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Conserved domains on  [gi|1720401215|ref|XP_030108085|]
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histone-lysine N-methyltransferase EHMT1 isoform X31 [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 ...
979-1209 1.13e-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: 530.28  E-value: 1.13e-180
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  979 TNYKYVSQNCVTSPMNIDRNITHLQYCVCVDDCSSSTCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 1058
Cdd:cd10535      1 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1059 RNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 1138
Cdd:cd10535     81 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720401215 1139 SRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLFSCRCGSSKCRHS 1209
Cdd:cd10535    161 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 231
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
459-589 9.60e-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: 220.73  E-value: 9.60e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  459 LQEVPLCSCRMETPKSREISTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCG 537
Cdd:cd20905      1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720401215  538 YFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEEAS-KAKEVTIAK 589
Cdd:cd20905     81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
663-919 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 1720401215  663 LESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQSkrSPLHAAAEAGHVDICHMLVQAGANI 742
Cdd:COG0666     36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEAGADV 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  743 DTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNGQmDVNCQDDGGWTPMIW 822
Cdd:COG0666    114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHL 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  823 ATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFL 902
Cdd:COG0666    193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
                          250
                   ....*....|....*..
gi 1720401215  903 SRDSDVTLKNKEGETPL 919
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 ...
979-1209 1.13e-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: 530.28  E-value: 1.13e-180
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  979 TNYKYVSQNCVTSPMNIDRNITHLQYCVCVDDCSSSTCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 1058
Cdd:cd10535      1 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1059 RNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 1138
Cdd:cd10535     81 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720401215 1139 SRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLFSCRCGSSKCRHS 1209
Cdd:cd10535    161 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 231
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
459-589 9.60e-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: 220.73  E-value: 9.60e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  459 LQEVPLCSCRMETPKSREISTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCG 537
Cdd:cd20905      1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720401215  538 YFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEEAS-KAKEVTIAK 589
Cdd:cd20905     81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
663-919 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 1720401215  663 LESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQSkrSPLHAAAEAGHVDICHMLVQAGANI 742
Cdd:COG0666     36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEAGADV 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  743 DTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNGQmDVNCQDDGGWTPMIW 822
Cdd:COG0666    114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHL 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  823 ATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFL 902
Cdd:COG0666    193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
                          250
                   ....*....|....*..
gi 1720401215  903 SRDSDVTLKNKEGETPL 919
Cdd:COG0666    273 LALLLLAAALLDLLTLL 289
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
1069-1191 2.00e-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: 2.00e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  1069 ARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKdgevYCIDARFYGNVSR 1140
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKaydtdgakAFYLFDIDSD----LCIDARRKGNLAR 76
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1720401215  1141 FINHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGERFWD 1191
Cdd:smart00317   77 FINHSCEPNCELLFVEVNGDD----RIVIFALRDIKPGEELTIDYGSDYAN 123
Ank_2 pfam12796
Ankyrin repeats (3 copies);
753-846 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 1720401215  753 LMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNgqMDVNCQDDgGWTPMIWATEYKHVELV 832
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDN-GRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 1720401215  833 KLLLSKGSDINIRD 846
Cdd:pfam12796   78 KLLLEKGADINVKD 91
Pre-SET pfam05033
Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines ...
957-1061 2.09e-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: 112.90  E-value: 2.09e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  957 IARGYERIPIPCVNAVDSELCPTNYKYVSQNCVTSPMNIDRnithLQYCVCvDDCSSSTCMCGQLSM---RCWYDKDGRL 1033
Cdd:pfam05033    1 ISKGKENVPIPVVNEVDDEPPPPDFTYITSYIYPKEFLLII----PQGCDC-GDCSSEKCSCAQLNGgefRFPYDKDGLL 75
                           90       100
                   ....*....|....*....|....*...
gi 1720401215 1034 LPEfnmaEPPLIFECNHACSCWRNCRNR 1061
Cdd:pfam05033   76 VPE----SKPPIYECNPLCGCPPSCPNR 99
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
1079-1208 1.91e-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: 1.91e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1079 MGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDS-----YLFDLDnkDGEVycIDARFYGNVSRFINHHCEPNLVPV 1153
Cdd:COG2940     16 HGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKeplhtYLFELD--DDGV--IDGALGGNPARFINHSCDPNCEAD 91
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720401215 1154 RvfmshqdlRFPRIAFFSTRLIQAGEQLGFDYGERFWDvkgKLFSCRCGssKCRH 1208
Cdd:COG2940     92 E--------EDGRIFIVALRDIAAGEELTYDYGLDYDE---EEYPCRCP--NCRG 133
PHA03100 PHA03100
ankyrin repeat protein; Provisional
693-926 1.14e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 108.60  E-value: 1.14e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  693 ELQKVLLMLVDGIDPNFKMehqsKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNH-----LDAVKY 767
Cdd:PHA03100    16 KNIKYIIMEDDLNDYSYKK----PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  768 LIKAGAQVDPKDAEGSTCLHLAA--KKGHYDVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVEL--VKLLLSKGSDIN 843
Cdd:PHA03100    92 LLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDIN 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  844 IRDNeeniclhwaafsgcvdiAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCAS 923
Cdd:PHA03100   171 AKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233

                   ...
gi 1720401215  924 LSS 926
Cdd:PHA03100   234 LNN 236
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
751-922 5.91e-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: 5.91e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  751 TPLMEAAENNHLDAVKYLIKAgAQVDP--KDAEGSTCLHLAAKKGHYDVVQYLLSNGQMDVN----CQDDGGWTPMIWAT 824
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKC-PSCDLfqRGALGETALHVAALYDNLEAAVVLMEAAPELVNepmtSDLYQGETALHIAV 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  825 EYKHVELVKLLLSKGSDIN--------IRDNEENICL---HWAAFSGCV---DIAEILLAAKCDLHAVNIHGDSPLHIAA 890
Cdd:cd22192     98 VNQNLNLVRELIARGADVVspratgtfFRPGPKNLIYygeHPLSFAACVgneEIVRLLIEHGADIRAQDSLGNTVLHILV 177
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1720401215  891 RENR-------YDcvvLFLSRDSDV------TLKNKEGETPLQCA 922
Cdd:cd22192    178 LQPNktfacqmYD---LILSYDKEDdlqpldLVPNNQGLTPFKLA 219
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
750-845 8.10e-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: 8.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  750 RTPLMEAA-ENNHLDAVKYLIKAGAQVDpkdaEGSTCLHLAAKKGH---YDVVQYLLSNGQMDVN-------CQDD--GG 816
Cdd:TIGR00870   53 RSALFVAAiENENLELTELLLNLSCRGA----VGDTLLHAISLEYVdavEAILLHLLAAFRKSGPlelandqYTSEftPG 128
                           90       100
                   ....*....|....*....|....*....
gi 1720401215  817 WTPMIWATEYKHVELVKLLLSKGSDINIR 845
Cdd:TIGR00870  129 ITALHLAAHRQNYEIVKLLLERGASVPAR 157
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
781-811 1.29e-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: 1.29e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 1720401215   781 EGSTCLHLAAKKGHYDVVQYLLSNGQmDVNC 811
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 ...
979-1209 1.13e-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: 530.28  E-value: 1.13e-180
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  979 TNYKYVSQNCVTSPMNIDRNITHLQYCVCVDDCSSSTCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 1058
Cdd:cd10535      1 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1059 RNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 1138
Cdd:cd10535     81 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720401215 1139 SRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLFSCRCGSSKCRHS 1209
Cdd:cd10535    161 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 231
SET_EHMT cd10543
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
979-1209 4.90e-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: 486.85  E-value: 4.90e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  979 TNYKYVSQNCVTSPMNIDRNITHLQYCVCVDDCSSSTCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 1058
Cdd:cd10543      1 PDFLYVTENCETSPLNIDRNITSLQTCSCRDDCSSDNCVCGRLSVRCWYDKEGRLLPDFNKLDPPLIFECNRACSCWRNC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1059 RNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 1138
Cdd:cd10543     81 RNRVVQNGIRYRLQLFRTRGMGWGVRALQDIPKGTFVCEYIGELISDSEADSREDDSYLFDLDNKDGETYCIDARRYGNI 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720401215 1139 SRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLFSCRCGSSKCRHS 1209
Cdd:cd10543    161 SRFINHLCEPNLIPVRVFVEHQDLRFPRIAFFASRDIKAGEELGFDYGEKFWRIKGKYFTCRCGSPKCKYS 231
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
979-1217 1.43e-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: 457.17  E-value: 1.43e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  979 TNYKYVSQNCVTSPMNIDRNITHLQYCVCVDDCSSSTCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 1058
Cdd:cd10533      1 EDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRNC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1059 RNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 1138
Cdd:cd10533     81 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNI 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720401215 1139 SRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLFSCRCGSSKCRHSSAALAQRQ 1217
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) ...
980-1186 1.37e-102

