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Conserved domains on  [gi|767958310|ref|XP_011517331|]
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histone-lysine N-methyltransferase EHMT1 isoform X24 [Homo sapiens]

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 ...
513-743 0e+00

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


:

Pssm-ID: 380933 [Multi-domain]  Cd Length: 231  Bit Score: 526.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 513 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 592
Cdd:cd10535    1 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 593 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 672
Cdd:cd10535   81 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958310 673 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 743
Cdd:cd10535  161 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 231
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
1-121 1.23e-59

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: 198.00  E-value: 1.23e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310   1 METPKSREITTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCGYFCTAGNFME 79
Cdd:cd20905   11 MESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCGLFCTQGTFVQ 90
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767958310  80 CQPESSISHRFHKDCASRVNNASYCPHCGEESS-KAKEVTIAK 121
Cdd:cd20905   91 CSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
197-453 2.84e-59

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.88  E-value: 2.84e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 197 LESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQNkrSPLHAAAEAGHVDICHMLVQAGANI 276
Cdd:COG0666   36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEAGADV 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 277 DTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIW 356
Cdd:COG0666  114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHL 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 357 ATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFL 436
Cdd:COG0666  193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
                        250
                 ....*....|....*..
gi 767958310 437 SRDSDVTLKNKEGETPL 453
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 ...
513-743 0e+00

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


Pssm-ID: 380933 [Multi-domain]  Cd Length: 231  Bit Score: 526.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 513 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 592
Cdd:cd10535    1 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 593 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 672
Cdd:cd10535   81 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958310 673 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 743
Cdd:cd10535  161 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 231
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
1-121 1.23e-59

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: 198.00  E-value: 1.23e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310   1 METPKSREITTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCGYFCTAGNFME 79
Cdd:cd20905   11 MESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCGLFCTQGTFVQ 90
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767958310  80 CQPESSISHRFHKDCASRVNNASYCPHCGEESS-KAKEVTIAK 121
Cdd:cd20905   91 CSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
197-453 2.84e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.88  E-value: 2.84e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 197 LESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQNkrSPLHAAAEAGHVDICHMLVQAGANI 276
Cdd:COG0666   36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEAGADV 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 277 DTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIW 356
Cdd:COG0666  114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHL 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 357 ATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFL 436
Cdd:COG0666  193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
                        250
                 ....*....|....*..
gi 767958310 437 SRDSDVTLKNKEGETPL 453
Cdd:COG0666  273 LALLLLAAALLDLLTLL 289
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
603-725 9.69e-40

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: 142.47  E-value: 9.69e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310   603 ARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKdgevYCIDARFYGNVSR 674
Cdd:smart00317   1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKaydtdgakAFYLFDIDSD----LCIDARRKGNLAR 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767958310   675 FINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGERFWD 725
Cdd:smart00317  77 FINHSCEPNCELLFVEVNGDD----RIVIFALRDIKPGEELTIDYGSDYAN 123
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
614-720 3.62e-29

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: 112.23  E-value: 3.62e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310  614 GWGVRSLQDIPPGTFVCEYVGE-LISDSEADVREE-----------DSYLFDLDNKDGevYCIDAR--FYGNVSRFINHH 679
Cdd:pfam00856   1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELlyydklelrlwGPYLFTLDEDSE--YCIDARalYYGNWARFINHS 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 767958310  680 CEPNLVPVRVFMAhqdlRFPRIAFFSTRLIEAGEQLGFDYG 720
Cdd:pfam00856  79 CDPNCEVRVVYVN----GGPRIVIFALRDIKPGEELTIDYG 115
Ank_2 pfam12796
Ankyrin repeats (3 copies);
287-380 5.76e-29

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 110.59  E-value: 5.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310  287 LMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNgqMDVNCQDDgGWTPMIWATEYKHVDLV 366
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDN-GRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 767958310  367 KLLLSKGSDINIRD 380
Cdd:pfam12796  78 KLLLEKGADINVKD 91
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
613-742 2.65e-28

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 110.44  E-value: 2.65e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 613 MGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDS-----YLFDLDNKDGevycIDARFYGNVSRFINHHCEPNLVPV 687
Cdd:COG2940   16 HGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKeplhtYLFELDDDGV----IDGALGGNPARFINHSCDPNCEAD 91
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767958310 688 RvfmahqdlRFPRIAFFSTRLIEAGEQLGFDYGERFWDikgKLFSCRCgsPKCRH 742
Cdd:COG2940   92 E--------EDGRIFIVALRDIAAGEELTYDYGLDYDE---EEYPCRC--PNCRG 133
PHA03100 PHA03100
ankyrin repeat protein; Provisional
227-460 4.48e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 111.68  E-value: 4.48e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 227 ELQKVLLMLVDGIDPNFKMehqnKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNH-----LEAVKY 301
Cdd:PHA03100  16 KNIKYIIMEDDLNDYSYKK----PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 302 LIKAGALVDPKDAEGSTCLHLAA--KKGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVDL--VKLLLSKGSDIN 377
Cdd:PHA03100  92 LLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDIN 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 378 IRDNeeniclhwaafsgcvdiAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCAS 457
Cdd:PHA03100 171 AKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233

                 ...
gi 767958310 458 LNS 460
Cdd:PHA03100 234 LNN 236
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
285-456 1.48e-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: 74.28  E-value: 1.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 285 TPLMEAAENNHLEAVKYLIKAGAlVDP--KDAEGSTCLHLAAKKGHYEVVQYLLSNGQMDVN----CQDDGGWTPMIWAT 358
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCPS-CDLfqRGALGETALHVAALYDNLEAAVVLMEAAPELVNepmtSDLYQGETALHIAV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 359 EYKHVDLVKLLLSKGSDIN--------IRDNEENICL---HWAAFSGCV---DIAEILLAAKCDLHAVNIHGDSPLHIAA 424
Cdd:cd22192   98 VNQNLNLVRELIARGADVVspratgtfFRPGPKNLIYygeHPLSFAACVgneEIVRLLIEHGADIRAQDSLGNTVLHILV 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767958310 425 RENR-------YDcvvLFLSRDSDV------TLKNKEGETPLQCA 456
Cdd:cd22192  178 LQPNktfacqmYD---LILSYDKEDdlqpldLVPNNQGLTPFKLA 219
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
284-379 7.20e-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: 49.69  E-value: 7.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310  284 RTPLMEAA-ENNHLEAVKYLIKAGALVDpkdaEGSTCLHLAAKKGH---YEVVQYLLSNGQMDVN-------CQDD--GG 350
Cdd:TIGR00870  53 RSALFVAAiENENLELTELLLNLSCRGA----VGDTLLHAISLEYVdavEAILLHLLAAFRKSGPlelandqYTSEftPG 128
                          90       100
                  ....*....|....*....|....*....
gi 767958310  351 WTPMIWATEYKHVDLVKLLLSKGSDINIR 379
Cdd:TIGR00870 129 ITALHLAAHRQNYEIVKLLLERGASVPAR 157
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
315-345 1.38e-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: 42.19  E-value: 1.38e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 767958310   315 EGSTCLHLAAKKGHYEVVQYLLSNGQmDVNC 345
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 ...
513-743 0e+00

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


Pssm-ID: 380933 [Multi-domain]  Cd Length: 231  Bit Score: 526.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 513 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 592
Cdd:cd10535    1 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 593 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 672
Cdd:cd10535   81 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958310 673 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 743
Cdd:cd10535  161 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 231
SET_EHMT cd10543
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
513-743 3.06e-168

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: 483.76  E-value: 3.06e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 513 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 592
Cdd:cd10543    1 PDFLYVTENCETSPLNIDRNITSLQTCSCRDDCSSDNCVCGRLSVRCWYDKEGRLLPDFNKLDPPLIFECNRACSCWRNC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 593 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 672
Cdd:cd10543   81 RNRVVQNGIRYRLQLFRTRGMGWGVRALQDIPKGTFVCEYIGELISDSEADSREDDSYLFDLDNKDGETYCIDARRYGNI 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958310 673 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 743
Cdd:cd10543  161 SRFINHLCEPNLIPVRVFVEHQDLRFPRIAFFASRDIKAGEELGFDYGEKFWRIKGKYFTCRCGSPKCKYS 231
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
513-751 2.09e-156

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: 454.09  E-value: 2.09e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 513 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 592
Cdd:cd10533    1 EDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRNC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 593 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 672
Cdd:cd10533   81 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNI 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767958310 673 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHSSAALAQRQ 751
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) ...
513-720 1.38e-104

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: 319.70  E-value: 1.38e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 513 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLS-MRCWYDKDGRLLPefnMAEPPLIFECNHACSCWRN 591
Cdd:cd10538    1 PSFTYIKDNIVGKNVQPFSNIIDSVGCKCKDDCLDSKCACAAESdGIFAYTKNGLLRL---NNSPPPIFECNSKCSCDDD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 592 CRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE------DSYLFDLDN-----KDGE 660
Cdd:cd10538   78 CKNRVVQRGLQARLQVFRTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRGKiydksgGSYLFDLDEfsdsdGDGE 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 661 VYCIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYG 720
Cdd:cd10538  158 ELCVDATFCGNVSRFINHSCDPNLFPFNVVIDHDDLRYPRIALFATRDILPGEELTFDYG 217
SET_SETDB1 cd10517
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
490-741 5.13e-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: 236.80  E-value: 5.13e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 490 DIARGYERIPIPCVNAVDSEPcPSNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCS-SSNCMCGQLS---MRCWYDKDG 565
Cdd:cd10517    8 DISYGKEGVPIPCVNEIDNSS-PPYVEYSKERIPGKGVNINLDPDFLVGCDCTDGCRdKSKCACQQLTieaTAATPGGQI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 566 --------RLLPEFnmaEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELI 637
Cdd:cd10517   87 npsagyqyRRLMEK---LPTGVYECNSRCKCDKRCYNRVVQNGLQVRLQVFKTEKKGWGIRCLDDIPKGSFVCIYAGQIL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 638 SDSEADVREE---DSYLFDLD------------NKDGEVYC--IDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPR 700
Cdd:cd10517  164 TEDEANEEGLqygDEYFAELDyievveklkegyESDVEEHCyiIDAKSEGNLGRYLNHSCSPNLFVQNVFVDTHDLRFPW 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 767958310 701 IAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCR 741
Cdd:cd10517  244 VAFFASRYIRAGTELTWDYNYEVGSVPGKVLYCYCGSSNCR 284
SET_SUV39H cd10542
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
513-741 9.19e-67

