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Conserved domains on  [gi|1907121895|ref|XP_036016155|]
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histone-lysine N-methyltransferase EHMT2 isoform X6 [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 ...
738-976 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: 533.06  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  738 EDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRSC 817
Cdd:cd10533      1 EDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRNC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  818 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNI 897
Cdd:cd10533     81 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNI 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907121895  898 SRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQ 976
Cdd:cd10533    161 SRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQ 239
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
210-339 2.60e-62

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: 207.24  E-value: 2.60e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  210 FEELPLCSCRMEAPKIDRISERAGHKCMATESVDGELLGC-NAAILKRETMRPSSRVALMVLCEAHRARMVKHHCCPGCG 288
Cdd:cd20905      1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCsNLPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907121895  289 YFCTAGTFLECHPDFRVAHRFHKACVSQLNGMVFCPHCGEDAS-EAQEVTIP 339
Cdd:cd20905     81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLP 132
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
418-677 9.32e-54

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 189.39  E-value: 9.32e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  418 GREALEKALVIQESERRKKLRFHPRQLYLSVKQGELQKVILMLLDNLDPNFQSDQQSkrTPLHAAAQKGSVEICHVLLQA 497
Cdd:COG0666     32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEA 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  498 GANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWT 577
Cdd:COG0666    110 GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDNDGET 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  578 PIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCV 657
Cdd:COG0666    189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
                          250       260
                   ....*....|....*....|
gi 1907121895  658 LLFLSRGANPELRNKEGDTA 677
Cdd:COG0666    269 KLLLLALLLLAAALLDLLTL 288
Amidase super family cl18951
Amidase;
344-379 7.18e-03

Amidase;


The actual alignment was detected with superfamily member PRK07042:

Pssm-ID: 450241 [Multi-domain]  Cd Length: 464  Bit Score: 39.96  E-value: 7.18e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1907121895  344 GTP-PIGTAAPALPPLAHDAPgradtsqPSARMRGHG 379
Cdd:PRK07042    87 GVPvPLGTAATDLPPAAADAP-------PAARLREAG 116
 
Name Accession Description Interval E-value
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
738-976 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: 533.06  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  738 EDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRSC 817
Cdd:cd10533      1 EDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRNC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  818 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNI 897
Cdd:cd10533     81 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNI 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907121895  898 SRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQ 976
Cdd:cd10533    161 SRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQ 239
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
210-339 2.60e-62

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: 207.24  E-value: 2.60e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  210 FEELPLCSCRMEAPKIDRISERAGHKCMATESVDGELLGC-NAAILKRETMRPSSRVALMVLCEAHRARMVKHHCCPGCG 288
Cdd:cd20905      1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCsNLPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907121895  289 YFCTAGTFLECHPDFRVAHRFHKACVSQLNGMVFCPHCGEDAS-EAQEVTIP 339
Cdd:cd20905     81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLP 132
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
418-677 9.32e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 189.39  E-value: 9.32e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  418 GREALEKALVIQESERRKKLRFHPRQLYLSVKQGELQKVILMLLDNLDPNFQSDQQSkrTPLHAAAQKGSVEICHVLLQA 497
Cdd:COG0666     32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEA 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  498 GANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWT 577
Cdd:COG0666    110 GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDNDGET 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  578 PIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCV 657
Cdd:COG0666    189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
                          250       260
                   ....*....|....*....|
gi 1907121895  658 LLFLSRGANPELRNKEGDTA 677
Cdd:COG0666    269 KLLLLALLLLAAALLDLLTL 288
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
828-950 2.44e-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: 144.78  E-value: 2.44e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895   828 VRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRE--------DDSYLFDLDNKdgevYCIDARYYGNISR 899
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPkaydtdgaKAFYLFDIDSD----LCIDARRKGNLAR 76
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1907121895   900 FINHLCDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWD 950
Cdd:smart00317   77 FINHSCEPNCELLFVEVNGDD----RIVIFALRDIKPGEELTIDYGSDYAN 123
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
839-945 1.79e-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: 116.08  E-value: 1.79e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  839 GWGVRALQTIPQGTFICEYVGE-LISDAEADVRED-----------DSYLFDLDNKDGevYCIDAR--YYGNISRFINHL 904
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELlyydklelrlwGPYLFTLDEDSE--YCIDARalYYGNWARFINHS 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1907121895  905 CDPNIIPVRVFMlhqdLRFPRIAFFSSRDIRTGEELGFDYG 945
Cdd:pfam00856   79 CDPNCEVRVVYV----NGGPRIVIFALRDIKPGEELTIDYG 115
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
826-967 2.38e-28

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 110.82  E-value: 2.38e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  826 IKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDS-----YLFDLDNKDGevycIDARYYGNISRF 900
Cdd:COG2940      4 LHPRIEVRPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKeplhtYLFELDDDGV----IDGALGGNPARF 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907121895  901 INHLCDPNIIPVRvfmlhqdlRFPRIAFFSSRDIRTGEELGFDYGDRFWDiksKYFTCQCGseKCKH 967
Cdd:COG2940     80 INHSCDPNCEADE--------EDGRIFIVALRDIAAGEELTYDYGLDYDE---EEYPCRCP--NCRG 133
Ank_2 pfam12796
Ankyrin repeats (3 copies);
512-605 2.30e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 2.30e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  512 LMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLStgQVDVNAQDSGgWTPIIWAAEHKHIDVI 591
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNG-RTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 1907121895  592 RMLLTRGADVTLTD 605
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
444-666 2.64e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.81  E-value: 2.64e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  444 LYLSVKQGELQKVILMLLDNLDPNFQSDQQSkrTPLHAAAQKGSV-----EICHVLLQAGANINAVDKQQRTPLMEAVVN 518
Cdd:PHA03100    39 LYLAKEARNIDVVKILLDNGADINSSTKNNS--TPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISK 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  519 --NHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIG--NLEMVSLLLSTGqVDVNAqdsggwtpiiwaaehkhIDVIRML 594
Cdd:PHA03100   117 ksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNkiDLKILKLLIDKG-VDINA-----------------KNRVNYL 178
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907121895  595 LTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGAN 666
Cdd:PHA03100   179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
506-647 6.58e-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: 6.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  506 KQQR---TPLMEAVVNNHLEVARYMVQLGGC-VYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGQVDVNAQDSG----GWT 577
Cdd:cd22192     12 QQKRiseSPLLLAAKENDVQAIKKLLKCPSCdLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSdlyqGET 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  578 PIIWAAEHKHIDVIRMLLTRGADVT--------LTDNEENIC------LHWASFTGSAAIAEVLLNAQCDLHAVNYHGDT 643
Cdd:cd22192     92 ALHIAVVNQNLNLVRELIARGADVVspratgtfFRPGPKNLIyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171

                   ....
gi 1907121895  644 PLHI 647
Cdd:cd22192    172 VLHI 175
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
500-676 1.20e-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: 1.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  500 NINAVDKQQRTPLMEAVV-NNHLEVARYMVQLGGCVYSkeedGSTCLHHAAK--IGNLEMVSLLLSTGQVD------VNA 570
Cdd:TIGR00870   44 NINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAV----GDTLLHAISLeyVDAVEAILLHLLAAFRKsgplelAND 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  571 QDSG----GWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNeENICLHwASFTGSAaiaevllnaqcdlhavnYHGDTPLH 646
Cdd:TIGR00870  120 QYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPARAC-GDFFVK-SQGVDSF-----------------YHGESPLN 180
                          170       180       190
                   ....*....|....*....|....*....|
gi 1907121895  647 IAARESYHDCVLLFLSRGANPELRNKEGDT 676
Cdd:TIGR00870  181 AAACLGSPSIVALLSEDPADILTADSLGNT 210
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
575-603 1.12e-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: 1.12e-05
                            10        20
                    ....*....|....*....|....*....
gi 1907121895   575 GWTPIIWAAEHKHIDVIRMLLTRGADVTL 603
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PRK07042 PRK07042
amidase; Provisional
344-379 7.18e-03

amidase; Provisional


Pssm-ID: 235915 [Multi-domain]  Cd Length: 464  Bit Score: 39.96  E-value: 7.18e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1907121895  344 GTP-PIGTAAPALPPLAHDAPgradtsqPSARMRGHG 379
Cdd:PRK07042    87 GVPvPLGTAATDLPPAAADAP-------PAARLREAG 116
 
Name Accession Description Interval E-value
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
738-976 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: 533.06  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  738 EDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRSC 817
Cdd:cd10533      1 EDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRNC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  818 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNI 897
Cdd:cd10533     81 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNI 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907121895  898 SRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQ 976
Cdd:cd10533    161 SRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQ 239
SET_EHMT cd10543
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
739-968 6.21e-170

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: 495.32  E-value: 6.21e-170
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  739 DYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRSCK 818
Cdd:cd10543      2 DFLYVTENCETSPLNIDRNITSLQTCSCRDDCSSDNCVCGRLSVRCWYDKEGRLLPDFNKLDPPLIFECNRACSCWRNCR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  819 NRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNIS 898
Cdd:cd10543     82 NRVVQNGIRYRLQLFRTRGMGWGVRALQDIPKGTFVCEYIGELISDSEADSREDDSYLFDLDNKDGETYCIDARRYGNIS 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  899 RFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHS 968
Cdd:cd10543    162 RFINHLCEPNLIPVRVFVEHQDLRFPRIAFFASRDIKAGEELGFDYGEKFWRIKGKYFTCRCGSPKCKYS 231
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
739-968 4.91e-167

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: 487.90  E-value: 4.91e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  739 DYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRSCK 818
Cdd:cd10535      2 NYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNCR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  819 NRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNIS 898
Cdd:cd10535     82 NRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNVS 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  899 RFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHS 968
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) ...
738-945 2.97e-94

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: 297.75  E-value: 2.97e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  738 EDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSI-RCWYDKDGRLlQEFNkiEPPLIFECNQACSCWRS 816
Cdd:cd10538      1 PSFTYIKDNIVGKNVQPFSNIIDSVGCKCKDDCLDSKCACAAESDgIFAYTKNGLL-RLNN--SPPPIFECNSKCSCDDD 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  817 CKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR------EDDSYLFDLDN-----KDGE 885
Cdd:cd10538     78 CKNRVVQRGLQARLQVFRTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRgkiydkSGGSYLFDLDEfsdsdGDGE 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  886 VYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYG 945
Cdd:cd10538    158 ELCVDATFCGNVSRFINHSCDPNLFPFNVVIDHDDLRYPRIALFATRDILPGEELTFDYG 217
SET_SUV39H cd10542
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
739-966 2.02e-72

