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Conserved domains on  [gi|557440769|ref|NP_001273504|]
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histone-lysine N-methyltransferase EHMT2 isoform d [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 944-1182 0e+00

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: 544.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  944 EDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRSC 1023
Cdd:cd10533     1 EDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRNC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1024 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNI 1103
Cdd:cd10533    81 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557440769 1104 SRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQ 1182
Cdd:cd10533   161 SRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQ 239
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
 416-545 3.15e-63

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: 210.71  E-value: 3.15e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  416 FEELPLCSCRMEAPKIDRISERAGHKCMATESVDGELLGC-NAAILKRETMRPSSRVALMVLCEAHRARMVKHHCCPGCG 494
Cdd:cd20905     1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCsNLPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 557440769  495 YFCTAGTFLECHPDFRVAHRFHKACVSQLNGMVFCPHCGEDAS-EAQEVTIP 545
Cdd:cd20905    81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLP 132
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
624-883 1.38e-53

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 189.39  E-value: 1.38e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  624 GREALEKALVIQESERRKKLRFHPRQLYLSVKQGELQKVILMLLDNLDPNFQSDQQSkrTPLHAAAQKGSVEICHVLLQA 703
Cdd:COG0666    32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  704 GANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWT 783
Cdd:COG0666   110 GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDNDGET 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  784 PIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCV 863
Cdd:COG0666   189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268

                         250       260
                  ....*....|....*....|
gi 557440769  864 LLFLSRGANPELRNKEGDTA 883
Cdd:COG0666   269 KLLLLALLLLAAALLDLLTL 288
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 23-201 1.82e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769   23 ALLLEKEPRGAAERVHSSLGDTPQSEETLPKANPDSLEPAGPSSPASVTVTVGDEGADTPVGAASLIGDEPesleGDGGR 102
Cdd:PHA03247 2734 ALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDP----ADPPA 2809

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  103 IVLGHATKSFPSSPSKGGACPSRAKMSMTGAGKSPPSVQSLAMRLLSMPGAQGAATAGPEPSPATTAAQEgQPKVHR-AR 181
Cdd:PHA03247 2810 AVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPA-RPPVRRlAR 2888

                         170       180
                  ....*....|....*....|..
gi 557440769  182 KTMSKP--SNGQPPIPEKRPPE 201
Cdd:PHA03247 2889 PAVSRSteSFALPPDQPERPPQ 2910
 
Name Accession Description Interval E-value
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 944-1182 0e+00

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: 544.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  944 EDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRSC 1023
Cdd:cd10533     1 EDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRNC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1024 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNI 1103
Cdd:cd10533    81 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557440769 1104 SRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQ 1182
Cdd:cd10533   161 SRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQ 239
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
 416-545 3.15e-63

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: 210.71  E-value: 3.15e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  416 FEELPLCSCRMEAPKIDRISERAGHKCMATESVDGELLGC-NAAILKRETMRPSSRVALMVLCEAHRARMVKHHCCPGCG 494
Cdd:cd20905     1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCsNLPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 557440769  495 YFCTAGTFLECHPDFRVAHRFHKACVSQLNGMVFCPHCGEDAS-EAQEVTIP 545
Cdd:cd20905    81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLP 132
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
624-883 1.38e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 189.39  E-value: 1.38e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  624 GREALEKALVIQESERRKKLRFHPRQLYLSVKQGELQKVILMLLDNLDPNFQSDQQSkrTPLHAAAQKGSVEICHVLLQA 703
Cdd:COG0666    32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  704 GANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWT 783
Cdd:COG0666   110 GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDNDGET 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  784 PIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCV 863
Cdd:COG0666   189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268

                         250       260
                  ....*....|....*....|
gi 557440769  864 LLFLSRGANPELRNKEGDTA 883
Cdd:COG0666   269 KLLLLALLLLAAALLDLLTL 288
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 1034-1156 1.37e-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: 145.56  E-value: 1.37e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769   1034 VRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRE--------DDSYLFDLDNKdgevYCIDARYYGNISR 1105
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPkaydtdgaKAFYLFDIDSD----LCIDARRKGNLAR 76

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 557440769   1106 FINHLCDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWD 1156
Cdd:smart00317   77 FINHSCEPNCELLFVEVNGDD----RIVIFALRDIKPGEELTIDYGSDYAN 123
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 1045-1151 1.23e-30

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure.


Pssm-ID: 459965 [Multi-domain]  Cd Length: 115  Bit Score: 116.85  E-value: 1.23e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  1045 GWGVRALQTIPQGTFICEYVGE-LISDAEADVRED-----------DSYLFDLDNKDGevYCIDAR--YYGNISRFINHL 1110
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELlyydklelrlwGPYLFTLDEDSE--YCIDARalYYGNWARFINHS 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 557440769  1111 CDPNIIPVRVFMlhqdLRFPRIAFFSSRDIRTGEELGFDYG 1151
Cdd:pfam00856   79 CDPNCEVRVVYV----NGGPRIVIFALRDIKPGEELTIDYG 115
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
1032-1173 6.48e-29

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 112.75  E-value: 6.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1032 IKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDS-----YLFDLDnkDGEVycIDARYYGNISRF 1106
Cdd:COG2940     4 LHPRIEVRPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKeplhtYLFELD--DDGV--IDGALGGNPARF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557440769 1107 INHLCDPNIIPVRvfmlhqdlRFPRIAFFSSRDIRTGEELGFDYGDRFWDiksKYFTCQCGseKCKH 1173
Cdd:COG2940    80 INHSCDPNCEADE--------EDGRIFIVALRDIAAGEELTYDYGLDYDE---EEYPCRCP--NCRG 133
Ank_2 pfam12796
Ankyrin repeats (3 copies);
718-811 2.79e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 2.79e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769   718 LMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLStgQVDVNAQDSGgWTPIIWAAEHKHIDVI 797
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNG-RTALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 557440769   798 RMLLTRGADVTLTD 811
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 650-872 3.42e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.81  E-value: 3.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  650 LYLSVKQGELQKVILMLLDNLDPNFQSDQQSkrTPLHAAAQKGSV-----EICHVLLQAGANINAVDKQQRTPLMEAVVN 724
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADINSSTKNNS--TPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISK 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  725 --NHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIG--NLEMVSLLLSTGqVDVNAqdsggwtpiiwaaehkhIDVIRML 800
Cdd:PHA03100  117 ksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNkiDLKILKLLIDKG-VDINA-----------------KNRVNYL 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557440769  801 LTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGAN 872
Cdd:PHA03100  179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 712-853 8.35e-09

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: 59.64  E-value: 8.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  712 KQQR---TPLMEAVVNNHLEVARYMVQLGGC-VYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGQVDVNAQDSG----GWT 783
Cdd:cd22192    12 QQKRiseSPLLLAAKENDVQAIKKLLKCPSCdLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSdlyqGET 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  784 PIIWAAEHKHIDVIRMLLTRGADVT--------LTDNEENIC------LHWASFTGSAAIAEVLLNAQCDLHAVNYHGDT 849
Cdd:cd22192    92 ALHIAVVNQNLNLVRELIARGADVVspratgtfFRPGPKNLIyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171


                  ....
gi 557440769  850 PLHI 853
Cdd:cd22192   172 VLHI 175
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 706-882 1.52e-07

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: 55.86  E-value: 1.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769   706 NINAVDKQQRTPLMEAVV-NNHLEVARYMVQLGGCVYSkeedGSTCLHHAAK--IGNLEMVSLLLSTGQVD------VNA 776
Cdd:TIGR00870   44 NINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAV----GDTLLHAISLeyVDAVEAILLHLLAAFRKsgplelAND 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769   777 QDSG----GWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNeENICLHwASFTGSAaiaevllnaqcdlhavnYHGDTPLH 852
Cdd:TIGR00870  120 QYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPARAC-GDFFVK-SQGVDSF-----------------YHGESPLN 180

                          170       180       190
                   ....*....|....*....|....*....|
gi 557440769   853 IAARESYHDCVLLFLSRGANPELRNKEGDT 882
Cdd:TIGR00870  181 AAACLGSPSIVALLSEDPADILTADSLGNT 210
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 781-809 1.22e-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: 1.22e-05
                            10        20
                    ....*....|....*....|....*....
gi 557440769    781 GWTPIIWAAEHKHIDVIRMLLTRGADVTL 809
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03247 PHA03247
large tegument protein UL36; Provisional
 23-201 1.82e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769   23 ALLLEKEPRGAAERVHSSLGDTPQSEETLPKANPDSLEPAGPSSPASVTVTVGDEGADTPVGAASLIGDEPesleGDGGR 102
Cdd:PHA03247 2734 ALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDP----ADPPA 2809

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  103 IVLGHATKSFPSSPSKGGACPSRAKMSMTGAGKSPPSVQSLAMRLLSMPGAQGAATAGPEPSPATTAAQEgQPKVHR-AR 181
Cdd:PHA03247 2810 AVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPA-RPPVRRlAR 2888

                         170       180
                  ....*....|....*....|..
gi 557440769  182 KTMSKP--SNGQPPIPEKRPPE 201
Cdd:PHA03247 2889 PAVSRSteSFALPPDQPERPPQ 2910
 
Name Accession Description Interval E-value
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 944-1182 0e+00

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: 544.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  944 EDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRSC 1023
Cdd:cd10533     1 EDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRNC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1024 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNI 1103
Cdd:cd10533    81 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557440769 1104 SRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQ 1182
Cdd:cd10533   161 SRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQ 239
SET_EHMT cd10543
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 945-1174 8.80e-172

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: 506.11  E-value: 8.80e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  945 DYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRSCK 1024
Cdd:cd10543     2 DFLYVTENCETSPLNIDRNITSLQTCSCRDDCSSDNCVCGRLSVRCWYDKEGRLLPDFNKLDPPLIFECNRACSCWRNCR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1025 NRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNIS 1104
Cdd:cd10543    82 NRVVQNGIRYRLQLFRTRGMGWGVRALQDIPKGTFVCEYIGELISDSEADSREDDSYLFDLDNKDGETYCIDARRYGNIS 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1105 RFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHS 1174
Cdd:cd10543   162 RFINHLCEPNLIPVRVFVEHQDLRFPRIAFFASRDIKAGEELGFDYGEKFWRIKGKYFTCRCGSPKCKYS 231
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 945-1174 5.63e-168

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: 496.38  E-value: 5.63e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  945 DYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRSCK 1024
Cdd:cd10535     2 NYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNCR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1025 NRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNIS 1104
Cdd:cd10535    82 NRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNVS 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1105 RFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHS 1174
Cdd:cd10535   162 RFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 231
SET_SETDB-like cd10538
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
 944-1151 1.63e-95