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: 221.40  E-value: 9.19e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 513 SNYKYVSQNCVTSPMNIDRNIthLQYCVCIDDCSSSNCMC--GQLSMRCWYDKDGRLLpeFNMAEPplIFECNHACSCWR 590
Cdd:cd10542    1 PNFQYINDYIPGDGVKIPEDF--LVGCECTEDCHNNNPTCcpAESGVKFAYDKQGRLR--LPPGTP--IYECNSRCKCGP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 591 NCRNRVVQNGLRARLQLYRTRD-MGWGVRSLQDIPPGTFVCEYVGELISDSEADVR------EEDSYLFDLD-NKDGEVY 662
Cdd:cd10542   75 DCPNRVVQRGRKVPLCIFRTSNgRGWGVKTLEDIKKGTFVMEYVGEIITSEEAERRgkiydaNGRTYLFDLDyNDDDCEY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 663 CIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDY---------GERFWDIKGKLFSC 733
Cdd:cd10542  155 TVDAAYYGNISHFINHSCDPNLAVYAVWINHLDPRLPRIAFFAKRDIKAGEELTFDYlmtgtggssESTIPKPKDVRVPC 234

                 ....*...
gi 767958310 734 RCGSPKCR 741
Cdd:cd10542  235 LCGSKNCR 242
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
1-121 1.23e-59

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: 198.00  E-value: 1.23e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310   1 METPKSREITTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCGYFCTAGNFME 79
Cdd:cd20905   11 MESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCGLFCTQGTFVQ 90
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767958310  80 CQPESSISHRFHKDCASRVNNASYCPHCGEESS-KAKEVTIAK 121
Cdd:cd20905   91 CSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
197-453 2.84e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.88  E-value: 2.84e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 197 LESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQNkrSPLHAAAEAGHVDICHMLVQAGANI 276
Cdd:COG0666   36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEAGADV 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 277 DTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIW 356
Cdd:COG0666  114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHL 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 357 ATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFL 436
Cdd:COG0666  193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
                        250
                 ....*....|....*..
gi 767958310 437 SRDSDVTLKNKEGETPL 453
Cdd:COG0666  273 LALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
200-479 4.31e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.49  E-value: 4.31e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 200 ALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKmeHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTC 279
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALA--DALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 280 SEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATE 359
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 360 YKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRD 439
Cdd:COG0666  163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 767958310 440 SDVTLKNKEGETPLQCASLNSQVWSALQMSKALQDSAPDR 479
Cdd:COG0666  243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
513-741 8.21e-53

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: 183.65  E-value: 8.21e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 513 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDD-CSSSNCMCgqlsMRCW---YDKDGRLLPEF-NMAEPplIFECNHACS 587
Cdd:cd10544    1 PDFQYTPENVPGPGADTDPNEITFPGCDCKTSsCEPETCSC----LRKYgpnYDDDGCLLDFDgKYSGP--VFECNSMCK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 588 CWRNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVR------EEDSYLFDLDN--KDG 659
Cdd:cd10544   75 CSESCQNRVVQNGLQFKLQVFKTPKKGWGLRTLEFIPKGRFVCEYAGEVIGFEEARRRtksqtkGDMNYIIVLREhlSSG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 660 EVY--CIDARFYGNVSRFINHHCEPNL--VPVRVfmahqDLRFPRIAFFSTRLIEAGEQLGFDYGERF-----------W 724
Cdd:cd10544  155 KVLetFVDPTYIGNIGRFLNHSCEPNLfmVPVRV-----DSMVPKLALFAARDIVAGEELSFDYSGEFsnsvesvtlarQ 229
                        250
                 ....*....|....*..
gi 767958310 725 DIKGKLFSCRCGSPKCR 741
Cdd:cd10544  230 DESKSRKPCLCGAENCR 246
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
232-459 4.47e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 183.23  E-value: 4.47e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 232 LLMLVDGIDPNFKMEHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDP 311
Cdd:COG0666    3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 312 KDAEGSTCLHLAAKKGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAA 391
Cdd:COG0666   83 KDDGGNTLLHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767958310 392 FSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLN 459
Cdd:COG0666  162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEN 229
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
539-720 2.97e-51

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: 178.75  E-value: 2.97e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 539 CVCIDDC--SSSNCMCGQL-SMRCWYDKDGRLLpefnmAEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTRDMGW 615
Cdd:cd10545   24 CDCKNRCtdGASDCACVKKnGGEIPYNFNGRLI-----RAKPAIYECGPLCKCPPSCYNRVTQKGLRYRLEVFKTAERGW 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 616 GVRSLQDIPPGTFVCEYVGELISDSEADVR-EEDSYLFDLDNK------DGEV---------------------YCIDAR 667
Cdd:cd10545   99 GVRSWDSIPAGSFICEYVGELLDTSEADTRsGNDDYLFDIDNRqtnrgwDGGQrldvgmsdgerssaedeesseFTIDAG 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767958310 668 FYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYG 720
Cdd:cd10545  179 SFGNVARFINHSCSPNLFVQCVLYDHNDLRLPRVMLFAADNIPPLQELTYDYG 231
SET_SETDB cd10541
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...
539-741 9.17e-49

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: 171.96  E-value: 9.17e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 539 CVCIDDC-SSSNCMCGQLSMRCWYDKDG-----------RLLPEfnmAEPPLIFECNHACSCWRN-CRNRVVQNGLRARL 605
Cdd:cd10541   18 CDCTDGCrDKSKCACHQLTIQATACTPGgqdnptagyqyKRLEE---CLPTGVYECNKLCKCDPNmCQNRLVQHGLQVRL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 606 QLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEAD---VREEDSYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEP 682
Cdd:cd10541   95 QLFKTQNKGWGIRCLDDIAKGTFVCIYAGKILTDDFADkegLEMGDEYFANLDHIEESCYIIDAKLEGNLGRYLNHSCSP 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767958310 683 NLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCR 741
Cdd:cd10541  175 NLFVQNVFVDTHDLRFPWVAFFASKRIKAGTELTWDYNYEVGSVEGKELLCCCGSNECR 233
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
514-741 7.54e-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: 164.68  E-value: 7.54e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 514 NYKYVSQNCVTSPMNIDRNITHlqyCVCiDDCSSS---NCMCGQLSMRCWYDKDGRLLPefnMAEPPlIFECNHACSCWR 590
Cdd:cd10525    2 DFVYINEYKVGEGVTLNQVAVG---CEC-QDCLSQpvgGCCPGASKHRFAYNEQGQVKV---RPGLP-IYECNSRCRCGP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 591 NCRNRVVQNGLRARLQLYRTRD-MGWGVRSLQDIPPGTFVCEYVGELISDSEADVR------EEDSYLFDLDNKDgEVYC 663
Cdd:cd10525   74 DCPNRVVQKGIQYDLCIFRTDNgRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRgqiydrQGATYLFDLDYVE-DVYT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 664 IDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDY---------------------GER 722
Cdd:cd10525  153 VDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIALFATRTIRAGEELTFDYnmqvdpvdaestkmdsnfglaGLP 232
                        250
                 ....*....|....*....
gi 767958310 723 FWDIKGKLFSCRCGSPKCR 741
Cdd:cd10525  233 GSPKKRVRIECKCGVRSCR 251
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
539-741 1.56e-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: 163.14  E-value: 1.56e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 539 CVCIDdCSSSNCMCGQLSMRCWYDKDGRLlpefnMAEPPL-IFECNHACSCWRNCRNRVVQNGLRARLQLYRTRD-MGWG 616
Cdd:cd10532   25 CDCSD-CFFGKCCPAEAGVLFAYNEHGQL-----KIPPGTpIYECNSRCKCGPDCPNRVVQKGTQYSLCIFRTSNgRGWG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 617 VRSLQDIPPGTFVCEYVGELISDSEADVREE------DSYLFDLDNKDGEvYCIDARFYGNVSRFINHHCEPNLVPVRVF 690
Cdd:cd10532   99 VKTLQKIKKNSFVMEYVGEVITSEEAERRGQfydskgITYLFDLDYESDE-FTVDAARYGNVSHFVNHSCDPNLQVFNVF 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958310 691 MAHQDLRFPRIAFFSTRLIEAGEQLGFDY-----GERFWDI-------KGKLFSCRCGSPKCR 741
Cdd:cd10532  178 IDNLDTRLPRIALFSTRTIKAGEELTFDYqmkgsGDLSSDSidnspakKRVRTVCKCGAVTCR 240
SET_SUV39H_DIM5-like cd19473
SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...
539-741 1.57e-44

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: 161.33  E-value: 1.57e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 539 CVCIDDCSSSNCMCGQLSMRCWY---DKDGRLLPEFNMAEPPlIFECNHACSCWRNCRNRVVQNGLRARLQLYRTRD-MG 614
Cdd:cd19473   39 CLCLQDVDPDDDRDPGKKKNAYHssgAKKGCLRGHMLNSRLP-IYECHEGCACSDDCPNRVVERGRKVPLQIFRTSDgRG 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 615 WGVRSLQDIPPGTFVCEYVGELISDSEADVREEDS--------YLFDLDN----------KDGEVYCIDARFYGNVSRFI 676
Cdd:cd19473  118 WGVRSTVDIKRGQFVDCYVGEIITPEEAQRRRDAAtiaqrkdvYLFALDKfsdpdsldprLRGDPYEIDGEFMSGPTRFI 197
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767958310 677 NHHCEPNLvpvRVFM---AHQDLRFPRIAFFSTRLIEAGEQLGFDY--------GERFWDIKGK-LFSCRCGSPKCR 741
Cdd:cd19473  198 NHSCDPNL---RIFArvgDHADKHIHDLAFFAIKDIPRGTELTFDYvdgvtgldDDAGDEEKEKeMTKCLCGSPKCR 271
SET_SUV39H_Clr4-like cd20073
SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 ...
542-741 4.27e-44

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: 159.66  E-value: 4.27e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 542 IDDCSSSNCMCGQLSMRCWYDKDGRLlpefNMAEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQ 621
Cdd:cd20073   36 LNNPGSCQCLEDSNEKSFAYDEYGRV----RANTGSIIYECNENCDCGINCPNRVVQRGRKLPLEIFKTKHKGWGLRCPR 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 622 DIPPGTFVCEYVGELISDSEADVREED------SYLFDLDNKDGEV---YCIDARFYGNVSRFINHHCEPNLVPVRVFMA 692
Cdd:cd20073  112 FIKAGTFIGVYLGEVITQSEAEIRGKKydnvgvTYLFDLDLFEDQVdeyYTVDAQYCGDVTRFINHSCDPNLAIYSVLRD 191
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767958310 693 HQDLRFPRIAFFSTRLIEAGEQLGFDYGER----------------FWDIKGKLfSCRCGSPKCR 741
Cdd:cd20073  192 KSDSKIYDLAFFAIKDIPALEELTFDYSGRnnfdqlgfignrsnskYINLKNKR-PCYCGSANCR 255
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
504-741 1.27e-42