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: 239.89  E-value: 2.02e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  739 DYKYIseNCETSTMNIDRNITHLQHCTCVDDC--SSSNClCGQLS-IRCWYDKDGRLlqefnKIEPPL-IFECNQACSCW 814
Cdd:cd10542      2 NFQYI--NDYIPGDGVKIPEDFLVGCECTEDChnNNPTC-CPAESgVKFAYDKQGRL-----RLPPGTpIYECNSRCKCG 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  815 RSCKNRVVQSGIKVRLQLYRTA-KMGWGVRALQTIPQGTFICEYVGELISDAEADVR------EDDSYLFDLD-NKDGEV 886
Cdd:cd10542     74 PDCPNRVVQRGRKVPLCIFRTSnGRGWGVKTLEDIKKGTFVMEYVGEIITSEEAERRgkiydaNGRTYLFDLDyNDDDCE 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  887 YCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYgDRFWDIKSKYFT--------- 957
Cdd:cd10542    154 YTVDAAYYGNISHFINHSCDPNLAVYAVWINHLDPRLPRIAFFAKRDIKAGEELTFDY-LMTGTGGSSESTipkpkdvrv 232
                          250
                   ....*....|
gi 1907121895  958 -CQCGSEKCK 966
Cdd:cd10542    233 pCLCGSKNCR 242
SET_SETDB1 cd10517
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
715-966 1.51e-71

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: 239.11  E-value: 1.51e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  715 DVARGYENVPIPCVNGVDGEPcPEDYKYISENCETSTMNIDRNITHLQHCTCVDDCS-SSNCLCGQLSI---RCWYDKD- 789
Cdd:cd10517      8 DISYGKEGVPIPCVNEIDNSS-PPYVEYSKERIPGKGVNINLDPDFLVGCDCTDGCRdKSKCACQQLTIeatAATPGGQi 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  790 --------GRLLQEFnkiePPLIFECNQACSCWRSCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGEL 861
Cdd:cd10517     87 npsagyqyRRLMEKL----PTGVYECNSRCKCDKRCYNRVVQNGLQVRLQVFKTEKKGWGIRCLDDIPKGSFVCIYAGQI 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  862 ISDAEADVRE---DDSYLFDLD------------NKDGEVYC--IDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFP 924
Cdd:cd10517    163 LTEDEANEEGlqyGDEYFAELDyievveklkegyESDVEEHCyiIDAKSEGNLGRYLNHSCSPNLFVQNVFVDTHDLRFP 242
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1907121895  925 RIAFFSSRDIRTGEELGFDYGdrfWDIKSKYFT---CQCGSEKCK 966
Cdd:cd10517    243 WVAFFASRYIRAGTELTWDYN---YEVGSVPGKvlyCYCGSSNCR 284
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
210-339 2.60e-62

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: 207.24  E-value: 2.60e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  210 FEELPLCSCRMEAPKIDRISERAGHKCMATESVDGELLGC-NAAILKRETMRPSSRVALMVLCEAHRARMVKHHCCPGCG 288
Cdd:cd20905      1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCsNLPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907121895  289 YFCTAGTFLECHPDFRVAHRFHKACVSQLNGMVFCPHCGEDAS-EAQEVTIP 339
Cdd:cd20905     81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLP 132
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
739-965 8.64e-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: 199.45  E-value: 8.64e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  739 DYKYISENCETSTMNIDRNITHLQHCTCVDD-CSSSNCLCgqlsIRCW---YDKDGRLLQEFNKIEPPlIFECNQACSCW 814
Cdd:cd10544      2 DFQYTPENVPGPGADTDPNEITFPGCDCKTSsCEPETCSC----LRKYgpnYDDDGCLLDFDGKYSGP-VFECNSMCKCS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  815 RSCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR------EDDSYLFDLDN--KDGEV 886
Cdd:cd10544     77 ESCQNRVVQNGLQFKLQVFKTPKKGWGLRTLEFIPKGRFVCEYAGEVIGFEEARRRtksqtkGDMNYIIVLREhlSSGKV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  887 Y--CIDARYYGNISRFINHLCDPN--IIPVRVfmlhqDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFT----- 957
Cdd:cd10544    157 LetFVDPTYIGNIGRFLNHSCEPNlfMVPVRV-----DSMVPKLALFAARDIVAGEELSFDYSGEFSNSVESVTLarqde 231
                          250
                   ....*....|....
gi 1907121895  958 ------CQCGSEKC 965
Cdd:cd10544    232 sksrkpCLCGAENC 245
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
764-945 1.15e-55

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: 192.62  E-value: 1.15e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  764 CTCVDDC--SSSNCLCGQL-SIRCWYDKDGRLlqefnkIEP-PLIFECNQACSCWRSCKNRVVQSGIKVRLQLYRTAKMG 839
Cdd:cd10545     24 CDCKNRCtdGASDCACVKKnGGEIPYNFNGRL------IRAkPAIYECGPLCKCPPSCYNRVTQKGLRYRLEVFKTAERG 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  840 WGVRALQTIPQGTFICEYVGELISDAEADVR-EDDSYLFDLDNK------DGEV---------------------YCIDA 891
Cdd:cd10545     98 WGVRSWDSIPAGSFICEYVGELLDTSEADTRsGNDDYLFDIDNRqtnrgwDGGQrldvgmsdgerssaedeesseFTIDA 177
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907121895  892 RYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYG 945
Cdd:cd10545    178 GSFGNVARFINHSCSPNLFVQCVLYDHNDLRLPRVMLFAADNIPPLQELTYDYG 231
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
418-677 9.32e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 189.39  E-value: 9.32e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  418 GREALEKALVIQESERRKKLRFHPRQLYLSVKQGELQKVILMLLDNLDPNFQSDQQSkrTPLHAAAQKGSVEICHVLLQA 497
Cdd:COG0666     32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEA 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  498 GANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWT 577
Cdd:COG0666    110 GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDNDGET 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  578 PIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCV 657
Cdd:COG0666    189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
                          250       260
                   ....*....|....*....|
gi 1907121895  658 LLFLSRGANPELRNKEGDTA 677
Cdd:COG0666    269 KLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
453-711 3.58e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 182.08  E-value: 3.58e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  453 LQKVILMLLDNLDPNFQSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGG 532
Cdd:COG0666     32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  533 CVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICL 612
Cdd:COG0666    112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  613 HWASFTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDLTPERSDVWFALQ 692
Cdd:COG0666    191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
                          250
                   ....*....|....*....
gi 1907121895  693 LNRKLRLGVGNRAVRTEKI 711
Cdd:COG0666    271 LLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
457-697 1.29e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 174.76  E-value: 1.29e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  457 ILMLLDNLDPNFQSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYS 536
Cdd:COG0666      3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  537 KEEDGSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWAS 616
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  617 FTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDLTPERSDVWFALQLNRK 696
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                   .
gi 1907121895  697 L 697
Cdd:COG0666    242 G 242
SET_SETDB cd10541
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...
764-966 2.91e-48

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


Pssm-ID: 380939 [Multi-domain]  Cd Length: 236  Bit Score: 171.57  E-value: 2.91e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  764 CTCVDDC-SSSNCLCGQLSIR----CWYDKD----GRLLQEFNKIEPPLIFECNQACSCWRS-CKNRVVQSGIKVRLQLY 833
Cdd:cd10541     18 CDCTDGCrDKSKCACHQLTIQatacTPGGQDnptaGYQYKRLEECLPTGVYECNKLCKCDPNmCQNRLVQHGLQVRLQLF 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  834 RTAKMGWGVRALQTIPQGTFICEYVGELISDAEAD---VREDDSYLFDLDNKDGEVYCIDARYYGNISRFINHLCDPNII 910
Cdd:cd10541     98 KTQNKGWGIRCLDDIAKGTFVCIYAGKILTDDFADkegLEMGDEYFANLDHIEESCYIIDAKLEGNLGRYLNHSCSPNLF 177
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907121895  911 PVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCK 966
Cdd:cd10541    178 VQNVFVDTHDLRFPWVAFFASKRIKAGTELTWDYNYEVGSVEGKELLCCCGSNECR 233
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
739-966 6.92e-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: 170.84  E-value: 6.92e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  739 DYKYISENCETSTMNIDRNITHlqHCTCVDdCSSSNCLCGQLSIRCWYDKDGRLlqefnKIEPPL-IFECNQACSCWRSC 817
Cdd:cd10532      2 DFYYINEYKPAPGINLDNEATV--GCDCSD-CFFGKCCPAEAGVLFAYNEHGQL-----KIPPGTpIYECNSRCKCGPDC 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  818 KNRVVQSGIKVRLQLYRTAK-MGWGVRALQTIPQGTFICEYVGELISDAEADVR------EDDSYLFDLDNKDGEvYCID 890
Cdd:cd10532     74 PNRVVQKGTQYSLCIFRTSNgRGWGVKTLQKIKKNSFVMEYVGEVITSEEAERRgqfydsKGITYLFDLDYESDE-FTVD 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  891 ARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDY-----GDRFWD------IKSKYFT-C 958
Cdd:cd10532    153 AARYGNVSHFVNHSCDPNLQVFNVFIDNLDTRLPRIALFSTRTIKAGEELTFDYqmkgsGDLSSDsidnspAKKRVRTvC 232

                   ....*...
gi 1907121895  959 QCGSEKCK 966
Cdd:cd10532    233 KCGAVTCR 240
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
739-944 9.82e-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: 170.84  E-value: 9.82e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  739 DYKYISENCETSTMNIDRNITHlqhCTCvDDCSSS---NCLCGQLSIRCWYDKDGRLlqefnKIEPPL-IFECNQACSCW 814
Cdd:cd10525      2 DFVYINEYKVGEGVTLNQVAVG---CEC-QDCLSQpvgGCCPGASKHRFAYNEQGQV-----KVRPGLpIYECNSRCRCG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  815 RSCKNRVVQSGIKVRLQLYRTAK-MGWGVRALQTIPQGTFICEYVGELISDAEADVR------EDDSYLFDLDNKDgEVY 887
Cdd:cd10525     73 PDCPNRVVQKGIQYDLCIFRTDNgRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRgqiydrQGATYLFDLDYVE-DVY 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907121895  888 CIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDY 944
Cdd:cd10525    152 TVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIALFATRTIRAGEELTFDY 208
SET_SUV39H_Clr4-like cd20073
SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 ...
757-966 2.58e-45

