA 766
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ--DKNGRTALHLAAKNGHLEIVKLLLE-HADVN-LKDNGRTALHYAARSGHLEI 76
                           90
                   ....*....|....*
gi 157838004   767 VKYLIKAGAQVDPKD 781
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
720-924 1.99e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 86.56  E-value: 1.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  720 SPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLI-----------------------KAGAQ 776
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIdngvdtsilpipciekdmiktilDCGID 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  777 VDPKDAEGSTCLHLAAKKGHYDVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVELVKLLLSKGSDINIRDNEENICLH 856
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  857 WAAFSGCVDIAEILL------AAKCD-----LHAVNIH--------------------GDSPLHIAAREN-RYDCVVLFL 904
Cdd:PHA02874  196 NAAEYGDYACIKLLIdhgnhiMNKCKngftpLHNAIIHnrsaiellinnasindqdidGSTPLHHAINPPcDIDIIDILL 275
                         250       260
                  ....*....|....*....|
gi 157838004  905 SRDSDVTLKNKEGETPLQCA 924
Cdd:PHA02874  276 YHKADISIKDNKGENPIDTA 295
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
1073-1208 2.34e-17

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: 79.97  E-value: 2.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1073 LQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVR-----EEDS---YLFDLDnKDgevYCIDARFYGNVSRFI 1144
Cdd:cd19210     4 VEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIDEEECRARiryaqEHDItnfYMLTLD-KD---RIIDAGPKGNYARFM 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157838004 1145 NHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGERFWDvKGKLfSCRCGSSKC 1208
Cdd:cd19210    80 NHCCQPNCETQKWTVNGDT----RVGLFALCDIKAGTELTFNYNLECLG-NGKT-VCKCGAPNC 137
SET_EZH1 cd19217
SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43) ...
1066-1187 2.39e-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: 79.73  E-value: 2.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1066 QNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE------DSYLFDLDNKdgevYCIDARFYGN 1139
Cdd:cd19217     1 QRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKvydkymSSFLFNLNND----FVVDATRKGN 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 157838004 1140 VSRFINHHCEPNLVpVRVFMSHQDlrfPRIAFFSTRLIQAGEQLGFDY 1187
Cdd:cd19217    77 KIRFANHSVNPNCY-AKVVMVNGD---HRIGIFAKRAIQQGEELFFDY 120
SET_EZH2 cd19218
SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...
1068-1187 2.69e-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: 76.10  E-value: 2.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1068 GLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREED------SYLFDLDNKdgevYCIDARFYGNVS 1141
Cdd:cd19218     1 GSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVydkymcSFLFNLNND----FVVDATRKGNKI 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 157838004 1142 RFINHHCEPNLVpVRVFMSHQDlrfPRIAFFSTRLIQAGEQLGFDY 1187
Cdd:cd19218    77 RFANHSVNPNCY-AKVMMVNGD---HRIGIFAKRAIQTGEELFFDY 118
PHA03095 PHA03095
ankyrin-like protein; Provisional
756-921 7.32e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 81.99  E-value: 7.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  756 MEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHY---DVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVE 832
Cdd:PHA03095   19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAG-ADVNAPERCGFTPLHLYLYNATTL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  833 -LVKLLLSKGSDINIRDNEENICLHWAAFSGCVD--IAEILLAAKCDLHAVNIHGDSPLHIAARENRYD--CVVLFLSRD 907
Cdd:PHA03095   98 dVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLLIDAG 177
                         170
                  ....*....|....
gi 157838004  908 SDVTLKNKEGETPL 921
Cdd:PHA03095  178 ADVYAVDDRFRSLL 191
SET_KMT2C cd19208
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) ...
1058-1209 7.83e-16

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: 76.20  E-value: 7.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1058 RNCRNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE-------DSYLFDLDNKdgevY 1130
Cdd:cd19208     2 KSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKlyesqnrGVYMFRIDND----H 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157838004 1131 CIDARFYGNVSRFINHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLfSCRCGSSKCR 1209
Cdd:cd19208    78 VIDATLTGGPARYINHSCAPNCVAEVVTFEKGH----KIIISSSRRIQKGEELCYDYKFDFEDDQHKI-PCHCGAVNCR 151
PHA02874 PHA02874
ankyrin repeat protein; Provisional
702-920 1.07e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 81.16  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  702 MLVDGIDPNFKmeHQSKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKD 781
Cdd:PHA02874  110 ILDCGIDVNIK--DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  782 AEGSTCLHLAAKKGHYDVVQYLLSNG-QMDVNCQDdgGWTPMIWATEYKHvELVKLLLSKGSdINIRDNEENICLHWAAF 860
Cdd:PHA02874  188 NNGESPLHNAAEYGDYACIKLLIDHGnHIMNKCKN--GFTPLHNAIIHNR-SAIELLINNAS-INDQDIDGSTPLHHAIN 263
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157838004  861 SGC-VDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSrdSDVTLKNKEGETP 920
Cdd:PHA02874  264 PPCdIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDII--ANAVLIKEADKLK 322
SET_KMT2B cd19207
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...
1061-1209 2.60e-15

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: 74.67  E-value: 2.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1061 RNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE-------DSYLFDLDNKDgevyCID 1133
Cdd:cd19207     4 RFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKfydskgiGCYMFRIDDFD----VVD 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157838004 1134 ARFYGNVSRFINHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLfSCRCGSSKCR 1209
Cdd:cd19207    80 ATMHGNAARFINHSCEPNCYSRVIHVEGQK----HIVIFALRKIYRGEELTYDYKFPIEDASNKL-PCNCGAKRCR 150
SET_KMT2D cd19209
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...
1058-1209 3.48e-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: 74.35  E-value: 3.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1058 RNCRNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE-------DSYLFDLDNKdgevY 1130
Cdd:cd19209     3 KSSQYRRLKTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKiyeeqnrGIYMFRINNE----H 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157838004 1131 CIDARFYGNVSRFINHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLfSCRCGSSKCR 1209
Cdd:cd19209    79 VIDATLTGGPARYINHSCAPNCVAEVVTFDKED----KIIIISSRRIPKGEELTYDYQFDFEDDQHKI-PCHCGAWNCR 152
SET_SETD1A cd19204
SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...
1070-1209 3.76e-15