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: 303.91  E-value: 1.63e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  944 EDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSI-RCWYDKDGRLlQEFNkiEPPLIFECNQACSCWRS 1022
Cdd:cd10538     1 PSFTYIKDNIVGKNVQPFSNIIDSVGCKCKDDCLDSKCACAAESDgIFAYTKNGLL-RLNN--SPPPIFECNSKCSCDDD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1023 CKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR------EDDSYLFDLDN-----KDGE 1091
Cdd:cd10538    78 CKNRVVQRGLQARLQVFRTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRgkiydkSGGSYLFDLDEfsdsdGDGE 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1092 VYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYG 1151
Cdd:cd10538   158 ELCVDATFCGNVSRFINHSCDPNLFPFNVVIDHDDLRYPRIALFATRDILPGEELTFDYG 217
SET_SUV39H cd10542
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 945-1172 1.50e-73

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: 244.51  E-value: 1.50e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  945 DYKYIseNCETSTMNIDRNITHLQHCTCVDDC--SSSNClCGQLS-IRCWYDKDGRLlqefnKIEPPL-IFECNQACSCW 1020
Cdd:cd10542     2 NFQYI--NDYIPGDGVKIPEDFLVGCECTEDChnNNPTC-CPAESgVKFAYDKQGRL-----RLPPGTpIYECNSRCKCG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1021 RSCKNRVVQSGIKVRLQLYRTA-KMGWGVRALQTIPQGTFICEYVGELISDAEADVR------EDDSYLFDLD-NKDGEV 1092
Cdd:cd10542    74 PDCPNRVVQRGRKVPLCIFRTSnGRGWGVKTLEDIKKGTFVMEYVGEIITSEEAERRgkiydaNGRTYLFDLDyNDDDCE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1093 YCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYgDRFWDIKSKYFT--------- 1163
Cdd:cd10542   154 YTVDAAYYGNISHFINHSCDPNLAVYAVWINHLDPRLPRIAFFAKRDIKAGEELTFDY-LMTGTGGSSESTipkpkdvrv 232

                         250
                  ....*....|
gi 557440769 1164 -CQCGSEKCK 1172
Cdd:cd10542   233 pCLCGSKNCR 242
SET_SETDB1 cd10517
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
 921-1172 9.73e-73

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


Pssm-ID: 380915 [Multi-domain]  Cd Length: 288  Bit Score: 243.74  E-value: 9.73e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  921 DVARGYENVPIPCVNGVDGEPcPEDYKYISENCETSTMNIDRNITHLQHCTCVDDCS-SSNCLCGQLSI---RCWYDKD- 995
Cdd:cd10517     8 DISYGKEGVPIPCVNEIDNSS-PPYVEYSKERIPGKGVNINLDPDFLVGCDCTDGCRdKSKCACQQLTIeatAATPGGQi 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  996 --------GRLLQEFnkiePPLIFECNQACSCWRSCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGEL 1067
Cdd:cd10517    87 npsagyqyRRLMEKL----PTGVYECNSRCKCDKRCYNRVVQNGLQVRLQVFKTEKKGWGIRCLDDIPKGSFVCIYAGQI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1068 ISDAEADVRE---DDSYLFDLD------------NKDGEVYC--IDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFP 1130
Cdd:cd10517   163 LTEDEANEEGlqyGDEYFAELDyievveklkegyESDVEEHCyiIDAKSEGNLGRYLNHSCSPNLFVQNVFVDTHDLRFP 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 557440769 1131 RIAFFSSRDIRTGEELGFDYGdrfWDIKSKYFT---CQCGSEKCK 1172
Cdd:cd10517   243 WVAFFASRYIRAGTELTWDYN---YEVGSVPGKvlyCYCGSSNCR 284
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
 416-545 3.15e-63

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: 210.71  E-value: 3.15e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  416 FEELPLCSCRMEAPKIDRISERAGHKCMATESVDGELLGC-NAAILKRETMRPSSRVALMVLCEAHRARMVKHHCCPGCG 494
Cdd:cd20905     1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCsNLPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 557440769  495 YFCTAGTFLECHPDFRVAHRFHKACVSQLNGMVFCPHCGEDAS-EAQEVTIP 545
Cdd:cd20905    81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLP 132
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
 945-1171 1.48e-58

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: 202.14  E-value: 1.48e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  945 DYKYISENCETSTMNIDRNITHLQHCTCVDD-CSSSNCLCgqlsIRCW---YDKDGRLLQEFNKIEPPlIFECNQACSCW 1020
Cdd:cd10544     2 DFQYTPENVPGPGADTDPNEITFPGCDCKTSsCEPETCSC----LRKYgpnYDDDGCLLDFDGKYSGP-VFECNSMCKCS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1021 RSCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR------EDDSYLFDLDN--KDGEV 1092
Cdd:cd10544    77 ESCQNRVVQNGLQFKLQVFKTPKKGWGLRTLEFIPKGRFVCEYAGEVIGFEEARRRtksqtkGDMNYIIVLREhlSSGKV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1093 Y--CIDARYYGNISRFINHLCDPN--IIPVRVfmlhqDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFT----- 1163
Cdd:cd10544   157 LetFVDPTYIGNIGRFLNHSCEPNlfMVPVRV-----DSMVPKLALFAARDIVAGEELSFDYSGEFSNSVESVTLarqde 231

                         250
                  ....*....|....
gi 557440769 1164 ------CQCGSEKC 1171
Cdd:cd10544   232 sksrkpCLCGAENC 245
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
 970-1151 3.42e-56

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: 194.54  E-value: 3.42e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  970 CTCVDDC--SSSNCLCGQL-SIRCWYDKDGRLlqefnkIEP-PLIFECNQACSCWRSCKNRVVQSGIKVRLQLYRTAKMG 1045
Cdd:cd10545    24 CDCKNRCtdGASDCACVKKnGGEIPYNFNGRL------IRAkPAIYECGPLCKCPPSCYNRVTQKGLRYRLEVFKTAERG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1046 WGVRALQTIPQGTFICEYVGELISDAEADVR-EDDSYLFDLDNK------DGEV---------------------YCIDA 1097
Cdd:cd10545    98 WGVRSWDSIPAGSFICEYVGELLDTSEADTRsGNDDYLFDIDNRqtnrgwDGGQrldvgmsdgerssaedeesseFTIDA 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 557440769 1098 RYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYG 1151
Cdd:cd10545   178 GSFGNVARFINHSCSPNLFVQCVLYDHNDLRLPRVMLFAADNIPPLQELTYDYG 231
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
624-883 1.38e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 189.39  E-value: 1.38e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  624 GREALEKALVIQESERRKKLRFHPRQLYLSVKQGELQKVILMLLDNLDPNFQSDQQSkrTPLHAAAQKGSVEICHVLLQA 703
Cdd:COG0666    32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  704 GANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWT 783
Cdd:COG0666   110 GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDNDGET 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  784 PIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCV 863
Cdd:COG0666   189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268

                         250       260
                  ....*....|....*....|
gi 557440769  864 LLFLSRGANPELRNKEGDTA 883
Cdd:COG0666   269 KLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
659-917 4.99e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 182.08  E-value: 4.99e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  659 LQKVILMLLDNLDPNFQSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGG 738
Cdd:COG0666    32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  739 CVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICL 818
Cdd:COG0666   112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  819 HWASFTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDLTPERSDVWFALQ 898
Cdd:COG0666   191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                         250
                  ....*....|....*....
gi 557440769  899 LNRKLRLGVGNRAVRTEKI 917
Cdd:COG0666   271 LLLALLLLAAALLDLLTLL 289
SET_SETDB cd10541
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...
 970-1172 2.98e-49

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


Pssm-ID: 380939 [Multi-domain]  Cd Length: 236  Bit Score: 175.04  E-value: 2.98e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  970 CTCVDDC-SSSNCLCGQLSIR----CWYDKD----GRLLQEFNKIEPPLIFECNQACSCWRS-CKNRVVQSGIKVRLQLY 1039
Cdd:cd10541    18 CDCTDGCrDKSKCACHQLTIQatacTPGGQDnptaGYQYKRLEECLPTGVYECNKLCKCDPNmCQNRLVQHGLQVRLQLF 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1040 RTAKMGWGVRALQTIPQGTFICEYVGELISDAEADvRED----DSYLFDLDNKDGEVYCIDARYYGNISRFINHLCDPNI 1115
Cdd:cd10541    98 KTQNKGWGIRCLDDIAKGTFVCIYAGKILTDDFAD-KEGlemgDEYFANLDHIEESCYIIDAKLEGNLGRYLNHSCSPNL 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 557440769 1116 IPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCK 1172
Cdd:cd10541   177 FVQNVFVDTHDLRFPWVAFFASKRIKAGTELTWDYNYEVGSVEGKELLCCCGSNECR 233
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
663-903 1.72e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 174.76  E-value: 1.72e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  663 ILMLLDNLDPNFQSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYS 742
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  743 KEEDGSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWAS 822
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  823 FTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDLTPERSDVWFALQLNRK 902
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241


                  .
gi 557440769  903 L 903
Cdd:COG0666   242 G 242
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 945-1172 1.91e-48

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: 173.15  E-value: 1.91e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  945 DYKYISENCETSTMNIDRNITHlqhCTCvDDCSSS---NCLCGQLSIRCWYDKDGRLlqefnKIEPPL-IFECNQACSCW 1020
Cdd:cd10525     2 DFVYINEYKVGEGVTLNQVAVG---CEC-QDCLSQpvgGCCPGASKHRFAYNEQGQV-----KVRPGLpIYECNSRCRCG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1021 RSCKNRVVQSGIKVRLQLYRTAK-MGWGVRALQTIPQGTFICEYVGELISDAEADVR------EDDSYLFDLDNKDgEVY 1093
Cdd:cd10525    73 PDCPNRVVQKGIQYDLCIFRTDNgRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRgqiydrQGATYLFDLDYVE-DVY 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1094 CIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDY---------------------GD 1152
Cdd:cd10525   152 TVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIALFATRTIRAGEELTFDYnmqvdpvdaestkmdsnfglaGL 231

                         250       260
                  ....*....|....*....|
gi 557440769 1153 RFWDIKSKYFTCQCGSEKCK 1172
Cdd:cd10525   232 PGSPKKRVRIECKCGVRSCR 251
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 945-1172 2.08e-48

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: 172.77  E-value: 2.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  945 DYKYISENCETSTMNIDRNITHlqHCTCVDdCSSSNCLCGQLSIRCWYDKDGRLlqefnKIEPPL-IFECNQACSCWRSC 1023
Cdd:cd10532     2 DFYYINEYKPAPGINLDNEATV--GCDCSD-CFFGKCCPAEAGVLFAYNEHGQL-----KIPPGTpIYECNSRCKCGPDC 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1024 KNRVVQSGIKVRLQLYRTAK-MGWGVRALQTIPQGTFICEYVGELISDAEADVR------EDDSYLFDLDNKDGEvYCID 1096
Cdd:cd10532    74 PNRVVQKGTQYSLCIFRTSNgRGWGVKTLQKIKKNSFVMEYVGEVITSEEAERRgqfydsKGITYLFDLDYESDE-FTVD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1097 ARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDY-----GDRFWD------IKSKYFT-C 1164
Cdd:cd10532   153 AARYGNVSHFVNHSCDPNLQVFNVFIDNLDTRLPRIALFSTRTIKAGEELTFDYqmkgsGDLSSDsidnspAKKRVRTvC 232