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


Pssm-ID: 380999 [Multi-domain]  Cd Length: 259  Bit Score: 164.28  E-value: 2.58e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  757 NITHLQHCTcVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIepplIFECNQACSCWRSCKNRVVQSGIKVRLQLYRTA 836
Cdd:cd20073     27 SCSKLGGCD-LNNPGSCQCLEDSNEKSFAYDEYGRVRANTGSI----IYECNENCDCGINCPNRVVQRGRKLPLEIFKTK 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  837 KMGWGVRALQTIPQGTFICEYVGELISDAEADVRE---DD---SYLFDLDNKDGEV---YCIDARYYGNISRFINHLCDP 907
Cdd:cd20073    102 HKGWGLRCPRFIKAGTFIGVYLGEVITQSEAEIRGkkyDNvgvTYLFDLDLFEDQVdeyYTVDAQYCGDVTRFINHSCDP 181
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907121895  908 NIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDR----------------FWDIKSKyFTCQCGSEKCK 966
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; ...
764-966 3.14e-45

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


Pssm-ID: 380996 [Multi-domain]  Cd Length: 274  Bit Score: 164.41  E-value: 3.14e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  764 CTCVDD--CSSSNCLCGQ-----------LSIRCWY---DKDGRLLQEF-NKIEPplIFECNQACSCWRSCKNRVVQSGI 826
Cdd:cd19473     26 CECTDDedCMYSGCLCLQdvdpdddrdpgKKKNAYHssgAKKGCLRGHMlNSRLP--IYECHEGCACSDDCPNRVVERGR 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  827 KVRLQLYRTA-KMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDS--------YLFDLDN----------KDGEVY 887
Cdd:cd19473    104 KVPLQIFRTSdGRGWGVRSTVDIKRGQFVDCYVGEIITPEEAQRRRDAAtiaqrkdvYLFALDKfsdpdsldprLRGDPY 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  888 CIDARYYGNISRFINHLCDPNIipvRVFML---HQDLRFPRIAFFSSRDIRTGEELGFDY--------GDRFWDIKSKYF 956
Cdd:cd19473    184 EIDGEFMSGPTRFINHSCDPNL---RIFARvgdHADKHIHDLAFFAIKDIPRGTELTFDYvdgvtgldDDAGDEEKEKEM 260
                          250
                   ....*....|.
gi 1907121895  957 T-CQCGSEKCK 966
Cdd:cd19473    261 TkCLCGSPKCR 271
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
731-966 4.10e-43

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


Pssm-ID: 380921 [Multi-domain]  Cd Length: 266  Bit Score: 158.07  E-value: 4.10e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  731 VDGEPCPEDYKYISENCETStmnidrNITHLQHCTCVDDCSS-SNCLCGQLSIR----CWYDKD-GRLLQEFNKIEPPL- 803
Cdd:cd10523      7 VQLDRNPQDQQQLVDDFDIS------NGAFVDSCDCTDGCIDiLKCACLQLTARafskSESSPSkGGRGYKYKRLQEPIp 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  804 --IFECNQACSCWRS-CKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELIS----------------- 863
Cdd:cd10523     81 sgLYECNVSCKCNRMlCQNRVVQHGLQVRLQVFKTEKKGWGVRCLDDIDKGTFVCIYAGRVLSrarspteplppklelps 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  864 DAEADVREDDSYLFDLDNKDGEVYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFD 943
Cdd:cd10523    161 ENEVEVVTSWLILSKKRKLRENVCFLDASKEGNVGRFLNHSCCPNLFVQNVFVDTHDKNFPWVAFFTNRVVKAGTELTWD 240
                          250       260
                   ....*....|....*....|...
gi 1907121895  944 YGDRFWDIKSKYFTCQCGSEKCK 966
Cdd:cd10523    241 YSYDAGTSPEQEIPCLCGVNKCQ 263
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
828-950 2.44e-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: 144.78  E-value: 2.44e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895   828 VRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRE--------DDSYLFDLDNKdgevYCIDARYYGNISR 899
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPkaydtdgaKAFYLFDIDSD----LCIDARRKGNLAR 76
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1907121895   900 FINHLCDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWD 950
Cdd:smart00317   77 FINHSCEPNCELLFVEVNGDD----RIVIFALRDIKPGEELTIDYGSDYAN 123
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
830-966 3.51e-35

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: 130.45  E-value: 3.51e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  830 LQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED--------DSYLFDLdnKDGEVycIDARYYGNISRFI 901
Cdd:cd10531      2 LELFRTEKKGWGVKAKEDIQKGEFIIEYVGEVIDKKEFKERLDeyeelgksNFYILSL--SDDVV--IDATRKGNLSRFI 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907121895  902 NHLCDPNIIPVRVFMLHQdlrfPRIAFFSSRDIRTGEELGFDYG-DRFWDIKSKyftCQCGSEKCK 966
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), ...
818-966 4.63e-33

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


Pssm-ID: 380916  Cd Length: 150  Bit Score: 125.02  E-value: 4.63e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  818 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED--------DSYLFDLDNKdgevYCI 889
Cdd:cd10518      4 RFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKrydeegggGTYMFRIDED----LVI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  890 DARYYGNISRFINHLCDPN----IIPVRVFMlhqdlrfpRIAFFSSRDIRTGEELGFDYgdRFWDIKSKYFTCQCGSEKC 965
Cdd:cd10518     80 DATKKGNIARFINHSCDPNcyakIITVDGEK--------HIVIFAKRDIAPGEELTYDY--KFPIEDEEKIPCLCGAPNC 149

                   .
gi 1907121895  966 K 966
Cdd:cd10518    150 R 150
PreSET smart00468
N-terminal to some SET domains; A Cys-rich putative Zn2+-binding domain that occurs N-terminal ...
713-812 6.03e-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: 119.83  E-value: 6.03e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895   713 CRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSN-CLCGQLSIRCW-YDKDG 790
Cdd:smart00468    1 CLDISNGKENVPVPLVNEVDEDPPPPDFEYISEYIYGQGVPIDRSPSPLVGCSCSGDCSSSNkCECARKNGGEFaYELNG 80
                            90       100
                    ....*....|....*....|..
gi 1907121895   791 RllqeFNKIEPPLIFECNQACS 812
Cdd:smart00468   81 G----LRLKRKPLIYECNSRCS 98
SET_EZH cd10519
SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...
829-946 1.32e-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: 1.32e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  829 RLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRE---DD---SYLFDLDNKdgevYCIDARYYGNISRFIN 902
Cdd:cd10519      2 RLLLGKSDVAGWGLFLKEPIKKDEFIGEYTGELISQDEADRRGkiyDKynsSYLFNLNDQ----FVVDATRKGNKIRFAN 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907121895  903 HLCDPNIIPvRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDYGD 946
Cdd:cd10519     78 HSSNPNCYA-KVMMVNGD---HRIGIFAKRDIEAGEELFFDYGY 117
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
830-966 1.76e-31

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: 120.09  E-value: 1.76e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  830 LQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNkdgevYC--------IDARYYGNISRFI 901
Cdd:cd19174      2 LERFRTEDKGWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRMIEQYHNHSHH-----YClnldsgmvIDGYRMGNEARFV 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907121895  902 NHLCDPNIIPVRVFMLHQdlrfPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYfTCQCGSEKCK 966
Cdd:cd19174     77 NHSCDPNCEMQKWSVNGV----YRIGLFALKDIPAGEELTYDYNFHSFNVEKQQ-PCKCGSPNCR 136
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
839-945 1.79e-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: 116.08  E-value: 1.79e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  839 GWGVRALQTIPQGTFICEYVGE-LISDAEADVRED-----------DSYLFDLDNKDGevYCIDAR--YYGNISRFINHL 904
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELlyydklelrlwGPYLFTLDEDSE--YCIDARalYYGNWARFINHS 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1907121895  905 CDPNIIPVRVFMlhqdLRFPRIAFFSSRDIRTGEELGFDYG 945
Cdd:pfam00856   79 CDPNCEVRVVYV----NGGPRIVIFALRDIKPGEELTIDYG 115
SET_SETD2 cd19172
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...
829-966 6.34e-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: 115.76  E-value: 6.34e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  829 RLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAE--------ADVREDDSYLFDLDNKDgevyCIDARYYGNISRF 900
Cdd:cd19172      3 KVEVFRTEKKGWGLRAAEDLPKGTFVIEYVGEVLDEKEfkrrmkeyAREGNRHYYFMALKSDE----IIDATKKGNLSRF 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907121895  901 INHLCDPNIIpVRVFMLHQDLrfpRIAFFSSRDIRTGEELGFDYG-DRFWDIKSKyftCQCGSEKCK 966
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 ...
716-820 1.80e-28

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


Pssm-ID: 461530 [Multi-domain]  Cd Length: 99  Bit Score: 109.82  E-value: 1.80e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  716 VARGYENVPIPCVNGVDGEPCPEDYKYISENCETSTMNIDRnithLQHCTCvDDCSSSNCLCGQLS---IRCWYDKDGRL 792
Cdd:pfam05033    1 ISKGKENVPIPVVNEVDDEPPPPDFTYITSYIYPKEFLLII----PQGCDC-GDCSSEKCSCAQLNggeFRFPYDKDGLL 75
                           90       100
                   ....*....|....*....|....*...
gi 1907121895  793 LQEfnkiEPPLIFECNQACSCWRSCKNR 820
Cdd:pfam05033   76 VPE----SKPPIYECNPLCGCPPSCPNR 99
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
826-967 2.38e-28

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 110.82  E-value: 2.38e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  826 IKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDS-----YLFDLDNKDGevycIDARYYGNISRF 900
Cdd:COG2940      4 LHPRIEVRPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKeplhtYLFELDDDGV----IDGALGGNPARF 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907121895  901 INHLCDPNIIPVRvfmlhqdlRFPRIAFFSSRDIRTGEELGFDYGDRFWDiksKYFTCQCGseKCKH 967
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, ...
828-965 3.62e-25