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: 323.55  E-value: 1.37e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  980 NYKYVSQNCVTSPMNIDRNITHLQYCVCVDDCSSSTCMCGQLS-MRCWYDKDGRLLPefnMAEPPLIFECNHACSCWRNC 1058
Cdd:cd10538      2 SFTYIKDNIVGKNVQPFSNIIDSVGCKCKDDCLDSKCACAAESdGIFAYTKNGLLRL---NNSPPPIFECNSKCSCDDDC 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1059 RNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE------DSYLFDLDN-----KDGEV 1127
Cdd:cd10538     79 KNRVVQRGLQARLQVFRTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRGKiydksgGSYLFDLDEfsdsdGDGEE 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720401215 1128 YCIDARFYGNVSRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDYG 1186
Cdd:cd10538    159 LCVDATFCGNVSRFINHSCDPNLFPFNVVIDHDDLRYPRIALFATRDILPGEELTFDYG 217
SET_SETDB1 cd10517
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
951-1207 3.03e-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: 242.58  E-value: 3.03e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  951 KTVSRDIARGYERIPIPCVNAVDSELcPTNYKYVSQNCVTSPMNIDRNITHLQYCVCVDDCS-SSTCMCGQLS---MRCW 1026
Cdd:cd10517      3 YYYICDISYGKEGVPIPCVNEIDNSS-PPYVEYSKERIPGKGVNINLDPDFLVGCDCTDGCRdKSKCACQQLTieaTAAT 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1027 YDKDG--------RLLPEFnmaEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEY 1098
Cdd:cd10517     82 PGGQInpsagyqyRRLMEK---LPTGVYECNSRCKCDKRCYNRVVQNGLQVRLQVFKTEKKGWGIRCLDDIPKGSFVCIY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1099 VGELISDSEADVREE---DSYLFDLD------------NKDGEVYC--IDARFYGNVSRFINHHCEPNLVPVRVFMSHQD 1161
Cdd:cd10517    159 AGQILTEDEANEEGLqygDEYFAELDyievveklkegyESDVEEHCyiIDAKSEGNLGRYLNHSCSPNLFVQNVFVDTHD 238
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1720401215 1162 LRFPRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLFSCRCGSSKCR 1207
Cdd:cd10517    239 LRFPWVAFFASRYIRAGTELTWDYNYEVGSVPGKVLYCYCGSSNCR 284
SET_SUV39H cd10542
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
980-1207 3.31e-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: 229.49  E-value: 3.31e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  980 NYKYVSQNCVTSPMNIDRNIthLQYCVCVDDC--SSSTCmCGQLS-MRCWYDKDGRLLpeFNMAEPplIFECNHACSCWR 1056
Cdd:cd10542      2 NFQYINDYIPGDGVKIPEDF--LVGCECTEDChnNNPTC-CPAESgVKFAYDKQGRLR--LPPGTP--IYECNSRCKCGP 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1057 NCRNRVVQNGLRARLQLYRTQD-MGWGVRSLQDIPLGTFVCEYVGELISDSEADVR------EEDSYLFDLD-NKDGEVY 1128
Cdd:cd10542     75 DCPNRVVQRGRKVPLCIFRTSNgRGWGVKTLEDIKKGTFVMEYVGEIITSEEAERRgkiydaNGRTYLFDLDyNDDDCEY 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1129 CIDARFYGNVSRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDY------------GERFWDVKGKl 1196
Cdd:cd10542    155 TVDAAYYGNISHFINHSCDPNLAVYAVWINHLDPRLPRIAFFAKRDIKAGEELTFDYlmtgtggssestIPKPKDVRVP- 233
                          250
                   ....*....|.
gi 1720401215 1197 fsCRCGSSKCR 1207
Cdd:cd10542    234 --CLCGSKNCR 242
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
459-589 9.60e-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: 220.73  E-value: 9.60e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  459 LQEVPLCSCRMETPKSREISTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCG 537
Cdd:cd20905      1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720401215  538 YFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEEAS-KAKEVTIAK 589
Cdd:cd20905     81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
663-919 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 1720401215  663 LESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQSkrSPLHAAAEAGHVDICHMLVQAGANI 742
Cdd:COG0666     36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEAGADV 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  743 DTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNGQmDVNCQDDGGWTPMIW 822
Cdd:COG0666    114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHL 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  823 ATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFL 902
Cdd:COG0666    193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
                          250
                   ....*....|....*..
gi 1720401215  903 SRDSDVTLKNKEGETPL 919
Cdd:COG0666    273 LALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
666-945 9.36e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 201.34  E-value: 9.36e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  666 ALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQskRSPLHAAAEAGHVDICHMLVQAGANIDTC 745
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALG--ALLLLAAALAGDLLVALLLLAAGADINAK 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  746 SEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNGqMDVNCQDDGGWTPMIWATE 825
Cdd:COG0666     84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  826 YKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRD 905
Cdd:COG0666    163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1720401215  906 SDVTLKNKEGETPLQCASLSSQVWSALQMSKALRDSAPDK 945
Cdd:COG0666    243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
979-1207 8.99e-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: 194.44  E-value: 8.99e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  979 TNYKYVSQNCVTSPMNIDRNITHLQYCVCVDD-CSSSTCMCgqlsMRCW---YDKDGRLLPEF-NMAEPplIFECNHACS 1053
Cdd:cd10544      1 PDFQYTPENVPGPGADTDPNEITFPGCDCKTSsCEPETCSC----LRKYgpnYDDDGCLLDFDgKYSGP--VFECNSMCK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1054 CWRNCRNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVR------EEDSYLFDLDN--KDG 1125
Cdd:cd10544     75 CSESCQNRVVQNGLQFKLQVFKTPKKGWGLRTLEFIPKGRFVCEYAGEVIGFEEARRRtksqtkGDMNYIIVLREhlSSG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1126 EVY--CIDARFYGNVSRFINHHCEPNL--VPVRVfmshqDLRFPRIAFFSTRLIQAGEQLGFDYGERF-----------W 1190
Cdd:cd10544    155 KVLetFVDPTYIGNIGRFLNHSCEPNLfmVPVRV-----DSMVPKLALFAARDIVAGEELSFDYSGEFsnsvesvtlarQ 229
                          250
                   ....*....|....*..
gi 1720401215 1191 DVKGKLFSCRCGSSKCR 1207
Cdd:cd10544    230 DESKSRKPCLCGAENCR 246
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
1005-1186 9.56e-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: 187.61  E-value: 9.56e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1005 CVCVDDC--SSSTCMCGQL-SMRCWYDKDGRLLpefnmAEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTQDMGW 1081
Cdd:cd10545     24 CDCKNRCtdGASDCACVKKnGGEIPYNFNGRLI-----RAKPAIYECGPLCKCPPSCYNRVTQKGLRYRLEVFKTAERGW 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1082 GVRSLQDIPLGTFVCEYVGELISDSEADVR-EEDSYLFDLDNK------DGEV---------------------YCIDAR 1133
Cdd:cd10545     99 GVRSWDSIPAGSFICEYVGELLDTSEADTRsGNDDYLFDIDNRqtnrgwDGGQrldvgmsdgerssaedeesseFTIDAG 178
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720401215 1134 FYGNVSRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDYG 1186
Cdd:cd10545    179 SFGNVARFINHSCSPNLFVQCVLYDHNDLRLPRVMLFAADNIPPLQELTYDYG 231
SET_SETDB cd10541
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...
1005-1207 1.30e-50

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: 178.89  E-value: 1.30e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1005 CVCVDDC-SSSTCMCGQLSMRCWYDKDG-----------RLLPEfnmAEPPLIFECNHACSCWRN-CRNRVVQNGLRARL 1071
Cdd:cd10541     18 CDCTDGCrDKSKCACHQLTIQATACTPGgqdnptagyqyKRLEE---CLPTGVYECNKLCKCDPNmCQNRLVQHGLQVRL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1072 QLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEAD---VREEDSYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEP 1148
Cdd:cd10541     95 QLFKTQNKGWGIRCLDDIAKGTFVCIYAGKILTDDFADkegLEMGDEYFANLDHIEESCYIIDAKLEGNLGRYLNHSCSP 174
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720401215 1149 NLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLFSCRCGSSKCR 1207
Cdd:cd10541    175 NLFVQNVFVDTHDLRFPWVAFFASKRIKAGTELTWDYNYEVGSVEGKELLCCCGSNECR 233
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
980-1207 3.93e-46

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


Pssm-ID: 380923 [Multi-domain]  Cd Length: 255  Bit Score: 166.61  E-value: 3.93e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  980 NYKYVSQNCVTSPMNIDRNITHlqyCVCVDDCSSST--CMCGQLSMRCWYDKDGRLLPefnMAEPPlIFECNHACSCWRN 1057
Cdd:cd10525      2 DFVYINEYKVGEGVTLNQVAVG---CECQDCLSQPVggCCPGASKHRFAYNEQGQVKV---RPGLP-IYECNSRCRCGPD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1058 CRNRVVQNGLRARLQLYRTQD-MGWGVRSLQDIPLGTFVCEYVGELISDSEADVR------EEDSYLFDLDNKDgEVYCI 1130
Cdd:cd10525     75 CPNRVVQKGIQYDLCIFRTDNgRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRgqiydrQGATYLFDLDYVE-DVYTV 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1131 DARFYGNVSRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDYGERFWDV------------------ 1192
Cdd:cd10525    154 DAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIALFATRTIRAGEELTFDYNMQVDPVdaestkmdsnfglaglpg 233
                          250
                   ....*....|....*...
gi 1720401215 1193 ---KGKLFSCRCGSSKCR 1207
Cdd:cd10525    234 spkKRVRIECKCGVRSCR 251
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
1005-1207 1.07e-45