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: 73.91  E-value: 3.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1070 RARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKDgevyCIDARFYGNVS 1141
Cdd:cd19204    13 KKKLRFGRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQVVADMREKryvqegigSSYLFRVDHDT----IIDATKCGNLA 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157838004 1142 RFINHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGERFWDVKgklFSCRCGSSKCR 1209
Cdd:cd19204    89 RFINHCCTPNCYAKVITIESQK----KIVIYSKQPIGVNEEITYDYKFPIEDNK---IPCLCGTENCR 149
SET_NSD3 cd19212
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
1074-1208 4.18e-15

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: 73.42  E-value: 4.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1074 QLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVR----EEDS----YLFDLdNKDgevYCIDARFYGNVSRFIN 1145
Cdd:cd19212     5 EIIKTERRGWGLRTKRSIKKGEFVNEYVGELIDEEECRLRikraHENSvtnfYMLTV-TKD---RIIDAGPKGNYSRFMN 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157838004 1146 HHCEPNlVPVRVFMSHQDLrfpRIAFFSTRLIQAGEQLGFDYGerfWDVKGK-LFSCRCGSSKC 1208
Cdd:cd19212    81 HSCNPN-CETQKWTVNGDV---RVGLFALCDIPAGMELTFNYN---LDCLGNgRTECHCGADNC 137
PHA02876 PHA02876
ankyrin repeat protein; Provisional
692-966 6.69e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 79.72  E-value: 6.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  692 RQGELQKVLLMLVDGIDPNFKMEHQskRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLI 771
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYC--ITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  772 ---------------------------------------------------------------KAGAQVDPKDAEGSTCL 788
Cdd:PHA02876  232 dnrsninkndlsllkairnedletslllydagfsvnsiddckntplhhasqapslsrlvpkllERGADVNAKNIKGETPL 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  789 HLAAKKGhYDV--VQYLLSNGQmDVNCQDDGGWTPMIWATEY-KHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCVD 865
Cdd:PHA02876  312 YLMAKNG-YDTenIRTLIMLGA-DVNAADRLYITPLHQASTLdRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVV 389
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  866 IAEILLAAKCDLHAVNIHGDSPLHIA-ARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLSSqvwSALQMSKALRDSA 944
Cdd:PHA02876  390 IINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKN---CKLDVIEMLLDNG 466
                         330       340
                  ....*....|....*....|...
gi 157838004  945 PD-KPVAVEKTVSRDIARGYERI 966
Cdd:PHA02876  467 ADvNAINIQNQYPLLIALEYHGI 489
PHA02878 PHA02878
ankyrin repeat protein; Provisional
721-985 3.90e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 76.46  E-value: 3.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  721 PLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVD-------------PKDAEGSTC 787
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSvfytlvaikdafnNRNVEIFKI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  788 LHLAAKKGHYD------------------VVQYLLSNGQmDVNCQD-DGGWTPMIWATEYKHVELVKLLLSKGSDINIRD 848
Cdd:PHA02878  120 ILTNRYKNIQTidlvyidkkskddiieaeITKLLLSYGA-DINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPD 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  849 NEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIA-ARENRYDCVVLFLSRDSDVTLKNK-EGETPLQCASL 926
Cdd:PHA02878  199 KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIK 278
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157838004  927 SSQVWSALQMSKA---LRDSAPDKP--VAVEKtvsrdiargyeRIPIPCVNAVDSELCPTNYKY 985
Cdd:PHA02878  279 SERKLKLLLEYGAdinSLNSYKLTPlsSAVKQ-----------YLCINIGRILISNICLLKRIK 331
SET_SETD5-like cd10529
SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...
1084-1187 4.23e-14

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: 70.00  E-value: 4.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1084 GVRSLQDIPLGTFVCEYVGELISDSEADVREE-----DSYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEPNlVPVRVF 1158
Cdd:cd10529    18 GLVATEDISPGEPILEYKGEVSLRSEFKEDNGffkrpSPFVFFYDGFEGLPLCVDARKYGNEARFIRRSCRPN-AELRHV 96
                          90       100       110
                  ....*....|....*....|....*....|.
gi 157838004 1159 MSHQDlrFPRIAFFSTRLIQAGEQ--LGFDY 1187
Cdd:cd10529    97 VVSNG--ELRLFIFALKDIRKGTEitIPFDY 125
SET_SpSET3-like cd19183
SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...
1084-1195 6.47e-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: 70.89  E-value: 6.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1084 GVRSLQDIPLGTFVCEYVGELISdseadvreEDSYLFDLDNKDGE-------VY-------CIDARFYGNVSRFINHHCE 1149
Cdd:cd19183    15 GLFADRPIPAGDPIQELLGEIGL--------QSEYIADPENQYQIlgapkphVFfhpqsplYIDTRRSGSVARFIRRSCR 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 157838004 1150 PN--LVPVRVfmshQDLRFPRIAFFSTRLIQAGEQLGFDYGerfWDVK 1195
Cdd:cd19183    87 PNaeLVTVAS----DSGSVLKFVLYASRDISPGEEITIGWD---WDNP 127
PHA02875 PHA02875
ankyrin repeat protein; Provisional
694-965 8.44e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 75.03  E-value: 8.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  694 GELQKVLLMLVDGIDPNFKMehQSKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLIKA 773
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEI--YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  774 GAQVDP---KDaeGSTCLHLAAKKGHYDVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVELVKLLLSKGSDINIRDNE 850
Cdd:PHA02875   91 GKFADDvfyKD--GMTPLHLATILKKLDIMKLLIARGA-DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  851 ENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGD-SPLHIAARENRYDCVVLFLSRDSD---VTLKNKEGETPLQ---- 922
Cdd:PHA02875  168 GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADcniMFMIEGEECTILDmicn 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 157838004  923 -CASLSSQVWSALQMSKALRDSapdkpvavEKTVSRDiaRGYER 965
Cdd:PHA02875  248 mCTNLESEAIDALIADIAIRIH--------KKTIRRD--EGFKN 281
Ank_4 pfam13637
Ankyrin repeats (many copies);
751-804 9.45e-14