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


Pssm-ID: 380950 [Multi-domain]  Cd Length: 142  Bit Score: 102.01  E-value: 3.62e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  828 VRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR--------EDDSYLFDLDNKdgevYCIDARYYGNISR 899
Cdd:cd19173      2 PPTEPFKTGDRGWGLRTKRDIKKGDFVIEYVGELIDEEECRRRlkkahennITNFYMLTLDKD----RIIDAGPKGNLSR 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907121895  900 FINHLCDPNiIPVRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDYG-DRFWDIKSKyftCQCGSEKC 965
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 ...
829-966 7.61e-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: 100.95  E-value: 7.61e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  829 RLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR--------EDDSYLFDLDnKDgevYCIDARYYGNISRF 900
Cdd:cd19175      1 KMKLVKTEKCGWGLVADEDINAGEFIIEYVGEVIDDKTCEERlwdmkhkgEKNFYMCEID-KD---MVIDATFKGNLSRF 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907121895  901 INHLCDPNIIpVRVFMLHQDLrfpRIAFFSSRDIRTGEELGFDYgdRFWDIKSKYfTCQCGSEKCK 966
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 ...
827-966 1.91e-24

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: 100.19  E-value: 1.91e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  827 KVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED--------DSYLFDLDnkdgEVYCIDARYYGNIS 898
Cdd:cd20072     12 KKQLKFARSAIHNWGLYAMENISAKDMVIEYVGEVIRQQVADEREKrylrqgigSSYLFRID----DDTVVDATKKGNIA 87
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907121895  899 RFINHLCDPNIIpVRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDYgdRFwDIKSKYFTCQCGSEKCK 966
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. ...
820-947 2.53e-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: 99.57  E-value: 2.53e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  820 RVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRE--------DDSYLFDLDNKdGEVYCIDA 891
Cdd:cd10528      9 ELILSGKEEGLKVIEIDGKGRGVIATRPFEKGDFVVEYHGDLITITEAKKREalyakdpsTGCYMYYFQYK-GKTYCVDA 87
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907121895  892 -RYYGNISRFINHLC-DPNIIPVRVFMlhQDLrfPRIAFFSSRDIRTGEELGFDYGDR 947
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 ...
839-948 5.18e-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: 5.18e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  839 GWGVRALQTIPQGTFICEYVGELISDAEADVRE------DDSYLFDLDNKdgevYCIDARYYGNISRFINHLCDP----N 908
Cdd:cd19168     13 GLGLFAAEDIKEGEFVIEYTGELISHDEGVRREhrrgdvSYLYLFEEQEG----IWVDAAIYGNLSRYINHATDKvktgN 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1907121895  909 IIPVRVFMLHQdlrfPRIAFFSSRDIRTGEELGFDYGDRF 948
Cdd:cd19168     89 CMPKIMYVNHE----WRIKFTAIKDIKIGEELFFNYGDNF 124
SET_SETD1 cd19169
SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...
827-966 1.31e-23

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


Pssm-ID: 380946  Cd Length: 148  Bit Score: 97.79  E-value: 1.31e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  827 KVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED--------DSYLFDLDnkdgEVYCIDARYYGNIS 898
Cdd:cd19169     12 KKQLKFAKSRIHDWGLFALEPIAADEMVIEYVGQVIRQSVADEREKryeaigigSSYLFRVD----DDTIIDATKCGNLA 87
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907121895  899 RFINHLCDPN----IIPVRvfmlhqdlRFPRIAFFSSRDIRTGEELGFDYgdRFwDIKSKYFTCQCGSEKCK 966
Cdd:cd19169     88 RFINHSCNPNcyakIITVE--------SQKKIVIYSKRPIAVNEEITYDY--KF-PIEDEKIPCLCGAPQCR 148
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
839-950 1.44e-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: 1.44e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  839 GWGVRALQTIPQGTFICEYVGELISDAEADVR----EDDSYLFDLDnkDGEVYcIDARYYGNISRFINHLCDPNIIPVrv 914
Cdd:cd10522     14 GLGLFAAETIAKGEFVGEYTGEVLDRWEEDRDsvyhYDPLYPFDLN--GDILV-IDAGKKGNLTRFINHSDQPNLELI-- 88
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1907121895  915 FMLHQDLrfPRIAFFSSRDIRTGEELGFDYGDRFWD 950
Cdd:cd10522     89 VRTLKGE--QHIGFVAIRDIKPGEELFISYGPKYWK 122
Ank_2 pfam12796
Ankyrin repeats (3 copies);
512-605 2.30e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 2.30e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  512 LMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLStgQVDVNAQDSGgWTPIIWAAEHKHIDVI 591
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNG-RTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 1907121895  592 RMLLTRGADVTLTD 605
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
444-666 2.64e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.81  E-value: 2.64e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  444 LYLSVKQGELQKVILMLLDNLDPNFQSDQQSkrTPLHAAAQKGSV-----EICHVLLQAGANINAVDKQQRTPLMEAVVN 518
Cdd:PHA03100    39 LYLAKEARNIDVVKILLDNGADINSSTKNNS--TPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISK 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  519 --NHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIG--NLEMVSLLLSTGqVDVNAqdsggwtpiiwaaehkhIDVIRML 594
Cdd:PHA03100   117 ksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNkiDLKILKLLIDKG-VDINA-----------------KNRVNYL 178
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907121895  595 LTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGAN 666
Cdd:PHA03100   179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
SET_KMT2A_2B cd19170
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...
820-966 3.98e-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: 90.91  E-value: 3.98e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  820 RVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED--DS-----YLFDLDnkdgEVYCIDAR 892
Cdd:cd19170      6 RHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKyyESkgigcYMFRID----DDEVVDAT 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907121895  893 YYGNISRFINHLCDPN----IIPVrvfmlhqDLRfPRIAFFSSRDIRTGEELGFDYGDRFWDIKskyFTCQCGSEKCK 966
Cdd:cd19170     82 MHGNAARFINHSCEPNcysrVVNI-------DGK-KHIVIFALRRILRGEELTYDYKFPIEDVK---IPCTCGSKKCR 148
Ank_2 pfam12796
Ankyrin repeats (3 copies);
479-572 1.61e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 1.61e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  479 LHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQlgGCVYSKEEDGSTCLHHAAKIGNLEMVS 558
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|....
gi 1907121895  559 LLLSTGqVDVNAQD 572
Cdd:pfam12796   79 LLLEKG-ADINVKD 91
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
827-966 1.92e-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: 1.92e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  827 KVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDS-------YLFDLDNKdgevYCIDARYYGNISR 899
Cdd:cd19171     13 RSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYesqnrgiYMFRIDND----WVIDATMTGGPAR 88
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907121895  900 FINHLCDPNIIpVRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKyFTCQCGSEKCK 966
Cdd:cd19171     89 YINHSCNPNCV-AEVVTFDKE---KKIIIISNRRIAKGEELTYDYKFDFEDDQHK-IPCLCGAPNCR 150
PHA03100 PHA03100
ankyrin repeat protein; Provisional
452-676 3.97e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 91.27  E-value: 3.97e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  452 ELQKVILMLLDNLDPNFQSdqqsKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNH-----LEVARY 526
Cdd:PHA03100    16 KNIKYIIMEDDLNDYSYKK----PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  527 MVQLGGCVYSKEEDGSTCLHHAA--KIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHID--VIRMLLTRGADVT 602
Cdd:PHA03100    92 LLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDIN 170
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907121895  603 LTDNeeniclhwasftgsaaiAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDT 676
Cdd:PHA03100   171 AKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
SET_NSD2 cd19211
SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...
831-965 1.70e-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: 1.70e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  831 QLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR-----EDDS---YLFDLDnKDgevYCIDARYYGNISRFIN 902
Cdd:cd19211      5 KIIKTEGKGWGLIAKRDIKKGEFVNEYVGELIDEEECMARikhahENDIthfYMLTID-KD---RIIDAGPKGNYSRFMN 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907121895  903 HLCDPNiIPVRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDYG-DRFWDIKSkyfTCQCGSEKC 965
Cdd:cd19211     81 HSCQPN-CETQKWTVNGD---TRVGLFAVCDIPAGTELTFNYNlDCLGNEKT---VCRCGAPNC 137
SET_EZH2 cd19218
SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...
825-944 7.89e-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: 7.89e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  825 GIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDD------SYLFDLDNKdgevYCIDARYYGNIS 898
Cdd:cd19218      1 GSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVydkymcSFLFNLNND----FVVDATRKGNKI 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1907121895  899 RFINHLCDPNIIpVRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDY 944
Cdd:cd19218     77 RFANHSVNPNCY-AKVMMVNGD---HRIGIFAKRAIQTGEELFFDY 118
SET_SETD5-like cd10529
SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...
841-944 1.26e-17

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: 80.01  E-value: 1.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  841 GVRALQTIPQGTFICEYVGE--LISDAEADVRED---DSYLFDLDNKDGEVYCIDARYYGNISRFINHLCDPNiipVRV- 914
Cdd:cd10529     18 GLVATEDISPGEPILEYKGEvsLRSEFKEDNGFFkrpSPFVFFYDGFEGLPLCVDARKYGNEARFIRRSCRPN---AELr 94
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1907121895  915 FMLHQDLRFpRIAFFSSRDIRTGEE--LGFDY 944
Cdd:cd10529     95 HVVVSNGEL-RLFIFALKDIRKGTEitIPFDY 125
SET_EZH1 cd19217
SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43) ...
823-944 1.65e-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: 1.65e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  823 QSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED------DSYLFDLDNKdgevYCIDARYYGN 896
Cdd:cd19217      1 QRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKvydkymSSFLFNLNND----FVVDATRKGN 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1907121895  897 ISRFINHLCDPNIIpVRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDY 944
Cdd:cd19217     77 KIRFANHSVNPNCY-AKVVMVNGD---HRIGIFAKRAIQQGEELFFDY 120
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
830-965 4.33e-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: 78.82  E-value: 4.33e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  830 LQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR-----EDD---SYLFDLDnKDgevYCIDARYYGNISRFI 901
Cdd:cd19210      4 VEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIDEEECRARiryaqEHDitnFYMLTLD-KD---RIIDAGPKGNYARFM 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907121895  902 NHLCDPNiIPVRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDYgdRFWDIKSKYFTCQCGSEKC 965
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) ...
832-966 4.71e-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: 79.30  E-value: 4.71e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  832 LYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRE---DDS----YLFDLDnkDGEVycIDARYYGNISRFINHL 904
Cdd:cd19206     18 VYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREkyyDSKgigcYMFRID--DSEV--VDATMHGNAARFINHS 93
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907121895  905 CDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWDIKSKyFTCQCGSEKCK 966
Cdd:cd19206     94 CEPNCYSRVINIDGQK----HIVIFAMRKIYRGEELTYDYKFPIEDASNK-LPCNCGAKKCR 150
Ank_2 pfam12796
Ankyrin repeats (3 copies);
579-671 4.99e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 4.99e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  579 IIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNaQCDLHAVNYhGDTPLHIAARESYHDCVL 658
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1907121895  659 LFLSRGANPELRN 671
Cdd:pfam12796   79 LLLEKGADINVKD 91
SET_SETD1A cd19204
SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...
827-966 7.14e-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: 7.14e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  827 KVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED--------DSYLFDLDNKDgevyCIDARYYGNIS 898
Cdd:cd19204     13 KKKLRFGRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQVVADMREKryvqegigSSYLFRVDHDT----IIDATKCGNLA 88
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907121895  899 RFINHLCDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGdrfWDIKSKYFTCQCGSEKCK 966
Cdd:cd19204     89 RFINHCCTPNCYAKVITIESQK----KIVIYSKQPIGVNEEITYDYK---FPIEDNKIPCLCGTENCR 149
SET_NSD3 cd19212
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
831-965 1.16e-16

SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing protein 3 (NSD3) and similar proteins; NSD3 (EC 2.1.1.43; also termed protein whistle, WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1L1), or WHSC1-like protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-4' and 'Lys-27' of histone H3. NSD3 is amplified and overexpressed in multiple cancer types, including acute myeloid leukemia (AML), breast, lung, pancreatic and bladder cancers, as well as squamous cell carcinoma of the head and neck (SCCHN). NSD3 contributes to tumorigenesis by interacting with bromodomain-containing protein 4 (BRD4), the bromodomain and extraterminal (BET) protein, which is a potential therapeutic target in acute myeloid leukemia (AML). NSD3 is amplified in primary tumors and cell lines from breast carcinoma, and can promote the cell viability of small-cell lung cancer and pancreatic ductal adenocarcinoma. High NSD3 expression is implicated in poor grade and heavy smoking history in SCCHN. Thus, NSD3 may serve as a potential druggable target for selective cancer therapy.


Pssm-ID: 380989 [Multi-domain]  Cd Length: 142  Bit Score: 77.66  E-value: 1.16e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  831 QLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDN-------KDgevYCIDARYYGNISRFINH 903
Cdd:cd19212      5 EIIKTERRGWGLRTKRSIKKGEFVNEYVGELIDEEECRLRIKRAHENSVTNfymltvtKD---RIIDAGPKGNYSRFMNH 81
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907121895  904 LCDPNiIPVRVFMLHQDLrfpRIAFFSSRDIRTGEELGFDYG-DRFWDIKSKyftCQCGSEKC 965
Cdd:cd19212     82 SCNPN-CETQKWTVNGDV---RVGLFALCDIPAGMELTFNYNlDCLGNGRTE---CHCGADNC 137
PHA03095 PHA03095
ankyrin-like protein; Provisional
476-669 5.64e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 81.99  E-value: 5.64e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  476 RTPLHA-----AAQKGSVEIchvLLQAGANINAVDKQQRTPLMEAVVNNH--LEVARYMVQLGGCVYSKEEDGSTCLHHA 548
Cdd:PHA03095   118 RTPLHVylsgfNINPKVIRL---LLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHHH 194
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  549 A---KIGNlEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEH---KHIdVIRMLLTRGADVTLTDNEENICLHWASFTGSAA 622
Cdd:PHA03095   195 LqsfKPRA-RIVRELIRAG-CDPAATDMLGNTPLHSMATGsscKRS-LVLPLLIAGISINARNRYGQTPLHYAAVFNNPR 271
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1907121895  623 IAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPEL 669
Cdd:PHA03095   272 ACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAET 318
PHA03095 PHA03095
ankyrin-like protein; Provisional
441-677 6.84e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 81.61  E-value: 6.84e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  441 PRQLYLSVKQGELQKVILMLLDN-LDPNFQSdqQSKRTPLHAAAQKGSVE-ICHVLLQAGANINAVDKQQRTPLME--AV 516
Cdd:PHA03095    50 PLHLYLHYSSEKVKDIVRLLLEAgADVNAPE--RCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVylSG 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  517 VNNHLEVARYMVQLGGCVYSKEEDGSTCLH-----HAAkigNLEMVSLLLSTGqVDVNAQDSGGWTPIiwaaeHKHID-- 589
Cdd:PHA03095   128 FNINPKVIRLLLRKGADVNALDLYGMTPLAvllksRNA---NVELLRLLIDAG-ADVYAVDDRFRSLL-----HHHLQsf 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  590 -----VIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEV--LLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLS 662
Cdd:PHA03095   199 kprarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIA 278
                          250
                   ....*....|....*
gi 1907121895  663 RGANPELRNKEGDTA 677
Cdd:PHA03095   279 LGADINAVSSDGNTP 293
PHA02876 PHA02876
ankyrin repeat protein; Provisional
448-677 1.08e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 81.65  E-value: 1.08e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  448 VKQGELQKVILMLLDNLDPNfqSDQQSKRTPLHAAAQKGSVEICHVLLQAGANIN------------AVD---------- 505
Cdd:PHA02876   153 IQQDELLIAEMLLEGGADVN--AKDIYCITPIHYAAERGNAKMVNLLLSYGADVNiialddlsvlecAVDsknidtikai 230
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  506 -------KQQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNL-EMVSLLLSTGqVDVNAQDSGGWT 577
Cdd:PHA02876   231 idnrsniNKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERG-ADVNAKNIKGET 309
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  578 PIIWAAEHKH-IDVIRMLLTRGADVTLTDNEENICLHWAS-FTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHD 655
Cdd:PHA02876   310 PLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVV 389
                          250       260
                   ....*....|....*....|..
gi 1907121895  656 CVLLFLSRGANPELRNKEGDTA 677
Cdd:PHA02876   390 IINTLLDYGADIEALSQKIGTA 411
PHA02874 PHA02874
ankyrin repeat protein; Provisional
477-676 2.53e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.62  E-value: 2.53e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  477 TPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGgcvyskeEDGST----CLhhaakig 552
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG-------VDTSIlpipCI------- 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  553 NLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNAQC 632
Cdd:PHA02874   103 EKDMIKTILDCG-IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1907121895  633 DLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDT 676
Cdd:PHA02874   182 YANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFT 225
SET_KMT2C cd19208
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) ...
815-966 6.51e-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: 73.12  E-value: 6.51e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  815 RSCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED-------DSYLFDLDNKdgevY 887
Cdd:cd19208      2 KSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKlyesqnrGVYMFRIDND----H 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907121895  888 CIDARYYGNISRFINHLCDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWDIKSKyFTCQCGSEKCK 966
Cdd:cd19208     78 VIDATLTGGPARYINHSCAPNCVAEVVTFEKGH----KIIISSSRRIQKGEELCYDYKFDFEDDQHK-IPCHCGAVNCR 151
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
476-602 7.34e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 79.14  E-value: 7.34e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  476 RTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCvySKEEDGSTCLHHAAKIGNLE 555
Cdd:PLN03192   559 RTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASI--SDPHAAGDLLCTAAKRNDLT 636
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1907121895  556 MVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIDVIRMLLTRGADVT 602
Cdd:PLN03192   637 AMKELLKQG-LNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVD 682
SET_SETD1B cd19205
SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...
827-966 8.64e-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: 72.78  E-value: 8.64e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  827 KVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED--------DSYLFDLDNKDgevyCIDARYYGNIS 898
Cdd:cd19205     13 KKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKryedegigSSYMFRVDHDT----IIDATKCGNFA 88
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907121895  899 RFINHLCDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGdrfWDIKSKYFTCQCGSEKCK 966
Cdd:cd19205     89 RFINHSCNPNCYAKVITVESQK----KIVIYSKQHINVNEEITYDYK---FPIEDVKIPCLCGSENCR 149
SET_SpSET3-like cd19183
SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...
830-989 2.60e-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: 72.05  E-value: 2.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  830 LQLYRTAKMGW-GVRALQTIPQGTFICEYVGELISDAEADVREDDSY----------LFDldnkDGEVYCIDARYYGNIS 898
Cdd:cd19183      3 ISSIGLANASRfGLFADRPIPAGDPIQELLGEIGLQSEYIADPENQYqilgapkphvFFH----PQSPLYIDTRRSGSVA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  899 RFINHLCDPN--IIPVRVfmlhQDLRFPRIAFFSSRDIRTGEELGFDYGdrfWDIkskyftcqcgsekcKHSAEAIALEQ 976
Cdd:cd19183     79 RFIRRSCRPNaeLVTVAS----DSGSVLKFVLYASRDISPGEEITIGWD---WDN--------------PHPFRRFALGE 137
                          170
                   ....*....|...
gi 1907121895  977 SRLARLDPHPELL 989
Cdd:cd19183    138 LVPSNLDLEQHLL 150
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
829-945 2.62e-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: 68.43  E-value: 2.62e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  829 RLQLYRTAKMGWGVRALQTIPQGTFICeyvgelisdaeadvreddsylfdldnkdgevycidaryygnISRFINHLCDPN 908
Cdd:cd08161      1 EIRPSTIPGAGFGLFATRDIPKGEVIG-----------------------------------------LARFINHSCEPN 39
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907121895  909 IIPVRVFmlhqDLRFPRIAFFSSRDIRTGEELGFDYG 945
Cdd:cd08161     40 CEFEEVY----VGGKPRVFIVALRDIKAGEELTVDYG 72
SET_KMT2D cd19209
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...
815-966 3.31e-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: 71.27  E-value: 3.31e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  815 RSCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED-------DSYLFDLDNKdgevY 887
Cdd:cd19209      3 KSSQYRRLKTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKiyeeqnrGIYMFRINNE----H 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907121895  888 CIDARYYGNISRFINHLCDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWDIKSKyFTCQCGSEKCK 966
Cdd:cd19209     79 VIDATLTGGPARYINHSCAPNCVAEVVTFDKED----KIIIISSRRIPKGEELTYDYQFDFEDDQHK-IPCHCGAWNCR 152
Ank_2 pfam12796
Ankyrin repeats (3 copies);
444-531 4.26e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 4.26e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  444 LYLSVKQGELQKVILMLLDNLDPNFQSdqQSKRTPLHAAAQKGSVEICHVLLQaGANINAVDkQQRTPLMEAVVNNHLEV 523
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQD--KNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEI 76

