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Conserved domains on  [gi|224465233|ref|NP_079033|]
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histone-lysine N-methyltransferase EHMT1 isoform 1 [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 ...
1036-1266 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: 542.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1036 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 1115
Cdd:cd10535     1 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1116 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 1195
Cdd:cd10535    81 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224465233 1196 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 1266
Cdd:cd10535   161 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 231
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
514-644 5.30e-68

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: 224.58  E-value: 5.30e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  514 LQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCG 592
Cdd:cd20905     1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 224465233  593 YFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEESS-KAKEVTIAK 644
Cdd:cd20905    81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
720-976 3.39e-58

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.88  E-value: 3.39e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  720 LESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQNkrSPLHAAAEAGHVDICHMLVQAGANI 799
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEAGADV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  800 DTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIW 879
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHL 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  880 ATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFL 959
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
                         250
                  ....*....|....*..
gi 224465233  960 SRDSDVTLKNKEGETPL 976
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 ...
1036-1266 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: 542.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1036 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 1115
Cdd:cd10535     1 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1116 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 1195
Cdd:cd10535    81 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224465233 1196 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 1266
Cdd:cd10535   161 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 231
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
514-644 5.30e-68

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: 224.58  E-value: 5.30e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  514 LQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCG 592
Cdd:cd20905     1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 224465233  593 YFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEESS-KAKEVTIAK 644
Cdd:cd20905    81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
720-976 3.39e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.88  E-value: 3.39e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  720 LESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQNkrSPLHAAAEAGHVDICHMLVQAGANI 799
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEAGADV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  800 DTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIW 879
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHL 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  880 ATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFL 959
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
                         250
                  ....*....|....*..
gi 224465233  960 SRDSDVTLKNKEGETPL 976
Cdd:COG0666   273 LALLLLAAALLDLLTLL 289
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
1126-1248 9.25e-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: 143.63  E-value: 9.25e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233   1126 ARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKdgevYCIDARFYGNVSR 1197
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKaydtdgakAFYLFDIDSD----LCIDARRKGNLAR 76
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 224465233   1198 FINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGERFWD 1248
Cdd:smart00317   77 FINHSCEPNCELLFVEVNGDD----RIVIFALRDIKPGEELTIDYGSDYAN 123
Pre-SET pfam05033
Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines ...
1014-1118 1.78e-30

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: 115.98  E-value: 1.78e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  1014 IARGYERIPIPCVNAVDSEPCPSNYKYVSQNCVTSPMNIDRnithLQYCVCiDDCSSSNCMCGQLSM---RCWYDKDGRL 1090
Cdd:pfam05033    1 ISKGKENVPIPVVNEVDDEPPPPDFTYITSYIYPKEFLLII----PQGCDC-GDCSSEKCSCAQLNGgefRFPYDKDGLL 75
                           90       100
                   ....*....|....*....|....*...
gi 224465233  1091 LPEfnmaEPPLIFECNHACSCWRNCRNR 1118
Cdd:pfam05033   76 VPE----SKPPIYECNPLCGCPPSCPNR 99
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
1136-1265 3.52e-29

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 113.52  E-value: 3.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1136 MGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDS-----YLFDLDnkDGEVycIDARFYGNVSRFINHHCEPNLVPV 1210
Cdd:COG2940    16 HGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKeplhtYLFELD--DDGV--IDGALGGNPARFINHSCDPNCEAD 91
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 224465233 1211 RvfmahqdlRFPRIAFFSTRLIEAGEQLGFDYGERFWDikgKLFSCRCgsPKCRH 1265
Cdd:COG2940    92 E--------EDGRIFIVALRDIAAGEELTYDYGLDYDE---EEYPCRC--PNCRG 133
Ank_2 pfam12796
Ankyrin repeats (3 copies);
810-903 5.60e-29

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 111.36  E-value: 5.60e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233   810 LMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNgqMDVNCQDDgGWTPMIWATEYKHVDLV 889
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDN-GRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 224465233   890 KLLLSKGSDINIRD 903
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
750-983 9.60e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 111.68  E-value: 9.60e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  750 ELQKVLLMLVDGIDPNFKMehqnKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNH-----LEAVKY 824
Cdd:PHA03100   16 KNIKYIIMEDDLNDYSYKK----PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  825 LIKAGALVDPKDAEGSTCLHLAA--KKGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVDL--VKLLLSKGSDIN 900
Cdd:PHA03100   92 LLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDIN 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  901 IRDNeeniclhwaafsgcvdiAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCAS 980
Cdd:PHA03100  171 AKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233

                  ...
gi 224465233  981 LNS 983
Cdd:PHA03100  234 LNN 236
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
808-979 3.09e-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: 3.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  808 TPLMEAAENNHLEAVKYLIKAGAlVDP--KDAEGSTCLHLAAKKGHYEVVQYLLSNGQMDVN----CQDDGGWTPMIWAT 881
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPS-CDLfqRGALGETALHVAALYDNLEAAVVLMEAAPELVNepmtSDLYQGETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  882 EYKHVDLVKLLLSKGSDIN--------IRDNEENICL---HWAAFSGCV---DIAEILLAAKCDLHAVNIHGDSPLHIAA 947
Cdd:cd22192    98 VNQNLNLVRELIARGADVVspratgtfFRPGPKNLIYygeHPLSFAACVgneEIVRLLIEHGADIRAQDSLGNTVLHILV 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 224465233  948 RENR-------YDcvvLFLSRDSDV------TLKNKEGETPLQCA 979
Cdd:cd22192   178 LQPNktfacqmYD---LILSYDKEDdlqpldLVPNNQGLTPFKLA 219
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
807-902 1.36e-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: 49.69  E-value: 1.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233   807 RTPLMEAA-ENNHLEAVKYLIKAGALVDpkdaEGSTCLHLAAKKGH---YEVVQYLLSNGQMDVN-------CQDD--GG 873
Cdd:TIGR00870   53 RSALFVAAiENENLELTELLLNLSCRGA----VGDTLLHAISLEYVdavEAILLHLLAAFRKSGPlelandqYTSEftPG 128
                           90       100
                   ....*....|....*....|....*....
gi 224465233   874 WTPMIWATEYKHVDLVKLLLSKGSDINIR 902
Cdd:TIGR00870  129 ITALHLAAHRQNYEIVKLLLERGASVPAR 157
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
838-868 1.41e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 1.41e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 224465233    838 EGSTCLHLAAKKGHYEVVQYLLSNGQmDVNC 868
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 ...
1036-1266 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: 542.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1036 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 1115
Cdd:cd10535     1 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1116 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 1195
Cdd:cd10535    81 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224465233 1196 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 1266
Cdd:cd10535   161 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 231
SET_EHMT cd10543
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
1036-1266 7.06e-169

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: 500.71  E-value: 7.06e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1036 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 1115
Cdd:cd10543     1 PDFLYVTENCETSPLNIDRNITSLQTCSCRDDCSSDNCVCGRLSVRCWYDKEGRLLPDFNKLDPPLIFECNRACSCWRNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1116 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 1195
Cdd:cd10543    81 RNRVVQNGIRYRLQLFRTRGMGWGVRALQDIPKGTFVCEYIGELISDSEADSREDDSYLFDLDNKDGETYCIDARRYGNI 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224465233 1196 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 1266
Cdd:cd10543   161 SRFINHLCEPNLIPVRVFVEHQDLRFPRIAFFASRDIKAGEELGFDYGEKFWRIKGKYFTCRCGSPKCKYS 231
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
1036-1274 3.58e-155

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: 465.65  E-value: 3.58e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1036 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 1115
Cdd:cd10533     1 EDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1116 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 1195
Cdd:cd10533    81 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNI 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224465233 1196 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHSSAALAQRQ 1274
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) ...
1036-1243 5.29e-105

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: 330.87  E-value: 5.29e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1036 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLS-MRCWYDKDGRLLPefnMAEPPLIFECNHACSCWRN 1114
Cdd:cd10538     1 PSFTYIKDNIVGKNVQPFSNIIDSVGCKCKDDCLDSKCACAAESdGIFAYTKNGLLRL---NNSPPPIFECNSKCSCDDD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1115 CRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE------DSYLFDLDN-----KDGE 1183
Cdd:cd10538    78 CKNRVVQRGLQARLQVFRTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRGKiydksgGSYLFDLDEfsdsdGDGE 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1184 VYCIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYG 1243
Cdd:cd10538   158 ELCVDATFCGNVSRFINHSCDPNLFPFNVVIDHDDLRYPRIALFATRDILPGEELTFDYG 217
SET_SETDB1 cd10517
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
1013-1264 1.03e-72

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


Pssm-ID: 380915 [Multi-domain]  Cd Length: 288  Bit Score: 244.12  E-value: 1.03e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1013 DIARGYERIPIPCVNAVDSEPcPSNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCS-SSNCMCGQLS---MRCWYDKDG 1088
Cdd:cd10517     8 DISYGKEGVPIPCVNEIDNSS-PPYVEYSKERIPGKGVNINLDPDFLVGCDCTDGCRdKSKCACQQLTieaTAATPGGQI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1089 --------RLLPEFnmaEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELI 1160
Cdd:cd10517    87 npsagyqyRRLMEK---LPTGVYECNSRCKCDKRCYNRVVQNGLQVRLQVFKTEKKGWGIRCLDDIPKGSFVCIYAGQIL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1161 SDSEADVREE---DSYLFDLD------------NKDGEVYC--IDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPR 1223
Cdd:cd10517   164 TEDEANEEGLqygDEYFAELDyievveklkegyESDVEEHCyiIDAKSEGNLGRYLNHSCSPNLFVQNVFVDTHDLRFPW 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 224465233 1224 IAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCR 1264
Cdd:cd10517   244 VAFFASRYIRAGTELTWDYNYEVGSVPGKVLYCYCGSSNCR 284
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
514-644 5.30e-68

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: 224.58  E-value: 5.30e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  514 LQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCG 592
Cdd:cd20905     1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 224465233  593 YFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEESS-KAKEVTIAK 644
Cdd:cd20905    81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
SET_SUV39H cd10542
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
1036-1264 6.93e-68