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: 165.06  E-value: 1.07e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1005 CVCVDdCSSSTCMCGQLSMRCWYDKDGRLlpefnMAEPPL-IFECNHACSCWRNCRNRVVQNGLRARLQLYRTQD-MGWG 1082
Cdd:cd10532     25 CDCSD-CFFGKCCPAEAGVLFAYNEHGQL-----KIPPGTpIYECNSRCKCGPDCPNRVVQKGTQYSLCIFRTSNgRGWG 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1083 VRSLQDIPLGTFVCEYVGELISDSEADVREE--DS----YLFDLDNKDGEvYCIDARFYGNVSRFINHHCEPNLVPVRVF 1156
Cdd:cd10532     99 VKTLQKIKKNSFVMEYVGEVITSEEAERRGQfyDSkgitYLFDLDYESDE-FTVDAARYGNVSHFVNHSCDPNLQVFNVF 177
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720401215 1157 MSHQDLRFPRIAFFSTRLIQAGEQLGFDY-----GERFWDV-------KGKLFSCRCGSSKCR 1207
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 ...
1027-1207 1.78e-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: 1.78e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1027 YDKDGRLlpefNMAEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDS 1106
Cdd:cd20073     55 YDEYGRV----RANTGSIIYECNENCDCGINCPNRVVQRGRKLPLEIFKTKHKGWGLRCPRFIKAGTFIGVYLGEVITQS 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1107 EADVREED------SYLFDLDNKDGEV---YCIDARFYGNVSRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQA 1177
Cdd:cd20073    131 EAEIRGKKydnvgvTYLFDLDLFEDQVdeyYTVDAQYCGDVTRFINHSCDPNLAIYSVLRDKSDSKIYDLAFFAIKDIPA 210
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1720401215 1178 GEQLGFDYGER----------------FWDVKGKLfSCRCGSSKCR 1207
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; ...
1005-1207 3.58e-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: 164.41  E-value: 3.58e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1005 CVCVDD--CSSSTCMCGQ-----------LSMRCWY---DKDGRLLPEFNMAEPPlIFECNHACSCWRNCRNRVVQNGLR 1068
Cdd:cd19473     26 CECTDDedCMYSGCLCLQdvdpdddrdpgKKKNAYHssgAKKGCLRGHMLNSRLP-IYECHEGCACSDDCPNRVVERGRK 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1069 ARLQLYRTQD-MGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDS--------YLFDLDN----------KDGEVYC 1129
Cdd:cd19473    105 VPLQIFRTSDgRGWGVRSTVDIKRGQFVDCYVGEIITPEEAQRRRDAAtiaqrkdvYLFALDKfsdpdsldprLRGDPYE 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1130 IDARFYGNVSRFINHHCEPNLvpvRVFM---SHQDLRFPRIAFFSTRLIQAGEQLGFDY--------GERFWDVKGK-LF 1197
Cdd:cd19473    185 IDGEFMSGPTRFINHSCDPNL---RIFArvgDHADKHIHDLAFFAIKDIPRGTELTFDYvdgvtgldDDAGDEEKEKeMT 261
                          250
                   ....*....|
gi 1720401215 1198 SCRCGSSKCR 1207
Cdd:cd19473    262 KCLCGSPKCR 271
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
1005-1207 2.99e-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: 161.54  E-value: 2.99e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1005 CVCVDDCSS-STCMCGQLSMR-------------CWYdKDGRLLpefnMAEPPLIFECNHACSCWRN-CRNRVVQNGLRA 1069
Cdd:cd10523     34 CDCTDGCIDiLKCACLQLTARafsksesspskggRGY-KYKRLQ----EPIPSGLYECNVSCKCNRMlCQNRVVQHGLQV 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1070 RLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELIS-----------------DSEADVREEDSYLFDLDNKDGEVYCIDA 1132
Cdd:cd10523    109 RLQVFKTEKKGWGVRCLDDIDKGTFVCIYAGRVLSrarspteplppklelpsENEVEVVTSWLILSKKRKLRENVCFLDA 188
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720401215 1133 RFYGNVSRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLFSCRCGSSKCR 1207
Cdd:cd10523    189 SKEGNVGRFLNHSCCPNLFVQNVFVDTHDKNFPWVAFFTNRVVKAGTELTWDYSYDAGTSPEQEIPCLCGVNKCQ 263
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
1069-1191 2.00e-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: 2.00e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  1069 ARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKdgevYCIDARFYGNVSR 1140
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKaydtdgakAFYLFDIDSD----LCIDARRKGNLAR 76
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1720401215  1141 FINHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGERFWD 1191
Cdd:smart00317   77 FINHSCEPNCELLFVEVNGDD----RIVIFALRDIKPGEELTIDYGSDYAN 123
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
1071-1207 3.05e-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: 133.92  E-value: 3.05e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1071 LQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVR--------EEDSYLFDLdnKDGEVycIDARFYGNVSRFI 1142
Cdd:cd10531      2 LELFRTEKKGWGVKAKEDIQKGEFIIEYVGEVIDKKEFKERldeyeelgKSNFYILSL--SDDVV--IDATRKGNLSRFI 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720401215 1143 NHHCEPNLVpVRVFMShqdLRFPRIAFFSTRLIQAGEQLGFDYGerFWDVKGKLFSCRCGSSKCR 1207
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; ...
1071-1207 2.27e-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: 125.87  E-value: 2.27e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1071 LQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDSYLFDLDNkdgevYC--------IDARFYGNVSRFI 1142
Cdd:cd19174      2 LERFRTEDKGWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRMIEQYHNHSHH-----YClnldsgmvIDGYRMGNEARFV 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720401215 1143 NHHCEPNLVPVRVFMSHQdlrfPRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLfSCRCGSSKCR 1207
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), ...
1059-1207 1.20e-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: 123.86  E-value: 1.20e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1059 RNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKdgevYCI 1130
Cdd:cd10518      4 RFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKrydeegggGTYMFRIDED----LVI 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720401215 1131 DARFYGNVSRFINHHCEPNLVpVRVfMSHQDLRfpRIAFFSTRLIQAGEQLGFDYgeRFWDVKGKLFSCRCGSSKCR 1207
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 ...
1069-1207 1.34e-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: 114.99  E-value: 1.34e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1069 ARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDS--------YLFDLDNKDgevyCIDARFYGNVSR 1140
Cdd:cd19172      2 AKVEVFRTEKKGWGLRAAEDLPKGTFVIEYVGEVLDEKEFKRRMKEYaregnrhyYFMALKSDE----IIDATKKGNLSR 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720401215 1141 FINHHCEPNLVpVRVFMSHQDLrfpRIAFFSTRLIQAGEQLGFDYG-ERFWDVKGKlfsCRCGSSKCR 1207
Cdd:cd19172     78 FINHSCEPNCE-TQKWTVNGEL---RVGFFAKRDIPAGEELTFDYQfERYGKEAQK---CYCGSPNCR 138
Ank_2 pfam12796
Ankyrin repeats (3 copies);
753-846 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 1720401215  753 LMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNgqMDVNCQDDgGWTPMIWATEYKHVELV 832
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDN-GRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 1720401215  833 KLLLSKGSDINIRD 846
Cdd:pfam12796   78 KLLLEKGADINVKD 91
Pre-SET pfam05033
Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines ...
957-1061 2.09e-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: 112.90  E-value: 2.09e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  957 IARGYERIPIPCVNAVDSELCPTNYKYVSQNCVTSPMNIDRnithLQYCVCvDDCSSSTCMCGQLSM---RCWYDKDGRL 1033
Cdd:pfam05033    1 ISKGKENVPIPVVNEVDDEPPPPDFTYITSYIYPKEFLLII----PQGCDC-GDCSSEKCSCAQLNGgefRFPYDKDGLL 75
                           90       100
                   ....*....|....*....|....*...
gi 1720401215 1034 LPEfnmaEPPLIFECNHACSCWRNCRNR 1061
Cdd:pfam05033   76 VPE----SKPPIYECNPLCGCPPSCPNR 99
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
1080-1186 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 1720401215 1080 GWGVRSLQDIPLGTFVCEYVGE-LISDSEADVREE-----------DSYLFDLDNKDGevYCIDAR--FYGNVSRFINHH 1145
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELlyydklelrlwGPYLFTLDEDSE--YCIDARalYYGNWARFINHS 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1720401215 1146 CEPNLVPVRVFMShqdlRFPRIAFFSTRLIQAGEQLGFDYG 1186
Cdd:pfam00856   79 CDPNCEVRVVYVN----GGPRIVIFALRDIKPGEELTIDYG 115
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
1079-1208 1.91e-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: 1.91e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1079 MGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDS-----YLFDLDnkDGEVycIDARFYGNVSRFINHHCEPNLVPV 1153
Cdd:COG2940     16 HGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKeplhtYLFELD--DDGV--IDGALGGNPARFINHSCDPNCEAD 91
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720401215 1154 RvfmshqdlRFPRIAFFSTRLIQAGEQLGFDYGERFWDvkgKLFSCRCGssKCRH 1208
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 ...
1070-1186 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 1720401215 1070 RLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVRE--ED----SYLFDLDNKdgevYCIDARFYGNVSRFIN 1143
Cdd:cd10519      2 RLLLGKSDVAGWGLFLKEPIKKDEFIGEYTGELISQDEADRRGkiYDkynsSYLFNLNDQ----FVVDATRKGNKIRFAN 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1720401215 1144 HHCEPNLVPvRVFMSHQDlrfPRIAFFSTRLIQAGEQLGFDYG 1186
Cdd:cd10519     78 HSSNPNCYA-KVMMVNGD---HRIGIFAKRDIEAGEELFFDYG 116
SET_NSD cd19173
SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...
1069-1206 2.76e-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: 2.76e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1069 ARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDS--------YLFDLDNKdgevYCIDARFYGNVSR 1140
Cdd:cd19173      2 PPTEPFKTGDRGWGLRTKRDIKKGDFVIEYVGELIDEEECRRRLKKAhennitnfYMLTLDKD----RIIDAGPKGNLSR 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720401215 1141 FINHHCEPNLvPVRVFMSHQDlrfPRIAFFSTRLIQAGEQLGFDYG-ERFWDVKGKlfsCRCGSSKC 1206
Cdd:cd19173     78 FMNHSCQPNC-ETQKWTVNGD---TRVGLFAVRDIPAGEELTFNYNlDCLGNEKKV---CRCGAPNC 137
Ank_2 pfam12796
Ankyrin repeats (3 copies);
720-813 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 1720401215  720 LHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLIKaGAQVDPKDaEGSTCLHLAAKKGHYDVVQ 799
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|....
gi 1720401215  800 YLLSNGQmDVNCQD 813
Cdd:pfam12796   79 LLLEKGA-DINVKD 91
SET_ASHR3-like cd19175
SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...
1070-1207 2.92e-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: 102.49  E-value: 2.92e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1070 RLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVR--------EEDSYLFDLDnKDgevYCIDARFYGNVSRF 1141
Cdd:cd19175      1 KMKLVKTEKCGWGLVADEDINAGEFIIEYVGEVIDDKTCEERlwdmkhkgEKNFYMCEID-KD---MVIDATFKGNLSRF 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720401215 1142 INHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYgeRFWDVkGKLFSCRCGSSKCR 1207
Cdd:cd19175     77 INHSCDPNCELQKWQVDGET----RIGVFAIRDIKKGEELTYDY--QFVQF-GADQDCHCGSKNCR 135
PreSET smart00468
N-terminal to some SET domains; A Cys-rich putative Zn2+-binding domain that occurs N-terminal ...
955-1053 6.58e-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: 100.18  E-value: 6.58e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215   955 RDIARGYERIPIPCVNAVDSELCPTNYKYVSQNCVTSPMNIDRNITHLQYCVCVDDCSSST-CMCGQLSMRCW-YDKDGR 1032
Cdd:smart00468    2 LDISNGKENVPVPLVNEVDEDPPPPDFEYISEYIYGQGVPIDRSPSPLVGCSCSGDCSSSNkCECARKNGGEFaYELNGG 81
                            90       100
                    ....*....|....*....|.
gi 1720401215  1033 LLPEfnmaEPPLIFECNHACS 1053
Cdd:smart00468   82 LRLK----RKPLIYECNSRCS 98
PHA03100 PHA03100
ankyrin repeat protein; Provisional
693-926 1.14e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 108.60  E-value: 1.14e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  693 ELQKVLLMLVDGIDPNFKMehqsKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNH-----LDAVKY 767
Cdd:PHA03100    16 KNIKYIIMEDDLNDYSYKK----PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  768 LIKAGAQVDPKDAEGSTCLHLAA--KKGHYDVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVEL--VKLLLSKGSDIN 843
Cdd:PHA03100    92 LLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDIN 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  844 IRDNeeniclhwaafsgcvdiAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCAS 923
Cdd:PHA03100   171 AKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233

