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Conserved domains on  [gi|2049844526|ref|NP_001382091|]
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histone-lysine N-methyltransferase EHMT2 isoform h [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SET super family cl40432
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
948-1160 5.45e-158

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.


The actual alignment was detected with superfamily member cd10533:

Pssm-ID: 394802 [Multi-domain]  Cd Length: 239  Bit Score: 470.27  E-value: 5.45e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  948 EDYKYISENCETSTMNIDRNITHLQ--------------------------DGRLLQEFNKIEPPLIFECNQACSCWRNC 1001
Cdd:cd10533      1 EDYKYISENCETSTMNIDRNITHLQhctcvddcsssnclcgqlsircwydkDGRLLQEFNKIEPPLIFECNQACSCWRNC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1002 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNI 1081
Cdd:cd10533     81 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNI 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2049844526 1082 SRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQ 1160
Cdd:cd10533    161 SRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQ 239
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
420-549 3.30e-64

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: 213.41  E-value: 3.30e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  420 FEELPLCSCRMEAPKIDRISERAGHKCMATESVDGELSGC-NAAILKRETMRPSSRVALMVLCETHRARMVKHHCCPGCG 498
Cdd:cd20905      1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCsNLPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2049844526  499 YFCTAGTFLECHPDFRVAHRFHKACVSQLNGMVFCPHCGEDAS-EAQEVTIP 549
Cdd:cd20905     81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLP 132
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
628-887 3.21e-54

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 191.32  E-value: 3.21e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  628 GREALEKALVIQESERRKKLRFHPRQLYLSVKQGELQKVILMLLDNLDPNFQSDQQSkrTPLHAAAQKGSVEICHVLLQA 707
Cdd:COG0666     32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEA 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  708 GANINAVDKQQRTPLMEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWT 787
Cdd:COG0666    110 GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDNDGET 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  788 PIIWAAEHKHIEVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNARCDLHAVNYHGDTPLHIAARESYHDCV 867
Cdd:COG0666    189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
                          250       260
                   ....*....|....*....|
gi 2049844526  868 LLFLSRGANPELRNKEGDTA 887
Cdd:COG0666    269 KLLLLALLLLAAALLDLLTL 288
2A1904 super family cl36772
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
218-326 6.63e-09

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


The actual alignment was detected with superfamily member TIGR00927:

Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 60.39  E-value: 6.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  218 GKVTSDLAKRRKLNSGG--GLSEELGSARRSGEVTLTKGDPGSLEEWETVVGDDFSLYYDSYSVDERVDSDSKSEVEalt 295
Cdd:TIGR00927  789 GEMKGDEGAEGKVEHEGetEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDGGDSEE--- 865
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2049844526  296 eqlsEEEEEEEEEEEEEEEEEEEEEEEEDEE 326
Cdd:TIGR00927  866 ----EEEEEEEEEEEEEEEEEEEEEEEENEE 892
PHA03247 super family cl33720
large tegument protein UL36; Provisional
42-204 1.98e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526   42 GDTPRSEETLPKATPDSLEPAGPSSPASVTVTVgdegadtPVGATPLIGDESENLEGDGDLRGGRILLGHATKSFPSSPS 121
Cdd:PHA03247  2753 GPARPARPPTTAGPPAPAPPAAPAAGPPRRLTR-------PAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPA 2825
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  122 kGGSCPSRAKMSMTGAGKSPPSVQSLAMRLLSMPGAQGAAAAGSEPPPATTSPEGQPKVHR-ARKTMSKPGN--GQPPVP 198
Cdd:PHA03247  2826 -GPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRlARPAVSRSTEsfALPPDQ 2904

                   ....*.
gi 2049844526  199 EKRPPE 204
Cdd:PHA03247  2905 PERPPQ 2910
 
Name Accession Description Interval E-value
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
948-1160 5.45e-158