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


Pssm-ID: 380940 [Multi-domain]  Cd Length: 245  Bit Score: 228.72  E-value: 6.93e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1036 SNYKYVSQNCVTSPMNIDRNIthLQYCVCIDDC--SSSNCmCGQLS-MRCWYDKDGRLLpeFNMAEPplIFECNHACSCW 1112
Cdd:cd10542     1 PNFQYINDYIPGDGVKIPEDF--LVGCECTEDChnNNPTC-CPAESgVKFAYDKQGRLR--LPPGTP--IYECNSRCKCG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1113 RNCRNRVVQNGLRARLQLYRTRD-MGWGVRSLQDIPPGTFVCEYVGELISDSEADVR------EEDSYLFDLD-NKDGEV 1184
Cdd:cd10542    74 PDCPNRVVQRGRKVPLCIFRTSNgRGWGVKTLEDIKKGTFVMEYVGEIITSEEAERRgkiydaNGRTYLFDLDyNDDDCE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1185 YCIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDY---------GERFWDIKGKLFS 1255
Cdd:cd10542   154 YTVDAAYYGNISHFINHSCDPNLAVYAVWINHLDPRLPRIAFFAKRDIKAGEELTFDYlmtgtggssESTIPKPKDVRVP 233

                  ....*....
gi 224465233 1256 CRCGSPKCR 1264
Cdd:cd10542   234 CLCGSKNCR 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
720-976 3.39e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.88  E-value: 3.39e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  720 LESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQNkrSPLHAAAEAGHVDICHMLVQAGANI 799
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEAGADV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  800 DTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIW 879
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHL 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  880 ATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFL 959
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
                         250
                  ....*....|....*..
gi 224465233  960 SRDSDVTLKNKEGETPL 976
Cdd:COG0666   273 LALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
723-1002 5.03e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.49  E-value: 5.03e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  723 ALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKmeHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTC 802
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALA--DALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  803 SEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATE 882
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  883 YKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRD 962
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 224465233  963 SDVTLKNKEGETPLQCASLNSQVWSALQMSKALQDSAPDR 1002
Cdd:COG0666   243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
1036-1264 3.75e-54

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: 189.82  E-value: 3.75e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1036 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDD-CSSSNCMCgqlsMRCW---YDKDGRLLPEF-NMAEPplIFECNHACS 1110
Cdd:cd10544     1 PDFQYTPENVPGPGADTDPNEITFPGCDCKTSsCEPETCSC----LRKYgpnYDDDGCLLDFDgKYSGP--VFECNSMCK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1111 CWRNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVR------EEDSYLFDLDN--KDG 1182
Cdd:cd10544    75 CSESCQNRVVQNGLQFKLQVFKTPKKGWGLRTLEFIPKGRFVCEYAGEVIGFEEARRRtksqtkGDMNYIIVLREhlSSG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1183 EVY--CIDARFYGNVSRFINHHCEPNL--VPVRVfmahqDLRFPRIAFFSTRLIEAGEQLGFDYGERF--WDIKGKLF-- 1254
Cdd:cd10544   155 KVLetFVDPTYIGNIGRFLNHSCEPNLfmVPVRV-----DSMVPKLALFAARDIVAGEELSFDYSGEFsnSVESVTLArq 229
                         250
                  ....*....|....*..
gi 224465233 1255 -------SCRCGSPKCR 1264
Cdd:cd10544   230 desksrkPCLCGAENCR 246
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
1062-1243 3.45e-52

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: 183.37  E-value: 3.45e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1062 CVCIDDC--SSSNCMCGQL-SMRCWYDKDGRLLpefnmAEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTRDMGW 1138
Cdd:cd10545    24 CDCKNRCtdGASDCACVKKnGGEIPYNFNGRLI-----RAKPAIYECGPLCKCPPSCYNRVTQKGLRYRLEVFKTAERGW 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1139 GVRSLQDIPPGTFVCEYVGELISDSEADVR-EEDSYLFDLDNK------DGEV---------------------YCIDAR 1190
Cdd:cd10545    99 GVRSWDSIPAGSFICEYVGELLDTSEADTRsGNDDYLFDIDNRqtnrgwDGGQrldvgmsdgerssaedeesseFTIDAG 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 224465233 1191 FYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYG 1243
Cdd:cd10545   179 SFGNVARFINHSCSPNLFVQCVLYDHNDLRLPRVMLFAADNIPPLQELTYDYG 231
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
755-982 2.37e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 183.23  E-value: 2.37e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  755 LLMLVDGIDPNFKMEHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDP 834
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  835 KDAEGSTCLHLAAKKGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAA 914
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224465233  915 FSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLN 982
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEN 229
SET_SETDB cd10541
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...
1062-1264 8.90e-50

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


Pssm-ID: 380939 [Multi-domain]  Cd Length: 236  Bit Score: 176.58  E-value: 8.90e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1062 CVCIDDC-SSSNCMCGQLSMRCWYDKDG-----------RLLPEfnmAEPPLIFECNHACSCWRN-CRNRVVQNGLRARL 1128
Cdd:cd10541    18 CDCTDGCrDKSKCACHQLTIQATACTPGgqdnptagyqyKRLEE---CLPTGVYECNKLCKCDPNmCQNRLVQHGLQVRL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1129 QLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEAD---VREEDSYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEP 1205
Cdd:cd10541    95 QLFKTQNKGWGIRCLDDIAKGTFVCIYAGKILTDDFADkegLEMGDEYFANLDHIEESCYIIDAKLEGNLGRYLNHSCSP 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 224465233 1206 NLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCR 1264
Cdd:cd10541   175 NLFVQNVFVDTHDLRFPWVAFFASKRIKAGTELTWDYNYEVGSVEGKELLCCCGSNECR 233
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
1037-1264 1.08e-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: 168.53  E-value: 1.08e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1037 NYKYVSQNCVTSPMNIDRNITHlqyCVCiDDCSSS---NCMCGQLSMRCWYDKDGRLLPefnMAEPPlIFECNHACSCWR 1113
Cdd:cd10525     2 DFVYINEYKVGEGVTLNQVAVG---CEC-QDCLSQpvgGCCPGASKHRFAYNEQGQVKV---RPGLP-IYECNSRCRCGP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1114 NCRNRVVQNGLRARLQLYRTRD-MGWGVRSLQDIPPGTFVCEYVGELISDSEADVR------EEDSYLFDLDNKDgEVYC 1186
Cdd:cd10525    74 DCPNRVVQKGIQYDLCIFRTDNgRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRgqiydrQGATYLFDLDYVE-DVYT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1187 IDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDY---------------------GER 1245
Cdd:cd10525   153 VDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIALFATRTIRAGEELTFDYnmqvdpvdaestkmdsnfglaGLP 232
                         250
                  ....*....|....*....
gi 224465233 1246 FWDIKGKLFSCRCGSPKCR 1264
Cdd:cd10525   233 GSPKKRVRIECKCGVRSCR 251
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
1036-1264 3.86e-46

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


Pssm-ID: 380930 [Multi-domain]  Cd Length: 243  Bit Score: 166.22  E-value: 3.86e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1036 SNYKYVSQNCVTSPMNIDRNITHlqYCVCIDdCSSSNCMCGQLSMRCWYDKDGRLlpefnMAEPPL-IFECNHACSCWRN 1114
Cdd:cd10532     1 IDFYYINEYKPAPGINLDNEATV--GCDCSD-CFFGKCCPAEAGVLFAYNEHGQL-----KIPPGTpIYECNSRCKCGPD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1115 CRNRVVQNGLRARLQLYRTRD-MGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--DS----YLFDLDNKDGEvYCI 1187
Cdd:cd10532    73 CPNRVVQKGTQYSLCIFRTSNgRGWGVKTLQKIKKNSFVMEYVGEVITSEEAERRGQfyDSkgitYLFDLDYESDE-FTV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1188 DARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDY-----GERFWDI-------KGKLFS 1255
Cdd:cd10532   152 DAARYGNVSHFVNHSCDPNLQVFNVFIDNLDTRLPRIALFSTRTIKAGEELTFDYqmkgsGDLSSDSidnspakKRVRTV 231

                  ....*....
gi 224465233 1256 CRCGSPKCR 1264
Cdd:cd10532   232 CKCGAVTCR 240
SET_SUV39H_DIM5-like cd19473
SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...
1062-1264 2.86e-45

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


Pssm-ID: 380996 [Multi-domain]  Cd Length: 274  Bit Score: 164.80  E-value: 2.86e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1062 CVCIDDCSSSNCMCGQLSMRCWY---DKDGRLLPEFNMAEPPlIFECNHACSCWRNCRNRVVQNGLRARLQLYRTRD-MG 1137
Cdd:cd19473    39 CLCLQDVDPDDDRDPGKKKNAYHssgAKKGCLRGHMLNSRLP-IYECHEGCACSDDCPNRVVERGRKVPLQIFRTSDgRG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1138 WGVRSLQDIPPGTFVCEYVGELISDSEADVREEDS--------YLFDLDN----------KDGEVYCIDARFYGNVSRFI 1199
Cdd:cd19473   118 WGVRSTVDIKRGQFVDCYVGEIITPEEAQRRRDAAtiaqrkdvYLFALDKfsdpdsldprLRGDPYEIDGEFMSGPTRFI 197
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224465233 1200 NHHCEPNLvpvRVFM---AHQDLRFPRIAFFSTRLIEAGEQLGFDY--------GERFWDIKGK-LFSCRCGSPKCR 1264
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 ...
1062-1264 5.31e-45

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


Pssm-ID: 380999 [Multi-domain]  Cd Length: 259  Bit Score: 163.51  E-value: 5.31e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1062 CVCIDDCSSSNCMcgqlsmrcwYDKDGRLlpefNMAEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTRDMGWGVR 1141
Cdd:cd20073    42 CQCLEDSNEKSFA---------YDEYGRV----RANTGSIIYECNENCDCGINCPNRVVQRGRKLPLEIFKTKHKGWGLR 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1142 SLQDIPPGTFVCEYVGELISDSEADVREED------SYLFDLDNKDGEV---YCIDARFYGNVSRFINHHCEPNLVPVRV 1212
Cdd:cd20073   109 CPRFIKAGTFIGVYLGEVITQSEAEIRGKKydnvgvTYLFDLDLFEDQVdeyYTVDAQYCGDVTRFINHSCDPNLAIYSV 188
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224465233 1213 FMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGER----------------FWDIKGKLfSCRCGSPKCR 1264
Cdd:cd20073   189 LRDKSDSKIYDLAFFAIKDIPALEELTFDYSGRnnfdqlgfignrsnskYINLKNKR-PCYCGSANCR 255
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
1027-1264 1.27e-43