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: 155.76  E-value: 1.27e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 504 NAVDSEPCPSNYKYVSQNCVTSpmnidrNITHLQYCVCIDDCSS-SNCMCGQLSMR-------------CWYdKDGRLLp 569
Cdd:cd10523    5 TYVQLDRNPQDQQQLVDDFDIS------NGAFVDSCDCTDGCIDiLKCACLQLTARafsksesspskggRGY-KYKRLQ- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 570 efnMAEPPLIFECNHACSCWRN-CRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELIS---------- 638
Cdd:cd10523   77 ---EPIPSGLYECNVSCKCNRMlCQNRVVQHGLQVRLQVFKTEKKGWGVRCLDDIDKGTFVCIYAGRVLSrarspteplp 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 639 -------DSEADVREEDSYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEA 711
Cdd:cd10523  154 pklelpsENEVEVVTSWLILSKKRKLRENVCFLDASKEGNVGRFLNHSCCPNLFVQNVFVDTHDKNFPWVAFFTNRVVKA 233
                        250       260       270
                 ....*....|....*....|....*....|
gi 767958310 712 GEQLGFDYGERFWDIKGKLFSCRCGSPKCR 741
Cdd:cd10523  234 GTELTWDYSYDAGTSPEQEIPCLCGVNKCQ 263
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
603-725 9.69e-40

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: 142.47  E-value: 9.69e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310   603 ARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKdgevYCIDARFYGNVSR 674
Cdd:smart00317   1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKaydtdgakAFYLFDIDSD----LCIDARRKGNLAR 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767958310   675 FINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGERFWD 725
Cdd:smart00317  77 FINHSCEPNCELLFVEVNGDD----RIVIFALRDIKPGEELTIDYGSDYAN 123
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
605-741 4.67e-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: 132.38  E-value: 4.67e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 605 LQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVR--------EEDSYLFDLdnKDGEVycIDARFYGNVSRFI 676
Cdd:cd10531    2 LELFRTEKKGWGVKAKEDIQKGEFIIEYVGEVIDKKEFKERldeyeelgKSNFYILSL--SDDVV--IDATRKGNLSRFI 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767958310 677 NHHCEPNLVpVRVFMAhqdLRFPRIAFFSTRLIEAGEQLGFDYGerFWDIKGKLFSCRCGSPKCR 741
Cdd:cd10531   78 NHSCEPNCE-TQKWIV---NGEYRIGIFALRDIPAGEELTFDYN--FVNYNEAKQVCLCGAQNCR 136
SET_SETD1-like cd10518
SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...
593-741 2.38e-33

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


Pssm-ID: 380916  Cd Length: 150  Bit Score: 125.40  E-value: 2.38e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 593 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKdgevYCI 664
Cdd:cd10518    4 RFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKrydeegggGTYMFRIDED----LVI 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767958310 665 DARFYGNVSRFINHHCEPNLVpVRVfMAHQDLRfpRIAFFSTRLIEAGEQLGFDYgeRFWDIKGKLFSCRCGSPKCR 741
Cdd:cd10518   80 DATKKGNIARFINHSCDPNCY-AKI-ITVDGEK--HIVIFAKRDIAPGEELTYDY--KFPIEDEEKIPCLCGAPNCR 150
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
605-741 1.02e-32

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: 123.17  E-value: 1.02e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 605 LQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNkdgevYC--------IDARFYGNVSRFI 676
Cdd:cd19174    2 LERFRTEDKGWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRMIEQYHNHSHH-----YClnldsgmvIDGYRMGNEARFV 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767958310 677 NHHCEPNLVPVRVFMAHQdlrfPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLfSCRCGSPKCR 741
Cdd:cd19174   77 NHSCDPNCEMQKWSVNGV----YRIGLFALKDIPAGEELTYDYNFHSFNVEKQQ-PCKCGSPNCR 136
SET_SETD2 cd19172
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...
603-741 7.17e-31

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


Pssm-ID: 380949 [Multi-domain]  Cd Length: 142  Bit Score: 118.07  E-value: 7.17e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 603 ARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDS--------YLFDLDNKDgevyCIDARFYGNVSR 674
Cdd:cd19172    2 AKVEVFRTEKKGWGLRAAEDLPKGTFVIEYVGEVLDEKEFKRRMKEYaregnrhyYFMALKSDE----IIDATKKGNLSR 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767958310 675 FINHHCEPNLVpVRVFMAHQDLrfpRIAFFSTRLIEAGEQLGFDYG-ERFWDIKGKlfsCRCGSPKCR 741
Cdd:cd19172   78 FINHSCEPNCE-TQKWTVNGEL---RVGFFAKRDIPAGEELTFDYQfERYGKEAQK---CYCGSPNCR 138
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
614-720 3.62e-29

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: 112.23  E-value: 3.62e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310  614 GWGVRSLQDIPPGTFVCEYVGE-LISDSEADVREE-----------DSYLFDLDNKDGevYCIDAR--FYGNVSRFINHH 679
Cdd:pfam00856   1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELlyydklelrlwGPYLFTLDEDSE--YCIDARalYYGNWARFINHS 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 767958310  680 CEPNLVPVRVFMAhqdlRFPRIAFFSTRLIEAGEQLGFDYG 720
Cdd:pfam00856  79 CDPNCEVRVVYVN----GGPRIVIFALRDIKPGEELTIDYG 115
Ank_2 pfam12796
Ankyrin repeats (3 copies);
287-380 5.76e-29

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 110.59  E-value: 5.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310  287 LMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNgqMDVNCQDDgGWTPMIWATEYKHVDLV 366
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDN-GRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 767958310  367 KLLLSKGSDINIRD 380
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Pre-SET pfam05033
Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines ...
491-595 1.99e-28

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: 109.43  E-value: 1.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310  491 IARGYERIPIPCVNAVDSEPCPSNYKYVSQNCVTSPMNIDRnithLQYCVCiDDCSSSNCMCGQLSM---RCWYDKDGRL 567
Cdd:pfam05033   1 ISKGKENVPIPVVNEVDDEPPPPDFTYITSYIYPKEFLLII----PQGCDC-GDCSSEKCSCAQLNGgefRFPYDKDGLL 75
                          90       100
                  ....*....|....*....|....*...
gi 767958310  568 LPEfnmaEPPLIFECNHACSCWRNCRNR 595
Cdd:pfam05033  76 VPE----SKPPIYECNPLCGCPPSCPNR 99
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
613-742 2.65e-28

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 110.44  E-value: 2.65e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 613 MGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDS-----YLFDLDNKDGevycIDARFYGNVSRFINHHCEPNLVPV 687
Cdd:COG2940   16 HGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKeplhtYLFELDDDGV----IDGALGGNPARFINHSCDPNCEAD 91
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767958310 688 RvfmahqdlRFPRIAFFSTRLIEAGEQLGFDYGERFWDikgKLFSCRCgsPKCRH 742
Cdd:COG2940   92 E--------EDGRIFIVALRDIAAGEELTYDYGLDYDE---EEYPCRC--PNCRG 133
SET_EZH cd10519
SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...
604-720 2.86e-27

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: 106.94  E-value: 2.86e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 604 RLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVRE--ED----SYLFDLDNKdgevYCIDARFYGNVSRFIN 677
Cdd:cd10519    2 RLLLGKSDVAGWGLFLKEPIKKDEFIGEYTGELISQDEADRRGkiYDkynsSYLFNLNDQ----FVVDATRKGNKIRFAN 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767958310 678 HHCEPNLVPvRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDYG 720
Cdd:cd10519   78 HSSNPNCYA-KVMMVNGD---HRIGIFAKRDIEAGEELFFDYG 116
PHA03100 PHA03100
ankyrin repeat protein; Provisional
227-460 4.48e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 111.68  E-value: 4.48e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 227 ELQKVLLMLVDGIDPNFKMehqnKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNH-----LEAVKY 301
Cdd:PHA03100  16 KNIKYIIMEDDLNDYSYKK----PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 302 LIKAGALVDPKDAEGSTCLHLAA--KKGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVDL--VKLLLSKGSDIN 377
Cdd:PHA03100  92 LLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDIN 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 378 IRDNeeniclhwaafsgcvdiAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCAS 457
Cdd:PHA03100 171 AKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233

                 ...
gi 767958310 458 LNS 460
Cdd:PHA03100 234 LNN 236
SET_NSD cd19173
SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...
603-740 1.04e-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: 103.16  E-value: 1.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 603 ARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDS--------YLFDLDNKdgevYCIDARFYGNVSR 674
Cdd:cd19173    2 PPTEPFKTGDRGWGLRTKRDIKKGDFVIEYVGELIDEEECRRRLKKAhennitnfYMLTLDKD----RIIDAGPKGNLSR 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767958310 675 FINHHCEPNLvPVRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDYGerfWDIKG-KLFSCRCGSPKC 740
Cdd:cd19173   78 FMNHSCQPNC-ETQKWTVNGD---TRVGLFAVRDIPAGEELTFNYN---LDCLGnEKKVCRCGAPNC 137
PreSET smart00468
N-terminal to some SET domains; A Cys-rich putative Zn2+-binding domain that occurs N-terminal ...
489-587 1.48e-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: 101.34  E-value: 1.48e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310   489 RDIARGYERIPIPCVNAVDSEPCPSNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSN-CMCGQLSMRCW-YDKDGR 566
Cdd:smart00468   2 LDISNGKENVPVPLVNEVDEDPPPPDFEYISEYIYGQGVPIDRSPSPLVGCSCSGDCSSSNkCECARKNGGEFaYELNGG 81
                           90       100
                   ....*....|....*....|.
gi 767958310   567 LLPEfnmaEPPLIFECNHACS 587
Cdd:smart00468  82 LRLK----RKPLIYECNSRCS 98
SET_ASHR3-like cd19175
SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...
604-741 2.57e-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: 102.11  E-value: 2.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 604 RLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVR--------EEDSYLFDLDnKDgevYCIDARFYGNVSRF 675
Cdd:cd19175    1 KMKLVKTEKCGWGLVADEDINAGEFIIEYVGEVIDDKTCEERlwdmkhkgEKNFYMCEID-KD---MVIDATFKGNLSRF 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767958310 676 INHHCEPNLVpVRVFMAHQDLrfpRIAFFSTRLIEAGEQLGFDYgeRFWDIkGKLFSCRCGSPKCR 741
Cdd:cd19175   77 INHSCDPNCE-LQKWQVDGET---RIGVFAIRDIKKGEELTYDY--QFVQF-GADQDCHCGSKNCR 135
Ank_2 pfam12796
Ankyrin repeats (3 copies);
254-347 4.67e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 99.42  E-value: 4.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310  254 LHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKaGALVDPKDaEGSTCLHLAAKKGHYEVVQ 333
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|....
gi 767958310  334 YLLSNGQmDVNCQD 347
Cdd:pfam12796  79 LLLEKGA-DINVKD 91
SET_SETD1 cd19169
SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...
599-741 5.03e-24