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: 470.27  E-value: 5.45e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  948 EDYKYISENCETSTMNIDRNITHLQ--------------------------DGRLLQEFNKIEPPLIFECNQACSCWRNC 1001
Cdd:cd10533      1 EDYKYISENCETSTMNIDRNITHLQhctcvddcsssnclcgqlsircwydkDGRLLQEFNKIEPPLIFECNQACSCWRNC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1002 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNI 1081
Cdd:cd10533     81 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNI 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2049844526 1082 SRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQ 1160
Cdd:cd10533    161 SRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQ 239
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
420-549 3.30e-64

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: 213.41  E-value: 3.30e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  420 FEELPLCSCRMEAPKIDRISERAGHKCMATESVDGELSGC-NAAILKRETMRPSSRVALMVLCETHRARMVKHHCCPGCG 498
Cdd:cd20905      1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCsNLPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2049844526  499 YFCTAGTFLECHPDFRVAHRFHKACVSQLNGMVFCPHCGEDAS-EAQEVTIP 549
Cdd:cd20905     81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLP 132
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
628-887 3.21e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 191.32  E-value: 3.21e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  628 GREALEKALVIQESERRKKLRFHPRQLYLSVKQGELQKVILMLLDNLDPNFQSDQQSkrTPLHAAAQKGSVEICHVLLQA 707
Cdd:COG0666     32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEA 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  708 GANINAVDKQQRTPLMEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWT 787
Cdd:COG0666    110 GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDNDGET 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  788 PIIWAAEHKHIEVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNARCDLHAVNYHGDTPLHIAARESYHDCV 867
Cdd:COG0666    189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
                          250       260
                   ....*....|....*....|
gi 2049844526  868 LLFLSRGANPELRNKEGDTA 887
Cdd:COG0666    269 KLLLLALLLLAAALLDLLTL 288
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
1012-1134 1.34e-40

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on outlier plant homologues


Pssm-ID: 214614 [Multi-domain]  Cd Length: 124  Bit Score: 145.56  E-value: 1.34e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  1012 VRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRE--------DDSYLFDLDNKdgevYCIDARYYGNISR 1083
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPkaydtdgaKAFYLFDIDSD----LCIDARRKGNLAR 76
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 2049844526  1084 FINHLCDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWD 1134
Cdd:smart00317   77 FINHSCEPNCELLFVEVNGDD----RIVIFALRDIKPGEELTIDYGSDYAN 123
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
1023-1129 1.21e-30

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


Pssm-ID: 459965 [Multi-domain]  Cd Length: 115  Bit Score: 116.85  E-value: 1.21e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1023 GWGVRALQTIPQGTFICEYVGE-LISDAEADVRED-----------DSYLFDLDNKDGevYCIDAR--YYGNISRFINHL 1088
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELlyydklelrlwGPYLFTLDEDSE--YCIDARalYYGNWARFINHS 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2049844526 1089 CDPNIIPVRVFMlhqdLRFPRIAFFSSRDIRTGEELGFDYG 1129
Cdd:pfam00856   79 CDPNCEVRVVYV----NGGPRIVIFALRDIKPGEELTIDYG 115
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
1010-1151 5.29e-29

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 113.13  E-value: 5.29e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1010 IKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDS-----YLFDLDnkDGEVycIDARYYGNISRF 1084
Cdd:COG2940      4 LHPRIEVRPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKeplhtYLFELD--DDGV--IDGALGGNPARF 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2049844526 1085 INHLCDPNIIPVRvfmlhqdlRFPRIAFFSSRDIRTGEELGFDYGDRFWDiksKYFTCQCGseKCKH 1151
Cdd:COG2940     80 INHSCDPNCEADE--------EDGRIFIVALRDIAAGEELTYDYGLDYDE---EEYPCRCP--NCRG 133
Ank_2 pfam12796
Ankyrin repeats (3 copies);
722-815 1.95e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 1.95e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  722 LMEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLStgQVDVNAQDSGgWTPIIWAAEHKHIEVI 801
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNG-RTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 2049844526  802 RMLLTRGADVTLTD 815
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
654-876 1.09e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 99.35  E-value: 1.09e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  654 LYLSVKQGELQKVILMLLDNLDPNFQSDQQSkrTPLHAAAQKGSV-----EICHVLLQAGANINAVDKQQRTPLMEAVVN 728
Cdd:PHA03100    39 LYLAKEARNIDVVKILLDNGADINSSTKNNS--TPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISK 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  729 --NHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIG--NLEMVSLLLSTGqVDVNAQDSggwtpiiwaaehkhievIRML 804
Cdd:PHA03100   117 ksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNkiDLKILKLLIDKG-VDINAKNR-----------------VNYL 178
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2049844526  805 LTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNARCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGAN 876
Cdd:PHA03100   179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
218-326 6.63e-09