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: 160.00  E-value: 1.27e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1027 NAVDSEPCPSNYKYVSQNCVTSpmnidrNITHLQYCVCIDDCSS-SNCMCGQLSMR-------------CWYdKDGRLLp 1092
Cdd:cd10523     5 TYVQLDRNPQDQQQLVDDFDIS------NGAFVDSCDCTDGCIDiLKCACLQLTARafsksesspskggRGY-KYKRLQ- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1093 efnMAEPPLIFECNHACSCWRN-CRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELIS---------- 1161
Cdd:cd10523    77 ---EPIPSGLYECNVSCKCNRMlCQNRVVQHGLQVRLQVFKTEKKGWGVRCLDDIDKGTFVCIYAGRVLSrarspteplp 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1162 -------DSEADVREEDSYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEA 1234
Cdd:cd10523   154 pklelpsENEVEVVTSWLILSKKRKLRENVCFLDASKEGNVGRFLNHSCCPNLFVQNVFVDTHDKNFPWVAFFTNRVVKA 233
                         250       260       270
                  ....*....|....*....|....*....|
gi 224465233 1235 GEQLGFDYGERFWDIKGKLFSCRCGSPKCR 1264
Cdd:cd10523   234 GTELTWDYSYDAGTSPEQEIPCLCGVNKCQ 263
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
1126-1248 9.25e-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: 143.63  E-value: 9.25e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233   1126 ARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKdgevYCIDARFYGNVSR 1197
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKaydtdgakAFYLFDIDSD----LCIDARRKGNLAR 76
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 224465233   1198 FINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGERFWD 1248
Cdd:smart00317   77 FINHSCEPNCELLFVEVNGDD----RIVIFALRDIKPGEELTIDYGSDYAN 123
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
1128-1264 2.83e-37

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: 136.62  E-value: 2.83e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1128 LQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVR--------EEDSYLFDLdnKDGEVycIDARFYGNVSRFI 1199
Cdd:cd10531     2 LELFRTEKKGWGVKAKEDIQKGEFIIEYVGEVIDKKEFKERldeyeelgKSNFYILSL--SDDVV--IDATRKGNLSRFI 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224465233 1200 NHHCEPNLVpVRVFMAhqdLRFPRIAFFSTRLIEAGEQLGFDYGerFWDIKGKLFSCRCGSPKCR 1264
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), ...
1116-1264 2.24e-34

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: 128.87  E-value: 2.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1116 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKdgevYCI 1187
Cdd:cd10518     4 RFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKrydeegggGTYMFRIDED----LVI 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224465233 1188 DARFYGNVSRFINHHCEPNLVpVRVfMAHQDLRfpRIAFFSTRLIEAGEQLGFDYgeRFWDIKGKLFSCRCGSPKCR 1264
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; ...
1128-1264 1.71e-33

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


Pssm-ID: 380951 [Multi-domain]  Cd Length: 141  Bit Score: 126.25  E-value: 1.71e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1128 LQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNkdgevYC--------IDARFYGNVSRFI 1199
Cdd:cd19174     2 LERFRTEDKGWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRMIEQYHNHSHH-----YClnldsgmvIDGYRMGNEARFV 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224465233 1200 NHHCEPNLVPVRVFMAHQdlrfPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLfSCRCGSPKCR 1264
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 ...
1126-1264 2.07e-31

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


Pssm-ID: 380949 [Multi-domain]  Cd Length: 142  Bit Score: 120.38  E-value: 2.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1126 ARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDS--------YLFDLDNKDgevyCIDARFYGNVSR 1197
Cdd:cd19172     2 AKVEVFRTEKKGWGLRAAEDLPKGTFVIEYVGEVLDEKEFKRRMKEYaregnrhyYFMALKSDE----IIDATKKGNLSR 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224465233 1198 FINHHCEPNLVpVRVFMAHQDLrfpRIAFFSTRLIEAGEQLGFDYG-ERFWDIKGKlfsCRCGSPKCR 1264
Cdd:cd19172    78 FINHSCEPNCE-TQKWTVNGEL---RVGFFAKRDIPAGEELTFDYQfERYGKEAQK---CYCGSPNCR 138
Pre-SET pfam05033
Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines ...
1014-1118 1.78e-30

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: 115.98  E-value: 1.78e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  1014 IARGYERIPIPCVNAVDSEPCPSNYKYVSQNCVTSPMNIDRnithLQYCVCiDDCSSSNCMCGQLSM---RCWYDKDGRL 1090
Cdd:pfam05033    1 ISKGKENVPIPVVNEVDDEPPPPDFTYITSYIYPKEFLLII----PQGCDC-GDCSSEKCSCAQLNGgefRFPYDKDGLL 75
                           90       100
                   ....*....|....*....|....*...
gi 224465233  1091 LPEfnmaEPPLIFECNHACSCWRNCRNR 1118
Cdd:pfam05033   76 VPE----SKPPIYECNPLCGCPPSCPNR 99
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
1136-1265 3.52e-29

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 113.52  E-value: 3.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1136 MGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDS-----YLFDLDnkDGEVycIDARFYGNVSRFINHHCEPNLVPV 1210
Cdd:COG2940    16 HGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKeplhtYLFELD--DDGV--IDGALGGNPARFINHSCDPNCEAD 91
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 224465233 1211 RvfmahqdlRFPRIAFFSTRLIEAGEQLGFDYGERFWDikgKLFSCRCgsPKCRH 1265
Cdd:COG2940    92 E--------EDGRIFIVALRDIAAGEELTYDYGLDYDE---EEYPCRC--PNCRG 133
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
1137-1243 3.68e-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: 113.00  E-value: 3.68e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  1137 GWGVRSLQDIPPGTFVCEYVGE-LISDSEADVREE-----------DSYLFDLDNKDGevYCIDAR--FYGNVSRFINHH 1202
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELlyydklelrlwGPYLFTLDEDSE--YCIDARalYYGNWARFINHS 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 224465233  1203 CEPNLVPVRVFMAhqdlRFPRIAFFSTRLIEAGEQLGFDYG 1243
Cdd:pfam00856   79 CDPNCEVRVVYVN----GGPRIVIFALRDIKPGEELTIDYG 115
Ank_2 pfam12796
Ankyrin repeats (3 copies);
810-903 5.60e-29

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 111.36  E-value: 5.60e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233   810 LMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNgqMDVNCQDDgGWTPMIWATEYKHVDLV 889
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDN-GRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 224465233   890 KLLLSKGSDINIRD 903
Cdd:pfam12796   78 KLLLEKGADINVKD 91
SET_EZH cd10519
SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...
1127-1243 4.96e-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: 4.96e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1127 RLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVRE--ED----SYLFDLDNKdgevYCIDARFYGNVSRFIN 1200
Cdd:cd10519     2 RLLLGKSDVAGWGLFLKEPIKKDEFIGEYTGELISQDEADRRGkiYDkynsSYLFNLNDQ----FVVDATRKGNKIRFAN 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 224465233 1201 HHCEPNLVPvRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDYG 1243
Cdd:cd10519    78 HSSNPNCYA-KVMMVNGD---HRIGIFAKRDIEAGEELFFDYG 116
PreSET smart00468
N-terminal to some SET domains; A Cys-rich putative Zn2+-binding domain that occurs N-terminal ...
1012-1110 7.23e-27

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: 105.58  E-value: 7.23e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233   1012 RDIARGYERIPIPCVNAVDSEPCPSNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSN-CMCGQLSMRCW-YDKDGR 1089
Cdd:smart00468    2 LDISNGKENVPVPLVNEVDEDPPPPDFEYISEYIYGQGVPIDRSPSPLVGCSCSGDCSSSNkCECARKNGGEFaYELNGG 81
                            90       100
                    ....*....|....*....|.
gi 224465233   1090 LLPEfnmaEPPLIFECNHACS 1110
Cdd:smart00468   82 LRLK----RKPLIYECNSRCS 98
SET_NSD cd19173
SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...
1126-1263 2.89e-26

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: 105.47  E-value: 2.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1126 ARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDS--------YLFDLDNKdgevYCIDARFYGNVSR 1197
Cdd:cd19173     2 PPTEPFKTGDRGWGLRTKRDIKKGDFVIEYVGELIDEEECRRRLKKAhennitnfYMLTLDKD----RIIDAGPKGNLSR 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224465233 1198 FINHHCEPNLvPVRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDYGerfWDIKG-KLFSCRCGSPKC 1263
Cdd:cd19173    78 FMNHSCQPNC-ETQKWTVNGD---TRVGLFAVRDIPAGEELTFNYN---LDCLGnEKKVCRCGAPNC 137
SET_ASHR3-like cd19175
SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...
1127-1264 6.43e-26

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


Pssm-ID: 380952 [Multi-domain]  Cd Length: 139  Bit Score: 104.42  E-value: 6.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1127 RLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVR--------EEDSYLFDLDnKDgevYCIDARFYGNVSRF 1198
Cdd:cd19175     1 KMKLVKTEKCGWGLVADEDINAGEFIIEYVGEVIDDKTCEERlwdmkhkgEKNFYMCEID-KD---MVIDATFKGNLSRF 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224465233 1199 INHHCEPNLVpVRVFMAHQDLrfpRIAFFSTRLIEAGEQLGFDYgeRFWDIkGKLFSCRCGSPKCR 1264
Cdd:cd19175    77 INHSCDPNCE-LQKWQVDGET---RIGVFAIRDIKKGEELTYDY--QFVQF-GADQDCHCGSKNCR 135
PHA03100 PHA03100
ankyrin repeat protein; Provisional
750-983 9.60e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 111.68  E-value: 9.60e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  750 ELQKVLLMLVDGIDPNFKMehqnKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNH-----LEAVKY 824
Cdd:PHA03100   16 KNIKYIIMEDDLNDYSYKK----PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  825 LIKAGALVDPKDAEGSTCLHLAA--KKGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVDL--VKLLLSKGSDIN 900
Cdd:PHA03100   92 LLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDIN 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  901 IRDNeeniclhwaafsgcvdiAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCAS 980
Cdd:PHA03100  171 AKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233

                  ...
gi 224465233  981 LNS 983
Cdd:PHA03100  234 LNN 236
Ank_2 pfam12796
Ankyrin repeats (3 copies);
777-870 4.28e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 100.19  E-value: 4.28e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233   777 LHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKaGALVDPKDaEGSTCLHLAAKKGHYEVVQ 856
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|....
gi 224465233   857 YLLSNGQmDVNCQD 870
Cdd:pfam12796   79 LLLEKGA-DINVKD 91
SET_SETD1 cd19169
SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...
1122-1264 3.97e-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: 99.72  E-value: 3.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1122 NGLRAR---LQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--------DSYLFDLDnkdgEVYCIDAR 1190
Cdd:cd19169     6 NQLKFRkkqLKFAKSRIHDWGLFALEPIAADEMVIEYVGQVIRQSVADEREKryeaigigSSYLFRVD----DDTIIDAT 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224465233 1191 FYGNVSRFINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGERFWDIKgklFSCRCGSPKCR 1264
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), ...
1125-1264 1.58e-23