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: 98.56  E-value: 5.03e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 599 NGLRAR---LQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--------DSYLFDLDnkdgEVYCIDAR 667
Cdd:cd19169    6 NQLKFRkkqLKFAKSRIHDWGLFALEPIAADEMVIEYVGQVIRQSVADEREKryeaigigSSYLFRVD----DDTIIDAT 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767958310 668 FYGNVSRFINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGERFWDIKgklFSCRCGSPKCR 741
Cdd:cd19169   82 KCGNLARFINHSCNPNCYAKIITVESQK----KIVIYSKRPIAVNEEITYDYKFPIEDEK---IPCLCGAPQCR 148
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
602-741 8.96e-24

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: 98.27  E-value: 8.96e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 602 RARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVRE---EDS----YLFDLDNKdgevYCIDARFYGNVSR 674
Cdd:cd19171   13 RSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREkiyESQnrgiYMFRIDND----WVIDATMTGGPAR 88
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767958310 675 FINHHCEPNLVpVRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLfSCRCGSPKCR 741
Cdd:cd19171   89 YINHSCNPNCV-AEVVTFDKE---KKIIIISNRRIAKGEELTYDYKFDFEDDQHKI-PCLCGAPNCR 150
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
614-725 4.52e-23

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: 95.10  E-value: 4.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 614 GWGVRSLQDIPPGTFVCEYVGELISD--SEADVREEDSYLFDLDNKDGEVYcIDARFYGNVSRFINHHCEPNLVPVRVFM 691
Cdd:cd10522   14 GLGLFAAETIAKGEFVGEYTGEVLDRweEDRDSVYHYDPLYPFDLNGDILV-IDAGKKGNLTRFINHSDQPNLELIVRTL 92
                         90       100       110
                 ....*....|....*....|....*....|....
gi 767958310 692 AHQdlrfPRIAFFSTRLIEAGEQLGFDYGERFWD 725
Cdd:cd10522   93 KGE----QHIGFVAIRDIKPGEELFISYGPKYWK 122
SET_SETD8 cd10528
SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2. ...
595-722 1.01e-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: 1.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 595 RVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE----DS------YLFDLDNKDgevYCI 664
Cdd:cd10528    9 ELILSGKEEGLKVIEIDGKGRGVIATRPFEKGDFVVEYHGDLITITEAKKREAlyakDPstgcymYYFQYKGKT---YCV 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 665 DA-RFYGNVSRFINHHC-EPNLVPVRVFMAHQdlrfPRIAFFSTRLIEAGEQLGFDYGER 722
Cdd:cd10528   86 DAtKESGRLGRLINHSKkKPNLKTKLLVIDGV----PHLILVAKRDIKPGEELLYDYGDR 141
SET_SET1 cd20072
SET domain (including post-SET domain) found in catalytic component of the Saccharomyces ...
599-741 5.70e-22

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


Pssm-ID: 380998  Cd Length: 148  Bit Score: 92.87  E-value: 5.70e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 599 NGLRAR---LQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--------DSYLFDLDnkdgEVYCIDAR 667
Cdd:cd20072    6 NQLKKRkkqLKFARSAIHNWGLYAMENISAKDMVIEYVGEVIRQQVADEREKrylrqgigSSYLFRID----DDTVVDAT 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767958310 668 FYGNVSRFINHHCEPNLVpVRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDYGERFWDIKgklFSCRCGSPKCR 741
Cdd:cd20072   82 KKGNIARFINHCCDPNCT-AKIIKVEGE---KRIVIYAKRDIAAGEELTYDYKFPREEDK---IPCLCGAPNCR 148
SET_EZH-like cd19168
SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb ...
614-723 1.86e-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: 90.33  E-value: 1.86e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 614 GWGVRSLQDIPPGTFVCEYVGELISDSEADVRE------EDSYLFDLDNKdgevYCIDARFYGNVSRFINHHCEP----N 683
Cdd:cd19168   13 GLGLFAAEDIKEGEFVIEYTGELISHDEGVRREhrrgdvSYLYLFEEQEG----IWVDAAIYGNLSRYINHATDKvktgN 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767958310 684 LVPVRVFMAHQdlrfPRIAFFSTRLIEAGEQLGFDYGERF 723
Cdd:cd19168   89 CMPKIMYVNHE----WRIKFTAIKDIKIGEELFFNYGDNF 124
SET_KMT2A_2B cd19170
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...
593-741 1.88e-21

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: 91.30  E-value: 1.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 593 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--DS-----YLFDLDnkdgEVYCID 665
Cdd:cd19170    4 RFRHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKyyESkgigcYMFRID----DDEVVD 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767958310 666 ARFYGNVSRFINHHCEPNLVPvRVfmAHQDLRfPRIAFFSTRLIEAGEQLGFDYGERFWDIKgklFSCRCGSPKCR 741
Cdd:cd19170   80 ATMHGNAARFINHSCEPNCYS-RV--VNIDGK-KHIVIFALRRILRGEELTYDYKFPIEDVK---IPCTCGSKKCR 148
PHA03100 PHA03100
ankyrin repeat protein; Provisional
221-413 1.11e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 95.50  E-value: 1.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 221 FSARQGELQKVLLMLVD-GIDPNFKMEhqNKRSPLHAAAEAGHV-----DICHMLVQAGANIDTCSEDQRTPLMEAAEN- 293
Cdd:PHA03100  40 YLAKEARNIDVVKILLDnGADINSSTK--NNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKk 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 294 -NHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEV------------------VQYLLSNGqMDVNCQDDGGWTPM 354
Cdd:PHA03100 118 sNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYG-VPINIKDVYGFTPL 196
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767958310 355 IWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVN 413
Cdd:PHA03100 197 HYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
SET_NSD2 cd19211
SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...
606-740 1.18e-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: 85.81  E-value: 1.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 606 QLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVR-----EEDS---YLFDLDnKDgevYCIDARFYGNVSRFIN 677
Cdd:cd19211    5 KIIKTEGKGWGLIAKRDIKKGEFVNEYVGELIDEEECMARikhahENDIthfYMLTID-KD---RIIDAGPKGNYSRFMN 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767958310 678 HHCEPNlVPVRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDYGerfWDIKGKLFS-CRCGSPKC 740
Cdd:cd19211   81 HSCQPN-CETQKWTVNGD---TRVGLFAVCDIPAGTELTFNYN---LDCLGNEKTvCRCGAPNC 137
SET_KMT2A cd19206
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...
593-741 1.90e-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: 1.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 593 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--DS-----YLFDLDnkDGEVycID 665
Cdd:cd19206    4 RFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREKyyDSkgigcYMFRID--DSEV--VD 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767958310 666 ARFYGNVSRFINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLfSCRCGSPKCR 741
Cdd:cd19206   80 ATMHGNAARFINHSCEPNCYSRVINIDGQK----HIVIFAMRKIYRGEELTYDYKFPIEDASNKL-PCNCGAKKCR 150
Ank_2 pfam12796
Ankyrin repeats (3 copies);
354-446 6.67e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.09  E-value: 6.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310  354 MIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLaAKCDLHAVNiHGDSPLHIAARENRYDCVV 433
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 767958310  434 LFLSRDSDVTLKN 446
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
224-483 3.35e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 88.10  E-value: 3.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 224 RQGELQKVLLMLVDGIDPNfkmeHQNKR--SPLHAAAEAGHVDICHMLVQAGANidtcsedqrTPLMEAAENNHlEAVKY 301
Cdd:PHA02874  44 RSGDAKIVELFIKHGADIN----HINTKipHPLLTAIKIGAHDIIKLLIDNGVD---------TSILPIPCIEK-DMIKT 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 302 LIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDN 381
Cdd:PHA02874 110 ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDN 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 382 eeniclhwaafsgcvdiaeillaakcdlhavniHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASL-NS 460
Cdd:PHA02874 189 ---------------------------------NGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIhNR 235
                        250       260
                 ....*....|....*....|...
gi 767958310 461 QVWSALQMSKALQDSAPDRPSPV 483
Cdd:PHA02874 236 SAIELLINNASINDQDIDGSTPL 258
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
605-740 3.40e-18

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: 81.90  E-value: 3.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 605 LQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVR-----EEDS---YLFDLDnKDgevYCIDARFYGNVSRFI 676
Cdd:cd19210    4 VEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIDEEECRARiryaqEHDItnfYMLTLD-KD---RIIDAGPKGNYARFM 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767958310 677 NHHCEPNlVPVRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDYGERFWDiKGKLfSCRCGSPKC 740
Cdd:cd19210   80 NHCCQPN-CETQKWTVNGD---TRVGLFALCDIKAGTELTFNYNLECLG-NGKT-VCKCGAPNC 137
Ank_2 pfam12796
Ankyrin repeats (3 copies);
219-313 2.47e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 2.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310  219 LYFSARQGELQKVLLMLVDGIDPNFKmeHQNKRSPLHAAAEAGHVDICHMLVQaGANIDtCSEDQRTPLMEAAENNHLEA 298
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQ--DKNGRTALHLAAKNGHLEIVKLLLE-HADVN-LKDNGRTALHYAARSGHLEI 76
                          90
                  ....*....|....*
gi 767958310  299 VKYLIKAGALVDPKD 313
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
SET_EZH1 cd19217
SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43) ...
598-719 2.69e-17

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


Pssm-ID: 380994  Cd Length: 136  Bit Score: 78.96  E-value: 2.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 598 QNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE------DSYLFDLDNKdgevYCIDARFYGN 671
Cdd:cd19217    1 QRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKvydkymSSFLFNLNND----FVVDATRKGN 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767958310 672 VSRFINHHCEPNLVpVRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDY 719
Cdd:cd19217   77 KIRFANHSVNPNCY-AKVVMVNGD---HRIGIFAKRAIQQGEELFFDY 120
SET_EZH2 cd19218
SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...
600-719 2.49e-16