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 66.53  E-value: 9.45e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 157838004   751 QRTPLMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLL 804
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
719-771 1.41e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 66.14  E-value: 1.41e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 157838004   719 RSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLI 771
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
695-875 2.29e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 74.15  E-value: 2.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  695 ELQKVLLMLVDGIDPNFKMEHQSKrSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLIKAG 774
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHKGN-TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  775 AQVDPKDAEGSTCLHLAAKK-GHYDVVQYLLSNGqMDVNCQDD-GGWTPMIWATEYKHVelVKLLLSKGSDINIRDNEEN 852
Cdd:PHA02878  225 ASTDARDKCGNTPLHISVGYcKDYDILKLLLEHG-VDVNAKSYiLGLTALHSSIKSERK--LKLLLEYGADINSLNSYKL 301
                         170       180
                  ....*....|....*....|....
gi 157838004  853 ICLHWAAFS-GCVDIAEILLAAKC 875
Cdd:PHA02878  302 TPLSSAVKQyLCINIGRILISNIC 325
SET_SETD1B cd19205
SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...
1070-1209 3.84e-13

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: 68.16  E-value: 3.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1070 RARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKDgevyCIDARFYGNVS 1141
Cdd:cd19205    13 KKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKryedegigSSYMFRVDHDT----IIDATKCGNFA 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157838004 1142 RFINHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGerfWDVKGKLFSCRCGSSKCR 1209
Cdd:cd19205    89 RFINHSCNPNCYAKVITVESQK----KIVIYSKQHINVNEEITYDYK---FPIEDVKIPCLCGSENCR 149
PHA02874 PHA02874
ankyrin repeat protein; Provisional
687-850 4.84e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 72.69  E-value: 4.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  687 LYFSARQGELQKVLLMLVDGIDPNfkMEHQSKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDA 766
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVN--IEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  767 VKYLIKAGAQVDPKDAEGSTCLHLAAKKGHyDVVQYLLSNGQmdVNCQDDGGWTPMIWATEYK-HVELVKLLLSKGSDIN 845
Cdd:PHA02874  206 IKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNAS--INDQDIDGSTPLHHAINPPcDIDIIDILLYHKADIS 282

                  ....*
gi 157838004  846 IRDNE 850
Cdd:PHA02874  283 IKDNK 287
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
753-924 5.92e-13

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: 73.12  E-value: 5.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  753 TPLMEAAENNHLDAVKYLIKAgAQVDP--KDAEGSTCLHLAAKKGHYDVVQYLLSNGQMDVN----CQDDGGWTPMIWAT 826
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKC-PSCDLfqRGALGETALHVAALYDNLEAAVVLMEAAPELVNepmtSDLYQGETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  827 EYKHVELVKLLLSKGSDIN--------IRDNEENICL---HWAAFSGCV---DIAEILLAAKCDLHAVNIHGDSPLHIAA 892
Cdd:cd22192    98 VNQNLNLVRELIARGADVVspratgtfFRPGPKNLIYygeHPLSFAACVgneEIVRLLIEHGADIRAQDSLGNTVLHILV 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 157838004  893 RENR-------YDcvvLFLSRDSDV------TLKNKEGETPLQCA 924
Cdd:cd22192   178 LQPNktfacqmYD---LILSYDKEDdlqpldLVPNNQGLTPFKLA 219
PHA02875 PHA02875
ankyrin repeat protein; Provisional
686-871 2.72e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.41  E-value: 2.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  686 QLYFSARQGELQKV--LLMLVDGIDPNFkmeHQSKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNH 763
Cdd:PHA02875   71 ELHDAVEEGDVKAVeeLLDLGKFADDVF---YKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGD 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  764 LDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNGQMDVNCQDDGGWTPMIWATEYKHVELVKLLLSKGSD 843
Cdd:PHA02875  148 IKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 157838004  844 INIR---DNEE--------NICLHWAAFSGCVDIAEILL 871
Cdd:PHA02875  228 CNIMfmiEGEEctildmicNMCTNLESEAIDALIADIAI 266
Ank_4 pfam13637
Ankyrin repeats (many copies);
784-838 3.27e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 62.29  E-value: 3.27e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 157838004   784 GSTCLHLAAKKGHYDVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVELVKLLL 838
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
1072-1188 6.94e-12