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: 1.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1125 RARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVRE---EDS----YLFDLDNKdgevYCIDARFYGNVSR 1197
Cdd:cd19171    13 RSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREkiyESQnrgiYMFRIDND----WVIDATMTGGPAR 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224465233 1198 FINHHCEPNLVpVRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLfSCRCGSPKCR 1264
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 ...
1137-1248 7.85e-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: 7.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1137 GWGVRSLQDIPPGTFVCEYVGELISD--SEADVREEDSYLFDLDNKDGEVYcIDARFYGNVSRFINHHCEPNLVPVRVFM 1214
Cdd:cd10522    14 GLGLFAAETIAKGEFVGEYTGEVLDRweEDRDSVYHYDPLYPFDLNGDILV-IDAGKKGNLTRFINHSDQPNLELIVRTL 92
                          90       100       110
                  ....*....|....*....|....*....|....
gi 224465233 1215 AHQdlrfPRIAFFSTRLIEAGEQLGFDYGERFWD 1248
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. ...
1118-1245 1.55e-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: 94.95  E-value: 1.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1118 RVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE----DS------YLFDLDNKDgevYCI 1187
Cdd:cd10528     9 ELILSGKEEGLKVIEIDGKGRGVIATRPFEKGDFVVEYHGDLITITEAKKREAlyakDPstgcymYYFQYKGKT---YCV 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1188 DA-RFYGNVSRFINHHC-EPNLVPVRVFMAHQdlrfPRIAFFSTRLIEAGEQLGFDYGER 1245
Cdd:cd10528    86 DAtKESGRLGRLINHSKkKPNLKTKLLVIDGV----PHLILVAKRDIKPGEELLYDYGDR 141
SET_SET1 cd20072
SET domain (including post-SET domain) found in catalytic component of the Saccharomyces ...
1122-1264 2.31e-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: 94.80  E-value: 2.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1122 NGLRAR---LQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--------DSYLFDLDnkdgEVYCIDAR 1190
Cdd:cd20072     6 NQLKKRkkqLKFARSAIHNWGLYAMENISAKDMVIEYVGEVIRQQVADEREKrylrqgigSSYLFRID----DDTVVDAT 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224465233 1191 FYGNVSRFINHHCEPNLVpVRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDYGERFWDIKgklFSCRCGSPKCR 1264
Cdd:cd20072    82 KKGNIARFINHCCDPNCT-AKIIKVEGE---KRIVIYAKRDIAAGEELTYDYKFPREEDK---IPCLCGAPNCR 148
SET_KMT2A_2B cd19170
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...
1116-1264 4.67e-22

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


Pssm-ID: 380947 [Multi-domain]  Cd Length: 152  Bit Score: 94.00  E-value: 4.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1116 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--DS-----YLFDLDnkdgEVYCID 1188
Cdd:cd19170     4 RFRHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKyyESkgigcYMFRID----DDEVVD 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224465233 1189 ARFYGNVSRFINHHCEPNLVPvRVfmAHQDLRfPRIAFFSTRLIEAGEQLGFDYGERFWDIKgklFSCRCGSPKCR 1264
Cdd:cd19170    80 ATMHGNAARFINHSCEPNCYS-RV--VNIDGK-KHIVIFALRRILRGEELTYDYKFPIEDVK---IPCTCGSKKCR 148
SET_EZH-like cd19168
SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb ...
1137-1246 3.24e-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: 3.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1137 GWGVRSLQDIPPGTFVCEYVGELISDSEADVRE------EDSYLFDLDNKdgevYCIDARFYGNVSRFINHHCEP----N 1206
Cdd:cd19168    13 GLGLFAAEDIKEGEFVIEYTGELISHDEGVRREhrrgdvSYLYLFEEQEG----IWVDAAIYGNLSRYINHATDKvktgN 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 224465233 1207 LVPVRVFMAHQdlrfPRIAFFSTRLIEAGEQLGFDYGERF 1246
Cdd:cd19168    89 CMPKIMYVNHE----WRIKFTAIKDIKIGEELFFNYGDNF 124
PHA03100 PHA03100
ankyrin repeat protein; Provisional
744-936 2.34e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 95.50  E-value: 2.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  744 FSARQGELQKVLLMLVD-GIDPNFKMEhqNKRSPLHAAAEAGHV-----DICHMLVQAGANIDTCSEDQRTPLMEAAEN- 816
Cdd:PHA03100   40 YLAKEARNIDVVKILLDnGADINSSTK--NNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKk 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  817 -NHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEV------------------VQYLLSNGqMDVNCQDDGGWTPM 877
Cdd:PHA03100  118 sNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYG-VPINIKDVYGFTPL 196
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 224465233  878 IWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVN 936
Cdd:PHA03100  197 HYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
SET_NSD2 cd19211
SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...
1129-1263 1.09e-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: 86.97  E-value: 1.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1129 QLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVR-----EEDS---YLFDLDnKDgevYCIDARFYGNVSRFIN 1200
Cdd:cd19211     5 KIIKTEGKGWGLIAKRDIKKGEFVNEYVGELIDEEECMARikhahENDIthfYMLTID-KD---RIIDAGPKGNYSRFMN 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224465233 1201 HHCEPNlVPVRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDYGerfWDIKGKLFS-CRCGSPKC 1263
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) ...
1116-1264 1.11e-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: 87.00  E-value: 1.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1116 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--DS-----YLFDLDnkDGEVycID 1188
Cdd:cd19206     4 RFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREKyyDSkgigcYMFRID--DSEV--VD 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224465233 1189 ARFYGNVSRFINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLfSCRCGSPKCR 1264
Cdd:cd19206    80 ATMHGNAARFINHSCEPNCYSRVINIDGQK----HIVIFAMRKIYRGEELTYDYKFPIEDASNKL-PCNCGAKKCR 150
Ank_2 pfam12796
Ankyrin repeats (3 copies);
877-969 7.14e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 7.14e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233   877 MIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLaAKCDLHAVNiHGDSPLHIAARENRYDCVV 956
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 224465233   957 LFLSRDSDVTLKN 969
Cdd:pfam12796   79 LLLEKGADINVKD 91
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
1128-1263 9.39e-19

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: 84.21  E-value: 9.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1128 LQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVR-----EEDS---YLFDLDnKDgevYCIDARFYGNVSRFI 1199
Cdd:cd19210     4 VEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIDEEECRARiryaqEHDItnfYMLTLD-KD---RIIDAGPKGNYARFM 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224465233 1200 NHHCEPNlVPVRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDYGERFWDiKGKLfSCRCGSPKC 1263
Cdd:cd19210    80 NHCCQPN-CETQKWTVNGD---TRVGLFALCDIKAGTELTFNYNLECLG-NGKT-VCKCGAPNC 137
PHA02874 PHA02874
ankyrin repeat protein; Provisional
747-1006 6.99e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 88.10  E-value: 6.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  747 RQGELQKVLLMLVDGIDPNfkmeHQNKR--SPLHAAAEAGHVDICHMLVQAGANidtcsedqrTPLMEAAENNHlEAVKY 824
Cdd:PHA02874   44 RSGDAKIVELFIKHGADIN----HINTKipHPLLTAIKIGAHDIIKLLIDNGVD---------TSILPIPCIEK-DMIKT 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  825 LIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDN 904
Cdd:PHA02874  110 ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDN 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  905 eeniclhwaafsgcvdiaeillaakcdlhavniHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASL-NS 983
Cdd:PHA02874  189 ---------------------------------NGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIhNR 235
                         250       260
                  ....*....|....*....|...
gi 224465233  984 QVWSALQMSKALQDSAPDRPSPV 1006
Cdd:PHA02874  236 SAIELLINNASINDQDIDGSTPL 258
Ank_2 pfam12796
Ankyrin repeats (3 copies);
742-836 2.72e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 2.72e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233   742 LYFSARQGELQKVLLMLVDGIDPNFKmeHQNKRSPLHAAAEAGHVDICHMLVQaGANIDtCSEDQRTPLMEAAENNHLEA 821
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ--DKNGRTALHLAAKNGHLEIVKLLLE-HADVN-LKDNGRTALHYAARSGHLEI 76
                           90
                   ....*....|....*
gi 224465233   822 VKYLIKAGALVDPKD 836
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) ...
1121-1242 4.70e-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: 4.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1121 QNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE------DSYLFDLDNKdgevYCIDARFYGN 1194
Cdd:cd19217     1 QRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKvydkymSSFLFNLNND----FVVDATRKGN 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 224465233 1195 VSRFINHHCEPNLVpVRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDY 1242
Cdd:cd19217    77 KIRFANHSVNPNCY-AKVVMVNGD---HRIGIFAKRAIQQGEELFFDY 120
SET_NSD3 cd19212
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
1129-1263 3.12e-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: 76.89  E-value: 3.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1129 QLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVR----EEDS----YLFDLdNKDgevYCIDARFYGNVSRFIN 1200
Cdd:cd19212     5 EIIKTERRGWGLRTKRSIKKGEFVNEYVGELIDEEECRLRikraHENSvtnfYMLTV-TKD---RIIDAGPKGNYSRFMN 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224465233 1201 HHCEPNlVPVRVFMAHQDLrfpRIAFFSTRLIEAGEQLGFDYGerfWDIKGK-LFSCRCGSPKC 1263
Cdd:cd19212    81 HSCNPN-CETQKWTVNGDV---RVGLFALCDIPAGMELTFNYN---LDCLGNgRTECHCGADNC 137
SET_EZH2 cd19218
SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...
1123-1242 4.32e-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: 4.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1123 GLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREED------SYLFDLDNKdgevYCIDARFYGNVS 1196
Cdd:cd19218     1 GSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVydkymcSFLFNLNND----FVVDATRKGNKI 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 224465233 1197 RFINHHCEPNLVpVRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDY 1242
Cdd:cd19218    77 RFANHSVNPNCY-AKVMMVNGD---HRIGIFAKRAIQTGEELFFDY 118
SET_KMT2C cd19208
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) ...
1113-1264 4.60e-16