                  ....*...
gi 557440769 1165 QCGSEKCK 1172
Cdd:cd10532   233 KCGAVTCR 240
SET_SUV39H_Clr4-like cd20073
SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 ...
 963-1172 5.22e-46

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


Pssm-ID: 380999 [Multi-domain]  Cd Length: 259  Bit Score: 166.59  E-value: 5.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  963 NITHLQHCTcVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIepplIFECNQACSCWRSCKNRVVQSGIKVRLQLYRTA 1042
Cdd:cd20073    27 SCSKLGGCD-LNNPGSCQCLEDSNEKSFAYDEYGRVRANTGSI----IYECNENCDCGINCPNRVVQRGRKLPLEIFKTK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1043 KMGWGVRALQTIPQGTFICEYVGELISDAEADVRE---DD---SYLFDLDNKDGEV---YCIDARYYGNISRFINHLCDP 1113
Cdd:cd20073   102 HKGWGLRCPRFIKAGTFIGVYLGEVITQSEAEIRGkkyDNvgvTYLFDLDLFEDQVdeyYTVDAQYCGDVTRFINHSCDP 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557440769 1114 NIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDR----------------FWDIKSKyFTCQCGSEKCK 1172
Cdd:cd20073   182 NLAIYSVLRDKSDSKIYDLAFFAIKDIPALEELTFDYSGRnnfdqlgfignrsnskYINLKNK-RPCYCGSANCR 255
SET_SUV39H_DIM5-like cd19473
SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...
 970-1172 5.42e-46

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: 166.72  E-value: 5.42e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  970 CTCVDD--CSSSNCLCGQ-----------LSIRCWY---DKDGRLLQEF-NKIEPplIFECNQACSCWRSCKNRVVQSGI 1032
Cdd:cd19473    26 CECTDDedCMYSGCLCLQdvdpdddrdpgKKKNAYHssgAKKGCLRGHMlNSRLP--IYECHEGCACSDDCPNRVVERGR 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1033 KVRLQLYRTA-KMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDS--------YLFDLDN----------KDGEVY 1093
Cdd:cd19473   104 KVPLQIFRTSdGRGWGVRSTVDIKRGQFVDCYVGEIITPEEAQRRRDAAtiaqrkdvYLFALDKfsdpdsldprLRGDPY 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1094 CIDARYYGNISRFINHLCDPNIipvRVFML---HQDLRFPRIAFFSSRDIRTGEELGFDY--------GDRFWDIKSKYF 1162
Cdd:cd19473   184 EIDGEFMSGPTRFINHSCDPNL---RIFARvgdHADKHIHDLAFFAIKDIPRGTELTFDYvdgvtgldDDAGDEEKEKEM 260

                         250
                  ....*....|.
gi 557440769 1163 T-CQCGSEKCK 1172
Cdd:cd19473   261 TkCLCGSPKCR 271
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
 937-1172 6.47e-44

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


Pssm-ID: 380921 [Multi-domain]  Cd Length: 266  Bit Score: 160.77  E-value: 6.47e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  937 VDGEPCPEDYKYISENCETStmnidrNITHLQHCTCVDDCSS-SNCLCGQLSIR----CWYDKD-GRLLQEFNKIEPPL- 1009
Cdd:cd10523     7 VQLDRNPQDQQQLVDDFDIS------NGAFVDSCDCTDGCIDiLKCACLQLTARafskSESSPSkGGRGYKYKRLQEPIp 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1010 --IFECNQACSCWRS-CKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELIS----------------- 1069
Cdd:cd10523    81 sgLYECNVSCKCNRMlCQNRVVQHGLQVRLQVFKTEKKGWGVRCLDDIDKGTFVCIYAGRVLSrarspteplppklelps 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1070 DAEADVREDDSYLFDLDNKDGEVYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFD 1149
Cdd:cd10523   161 ENEVEVVTSWLILSKKRKLRENVCFLDASKEGNVGRFLNHSCCPNLFVQNVFVDTHDKNFPWVAFFTNRVVKAGTELTWD 240

                         250       260
                  ....*....|....*....|...
gi 557440769 1150 YGDRFWDIKSKYFTCQCGSEKCK 1172
Cdd:cd10523   241 YSYDAGTSPEQEIPCLCGVNKCQ 263
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 1034-1156 1.37e-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: 145.56  E-value: 1.37e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769   1034 VRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRE--------DDSYLFDLDNKdgevYCIDARYYGNISR 1105
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPkaydtdgaKAFYLFDIDSD----LCIDARRKGNLAR 76

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 557440769   1106 FINHLCDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWD 1156
Cdd:smart00317   77 FINHSCEPNCELLFVEVNGDD----RIVIFALRDIKPGEELTIDYGSDYAN 123
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
 1036-1172 3.13e-36

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


Pssm-ID: 380929  Cd Length: 136  Bit Score: 133.53  E-value: 3.13e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1036 LQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED--------DSYLFDLdnKDGEVycIDARYYGNISRFI 1107
Cdd:cd10531     2 LELFRTEKKGWGVKAKEDIQKGEFIIEYVGEVIDKKEFKERLDeyeelgksNFYILSL--SDDVV--IDATRKGNLSRFI 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 557440769 1108 NHLCDPNIIPVRVFMLHQdlrfPRIAFFSSRDIRTGEELGFDYG-DRFWDIKSKyftCQCGSEKCK 1172
Cdd:cd10531    78 NHSCEPNCETQKWIVNGE----YRIGIFALRDIPAGEELTFDYNfVNYNEAKQV---CLCGAQNCR 136
SET_SETD1-like cd10518
SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...
 1024-1172 7.22e-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: 127.33  E-value: 7.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1024 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED--------DSYLFDLDNKdgevYCI 1095
Cdd:cd10518     4 RFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKrydeegggGTYMFRIDED----LVI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1096 DARYYGNISRFINHLCDPN----IIPVRVFMlhqdlrfpRIAFFSSRDIRTGEELGFDYgdRFWDIKSKYFTCQCGSEKC 1171
Cdd:cd10518    80 DATKKGNIARFINHSCDPNcyakIITVDGEK--------HIVIFAKRDIAPGEELTYDY--KFPIEDEEKIPCLCGAPNC 149


                  .
gi 557440769 1172 K 1172
Cdd:cd10518   150 R 150
PreSET smart00468
N-terminal to some SET domains; A Cys-rich putative Zn2+-binding domain that occurs N-terminal ...
 919-1018 1.37e-32

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: 121.75  E-value: 1.37e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769    919 CRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSN-CLCGQLSIRCW-YDKDG 996
Cdd:smart00468    1 CLDISNGKENVPVPLVNEVDEDPPPPDFEYISEYIYGQGVPIDRSPSPLVGCSCSGDCSSSNkCECARKNGGEFaYELNG 80

                            90       100
                    ....*....|....*....|..
gi 557440769    997 RllqeFNKIEPPLIFECNQACS 1018
Cdd:smart00468   81 G----LRLKRKPLIYECNSRCS 98
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
 1036-1172 4.74e-32

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


Pssm-ID: 380951 [Multi-domain]  Cd Length: 141  Bit Score: 122.02  E-value: 4.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1036 LQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNkdgevYC--------IDARYYGNISRFI 1107
Cdd:cd19174     2 LERFRTEDKGWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRMIEQYHNHSHH-----YClnldsgmvIDGYRMGNEARFV 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557440769 1108 NHLCDPNIIPVRVFMLHQdlrfPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYfTCQCGSEKCK 1172
Cdd:cd19174    77 NHSCDPNCEMQKWSVNGV----YRIGLFALKDIPAGEELTYDYNFHSFNVEKQQ-PCKCGSPNCR 136
SET_EZH cd10519
SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...
 1035-1152 1.61e-31

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: 119.66  E-value: 1.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1035 RLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRE---DD---SYLFDLDNKdgevYCIDARYYGNISRFIN 1108
Cdd:cd10519     2 RLLLGKSDVAGWGLFLKEPIKKDEFIGEYTGELISQDEADRRGkiyDKynsSYLFNLNDQ----FVVDATRKGNKIRFAN 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 557440769 1109 HLCDPNIIPvRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDYGD 1152
Cdd:cd10519    78 HSSNPNCYA-KVMMVNGD---HRIGIFAKRDIEAGEELFFDYGY 117
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 1045-1151 1.23e-30

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure.


Pssm-ID: 459965 [Multi-domain]  Cd Length: 115  Bit Score: 116.85  E-value: 1.23e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  1045 GWGVRALQTIPQGTFICEYVGE-LISDAEADVRED-----------DSYLFDLDNKDGevYCIDAR--YYGNISRFINHL 1110
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELlyydklelrlwGPYLFTLDEDSE--YCIDARalYYGNWARFINHS 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 557440769  1111 CDPNIIPVRVFMlhqdLRFPRIAFFSSRDIRTGEELGFDYG 1151
Cdd:pfam00856   79 CDPNCEVRVVYV----NGGPRIVIFALRDIKPGEELTIDYG 115
SET_SETD2 cd19172
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...
 1035-1172 2.20e-30

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: 117.30  E-value: 2.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1035 RLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAE--------ADVREDDSYLFDLDNKDgevyCIDARYYGNISRF 1106
Cdd:cd19172     3 KVEVFRTEKKGWGLRAAEDLPKGTFVIEYVGEVLDEKEfkrrmkeyAREGNRHYYFMALKSDE----IIDATKKGNLSRF 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557440769 1107 INHLCDPNIIpVRVFMLHQDLrfpRIAFFSSRDIRTGEELGFDYG-DRFWDIKSKyftCQCGSEKCK 1172
Cdd:cd19172    79 INHSCEPNCE-TQKWTVNGEL---RVGFFAKRDIPAGEELTFDYQfERYGKEAQK---CYCGSPNCR 138
Pre-SET pfam05033
Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines ...
 922-1026 2.01e-29

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


Pssm-ID: 461530 [Multi-domain]  Cd Length: 99  Bit Score: 112.90  E-value: 2.01e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769   922 VARGYENVPIPCVNGVDGEPCPEDYKYISENCETSTMNIDRnithLQHCTCvDDCSSSNCLCGQLS---IRCWYDKDGRL 998
Cdd:pfam05033    1 ISKGKENVPIPVVNEVDDEPPPPDFTYITSYIYPKEFLLII----PQGCDC-GDCSSEKCSCAQLNggeFRFPYDKDGLL 75