                   ....*...
gi 1907121895  524 ARYMVQLG 531
Cdd:pfam12796   77 VKLLLEKG 84
PHA02878 PHA02878
ankyrin repeat protein; Provisional
431-674 4.98e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 75.69  E-value: 4.98e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  431 SERRKKLRFHPRQLYLSvkqgelqKVILmlLDNLDPNFQSDQQSKRTPLHAAAQKgsVEICHVLLQAGANINAVDKQQ-R 509
Cdd:PHA02878   101 TLVAIKDAFNNRNVEIF-------KIIL--TNRYKNIQTIDLVYIDKKSKDDIIE--AEITKLLLSYGADINMKDRHKgN 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  510 TPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGQvDVNAQDSGGWTPIIWAAEH-KHI 588
Cdd:PHA02878   170 TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA-STDARDKCGNTPLHISVGYcKDY 248
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  589 DVIRMLLTRGADVTLTDNEENIC-LHWAsfTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESY----------HDCV 657
Cdd:PHA02878   249 DILKLLLEHGVDVNAKSYILGLTaLHSS--IKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLcinigrilisNICL 326
                          250
                   ....*....|....*..
gi 1907121895  658 LLFLsrgaNPELRNKEG 674
Cdd:PHA02878   327 LKRI----KPDIKNSEG 339
SET_KMT2B cd19207
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...
832-966 7.41e-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: 70.05  E-value: 7.41e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  832 LYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED-------DSYLFDLDNKDgevyCIDARYYGNISRFINHL 904
Cdd:cd19207     18 VYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKfydskgiGCYMFRIDDFD----VVDATMHGNAARFINHS 93
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907121895  905 CDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWDIKSKyFTCQCGSEKCK 966
Cdd:cd19207     94 CEPNCYSRVIHVEGQK----HIVIFALRKIYRGEELTYDYKFPIEDASNK-LPCNCGAKRCR 150
PHA03095 PHA03095
ankyrin-like protein; Provisional
487-677 9.38e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 74.68  E-value: 9.38e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  487 SVEICHVLLQAGANINAVDKQQRTPL---MEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGN-LEMVSLLLS 562
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIK 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  563 TGqVDVNAQDSGGWTPIiwaaeHKHI-------DVIRMLLTRGADVTLTDNEENICLH-WASFTG-SAAIAEVLLNAQCD 633
Cdd:PHA03095   106 AG-ADVNAKDKVGRTPL-----HVYLsgfninpKVIRLLLRKGADVNALDLYGMTPLAvLLKSRNaNVELLRLLIDAGAD 179
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1907121895  634 LHAVNYHGDTPLHIAAR--ESYHDCVLLFLSRGANPELRNKEGDTA 677
Cdd:PHA03095   180 VYAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTP 225
PHA02874 PHA02874
ankyrin repeat protein; Provisional
444-607 1.19e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 74.23  E-value: 1.19e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  444 LYLSVKQGELQKVILMLLDNLDPNFQSDQQSkrTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEV 523
Cdd:PHA02874   128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGC--YPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  524 ARYMVQLGGCVYSKEEDGSTCLHHAAkIGNLEMVSLLLSTGQvdVNAQDSGGWTPIIWAAEHK-HIDVIRMLLTRGADVT 602
Cdd:PHA02874   206 IKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLINNAS--INDQDIDGSTPLHHAINPPcDIDIIDILLYHKADIS 282

                   ....*
gi 1907121895  603 LTDNE 607
Cdd:PHA02874   283 IKDNK 287
PHA02876 PHA02876
ankyrin repeat protein; Provisional
475-666 3.46e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.56  E-value: 3.46e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  475 KRTPLHAAAQKGSV-EICHVLLQAGANINAVDKQQRTPLMEAVVNNH-LEVARYMVQLGGCVYSKEEDGSTCLHHAAKIG 552
Cdd:PHA02876   273 KNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLD 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  553 -NLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWASF-TGSAAIAEVLLNA 630
Cdd:PHA02876   353 rNKDIVITLLELG-ANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCgTNPYMSVKTLIDR 431
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1907121895  631 QCDLHAVNYHGDTPLHIAARESYH-DCVLLFLSRGAN 666
Cdd:PHA02876   432 GANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGAD 468
PHA02875 PHA02875
ankyrin repeat protein; Provisional
444-666 4.94e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.25  E-value: 4.94e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  444 LYLSVKQGELQKVILMLLDNLDPNFQsdQQSKRTPLHAAAQKGSVEICHVLLQAGANINAV-DKQQRTPLMEAVVNNHLE 522
Cdd:PHA02875    39 IKLAMKFRDSEAIKLLMKHGAIPDVK--YPDIESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLD 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  523 VARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTgQVDVNAQDSGGWTPIIWAAEHKHIDVIRMLLTRGADVt 602
Cdd:PHA02875   117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH-KACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI- 194
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907121895  603 ltdneeniclhwasftgsaaiaevllnaqcdlhavNYHGDTP----LHIAARESYHDCVLLFLSRGAN 666
Cdd:PHA02875   195 -----------------------------------DYFGKNGcvaaLCYAIENNKIDIVRLFIKRGAD 227
PHA02875 PHA02875
ankyrin repeat protein; Provisional
443-628 6.27e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 68.86  E-value: 6.27e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  443 QLYLSVKQGELQKVILMLLDNldpNFQSDQQSKR--TPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNH 520
Cdd:PHA02875    71 ELHDAVEEGDVKAVEELLDLG---KFADDVFYKDgmTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGD 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  521 LEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGQVDVNAQDSGGWTPIIWAAEHKHIDVIRMLLTRGAD 600
Cdd:PHA02875   148 IKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1907121895  601 ---VTLTDNEE--------NICLHWASFTGSAAIAEVLL 628
Cdd:PHA02875   228 cniMFMIEGEEctildmicNMCTNLESEAIDALIADIAI 266
PHA03095 PHA03095
ankyrin-like protein; Provisional
518-669 2.71e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.97  E-value: 2.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  518 NNHLEVARYMVQLGGCVYSKEEDGSTCLH---HAAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKH-IDVIRM 593
Cdd:PHA03095    24 NVTVEEVRRLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAG-ADVNAPERCGFTPLHLYLYNATtLDVIKL 102
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907121895  594 LLTRGADVTLTDNEENICLH--WASFTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIaaresyhdcvlLFLSRGANPEL 669
Cdd:PHA03095   103 LIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAV-----------LLKSRNANVEL 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
476-528 2.91e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.21  E-value: 2.91e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907121895  476 RTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMV 528
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
476-677 3.07e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.55  E-value: 3.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  476 RTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLE 555
Cdd:PHA02875     3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  556 MVSLLLSTGQV--DVNAQDsgGWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNAQCD 633
Cdd:PHA02875    83 AVEELLDLGKFadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1907121895  634 LHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTA 677
Cdd:PHA02875   161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVA 204
Ank_4 pfam13637
Ankyrin repeats (many copies);
541-595 3.18e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.21  E-value: 3.18e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907121895  541 GSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIDVIRMLL 595
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
471-674 8.33e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 65.37  E-value: 8.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  471 DQQSKrTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAK 550
Cdd:PHA02874   121 DAELK-TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  551 IGNLEMVSLLLSTGQvDVNAQDSGGWTPIIWAAEHKHIDVirMLLTRGADVTLTDNEENICLHWA-SFTGSAAIAEVLLN 629
Cdd:PHA02874   200 YGDYACIKLLIDHGN-HIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAiNPPCDIDIIDILLY 276
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907121895  630 AQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSrgANPELRNKEG 674
Cdd:PHA02874   277 HKADISIKDNKGENPIDTAFKYINKDPVIKDII--ANAVLIKEAD 319
Ank_4 pfam13637
Ankyrin repeats (many copies);
508-561 4.20e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 4.20e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907121895  508 QRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLL 561
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
555-677 4.29e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.89  E-value: 4.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  555 EMVSLLLSTGQVDVNAQDSGGWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNAQCDL 634
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1907121895  635 HAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTA 677
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123
PHA02876 PHA02876
ankyrin repeat protein; Provisional
489-666 5.63e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.16  E-value: 5.63e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  489 EIC-HVLLQA--GANI--NAVDK--QQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLL 561
Cdd:PHA02876   119 EACiHILKEAisGNDIhyDKINEsiEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLL 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  562 STGqVDVNAQDSGGWTPIIWAAEHKHIDVIR-----------------------------MLLTRGADVTLTDNEENICL 612
Cdd:PHA02876   199 SYG-ADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsninkndlsllkairnedletslLLYDAGFSVNSIDDCKNTPL 277
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907121895  613 HWASFTGS-AAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYH-DCVLLFLSRGAN 666
Cdd:PHA02876   278 HHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGAD 333
PHA03100 PHA03100
ankyrin repeat protein; Provisional
455-601 5.71e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 62.76  E-value: 5.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  455 KVILMLLDN-LDPNFQSDQQSkrTPLHAAAQK--GSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNH--LEVAR---- 525
Cdd:PHA03100    87 EIVKLLLEYgANVNAPDNNGI--TPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKllid 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  526 ------------YMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIDVIRM 593
Cdd:PHA03100   165 kgvdinaknrvnYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLG-ANPNLVNKYGDTPLHIAILNNNKEIFKL 243

                   ....*...
gi 1907121895  594 LLTRGADV 601
Cdd:PHA03100   244 LLNNGPSI 251
PHA02798 PHA02798
ankyrin-like protein; Provisional
487-608 6.46e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 62.93  E-value: 6.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  487 SVEICHVLLQAGANINAVDKQQRTPLMEAVVN----NH-LEVARYMVQLGGCVYSKEEDGST---CLHHAAKIGNLEMVS 558
Cdd:PHA02798    50 STDIVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHmLDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILL 129
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907121895  559 LLLSTGqVDVNAQDSGGWTPI---IWAAEHKHIDVIRMLLTRGADVTLTDNEE 608
Cdd:PHA02798   130 FMIENG-ADTTLLDKDGFTMLqvyLQSNHHIDIEIIKLLLEKGVDINTHNNKE 181
PHA03100 PHA03100
ankyrin repeat protein; Provisional
517-666 1.01e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.99  E-value: 1.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  517 VNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHI-----DVI 591
Cdd:PHA03100    11 RIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNG-ADINSSTKNNSTPLHYLSNIKYNltdvkEIV 89
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907121895  592 RMLLTRGADVTLTDNEENICLHWASFT--GSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHD--CVLLFLSRGAN 666
Cdd:PHA03100    90 KLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVD 168
PHA03100 PHA03100
ankyrin repeat protein; Provisional
440-564 1.38e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.60  E-value: 1.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  440 HPRQLYLSVKQGELqKVILMLLDNlDPNFQSDQQSKRTPLHAAAQ--KGSVEICHVLLQAGANINA-------------- 503
Cdd:PHA03100   108 TPLLYAISKKSNSY-SIVEYLLDN-GANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKGVDINAknrvnyllsygvpi 185
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907121895  504 --VDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTG 564
Cdd:PHA03100   186 niKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
PHA02876 PHA02876
ankyrin repeat protein; Provisional
455-601 1.68e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.62  E-value: 1.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  455 KVILMLLDNLDPNFQSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAV--VNNHLEVaRYMVQLGG 532
Cdd:PHA02876   355 KDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALcgTNPYMSV-KTLIDRGA 433
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  533 CVYSKEEDGSTCLHHAAKIG-NLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIdvIRMLLTRGADV 601
Cdd:PHA02876   434 NVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNG-ADVNAINIQNQYPLLIALEYHGI--VNILLHYGAEL 500
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
506-647 6.58e-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: 6.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  506 KQQR---TPLMEAVVNNHLEVARYMVQLGGC-VYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGQVDVNAQDSG----GWT 577
Cdd:cd22192     12 QQKRiseSPLLLAAKENDVQAIKKLLKCPSCdLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSdlyqGET 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  578 PIIWAAEHKHIDVIRMLLTRGADVT--------LTDNEENIC------LHWASFTGSAAIAEVLLNAQCDLHAVNYHGDT 643
Cdd:cd22192     92 ALHIAVVNQNLNLVRELIARGADVVspratgtfFRPGPKNLIyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171