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: 61.88  E-value: 6.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1072 RLQLYRTQDMGWGVRSLQDIPLGTFVCeyvgelisdseadvreedsylfdldnkdgevycidarfygnVSRFINHHCEPN 1151
Cdd:cd08161     1 EIRPSTIPGAGFGLFATRDIPKGEVIG-----------------------------------------LARFINHSCEPN 39
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 157838004 1152 LVPVRVFmshqDLRFPRIAFFSTRLIQAGEQLGFDYG 1188
Cdd:cd08161    40 CEFEEVY----VGGKPRVFIVALRDIKAGEELTVDYG 72
PHA03095 PHA03095
ankyrin-like protein; Provisional
699-880 2.30e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.74  E-value: 2.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  699 VLLMLVDGIDPNFKMEHQskRSPLHAAAEAGHVDI--CHMLVQAGANIDTCSEDQRTPLMEAAENNHLDA--VKYLIKAG 774
Cdd:PHA03095  135 IRLLLRKGADVNALDLYG--MTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRAriVRELIRAG 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  775 AQVDPKDAEGSTCLHLAAKKG---HYDVVQYLLSNgqMDVNCQDDGGWTPMIWATEYKHVELVKLLLSKGSDINIRDNEE 851
Cdd:PHA03095  213 CDPAATDMLGNTPLHSMATGSsckRSLVLPLLIAG--ISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG 290
                         170       180
                  ....*....|....*....|....*....
gi 157838004  852 NICLHWAAFSGCVDIAEILLAAKCDLHAV 880
Cdd:PHA03095  291 NTPLSLMVRNNNGRAVRAALAKNPSAETV 319
PHA02876 PHA02876
ankyrin repeat protein; Provisional
718-943 3.27e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.78  E-value: 3.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  718 KRSPLHAAAEAGHVD-ICHMLVQAGANIDTCSEDQRTPLMEAAENNH-LDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKG 795
Cdd:PHA02876  273 KNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLD 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  796 HY-DVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAF-SGCVDIAEILLAA 873
Cdd:PHA02876  353 RNkDIVITLLELGA-NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCgTNPYMSVKTLIDR 431
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157838004  874 KCDLHAVNIHGDSPLHIAAREN-RYDCVVLFLSRDSDVTLKNKEGETPLQCA-SLSSQVWSALQMSKALRDS 943
Cdd:PHA02876  432 GANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAlEYHGIVNILLHYGAELRDS 503
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
652-931 4.17e-11

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: 67.48  E-value: 4.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  652 PTSGLSQGPGKETLESALIALDSEKPKKLRFHPKQLYFSARQGELQKV---LLMLVDGIDPNFKMEHQSKrsplhaAAEA 728
Cdd:cd22194    20 PQSPQDDTPSNPNSPSAELAKEEQRDKKKRLKKVSEAAVEELGELLKElkdLSRRRRKTDVPDFLMHKLT------ASDT 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  729 GHVdiChmLVQAGANIDTCSEDQRTPLMEAAENNhlDAVKYLIKAgaQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNGQ 808
Cdd:cd22194    94 GKT--C--LMKALLNINENTKEIVRILLAFAEEN--GILDRFINA--EYTEEAYEGQTALNIAIERRQGDIVKLLIAKGA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  809 mDVNCQ-----------DDG---GWTPMIWATEYKHVELVKLLLSKGSD-INIRDNEENICLHwaafsGCVDIAEillaa 873
Cdd:cd22194   166 -DVNAHakgvffnpkykHEGfyfGETPLALAACTNQPEIVQLLMEKESTdITSQDSRGNTVLH-----ALVTVAE----- 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157838004  874 kcdlhavnihgDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLSSQVW 931
Cdd:cd22194   235 -----------DSKTQNDFVKRMYDMILLKSENKNLETIRNNEGLTPLQLAAKMGKAE 281
PHA02876 PHA02876
ankyrin repeat protein; Provisional
757-921 1.02e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.24  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  757 EAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVELVKL 836
Cdd:PHA02876  151 ERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGA-DVNIIALDDLSVLECAVDSKNIDTIKA 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  837 LLSKGSDINIRDneenICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVV-LFLSRDSDVTLKNK 915
Cdd:PHA02876  230 IIDNRSNINKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVpKLLERGADVNAKNI 305

                  ....*.
gi 157838004  916 EGETPL 921
Cdd:PHA02876  306 KGETPL 311
PHA02798 PHA02798
ankyrin-like protein; Provisional
731-851 2.78e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 61.00  E-value: 2.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  731 VDICHMLVQAGANIDTCSEDQRTPLMEAAEN----NH-LDAVKYLIKAGAQVDPKDAEGST---CLHLAAKKGHYDVVQY 802
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHmLDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLF 130
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157838004  803 LLSNGqMDVNCQDDGGWTPM-IWATEYKHV--ELVKLLLSKGSDINIRDNEE 851
Cdd:PHA02798  131 MIENG-ADTTLLDKDGFTMLqVYLQSNHHIdiEIIKLLLEKGVDINTHNNKE 181
Ank_4 pfam13637
Ankyrin repeats (many copies);
854-904 3.74e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 3.74e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 157838004   854 CLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFL 904
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
720-931 5.30e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.65  E-value: 5.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  720 SPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDV 799
Cdd:PLN03192  527 SNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKI 606
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  800 VQYL-----LSNGQM--DVNCQddggwtpmiwATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLA 872
Cdd:PLN03192  607 FRILyhfasISDPHAagDLLCT----------AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157838004  873 AKCDLHAVNIHGD-SPLH----IAARENRYDCVVLFLSRDSDVTLKNKEGETP--LQCASLSSQVW 931
Cdd:PLN03192  677 NGADVDKANTDDDfSPTElrelLQKRELGHSITIVDSVPADEPDLGRDGGSRPgrLQGTSSDNQCR 742
Ank_4 pfam13637
Ankyrin repeats (many copies);
818-871 2.89e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 2.89e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 157838004   818 GWTPMIWATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILL 871
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
719-844 3.65e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 3.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  719 RSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTClhLAAKKGHYD 798
Cdd:PLN03192  559 RTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLC--TAAKRNDLT 636
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 157838004  799 VVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVELVKLLLSKGSDI 844
Cdd:PLN03192  637 AMKELLKQG-LNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_5 pfam13857
Ankyrin repeats (many copies);
803-850 4.92e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 4.92e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 157838004   803 LLSNGQMDVNCQDDGGWTPMIWATEYKHVELVKLLLSKGSDINIRDNE 850
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE 48
Ank_5 pfam13857
Ankyrin repeats (many copies);
770-825 6.54e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.04  E-value: 6.54e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157838004   770 LIKAG-AQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNGQmDVNCQDDGGWTPMIWA 825
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGV-DLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
795-992 7.44e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 7.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  795 GHYDVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAK 874
Cdd:PHA02875   13 GELDIARRLLDIG-INPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  875 CDLHAVNIH-GDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLSSQVwsalQMSKALrdsapdkpvaVEK 953
Cdd:PHA02875   92 KFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI----KGIELL----------IDH 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 157838004  954 TVSRDIARGYERIP-IPCVNAVDSELCP------TNYKYVSQN-CVT 992
Cdd:PHA02875  158 KACLDIEDCCGCTPlIIAMAKGDIAICKmlldsgANIDYFGKNgCVA 204
Ank_5 pfam13857
Ankyrin repeats (many copies);
870-924 1.81e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 1.81e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 157838004   870 LLAAK-CDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCA 924
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
1082-1208 1.24e-06