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


Pssm-ID: 380995  Cd Length: 120  Bit Score: 75.72  E-value: 2.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 600 GLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREED------SYLFDLDNKdgevYCIDARFYGNVS 673
Cdd:cd19218    1 GSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVydkymcSFLFNLNND----FVVDATRKGNKI 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767958310 674 RFINHHCEPNLVpVRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDY 719
Cdd:cd19218   77 RFANHSVNPNCY-AKVMMVNGD---HRIGIFAKRAIQTGEELFFDY 118
PHA02874 PHA02874
ankyrin repeat protein; Provisional
234-452 4.29e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 81.55  E-value: 4.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 234 MLVDGIDPNFKmeHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKD 313
Cdd:PHA02874 110 ILDCGIDVNIK--DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 314 AEGSTCLHLAAKKGHYEVVQYLLSNG-QMDVNCQDdgGWTPMIWATEYKHvDLVKLLLSKGSdINIRDNEENICLHWAAF 392
Cdd:PHA02874 188 NNGESPLHNAAEYGDYACIKLLIDHGnHIMNKCKN--GFTPLHNAIIHNR-SAIELLINNAS-INDQDIDGSTPLHHAIN 263
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958310 393 SGC-VDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSrdSDVTLKNKEGETP 452
Cdd:PHA02874 264 PPCdIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDII--ANAVLIKEADKLK 322
SET_KMT2C cd19208
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) ...
590-741 5.53e-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: 75.82  E-value: 5.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 590 RNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE-------DSYLFDLDNKdgevY 662
Cdd:cd19208    2 KSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKlyesqnrGVYMFRIDND----H 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767958310 663 CIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLfSCRCGSPKCR 741
Cdd:cd19208   78 VIDATLTGGPARYINHSCAPNCVAEVVTFEKGH----KIIISSSRRIQKGEELCYDYKFDFEDDQHKI-PCHCGAVNCR 151
SET_NSD3 cd19212
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
606-740 6.02e-16

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: 75.35  E-value: 6.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 606 QLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDN-------KDgevYCIDARFYGNVSRFINH 678
Cdd:cd19212    5 EIIKTERRGWGLRTKRSIKKGEFVNEYVGELIDEEECRLRIKRAHENSVTNfymltvtKD---RIIDAGPKGNYSRFMNH 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958310 679 HCEPNlVPVRVFMAHQDLrfpRIAFFSTRLIEAGEQLGFDYGerfWDIKGK-LFSCRCGSPKC 740
Cdd:cd19212   82 SCNPN-CETQKWTVNGDV---RVGLFALCDIPAGMELTFNYN---LDCLGNgRTECHCGADNC 137
SET_KMT2D cd19209
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...
590-741 7.79e-16

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: 75.50  E-value: 7.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 590 RNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE-------DSYLFDLDNKdgevY 662
Cdd:cd19209    3 KSSQYRRLKTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKiyeeqnrGIYMFRINNE----H 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767958310 663 CIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLfSCRCGSPKCR 741
Cdd:cd19209   79 VIDATLTGGPARYINHSCAPNCVAEVVTFDKED----KIIIISSRRIPKGEELTYDYQFDFEDDQHKI-PCHCGAWNCR 152
SET_SETD1A cd19204
SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...
602-741 1.02e-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: 75.06  E-value: 1.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 602 RARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKDgevyCIDARFYGNVS 673
Cdd:cd19204   13 KKKLRFGRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQVVADMREKryvqegigSSYLFRVDHDT----IIDATKCGNLA 88
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767958310 674 RFINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGerfWDIKGKLFSCRCGSPKCR 741
Cdd:cd19204   89 RFINHCCTPNCYAKVITIESQK----KIVIYSKQPIGVNEEITYDYK---FPIEDNKIPCLCGTENCR 149
SET_SETD5-like cd10529
SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...
616-719 1.33e-15

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: 73.85  E-value: 1.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 616 GVRSLQDIPPGTFVCEYVGELISDSEADVREE-----DSYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEPNlVPVRVF 690
Cdd:cd10529   18 GLVATEDISPGEPILEYKGEVSLRSEFKEDNGffkrpSPFVFFYDGFEGLPLCVDARKYGNEARFIRRSCRPN-AELRHV 96
                         90       100       110
                 ....*....|....*....|....*....|.
gi 767958310 691 MAHQDlrFPRIAFFSTRLIEAGEQ--LGFDY 719
Cdd:cd10529   97 VVSNG--ELRLFIFALKDIRKGTEitIPFDY 125
PHA03095 PHA03095
ankyrin-like protein; Provisional
288-453 2.33e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 79.30  E-value: 2.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 288 MEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHY---EVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHV- 363
Cdd:PHA03095  19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAG-ADVNAPERCGFTPLHLYLYNATTl 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 364 DLVKLLLSKGSDINIRDNEENICLHWAAFSGCVD--IAEILLAAKCDLHAVNIHGDSPLHIAARENRYD--CVVLFLSRD 439
Cdd:PHA03095  98 DVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLLIDAG 177
                        170
                 ....*....|....
gi 767958310 440 SDVTLKNKEGETPL 453
Cdd:PHA03095 178 ADVYAVDDRFRSLL 191
PHA02876 PHA02876
ankyrin repeat protein; Provisional
224-478 2.97e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 79.72  E-value: 2.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 224 RQGELQKVLLMLVDGIDPNFKMEHQnkRSPLHAAAEAGHVDICHMLVQAGA--------------------NIDTCSE-- 281
Cdd:PHA02876 154 QQDELLIAEMLLEGGADVNAKDIYC--ITPIHYAAERGNAKMVNLLLSYGAdvniialddlsvlecavdskNIDTIKAii 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 282 DQRT-------PLMEAAENNHLEA----------------------------------VKYLIKAGALVDPKDAEGSTCL 320
Cdd:PHA02876 232 DNRSninkndlSLLKAIRNEDLETslllydagfsvnsiddckntplhhasqapslsrlVPKLLERGADVNAKNIKGETPL 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 321 HLAAKKGH-YEVVQYLLSNGQmDVNCQDDGGWTPMIWATEY-KHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDI 398
Cdd:PHA02876 312 YLMAKNGYdTENIRTLIMLGA-DVNAADRLYITPLHQASTLdRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 399 AEILLAAKCDLHAVNIHGDSPLHIA-ARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNSqvwSALQMSKALQDSAP 477
Cdd:PHA02876 391 INTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKN---CKLDVIEMLLDNGA 467

                 .
gi 767958310 478 D 478
Cdd:PHA02876 468 D 468
SET_SpSET3-like cd19183
SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...
616-727 4.56e-15

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: 73.59  E-value: 4.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 616 GVRSLQDIPPGTFVCEYVGELISdseadvreEDSYLFDLDNKDGE-------VY-------CIDARFYGNVSRFINHHCE 681
Cdd:cd19183   15 GLFADRPIPAGDPIQELLGEIGL--------QSEYIADPENQYQIlgapkphVFfhpqsplYIDTRRSGSVARFIRRSCR 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767958310 682 PN--LVPVRVfmahQDLRFPRIAFFSTRLIEAGEQLGFDYGerfWDIK 727
Cdd:cd19183   87 PNaeLVTVAS----DSGSVLKFVLYASRDISPGEEITIGWD---WDNP 127
PHA02874 PHA02874
ankyrin repeat protein; Provisional
184-382 8.41e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 77.31  E-value: 8.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 184 PTPGLSQGPGKETLESAlIALDSEKPKKLRFhpkqLYFSARQGELQKVLLMLVDGIDPNfkMEHQNKRSPLHAAAEAGHV 263
Cdd:PHA02874  98 PIPCIEKDMIKTILDCG-IDVNIKDAELKTF----LHYAIKKGDLESIKMLFEYGADVN--IEDDNGCYPIHIAIKHNFF 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 264 DICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHyEVVQYLLSNGQmdV 343
Cdd:PHA02874 171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNAS--I 247
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767958310 344 NCQDDGGWTPMIWATEYK-HVDLVKLLLSKGSDINIRDNE 382
Cdd:PHA02874 248 NDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNK 287
SET_KMT2B cd19207
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...
593-741 9.18e-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: 72.36  E-value: 9.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 593 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE-------DSYLFDLDNKDgevyCID 665
Cdd:cd19207    4 RFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKfydskgiGCYMFRIDDFD----VVD 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767958310 666 ARFYGNVSRFINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLfSCRCGSPKCR 741
Cdd:cd19207   80 ATMHGNAARFINHSCEPNCYSRVIHVEGQK----HIVIFALRKIYRGEELTYDYKFPIEDASNKL-PCNCGAKRCR 150
PHA02875 PHA02875
ankyrin repeat protein; Provisional
226-466 2.35e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 75.80  E-value: 2.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 226 GELQKVLLMLVDGIDPNFKMehQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKA 305
Cdd:PHA02875  13 GELDIARRLLDIGINPNFEI--YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 306 GALVDP---KDaeGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNE 382
Cdd:PHA02875  91 GKFADDvfyKD--GMTPLHLATILKKLDIMKLLIARGA-DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 383 ENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGD-SPLHIAARENRYDCVVLFLSRDSD---VTLKNKEGETPLQ---- 454
Cdd:PHA02875 168 GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADcniMFMIEGEECTILDmicn 247
                        250
                 ....*....|...
gi 767958310 455 -CASLNSQVWSAL 466
Cdd:PHA02875 248 mCTNLESEAIDAL 260
PHA02875 PHA02875
ankyrin repeat protein; Provisional
249-444 2.73e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 75.80  E-value: 2.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 249 NKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGH 328
Cdd:PHA02875   1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 329 YEVVQYLLSNGQM--DVNCQDdgGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAK 406
Cdd:PHA02875  81 VKAVEELLDLGKFadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767958310 407 CDLHAVNIHGDSPLHIA-ARENRYDCVVL--------FLSRDSDVTL 444
Cdd:PHA02875 159 ACLDIEDCCGCTPLIIAmAKGDIAICKMLldsganidYFGKNGCVAA 205
PHA03100 PHA03100
ankyrin repeat protein; Provisional
242-381 4.93e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.09  E-value: 4.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 242 NFKMEHQNKRSPLHAAAEA--GHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLE------------------AVKY 301
Cdd:PHA03100  98 NVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkilkllidkgvdinaknRVNY 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 302 LIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDN 381
Cdd:PHA03100 178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA-NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
604-720 5.84e-14