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


Pssm-ID: 380985 [Multi-domain]  Cd Length: 154  Bit Score: 76.97  E-value: 4.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1113 RNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE-------DSYLFDLDNKdgevY 1185
Cdd:cd19208     2 KSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKlyesqnrGVYMFRIDND----H 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224465233 1186 CIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLfSCRCGSPKCR 1264
Cdd:cd19208    78 VIDATLTGGPARYINHSCAPNCVAEVVTFEKGH----KIIISSSRRIQKGEELCYDYKFDFEDDQHKI-PCHCGAVNCR 151
SET_KMT2D cd19209
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...
1113-1264 6.94e-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: 76.27  E-value: 6.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1113 RNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE-------DSYLFDLDNKdgevY 1185
Cdd:cd19209     3 KSSQYRRLKTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKiyeeqnrGIYMFRINNE----H 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224465233 1186 CIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLfSCRCGSPKCR 1264
Cdd:cd19209    79 VIDATLTGGPARYINHSCAPNCVAEVVTFDKED----KIIIISSRRIPKGEELTYDYQFDFEDDQHKI-PCHCGAWNCR 152
SET_SETD5-like cd10529
SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...
1139-1242 7.33e-16

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


Pssm-ID: 380927  Cd Length: 127  Bit Score: 75.39  E-value: 7.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1139 GVRSLQDIPPGTFVCEYVGELISDSEADVREE-----DSYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEPNlVPVRVF 1213
Cdd:cd10529    18 GLVATEDISPGEPILEYKGEVSLRSEFKEDNGffkrpSPFVFFYDGFEGLPLCVDARKYGNEARFIRRSCRPN-AELRHV 96
                          90       100       110
                  ....*....|....*....|....*....|.
gi 224465233 1214 MAHQDlrFPRIAFFSTRLIEAGEQ--LGFDY 1242
Cdd:cd10529    97 VVSNG--ELRLFIFALKDIRKGTEitIPFDY 125
PHA02874 PHA02874
ankyrin repeat protein; Provisional
757-975 8.85e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 81.55  E-value: 8.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  757 MLVDGIDPNFKmeHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKD 836
Cdd:PHA02874  110 ILDCGIDVNIK--DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  837 AEGSTCLHLAAKKGHYEVVQYLLSNG-QMDVNCQDdgGWTPMIWATEYKHvDLVKLLLSKGSdINIRDNEENICLHWAAF 915
Cdd:PHA02874  188 NNGESPLHNAAEYGDYACIKLLIDHGnHIMNKCKN--GFTPLHNAIIHNR-SAIELLINNAS-INDQDIDGSTPLHHAIN 263
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224465233  916 SGC-VDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSrdSDVTLKNKEGETP 975
Cdd:PHA02874  264 PPCdIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDII--ANAVLIKEADKLK 322
SET_SETD1A cd19204
SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...
1125-1264 1.43e-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: 75.45  E-value: 1.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1125 RARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKDgevyCIDARFYGNVS 1196
Cdd:cd19204    13 KKKLRFGRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQVVADMREKryvqegigSSYLFRVDHDT----IIDATKCGNLA 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224465233 1197 RFINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGerfWDIKGKLFSCRCGSPKCR 1264
Cdd:cd19204    89 RFINHCCTPNCYAKVITIESQK----KIVIYSKQPIGVNEEITYDYK---FPIEDNKIPCLCGTENCR 149
PHA03095 PHA03095
ankyrin-like protein; Provisional
811-976 1.90e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.84  E-value: 1.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  811 MEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHY---EVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHV- 886
Cdd:PHA03095   19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAG-ADVNAPERCGFTPLHLYLYNATTl 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  887 DLVKLLLSKGSDINIRDNEENICLHWAAFSGCVD--IAEILLAAKCDLHAVNIHGDSPLHIAARENRYD--CVVLFLSRD 962
Cdd:PHA03095   98 DVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLLIDAG 177
                         170
                  ....*....|....
gi 224465233  963 SDVTLKNKEGETPL 976
Cdd:PHA03095  178 ADVYAVDDRFRSLL 191
SET_KMT2B cd19207
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...
1116-1264 5.19e-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: 73.90  E-value: 5.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1116 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE-------DSYLFDLDNKDgevyCID 1188
Cdd:cd19207     4 RFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKfydskgiGCYMFRIDDFD----VVD 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224465233 1189 ARFYGNVSRFINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLfSCRCGSPKCR 1264
Cdd:cd19207    80 ATMHGNAARFINHSCEPNCYSRVIHVEGQK----HIVIFALRKIYRGEELTYDYKFPIEDASNKL-PCNCGAKRCR 150
SET_SpSET3-like cd19183
SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...
1139-1250 5.59e-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: 74.36  E-value: 5.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1139 GVRSLQDIPPGTFVCEYVGELISdseadvreEDSYLFDLDNKDGE-------VY-------CIDARFYGNVSRFINHHCE 1204
Cdd:cd19183    15 GLFADRPIPAGDPIQELLGEIGL--------QSEYIADPENQYQIlgapkphVFfhpqsplYIDTRRSGSVARFIRRSCR 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 224465233 1205 PN--LVPVRVfmahQDLRFPRIAFFSTRLIEAGEQLGFDYGerfWDIK 1250
Cdd:cd19183    87 PNaeLVTVAS----DSGSVLKFVLYASRDISPGEEITIGWD---WDNP 127
PHA02876 PHA02876
ankyrin repeat protein; Provisional
747-1001 6.40e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 79.72  E-value: 6.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  747 RQGELQKVLLMLVDGIDPNFKMEHQnkRSPLHAAAEAGHVDICHMLVQAGA--------------------NIDTCSE-- 804
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYC--ITPIHYAAERGNAKMVNLLLSYGAdvniialddlsvlecavdskNIDTIKAii 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  805 DQRT-------PLMEAAENNHLEA----------------------------------VKYLIKAGALVDPKDAEGSTCL 843
Cdd:PHA02876  232 DNRSninkndlSLLKAIRNEDLETslllydagfsvnsiddckntplhhasqapslsrlVPKLLERGADVNAKNIKGETPL 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  844 HLAAKKGH-YEVVQYLLSNGQmDVNCQDDGGWTPMIWATEY-KHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDI 921
Cdd:PHA02876  312 YLMAKNGYdTENIRTLIMLGA-DVNAADRLYITPLHQASTLdRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  922 AEILLAAKCDLHAVNIHGDSPLHIA-ARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNSqvwSALQMSKALQDSAP 1000
Cdd:PHA02876  391 INTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKN---CKLDVIEMLLDNGA 467

                  .
gi 224465233 1001 D 1001
Cdd:PHA02876  468 D 468
PHA02874 PHA02874
ankyrin repeat protein; Provisional
707-905 1.72e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 77.31  E-value: 1.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  707 PTPGLSQGPGKETLESAlIALDSEKPKKLRFhpkqLYFSARQGELQKVLLMLVDGIDPNfkMEHQNKRSPLHAAAEAGHV 786
Cdd:PHA02874   98 PIPCIEKDMIKTILDCG-IDVNIKDAELKTF----LHYAIKKGDLESIKMLFEYGADVN--IEDDNGCYPIHIAIKHNFF 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  787 DICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHyEVVQYLLSNGQmdV 866
Cdd:PHA02874  171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNAS--I 247
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 224465233  867 NCQDDGGWTPMIWATEYK-HVDLVKLLLSKGSDINIRDNE 905
Cdd:PHA02874  248 NDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNK 287
PHA02875 PHA02875
ankyrin repeat protein; Provisional
749-989 4.74e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 75.80  E-value: 4.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  749 GELQKVLLMLVDGIDPNFKMehQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKA 828
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEI--YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  829 GALVDP---KDaeGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNE 905
Cdd:PHA02875   91 GKFADDvfyKD--GMTPLHLATILKKLDIMKLLIARGA-DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  906 ENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGD-SPLHIAARENRYDCVVLFLSRDSD---VTLKNKEGETPLQ---- 977
Cdd:PHA02875  168 GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADcniMFMIEGEECTILDmicn 247
                         250
                  ....*....|...
gi 224465233  978 -CASLNSQVWSAL 989
Cdd:PHA02875  248 mCTNLESEAIDAL 260
PHA02875 PHA02875
ankyrin repeat protein; Provisional
772-967 5.52e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 75.80  E-value: 5.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  772 NKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGH 851
Cdd:PHA02875    1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  852 YEVVQYLLSNGQM--DVNCQDdgGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAK 929
Cdd:PHA02875   81 VKAVEELLDLGKFadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 224465233  930 CDLHAVNIHGDSPLHIA-ARENRYDCVVL--------FLSRDSDVTL 967
Cdd:PHA02875  159 ACLDIEDCCGCTPLIIAmAKGDIAICKMLldsganidYFGKNGCVAA 205
Ank_4 pfam13637
Ankyrin repeats (many copies);
774-826 9.13e-14