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: 48.53  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1082 GWGVRSLQDIPlgtfvceyVGELISDSEADVREEDSYLFDLDNKDGEVYCIdarfYGNVSRFiNHHCEPNlvpVRVFMSH 1161
Cdd:cd20071    10 GRGLVATRDIE--------PGELILVEKPLVSVPSNSFSLTDGLNEIGVGL----FPLASLL-NHSCDPN---AVVVFDG 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 157838004 1162 QDlrfpRIAFFSTRLIQAGEQLGFDYGERFWDV--------KGKLFSCRCgsSKC 1208
Cdd:cd20071    74 NG----TLRVRALRDIKAGEELTISYIDPLLPRterrrellEKYGFTCSC--PRC 122
Ank_5 pfam13857
Ankyrin repeats (many copies);
837-891 1.69e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 1.69e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 157838004   837 LLSKGS-DINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIA 891
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SET_ATXR5_6-like cd10539
SET domain found in fungal protein lysine methyltransferase SET5 and similar protein; The ...
1082-1189 1.78e-06

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: 48.56  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1082 GWGVRSLQDIPLGTFVCEYVGEL--ISDSEADvrEEDSYLFDLDNKDGE---VYCIDARfyGNVSRFI----NHHCE--- 1149
Cdd:cd10539    15 GFTVEADGFIKDLTIIAEYTGDVdyIRNREFD--DNDSIMTLLLAGDPSkslVICPDKR--GNIARFIsginNHTKDgkk 90
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 157838004 1150 -PNLVPVRVFMSHQdlrfPRIAFFSTRLIQAGEQLGFDYGE 1189
Cdd:cd10539    91 kQNCKCVRYSINGE----ARVLLVATRDIAKGERLYYDYNG 127
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
731-812 2.10e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 2.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  731 VDICHM-----------LVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDV 799
Cdd:PTZ00322   84 VELCQLaasgdavgariLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163
                          90
                  ....*....|...
gi 157838004  800 VQYLLSNGQMDVN 812
Cdd:PTZ00322  164 VQLLSRHSQCHFE 176
PHA03100 PHA03100
ankyrin repeat protein; Provisional
720-782 7.01e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.05  E-value: 7.01e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157838004  720 SPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKDA 782
Cdd:PHA03100  194 TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
818-849 7.64e-06

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: 43.82  E-value: 7.64e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 157838004   818 GWTPMIWA-TEYKHVELVKLLLSKGSDINIRDN 849
Cdd:pfam00023    2 GNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
750-839 7.74e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 7.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  750 DQRTPLMEAAENNHLDA------VKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNGQmDVNCQDDGGWTPMI 823
Cdd:PTZ00322   75 DPVVAHMLTVELCQLAAsgdavgARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA-DPTLLDKDGKTPLE 153
                          90
                  ....*....|....*.
gi 157838004  824 WATEYKHVELVKLLLS 839
Cdd:PTZ00322  154 LAEENGFREVVQLLSR 169
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
752-847 8.12e-06

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: 50.08  E-value: 8.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004   752 RTPLMEAA-ENNHLDAVKYLIKAGAQVDpkdaEGSTCLHLAAKKGH---YDVVQYLLSNGQMDVN-------CQDD--GG 818
Cdd:TIGR00870   53 RSALFVAAiENENLELTELLLNLSCRGA----VGDTLLHAISLEYVdavEAILLHLLAAFRKSGPlelandqYTSEftPG 128
                           90       100
                   ....*....|....*....|....*....
gi 157838004   819 WTPMIWATEYKHVELVKLLLSKGSDINIR 847
Cdd:TIGR00870  129 ITALHLAAHRQNYEIVKLLLERGASVPAR 157
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
783-813 1.30e-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: 42.96  E-value: 1.30e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 157838004    783 EGSTCLHLAAKKGHYDVVQYLLSNGQmDVNC 813
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA-DINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
783-816 1.68e-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: 42.66  E-value: 1.68e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 157838004   783 EGSTCLHLAAKK-GHYDVVQYLLSNGQmDVNCQDD 816
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGA-DVNARDK 34
PHA02989 PHA02989
ankyrin repeat protein; Provisional
701-874 1.80e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 48.97  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  701 LMLVDGIDPNfKMEHQSKRSPLHAAAEAGHV--DICHMLVQAGANI-DTCSEDQRTP----LMEAAENNHLDAVKYLIKA 773
Cdd:PHA02989  129 FLLSKGINVN-DVKNSRGYNLLHMYLESFSVkkDVIKILLSFGVNLfEKTSLYGLTPmniyLRNDIDVISIKVIKYLIKK 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  774 GAQVDPKDAEGSTCL------HLAAKKGHYDVVQYLLSngQMDVNCQDDGGWTPMIWATEYKHVELVKLLLSKGSDINIR 847
Cdd:PHA02989  208 GVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILK--YIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNV 285
                         170       180
                  ....*....|....*....|....*..
gi 157838004  848 DNEENICLHWAAFSGCVDIAEILLAAK 874
Cdd:PHA02989  286 SKDGDTVLTYAIKHGNIDMLNRILQLK 312
Ank_5 pfam13857
Ankyrin repeats (many copies);
737-791 2.03e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 2.03e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 157838004   737 LVQAG-ANIDTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLA 791
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
834-905 4.15e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 4.15e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157838004  834 VKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLS 905
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
884-936 4.81e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 4.81e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 157838004   884 GDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLSSQVwSALQM 936
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNV-EVLKL 52
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
759-921 5.07e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 47.60  E-value: 5.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  759 AENNHLDAVKYLIKAGAQVDPKDAEGSTCLHlaakkghydvvQYLLSNgqmdvncqddggwtpmiwateYKHVELVKLLL 838
Cdd:PHA02716  292 ARNIDISVVYSFLQPGVKLHYKDSAGRTCLH-----------QYILRH---------------------NISTDIIKLLH 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  839 SKGSDINIRDNEENICLHwaafsgcvdiaeILLAAKCDLHAVNIHGDSPLhiaarenRYDCVVLFLSRDSDVTLKNKEGE 918
Cdd:PHA02716  340 EYGNDLNEPDNIGNTVLH------------TYLSMLSVVNILDPETDNDI-------RLDVIQCLISLGADITAVNCLGY 400