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: 67.28  E-value: 5.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 604 RLQLYRTRDMGWGVRSLQDIPPGTFVCeyvgelisdseadvreedsylfdldnkdgevycidarfygnVSRFINHHCEPN 683
Cdd:cd08161    1 EIRPSTIPGAGFGLFATRDIPKGEVIG-----------------------------------------LARFINHSCEPN 39
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767958310 684 LVPVRVFmahqDLRFPRIAFFSTRLIEAGEQLGFDYG 720
Cdd:cd08161   40 CEFEEVY----VGGKPRVFIVALRDIKAGEELTVDYG 72
PHA02875 PHA02875
ankyrin repeat protein; Provisional
218-403 7.03e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 74.26  E-value: 7.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 218 QLYFSARQGELQKV--LLMLVDGIDPNFkmeHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNH 295
Cdd:PHA02875  71 ELHDAVEEGDVKAVeeLLDLGKFADDVF---YKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGD 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 296 LEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSD 375
Cdd:PHA02875 148 IKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767958310 376 INIR---DNEE--------NICLHWAAFSGCVDIAEILL 403
Cdd:PHA02875 228 CNIMfmiEGEEctildmicNMCTNLESEAIDALIADIAI 266
PHA02878 PHA02878
ankyrin repeat protein; Provisional
253-575 7.34e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 74.92  E-value: 7.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 253 PLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIK-------AGALVDPKDA------EGSTC 319
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcsvFYTLVAIKDAfnnrnvEIFKI 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 320 LHLAAKKGHY------------------EVVQYLLSNGQmDVNCQD-DGGWTPMIWATEYKHVDLVKLLLSKGSDINIRD 380
Cdd:PHA02878 120 ILTNRYKNIQtidlvyidkkskddiieaEITKLLLSYGA-DINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPD 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 381 NEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIA-ARENRYDCVVLFLSRDSDVTLKNK-EGETPLQCASL 458
Cdd:PHA02878 199 KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIK 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 459 NSQVWSALQMSKALQDSAP-DRPSPVERIVSRdiargyeRIPIPCVNAVDSEPCPSNYKYVSqncVTSPMNIDRNIthlq 537
Cdd:PHA02878 279 SERKLKLLLEYGADINSLNsYKLTPLSSAVKQ-------YLCINIGRILISNICLLKRIKPD---IKNSEGFIDNM---- 344
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 767958310 538 ycvcidDCSSSNCMCGQLSMRCWYD----KDGRLLPEFNMAE 575
Cdd:PHA02878 345 ------DCITSNKRLNQIKDKCEDElnrlASIKITNTYSFDD 380
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
285-456 1.48e-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: 74.28  E-value: 1.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 285 TPLMEAAENNHLEAVKYLIKAGAlVDP--KDAEGSTCLHLAAKKGHYEVVQYLLSNGQMDVN----CQDDGGWTPMIWAT 358
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCPS-CDLfqRGALGETALHVAALYDNLEAAVVLMEAAPELVNepmtSDLYQGETALHIAV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 359 EYKHVDLVKLLLSKGSDIN--------IRDNEENICL---HWAAFSGCV---DIAEILLAAKCDLHAVNIHGDSPLHIAA 424
Cdd:cd22192   98 VNQNLNLVRELIARGADVVspratgtfFRPGPKNLIYygeHPLSFAACVgneEIVRLLIEHGADIRAQDSLGNTVLHILV 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767958310 425 RENR-------YDcvvLFLSRDSDV------TLKNKEGETPLQCA 456
Cdd:cd22192  178 LQPNktfacqmYD---LILSYDKEDdlqpldLVPNNQGLTPFKLA 219
PHA03095 PHA03095
ankyrin-like protein; Provisional
230-438 1.50e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.52  E-value: 1.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 230 KVLLMLVD-GIDPNFKmeHQNKRSPLHA--AAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNH--LEAVKYLIK 304
Cdd:PHA03095  98 DVIKLLIKaGADVNAK--DKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLID 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 305 AGALVDPKDAEGSTCLHLAAK--KGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATEY---KHVDLVKLLLsKGSDINIR 379
Cdd:PHA03095 176 AGADVYAVDDRFRSLLHHHLQsfKPRARIVRELIRAG-CDPAATDMLGNTPLHSMATGsscKRSLVLPLLI-AGISINAR 253
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767958310 380 DNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSR 438
Cdd:PHA03095 254 NRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
Ank_4 pfam13637
Ankyrin repeats (many copies);
251-303 1.65e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 65.37  E-value: 1.65e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767958310  251 RSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLI 303
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
216-457 1.71e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.52  E-value: 1.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 216 PKQLYFSARQGELQKVLLMLVD-GIDPNFKmeHQNKRSPLHAAAEAGHV-DICHMLVQAGANIDTCSEDQRTPLmeaaen 293
Cdd:PHA03095  50 PLHLYLHYSSEKVKDIVRLLLEaGADVNAP--ERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPL------ 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 294 nHleavkylikagalvdpkdaegstcLHLAAKKGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVD--LVKLLLS 371
Cdd:PHA03095 122 -H------------------------VYLSGFNINPKVIRLLLRKG-ADVNALDLYGMTPLAVLLKSRNANveLLRLLID 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 372 KGSDINIRDNEENICLHWAAFSgCVDIAEI---LLAAKCDLHAVNIHGDSPLHIAARENRYDCVVL--FLSRDSDVTLKN 446
Cdd:PHA03095 176 AGADVYAVDDRFRSLLHHHLQS-FKPRARIvreLIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARN 254
                        250
                 ....*....|.
gi 767958310 447 KEGETPLQCAS 457
Cdd:PHA03095 255 RYGQTPLHYAA 265
PHA02878 PHA02878
ankyrin repeat protein; Provisional
227-407 2.69e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.99  E-value: 2.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 227 ELQKVLLMLVDGIDPNFKMEHQNKrSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAG 306
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHKGN-TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 307 ALVDPKDAEGSTCLHLAAKK-GHYEVVQYLLSNGqMDVNCQDD-GGWTPMiwATEYKHVDLVKLLLSKGSDINIRDNEEN 384
Cdd:PHA02878 225 ASTDARDKCGNTPLHISVGYcKDYDILKLLLEHG-VDVNAKSYiLGLTAL--HSSIKSERKLKLLLEYGADINSLNSYKL 301
                        170       180
                 ....*....|....*....|....
gi 767958310 385 ICLHWAAFS-GCVDIAEILLAAKC 407
Cdd:PHA02878 302 TPLSSAVKQyLCINIGRILISNIC 325
SET_SETD1B cd19205
SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...
602-741 5.03e-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: 67.39  E-value: 5.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 602 RARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKDgevyCIDARFYGNVS 673
Cdd:cd19205   13 KKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKryedegigSSYMFRVDHDT----IIDATKCGNFA 88
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767958310 674 RFINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGerfWDIKGKLFSCRCGSPKCR 741
Cdd:cd19205   89 RFINHSCNPNCYAKVITVESQK----KIVIYSKQHINVNEEITYDYK---FPIEDVKIPCLCGSENCR 149
Ank_4 pfam13637
Ankyrin repeats (many copies);
283-336 5.71e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 63.83  E-value: 5.71e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767958310  283 QRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLL 336
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
387-465 3.61e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 3.61e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767958310  387 LHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDsDVTLKNkEGETPLQCASLNSQVWSA 465
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIV 77
Ank_4 pfam13637
Ankyrin repeats (many copies);
316-370 1.05e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 1.05e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767958310  316 GSTCLHLAAKKGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVDLVKLLL 370
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
289-459 1.45e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.78  E-value: 1.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 289 EAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKL 368
Cdd:PHA02876 151 ERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGA-DVNIIALDDLSVLECAVDSKNIDTIKA 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 369 LLSKGSDINIRDneenICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVV-LFLSRDSDVTLKNK 447
Cdd:PHA02876 230 IIDNRSNINKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVpKLLERGADVNAKNI 305
                        170
                 ....*....|..
gi 767958310 448 EGETPLQCASLN 459
Cdd:PHA02876 306 KGETPLYLMAKN 317
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
159-463 8.34e-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: 65.55  E-value: 8.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 159 DDKLQGAASHVPEgfDPTGPAGLGRPTPGLSQGPGKETlesaliALDSEKPKKLRFHPKQLYFSARQGELQKV---LLML 235
Cdd:cd22194    3 DSNIRQCPSGNCD--DMDSPQSPQDDTPSNPNSPSAEL------AKEEQRDKKKRLKKVSEAAVEELGELLKElkdLSRR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 236 VDGIDPNFKMEHQNKrsplhaAAEAGHVdiChmLVQAGANIDTCSEDQRTPLMEAAENNHLeaVKYLIKAGalVDPKDAE 315
Cdd:cd22194   75 RRKTDVPDFLMHKLT------ASDTGKT--C--LMKALLNINENTKEIVRILLAFAEENGI--LDRFINAE--YTEEAYE 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 316 GSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQ-----------DDG---GWTPMIWATEYKHVDLVKLLLSKGSD-INIRD 380
Cdd:cd22194  141 GQTALNIAIERRQGDIVKLLIAKGA-DVNAHakgvffnpkykHEGfyfGETPLALAACTNQPEIVQLLMEKESTdITSQD 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 381 NEENICLHwaafsGCVDIAEillaakcdlhavnihgDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNS 460
Cdd:cd22194  220 SRGNTVLH-----ALVTVAE----------------DSKTQNDFVKRMYDMILLKSENKNLETIRNNEGLTPLQLAAKMG 278