                   ...
gi 1720401215  924 LSS 926
Cdd:PHA03100   234 LNN 236
SET_SETD1 cd19169
SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...
1065-1207 1.61e-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: 1.61e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1065 NGLRAR---LQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE--------DSYLFDLDnkdgEVYCIDAR 1133
Cdd:cd19169      6 NQLKFRkkqLKFAKSRIHDWGLFALEPIAADEMVIEYVGQVIRQSVADEREKryeaigigSSYLFRVD----DDTIIDAT 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720401215 1134 FYGNVSRFINHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGERFWDVKgklFSCRCGSSKCR 1207
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), ...
1059-1207 1.38e-22

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: 95.15  E-value: 1.38e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1059 RNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE--DS-----YLFDLDnkdgEVYCID 1131
Cdd:cd19170      4 RFRHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKyyESkgigcYMFRID----DDEVVD 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720401215 1132 ARFYGNVSRFINHHCEPNLVPvRVFmsHQDLRfPRIAFFSTRLIQAGEQLGFDYGERFWDVKgklFSCRCGSSKCR 1207
Cdd:cd19170     80 ATMHGNAARFINHSCEPNCYS-RVV--NIDGK-KHIVIFALRRILRGEELTYDYKFPIEDVK---IPCTCGSKKCR 148
PHA03095 PHA03095
ankyrin-like protein; Provisional
697-923 1.69e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 102.41  E-value: 1.69e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  697 VLLMLVDGIDPNFKMEHqsKRSPLHAAAEAGH---VDICHMLVQAGANIDTCSEDQRTPLMEAAEN-NHLDAVKYLIKAG 772
Cdd:PHA03095    30 VRRLLAAGADVNFRGEY--GKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNaTTLDVIKLLIKAG 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  773 AQVDPKDAEGSTCLH--LAAKKGHYDVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKH--VELVKLLLSKGSDINIRDNE 848
Cdd:PHA03095   108 ADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKG-ADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDR 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  849 ENICLHWAAFSgCVDIAEI---LLAAKCDLHAVNIHGDSPLHIAARENRYDCVVL--FLSRDSDVTLKNKEGETPLQCAS 923
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. ...
1061-1188 1.81e-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: 1.81e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1061 RVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE----DS------YLFDLDNKDgevYCI 1130
Cdd:cd10528      9 ELILSGKEEGLKVIEIDGKGRGVIATRPFEKGDFVVEYHGDLITITEAKKREAlyakDPstgcymYYFQYKGKT---YCV 85
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1131 DA-RFYGNVSRFINHHC-EPNLVPVRVFMSHQdlrfPRIAFFSTRLIQAGEQLGFDYGER 1188
Cdd:cd10528     86 DAtKESGRLGRLINHSKkKPNLKTKLLVIDGV----PHLILVAKRDIKPGEELLYDYGDR 141
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
1080-1191 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 1720401215 1080 GWGVRSLQDIPLGTFVCEYVGELISD--SEADVREEDSYLFDLDNKDGEVYcIDARFYGNVSRFINHHCEPNLVPVrvFM 1157
Cdd:cd10522     14 GLGLFAAETIAKGEFVGEYTGEVLDRweEDRDSVYHYDPLYPFDLNGDILV-IDAGKKGNLTRFINHSDQPNLELI--VR 90
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1720401215 1158 SHQDLrfPRIAFFSTRLIQAGEQLGFDYGERFWD 1191
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 ...
1080-1189 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 1720401215 1080 GWGVRSLQDIPLGTFVCEYVGELISDSEADVRE------EDSYLFDLDNKdgevYCIDARFYGNVSRFINHHCEP----N 1149
Cdd:cd19168     13 GLGLFAAEDIKEGEFVIEYTGELISHDEGVRREhrrgdvSYLYLFEEQEG----IWVDAAIYGNLSRYINHATDKvktgN 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1720401215 1150 LVPVRVFMSHQdlrfPRIAFFSTRLIQAGEQLGFDYGERF 1189
Cdd:cd19168     89 CMPKIMYVNHE----WRIKFTAIKDIKIGEELFFNYGDNF 124
SET_SET1 cd20072
SET domain (including post-SET domain) found in catalytic component of the Saccharomyces ...
1065-1207 6.95e-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: 6.95e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1065 NGLRAR---LQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE--------DSYLFDLDnkdgEVYCIDAR 1133
Cdd:cd20072      6 NQLKKRkkqLKFARSAIHNWGLYAMENISAKDMVIEYVGEVIRQQVADEREKrylrqgigSSYLFRID----DDTVVDAT 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720401215 1134 FYGNVSRFINHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGERFWDVKgklFSCRCGSSKCR 1207
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), ...
1068-1207 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 1720401215 1068 RARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVRE---EDS----YLFDLDNKdgevYCIDARFYGNVSR 1140
Cdd:cd19171     13 RSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREkiyESQnrgiYMFRIDND----WVIDATMTGGPAR 88
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720401215 1141 FINHHCEPNLVP-VRVFMSHQdlrfpRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLfSCRCGSSKCR 1207
Cdd:cd19171     89 YINHSCNPNCVAeVVTFDKEK-----KIIIISNRRIAKGEELTYDYKFDFEDDQHKI-PCLCGAPNCR 150
PHA03100 PHA03100
ankyrin repeat protein; Provisional
687-879 1.66e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 95.89  E-value: 1.66e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  687 FSARQGELQKVLLMLVD-GIDPNFKMEHQSkrSPLHAAAEAGHV-----DICHMLVQAGANIDTCSEDQRTPLMEAAEN- 759
Cdd:PHA03100    40 YLAKEARNIDVVKILLDnGADINSSTKNNS--TPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKk 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  760 -NHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDV------------------VQYLLSNGqMDVNCQDDGGWTPM 820
Cdd:PHA03100   118 sNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYG-VPINIKDVYGFTPL 196
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720401215  821 IWATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVN 879
Cdd:PHA03100   197 HYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
SET_KMT2A cd19206
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...
1059-1207 3.56e-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: 3.56e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1059 RNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE--DS-----YLFDLDnkDGEVycID 1131
Cdd:cd19206      4 RFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREKyyDSkgigcYMFRID--DSEV--VD 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720401215 1132 ARFYGNVSRFINHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLfSCRCGSSKCR 1207
Cdd:cd19206     80 ATMHGNAARFINHSCEPNCYSRVINIDGQK----HIVIFAMRKIYRGEELTYDYKFPIEDASNKL-PCNCGAKKCR 150
Ank_2 pfam12796
Ankyrin repeats (3 copies);
820-912 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 1720401215  820 MIWATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLaAKCDLHAVNiHGDSPLHIAARENRYDCVV 899
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1720401215  900 LFLSRDSDVTLKN 912
Cdd:pfam12796   79 LLLEKGADINVKD 91
SET_NSD2 cd19211
SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...
1072-1206 6.28e-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: 6.28e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1072 QLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVR-----EEDS---YLFDLDnKDgevYCIDARFYGNVSRFIN 1143
Cdd:cd19211      5 KIIKTEGKGWGLIAKRDIKKGEFVNEYVGELIDEEECMARikhahENDIthfYMLTID-KD---RIIDAGPKGNYSRFMN 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720401215 1144 HHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGerfWDVKGKLFS-CRCGSSKC 1206
Cdd:cd19211     81 HSCQPNCETQKWTVNGDT----RVGLFAVCDIPAGTELTFNYN---LDCLGNEKTvCRCGAPNC 137
PHA02874 PHA02874
ankyrin repeat protein; Provisional
726-924 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 1720401215  726 AGHVDICHMLVQAGAN-IDTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSN 804
Cdd:PHA02874    11 SGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  805 G----------------------QMDVNCQDDGGWTPMIWATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCV 862
Cdd:PHA02874    91 GvdtsilpipciekdmiktildcGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFF 170
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720401215  863 DIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASL 924
Cdd:PHA02874   171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
685-779 1.61e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 1.61e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  685 LYFSARQGELQKVLLMLVDGIDPNFKmeHQSKRSPLHAAAEAGHVDICHMLVQaGANIDtCSEDQRTPLMEAAENNHLDA 764
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ--DKNGRTALHLAAKNGHLEIVKLLLE-HADVN-LKDNGRTALHYAARSGHLEI 76
                           90
                   ....*....|....*
gi 1720401215  765 VKYLIKAGAQVDPKD 779
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
718-922 1.98e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 86.56  E-value: 1.98e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  718 SPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLI-----------------------KAGAQ 774
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIdngvdtsilpipciekdmiktilDCGID 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  775 VDPKDAEGSTCLHLAAKKGHYDVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVELVKLLLSKGSDINIRDNEENICLH 854
Cdd:PHA02874   117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  855 WAAFSGCVDIAEILL------AAKCD-----LHAVNIH--------------------GDSPLHIAAREN-RYDCVVLFL 902
Cdd:PHA02874   196 NAAEYGDYACIKLLIdhgnhiMNKCKngftpLHNAIIHnrsaiellinnasindqdidGSTPLHHAINPPcDIDIIDILL 275
                          250       260
                   ....*....|....*....|
gi 1720401215  903 SRDSDVTLKNKEGETPLQCA 922
Cdd:PHA02874   276 YHKADISIKDNKGENPIDTA 295
SET_EZH1 cd19217
SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43) ...
1064-1185 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 1720401215 1064 QNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE------DSYLFDLDNKdgevYCIDARFYGN 1137
Cdd:cd19217      1 QRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKvydkymSSFLFNLNND----FVVDATRKGN 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1720401215 1138 VSRFINHHCEPNLVpVRVFMSHQDlrfPRIAFFSTRLIQAGEQLGFDY 1185
Cdd:cd19217     77 KIRFANHSVNPNCY-AKVVMVNGD---HRIGIFAKRAIQQGEELFFDY 120
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
1071-1206 3.06e-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: 79.59  E-value: 3.06e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1071 LQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVR-----EED---SYLFDLDnKDgevYCIDARFYGNVSRFI 1142
Cdd:cd19210      4 VEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIDEEECRARiryaqEHDitnFYMLTLD-KD---RIIDAGPKGNYARFM 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720401215 1143 NHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGERFWDvKGKLfSCRCGSSKC 1206
Cdd:cd19210     80 NHCCQPNCETQKWTVNGDT----RVGLFALCDIKAGTELTFNYNLECLG-NGKT-VCKCGAPNC 137
SET_EZH2 cd19218
SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...
1066-1185 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 1720401215 1066 GLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREED------SYLFDLDNKdgevYCIDARFYGNVS 1139
Cdd:cd19218      1 GSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVydkymcSFLFNLNND----FVVDATRKGNKI 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1720401215 1140 RFINHHCEPNLVpVRVFMSHQDlrfPRIAFFSTRLIQAGEQLGFDY 1185
Cdd:cd19218     77 RFANHSVNPNCY-AKVMMVNGD---HRIGIFAKRAIQTGEELFFDY 118
PHA03095 PHA03095
ankyrin-like protein; Provisional
754-919 7.31e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 81.99  E-value: 7.31e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  754 MEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHY---DVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVE 830
Cdd:PHA03095    19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAG-ADVNAPERCGFTPLHLYLYNATTL 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  831 -LVKLLLSKGSDINIRDNEENICLHWAAFSGCVD--IAEILLAAKCDLHAVNIHGDSPLHIAARENRYD--CVVLFLSRD 905
Cdd:PHA03095    98 dVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLLIDAG 177
                          170
                   ....*....|....
gi 1720401215  906 SDVTLKNKEGETPL 919
Cdd:PHA03095   178 ADVYAVDDRFRSLL 191
SET_KMT2C cd19208
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) ...
1056-1207 7.90e-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: 7.90e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1056 RNCRNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE-------DSYLFDLDNKdgevY 1128
Cdd:cd19208      2 KSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKlyesqnrGVYMFRIDND----H 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720401215 1129 CIDARFYGNVSRFINHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLfSCRCGSSKCR 1207
Cdd:cd19208     78 VIDATLTGGPARYINHSCAPNCVAEVVTFEKGH----KIIISSSRRIQKGEELCYDYKFDFEDDQHKI-PCHCGAVNCR 151
PHA02874 PHA02874
ankyrin repeat protein; Provisional
700-918 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 1720401215  700 MLVDGIDPNFKmeHQSKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKD 779
Cdd:PHA02874   110 ILDCGIDVNIK--DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  780 AEGSTCLHLAAKKGHYDVVQYLLSNG-QMDVNCQDdgGWTPMIWATEYKHvELVKLLLSKGSdINIRDNEENICLHWAAF 858
Cdd:PHA02874   188 NNGESPLHNAAEYGDYACIKLLIDHGnHIMNKCKN--GFTPLHNAIIHNR-SAIELLINNAS-INDQDIDGSTPLHHAIN 263
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720401215  859 SGC-VDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSrdSDVTLKNKEGETP 918
Cdd:PHA02874   264 PPCdIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDII--ANAVLIKEADKLK 322
SET_KMT2D cd19209
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...
1056-1207 3.38e-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: 3.38e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1056 RNCRNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE-------DSYLFDLDNKdgevY 1128
Cdd:cd19209      3 KSSQYRRLKTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKiyeeqnrGIYMFRINNE----H 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720401215 1129 CIDARFYGNVSRFINHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLfSCRCGSSKCR 1207
Cdd:cd19209     79 VIDATLTGGPARYINHSCAPNCVAEVVTFDKED----KIIIISSRRIPKGEELTYDYQFDFEDDQHKI-PCHCGAWNCR 152
SET_KMT2B cd19207
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...
1059-1207 3.40e-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: 74.29  E-value: 3.40e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1059 RNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE-------DSYLFDLDNKDgevyCID 1131
Cdd:cd19207      4 RFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKfydskgiGCYMFRIDDFD----VVD 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720401215 1132 ARFYGNVSRFINHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLfSCRCGSSKCR 1207
Cdd:cd19207     80 ATMHGNAARFINHSCEPNCYSRVIHVEGQK----HIVIFALRKIYRGEELTYDYKFPIEDASNKL-PCNCGAKRCR 150
SET_SETD1A cd19204
SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...
1068-1207 3.75e-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: 3.75e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1068 RARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKDgevyCIDARFYGNVS 1139
Cdd:cd19204     13 KKKLRFGRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQVVADMREKryvqegigSSYLFRVDHDT----IIDATKCGNLA 88
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720401215 1140 RFINHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGERFWDVKgklFSCRCGSSKCR 1207
Cdd:cd19204     89 RFINHCCTPNCYAKVITIESQK----KIVIYSKQPIGVNEEITYDYKFPIEDNK---IPCLCGTENCR 149
SET_NSD3 cd19212
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
1072-1206 5.11e-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: 5.11e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1072 QLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVR----EEDS----YLFDLdNKDgevYCIDARFYGNVSRFIN 1143
Cdd:cd19212      5 EIIKTERRGWGLRTKRSIKKGEFVNEYVGELIDEEECRLRikraHENSvtnfYMLTV-TKD---RIIDAGPKGNYSRFMN 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720401215 1144 HHCEPNlVPVRVFMSHQDLrfpRIAFFSTRLIQAGEQLGFDYGerfWDVKGK-LFSCRCGSSKC 1206
Cdd:cd19212     81 HSCNPN-CETQKWTVNGDV---RVGLFALCDIPAGMELTFNYN---LDCLGNgRTECHCGADNC 137
PHA02876 PHA02876
ankyrin repeat protein; Provisional
690-964 6.68e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 79.72  E-value: 6.68e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  690 RQGELQKVLLMLVDGIDPNFKMEHQskRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLI 769
Cdd:PHA02876   154 QQDELLIAEMLLEGGADVNAKDIYC--ITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  770 ---------------------------------------------------------------KAGAQVDPKDAEGSTCL 786
Cdd:PHA02876   232 dnrsninkndlsllkairnedletslllydagfsvnsiddckntplhhasqapslsrlvpkllERGADVNAKNIKGETPL 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  787 HLAAKKGhYDV--VQYLLSNGQmDVNCQDDGGWTPMIWATEY-KHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCVD 863
Cdd:PHA02876   312 YLMAKNG-YDTenIRTLIMLGA-DVNAADRLYITPLHQASTLdRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVV 389
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  864 IAEILLAAKCDLHAVNIHGDSPLHIA-ARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLSSqvwSALQMSKALRDSA 942
Cdd:PHA02876   390 IINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKN---CKLDVIEMLLDNG 466
                          330       340
                   ....*....|....*....|...
gi 1720401215  943 PD-KPVAVEKTVSRDIARGYERI 964
Cdd:PHA02876   467 ADvNAINIQNQYPLLIALEYHGI 489
PHA02878 PHA02878
ankyrin repeat protein; Provisional
719-983 3.89e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 76.46  E-value: 3.89e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  719 PLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVD-------------PKDAEGSTC 785
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSvfytlvaikdafnNRNVEIFKI 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  786 LHLAAKKGHYD------------------VVQYLLSNGQmDVNCQD-DGGWTPMIWATEYKHVELVKLLLSKGSDINIRD 846
Cdd:PHA02878   120 ILTNRYKNIQTidlvyidkkskddiieaeITKLLLSYGA-DINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPD 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  847 NEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIA-ARENRYDCVVLFLSRDSDVTLKNK-EGETPLQCASL 924
Cdd:PHA02878   199 KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIK 278
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720401215  925 SSQVWSALQMSKA---LRDSAPDKP--VAVEKtvsrdiargyeRIPIPCVNAVDSELCPTNYKY 983
Cdd:PHA02878   279 SERKLKLLLEYGAdinSLNSYKLTPlsSAVKQ-----------YLCINIGRILISNICLLKRIK 331
SET_SETD5-like cd10529
SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...
1082-1185 4.22e-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: 4.22e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1082 GVRSLQDIPLGTFVCEYVGELISDSEADVREE-----DSYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEPNlVPVRVF 1156
Cdd:cd10529     18 GLVATEDISPGEPILEYKGEVSLRSEFKEDNGffkrpSPFVFFYDGFEGLPLCVDARKYGNEARFIRRSCRPN-AELRHV 96
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1720401215 1157 MSHQDlrFPRIAFFSTRLIQAGEQ--LGFDY 1185
Cdd:cd10529     97 VVSNG--ELRLFIFALKDIRKGTEitIPFDY 125
SET_SpSET3-like cd19183
SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...
1082-1193 6.46e-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: 6.46e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1082 GVRSLQDIPLGTFVCEYVGELISdseadvreEDSYLFDLDNKDGE-------VY-------CIDARFYGNVSRFINHHCE 1147
Cdd:cd19183     15 GLFADRPIPAGDPIQELLGEIGL--------QSEYIADPENQYQIlgapkphVFfhpqsplYIDTRRSGSVARFIRRSCR 86
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1720401215 1148 PN--LVPVRVfmshQDLRFPRIAFFSTRLIQAGEQLGFDYGerfWDVK 1193
Cdd:cd19183     87 PNaeLVTVAS----DSGSVLKFVLYASRDISPGEEITIGWD---WDNP 127
PHA02875 PHA02875
ankyrin repeat protein; Provisional
692-963 8.42e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 75.03  E-value: 8.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  692 GELQKVLLMLVDGIDPNFKMehQSKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLIKA 771
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEI--YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  772 GAQVDP---KDaeGSTCLHLAAKKGHYDVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVELVKLLLSKGSDINIRDNE 848
Cdd:PHA02875    91 GKFADDvfyKD--GMTPLHLATILKKLDIMKLLIARGA-DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  849 ENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGD-SPLHIAARENRYDCVVLFLSRDSD---VTLKNKEGETPLQ---- 920
Cdd:PHA02875   168 GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADcniMFMIEGEECTILDmicn 247
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1720401215  921 -CASLSSQVWSALQMSKALRDSapdkpvavEKTVSRDiaRGYER 963
Cdd:PHA02875   248 mCTNLESEAIDALIADIAIRIH--------KKTIRRD--EGFKN 281
Ank_4 pfam13637
Ankyrin repeats (many copies);
749-802 9.43e-14