                           90       100
                   ....*....|....*....|....*...
gi 557440769   999 LQEfnkiEPPLIFECNQACSCWRSCKNR 1026
Cdd:pfam05033   76 VPE----SKPPIYECNPLCGCPPSCPNR 99
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
1032-1173 6.48e-29

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 112.75  E-value: 6.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1032 IKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDS-----YLFDLDnkDGEVycIDARYYGNISRF 1106
Cdd:COG2940     4 LHPRIEVRPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKeplhtYLFELD--DDGV--IDGALGGNPARF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557440769 1107 INHLCDPNIIPVRvfmlhqdlRFPRIAFFSSRDIRTGEELGFDYGDRFWDiksKYFTCQCGseKCKH 1173
Cdd:COG2940    80 INHSCDPNCEADE--------EDGRIFIVALRDIAAGEELTYDYGLDYDE---EEYPCRCP--NCRG 133
SET_NSD cd19173
SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...
 1034-1171 1.02e-25

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


Pssm-ID: 380950 [Multi-domain]  Cd Length: 142  Bit Score: 103.93  E-value: 1.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1034 VRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR------EDDS--YLFDLDNKdgevYCIDARYYGNISR 1105
Cdd:cd19173     2 PPTEPFKTGDRGWGLRTKRDIKKGDFVIEYVGELIDEEECRRRlkkaheNNITnfYMLTLDKD----RIIDAGPKGNLSR 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557440769 1106 FINHLCDPNiIPVRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDYG-DRFWDIKSKyftCQCGSEKC 1171
Cdd:cd19173    78 FMNHSCQPN-CETQKWTVNGD---TRVGLFAVRDIPAGEELTFNYNlDCLGNEKKV---CRCGAPNC 137
SET_ASHR3-like cd19175
SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...
 1035-1172 2.47e-25

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


Pssm-ID: 380952 [Multi-domain]  Cd Length: 139  Bit Score: 102.88  E-value: 2.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1035 RLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR--------EDDSYLFDLDnKDgevYCIDARYYGNISRF 1106
Cdd:cd19175     1 KMKLVKTEKCGWGLVADEDINAGEFIIEYVGEVIDDKTCEERlwdmkhkgEKNFYMCEID-KD---MVIDATFKGNLSRF 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 557440769 1107 INHLCDPNIIpVRVFMLHQDLrfpRIAFFSSRDIRTGEELGFDYgdRFWDIKSKYfTCQCGSEKCK 1172
Cdd:cd19175    77 INHSCDPNCE-LQKWQVDGET---RIGVFAIRDIKKGEELTYDY--QFVQFGADQ-DCHCGSKNCR 135
SET_SET1 cd20072
SET domain (including post-SET domain) found in catalytic component of the Saccharomyces ...
 1033-1172 6.65e-25

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: 101.73  E-value: 6.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1033 KVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED--------DSYLFDLDnkdgEVYCIDARYYGNIS 1104
Cdd:cd20072    12 KKQLKFARSAIHNWGLYAMENISAKDMVIEYVGEVIRQQVADEREKrylrqgigSSYLFRID----DDTVVDATKKGNIA 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557440769 1105 RFINHLCDPNIIpVRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDYgdRFwDIKSKYFTCQCGSEKCK 1172
Cdd:cd20072    88 RFINHCCDPNCT-AKIIKVEGE---KRIVIYAKRDIAAGEELTYDY--KF-PREEDKIPCLCGAPNCR 148
SET_SETD8 cd10528
SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2. ...
 1026-1153 2.38e-24

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


Pssm-ID: 380926 [Multi-domain]  Cd Length: 141  Bit Score: 99.96  E-value: 2.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1026 RVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRE--------DDSYLFDLDNKdGEVYCIDA 1097
Cdd:cd10528     9 ELILSGKEEGLKVIEIDGKGRGVIATRPFEKGDFVVEYHGDLITITEAKKREalyakdpsTGCYMYYFQYK-GKTYCVDA 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 557440769 1098 -RYYGNISRFINHLC-DPNIIPVRVFMlhQDLrfPRIAFFSSRDIRTGEELGFDYGDR 1153
Cdd:cd10528    88 tKESGRLGRLINHSKkKPNLKTKLLVI--DGV--PHLILVAKRDIKPGEELLYDYGDR 141
SET_EZH-like cd19168
SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb ...
 1045-1154 6.32e-24

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: 98.03  E-value: 6.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1045 GWGVRALQTIPQGTFICEYVGELISDAEADVRE------DDSYLFDLDNKdgevYCIDARYYGNISRFINHLCDP----N 1114
Cdd:cd19168    13 GLGLFAAEDIKEGEFVIEYTGELISHDEGVRREhrrgdvSYLYLFEEQEG----IWVDAAIYGNLSRYINHATDKvktgN 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 557440769 1115 IIPVRVFMLHQdlrfPRIAFFSSRDIRTGEELGFDYGDRF 1154
Cdd:cd19168    89 CMPKIMYVNHE----WRIKFTAIKDIKIGEELFFNYGDNF 124
SET_SETD1 cd19169
SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...
 1033-1172 1.29e-23

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


Pssm-ID: 380946  Cd Length: 148  Bit Score: 98.18  E-value: 1.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1033 KVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED--------DSYLFDLDnkdgEVYCIDARYYGNIS 1104
Cdd:cd19169    12 KKQLKFAKSRIHDWGLFALEPIAADEMVIEYVGQVIRQSVADEREKryeaigigSSYLFRVD----DDTIIDATKCGNLA 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557440769 1105 RFINHLCDPN----IIPVRvfmlhqdlRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKskyFTCQCGSEKCK 1172
Cdd:cd19169    88 RFINHSCNPNcyakIITVE--------SQKKIVIYSKRPIAVNEEITYDYKFPIEDEK---IPCLCGAPQCR 148
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
 1045-1156 1.76e-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: 96.64  E-value: 1.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1045 GWGVRALQTIPQGTFICEYVGELISDAEADVR----EDDSYLFDLDnkDGEVYcIDARYYGNISRFINHLCDPNIIPVrv 1120
Cdd:cd10522    14 GLGLFAAETIAKGEFVGEYTGEVLDRWEEDRDsvyhYDPLYPFDLN--GDILV-IDAGKKGNLTRFINHSDQPNLELI-- 88

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 557440769 1121 FMLHQDLrfPRIAFFSSRDIRTGEELGFDYGDRFWD 1156
Cdd:cd10522    89 VRTLKGE--QHIGFVAIRDIKPGEELFISYGPKYWK 122
Ank_2 pfam12796
Ankyrin repeats (3 copies);
718-811 2.79e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 2.79e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769   718 LMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLStgQVDVNAQDSGgWTPIIWAAEHKHIDVI 797
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNG-RTALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 557440769   798 RMLLTRGADVTLTD 811
Cdd:pfam12796   78 KLLLEKGADINVKD 91
SET_KMT2A_2B cd19170
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...
 1026-1172 1.29e-21

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


Pssm-ID: 380947 [Multi-domain]  Cd Length: 152  Bit Score: 92.45  E-value: 1.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1026 RVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED--DS-----YLFDLDnkdgEVYCIDAR 1098
Cdd:cd19170     6 RHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKyyESkgigcYMFRID----DDEVVDAT 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557440769 1099 YYGNISRFINHLCDPN----IIPVrvfmlhqDLRfPRIAFFSSRDIRTGEELGFDYGDRFWDIKskyFTCQCGSEKCK 1172
Cdd:cd19170    82 MHGNAARFINHSCEPNcysrVVNI-------DGK-KHIVIFALRRILRGEELTYDYKFPIEDVK---IPCTCGSKKCR 148
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 650-872 3.42e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.81  E-value: 3.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  650 LYLSVKQGELQKVILMLLDNLDPNFQSDQQSkrTPLHAAAQKGSV-----EICHVLLQAGANINAVDKQQRTPLMEAVVN 724
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADINSSTKNNS--TPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISK 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  725 --NHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIG--NLEMVSLLLSTGqVDVNAqdsggwtpiiwaaehkhIDVIRML 800
Cdd:PHA03100  117 ksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNkiDLKILKLLIDKG-VDINA-----------------KNRVNYL 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557440769  801 LTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGAN 872
Cdd:PHA03100  179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
685-778 1.96e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 1.96e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769   685 LHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQlgGCVYSKEEDGSTCLHHAAKIGNLEMVS 764
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|....
gi 557440769   765 LLLSTGqVDVNAQD 778
Cdd:pfam12796   79 LLLEKG-ADINVKD 91
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
 1033-1172 2.36e-19

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: 85.94  E-value: 2.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1033 KVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDS-------YLFDLDNKdgevYCIDARYYGNISR 1105
Cdd:cd19171    13 RSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYesqnrgiYMFRIDND----WVIDATMTGGPAR 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557440769 1106 FINHLCDPNIIpVRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKyFTCQCGSEKCK 1172
Cdd:cd19171    89 YINHSCNPNCV-AEVVTFDKE---KKIIIISNRRIAKGEELTYDYKFDFEDDQHK-IPCLCGAPNCR 150
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 658-882 5.13e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 91.27  E-value: 5.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  658 ELQKVILMLLDNLDPNFQSdqqsKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNH-----LEVARY 732
Cdd:PHA03100   16 KNIKYIIMEDDLNDYSYKK----PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  733 MVQLGGCVYSKEEDGSTCLHHAA--KIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHID--VIRMLLTRGADVT 808
Cdd:PHA03100   92 LLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDIN 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557440769  809 LTDNeeniclhwasftgsaaiAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDT 882
Cdd:PHA03100  171 AKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
SET_NSD2 cd19211
SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...
 1037-1171 1.72e-18

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: 83.12  E-value: 1.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1037 QLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR-----EDDS---YLFDLDnKDgevYCIDARYYGNISRFIN 1108
Cdd:cd19211     5 KIIKTEGKGWGLIAKRDIKKGEFVNEYVGELIDEEECMARikhahENDIthfYMLTID-KD---RIIDAGPKGNYSRFMN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557440769 1109 HLCDPNiIPVRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDYG-DRFWDIKSkyfTCQCGSEKC 1171
Cdd:cd19211    81 HSCQPN-CETQKWTVNGD---TRVGLFAVCDIPAGTELTFNYNlDCLGNEKT---VCRCGAPNC 137
SET_SETD5-like cd10529
SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...
 1047-1150 5.11e-18

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: 81.17  E-value: 5.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1047 GVRALQTIPQGTFICEYVGE--LISDAEADVRED---DSYLFDLDNKDGEVYCIDARYYGNISRFINHLCDPNiipVRV- 1120
Cdd:cd10529    18 GLVATEDISPGEPILEYKGEvsLRSEFKEDNGFFkrpSPFVFFYDGFEGLPLCVDARKYGNEARFIRRSCRPN---AELr 94