                 ...
gi 767958310 461 QVW 463
Cdd:cd22194  279 KAE 281
PHA02876 PHA02876
ankyrin repeat protein; Provisional
224-475 1.00e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.08  E-value: 1.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 224 RQGELQKVLLMLVDGIDPNFKMEHQNkrSPLHAAAEAGHVD-ICHMLVQAGANIDTCSEDQRTPLMEAAENNH-LEAVKY 301
Cdd:PHA02876 249 RNEDLETSLLLYDAGFSVNSIDDCKN--TPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRT 326
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 302 LIKAGALVDPKDAEGSTCLHLAAKKGHY-EVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRD 380
Cdd:PHA02876 327 LIMLGADVNAADRLYITPLHQASTLDRNkDIVITLLELGA-NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALS 405
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 381 NEENICLHWAAF-SGCVDIAEILLAAKCDLHAVNIHGDSPLHIAAREN-RYDCVVLFLSRDSDVTLKNKEGETPLQCA-S 457
Cdd:PHA02876 406 QKIGTALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAlE 485
                        250
                 ....*....|....*...
gi 767958310 458 LNSQVWSALQMSKALQDS 475
Cdd:PHA02876 486 YHGIVNILLHYGAELRDS 503
PHA03095 PHA03095
ankyrin-like protein; Provisional
231-412 6.84e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.96  E-value: 6.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 231 VLLMLVDGIDPNFKMEHQnkRSPLHAAAEAGHVDI--CHMLVQAGANIDTCSEDQRTPLmeaaeNNHLEAVK-------Y 301
Cdd:PHA03095 135 IRLLLRKGADVNALDLYG--MTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLL-----HHHLQSFKprarivrE 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 302 LIKAGALVDPKDAEGSTCLHLAAKKGHYE---VVQYLLSNgqMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINI 378
Cdd:PHA03095 208 LIRAGCDPAATDMLGNTPLHSMATGSSCKrslVLPLLIAG--ISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285
                        170       180       190
                 ....*....|....*....|....*....|....
gi 767958310 379 RDNEENICLHWAAFSGCVDIAEILLAAKCDLHAV 412
Cdd:PHA03095 286 VSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
PHA02798 PHA02798
ankyrin-like protein; Provisional
263-383 2.59e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 60.23  E-value: 2.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 263 VDICHMLVQAGANIDTCSEDQRTPLMEAAEN----NH-LEAVKYLIKAGALVDPKDAEGST---CLHLAAKKGHYEVVQY 334
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHmLDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLF 130
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767958310 335 LLSNGqMDVNCQDDGGWTPM-IWATEYKHVDL--VKLLLSKGSDINIRDNEE 383
Cdd:PHA02798 131 MIENG-ADTTLLDKDGFTMLqVYLQSNHHIDIeiIKLLLEKGVDINTHNNKE 181
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
246-463 2.75e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.65  E-value: 2.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 246 EHQNKR--SPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLA 323
Cdd:PLN03192 519 EHDDPNmaSNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNA 598
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 324 AKKGHYEVVQYL-----LSNGQM--DVNCQddggwtpmiwATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCV 396
Cdd:PLN03192 599 ISAKHHKIFRILyhfasISDPHAagDLLCT----------AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHV 668
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767958310 397 DIAEILLAAKCDLHAVNIHGD-SPLH----IAARENRYDCVVLFLSRDSDVTLKNKEGETP--LQCASLNSQVW 463
Cdd:PLN03192 669 DMVRLLIMNGADVDKANTDDDfSPTElrelLQKRELGHSITIVDSVPADEPDLGRDGGSRPgrLQGTSSDNQCR 742
Ank_4 pfam13637
Ankyrin repeats (many copies);
386-436 5.83e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 5.83e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767958310  386 CLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFL 436
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
350-403 3.86e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 3.86e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767958310  350 GWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILL 403
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
335-382 8.54e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 8.54e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 767958310  335 LLSNGQMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNE 382
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE 48
Ank_5 pfam13857
Ankyrin repeats (many copies);
302-357 9.24e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 9.24e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767958310  302 LIKAG-ALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWA 357
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGV-DLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
219-345 3.10e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.10  E-value: 3.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 219 LYFSARQGELQKVLLMLVDGIdpNFKMEHQNKRSPLHAAAEAGHVDICHMLVQ-AGANIDTCSEDQrtpLMEAAENNHLE 297
Cdd:PLN03192 562 LHIAASKGYEDCVLVLLKHAC--NVHIRDANGNTALWNAISAKHHKIFRILYHfASISDPHAAGDL---LCTAAKRNDLT 636
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767958310 298 AVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNC 345
Cdd:PLN03192 637 AMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA-DVDK 683
Ank_5 pfam13857
Ankyrin repeats (many copies);
402-456 3.30e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 3.30e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767958310  402 LLAAK-CDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCA 456
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
263-344 2.20e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 2.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 263 VDICHM-----------LVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEV 331
Cdd:PTZ00322  84 VELCQLaasgdavgariLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163
                         90
                 ....*....|...
gi 767958310 332 VQYLLSNGQMDVN 344
Cdd:PTZ00322 164 VQLLSRHSQCHFE 176
Ank_5 pfam13857
Ankyrin repeats (many copies);
369-423 2.92e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 2.92e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767958310  369 LLSKGS-DINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIA 423
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SET_ATXR5_6-like cd10539
SET domain found in fungal protein lysine methyltransferase SET5 and similar protein; The ...
614-721 3.52e-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: 47.02  E-value: 3.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 614 GWGVRSLQDIPPGTFVCEYVGEL--ISDSEADvrEEDSYLFDLDNKDGE---VYCIDARfyGNVSRFI----NHHCE--- 681
Cdd:cd10539   15 GFTVEADGFIKDLTIIAEYTGDVdyIRNREFD--DNDSIMTLLLAGDPSkslVICPDKR--GNIARFIsginNHTKDgkk 90
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767958310 682 -PNLVPVRVFMAHQdlrfPRIAFFSTRLIEAGEQLGFDYGE 721
Cdd:cd10539   91 kQNCKCVRYSINGE----ARVLLVATRDIAKGERLYYDYNG 127
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
614-740 3.95e-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: 46.60  E-value: 3.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 614 GWGVRSLQDIPPGTFVCeyvgelisdSEADVREEDSYLFDLDNKDGEVYCidaRFYGNVSRFiNHHCEPNLVpvrvfmaH 693
Cdd:cd20071   10 GRGLVATRDIEPGELIL---------VEKPLVSVPSNSFSLTDGLNEIGV---GLFPLASLL-NHSCDPNAV-------V 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767958310 694 QDLRFPRIAFFSTRLIEAGEQLGFDYGERFWD--------IKGKLFSCRCgsPKC 740
Cdd:cd20071   70 VFDGNGTLRVRALRDIKAGEELTISYIDPLLPrterrrelLEKYGFTCSC--PRC 122
PHA02875 PHA02875
ankyrin repeat protein; Provisional
327-524 4.27e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.99  E-value: 4.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 327 GHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAK 406
Cdd:PHA02875  13 GELDIARRLLDIG-INPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 407 CDLHAVNIH-GDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNSQVwsalQMSKALQDSApdrpspver 485
Cdd:PHA02875  92 KFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI----KGIELLIDHK--------- 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767958310 486 iVSRDIARGYERIP-IPCVNAVDSEPCP------SNYKYVSQN-CVT 524
Cdd:PHA02875 159 -ACLDIEDCCGCTPlIIAMAKGDIAICKmlldsgANIDYFGKNgCVA 204
SET_KMT2E cd19182
SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...
617-720 5.25e-06

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: 46.42  E-value: 5.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 617 VRSLQDIPPGTFVCEYVGELISDSEAdvrEEDSYLFD--------LDNKDGEVYCIDARFYGNVSRFINHHCEPNlVPVR 688
Cdd:cd19182   21 LKAAKDLPPDTLIIEYRGKFMLREQF---EANGYFFKrpypfvlfYSKFHGLEMCVDARTFGNEARFIRRSCTPN-AEVR 96
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767958310 689 VFMAHQDLrfpRIAFFSTRLIEAGEQL----GFDYG 720
Cdd:cd19182   97 HVIEDGTI---HLYIYSIRSIPKGTEItiafDFDYG 129
PHA03100 PHA03100
ankyrin repeat protein; Provisional
230-314 6.00e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 6.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 230 KVLLMLVDGIDPNFKmehqNKR--SPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGA 307
Cdd:PHA03100 174 RVNYLLSYGVPINIK----DVYgfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249

                 ....*..
gi 767958310 308 LVDPKDA 314
Cdd:PHA03100 250 SIKTIIE 256
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
282-371 6.05e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 6.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 282 DQRTPLMEAAENNHLEA------VKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMI 355
Cdd:PTZ00322  75 DPVVAHMLTVELCQLAAsgdavgARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA-DPTLLDKDGKTPLE 153
                         90
                 ....*....|....*.
gi 767958310 356 WATEYKHVDLVKLLLS 371
Cdd:PTZ00322 154 LAEENGFREVVQLLSR 169
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
284-379 7.20e-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: 49.69  E-value: 7.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310  284 RTPLMEAA-ENNHLEAVKYLIKAGALVDpkdaEGSTCLHLAAKKGH---YEVVQYLLSNGQMDVN-------CQDD--GG 350
Cdd:TIGR00870  53 RSALFVAAiENENLELTELLLNLSCRGA----VGDTLLHAISLEYVdavEAILLHLLAAFRKSGPlelandqYTSEftPG 128
                          90       100
                  ....*....|....*....|....*....
gi 767958310  351 WTPMIWATEYKHVDLVKLLLSKGSDINIR 379
Cdd:TIGR00870 129 ITALHLAAHRQNYEIVKLLLERGASVPAR 157
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
350-381 9.05e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.05  E-value: 9.05e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 767958310  350 GWTPMIWA-TEYKHVDLVKLLLSKGSDINIRDN 381
Cdd:pfam00023   2 GNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
315-345 1.38e-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: 42.19  E-value: 1.38e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 767958310   315 EGSTCLHLAAKKGHYEVVQYLLSNGQmDVNC 345
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA-DINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
249-277 1.69e-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: 42.19  E-value: 1.69e-05
                           10        20
                   ....*....|....*....|....*....
gi 767958310   249 NKRSPLHAAAEAGHVDICHMLVQAGANID 277
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
SET_SETD5 cd19181
SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...
597-683 1.72e-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: 45.38  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 597 VQNGLRARLQLYRTRdmgwgVRSLQDIPPGTFVCEYVGELISDSEADVRE---EDSYLFDL--DNKDGEVYCIDARFYGN 671
Cdd:cd19181    6 LQLGRVTRVQKHRKI-----LRAARDLALDTLIIEYRGKVMLRQQFEVNGhffKRPYPFVLfySKFNGVEMCVDARTFGN 80
                         90
                 ....*....|..
gi 767958310 672 VSRFINHHCEPN 683
Cdd:cd19181   81 DARFIRRSCTPN 92
Ank_4 pfam13637
Ankyrin repeats (many copies);
416-468 1.85e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 1.85e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767958310  416 GDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNSQVwSALQM 468
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNV-EVLKL 52
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
315-348 1.91e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.89  E-value: 1.91e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 767958310  315 EGSTCLHLAAKK-GHYEVVQYLLSNGQmDVNCQDD 348
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGA-DVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
366-437 2.15e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 2.15e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767958310 366 VKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLS 437
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
399-459 3.18e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 3.18e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958310 399 AEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLN 459
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
Ank_5 pfam13857
Ankyrin repeats (many copies);
269-323 3.64e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 3.64e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767958310  269 LVQAG-ANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLA 323
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
291-453 4.20e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 47.21  E-value: 4.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 291 AENNHLEAVKYLIKAGALVDPKDAEGSTCLHlaakkghyevvQYLLSNgqmdvncqddggwtpmiwateYKHVDLVKLLL 370
Cdd:PHA02716 292 ARNIDISVVYSFLQPGVKLHYKDSAGRTCLH-----------QYILRH---------------------NISTDIIKLLH 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 371 SKGSDINIRDNEENICLHwaafsgcvdiaeILLAAKCDLHAVNIHGDSPLHIaarenryDCVVLFLSRDSDVTLKNKEGE 450
Cdd:PHA02716 340 EYGNDLNEPDNIGNTVLH------------TYLSMLSVVNILDPETDNDIRL-------DVIQCLISLGADITAVNCLGY 400

                 ...
gi 767958310 451 TPL 453
Cdd:PHA02716 401 TPL 403
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
350-378 4.88e-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: 4.88e-05
                           10        20
                   ....*....|....*....|....*....
gi 767958310   350 GWTPMIWATEYKHVDLVKLLLSKGSDINI 378
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
223-304 4.89e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 4.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 223 ARQGELQKVLLMLVDGIDPNFKMEHQnkRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYL 302
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDG--RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167