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 66.53  E-value: 9.43e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720401215  749 QRTPLMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLL 802
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
717-769 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 1720401215  717 RSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLI 769
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
693-873 2.28e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 74.15  E-value: 2.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  693 ELQKVLLMLVDGIDPNFKMEHQSKrSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLIKAG 772
Cdd:PHA02878   146 EAEITKLLLSYGADINMKDRHKGN-TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  773 AQVDPKDAEGSTCLHLAAKK-GHYDVVQYLLSNGqMDVNCQDD-GGWTPMIWATEYKHVelVKLLLSKGSDINIRDNEEN 850
Cdd:PHA02878   225 ASTDARDKCGNTPLHISVGYcKDYDILKLLLEHG-VDVNAKSYiLGLTALHSSIKSERK--LKLLLEYGADINSLNSYKL 301
                          170       180
                   ....*....|....*....|....
gi 1720401215  851 ICLHWAAFS-GCVDIAEILLAAKC 873
Cdd:PHA02878   302 TPLSSAVKQyLCINIGRILISNIC 325
SET_SETD1B cd19205
SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...
1068-1207 3.26e-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: 68.54  E-value: 3.26e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1068 RARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKDgevyCIDARFYGNVS 1139
Cdd:cd19205     13 KKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKryedegigSSYMFRVDHDT----IIDATKCGNFA 88
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720401215 1140 RFINHHCEPNLVPVRVFMSHQDlrfpRIAFFSTRLIQAGEQLGFDYGerfWDVKGKLFSCRCGSSKCR 1207
Cdd:cd19205     89 RFINHSCNPNCYAKVITVESQK----KIVIYSKQHINVNEEITYDYK---FPIEDVKIPCLCGSENCR 149
PHA02874 PHA02874
ankyrin repeat protein; Provisional
685-848 4.83e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 72.69  E-value: 4.83e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  685 LYFSARQGELQKVLLMLVDGIDPNfkMEHQSKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDA 764
Cdd:PHA02874   128 LHYAIKKGDLESIKMLFEYGADVN--IEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  765 VKYLIKAGAQVDPKDAEGSTCLHLAAKKGHyDVVQYLLSNGQmdVNCQDDGGWTPMIWATEYK-HVELVKLLLSKGSDIN 843
Cdd:PHA02874   206 IKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNAS--INDQDIDGSTPLHHAINPPcDIDIIDILLYHKADIS 282