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 60.39  E-value: 6.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  218 GKVTSDLAKRRKLNSGG--GLSEELGSARRSGEVTLTKGDPGSLEEWETVVGDDFSLYYDSYSVDERVDSDSKSEVEalt 295
Cdd:TIGR00927  789 GEMKGDEGAEGKVEHEGetEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDGGDSEE--- 865
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2049844526  296 eqlsEEEEEEEEEEEEEEEEEEEEEEEEDEE 326
Cdd:TIGR00927  866 ----EEEEEEEEEEEEEEEEEEEEEEEENEE 892
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
716-857 9.28e-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: 9.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  716 KQQR---TPLMEAVVNNHLEVARYMVQRGGC-VYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGQVDVNAQDSG----GWT 787
Cdd:cd22192     12 QQKRiseSPLLLAAKENDVQAIKKLLKCPSCdLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSdlyqGET 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  788 PIIWAAEHKHIEVIRMLLTRGADVT--------LTDNEENIC------LHWASFTGSAAIAEVLLNARCDLHAVNYHGDT 853
Cdd:cd22192     92 ALHIAVVNQNLNLVRELIARGADVVspratgtfFRPGPKNLIyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171

                   ....
gi 2049844526  854 PLHI 857
Cdd:cd22192    172 VLHI 175
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
710-886 2.68e-08

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: 58.17  E-value: 2.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  710 NINAVDKQQRTPLMEAVV-NNHLEVARYMVQRGGCVYSkeedGSTCLHHAAK--IGNLEMVSLLLSTGQVD------VNA 780
Cdd:TIGR00870   44 NINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAV----GDTLLHAISLeyVDAVEAILLHLLAAFRKsgplelAND 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  781 QDSG----GWTPIIWAAEHKHIEVIRMLLTRGADVtltdneeniclhwasftgsaaiaevllNARC--------DLHAVN 848
Cdd:TIGR00870  120 QYTSeftpGITALHLAAHRQNYEIVKLLLERGASV---------------------------PARAcgdffvksQGVDSF 172
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2049844526  849 YHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDT 886
Cdd:TIGR00870  173 YHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNT 210
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
785-813 1.25e-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: 1.25e-05
                            10        20
                    ....*....|....*....|....*....
gi 2049844526   785 GWTPIIWAAEHKHIEVIRMLLTRGADVTL 813
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03247 PHA03247
large tegument protein UL36; Provisional
42-204 1.98e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526   42 GDTPRSEETLPKATPDSLEPAGPSSPASVTVTVgdegadtPVGATPLIGDESENLEGDGDLRGGRILLGHATKSFPSSPS 121
Cdd:PHA03247  2753 GPARPARPPTTAGPPAPAPPAAPAAGPPRRLTR-------PAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPA 2825
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  122 kGGSCPSRAKMSMTGAGKSPPSVQSLAMRLLSMPGAQGAAAAGSEPPPATTSPEGQPKVHR-ARKTMSKPGN--GQPPVP 198
Cdd:PHA03247  2826 -GPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRlARPAVSRSTEsfALPPDQ 2904

                   ....*.
gi 2049844526  199 EKRPPE 204
Cdd:PHA03247  2905 PERPPQ 2910
 
Name Accession Description Interval E-value
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
948-1160 5.45e-158