                 ..
gi 767958310 303 IK 304
Cdd:PTZ00322 168 SR 169
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
614-725 5.17e-05

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


Pssm-ID: 380938  Cd Length: 112  Bit Score: 43.01  E-value: 5.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 614 GWGVRSLQDIPPGTFVcEYVGELISDSEADVREEDSYLFDLdnkdgeVYCIDARFY----GNVSRFiNHHCEPNLVPVRV 689
Cdd:cd10540   11 GRGVFATRPIKKGEVI-EEAPVIVLPKEEYQHLCKTVLDHY------VFSWGDGCLalalGYGSMF-NHSYTPNAEYEID 82
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767958310 690 FMAHqdlrfpRIAFFSTRLIEAGEQLGFDYGERFWD 725
Cdd:cd10540   83 FENQ------TIVFYALRDIEAGEELTINYGDDLWD 112
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
323-445 9.03e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.84  E-value: 9.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310  323 AAKKGHYEVVQYLLSNGQMD-VNCQDDGGWTPMIW-ATEYKHVDLVKLLLSKGSDINIRDNeeniCLHWAA---FSGCVD 397
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKKLnINCPDRLGRSALFVaAIENENLELTELLLNLSCRGAVGDT----LLHAISleyVDAVEA 99
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767958310  398 IAEILLAAKCD----LHAVNI------HGDSPLHIAARENRYDCVVLFLSRDSDVTLK 445
Cdd:TIGR00870 100 ILLHLLAAFRKsgplELANDQytseftPGITALHLAAHRQNYEIVKLLLERGASVPAR 157
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
249-277 1.13e-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: 1.13e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 767958310  249 NKRSPLHAAAE-AGHVDICHMLVQAGANID 277
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVN 30
PHA02989 PHA02989
ankyrin repeat protein; Provisional
233-406 1.16e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 45.50  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 233 LMLVDGIDPNfkmEHQNKR--SPLHAAAEAGHV--DICHMLVQAGANI-DTCSEDQRTP----LMEAAENNHLEAVKYLI 303
Cdd:PHA02989 129 FLLSKGINVN---DVKNSRgyNLLHMYLESFSVkkDVIKILLSFGVNLfEKTSLYGLTPmniyLRNDIDVISIKVIKYLI 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 304 KAGALVDPKDAEGSTCL------HLAAKKGHYEVVQYLLSngQMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDIN 377
Cdd:PHA02989 206 KKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILK--YIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIY 283
                        170       180
                 ....*....|....*....|....*....
gi 767958310 378 IRDNEENICLHWAAFSGCVDIAEILLAAK 406
Cdd:PHA02989 284 NVSKDGDTVLTYAIKHGNIDMLNRILQLK 312
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
282-310 1.87e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 1.87e-04
                           10        20
                   ....*....|....*....|....*....
gi 767958310   282 DQRTPLMEAAENNHLEAVKYLIKAGALVD 310
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02989 PHA02989
ankyrin repeat protein; Provisional
230-456 2.54e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 44.35  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 230 KVLLMLVD-GIDPNFK--MEhqnkrSPLHAAAEAGHVD------ICHMLVQAGANIDTCSEDQRTPLMEAAEN---NHLE 297
Cdd:PHA02989  51 KIVKLLIDnGADVNYKgyIE-----TPLCAVLRNREITsnkikkIVKLLLKFGADINLKTFNGVSPIVCFIYNsniNNCD 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 298 AVKYLIKAGALV-DPKDAEGSTCLH--LAAKKGHYEVVQYLLSNGQMDVNCQDDGGWTPM-IW---ATEYKHVDLVKLLL 370
Cdd:PHA02989 126 MLRFLLSKGINVnDVKNSRGYNLLHmyLESFSVKKDVIKILLSFGVNLFEKTSLYGLTPMnIYlrnDIDVISIKVIKYLI 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 371 SKGSDInirdnEENICLHWAAFSGCVDIAEILLAaKC-----------DLHAVNIHGDSPLHIAARENRYDCVVLFLSRD 439
Cdd:PHA02989 206 KKGVNI-----ETNNNGSESVLESFLDNNKILSK-KEfkvlnfilkyiKINKKDKKGFNPLLISAKVDNYEAFNYLLKLG 279
                        250
                 ....*....|....*..
gi 767958310 440 SDVTLKNKEGETPLQCA 456
Cdd:PHA02989 280 DDIYNVSKDGDTVLTYA 296
PHA02859 PHA02859
ankyrin repeat protein; Provisional
276-422 2.63e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.88  E-value: 2.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 276 IDTCSEDQRTPLMEAAENNH--LEAVKYLIKAGALVDPK-DAEGSTCLH--LAAKKG-HYEVVQYLLSNGQmDVNCQDDG 349
Cdd:PHA02859  44 VNDCNDLYETPIFSCLEKDKvnVEILKFLIENGADVNFKtRDNNLSALHhyLSFNKNvEPEILKILIDSGS-SITEEDED 122
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767958310 350 GWTPM-IWATEYK-HVDLVKLLLSKGSDINIRDNEENICLH-WAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHI 422
Cdd:PHA02859 123 GKNLLhMYMCNFNvRINVIKLLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNCYDL 198
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
321-403 3.68e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 3.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 321 HLAAKkGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAE 400
Cdd:PTZ00322  88 QLAAS-GDAVGARILLTGGA-DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                 ...
gi 767958310 401 ILL 403
Cdd:PTZ00322 166 LLS 168
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
415-444 5.41e-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: 37.95  E-value: 5.41e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 767958310   415 HGDSPLHIAARENRYDCVVLFLSRDSDVTL 444
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
282-313 5.88e-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: 37.65  E-value: 5.88e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 767958310  282 DQRTPLMEAAE-NNHLEAVKYLIKAGALVDPKD 313
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02884 PHA02884
ankyrin repeat protein; Provisional
352-425 6.36e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 42.66  E-value: 6.36e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767958310 352 TPMIWATEYKHVDLVKLLLSKGSDINIRDNEENIC-LHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAAR 425
Cdd:PHA02884  72 NPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITpLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
415-447 7.74e-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: 37.65  E-value: 7.74e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767958310  415 HGDSPLHIAA-RENRYDCVVLFLSRDSDVTLKNK 447
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
350-378 1.07e-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: 1.07e-03
                          10        20
                  ....*....|....*....|....*....
gi 767958310  350 GWTPMIWATEYKHVDLVKLLLSKGSDINI 378
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
282-307 1.30e-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: 1.30e-03
                          10        20
                  ....*....|....*....|....*.
gi 767958310  282 DQRTPLMEAAENNHLEAVKYLIKAGA 307
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGA 26
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
249-278 1.31e-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: 1.31e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 767958310  249 NKRSPLHAAAEAGHVDICHMLVQAGANIDT 278
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
315-345 1.33e-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: 1.33e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 767958310  315 EGSTCLHLAAKKGHYEVVQYLLSNGqMDVNC 345
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENG-ADINA 30
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
611-723 1.33e-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: 39.52  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 611 RDMGWGVRSLQDIPPGTFVCEYVGELISDSEAdvrEEDSYLFDLDNKDGEVYCIDAR--FYGNVSRFIN---HHCEPNLV 685
Cdd:cd19193   16 PGAGLGVWAEAPIPKGMVFGPYEGEIVEDEEA---ADSGYSWQIYKGGKLSHYIDAKdeSKSNWMRYVNcarNEEEQNLV 92
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767958310 686 pvrvfmAHQDLRfpRIAFFSTRLIEAGEQLGFDYGERF 723
Cdd:cd19193   93 ------AFQYRG--KIYYRTCKDIAPGTELLVWYGDEY 122
PHA02946 PHA02946
ankyin-like protein; Provisional
234-420 3.61e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.42  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 234 MLVDGIDPNFKMEHQNkrSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPL--MEAAENNHLEAVKYLIKAGALVDP 311
Cdd:PHA02946  58 LLHRGYSPNETDDDGN--YPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKINN 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 312 K-DAEGSTCLhLAAKKGHYEVVQYLLSNGqMDVNCQDDGGWTPM--IWATEYKHVDLVKLLLSKGSDINIRDNEENICLH 388
Cdd:PHA02946 136 SvDEEGCGPL-LACTDPSERVFKKIMSIG-FEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLH 213
                        170       180       190
                 ....*....|....*....|....*....|....
gi 767958310 389 WAAFSGC--VDIAEILLAAKcDLHAVNIHGDSPL 420
Cdd:PHA02946 214 IVCSKTVknVDIINLLLPST-DVNKQNKFGDSPL 246
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
269-388 3.73e-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: 40.63  E-value: 3.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 269 LVQAGANIDTCSEDQRTPLMEAAENNhlEAVKYLIKAGALVDPkdAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDD 348
Cdd:cd21882   30 LHKAALNLNDGVNEAIMLLLEAAPDS--GNPKELVNAPCTDEF--YQGQTALHIAIENRNLNLVRLLVENGA-DVSARAT 104
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767958310 349 G-------------GWTPMIWATEYKHVDLVKLLLSKGSDI---NIRDNEENICLH 388
Cdd:cd21882  105 GrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNTVLH 160
PHA02859 PHA02859
ankyrin repeat protein; Provisional
252-377 5.36e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.03  E-value: 5.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310 252 SPLHAAAEAGHV--DICHMLVQAGANIDTCSEDQRTPLMEA----AENNHLEAVKYLIKAGALVDPKDAEGSTCLH--LA 323
Cdd:PHA02859  53 TPIFSCLEKDKVnvEILKFLIENGADVNFKTRDNNLSALHHylsfNKNVEPEILKILIDSGSSITEEDEDGKNLLHmyMC 132
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767958310 324 AKKGHYEVVQYLLSNGQMDVNCQDDGG---WTPMIWATEYKHVDlvkLLLSKGSDIN 377
Cdd:PHA02859 133 NFNVRINVIKLLIDSGVSFLNKDFDNNnilYSYILFHSDKKIFD---FLTSLGIDIN 186
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
395-462 6.40e-03

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: 40.00  E-value: 6.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767958310 395 CVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLsrDSDVTLKNK-------EGETPLQCASLNSQV 462
Cdd:cd22192   30 VQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLM--EAAPELVNEpmtsdlyQGETALHIAVVNQNL 102
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
252-324 7.40e-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: 39.68  E-value: 7.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958310  252 SPLHAAAEAGHVDICHMLVQAGANID---TCSEDQRT-----------PLMEAAENNHLEAVKYLIKAGALVDPKDAEGS 317
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVParaCGDFFVKSqgvdsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209

                  ....*..
gi 767958310  318 TCLHLAA 324
Cdd:TIGR00870 210 TLLHLLV 216
 
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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