                   ....
gi 1907121895  644 PLHI 647
Cdd:cd22192    172 VLHI 175
PHA02878 PHA02878
ankyrin repeat protein; Provisional
478-676 7.52e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.12  E-value: 7.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  478 PLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQlggcVYSKEEDGST--CLHHAAKIGNLE 555
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR----SINKCSVFYTlvAIKDAFNNRNVE 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  556 MVSLLLSTG-----QVDVNAQDSGGWTPIIWAaehkhiDVIRMLLTRGADVTLTD-NEENICLHWASFTGSAAIAEVLLN 629
Cdd:PHA02878   116 IFKIILTNRykniqTIDLVYIDKKSKDDIIEA------EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLS 189
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1907121895  630 AQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDT 676
Cdd:PHA02878   190 YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236
Ank_2 pfam12796
Ankyrin repeats (3 copies);
424-505 9.76e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.58  E-value: 9.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  424 KALVIQESERRKKLRFHPRQLYLSVKQGELQKVILmLLDNLDPNFQSDQqskRTPLHAAAQKGSVEICHVLLQAGANINA 503
Cdd:pfam12796   14 KLLLENGADANLQDKNGRTALHLAAKNGHLEIVKL-LLEHADVNLKDNG---RTALHYAARSGHLEIVKLLLEKGADINV 89

                   ..
gi 1907121895  504 VD 505
Cdd:pfam12796   90 KD 91
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
837-965 2.64e-08

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: 53.15  E-value: 2.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  837 KMGWGVRALQTIPQGtficeyvgELISDAEADVREDDSYLFDLDNKDGEVYCIdaryYGNISRFiNHLCDPNiipVRVFM 916
Cdd:cd20071      8 SKGRGLVATRDIEPG--------ELILVEKPLVSVPSNSFSLTDGLNEIGVGL----FPLASLL-NHSCDPN---AVVVF 71
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907121895  917 LHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWD--------IKSKYFTCQCgsEKC 965
Cdd:cd20071     72 DGNG----TLRVRALRDIKAGEELTISYIDPLLPrterrrelLEKYGFTCSC--PRC 122
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
618-679 2.66e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 2.66e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907121895  618 TGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTA-WD 679
Cdd:PLN03192   535 TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAlWN 597
SET_ATXR5_6-like cd10539
SET domain found in fungal protein lysine methyltransferase SET5 and similar protein; The ...
837-944 3.57e-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: 3.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  837 KMGWGVRALQTIPQGTFICEYVGEL--ISDAEADvrEDDSYLFDLDNKDGE---VYCIDARyyGNISRFI----NHLCD- 906
Cdd:cd10539     13 REGFTVEADGFIKDLTIIAEYTGDVdyIRNREFD--DNDSIMTLLLAGDPSkslVICPDKR--GNIARFIsginNHTKDg 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1907121895  907 ---PNIIPVRVFMLHQdlrfPRIAFFSSRDIRTGEELGFDY 944
Cdd:cd10539     89 kkkQNCKCVRYSINGE----ARVLLVATRDIAKGERLYYDY 125
Ank_4 pfam13637
Ankyrin repeats (many copies);
575-628 3.87e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 3.87e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907121895  575 GWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLL 628
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
560-607 3.87e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 3.87e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1907121895  560 LLSTGQVDVNAQDSGGWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNE 607
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE 48
Ank_2 pfam12796
Ankyrin repeats (3 copies);
612-677 4.52e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.66  E-value: 4.52e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907121895  612 LHWASFTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRgANPELRNkEGDTA 677
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTA 64
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
500-676 1.20e-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: 1.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  500 NINAVDKQQRTPLMEAVV-NNHLEVARYMVQLGGCVYSkeedGSTCLHHAAK--IGNLEMVSLLLSTGQVD------VNA 570
Cdd:TIGR00870   44 NINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAV----GDTLLHAISLeyVDAVEAILLHLLAAFRKsgplelAND 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  571 QDSG----GWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNeENICLHwASFTGSAaiaevllnaqcdlhavnYHGDTPLH 646
Cdd:TIGR00870  120 QYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPARAC-GDFFVK-SQGVDSF-----------------YHGESPLN 180
                          170       180       190
                   ....*....|....*....|....*....|
gi 1907121895  647 IAARESYHDCVLLFLSRGANPELRNKEGDT 676
Cdd:TIGR00870  181 AAACLGSPSIVALLSEDPADILTADSLGNT 210
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
487-570 2.31e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 2.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  487 SVEICH-----------VLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLE 555
Cdd:PTZ00322    83 TVELCQlaasgdavgarILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFRE 162
                           90
                   ....*....|....*
gi 1907121895  556 MVSLLLSTGQVDVNA 570
Cdd:PTZ00322   163 VVQLLSRHSQCHFEL 177
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
476-506 1.09e-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: 45.74  E-value: 1.09e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1907121895  476 RTPLHAAA-QKGSVEICHVLLQAGANINAVDK 506
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
627-680 2.03e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 2.03e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907121895  627 LLNA-QCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDL 680
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
438-655 4.75e-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: 4.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  438 RFHPRQLYLSVKQGELQKVILMLLdnldpNFQSDQQSKRTPLHAAAqKGSVEICHVLLQ--------AGANINAVDKQQ- 508
Cdd:TIGR00870   50 RLGRSALFVAAIENENLELTELLL-----NLSCRGAVGDTLLHAIS-LEYVDAVEAILLhllaafrkSGPLELANDQYTs 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  509 -----RTPLMEAVVNNHLEVARYMVQLG-------GCVYSKEEDGSTCLHH-------AAKIGNLEMVSLLLSTGQvDVN 569
Cdd:TIGR00870  124 eftpgITALHLAAHRQNYEIVKLLLERGasvparaCGDFFVKSQGVDSFYHgesplnaAACLGSPSIVALLSEDPA-DIL 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  570 AQDSGGWTPiiwaaehKHIDVIRMLLTrgadvtlTDNEENICL-------HWASFTGSAAIAEVLlnaqcdlhavNYHGD 642
Cdd:TIGR00870  203 TADSLGNTL-------LHLLVMENEFK-------AEYEELSCQmynfalsLLDKLRDSKELEVIL----------NHQGL 258
                          250
                   ....*....|...
gi 1907121895  643 TPLHIAARESYHD 655
Cdd:TIGR00870  259 TPLKLAAKEGRIV 271
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
618-683 5.70e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 5.70e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907121895  618 TGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDLTPE 683
Cdd:PTZ00322    92 SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
PHA02875 PHA02875
ankyrin repeat protein; Provisional
548-687 5.84e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.99  E-value: 5.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  548 AAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIDVIRMLLTRGA--DVTLTDNEENicLHWASFTGSAAIAE 625
Cdd:PHA02875     9 AILFGELDIARRLLDIG-INPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIESE--LHDAVEEGDVKAVE 85
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907121895  626 VLLNAQCDLHAVNYH-GDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDLTPERSDV 687
Cdd:PHA02875    86 ELLDLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
545-633 9.85e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 9.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  545 LHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIA 624
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
                           90
                   ....*....|
gi 1907121895  625 EVLLN-AQCD 633
Cdd:PTZ00322   165 QLLSRhSQCH 174
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
575-603 1.12e-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: 1.12e-05
                            10        20
                    ....*....|....*....|....*....
gi 1907121895   575 GWTPIIWAAEHKHIDVIRMLLTRGADVTL 603
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
640-672 1.20e-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: 43.05  E-value: 1.20e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1907121895  640 HGDTPLHIAA-RESYHDCVLLFLSRGANPELRNK 672
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
458-541 1.77e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 1.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  458 LMLLDNLDPNfqSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYSK 537
Cdd:PTZ00322   100 ILLTGGADPN--CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177