                   ....*
gi 1720401215  844 IRDNE 848
Cdd:PHA02874   283 IKDNK 287
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
751-922 5.91e-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: 5.91e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  751 TPLMEAAENNHLDAVKYLIKAgAQVDP--KDAEGSTCLHLAAKKGHYDVVQYLLSNGQMDVN----CQDDGGWTPMIWAT 824
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKC-PSCDLfqRGALGETALHVAALYDNLEAAVVLMEAAPELVNepmtSDLYQGETALHIAV 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  825 EYKHVELVKLLLSKGSDIN--------IRDNEENICL---HWAAFSGCV---DIAEILLAAKCDLHAVNIHGDSPLHIAA 890
Cdd:cd22192     98 VNQNLNLVRELIARGADVVspratgtfFRPGPKNLIYygeHPLSFAACVgneEIVRLLIEHGADIRAQDSLGNTVLHILV 177
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1720401215  891 RENR-------YDcvvLFLSRDSDV------TLKNKEGETPLQCA 922
Cdd:cd22192    178 LQPNktfacqmYD---LILSYDKEDdlqpldLVPNNQGLTPFKLA 219
PHA02875 PHA02875
ankyrin repeat protein; Provisional
684-869 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 1720401215  684 QLYFSARQGELQKV--LLMLVDGIDPNFkmeHQSKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNH 761
Cdd:PHA02875    71 ELHDAVEEGDVKAVeeLLDLGKFADDVF---YKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGD 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  762 LDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNGQMDVNCQDDGGWTPMIWATEYKHVELVKLLLSKGSD 841
Cdd:PHA02875   148 IKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1720401215  842 INIR---DNEE--------NICLHWAAFSGCVDIAEILL 869
Cdd:PHA02875   228 CNIMfmiEGEEctildmicNMCTNLESEAIDALIADIAI 266
Ank_4 pfam13637
Ankyrin repeats (many copies);
782-836 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 1720401215  782 GSTCLHLAAKKGHYDVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVELVKLLL 836
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
853-945 4.36e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 4.36e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  853 LHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDsDVTLKNkEGETPLQCASLSSQVWSAl 932
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIV- 77
                           90
                   ....*....|...
gi 1720401215  933 qmsKALRDSAPDK 945
Cdd:pfam12796   78 ---KLLLEKGADI 87
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
1070-1186 6.93e-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: 6.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1070 RLQLYRTQDMGWGVRSLQDIPLGTFVCeyvgelisdseadvreedsylfdldnkdgevycidarfygnVSRFINHHCEPN 1149
Cdd:cd08161      1 EIRPSTIPGAGFGLFATRDIPKGEVIG-----------------------------------------LARFINHSCEPN 39
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1720401215 1150 LVPVRVFmshqDLRFPRIAFFSTRLIQAGEQLGFDYG 1186
Cdd:cd08161     40 CEFEEVY----VGGKPRVFIVALRDIKAGEELTVDYG 72
PHA03095 PHA03095
ankyrin-like protein; Provisional
697-878 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 1720401215  697 VLLMLVDGIDPNFKMEHQskRSPLHAAAEAGHVDI--CHMLVQAGANIDTCSEDQRTPLMEAAENNHLDA--VKYLIKAG 772
Cdd:PHA03095   135 IRLLLRKGADVNALDLYG--MTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRAriVRELIRAG 212
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  773 AQVDPKDAEGSTCLHLAAKKG---HYDVVQYLLSNgqMDVNCQDDGGWTPMIWATEYKHVELVKLLLSKGSDINIRDNEE 849
Cdd:PHA03095   213 CDPAATDMLGNTPLHSMATGSsckRSLVLPLLIAG--ISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG 290
                          170       180
                   ....*....|....*....|....*....
gi 1720401215  850 NICLHWAAFSGCVDIAEILLAAKCDLHAV 878
Cdd:PHA03095   291 NTPLSLMVRNNNGRAVRAALAKNPSAETV 319
PHA02876 PHA02876
ankyrin repeat protein; Provisional
716-941 3.26e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.78  E-value: 3.26e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  716 KRSPLHAAAEAGHVD-ICHMLVQAGANIDTCSEDQRTPLMEAAENNH-LDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKG 793
Cdd:PHA02876   273 KNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLD 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  794 HY-DVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAF-SGCVDIAEILLAA 871
Cdd:PHA02876   353 RNkDIVITLLELGA-NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCgTNPYMSVKTLIDR 431
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720401215  872 KCDLHAVNIHGDSPLHIAAREN-RYDCVVLFLSRDSDVTLKNKEGETPLQCA-SLSSQVWSALQMSKALRDS 941
Cdd:PHA02876   432 GANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAlEYHGIVNILLHYGAELRDS 503
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
650-929 4.16e-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: 4.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  650 PTSGLSQGPGKETLESALIALDSEKPKKLRFHPKQLYFSARQGELQKV---LLMLVDGIDPNFKMEHQSKrsplhaAAEA 726
Cdd:cd22194     20 PQSPQDDTPSNPNSPSAELAKEEQRDKKKRLKKVSEAAVEELGELLKElkdLSRRRRKTDVPDFLMHKLT------ASDT 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  727 GHVdiChmLVQAGANIDTCSEDQRTPLMEAAENNhlDAVKYLIKAgaQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNGQ 806
Cdd:cd22194     94 GKT--C--LMKALLNINENTKEIVRILLAFAEEN--GILDRFINA--EYTEEAYEGQTALNIAIERRQGDIVKLLIAKGA 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  807 mDVNCQ-----------DDG---GWTPMIWATEYKHVELVKLLLSKGSD-INIRDNEENICLHwaafsGCVDIAEillaa 871
Cdd:cd22194    166 -DVNAHakgvffnpkykHEGfyfGETPLALAACTNQPEIVQLLMEKESTdITSQDSRGNTVLH-----ALVTVAE----- 234
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720401215  872 kcdlhavnihgDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLSSQVW 929
Cdd:cd22194    235 -----------DSKTQNDFVKRMYDMILLKSENKNLETIRNNEGLTPLQLAAKMGKAE 281
PHA02876 PHA02876
ankyrin repeat protein; Provisional
755-919 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 1720401215  755 EAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVELVKL 834
Cdd:PHA02876   151 ERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGA-DVNIIALDDLSVLECAVDSKNIDTIKA 229
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  835 LLSKGSDINIRDneenICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVV-LFLSRDSDVTLKNK 913
Cdd:PHA02876   230 IIDNRSNINKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVpKLLERGADVNAKNI 305

                   ....*.
gi 1720401215  914 EGETPL 919
Cdd:PHA02876   306 KGETPL 311
PHA02798 PHA02798
ankyrin-like protein; Provisional
729-849 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 1720401215  729 VDICHMLVQAGANIDTCSEDQRTPLMEAAEN----NH-LDAVKYLIKAGAQVDPKDAEGST---CLHLAAKKGHYDVVQY 800
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHmLDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLF 130
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720401215  801 LLSNGqMDVNCQDDGGWTPM-IWATEYKHV--ELVKLLLSKGSDINIRDNEE 849
Cdd:PHA02798   131 MIENG-ADTTLLDKDGFTMLqVYLQSNHHIdiEIIKLLLEKGVDINTHNNKE 181
Ank_4 pfam13637
Ankyrin repeats (many copies);
852-902 3.73e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 3.73e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720401215  852 CLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFL 902
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
718-929 5.29e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.65  E-value: 5.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  718 SPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDV 797
Cdd:PLN03192   527 SNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKI 606
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  798 VQYL-----LSNGQM--DVNCQddggwtpmiwATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLA 870
Cdd:PLN03192   607 FRILyhfasISDPHAagDLLCT----------AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720401215  871 AKCDLHAVNIHGD-SPLH----IAARENRYDCVVLFLSRDSDVTLKNKEGETP--LQCASLSSQVW 929
Cdd:PLN03192   677 NGADVDKANTDDDfSPTElrelLQKRELGHSITIVDSVPADEPDLGRDGGSRPgrLQGTSSDNQCR 742
Ank_4 pfam13637
Ankyrin repeats (many copies);
816-869 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 1720401215  816 GWTPMIWATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILL 869
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
717-842 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 1720401215  717 RSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTClhLAAKKGHYD 796
Cdd:PLN03192   559 RTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLC--TAAKRNDLT 636
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1720401215  797 VVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVELVKLLLSKGSDI 842
Cdd:PLN03192   637 AMKELLKQG-LNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_5 pfam13857
Ankyrin repeats (many copies);
801-848 4.63e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 4.63e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1720401215  801 LLSNGQMDVNCQDDGGWTPMIWATEYKHVELVKLLLSKGSDINIRDNE 848
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE 48
Ank_5 pfam13857
Ankyrin repeats (many copies);
768-823 5.69e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 5.69e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720401215  768 LIKAG-AQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNGQmDVNCQDDGGWTPMIWA 823
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGV-DLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
793-990 7.43e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 7.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  793 GHYDVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAK 872
Cdd:PHA02875    13 GELDIARRLLDIG-INPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLG 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  873 CDLHAVNIH-GDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLSSQVwsalQMSKALrdsapdkpvaVEK 951
Cdd:PHA02875    92 KFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI----KGIELL----------IDH 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1720401215  952 TVSRDIARGYERIP-IPCVNAVDSELCP------TNYKYVSQN-CVT 990
Cdd:PHA02875   158 KACLDIEDCCGCTPlIIAMAKGDIAICKmlldsgANIDYFGKNgCVA 204
Ank_5 pfam13857
Ankyrin repeats (many copies);
868-922 1.69e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 1.69e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720401215  868 LLAAK-CDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCA 922
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
1080-1206 1.42e-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: 1.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1080 GWGVRSLQDIPlgtfvceyVGELISDSEADVREEDSYLFDLDNKDGEVYCIdarfYGNVSRFiNHHCEPNlvpVRVFMSH 1159
Cdd:cd20071     10 GRGLVATRDIE--------PGELILVEKPLVSVPSNSFSLTDGLNEIGVGL----FPLASLL-NHSCDPN---AVVVFDG 73
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720401215 1160 QDlrfpRIAFFSTRLIQAGEQLGFDYGERFWDV--------KGKLFSCRCgsSKC 1206
Cdd:cd20071     74 NG----TLRVRALRDIKAGEELTISYIDPLLPRterrrellEKYGFTCSC--PRC 122
Ank_5 pfam13857
Ankyrin repeats (many copies);
835-889 1.55e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 1.55e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720401215  835 LLSKGS-DINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIA 889
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SET_ATXR5_6-like cd10539
SET domain found in fungal protein lysine methyltransferase SET5 and similar protein; The ...
1080-1187 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 1720401215 1080 GWGVRSLQDIPLGTFVCEYVGEL--ISDSEADvrEEDSYLFDLDNKDGE---VYCIDARfyGNVSRFI----NHHCE--- 1147
Cdd:cd10539     15 GFTVEADGFIKDLTIIAEYTGDVdyIRNREFD--DNDSIMTLLLAGDPSkslVICPDKR--GNIARFIsginNHTKDgkk 90
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1720401215 1148 -PNLVPVRVFMSHQdlrfPRIAFFSTRLIQAGEQLGFDYGE 1187
Cdd:cd10539     91 kQNCKCVRYSINGE----ARVLLVATRDIAKGERLYYDYNG 127
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
729-810 1.92e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 1.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  729 VDICHM-----------LVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDV 797
Cdd:PTZ00322    84 VELCQLaasgdavgariLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163
                           90
                   ....*....|...
gi 1720401215  798 VQYLLSNGQMDVN 810
Cdd:PTZ00322   164 VQLLSRHSQCHFE 176
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
816-847 6.03e-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: 44.20  E-value: 6.03e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1720401215  816 GWTPMIWA-TEYKHVELVKLLLSKGSDINIRDN 847
Cdd:pfam00023    2 GNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
PHA03100 PHA03100
ankyrin repeat protein; Provisional
718-780 7.00e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.05  E-value: 7.00e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720401215  718 SPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKDA 780
Cdd:PHA03100   194 TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
748-837 7.34e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 7.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  748 DQRTPLMEAAENNHLDA------VKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNGQmDVNCQDDGGWTPMI 821
Cdd:PTZ00322    75 DPVVAHMLTVELCQLAAsgdavgARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA-DPTLLDKDGKTPLE 153
                           90
                   ....*....|....*.
gi 1720401215  822 WATEYKHVELVKLLLS 837
Cdd:PTZ00322   154 LAEENGFREVVQLLSR 169
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
750-845 8.10e-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: 8.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  750 RTPLMEAA-ENNHLDAVKYLIKAGAQVDpkdaEGSTCLHLAAKKGH---YDVVQYLLSNGQMDVN-------CQDD--GG 816
Cdd:TIGR00870   53 RSALFVAAiENENLELTELLLNLSCRGA----VGDTLLHAISLEYVdavEAILLHLLAAFRKSGPlelandqYTSEftPG 128
                           90       100
                   ....*....|....*....|....*....
gi 1720401215  817 WTPMIWATEYKHVELVKLLLSKGSDINIR 845
Cdd:TIGR00870  129 ITALHLAAHRQNYEIVKLLLERGASVPAR 157
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
781-811 1.29e-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: 1.29e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 1720401215   781 EGSTCLHLAAKKGHYDVVQYLLSNGQmDVNC 811
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA-DINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
781-814 1.31e-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: 43.05  E-value: 1.31e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720401215  781 EGSTCLHLAAKK-GHYDVVQYLLSNGQmDVNCQDD 814
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGA-DVNARDK 34
PHA02989 PHA02989
ankyrin repeat protein; Provisional
699-872 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 1720401215  699 LMLVDGIDPNfKMEHQSKRSPLHAAAEAGHV--DICHMLVQAGANI-DTCSEDQRTP----LMEAAENNHLDAVKYLIKA 771
Cdd:PHA02989   129 FLLSKGINVN-DVKNSRGYNLLHMYLESFSVkkDVIKILLSFGVNLfEKTSLYGLTPmniyLRNDIDVISIKVIKYLIKK 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  772 GAQVDPKDAEGSTCL------HLAAKKGHYDVVQYLLSngQMDVNCQDDGGWTPMIWATEYKHVELVKLLLSKGSDINIR 845
Cdd:PHA02989   208 GVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILK--YIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNV 285
                          170       180
                   ....*....|....*....|....*..
gi 1720401215  846 DNEENICLHWAAFSGCVDIAEILLAAK 872
Cdd:PHA02989   286 SKDGDTVLTYAIKHGNIDMLNRILQLK 312
Ank_5 pfam13857
Ankyrin repeats (many copies);
735-789 1.84e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.84e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720401215  735 LVQAG-ANIDTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLA 789
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
832-903 4.00e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 4.00e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720401215  832 VKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLS 903
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
882-934 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 1720401215  882 GDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLSSQVwSALQM 934
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNV-EVLKL 52
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
757-919 5.06e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 47.60  E-value: 5.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  757 AENNHLDAVKYLIKAGAQVDPKDAEGSTCLHlaakkghydvvQYLLSNgqmdvncqddggwtpmiwateYKHVELVKLLL 836
Cdd:PHA02716   292 ARNIDISVVYSFLQPGVKLHYKDSAGRTCLH-----------QYILRH---------------------NISTDIIKLLH 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  837 SKGSDINIRDNEENICLHwaafsgcvdiaeILLAAKCDLHAVNIHGDSPLhiaarenRYDCVVLFLSRDSDVTLKNKEGE 916
Cdd:PHA02716   340 EYGNDLNEPDNIGNTVLH------------TYLSMLSVVNILDPETDNDI-------RLDVIQCLISLGADITAVNCLGY 400

                   ...
gi 1720401215  917 TPL 919
Cdd:PHA02716   401 TPL 403
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
717-743 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 1720401215   717 RSPLHAAAEAGHVDICHMLVQAGANID 743
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
816-844 5.26e-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: 5.26e-05
                            10        20
                    ....*....|....*....|....*....
gi 1720401215   816 GWTPMIWATEYKHVELVKLLLSKGSDINI 844
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02989 PHA02989
ankyrin repeat protein; Provisional
696-922 6.41e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 47.04  E-value: 6.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  696 KVLLMLVD-GIDPNFK--MEhqskrSPLHAAAEAGHVD------ICHMLVQAGANIDTCSEDQRTPLMEAAEN---NHLD 763
Cdd:PHA02989    51 KIVKLLIDnGADVNYKgyIE-----TPLCAVLRNREITsnkikkIVKLLLKFGADINLKTFNGVSPIVCFIYNsniNNCD 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  764 AVKYLIKAGAQV-DPKDAEGSTCLH--LAAKKGHYDVVQYLLSNGQMDVNCQDDGGWTPM-IW---ATEYKHVELVKLLL 836
Cdd:PHA02989   126 MLRFLLSKGINVnDVKNSRGYNLLHmyLESFSVKKDVIKILLSFGVNLFEKTSLYGLTPMnIYlrnDIDVISIKVIKYLI 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  837 SKGSDInirdnEENICLHWAAFSGCVDIAEILLAaKC-----------DLHAVNIHGDSPLHIAARENRYDCVVLFLSRD 905
Cdd:PHA02989   206 KKGVNI-----ETNNNGSESVLESFLDNNKILSK-KEfkvlnfilkyiKINKKDKKGFNPLLISAKVDNYEAFNYLLKLG 279
                          250
                   ....*....|....*..
gi 1720401215  906 SDVTLKNKEGETPLQCA 922
Cdd:PHA02989   280 DDIYNVSKDGDTVLTYA 296
SET_SETD5 cd19181
SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...
1066-1149 6.53e-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: 6.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1066 GLRARLQL---YRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVRE---EDSYLFDL--DNKDGEVYCIDARFYGN 1137
Cdd:cd19181      1 GSQMQLQLgrvTRVQKHRKILRAARDLALDTLIIEYRGKVMLRQQFEVNGhffKRPYPFVLfySKFNGVEMCVDARTFGN 80
                           90
                   ....*....|..
gi 1720401215 1138 VSRFINHHCEPN 1149
Cdd:cd19181     81 DARFIRRSCTPN 92
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
689-770 8.76e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 8.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  689 ARQGELQKVLLMLVDGIDPNFKMEHQskRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYL 768
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDG--RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167