                  ...
gi 157838004  919 TPL 921
Cdd:PHA02716  401 TPL 403
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
719-745 5.16e-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: 5.16e-05
                            10        20
                    ....*....|....*....|....*..
gi 157838004    719 RSPLHAAAEAGHVDICHMLVQAGANID 745
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
818-846 5.27e-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: 5.27e-05
                            10        20
                    ....*....|....*....|....*....
gi 157838004    818 GWTPMIWATEYKHVELVKLLLSKGSDINI 846
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02989 PHA02989
ankyrin repeat protein; Provisional
698-924 6.43e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 47.04  E-value: 6.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  698 KVLLMLVD-GIDPNFK--MEhqskrSPLHAAAEAGHVD------ICHMLVQAGANIDTCSEDQRTPLMEAAEN---NHLD 765
Cdd:PHA02989   51 KIVKLLIDnGADVNYKgyIE-----TPLCAVLRNREITsnkikkIVKLLLKFGADINLKTFNGVSPIVCFIYNsniNNCD 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  766 AVKYLIKAGAQV-DPKDAEGSTCLH--LAAKKGHYDVVQYLLSNGQMDVNCQDDGGWTPM-IW---ATEYKHVELVKLLL 838
Cdd:PHA02989  126 MLRFLLSKGINVnDVKNSRGYNLLHmyLESFSVKKDVIKILLSFGVNLFEKTSLYGLTPMnIYlrnDIDVISIKVIKYLI 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  839 SKGSDInirdnEENICLHWAAFSGCVDIAEILLAaKC-----------DLHAVNIHGDSPLHIAARENRYDCVVLFLSRD 907
Cdd:PHA02989  206 KKGVNI-----ETNNNGSESVLESFLDNNKILSK-KEfkvlnfilkyiKINKKDKKGFNPLLISAKVDNYEAFNYLLKLG 279
                         250
                  ....*....|....*..
gi 157838004  908 SDVTLKNKEGETPLQCA 924
Cdd:PHA02989  280 DDIYNVSKDGDTVLTYA 296
SET_SETD5 cd19181
SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...
1068-1151 6.54e-05

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: 44.61  E-value: 6.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1068 GLRARLQL---YRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVRE---EDSYLFDL--DNKDGEVYCIDARFYGN 1139
Cdd:cd19181     1 GSQMQLQLgrvTRVQKHRKILRAARDLALDTLIIEYRGKVMLRQQFEVNGhffKRPYPFVLfySKFNGVEMCVDARTFGN 80
                          90
                  ....*....|..
gi 157838004 1140 VSRFINHHCEPN 1151
Cdd:cd19181    81 DARFIRRSCTPN 92
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
691-772 9.16e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 9.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  691 ARQGELQKVLLMLVDGIDPNFKMEHQskRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYL 770
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDG--RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167

                  ..
gi 157838004  771 IK 772
Cdd:PTZ00322  168 SR 169
Ank_2 pfam12796
Ankyrin repeats (3 copies);
888-930 9.27e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.41  E-value: 9.27e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 157838004   888 LHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLSSQV 930
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHL 43
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
750-778 9.49e-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: 40.65  E-value: 9.49e-05
                            10        20
                    ....*....|....*....|....*....
gi 157838004    750 DQRTPLMEAAENNHLDAVKYLIKAGAQVD 778
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
867-924 1.02e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 1.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157838004  867 AEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCA 924
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
791-913 1.22e-04

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: 46.23  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004   791 AAKKGHYDVVQYLLSNGQMD-VNCQDDGGWTPMIW-ATEYKHVELVKLLLSKGSDINIRDNeeniCLHWAA---FSGCVD 865
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKKLnINCPDRLGRSALFVaAIENENLELTELLLNLSCRGAVGDT----LLHAISleyVDAVEA 99
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 157838004   866 IAEILLAAKCD----LHAVNI------HGDSPLHIAARENRYDCVVLFLSRDSDVTLK 913
Cdd:TIGR00870  100 ILLHLLAAFRKsgplELANDQytseftPGITALHLAAHRQNYEIVKLLLERGASVPAR 157
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
719-745 1.79e-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: 39.97  E-value: 1.79e-04
                           10        20
                   ....*....|....*....|....*...
gi 157838004   719 RSPLHAAAE-AGHVDICHMLVQAGANID 745
Cdd:pfam00023    3 NTPLHLAAGrRGNLEIVKLLLSKGADVN 30
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
1072-1193 1.85e-04