                          90       100       110
                  ....*....|....*....|....*....|..
gi 557440769 1121 FMLHQDLRFpRIAFFSSRDIRTGEE--LGFDY 1150
Cdd:cd10529    95 HVVVSNGEL-RLFIFALKDIRKGTEitIPFDY 125
SET_EZH2 cd19218
SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...
 1031-1150 9.62e-18

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: 80.34  E-value: 9.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1031 GIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDD------SYLFDLDNKdgevYCIDARYYGNIS 1104
Cdd:cd19218     1 GSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVydkymcSFLFNLNND----FVVDATRKGNKI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 557440769 1105 RFINHLCDPNIIpVRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDY 1150
Cdd:cd19218    77 RFANHSVNPNCY-AKVMMVNGD---HRIGIFAKRAIQTGEELFFDY 118
SET_EZH1 cd19217
SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43) ...
 1029-1150 2.02e-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: 80.11  E-value: 2.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1029 QSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED------DSYLFDLDNKdgevYCIDARYYGN 1102
Cdd:cd19217     1 QRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKvydkymSSFLFNLNND----FVVDATRKGN 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 557440769 1103 ISRFINHLCDPNIIpVRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDY 1150
Cdd:cd19217    77 KIRFANHSVNPNCY-AKVVMVNGD---HRIGIFAKRAIQQGEELFFDY 120
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
 1036-1171 2.05e-17

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


Pssm-ID: 380987 [Multi-domain]  Cd Length: 142  Bit Score: 79.97  E-value: 2.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1036 LQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR-----EDD---SYLFDLDnKDgevYCIDARYYGNISRFI 1107
Cdd:cd19210     4 VEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIDEEECRARiryaqEHDitnFYMLTLD-KD---RIIDAGPKGNYARFM 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557440769 1108 NHLCDPNiIPVRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDYgdRFWDIKSKYFTCQCGSEKC 1171
Cdd:cd19210    80 NHCCQPN-CETQKWTVNGD---TRVGLFALCDIKAGTELTFNY--NLECLGNGKTVCKCGAPNC 137
SET_KMT2A cd19206
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...
 1038-1172 3.78e-17

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


Pssm-ID: 380983 [Multi-domain]  Cd Length: 154  Bit Score: 79.68  E-value: 3.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1038 LYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRE---DDS----YLFDLDnkDGEVycIDARYYGNISRFINHL 1110
Cdd:cd19206    18 VYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREkyyDSKgigcYMFRID--DSEV--VDATMHGNAARFINHS 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557440769 1111 CDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWDIKSKyFTCQCGSEKCK 1172
Cdd:cd19206    94 CEPNCYSRVINIDGQK----HIVIFAMRKIYRGEELTYDYKFPIEDASNK-LPCNCGAKKCR 150
SET_NSD3 cd19212
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
 1037-1171 5.26e-17

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: 78.81  E-value: 5.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1037 QLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDN-------KDgevYCIDARYYGNISRFINH 1109
Cdd:cd19212     5 EIIKTERRGWGLRTKRSIKKGEFVNEYVGELIDEEECRLRIKRAHENSVTNfymltvtKD---RIIDAGPKGNYSRFMNH 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557440769 1110 LCDPNiIPVRVFMLHQDLrfpRIAFFSSRDIRTGEELGFDYG-DRFWDIKSKyftCQCGSEKC 1171
Cdd:cd19212    82 SCNPN-CETQKWTVNGDV---RVGLFALCDIPAGMELTFNYNlDCLGNGRTE---CHCGADNC 137
Ank_2 pfam12796
Ankyrin repeats (3 copies);
785-877 6.06e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 6.06e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769   785 IIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNaQCDLHAVNYhGDTPLHIAARESYHDCVL 864
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 557440769   865 LFLSRGANPELRN 877
Cdd:pfam12796   79 LLLEKGADINVKD 91
SET_SETD1A cd19204
SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...
 1033-1172 8.76e-17

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


Pssm-ID: 380981 [Multi-domain]  Cd Length: 153  Bit Score: 78.91  E-value: 8.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1033 KVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED--------DSYLFDLDNKDgevyCIDARYYGNIS 1104
Cdd:cd19204    13 KKKLRFGRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQVVADMREKryvqegigSSYLFRVDHDT----IIDATKCGNLA 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557440769 1105 RFINHLCDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGdrfWDIKSKYFTCQCGSEKCK 1172
Cdd:cd19204    89 RFINHCCTPNCYAKVITIESQK----KIVIYSKQPIGVNEEITYDYK---FPIEDNKIPCLCGTENCR 149
PHA03095 PHA03095
ankyrin-like protein; Provisional
 682-875 4.77e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 82.38  E-value: 4.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  682 RTPLHA-----AAQKGSVEIchvLLQAGANINAVDKQQRTPLMEAVVNNH--LEVARYMVQLGGCVYSKEEDGSTCLHHA 754
Cdd:PHA03095  118 RTPLHVylsgfNINPKVIRL---LLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHHH 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  755 A---KIGNlEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEH---KHIdVIRMLLTRGADVTLTDNEENICLHWASFTGSAA 828
Cdd:PHA03095  195 LqsfKPRA-RIVRELIRAG-CDPAATDMLGNTPLHSMATGsscKRS-LVLPLLIAGISINARNRYGQTPLHYAAVFNNPR 271

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 557440769  829 IAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPEL 875
Cdd:PHA03095  272 ACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAET 318
PHA03095 PHA03095
ankyrin-like protein; Provisional
 647-883 5.26e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 82.38  E-value: 5.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  647 PRQLYLSVKQGELQKVILMLLDN-LDPNFQSdqQSKRTPLHAAAQKGSVE-ICHVLLQAGANINAVDKQQRTPLME--AV 722
Cdd:PHA03095   50 PLHLYLHYSSEKVKDIVRLLLEAgADVNAPE--RCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVylSG 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  723 VNNHLEVARYMVQLGGCVYSKEEDGSTCLH-----HAAkigNLEMVSLLLSTGqVDVNAQDSGGWTPIiwaaeHKHID-- 795
Cdd:PHA03095  128 FNINPKVIRLLLRKGADVNALDLYGMTPLAvllksRNA---NVELLRLLIDAG-ADVYAVDDRFRSLL-----HHHLQsf 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  796 -----VIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEV--LLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLS 868
Cdd:PHA03095  199 kprarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIA 278

                         250
                  ....*....|....*
gi 557440769  869 RGANPELRNKEGDTA 883
Cdd:PHA03095  279 LGADINAVSSDGNTP 293
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 654-883 1.41e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 81.65  E-value: 1.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  654 VKQGELQKVILMLLDNLDPNfqSDQQSKRTPLHAAAQKGSVEICHVLLQAGANIN------------AVD---------- 711
Cdd:PHA02876  153 IQQDELLIAEMLLEGGADVN--AKDIYCITPIHYAAERGNAKMVNLLLSYGADVNiialddlsvlecAVDsknidtikai 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  712 -------KQQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNL-EMVSLLLSTGqVDVNAQDSGGWT 783
Cdd:PHA02876  231 idnrsniNKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERG-ADVNAKNIKGET 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  784 PIIWAAEHKH-IDVIRMLLTRGADVTLTDNEENICLHWAS-FTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHD 861
Cdd:PHA02876  310 PLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVV 389

                         250       260
                  ....*....|....*....|..
gi 557440769  862 CVLLFLSRGANPELRNKEGDTA 883
Cdd:PHA02876  390 IINTLLDYGADIEALSQKIGTA 411
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 683-882 3.25e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.62  E-value: 3.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  683 TPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGgcvyskeEDGST----CLhhaakig 758
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG-------VDTSIlpipCI------- 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  759 NLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNAQC 838
Cdd:PHA02874  103 EKDMIKTILDCG-IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 557440769  839 DLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDT 882
Cdd:PHA02874  182 YANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFT 225
SET_KMT2C cd19208
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) ...
 1021-1172 3.29e-15

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


Pssm-ID: 380985 [Multi-domain]  Cd Length: 154  Bit Score: 74.28  E-value: 3.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1021 RSCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED-------DSYLFDLDNKdgevY 1093
Cdd:cd19208     2 KSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKlyesqnrGVYMFRIDND----H 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557440769 1094 CIDARYYGNISRFINHLCDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWDIKSKyFTCQCGSEKCK 1172
Cdd:cd19208    78 VIDATLTGGPARYINHSCAPNCVAEVVTFEKGH----KIIISSSRRIQKGEELCYDYKFDFEDDQHK-IPCHCGAVNCR 151
SET_SETD1B cd19205
SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...
 1033-1172 3.63e-15

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: 73.94  E-value: 3.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1033 KVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED--------DSYLFDLDNKDgevyCIDARYYGNIS 1104
Cdd:cd19205    13 KKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKryedegigSSYMFRVDHDT----IIDATKCGNFA 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557440769 1105 RFINHLCDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGdrfWDIKSKYFTCQCGSEKCK 1172
Cdd:cd19205    89 RFINHSCNPNCYAKVITVESQK----KIVIYSKQHINVNEEITYDYK---FPIEDVKIPCLCGSENCR 149
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 682-808 9.59e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 79.14  E-value: 9.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  682 RTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCvySKEEDGSTCLHHAAKIGNLE 761
Cdd:PLN03192  559 RTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASI--SDPHAAGDLLCTAAKRNDLT 636

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 557440769  762 MVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIDVIRMLLTRGADVT 808
Cdd:PLN03192  637 AMKELLKQG-LNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVD 682
SET_KMT2D cd19209
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...
 1021-1172 1.64e-14

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: 72.42  E-value: 1.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1021 RSCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED-------DSYLFDLDNKdgevY 1093
Cdd:cd19209     3 KSSQYRRLKTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKiyeeqnrGIYMFRINNE----H 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557440769 1094 CIDARYYGNISRFINHLCDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWDIKSKyFTCQCGSEKCK 1172
Cdd:cd19209    79 VIDATLTGGPARYINHSCAPNCVAEVVTFDKED----KIIIISSRRIPKGEELTYDYQFDFEDDQHK-IPCHCGAWNCR 152
SET_SpSET3-like cd19183
SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...
 1036-1195 1.92e-14

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


Pssm-ID: 380960  Cd Length: 173  Bit Score: 72.44  E-value: 1.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1036 LQLYRTAKMGW-GVRALQTIPQGTFICEYVGELISDAEADVREDDSY----------LFDldnkDGEVYCIDARYYGNIS 1104
Cdd:cd19183     3 ISSIGLANASRfGLFADRPIPAGDPIQELLGEIGLQSEYIADPENQYqilgapkphvFFH----PQSPLYIDTRRSGSVA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1105 RFINHLCDPN--IIPVRVfmlhQDLRFPRIAFFSSRDIRTGEELGFDYGdrfWDIkskyftcqcgsekcKHSAEAIALEQ 1182
Cdd:cd19183    79 RFIRRSCRPNaeLVTVAS----DSGSVLKFVLYASRDISPGEEITIGWD---WDN--------------PHPFRRFALGE 137