                   ..
gi 1720401215  769 IK 770
Cdd:PTZ00322   168 SR 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
748-776 9.47e-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: 9.47e-05
                            10        20
                    ....*....|....*....|....*....
gi 1720401215   748 DQRTPLMEAAENNHLDAVKYLIKAGAQVD 776
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
865-922 9.87e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 9.87e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720401215  865 AEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCA 922
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
789-911 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 1720401215  789 AAKKGHYDVVQYLLSNGQMD-VNCQDDGGWTPMIW-ATEYKHVELVKLLLSKGSDINIRDNeeniCLHWAA---FSGCVD 863
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKKLnINCPDRLGRSALFVaAIENENLELTELLLNLSCRGAVGDT----LLHAISleyVDAVEA 99
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720401215  864 IAEILLAAKCD----LHAVNI------HGDSPLHIAARENRYDCVVLFLSRDSDVTLK 911
Cdd:TIGR00870  100 ILLHLLAAFRKsgplELANDQytseftPGITALHLAAHRQNYEIVKLLLERGASVPAR 157
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
717-743 1.44e-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: 1.44e-04
                           10        20
                   ....*....|....*....|....*...
gi 1720401215  717 RSPLHAAAE-AGHVDICHMLVQAGANID 743
Cdd:pfam00023    3 NTPLHLAAGrRGNLEIVKLLLSKGADVN 30
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
1070-1191 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 1720401215 1070 RLQLYRTQDMGWGVRSLQDIPLGTFVcEYVGELISDSEADVREEDSYLFDLdnkdgeVYCIDARFY----GNVSRFiNHH 1145
Cdd:cd10540      1 RLEVKPSTLKGRGVFATRPIKKGEVI-EEAPVIVLPKEEYQHLCKTVLDHY------VFSWGDGCLalalGYGSMF-NHS 72
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1720401215 1146 CEPNLVPVRVFMSHqdlrfpRIAFFSTRLIQAGEQLGFDYGERFWD 1191
Cdd:cd10540     73 YTPNAEYEIDFENQ------TIVFYALRDIEAGEELTINYGDDLWD 112
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
748-779 1.99e-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: 1.99e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1720401215  748 DQRTPLMEAAE-NNHLDAVKYLIKAGAQVDPKD 779
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
SET_KMT2E cd19182
SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...
1083-1186 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 1720401215 1083 VRSLQDIPLGTFVCEYVGELISDSEAdvrEEDSYLFD--------LDNKDGEVYCIDARFYGNVSRFINHHCEPNlVPVR 1154
Cdd:cd19182     21 LKAAKDLPPDTLIIEYRGKFMLREQF---EANGYFFKrpypfvlfYSKFHGLEMCVDARTFGNEARFIRRSCTPN-AEVR 96
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1720401215 1155 VFMSHQDLrfpRIAFFSTRLIQAGEQL----GFDYG 1186
Cdd:cd19182     97 HVIEDGTI---HLYIYSIRSIPKGTEItiafDFDYG 129
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
748-776 4.26e-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: 4.26e-04
                           10        20
                   ....*....|....*....|....*....
gi 1720401215  748 DQRTPLMEAAENNHLDAVKYLIKAGAQVD 776
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
881-913 5.86e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 5.86e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1720401215  881 HGDSPLHIAA-RENRYDCVVLFLSRDSDVTLKNK 913
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
881-910 6.00e-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: 6.00e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1720401215   881 HGDSPLHIAARENRYDCVVLFLSRDSDVTL 910
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
742-888 6.52e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.50  E-value: 6.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  742 IDTCSEDQRTPLMEAAENNH--LDAVKYLIKAGAQVDPK-DAEGSTCLH--LAAKKG-HYDVVQYLLSNGQmDVNCQDDG 815
Cdd:PHA02859    44 VNDCNDLYETPIFSCLEKDKvnVEILKFLIENGADVNFKtRDNNLSALHhyLSFNKNvEPEILKILIDSGS-SITEEDED 122
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720401215  816 GWTPM-IWATEYK-HVELVKLLLSKGSDINIRDNEENICLH-WAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHI 888
Cdd:PHA02859   123 GKNLLhMYMCNFNvRINVIKLLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNCYDL 198
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
787-869 6.88e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 6.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  787 HLAAKkGHYDVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAE 866
Cdd:PTZ00322    88 QLAAS-GDAVGARILLTGGA-DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                   ...
gi 1720401215  867 ILL 869
Cdd:PTZ00322   166 LLS 168
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
816-844 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 1720401215  816 GWTPMIWATEYKHVELVKLLLSKGSDINI 844
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
781-811 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 1720401215  781 EGSTCLHLAAKKGHYDVVQYLLSNGqMDVNC 811
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENG-ADINA 30
PHA02741 PHA02741
hypothetical protein; Provisional
778-889 1.78e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 40.80  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  778 KDAEGSTCLHLAAKKGHYDVVQ----YLLSNG-QMDVNCQDDGGWTPMIWATEyKH-----VELVKLLLSKGSDINIRDN 847
Cdd:PHA02741    17 KNSEGENFFHEAARCGCFDIIArftpFIRGDChAAALNATDDAGQMCIHIAAE-KHeaqlaAEIIDHLIELGADINAQEM 95
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1720401215  848 -EENICLHWAAFSGCVDIAEILL-AAKCDLHAVNIHGDSPLHIA 889
Cdd:PHA02741    96 lEGDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFELA 139
PHA02884 PHA02884
ankyrin repeat protein; Provisional
783-891 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 1720401215  783 STCLHLAAKKGHYDVVQYLLSNGqMDVNCQ----DDGGWTPMIWATEYKHVELVKLLLSKGSDINIRDNEENIC-LHWAA 857
Cdd:PHA02884    34 ANILYSSIKFHYTDIIDAILKLG-ADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITpLYISV 112
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1720401215  858 FSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAAR 891
Cdd:PHA02884   113 LHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
717-744 2.11e-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: 2.11e-03
                           10        20
                   ....*....|....*....|....*...
gi 1720401215  717 RSPLHAAAEAGHVDICHMLVQAGANIDT 744
Cdd:pfam13606    3 NTPLHLAARNGRLEIVKLLLENGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
685-894 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 1720401215  685 LYFSARQGELQKVLLMLvdgidPNFKMEHQSKRSPLHAAAEaGHVDIC-----HMLVQAG-------AN---IDTCSEDQ 749
Cdd:TIGR00870   56 LFVAAIENENLELTELL-----LNLSCRGAVGDTLLHAISL-EYVDAVeaillHLLAAFRksgplelANdqyTSEFTPGI 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  750 rTPLMEAAENNHLDAVKYLIKAGAQVdPKDAEGSTCLhlaaKKGHYDVVQYllsngqmdvncqddgGWTPMIWATEYKHV 829
Cdd:TIGR00870  130 -TALHLAAHRQNYEIVKLLLERGASV-PARACGDFFV----KSQGVDSFYH---------------GESPLNAAACLGSP 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  830 ELVKLLLSKGSDINIRDNEENICLHWAAF------------SGCVDIAEILLAAKCDL----HAVNIHGDSPLHIAAREN 893
Cdd:TIGR00870  189 SIVALLSEDPADILTADSLGNTLLHLLVMenefkaeyeelsCQMYNFALSLLDKLRDSkeleVILNHQGLTPLKLAAKEG 268

                   .
gi 1720401215  894 R 894
Cdd:TIGR00870  269 R 269
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
735-928 3.96e-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: 3.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  735 LVQAGANIDTCSEDQRTPLMEAAENNhlDAVKYLIKAGAQVDPkdAEGSTCLHLAAKKGHYDVVQYLLSNGQmDVNCQDD 814
Cdd:cd21882     30 LHKAALNLNDGVNEAIMLLLEAAPDS--GNPKELVNAPCTDEF--YQGQTALHIAIENRNLNLVRLLVENGA-DVSARAT 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  815 G-------------GWTPMIWATEYKHVELVKLLLSKGSDI---NIRDNEENICLHwaafsgcvdiAEILLAAKcdlhav 878
Cdd:cd21882    105 GrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNTVLH----------ALVLQADN------ 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720401215  879 nihgdSPLHIAARENRYDcVVLFLSRDSDVTLK-----NKEGETPLQCASLSSQV 928
Cdd:cd21882    169 -----TPENSAFVCQMYN-LLLSYGAHLDPTQQleeipNHQGLTPLKLAAVEGKI 217
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
712-787 4.23e-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: 4.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  712 EHQSKRSPLHAAAEAGHVDICHMLVQAGANI-------------DTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQ---V 775
Cdd:cd22197     90 EYYRGHSALHIAIEKRSLQCVKLLVENGADVharacgrffqkkqGTCFYFGELPLSLAACTKQWDVVNYLLENPHQpasL 169
                           90
                   ....*....|..
gi 1720401215  776 DPKDAEGSTCLH 787
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 ...
1080-1189 4.37e-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: 4.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215 1080 GWGVRSLQDIPLGTFVCEYVGELISDSEAdvrEEDSYLFDLDNKDGEVYCIDAR--FYGNVSRFIN---HHCEPNLVpvr 1154
Cdd:cd19193     19 GLGVWAEAPIPKGMVFGPYEGEIVEDEEA---ADSGYSWQIYKGGKLSHYIDAKdeSKSNWMRYVNcarNEEEQNLV--- 92
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1720401215 1155 VFMSHQDlrfprIAFFSTRLIQAGEQLGFDYGERF 1189
Cdd:cd19193     93 AFQYRGK-----IYYRTCKDIAPGTELLVWYGDEY 122
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
714-923 6.19e-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: 6.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  714 QSKRSPLHAAAEAGHVDIChmLVQAGANIDTCSEDQRTPLMEAAENNhlDAVKYLIKAgaQVDPKDAEGSTCLHLAAKKG 793
Cdd:cd22193     14 RRKDLTDSEFTESSTGKTC--LMKALLNLNPGTNDTIRILLDIAEKT--DNLKRFINA--EYTDEYYEGQTALHIAIERR 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  794 HYDVVQYLLSNGQmDVNCQDDG--------------GWTPMIWATEYKHVELVKLLLS---KGSDINIRDNEENICLHwa 856
Cdd:cd22193     88 QGDIVALLVENGA-DVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLH-- 164
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720401215  857 afsGCVDIAEillaakcdlhavnihgDSPLHIAARENRYDCVVLF---LSRDSDV-TLKNKEGETPLQCAS 923
Cdd:cd22193    165 ---ALVTVAD----------------NTKENTKFVTRMYDMILIRgakLCPTVELeEIRNNDGLTPLQLAA 216
PHA02859 PHA02859
ankyrin repeat protein; Provisional
718-843 7.24e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.42  E-value: 7.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  718 SPLHAAAEAGHV--DICHMLVQAGANIDTCSEDQRTPLMEA----AENNHLDAVKYLIKAGAQVDPKDAEGSTCLH--LA 789
Cdd:PHA02859    53 TPIFSCLEKDKVnvEILKFLIENGADVNFKTRDNNLSALHHylsfNKNVEPEILKILIDSGSSITEEDEDGKNLLHmyMC 132
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720401215  790 AKKGHYDVVQYLLSNGQMDVNCQDDGG---WTPMIWATEYKhveLVKLLLSKGSDIN 843
Cdd:PHA02859   133 NFNVRINVIKLLIDSGVSFLNKDFDNNnilYSYILFHSDKK---IFDFLTSLGIDIN 186
PHA02946 PHA02946
ankyin-like protein; Provisional
719-886 8.98e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.04  E-value: 8.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  719 PLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPL--MEAAENNHLDAVKYLIKAGAQVDPK-DAEGSTCLhLAAKKGHY 795
Cdd:PHA02946    75 PLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKINNSvDEEGCGPL-LACTDPSE 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401215  796 DVVQYLLSNGqMDVNCQDDGGWTPM--IWATEYKHVELVKLLLSKGSDINIRDNEENICLHWAAFSGC--VDIAEILLAA 871
Cdd:PHA02946   154 RVFKKIMSIG-FEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVknVDIINLLLPS 232
                          170
                   ....*....|....*
gi 1720401215  872 KcDLHAVNIHGDSPL 886
Cdd:PHA02946   233 T-DVNKQNKFGDSPL 246
 
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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