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 66.91  E-value: 9.13e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 224465233   774 RSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLI 826
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
1127-1243 9.89e-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: 9.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1127 RLQLYRTRDMGWGVRSLQDIPPGTFVCeyvgelisdseadvreedsylfdldnkdgevycidarfygnVSRFINHHCEPN 1206
Cdd:cd08161     1 EIRPSTIPGAGFGLFATRDIPKGEVIG-----------------------------------------LARFINHSCEPN 39
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 224465233 1207 LVPVRVFmahqDLRFPRIAFFSTRLIEAGEQLGFDYG 1243
Cdd:cd08161    40 CEFEEVY----VGGKPRVFIVALRDIKAGEELTVDYG 72
PHA03100 PHA03100
ankyrin repeat protein; Provisional
765-904 9.97e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.09  E-value: 9.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  765 NFKMEHQNKRSPLHAAAEA--GHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLE------------------AVKY 824
Cdd:PHA03100   98 NVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkilkllidkgvdinaknRVNY 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  825 LIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDN 904
Cdd:PHA03100  178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA-NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA03095 PHA03095
ankyrin-like protein; Provisional
753-961 1.06e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.06  E-value: 1.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  753 KVLLMLVD-GIDPNFKmeHQNKRSPLHA--AAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNH--LEAVKYLIK 827
Cdd:PHA03095   98 DVIKLLIKaGADVNAK--DKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLID 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  828 AGALVDPKDAEGSTCLHLAAK--KGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATEY---KHVDLVKLLLsKGSDINIR 902
Cdd:PHA03095  176 AGADVYAVDDRFRSLLHHHLQsfKPRARIVRELIRAG-CDPAATDMLGNTPLHSMATGsscKRSLVLPLLI-AGISINAR 253
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 224465233  903 DNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSR 961
Cdd:PHA03095  254 NRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
PHA03095 PHA03095
ankyrin-like protein; Provisional
739-980 1.10e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.06  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  739 PKQLYFSARQGELQKVLLMLVD-GIDPNFKmeHQNKRSPLHAAAEAGHV-DICHMLVQAGANIDTCSEDQRTPLME--AA 814
Cdd:PHA03095   50 PLHLYLHYSSEKVKDIVRLLLEaGADVNAP--ERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLHVylSG 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  815 ENNHLEAVKYLIKAGALVDPKDAEGSTCLHLaakkghyevvqyLLSNGqmDVNcqddggwtpmiwateykhVDLVKLLLS 894
Cdd:PHA03095  128 FNINPKVIRLLLRKGADVNALDLYGMTPLAV------------LLKSR--NAN------------------VELLRLLID 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  895 KGSDINIRDNEENICLHWAAFSgCVDIAEI---LLAAKCDLHAVNIHGDSPLHIAARENRYDCVVL--FLSRDSDVTLKN 969
Cdd:PHA03095  176 AGADVYAVDDRFRSLLHHHLQS-FKPRARIvreLIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARN 254
                         250
                  ....*....|.
gi 224465233  970 KEGETPLQCAS 980
Cdd:PHA03095  255 RYGQTPLHYAA 265
PHA02875 PHA02875
ankyrin repeat protein; Provisional
741-926 1.41e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 74.26  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  741 QLYFSARQGELQKV--LLMLVDGIDPNFkmeHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNH 818
Cdd:PHA02875   71 ELHDAVEEGDVKAVeeLLDLGKFADDVF---YKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGD 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  819 LEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSD 898
Cdd:PHA02875  148 IKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 224465233  899 INIR---DNEE--------NICLHWAAFSGCVDIAEILL 926
Cdd:PHA02875  228 CNIMfmiEGEEctildmicNMCTNLESEAIDALIADIAI 266
PHA02878 PHA02878
ankyrin repeat protein; Provisional
776-1098 1.43e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 74.92  E-value: 1.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  776 PLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIK-------AGALVDPKDA------EGSTC 842
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcsvFYTLVAIKDAfnnrnvEIFKI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  843 LHLAAKKGHY------------------EVVQYLLSNGQmDVNCQD-DGGWTPMIWATEYKHVDLVKLLLSKGSDINIRD 903
Cdd:PHA02878  120 ILTNRYKNIQtidlvyidkkskddiieaEITKLLLSYGA-DINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPD 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  904 NEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIA-ARENRYDCVVLFLSRDSDVTLKNK-EGETPLQCASL 981
Cdd:PHA02878  199 KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIK 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  982 NSQVWSALQMSKALQDSAP-DRPSPVERIVSRdiargyeRIPIPCVNAVDSEPCPSNYKYVSqncVTSPMNIDRNIthlq 1060
Cdd:PHA02878  279 SERKLKLLLEYGADINSLNsYKLTPLSSAVKQ-------YLCINIGRILISNICLLKRIKPD---IKNSEGFIDNM---- 344
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 224465233 1061 ycvcidDCSSSNCMCGQLSMRCWYD----KDGRLLPEFNMAE 1098
Cdd:PHA02878  345 ------DCITSNKRLNQIKDKCEDElnrlASIKITNTYSFDD 380
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
808-979 3.09e-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: 3.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  808 TPLMEAAENNHLEAVKYLIKAGAlVDP--KDAEGSTCLHLAAKKGHYEVVQYLLSNGQMDVN----CQDDGGWTPMIWAT 881
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPS-CDLfqRGALGETALHVAALYDNLEAAVVLMEAAPELVNepmtSDLYQGETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  882 EYKHVDLVKLLLSKGSDIN--------IRDNEENICL---HWAAFSGCV---DIAEILLAAKCDLHAVNIHGDSPLHIAA 947
Cdd:cd22192    98 VNQNLNLVRELIARGADVVspratgtfFRPGPKNLIYygeHPLSFAACVgneEIVRLLIEHGADIRAQDSLGNTVLHILV 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 224465233  948 RENR-------YDcvvLFLSRDSDV------TLKNKEGETPLQCA 979
Cdd:cd22192   178 LQPNktfacqmYD---LILSYDKEDdlqpldLVPNNQGLTPFKLA 219
SET_SETD1B cd19205
SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...
1125-1264 3.13e-13

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


Pssm-ID: 380982 [Multi-domain]  Cd Length: 153  Bit Score: 68.54  E-value: 3.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1125 RARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKDgevyCIDARFYGNVS 1196
Cdd:cd19205    13 KKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKryedegigSSYMFRVDHDT----IIDATKCGNFA 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224465233 1197 RFINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGerfWDIKGKLFSCRCGSPKCR 1264
Cdd:cd19205    89 RFINHSCNPNCYAKVITVESQK----KIVIYSKQHINVNEEITYDYK---FPIEDVKIPCLCGSENCR 149
Ank_4 pfam13637
Ankyrin repeats (many copies);
806-859 3.28e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 65.37  E-value: 3.28e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 224465233   806 QRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLL 859
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
750-930 5.31e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.99  E-value: 5.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  750 ELQKVLLMLVDGIDPNFKMEHQNKrSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAG 829
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHKGN-TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  830 ALVDPKDAEGSTCLHLAAKK-GHYEVVQYLLSNGqMDVNCQDD-GGWTPMiwATEYKHVDLVKLLLSKGSDINIRDNEEN 907
Cdd:PHA02878  225 ASTDARDKCGNTPLHISVGYcKDYDILKLLLEHG-VDVNAKSYiLGLTAL--HSSIKSERKLKLLLEYGADINSLNSYKL 301
                         170       180
                  ....*....|....*....|....
gi 224465233  908 ICLHWAAFS-GCVDIAEILLAAKC 930
Cdd:PHA02878  302 TPLSSAVKQyLCINIGRILISNIC 325
Ank_2 pfam12796
Ankyrin repeats (3 copies);
910-988 4.22e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 4.22e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224465233   910 LHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDsDVTLKNkEGETPLQCASLNSQVWSA 988
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIV 77
Ank_4 pfam13637
Ankyrin repeats (many copies);
839-893 5.74e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.52  E-value: 5.74e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 224465233   839 GSTCLHLAAKKGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVDLVKLLL 893
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
812-982 2.96e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.78  E-value: 2.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  812 EAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKL 891
Cdd:PHA02876  151 ERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGA-DVNIIALDDLSVLECAVDSKNIDTIKA 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  892 LLSKGSDINIRDneenICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVV-LFLSRDSDVTLKNK 970
Cdd:PHA02876  230 IIDNRSNINKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVpKLLERGADVNAKNI 305
                         170
                  ....*....|..
gi 224465233  971 EGETPLQCASLN 982
Cdd:PHA02876  306 KGETPLYLMAKN 317
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
682-986 1.69e-10

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: 1.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  682 DDKLQGAASHVPEgfDPTGPAGLGRPTPGLSQGPGKETlesaliALDSEKPKKLRFHPKQLYFSARQGELQKV---LLML 758
Cdd:cd22194     3 DSNIRQCPSGNCD--DMDSPQSPQDDTPSNPNSPSAEL------AKEEQRDKKKRLKKVSEAAVEELGELLKElkdLSRR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  759 VDGIDPNFKMEHQNKrsplhaAAEAGHVdiChmLVQAGANIDTCSEDQRTPLMEAAENNHLeaVKYLIKAGalVDPKDAE 838
Cdd:cd22194    75 RRKTDVPDFLMHKLT------ASDTGKT--C--LMKALLNINENTKEIVRILLAFAEENGI--LDRFINAE--YTEEAYE 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  839 GSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQ-----------DDG---GWTPMIWATEYKHVDLVKLLLSKGSD-INIRD 903
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGA-DVNAHakgvffnpkykHEGfyfGETPLALAACTNQPEIVQLLMEKESTdITSQD 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  904 NEENICLHwaafsGCVDIAEillaakcdlhavnihgDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNS 983
Cdd:cd22194   220 SRGNTVLH-----ALVTVAE----------------DSKTQNDFVKRMYDMILLKSENKNLETIRNNEGLTPLQLAAKMG 278