                   ....
gi 1907121895  538 EEDG 541
Cdd:PTZ00322   178 GANA 181
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
829-950 1.87e-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: 1.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  829 RLQLYRTAKMGWGVRALQTIPQGTFIcEYVGELISDAEADVREDDSYLFDLdnkdgeVYCIDARYY----GNISRFiNHL 904
Cdd:cd10540      1 RLEVKPSTLKGRGVFATRPIKKGEVI-EEAPVIVLPKEEYQHLCKTVLDHY------VFSWGDGCLalalGYGSMF-NHS 72
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1907121895  905 CDPNIIPVRVFMLHqdlrfpRIAFFSSRDIRTGEELGFDYGDRFWD 950
Cdd:cd10540     73 YTPNAEYEIDFENQ------TIVFYALRDIEAGEELTINYGDDLWD 112
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
476-503 2.14e-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: 2.14e-05
                            10        20
                    ....*....|....*....|....*...
gi 1907121895   476 RTPLHAAAQKGSVEICHVLLQAGANINA 503
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
487-579 2.40e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 46.35  E-value: 2.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  487 SVEICHVLLQAGANINAVDKQQRTPLMEAV--VNNHLEVARYMVQLGGCVYSKEEDGSTCLH-----HAAKignlEMVSL 559
Cdd:PHA02859   102 EPEILKILIDSGSSITEEDEDGKNLLHMYMcnFNVRINVIKLLIDSGVSFLNKDFDNNNILYsyilfHSDK----KIFDF 177
                           90       100
                   ....*....|....*....|
gi 1907121895  560 LLSTGqVDVNAQDSGGWTPI 579
Cdd:PHA02859   178 LTSLG-IDINETNKSGYNCY 196
PHA02798 PHA02798
ankyrin-like protein; Provisional
457-569 2.43e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.91  E-value: 2.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  457 ILMLLDNLDPNFQSDQQSKRTPL-----HAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVN---NHLEVARYMV 528
Cdd:PHA02798    53 IVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMI 132
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907121895  529 QLGGCVYSKEEDGSTCLHHAAKIGN---LEMVSLLLSTGqVDVN 569
Cdd:PHA02798   133 ENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKG-VDIN 175
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
575-606 3.02e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.89  E-value: 3.02e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1907121895  575 GWTPIIWAAEH-KHIDVIRMLLTRGADVTLTDN 606
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
591-662 3.40e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 3.40e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907121895  591 IRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLS 662
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_5 pfam13857
Ankyrin repeats (many copies);
534-582 3.54e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.54e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1907121895  534 VYSKEEDGSTCLHHAAKIGNLEMVSLLLsTGQVDVNAQDSGGWTPIIWA 582
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
540-572 4.01e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 4.01e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1907121895  540 DGSTCLHHAA-KIGNLEMVSLLLSTGqVDVNAQD 572
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKG-ADVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
444-651 4.73e-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: 4.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  444 LYLSVKQGELQKVILMLLDNLDPNFQSDQQSKrTPLHAAAQKGSVEICHVLLQAGAN-INAVDK----QQRTPLMEAVVN 518
Cdd:cd22192     21 LLLAAKENDVQAIKKLLKCPSCDLFQRGALGE-TALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVVN 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  519 NHLEVARYMVQLGGCVYSKEEDGS------TCLHH--------AAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIiwaae 584
Cdd:cd22192    100 QNLNLVRELIARGADVVSPRATGTffrpgpKNLIYygehplsfAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVL----- 173
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907121895  585 hkHIdvirmlltrgadVTLTDNEENICLHWASFTGSaaiaEVLLNAQCDLHAVNYHGDTPLHIAARE 651
Cdd:cd22192    174 --HI------------LVLQPNKTFACQMYDLILSY----DKEDDLQPLDLVPNNQGLTPFKLAAKE 222
Ank_4 pfam13637
Ankyrin repeats (many copies);
611-661 6.90e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 6.90e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907121895  611 CLHWASFTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFL 661
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
438-531 9.27e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.14  E-value: 9.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  438 RFHPrqLYLSVKQGELQKVILMLLDNLDPNFQSDQQSkrTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLM-EAV 516
Cdd:PHA02875   135 KFSP--LHLAVMMGDIKGIELLIDHKACLDIEDCCGC--TPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAI 210
                           90
                   ....*....|....*
gi 1907121895  517 VNNHLEVARYMVQLG 531
Cdd:PHA02875   211 ENNKIDIVRLFIKRG 225
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
640-669 1.01e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 1.01e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1907121895   640 HGDTPLHIAARESYHDCVLLFLSRGANPEL 669
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
839-948 1.18e-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: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  839 GWGVRALQTIPQGTFICEYVGELISDAEAdvrEDDSYLFDLDNKDGEVYCIDAR--YYGNISRFIN---HLCDPNIIpvr 913
Cdd:cd19193     19 GLGVWAEAPIPKGMVFGPYEGEIVEDEEA---ADSGYSWQIYKGGKLSHYIDAKdeSKSNWMRYVNcarNEEEQNLV--- 92
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1907121895  914 VFMLHQDlrfprIAFFSSRDIRTGEELGFDYGDRF 948
Cdd:cd19193     93 AFQYRGK-----IYYRTCKDIAPGTELLVWYGDEY 122
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
540-570 1.19e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.88  E-value: 1.19e-04
                            10        20        30
                    ....*....|....*....|....*....|.
gi 1907121895   540 DGSTCLHHAAKIGNLEMVSLLLSTGqVDVNA 570
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKG-ADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
460-512 1.96e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 1.96e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907121895  460 LLDNLDPNFQSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPL 512
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
SET_KMT2E cd19182
SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...
842-945 2.54e-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: 2.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  842 VRALQTIPQGTFICEYVGELISDAEAdvrEDDSYLFD--------LDNKDGEVYCIDARYYGNISRFINHLCDPNIIPVR 913
Cdd:cd19182     21 LKAAKDLPPDTLIIEYRGKFMLREQF---EANGYFFKrpypfvlfYSKFHGLEMCVDARTFGNEARFIRRSCTPNAEVRH 97
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907121895  914 VF---MLHqdlrfprIAFFSSRDIRTGEEL----GFDYG 945
Cdd:cd19182     98 VIedgTIH-------LYIYSIRSIPKGTEItiafDFDYG 129
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
476-503 5.79e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 5.79e-04
                           10        20
                   ....*....|....*....|....*...
gi 1907121895  476 RTPLHAAAQKGSVEICHVLLQAGANINA 503
Cdd:pfam13606    3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PR-SET_PRDM6 cd19191
PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 ...
839-948 7.30e-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: 40.54  E-value: 7.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  839 GWGVRALQTIPQGTFICEYVGELIS-DAEADVREDDSYLFDLDNKDGEV-YCIDAR--YYGNISRFIN---HLCDPNIIP 911
Cdd:cd19191     16 GYGICAAQRIPQGTWIGPFEGVLVSpEKQIGAVRNTQHLWEIYDQEGTLqHFIDGGdpSKSSWMRYIRcarHCGEQNLTV 95
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907121895  912 VRvfmlHQDLRFPRIAffssRDIRTGEELGFDYGDRF 948
Cdd:cd19191     96 VQ----YRGCIFYRAC----RDIPRGTELLVWYDDSY 124
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
575-601 8.09e-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: 37.62  E-value: 8.09e-04
                           10        20
                   ....*....|....*....|....*..
gi 1907121895  575 GWTPIIWAAEHKHIDVIRMLLTRGADV 601
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADI 28
PR-SET_PRDM14 cd19198
PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 ...
830-948 8.78e-04

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: 8.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  830 LQLYRTAKMG---WGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLdNKDGEV-YCIDAR-YYGNISRFINhl 904
Cdd:cd19198      7 LRVLQTSFGGtphYGVFCKKTIPKGTRFGPFRGRVVNTSEIKTYDDNSFMWEI-FEDGKLsHFIDGRgSTGNWMSYVN-- 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1907121895  905 C-----DPNIIPVRvfmlHQDlrfpRIAFFSSRDIRTGEELGFDYGDRF 948
Cdd:cd19198     84 CaryaeEQNLIAIQ----CQG----QIFYESCKEILQGQELLVWYGDCY 124
SET_SETD5 cd19181
SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...
822-908 1.43e-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: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  822 VQSGIKVRLQLYRTAkmgwgVRALQTIPQGTFICEYVGELISDAEADV-----REDDSYLFDLDNKDGEVYCIDARYYGN 896
Cdd:cd19181      6 LQLGRVTRVQKHRKI-----LRAARDLALDTLIIEYRGKVMLRQQFEVnghffKRPYPFVLFYSKFNGVEMCVDARTFGN 80
                           90
                   ....*....|..
gi 1907121895  897 ISRFINHLCDPN 908
Cdd:cd19181     81 DARFIRRSCTPN 92
Ank_5 pfam13857
Ankyrin repeats (many copies);
494-548 1.49e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 1.49e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907121895  494 LLQAG-ANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHA 548
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SET_SMYD4 cd10536
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
900-960 1.76e-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: 41.13  E-value: 1.76e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907121895  900 FINHLCDPNIIpvRVFMLHQdlrfprIAFFSSRDIRTGEELGFDYG------DRFW---DIKSKY-FTCQC 960
Cdd:cd10536    153 LLNHSCDPNTI--RSFYGNT------IVVRATRPIKKGEEITICYGphfsrmKRSErqrLLKEQYfFDCSC 215
PHA02989 PHA02989
ankyrin repeat protein; Provisional
501-561 2.05e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 42.04  E-value: 2.05e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907121895  501 INAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLL 561
Cdd:PHA02989   249 INKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRIL 309
PHA02946 PHA02946
ankyin-like protein; Provisional
439-680 4.72e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.81  E-value: 4.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  439 FHPRQLYLSVKQGELQKVILMLLDNLDPNFQSDQQSkrTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMeavvn 518
Cdd:PHA02946    38 YHILHAYCGIKGLDERFVEELLHRGYSPNETDDDGN--YPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY----- 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  519 nhlevarymvqlggcvYSKEEDGSTclhhaakignLEMVSLLLSTGQVDVNAQDSGGWTPIIwAAEHKHIDVIRMLLTRG 598
Cdd:PHA02946   111 ----------------YLSGTDDEV----------IERINLLVQYGAKINNSVDEEGCGPLL-ACTDPSERVFKKIMSIG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  599 ADVTLTDN--EENICLHWASFTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDC-VLLFLSRGANPELRNKEGD 675
Cdd:PHA02946   164 FEARIVDKfgKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNVdIINLLLPSTDVNKQNKFGD 243

                   ....*
gi 1907121895  676 TAWDL 680
Cdd:PHA02946   244 SPLTL 248
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
540-570 6.13e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 6.13e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1907121895  540 DGSTCLHHAAKIGNLEMVSLLLSTGqVDVNA 570
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENG-ADINA 30
PRK07042 PRK07042
amidase; Provisional
344-379 7.18e-03

amidase; Provisional


Pssm-ID: 235915 [Multi-domain]  Cd Length: 464  Bit Score: 39.96  E-value: 7.18e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1907121895  344 GTP-PIGTAAPALPPLAHDAPgradtsqPSARMRGHG 379
Cdd:PRK07042    87 GVPvPLGTAATDLPPAAADAP-------PAARLREAG 116
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
534-676 7.90e-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: 7.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907121895  534 VYSKEEDGSTCLHHAA---KIGNLEMVSLLLSTGQVD------VNAQDSG----GWTPIIWAAEHKHIDVIRMLLTRGAD 600
Cdd:cd21882     19 AYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSgnpkelVNAPCTDefyqGQTALHIAIENRNLNLVRLLVENGAD 98
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907121895  601 VTLtdneeniclhwasftgsAAIAEVLLNAQCDLHavnYHGDTPLHIAARESYHDCVLLFLSRGANP---ELRNKEGDT 676
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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