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: 42.24  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1072 RLQLYRTQDMGWGVRSLQDIPLGTFVcEYVGELISDSEADVREEDSYLFDLdnkdgeVYCIDARFY----GNVSRFiNHH 1147
Cdd:cd10540     1 RLEVKPSTLKGRGVFATRPIKKGEVI-EEAPVIVLPKEEYQHLCKTVLDHY------VFSWGDGCLalalGYGSMF-NHS 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 157838004 1148 CEPNLVPVRVFMSHqdlrfpRIAFFSTRLIQAGEQLGFDYGERFWD 1193
Cdd:cd10540    73 YTPNAEYEIDFENQ------TIVFYALRDIEAGEELTINYGDDLWD 112
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
750-781 2.47e-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: 39.58  E-value: 2.47e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 157838004   750 DQRTPLMEAAE-NNHLDAVKYLIKAGAQVDPKD 781
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
SET_KMT2E cd19182
SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...
1085-1188 2.59e-04

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: 42.19  E-value: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1085 VRSLQDIPLGTFVCEYVGELISDSEAdvrEEDSYLFD--------LDNKDGEVYCIDARFYGNVSRFINHHCEPNlVPVR 1156
Cdd:cd19182    21 LKAAKDLPPDTLIIEYRGKFMLREQF---EANGYFFKrpypfvlfYSKFHGLEMCVDARTFGNEARFIRRSCTPN-AEVR 96
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 157838004 1157 VFMSHQDLrfpRIAFFSTRLIQAGEQL----GFDYG 1188
Cdd:cd19182    97 HVIEDGTI---HLYIYSIRSIPKGTEItiafDFDYG 129
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
750-778 4.27e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 4.27e-04
                           10        20
                   ....*....|....*....|....*....
gi 157838004   750 DQRTPLMEAAENNHLDAVKYLIKAGAQVD 778
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
883-912 6.01e-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: 38.34  E-value: 6.01e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 157838004    883 HGDSPLHIAARENRYDCVVLFLSRDSDVTL 912
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
744-890 6.53e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.50  E-value: 6.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  744 IDTCSEDQRTPLMEAAENNH--LDAVKYLIKAGAQVDPK-DAEGSTCLH--LAAKKG-HYDVVQYLLSNGQmDVNCQDDG 817
Cdd:PHA02859   44 VNDCNDLYETPIFSCLEKDKvnVEILKFLIENGADVNFKtRDNNLSALHhyLSFNKNvEPEILKILIDSGS-SITEEDED 122
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157838004  818 GWTPM-IWATEYK-HVELVKLLLSKGSDINIRDNEENICLH-WAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHI 890
Cdd:PHA02859  123 GKNLLhMYMCNFNvRINVIKLLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNCYDL 198
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
789-871 6.96e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 6.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  789 HLAAKkGHYDVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAE 868
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGA-DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                  ...
gi 157838004  869 ILL 871
Cdd:PTZ00322  166 LLS 168
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
883-915 7.21e-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: 38.04  E-value: 7.21e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 157838004   883 HGDSPLHIAA-RENRYDCVVLFLSRDSDVTLKNK 915
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
818-846 1.13e-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: 37.62  E-value: 1.13e-03
                           10        20
                   ....*....|....*....|....*....
gi 157838004   818 GWTPMIWATEYKHVELVKLLLSKGSDINI 846
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
783-813 1.43e-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: 37.24  E-value: 1.43e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 157838004   783 EGSTCLHLAAKKGHYDVVQYLLSNGqMDVNC 813
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENG-ADINA 30
PHA02884 PHA02884
ankyrin repeat protein; Provisional
785-893 1.99e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 41.89  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  785 STCLHLAAKKGHYDVVQYLLSNGqMDVNCQ----DDGGWTPMIWATEYKHVELVKLLLSKGSDINIRDNEENIC-LHWAA 859
Cdd:PHA02884   34 ANILYSSIKFHYTDIIDAILKLG-ADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITpLYISV 112
                          90       100       110
                  ....*....|....*....|....*....|....
gi 157838004  860 FSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAAR 893
Cdd:PHA02884  113 LHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
PHA02741 PHA02741
hypothetical protein; Provisional
780-891 2.07e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 40.41  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  780 KDAEGSTCLHLAAKKGHYDVVQ----YLLSNG-QMDVNCQDDGGWTPMIWATEyKH-----VELVKLLLSKGSDINIRDN 849
Cdd:PHA02741   17 KNSEGENFFHEAARCGCFDIIArftpFIRGDChAAALNATDDAGQMCIHIAAE-KHeaqlaAEIIDHLIELGADINAQEM 95
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 157838004  850 -EENICLHWAAFSGCVDIAEILL-AAKCDLHAVNIHGDSPLHIA 891
Cdd:PHA02741   96 lEGDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFELA 139
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
719-746 2.12e-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: 36.85  E-value: 2.12e-03
                           10        20
                   ....*....|....*....|....*...
gi 157838004   719 RSPLHAAAEAGHVDICHMLVQAGANIDT 746
Cdd:pfam13606    3 NTPLHLAARNGRLEIVKLLLENGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
687-896 3.51e-03

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: 41.61  E-value: 3.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004   687 LYFSARQGELQKVLLMLvdgidPNFKMEHQSKRSPLHAAAEaGHVDIC-----HMLVQAG-------AN---IDTCSEDQ 751
Cdd:TIGR00870   56 LFVAAIENENLELTELL-----LNLSCRGAVGDTLLHAISL-EYVDAVeaillHLLAAFRksgplelANdqyTSEFTPGI 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004   752 rTPLMEAAENNHLDAVKYLIKAGAQVdPKDAEGSTCLhlaaKKGHYDVVQYllsngqmdvncqddgGWTPMIWATEYKHV 831
Cdd:TIGR00870  130 -TALHLAAHRQNYEIVKLLLERGASV-PARACGDFFV----KSQGVDSFYH---------------GESPLNAAACLGSP 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004   832 ELVKLLLSKGSDINIRDNEENICLHWAAF------------SGCVDIAEILLAAKCDL----HAVNIHGDSPLHIAAREN 895
Cdd:TIGR00870  189 SIVALLSEDPADILTADSLGNTLLHLLVMenefkaeyeelsCQMYNFALSLLDKLRDSkeleVILNHQGLTPLKLAAKEG 268