                  ...
gi 224465233  984 QVW 986
Cdd:cd22194   279 KAE 281
PHA02876 PHA02876
ankyrin repeat protein; Provisional
747-998 2.02e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.08  E-value: 2.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  747 RQGELQKVLLMLVDGIDPNFKMEHQNkrSPLHAAAEAGHVD-ICHMLVQAGANIDTCSEDQRTPLMEAAENNH-LEAVKY 824
Cdd:PHA02876  249 RNEDLETSLLLYDAGFSVNSIDDCKN--TPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRT 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  825 LIKAGALVDPKDAEGSTCLHLAAKKGHY-EVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRD 903
Cdd:PHA02876  327 LIMLGADVNAADRLYITPLHQASTLDRNkDIVITLLELGA-NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALS 405
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  904 NEENICLHWAAF-SGCVDIAEILLAAKCDLHAVNIHGDSPLHIAAREN-RYDCVVLFLSRDSDVTLKNKEGETPLQCA-S 980
Cdd:PHA02876  406 QKIGTALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAlE 485
                         250
                  ....*....|....*...
gi 224465233  981 LNSQVWSALQMSKALQDS 998
Cdd:PHA02876  486 YHGIVNILLHYGAELRDS 503
PHA03095 PHA03095
ankyrin-like protein; Provisional
754-935 6.27e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.12  E-value: 6.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  754 VLLMLVDGIDPNFKMEHQnkRSPLHAAAEAGHVDI--CHMLVQAGANIDTCSEDQRTPLmeaaeNNHLEAVK-------Y 824
Cdd:PHA03095  135 IRLLLRKGADVNALDLYG--MTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLL-----HHHLQSFKprarivrE 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  825 LIKAGALVDPKDAEGSTCLHLAAKKGHYE---VVQYLLSNgqMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINI 901
Cdd:PHA03095  208 LIRAGCDPAATDMLGNTPLHSMATGSSCKrslVLPLLIAG--ISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285
                         170       180       190
                  ....*....|....*....|....*....|....
gi 224465233  902 RDNEENICLHWAAFSGCVDIAEILLAAKCDLHAV 935
Cdd:PHA03095  286 VSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
Ank_4 pfam13637
Ankyrin repeats (many copies);
909-959 3.90e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 3.90e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 224465233   909 CLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFL 959
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
786-906 5.06e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 60.23  E-value: 5.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  786 VDICHMLVQAGANIDTCSEDQRTPLMEAAEN----NH-LEAVKYLIKAGALVDPKDAEGST---CLHLAAKKGHYEVVQY 857
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHmLDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLF 130
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 224465233  858 LLSNGqMDVNCQDDGGWTPM-IWATEYKHVDL--VKLLLSKGSDINIRDNEE 906
Cdd:PHA02798  131 MIENG-ADTTLLDKDGFTMLqVYLQSNHHIDIeiIKLLLEKGVDINTHNNKE 181
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
769-986 5.45e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.65  E-value: 5.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  769 EHQNKR--SPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLA 846
Cdd:PLN03192  519 EHDDPNmaSNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNA 598
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  847 AKKGHYEVVQYL-----LSNGQM--DVNCQddggwtpmiwATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCV 919
Cdd:PLN03192  599 ISAKHHKIFRILyhfasISDPHAagDLLCT----------AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHV 668
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224465233  920 DIAEILLAAKCDLHAVNIHGD-SPLH----IAARENRYDCVVLFLSRDSDVTLKNKEGETP--LQCASLNSQVW 986
Cdd:PLN03192  669 DMVRLLIMNGADVDKANTDDDfSPTElrelLQKRELGHSITIVDSVPADEPDLGRDGGSRPgrLQGTSSDNQCR 742
Ank_4 pfam13637
Ankyrin repeats (many copies);
873-926 2.91e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 2.91e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 224465233   873 GWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILL 926
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
825-880 5.72e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 5.72e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 224465233   825 LIKAG-ALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWA 880
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGV-DLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
858-905 5.95e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 5.95e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 224465233   858 LLSNGQMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNE 905
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE 48
Ank_5 pfam13857
Ankyrin repeats (many copies);
925-979 2.21e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 2.21e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 224465233   925 LLAAK-CDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCA 979
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
742-868 5.99e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.10  E-value: 5.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  742 LYFSARQGELQKVLLMLVDGIdpNFKMEHQNKRSPLHAAAEAGHVDICHMLVQ-AGANIDTCSEDQrtpLMEAAENNHLE 820
Cdd:PLN03192  562 LHIAASKGYEDCVLVLLKHAC--NVHIRDANGNTALWNAISAKHHKIFRILYHfASISDPHAAGDL---LCTAAKRNDLT 636
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 224465233  821 AVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNC 868
Cdd:PLN03192  637 AMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA-DVDK 683
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
1137-1263 8.73e-07

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: 49.30  E-value: 8.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1137 GWGVRSLQDIPPGTFVCEyvgelisdseadvreEDSYLFDLDN---KDGEVYCIDARFYGNVSRFiNHHCEPNLVpvrvf 1213
Cdd:cd20071    10 GRGLVATRDIEPGELILV---------------EKPLVSVPSNsfsLTDGLNEIGVGLFPLASLL-NHSCDPNAV----- 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 224465233 1214 maHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWD--------IKGKLFSCRCgsPKC 1263
Cdd:cd20071    69 --VVFDGNGTLRVRALRDIKAGEELTISYIDPLLPrterrrelLEKYGFTCSC--PRC 122
Ank_5 pfam13857
Ankyrin repeats (many copies);
892-946 2.07e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 2.07e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 224465233   892 LLSKGS-DINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIA 946
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
786-867 4.72e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 4.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  786 VDICHM-----------LVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEV 854
Cdd:PTZ00322   84 VELCQLaasgdavgariLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163
                          90
                  ....*....|...
gi 224465233  855 VQYLLSNGQMDVN 867
Cdd:PTZ00322  164 VQLLSRHSQCHFE 176
SET_ATXR5_6-like cd10539
SET domain found in fungal protein lysine methyltransferase SET5 and similar protein; The ...
1137-1244 5.43e-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: 47.40  E-value: 5.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1137 GWGVRSLQDIPPGTFVCEYVGEL--ISDSEADvrEEDSYLFDLDNKDGE---VYCIDARfyGNVSRFI----NHHCE--- 1204
Cdd:cd10539    15 GFTVEADGFIKDLTIIAEYTGDVdyIRNREFD--DNDSIMTLLLAGDPSkslVICPDKR--GNIARFIsginNHTKDgkk 90
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 224465233 1205 -PNLVPVRVFMAHQdlrfPRIAFFSTRLIEAGEQLGFDYGE 1244
Cdd:cd10539    91 kQNCKCVRYSINGE----ARVLLVATRDIAKGERLYYDYNG 127
PHA02875 PHA02875
ankyrin repeat protein; Provisional
850-1047 8.02e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.99  E-value: 8.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  850 GHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAK 929
Cdd:PHA02875   13 GELDIARRLLDIG-INPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  930 CDLHAVNIH-GDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNSQVwsalQMSKALQDSApdrpspver 1008
Cdd:PHA02875   92 KFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI----KGIELLIDHK--------- 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 224465233 1009 iVSRDIARGYERIP-IPCVNAVDSEPCP------SNYKYVSQN-CVT 1047
Cdd:PHA02875  159 -ACLDIEDCCGCTPlIIAMAKGDIAICKmlldsgANIDYFGKNgCVA 204
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
873-904 8.38e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.82  E-value: 8.38e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 224465233   873 GWTPMIWA-TEYKHVDLVKLLLSKGSDINIRDN 904
Cdd:pfam00023    2 GNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
SET_KMT2E cd19182
SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...
1140-1243 9.14e-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: 9.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1140 VRSLQDIPPGTFVCEYVGELISDSEAdvrEEDSYLFD--------LDNKDGEVYCIDARFYGNVSRFINHHCEPNlVPVR 1211
Cdd:cd19182    21 LKAAKDLPPDTLIIEYRGKFMLREQF---EANGYFFKrpypfvlfYSKFHGLEMCVDARTFGNEARFIRRSCTPN-AEVR 96
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 224465233 1212 VFMAHQDLrfpRIAFFSTRLIEAGEQL----GFDYG 1243
Cdd:cd19182    97 HVIEDGTI---HLYIYSIRSIPKGTEItiafDFDYG 129
PHA03100 PHA03100
ankyrin repeat protein; Provisional
753-837 1.13e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  753 KVLLMLVDGIDPNFKmehqNKR--SPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGA 830
Cdd:PHA03100  174 RVNYLLSYGVPINIK----DVYgfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249

                  ....*..
gi 224465233  831 LVDPKDA 837
Cdd:PHA03100  250 SIKTIIE 256
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
805-894 1.29e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  805 DQRTPLMEAAENNHLEA------VKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMI 878
Cdd:PTZ00322   75 DPVVAHMLTVELCQLAAsgdavgARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA-DPTLLDKDGKTPLE 153
                          90
                  ....*....|....*.
gi 224465233  879 WATEYKHVDLVKLLLS 894
Cdd:PTZ00322  154 LAEENGFREVVQLLSR 169
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
807-902 1.36e-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: 49.69  E-value: 1.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233   807 RTPLMEAA-ENNHLEAVKYLIKAGALVDpkdaEGSTCLHLAAKKGH---YEVVQYLLSNGQMDVN-------CQDD--GG 873
Cdd:TIGR00870   53 RSALFVAAiENENLELTELLLNLSCRGA----VGDTLLHAISLEYVdavEAILLHLLAAFRKSGPlelandqYTSEftPG 128
                           90       100
                   ....*....|....*....|....*....
gi 224465233   874 WTPMIWATEYKHVDLVKLLLSKGSDINIR 902
Cdd:TIGR00870  129 ITALHLAAHRQNYEIVKLLLERGASVPAR 157
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
838-868 1.41e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 1.41e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 224465233    838 EGSTCLHLAAKKGHYEVVQYLLSNGQmDVNC 868
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA-DINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
939-991 1.49e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 1.49e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 224465233   939 GDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNSQVwSALQM 991
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNV-EVLKL 52
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
838-871 1.77e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 1.77e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 224465233   838 EGSTCLHLAAKK-GHYEVVQYLLSNGQmDVNCQDD 871
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGA-DVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
772-800 1.91e-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: 42.57  E-value: 1.91e-05
                            10        20
                    ....*....|....*....|....*....
gi 224465233    772 NKRSPLHAAAEAGHVDICHMLVQAGANID 800
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
SET_SETD5 cd19181
SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...
1120-1206 2.69e-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: 45.77  E-value: 2.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1120 VQNGLRARLQLYRTRdmgwgVRSLQDIPPGTFVCEYVGELISDSEADVRE---EDSYLFDL--DNKDGEVYCIDARFYGN 1194
Cdd:cd19181     6 LQLGRVTRVQKHRKI-----LRAARDLALDTLIIEYRGKVMLRQQFEVNGhffKRPYPFVLfySKFNGVEMCVDARTFGN 80
                          90
                  ....*....|..
gi 224465233 1195 VSRFINHHCEPN 1206
Cdd:cd19181    81 DARFIRRSCTPN 92
Ank_5 pfam13857
Ankyrin repeats (many copies);
792-846 2.90e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 2.90e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 224465233   792 LVQAG-ANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLA 846
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
889-960 4.36e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 4.36e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224465233  889 VKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLS 960
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
873-901 5.29e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 5.29e-05
                            10        20
                    ....*....|....*....|....*....
gi 224465233    873 GWTPMIWATEYKHVDLVKLLLSKGSDINI 901
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
814-976 5.62e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 47.60  E-value: 5.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  814 AENNHLEAVKYLIKAGALVDPKDAEGSTCLHlaakkghyevvQYLLSNgqmdvncqddggwtpmiwateYKHVDLVKLLL 893
Cdd:PHA02716  292 ARNIDISVVYSFLQPGVKLHYKDSAGRTCLH-----------QYILRH---------------------NISTDIIKLLH 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  894 SKGSDINIRDNEENICLHwaafsgcvdiaeILLAAKCDLHAVNIHGDSPLhiaarenRYDCVVLFLSRDSDVTLKNKEGE 973
Cdd:PHA02716  340 EYGNDLNEPDNIGNTVLH------------TYLSMLSVVNILDPETDNDI-------RLDVIQCLISLGADITAVNCLGY 400