                         170
                  ....*....|...
gi 557440769 1183 SRLARLDPHPELL 1195
Cdd:cd19183   138 LVPSNLDLEQHLL 150
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 1035-1151 2.99e-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: 68.82  E-value: 2.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1035 RLQLYRTAKMGWGVRALQTIPQGTFICeyvgelisdaeadvreddsylfdldnkdgevycidaryygnISRFINHLCDPN 1114
Cdd:cd08161     1 EIRPSTIPGAGFGLFATRDIPKGEVIG-----------------------------------------LARFINHSCEPN 39

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 557440769 1115 IIPVRVFmlhqDLRFPRIAFFSSRDIRTGEELGFDYG 1151
Cdd:cd08161    40 CEFEEVY----VGGKPRVFIVALRDIKAGEELTVDYG 72
SET_KMT2B cd19207
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...
 1038-1172 3.67e-14

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


Pssm-ID: 380984 [Multi-domain]  Cd Length: 154  Bit Score: 71.21  E-value: 3.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1038 LYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED-------DSYLFDLDNKDgevyCIDARYYGNISRFINHL 1110
Cdd:cd19207    18 VYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKfydskgiGCYMFRIDDFD----VVDATMHGNAARFINHS 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557440769 1111 CDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWDIKSKyFTCQCGSEKCK 1172
Cdd:cd19207    94 CEPNCYSRVIHVEGQK----HIVIFALRKIYRGEELTYDYKFPIEDASNK-LPCNCGAKRCR 150
Ank_2 pfam12796
Ankyrin repeats (3 copies);
650-737 5.17e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 5.17e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769   650 LYLSVKQGELQKVILMLLDNLDPNFQSdqQSKRTPLHAAAQKGSVEICHVLLQaGANINAVDkQQRTPLMEAVVNNHLEV 729
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQD--KNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEI 76


                   ....*...
gi 557440769   730 ARYMVQLG 737
Cdd:pfam12796   77 VKLLLEKG 84
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 637-880 6.40e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 75.69  E-value: 6.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  637 SERRKKLRFHPRQLYLSvkqgelqKVILmlLDNLDPNFQSDQQSKRTPLHAAAQKgsVEICHVLLQAGANINAVDKQQ-R 715
Cdd:PHA02878  101 TLVAIKDAFNNRNVEIF-------KIIL--TNRYKNIQTIDLVYIDKKSKDDIIE--AEITKLLLSYGADINMKDRHKgN 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  716 TPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGQvDVNAQDSGGWTPIIWAAEH-KHI 794
Cdd:PHA02878  170 TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA-STDARDKCGNTPLHISVGYcKDY 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  795 DVIRMLLTRGADVTLTDNEENIC-LHWAsfTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESY----------HDCV 863
Cdd:PHA02878  249 DILKLLLEHGVDVNAKSYILGLTaLHSS--IKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLcinigrilisNICL 326

                         250
                  ....*....|....*..
gi 557440769  864 LLFLsrgaNPELRNKEG 880
Cdd:PHA02878  327 LKRI----KPDIKNSEG 339
PHA03095 PHA03095
ankyrin-like protein; Provisional
 693-883 7.19e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.45  E-value: 7.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  693 SVEICHVLLQAGANINAVDKQQRTPL---MEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGN-LEMVSLLLS 768
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIK 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  769 TGqVDVNAQDSGGWTPIiwaaeHKHI-------DVIRMLLTRGADVTLTDNEENICLH-WASFTG-SAAIAEVLLNAQCD 839
Cdd:PHA03095  106 AG-ADVNAKDKVGRTPL-----HVYLsgfninpKVIRLLLRKGADVNALDLYGMTPLAvLLKSRNaNVELLRLLIDAGAD 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 557440769  840 LHAVNYHGDTPLHIAAR--ESYHDCVLLFLSRGANPELRNKEGDTA 883
Cdd:PHA03095  180 VYAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTP 225
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 650-813 1.52e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 74.23  E-value: 1.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  650 LYLSVKQGELQKVILMLLDNLDPNFQSDQQSkrTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEV 729
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGC--YPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  730 ARYMVQLGGCVYSKEEDGSTCLHHAAkIGNLEMVSLLLSTGQvdVNAQDSGGWTPIIWAAEHK-HIDVIRMLLTRGADVT 808
Cdd:PHA02874  206 IKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLINNAS--INDQDIDGSTPLHHAINPPcDIDIIDILLYHKADIS 282


                  ....*
gi 557440769  809 LTDNE 813
Cdd:PHA02874  283 IKDNK 287
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 681-872 4.47e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.56  E-value: 4.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  681 KRTPLHAAAQKGSV-EICHVLLQAGANINAVDKQQRTPLMEAVVNNH-LEVARYMVQLGGCVYSKEEDGSTCLHHAAKIG 758
Cdd:PHA02876  273 KNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLD 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  759 -NLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWASF-TGSAAIAEVLLNA 836
Cdd:PHA02876  353 rNKDIVITLLELG-ANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCgTNPYMSVKTLIDR 431

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 557440769  837 QCDLHAVNYHGDTPLHIAARESYH-DCVLLFLSRGAN 872
Cdd:PHA02876  432 GANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGAD 468
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 649-834 7.97e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 68.86  E-value: 7.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  649 QLYLSVKQGELQKVILMLLDNldpNFQSDQQSKR--TPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNH 726
Cdd:PHA02875   71 ELHDAVEEGDVKAVEELLDLG---KFADDVFYKDgmTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGD 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  727 LEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGQVDVNAQDSGGWTPIIWAAEHKHIDVIRMLLTRGAD 806
Cdd:PHA02875  148 IKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 557440769  807 ---VTLTDNEE--------NICLHWASFTGSAAIAEVLL 834
Cdd:PHA02875  228 cniMFMIEGEEctildmicNMCTNLESEAIDALIADIAI 266
Ank_4 pfam13637
Ankyrin repeats (many copies);
682-734 1.77e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 1.77e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 557440769   682 RTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMV 734
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
747-801 1.88e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 1.88e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 557440769   747 GSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIDVIRMLL 801
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 724-875 2.20e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.74  E-value: 2.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  724 NNHLEVARYMVQLGGCVYSKEEDGSTCLH---HAAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKH-IDVIRM 799
Cdd:PHA03095   24 NVTVEEVRRLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAG-ADVNAPERCGFTPLHLYLYNATtLDVIKL 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557440769  800 LLTRGADVTLTDNEENICLH--WASFTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIaaresyhdcvlLFLSRGANPEL 875
Cdd:PHA03095  103 LIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAV-----------LLKSRNANVEL 169
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 682-883 3.89e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.55  E-value: 3.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  682 RTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLE 761
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  762 MVSLLLSTGQV--DVNAQDsgGWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNAQCD 839
Cdd:PHA02875   83 AVEELLDLGKFadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 557440769  840 LHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTA 883
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVA 204
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 677-880 1.06e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 65.37  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  677 DQQSKrTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAK 756
Cdd:PHA02874  121 DAELK-TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  757 IGNLEMVSLLLSTGQvDVNAQDSGGWTPIIWAAEHKHIDVirMLLTRGADVTLTDNEENICLHWA-SFTGSAAIAEVLLN 835
Cdd:PHA02874  200 YGDYACIKLLIDHGN-HIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAiNPPCDIDIIDILLY 276

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 557440769  836 AQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSrgANPELRNKEG 880
Cdd:PHA02874  277 HKADISIKDNKGENPIDTAFKYINKDPVIKDII--ANAVLIKEAD 319
Ank_4 pfam13637
Ankyrin repeats (many copies);
714-767 2.71e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.90  E-value: 2.71e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 557440769   714 QRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLL 767
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
761-883 5.37e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.89  E-value: 5.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  761 EMVSLLLSTGQVDVNAQDSGGWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNAQCDL 840
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 557440769  841 HAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTA 883
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 695-872 7.18e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.16  E-value: 7.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  695 EIC-HVLLQA--GANI--NAVDK--QQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLL 767
Cdd:PHA02876  119 EACiHILKEAisGNDIhyDKINEsiEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLL 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  768 STGqVDVNAQDSGGWTPIIWAAEHKHIDVIR-----------------------------MLLTRGADVTLTDNEENICL 818
Cdd:PHA02876  199 SYG-ADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsninkndlsllkairnedletslLLYDAGFSVNSIDDCKNTPL 277

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 557440769  819 HWASFTGS-AAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYH-DCVLLFLSRGAN 872
Cdd:PHA02876  278 HHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGAD 333
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 661-807 7.23e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 62.76  E-value: 7.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  661 KVILMLLDN-LDPNFQSDQQSkrTPLHAAAQK--GSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNH--LEVAR---- 731
Cdd:PHA03100   87 EIVKLLLEYgANVNAPDNNGI--TPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKllid 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  732 ------------YMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIDVIRM 799
Cdd:PHA03100  165 kgvdinaknrvnYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLG-ANPNLVNKYGDTPLHIAILNNNKEIFKL 243


                  ....*...
gi 557440769  800 LLTRGADV 807
Cdd:PHA03100  244 LLNNGPSI 251
PHA02798 PHA02798
ankyrin-like protein; Provisional
 693-814 8.20e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 62.93  E-value: 8.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  693 SVEICHVLLQAGANINAVDKQQRTPLMEAVVN----NH-LEVARYMVQLGGCVYSKEEDGST---CLHHAAKIGNLEMVS 764
Cdd:PHA02798   50 STDIVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHmLDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILL 129

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 557440769  765 LLLSTGqVDVNAQDSGGWTPI---IWAAEHKHIDVIRMLLTRGADVTLTDNEE 814
Cdd:PHA02798  130 FMIENG-ADTTLLDKDGFTMLqvyLQSNHHIDIEIIKLLLEKGVDINTHNNKE 181
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 723-872 1.28e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.99  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  723 VNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHI-----DVI 797
Cdd:PHA03100   11 RIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNG-ADINSSTKNNSTPLHYLSNIKYNltdvkEIV 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557440769  798 RMLLTRGADVTLTDNEENICLHWASFT--GSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHD--CVLLFLSRGAN 872
Cdd:PHA03100   90 KLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVD 168
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 646-770 1.75e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.60  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  646 HPRQLYLSVKQGELqKVILMLLDNlDPNFQSDQQSKRTPLHAAAQ--KGSVEICHVLLQAGANINA-------------- 709
Cdd:PHA03100  108 TPLLYAISKKSNSY-SIVEYLLDN-GANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKGVDINAknrvnyllsygvpi 185

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557440769  710 --VDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTG 770
Cdd:PHA03100  186 niKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 661-807 2.14e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.62  E-value: 2.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  661 KVILMLLDNLDPNFQSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAV--VNNHLEVaRYMVQLGG 738
Cdd:PHA02876  355 KDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALcgTNPYMSV-KTLIDRGA 433

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  739 CVYSKEEDGSTCLHHAAKIG-NLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIdvIRMLLTRGADV 807
Cdd:PHA02876  434 NVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNG-ADVNAINIQNQYPLLIALEYHGI--VNILLHYGAEL 500
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 712-853 8.35e-09

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: 59.64  E-value: 8.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  712 KQQR---TPLMEAVVNNHLEVARYMVQLGGC-VYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGQVDVNAQDSG----GWT 783
Cdd:cd22192    12 QQKRiseSPLLLAAKENDVQAIKKLLKCPSCdLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSdlyqGET 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  784 PIIWAAEHKHIDVIRMLLTRGADVT--------LTDNEENIC------LHWASFTGSAAIAEVLLNAQCDLHAVNYHGDT 849
Cdd:cd22192    92 ALHIAVVNQNLNLVRELIARGADVVspratgtfFRPGPKNLIyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171


                  ....
gi 557440769  850 PLHI 853
Cdd:cd22192   172 VLHI 175
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 684-882 9.52e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.12  E-value: 9.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  684 PLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQlggcVYSKEEDGST--CLHHAAKIGNLE 761
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR----SINKCSVFYTlvAIKDAFNNRNVE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  762 MVSLLLSTG-----QVDVNAQDSGGWTPIIWAaehkhiDVIRMLLTRGADVTLTD-NEENICLHWASFTGSAAIAEVLLN 835
Cdd:PHA02878  116 IFKIILTNRykniqTIDLVYIDKKSKDDIIEA------EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLS 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 557440769  836 AQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDT 882
Cdd:PHA02878  190 YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
 1043-1171 9.58e-09

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: 54.69  E-value: 9.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1043 KMGWGVRALQTIPQGtficeyvgELISDAEADVREDDSYLFDLDNKDGEVYCIdaryYGNISRFiNHLCDPNiipVRVFM 1122
Cdd:cd20071     8 SKGRGLVATRDIEPG--------ELILVEKPLVSVPSNSFSLTDGLNEIGVGL----FPLASLL-NHSCDPN---AVVVF 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 557440769 1123 LHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWD--------IKSKYFTCQCgsEKC 1171
Cdd:cd20071    72 DGNG----TLRVRALRDIKAGEELTISYIDPLLPrterrrelLEKYGFTCSC--PRC 122
Ank_2 pfam12796
Ankyrin repeats (3 copies);
630-711 1.19e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.58  E-value: 1.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769   630 KALVIQESERRKKLRFHPRQLYLSVKQGELQKVILmLLDNLDPNFQSDQqskRTPLHAAAQKGSVEICHVLLQAGANINA 709
Cdd:pfam12796   14 KLLLENGADANLQDKNGRTALHLAAKNGHLEIVKL-LLEHADVNLKDNG---RTALHYAARSGHLEIVKLLLEKGADINV 89


                   ..
gi 557440769   710 VD 711
Cdd:pfam12796   90 KD 91
Ank_5 pfam13857
Ankyrin repeats (many copies);
766-813 2.43e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.58  E-value: 2.43e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 557440769   766 LLSTGQVDVNAQDSGGWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNE 813
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE 48
Ank_4 pfam13637
Ankyrin repeats (many copies);
781-834 2.83e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 2.83e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 557440769   781 GWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLL 834
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 824-885 3.37e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 3.37e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557440769  824 TGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTA-WD 885
Cdd:PLN03192  535 TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAlWN 597
SET_ATXR5_6-like cd10539
SET domain found in fungal protein lysine methyltransferase SET5 and similar protein; The ...
 1043-1150 4.37e-08

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: 53.18  E-value: 4.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1043 KMGWGVRALQTIPQGTFICEYVGEL--ISDAEADvrEDDSYLFDLDNKDGE---VYCIDARyyGNISRFI----NHLCD- 1112
Cdd:cd10539    13 REGFTVEADGFIKDLTIIAEYTGDVdyIRNREFD--DNDSIMTLLLAGDPSkslVICPDKR--GNIARFIsginNHTKDg 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 557440769 1113 ---PNIIPVRVFMLHQdlrfPRIAFFSSRDIRTGEELGFDY 1150
Cdd:cd10539    89 kkkQNCKCVRYSINGE----ARVLLVATRDIAKGERLYYDY 125
Ank_2 pfam12796
Ankyrin repeats (3 copies);
818-883 5.49e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.66  E-value: 5.49e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 557440769   818 LHWASFTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRgANPELRNkEGDTA 883
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTA 64
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 706-882 1.52e-07

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: 55.86  E-value: 1.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769   706 NINAVDKQQRTPLMEAVV-NNHLEVARYMVQLGGCVYSkeedGSTCLHHAAK--IGNLEMVSLLLSTGQVD------VNA 776
Cdd:TIGR00870   44 NINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAV----GDTLLHAISLeyVDAVEAILLHLLAAFRKsgplelAND 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769   777 QDSG----GWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNeENICLHwASFTGSAaiaevllnaqcdlhavnYHGDTPLH 852
Cdd:TIGR00870  120 QYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPARAC-GDFFVK-SQGVDSF-----------------YHGESPLN 180

                          170       180       190
                   ....*....|....*....|....*....|
gi 557440769   853 IAARESYHDCVLLFLSRGANPELRNKEGDT 882
Cdd:TIGR00870  181 AAACLGSPSIVALLSEDPADILTADSLGNT 210
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 693-776 3.18e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 3.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  693 SVEICH-----------VLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLE 761
Cdd:PTZ00322   83 TVELCQlaasgdavgarILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFRE 162

                          90
                  ....*....|....*
gi 557440769  762 MVSLLLSTGQVDVNA 776
Cdd:PTZ00322  163 VVQLLSRHSQCHFEL 177
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 682-712 7.70e-07

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: 46.51  E-value: 7.70e-07
                           10        20        30
                   ....*....|....*....|....*....|..
gi 557440769   682 RTPLHAAA-QKGSVEICHVLLQAGANINAVDK 712
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
833-886 1.26e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 1.26e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 557440769   833 LLNA-QCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDL 886
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 644-861 5.97e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.46  E-value: 5.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769   644 RFHPRQLYLSVKQGELQKVILMLLdnldpNFQSDQQSKRTPLHAAAqKGSVEICHVLLQ--------AGANINAVDKQQ- 714
Cdd:TIGR00870   50 RLGRSALFVAAIENENLELTELLL-----NLSCRGAVGDTLLHAIS-LEYVDAVEAILLhllaafrkSGPLELANDQYTs 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769   715 -----RTPLMEAVVNNHLEVARYMVQLG-------GCVYSKEEDGSTCLHH-------AAKIGNLEMVSLLLSTGQvDVN 775
Cdd:TIGR00870  124 eftpgITALHLAAHRQNYEIVKLLLERGasvparaCGDFFVKSQGVDSFYHgesplnaAACLGSPSIVALLSEDPA-DIL 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769   776 AQDSGGWTPiiwaaehKHIDVIRMLLTrgadvtlTDNEENICL-------HWASFTGSAAIAEVLlnaqcdlhavNYHGD 848
Cdd:TIGR00870  203 TADSLGNTL-------LHLLVMENEFK-------AEYEELSCQmynfalsLLDKLRDSKELEVIL----------NHQGL 258

                          250
                   ....*....|...
gi 557440769   849 TPLHIAARESYHD 861
Cdd:TIGR00870  259 TPLKLAAKEGRIV 271
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 754-893 7.30e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.99  E-value: 7.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  754 AAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIDVIRMLLTRGA--DVTLTDNEENicLHWASFTGSAAIAE 831
Cdd:PHA02875    9 AILFGELDIARRLLDIG-INPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIESE--LHDAVEEGDVKAVE 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557440769  832 VLLNAQCDLHAVNYH-GDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDLTPERSDV 893
Cdd:PHA02875   86 ELLDLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 824-889 7.66e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 7.66e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 557440769  824 TGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDLTPE 889
Cdd:PTZ00322   92 SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 846-878 8.43e-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: 43.43  E-value: 8.43e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 557440769   846 HGDTPLHIAA-RESYHDCVLLFLSRGANPELRNK 878
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 781-809 1.22e-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: 1.22e-05
                            10        20
                    ....*....|....*....|....*....
gi 557440769    781 GWTPIIWAAEHKHIDVIRMLLTRGADVTL 809
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 751-839 1.38e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  751 LHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIA 830
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164

                          90
                  ....*....|
gi 557440769  831 EVLLN-AQCD 839
Cdd:PTZ00322  165 QLLSRhSQCH 174
PHA03247 PHA03247
large tegument protein UL36; Provisional
 23-201 1.82e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769   23 ALLLEKEPRGAAERVHSSLGDTPQSEETLPKANPDSLEPAGPSSPASVTVTVGDEGADTPVGAASLIGDEPesleGDGGR 102
Cdd:PHA03247 2734 ALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDP----ADPPA 2809

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  103 IVLGHATKSFPSSPSKGGACPSRAKMSMTGAGKSPPSVQSLAMRLLSMPGAQGAATAGPEPSPATTAAQEgQPKVHR-AR 181
Cdd:PHA03247 2810 AVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPA-RPPVRRlAR 2888

                         170       180
                  ....*....|....*....|..
gi 557440769  182 KTMSKP--SNGQPPIPEKRPPE 201
Cdd:PHA03247 2889 PAVSRSteSFALPPDQPERPPQ 2910
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 781-812 2.20e-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: 42.28  E-value: 2.20e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 557440769   781 GWTPIIWAAEH-KHIDVIRMLLTRGADVTLTDN 812
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
 1035-1156 2.28e-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: 44.55  E-value: 2.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1035 RLQLYRTAKMGWGVRALQTIPQGTFIcEYVGELISDAEADVREDDSYLFDLdnkdgeVYCIDARYY----GNISRFiNHL 1110
Cdd:cd10540     1 RLEVKPSTLKGRGVFATRPIKKGEVI-EEAPVIVLPKEEYQHLCKTVLDHY------VFSWGDGCLalalGYGSMF-NHS 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 557440769 1111 CDPNIIPVRVFMLHqdlrfpRIAFFSSRDIRTGEELGFDYGDRFWD 1156
Cdd:cd10540    73 YTPNAEYEIDFENQ------TIVFYALRDIEAGEELTINYGDDLWD 112
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 664-747 2.36e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  664 LMLLDNLDPNfqSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYSK 743
Cdd:PTZ00322  100 ILLTGGADPN--CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177