                   .
gi 157838004   896 R 896
Cdd:TIGR00870  269 R 269
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
737-930 3.97e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (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. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 41.40  E-value: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  737 LVQAGANIDTCSEDQRTPLMEAAENNhlDAVKYLIKAGAQVDPkdAEGSTCLHLAAKKGHYDVVQYLLSNGQmDVNCQDD 816
Cdd:cd21882    30 LHKAALNLNDGVNEAIMLLLEAAPDS--GNPKELVNAPCTDEF--YQGQTALHIAIENRNLNLVRLLVENGA-DVSARAT 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  817 G-------------GWTPMIWATEYKHVELVKLLLSKGSDI---NIRDNEENICLHwaafsgcvdiAEILLAAKcdlhav 880
Cdd:cd21882   105 GrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNTVLH----------ALVLQADN------ 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 157838004  881 nihgdSPLHIAARENRYDcVVLFLSRDSDVTLK-----NKEGETPLQCASLSSQV 930
Cdd:cd21882   169 -----TPENSAFVCQMYN-LLLSYGAHLDPTQQleeipNHQGLTPLKLAAVEGKI 217
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
714-789 4.24e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 Transient Receptor Potential (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: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 41.38  E-value: 4.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  714 EHQSKRSPLHAAAEAGHVDICHMLVQAGANI-------------DTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQ---V 777
Cdd:cd22197    90 EYYRGHSALHIAIEKRSLQCVKLLVENGADVharacgrffqkkqGTCFYFGELPLSLAACTKQWDVVNYLLENPHQpasL 169
                          90
                  ....*....|..
gi 157838004  778 DPKDAEGSTCLH 789
Cdd:cd22197   170 QAQDSLGNTVLH 181
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
1082-1191 4.38e-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: 38.75  E-value: 4.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004 1082 GWGVRSLQDIPLGTFVCEYVGELISDSEAdvrEEDSYLFDLDNKDGEVYCIDAR--FYGNVSRFIN---HHCEPNLVpvr 1156
Cdd:cd19193    19 GLGVWAEAPIPKGMVFGPYEGEIVEDEEA---ADSGYSWQIYKGGKLSHYIDAKdeSKSNWMRYVNcarNEEEQNLV--- 92
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 157838004 1157 VFMSHQDlrfprIAFFSTRLIQAGEQLGFDYGERF 1191
Cdd:cd19193    93 AFQYRGK-----IYYRTCKDIAPGTELLVWYGDEY 122
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
716-925 6.20e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong 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: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.93  E-value: 6.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  716 QSKRSPLHAAAEAGHVDIChmLVQAGANIDTCSEDQRTPLMEAAENNhlDAVKYLIKAgaQVDPKDAEGSTCLHLAAKKG 795
Cdd:cd22193    14 RRKDLTDSEFTESSTGKTC--LMKALLNLNPGTNDTIRILLDIAEKT--DNLKRFINA--EYTDEYYEGQTALHIAIERR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  796 HYDVVQYLLSNGQmDVNCQDDG--------------GWTPMIWATEYKHVELVKLLLS---KGSDINIRDNEENICLHwa 858
Cdd:cd22193    88 QGDIVALLVENGA-DVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLH-- 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157838004  859 afsGCVDIAEillaakcdlhavnihgDSPLHIAARENRYDCVVLF---LSRDSDV-TLKNKEGETPLQCAS 925
Cdd:cd22193   165 ---ALVTVAD----------------NTKENTKFVTRMYDMILIRgakLCPTVELeEIRNNDGLTPLQLAA 216
PHA02859 PHA02859
ankyrin repeat protein; Provisional
720-845 7.25e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.42  E-value: 7.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  720 SPLHAAAEAGHV--DICHMLVQAGANIDTCSEDQRTPLMEA----AENNHLDAVKYLIKAGAQVDPKDAEGSTCLH--LA 791
Cdd:PHA02859   53 TPIFSCLEKDKVnvEILKFLIENGADVNFKTRDNNLSALHHylsfNKNVEPEILKILIDSGSSITEEDEDGKNLLHmyMC 132
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157838004  792 AKKGHYDVVQYLLSNGQMDVNCQDDGG---WTPMIWATEYKhveLVKLLLSKGSDIN 845
Cdd:PHA02859  133 NFNVRINVIKLLIDSGVSFLNKDFDNNnilYSYILFHSDKK---IFDFLTSLGIDIN 186
PHA02946 PHA02946
ankyin-like protein; Provisional
721-888 9.31e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.04  E-value: 9.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  721 PLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPL--MEAAENNHLDAVKYLIKAGAQVDPK-DAEGSTCLhLAAKKGHY 797
Cdd:PHA02946   75 PLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKINNSvDEEGCGPL-LACTDPSE 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157838004  798 DVVQYLLSNGqMDVNCQDDGGWTPM--IWATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGC--VDIAEILLAA 873
Cdd:PHA02946  154 RVFKKIMSIG-FEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVknVDIINLLLPS 232
                         170
                  ....*....|....*
gi 157838004  874 KcDLHAVNIHGDSPL 888
Cdd:PHA02946  233 T-DVNKQNKFGDSPL 246
SET_Suv4-20-like cd10524
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
1142-1213 9.76e-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: 9.76e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157838004 1142 RFINHHCEPN--LVPVRVfmshqdlrfPRIAFFSTRLIQAGEQLGFDYGERFWDVKgklfSCRCGSSKCRHSSA 1213
Cdd:cd10524    78 AFINHDCRPNckFVPTGK---------STACVKVLRDIEPGEEITVYYGDNYFGEN----NEECECETCERRGR 138
 
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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