                  ...
gi 224465233  974 TPL 976
Cdd:PHA02716  401 TPL 403
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
922-982 6.74e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 6.74e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224465233  922 AEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLN 982
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
1137-1248 8.93e-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: 8.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1137 GWGVRSLQDIPPGTFVcEYVGELISDSEADVREEDSYLFDLdnkdgeVYCIDARFY----GNVSRFiNHHCEPNLVPVRV 1212
Cdd:cd10540    11 GRGVFATRPIKKGEVI-EEAPVIVLPKEEYQHLCKTVLDHY------VFSWGDGCLalalGYGSMF-NHSYTPNAEYEID 82
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 224465233 1213 FMAHqdlrfpRIAFFSTRLIEAGEQLGFDYGERFWD 1248
Cdd:cd10540    83 FENQ------TIVFYALRDIEAGEELTINYGDDLWD 112
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
746-827 1.02e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  746 ARQGELQKVLLMLVDGIDPNFKMEHQnkRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYL 825
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDG--RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167

                  ..
gi 224465233  826 IK 827
Cdd:PTZ00322  168 SR 169
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
772-800 1.17e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 1.17e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 224465233   772 NKRSPLHAAAE-AGHVDICHMLVQAGANID 800
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVN 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
846-968 1.69e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.84  E-value: 1.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233   846 AAKKGHYEVVQYLLSNGQMD-VNCQDDGGWTPMIW-ATEYKHVDLVKLLLSKGSDINIRDNeeniCLHWAA---FSGCVD 920
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKKLnINCPDRLGRSALFVaAIENENLELTELLLNLSCRGAVGDT----LLHAISleyVDAVEA 99
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 224465233   921 IAEILLAAKCD----LHAVNI------HGDSPLHIAARENRYDCVVLFLSRDSDVTLK 968
Cdd:TIGR00870  100 ILLHLLAAFRKsgplELANDQytseftPGITALHLAAHRQNYEIVKLLLERGASVPAR 157
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
805-833 2.15e-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: 39.49  E-value: 2.15e-04
                            10        20
                    ....*....|....*....|....*....
gi 224465233    805 DQRTPLMEAAENNHLEAVKYLIKAGALVD 833
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02989 PHA02989
ankyrin repeat protein; Provisional
756-929 2.15e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 45.50  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  756 LMLVDGIDPNfkmEHQNKR--SPLHAAAEAGHV--DICHMLVQAGANI-DTCSEDQRTP----LMEAAENNHLEAVKYLI 826
Cdd:PHA02989  129 FLLSKGINVN---DVKNSRgyNLLHMYLESFSVkkDVIKILLSFGVNLfEKTSLYGLTPmniyLRNDIDVISIKVIKYLI 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  827 KAGALVDPKDAEGSTCL------HLAAKKGHYEVVQYLLSngQMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDIN 900
Cdd:PHA02989  206 KKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILK--YIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIY 283
                         170       180
                  ....*....|....*....|....*....
gi 224465233  901 IRDNEENICLHWAAFSGCVDIAEILLAAK 929
Cdd:PHA02989  284 NVSKDGDTVLTYAIKHGNIDMLNRILQLK 312
PHA02989 PHA02989
ankyrin repeat protein; Provisional
753-979 4.70e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 44.35  E-value: 4.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  753 KVLLMLVD-GIDPNFK--MEhqnkrSPLHAAAEAGHVD------ICHMLVQAGANIDTCSEDQRTPLMEAAEN---NHLE 820
Cdd:PHA02989   51 KIVKLLIDnGADVNYKgyIE-----TPLCAVLRNREITsnkikkIVKLLLKFGADINLKTFNGVSPIVCFIYNsniNNCD 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  821 AVKYLIKAGALV-DPKDAEGSTCLH--LAAKKGHYEVVQYLLSNGQMDVNCQDDGGWTPM-IW---ATEYKHVDLVKLLL 893
Cdd:PHA02989  126 MLRFLLSKGINVnDVKNSRGYNLLHmyLESFSVKKDVIKILLSFGVNLFEKTSLYGLTPMnIYlrnDIDVISIKVIKYLI 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  894 SKGSDInirdnEENICLHWAAFSGCVDIAEILLAaKC-----------DLHAVNIHGDSPLHIAARENRYDCVVLFLSRD 962
Cdd:PHA02989  206 KKGVNI-----ETNNNGSESVLESFLDNNKILSK-KEfkvlnfilkyiKINKKDKKGFNPLLISAKVDNYEAFNYLLKLG 279
                         250
                  ....*....|....*..
gi 224465233  963 SDVTLKNKEGETPLQCA 979
Cdd:PHA02989  280 DDIYNVSKDGDTVLTYA 296
PHA02859 PHA02859
ankyrin repeat protein; Provisional
799-945 4.70e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.88  E-value: 4.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  799 IDTCSEDQRTPLMEAAENNH--LEAVKYLIKAGALVDPK-DAEGSTCLH--LAAKKG-HYEVVQYLLSNGQmDVNCQDDG 872
Cdd:PHA02859   44 VNDCNDLYETPIFSCLEKDKvnVEILKFLIENGADVNFKtRDNNLSALHhyLSFNKNvEPEILKILIDSGS-SITEEDED 122
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224465233  873 GWTPM-IWATEYK-HVDLVKLLLSKGSDINIRDNEENICLH-WAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHI 945
Cdd:PHA02859  123 GKNLLhMYMCNFNvRINVIKLLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNCYDL 198
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
805-836 6.12e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 6.12e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 224465233   805 DQRTPLMEAAE-NNHLEAVKYLIKAGALVDPKD 836
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
938-967 6.27e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 6.27e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 224465233    938 HGDSPLHIAARENRYDCVVLFLSRDSDVTL 967
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
844-926 7.63e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 7.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  844 HLAAKkGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAE 923
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGA-DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                  ...
gi 224465233  924 ILL 926
Cdd:PTZ00322  166 LLS 168
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
938-970 7.75e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 7.75e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 224465233   938 HGDSPLHIAA-RENRYDCVVLFLSRDSDVTLKNK 970
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02884 PHA02884
ankyrin repeat protein; Provisional
875-948 1.16e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 42.66  E-value: 1.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224465233  875 TPMIWATEYKHVDLVKLLLSKGSDINIRDNEENIC-LHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAAR 948
Cdd:PHA02884   72 NPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITpLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
873-901 1.23e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 1.23e-03
                           10        20
                   ....*....|....*....|....*....
gi 224465233   873 GWTPMIWATEYKHVDLVKLLLSKGSDINI 901
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
838-868 1.43e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.43e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 224465233   838 EGSTCLHLAAKKGHYEVVQYLLSNGqMDVNC 868
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENG-ADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
772-801 1.51e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.51e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 224465233   772 NKRSPLHAAAEAGHVDICHMLVQAGANIDT 801
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
805-830 1.52e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.52e-03
                           10        20
                   ....*....|....*....|....*.
gi 224465233   805 DQRTPLMEAAENNHLEAVKYLIKAGA 830
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGA 26
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
1134-1246 2.32e-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: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1134 RDMGWGVRSLQDIPPGTFVCEYVGELISDSEAdvrEEDSYLFDLDNKDGEVYCIDAR--FYGNVSRFIN---HHCEPNLV 1208
Cdd:cd19193    16 PGAGLGVWAEAPIPKGMVFGPYEGEIVEDEEA---ADSGYSWQIYKGGKLSHYIDAKdeSKSNWMRYVNcarNEEEQNLV 92
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 224465233 1209 pvrvfmAHQDLRfpRIAFFSTRLIEAGEQLGFDYGERF 1246
Cdd:cd19193    93 ------AFQYRG--KIYYRTCKDIAPGTELLVWYGDEY 122
SET_Suv4-20-like cd10524
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
1136-1268 4.10e-03

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


Pssm-ID: 380922 [Multi-domain]  Cd Length: 141  Bit Score: 39.19  E-value: 4.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233 1136 MGWGVRSLQDIPPGTFVCEYVGELISDSEADV-----REED-SYLFDLDNKDgevycidARFYGNVSRFINHHCEPN--L 1207
Cdd:cd10524    18 YGAKIIATKPIKKGEKIHELCGCIAELSEEEEallrpGGNDfSVMYSSRKKC-------SQLWLGPAAFINHDCRPNckF 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224465233 1208 VPVRVfmahqdlrfPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKlfSCRCGSpkCRHSSA 1268
Cdd:cd10524    91 VPTGK---------STACVKVLRDIEPGEEITVYYGDNYFGENNE--ECECET--CERRGR 138
PHA02946 PHA02946
ankyin-like protein; Provisional
757-943 4.36e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.19  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  757 MLVDGIDPNFKMEHQNkrSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPL--MEAAENNHLEAVKYLIKAGALVDP 834
Cdd:PHA02946   58 LLHRGYSPNETDDDGN--YPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKINN 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  835 K-DAEGSTCLhLAAKKGHYEVVQYLLSNGqMDVNCQDDGGWTPM--IWATEYKHVDLVKLLLSKGSDINIRDNEENICLH 911
Cdd:PHA02946  136 SvDEEGCGPL-LACTDPSERVFKKIMSIG-FEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLH 213
                         170       180       190
                  ....*....|....*....|....*....|....
gi 224465233  912 WAAFSGC--VDIAEILLAAKcDLHAVNIHGDSPL 943
Cdd:PHA02946  214 IVCSKTVknVDIINLLLPST-DVNKQNKFGDSPL 246
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
792-911 6.84e-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: 6.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  792 LVQAGANIDTCSEDQRTPLMEAAENNhlEAVKYLIKAGALVDPkdAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDD 871
Cdd:cd21882    30 LHKAALNLNDGVNEAIMLLLEAAPDS--GNPKELVNAPCTDEF--YQGQTALHIAIENRNLNLVRLLVENGA-DVSARAT 104
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 224465233  872 G-------------GWTPMIWATEYKHVDLVKLLLSKGSDI---NIRDNEENICLH 911
Cdd:cd21882   105 GrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNTVLH 160
PHA02859 PHA02859
ankyrin repeat protein; Provisional
775-900 9.54e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.03  E-value: 9.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465233  775 SPLHAAAEAGHV--DICHMLVQAGANIDTCSEDQRTPLMEA----AENNHLEAVKYLIKAGALVDPKDAEGSTCLH--LA 846
Cdd:PHA02859   53 TPIFSCLEKDKVnvEILKFLIENGADVNFKTRDNNLSALHHylsfNKNVEPEILKILIDSGSSITEEDEDGKNLLHmyMC 132
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 224465233  847 AKKGHYEVVQYLLSNGQMDVNCQDDGG---WTPMIWATEYKHVDlvkLLLSKGSDIN 900
Cdd:PHA02859  133 NFNVRINVIKLLIDSGVSFLNKDFDNNnilYSYILFHSDKKIFD---FLTSLGIDIN 186
 
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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