                  ....
gi 557440769  744 EEDG 747
Cdd:PTZ00322  178 GANA 181
Ank_5 pfam13857
Ankyrin repeats (many copies);
740-788 2.37e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 2.37e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 557440769   740 VYSKEEDGSTCLHHAAKIGNLEMVSLLLsTGQVDVNAQDSGGWTPIIWA 788
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 682-709 2.42e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 2.42e-05
                            10        20
                    ....*....|....*....|....*...
gi 557440769    682 RTPLHAAAQKGSVEICHVLLQAGANINA 709
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 746-778 2.76e-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: 42.28  E-value: 2.76e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 557440769   746 DGSTCLHHAA-KIGNLEMVSLLLSTGqVDVNAQD 778
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKG-ADVNARD 33
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 693-785 2.96e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 46.35  E-value: 2.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  693 SVEICHVLLQAGANINAVDKQQRTPLMEAV--VNNHLEVARYMVQLGGCVYSKEEDGSTCLH-----HAAKignlEMVSL 765
Cdd:PHA02859  102 EPEILKILIDSGSSITEEDEDGKNLLHMYMcnFNVRINVIKLLIDSGVSFLNKDFDNNNILYsyilfHSDK----KIFDF 177

                          90       100
                  ....*....|....*....|
gi 557440769  766 LLSTGqVDVNAQDSGGWTPI 785
Cdd:PHA02859  178 LTSLG-IDINETNKSGYNCY 196
PHA02798 PHA02798
ankyrin-like protein; Provisional
 663-775 3.03e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.91  E-value: 3.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  663 ILMLLDNLDPNFQSDQQSKRTPL-----HAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVN---NHLEVARYMV 734
Cdd:PHA02798   53 IVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMI 132

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 557440769  735 QLGGCVYSKEEDGSTCLHHAAKIGN---LEMVSLLLSTGqVDVN 775
Cdd:PHA02798  133 ENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKG-VDIN 175
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 797-868 4.40e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 4.40e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557440769  797 IRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLS 868
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
817-867 5.46e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 5.46e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 557440769   817 CLHWASFTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFL 867
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 650-857 5.92e-05

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: 47.31  E-value: 5.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  650 LYLSVKQGELQKVILMLLDNLDPNFQSDQQSKrTPLHAAAQKGSVEICHVLLQAGAN-INAVDK----QQRTPLMEAVVN 724
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPSCDLFQRGALGE-TALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVVN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  725 NHLEVARYMVQLGGCVYSKEEDGS------TCLHH--------AAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIiwaae 790
Cdd:cd22192   100 QNLNLVRELIARGADVVSPRATGTffrpgpKNLIYygehplsfAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVL----- 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557440769  791 hkHIdvirmlltrgadVTLTDNEENICLHWASFTGSaaiaEVLLNAQCDLHAVNYHGDTPLHIAARE 857
Cdd:cd22192   174 --HI------------LVLQPNKTFACQMYDLILSY----DKEDDLQPLDLVPNNQGLTPFKLAAKE 222
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 846-875 1.14e-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: 40.26  E-value: 1.14e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 557440769    846 HGDTPLHIAARESYHDCVLLFLSRGANPEL 875
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 644-737 1.15e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.14  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  644 RFHPrqLYLSVKQGELQKVILMLLDNLDPNFQSDQQSkrTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLM-EAV 722
Cdd:PHA02875  135 KFSP--LHLAVMMGDIKGIELLIDHKACLDIEDCCGC--TPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAI 210

                          90
                  ....*....|....*
gi 557440769  723 VNNHLEVARYMVQLG 737
Cdd:PHA02875  211 ENNKIDIVRLFIKRG 225
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 746-776 1.32e-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: 40.26  E-value: 1.32e-04
                            10        20        30
                    ....*....|....*....|....*....|.
gi 557440769    746 DGSTCLHHAAKIGNLEMVSLLLSTGqVDVNA 776
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKG-ADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
666-718 1.39e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 1.39e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 557440769   666 LLDNLDPNFQSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPL 718
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
 1045-1154 1.44e-04

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: 42.99  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1045 GWGVRALQTIPQGTFICEYVGELISDAEAdvrEDDSYLFDLDNKDGEVYCIDAR--YYGNISRFIN---HLCDPNIIpvr 1119
Cdd:cd19193    19 GLGVWAEAPIPKGMVFGPYEGEIVEDEEA---ADSGYSWQIYKGGKLSHYIDAKdeSKSNWMRYVNcarNEEEQNLV--- 92

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 557440769 1120 VFMLHQDlrfprIAFFSSRDIRTGEELGFDYGDRF 1154
Cdd:cd19193    93 AFQYRGK-----IYYRTCKDIAPGTELLVWYGDEY 122
SET_KMT2E cd19182
SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...
 1048-1151 3.10e-04

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


Pssm-ID: 380959  Cd Length: 129  Bit Score: 41.80  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1048 VRALQTIPQGTFICEYVGELISDAEAdvrEDDSYLFD--------LDNKDGEVYCIDARYYGNISRFINHLCDPNIIPVR 1119
Cdd:cd19182    21 LKAAKDLPPDTLIIEYRGKFMLREQF---EANGYFFKrpypfvlfYSKFHGLEMCVDARTFGNEARFIRRSCTPNAEVRH 97

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 557440769 1120 VF---MLHqdlrfprIAFFSSRDIRTGEEL----GFDYG 1151
Cdd:cd19182    98 VIedgTIH-------LYIYSIRSIPKGTEItiafDFDYG 129
PR-SET_PRDM6 cd19191
PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 ...
 1045-1154 5.30e-04

PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 (also termed PR domain-containing protein 6) is a putative histone-lysine N-methyltransferase that acts as a transcriptional repressor of smooth muscle gene expression. It may specifically methylate 'Lys-20' of histone H4 when associated with other proteins and in vitro.


Pssm-ID: 380968  Cd Length: 128  Bit Score: 41.31  E-value: 5.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1045 GWGVRALQTIPQGTFICEYVGELIS-DAEADVREDDSYLFDLDNKDGEV-YCIDAR--YYGNISRFIN---HLCDPNIIP 1117
Cdd:cd19191    16 GYGICAAQRIPQGTWIGPFEGVLVSpEKQIGAVRNTQHLWEIYDQEGTLqHFIDGGdpSKSSWMRYIRcarHCGEQNLTV 95

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 557440769 1118 VRvfmlHQDLRFPRIAffssRDIRTGEELGFDYGDRF 1154
Cdd:cd19191    96 VQ----YRGCIFYRAC----RDIPRGTELLVWYDDSY 124
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 682-709 5.78e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.39  E-value: 5.78e-04
                           10        20
                   ....*....|....*....|....*...
gi 557440769   682 RTPLHAAAQKGSVEICHVLLQAGANINA 709
Cdd:pfam13606    3 NTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 781-807 8.32e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 8.32e-04
                           10        20
                   ....*....|....*....|....*..
gi 557440769   781 GWTPIIWAAEHKHIDVIRMLLTRGADV 807
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADI 28
Ank_5 pfam13857
Ankyrin repeats (many copies);
700-754 1.05e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 1.05e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 557440769   700 LLQAG-ANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHA 754
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PR-SET_PRDM14 cd19198
PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 ...
 1036-1154 1.07e-03

PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 (also termed PR domain-containing protein 14) acts as a transcription factor that has both positive and negative roles on transcription. It acts on regulating epigenetic modifications in the cells, playing a key role in the regulation of cell pluripotency, epigenetic reprogramming, differentiation and development. Aberrant PRDM14 expression is associated with tumorigenesis, cell migration and cell chemotherapeutic drugs resistance.


Pssm-ID: 380975  Cd Length: 133  Bit Score: 40.46  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1036 LQLYRTAKMG---WGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLdNKDGEV-YCIDAR-YYGNISRFINhl 1110
Cdd:cd19198     7 LRVLQTSFGGtphYGVFCKKTIPKGTRFGPFRGRVVNTSEIKTYDDNSFMWEI-FEDGKLsHFIDGRgSTGNWMSYVN-- 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 557440769 1111 C-----DPNIIPVRvfmlHQDlrfpRIAFFSSRDIRTGEELGFDYGDRF 1154
Cdd:cd19198    84 CaryaeEQNLIAIQ----CQG----QIFYESCKEILQGQELLVWYGDCY 124
SET_SMYD4 cd10536
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
 1106-1166 1.12e-03

SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing protein 4 (SMYD4) and similar proteins; 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. In zebrafish, SMYD4 is ubiquitously expressed in early embryos and becomes enriched in the developing heart; mutants show a strong defect in cardiomyocyte proliferation, which lead to a severe cardiac malformation.


Pssm-ID: 380934 [Multi-domain]  Cd Length: 218  Bit Score: 41.90  E-value: 1.12e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557440769 1106 FINHLCDPNIIpvRVFMLHQdlrfprIAFFSSRDIRTGEELGFDYG------DRFW---DIKSKY-FTCQC 1166
Cdd:cd10536   153 LLNHSCDPNTI--RSFYGNT------IVVRATRPIKKGEEITICYGphfsrmKRSErqrLLKEQYfFDCSC 215
SET_SETD5 cd19181
SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...
 1028-1114 1.75e-03

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


Pssm-ID: 380958  Cd Length: 150  Bit Score: 40.38  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769 1028 VQSGIKVRLQLYRTAkmgwgVRALQTIPQGTFICEYVGELISDAEADV-----REDDSYLFDLDNKDGEVYCIDARYYGN 1102
Cdd:cd19181     6 LQLGRVTRVQKHRKI-----LRAARDLALDTLIIEYRGKVMLRQQFEVnghffKRPYPFVLFYSKFNGVEMCVDARTFGN 80

                          90
                  ....*....|..
gi 557440769 1103 ISRFINHLCDPN 1114
Cdd:cd19181    81 DARFIRRSCTPN 92
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 707-767 2.55e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 42.04  E-value: 2.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557440769  707 INAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLL 767
Cdd:PHA02989  249 INKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRIL 309
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 746-776 6.06e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 6.06e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 557440769   746 DGSTCLHHAAKIGNLEMVSLLLSTGqVDVNA 776
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENG-ADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 740-882 9.80e-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: 40.25  E-value: 9.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440769  740 VYSKEEDGSTCLHHAA---KIGNLEMVSLLLSTGQVD------VNAQDSG----GWTPIIWAAEHKHIDVIRMLLTRGAD 806
Cdd:cd21882    19 AYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSgnpkelVNAPCTDefyqGQTALHIAIENRNLNLVRLLVENGAD 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557440769  807 VTLtdneeniclhwasftgsAAIAEVLLNAQCDLHavnYHGDTPLHIAARESYHDCVLLFLSRGANP---ELRNKEGDT 882
Cdd:cd21882    99 VSA-----------------RATGRFFRKSPGNLF---YFGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNT 157
 
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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