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: 470.27  E-value: 5.45e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  948 EDYKYISENCETSTMNIDRNITHLQ--------------------------DGRLLQEFNKIEPPLIFECNQACSCWRNC 1001
Cdd:cd10533      1 EDYKYISENCETSTMNIDRNITHLQhctcvddcsssnclcgqlsircwydkDGRLLQEFNKIEPPLIFECNQACSCWRNC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1002 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNI 1081
Cdd:cd10533     81 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNI 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2049844526 1082 SRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQ 1160
Cdd:cd10533    161 SRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQ 239
SET_EHMT cd10543
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
949-1152 3.92e-146

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: 438.70  E-value: 3.92e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  949 DYKYISENCETSTMNIDRNITHLQ--------------------------DGRLLQEFNKIEPPLIFECNQACSCWRNCK 1002
Cdd:cd10543      2 DFLYVTENCETSPLNIDRNITSLQtcscrddcssdncvcgrlsvrcwydkEGRLLPDFNKLDPPLIFECNRACSCWRNCR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1003 NRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNIS 1082
Cdd:cd10543     82 NRVVQNGIRYRLQLFRTRGMGWGVRALQDIPKGTFVCEYIGELISDSEADSREDDSYLFDLDNKDGETYCIDARRYGNIS 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1083 RFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHS 1152
Cdd:cd10543    162 RFINHLCEPNLIPVRVFVEHQDLRFPRIAFFASRDIKAGEELGFDYGEKFWRIKGKYFTCRCGSPKCKYS 231
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
949-1152 2.25e-140

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: 423.58  E-value: 2.25e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  949 DYKYISENCETSTMNIDRNITHLQ--------------------------DGRLLQEFNKIEPPLIFECNQACSCWRNCK 1002
Cdd:cd10535      2 NYKYVSQNCVTSPMNIDRNITHLQycvciddcsssncmcgqlsmrcwydkDGRLLPEFNMAEPPLIFECNHACSCWRNCR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1003 NRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNIS 1082
Cdd:cd10535     82 NRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNVS 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1083 RFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHS 1152
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) ...
948-1129 5.16e-80

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: 261.15  E-value: 5.16e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  948 EDYKYISENCETSTMNIDRNITHL--------------------------QDGRLLQEFNkiEPPLIFECNQACSCWRNC 1001
Cdd:cd10538      1 PSFTYIKDNIVGKNVQPFSNIIDSvgckckddcldskcacaaesdgifayTKNGLLRLNN--SPPPIFECNSKCSCDDDC 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1002 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR------EDDSYLFDLDN-----KDGEV 1070
Cdd:cd10538     79 KNRVVQRGLQARLQVFRTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRgkiydkSGGSYLFDLDEfsdsdGDGEE 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2049844526 1071 YCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYG 1129
Cdd:cd10538    159 LCVDATFCGNVSRFINHSCDPNLFPFNVVIDHDDLRYPRIALFATRDILPGEELTFDYG 217
SET_SUV39H cd10542
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
988-1150 5.68e-67

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


Pssm-ID: 380940 [Multi-domain]  Cd Length: 245  Bit Score: 226.02  E-value: 5.68e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  988 IFECNQACSCWRNCKNRVVQSGIKVRLQLYRTA-KMGWGVRALQTIPQGTFICEYVGELISDAEADVR------EDDSYL 1060
Cdd:cd10542     63 IYECNSRCKCGPDCPNRVVQRGRKVPLCIFRTSnGRGWGVKTLEDIKKGTFVMEYVGEIITSEEAERRgkiydaNGRTYL 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1061 FDLD-NKDGEVYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYgDRFWDIKSKY 1139
Cdd:cd10542    143 FDLDyNDDDCEYTVDAAYYGNISHFINHSCDPNLAVYAVWINHLDPRLPRIAFFAKRDIKAGEELTFDY-LMTGTGGSSE 221
                          170       180
                   ....*....|....*....|.
gi 2049844526 1140 FT----------CQCGSEKCK 1150
Cdd:cd10542    222 STipkpkdvrvpCLCGSKNCR 242
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
420-549 3.30e-64

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: 213.41  E-value: 3.30e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  420 FEELPLCSCRMEAPKIDRISERAGHKCMATESVDGELSGC-NAAILKRETMRPSSRVALMVLCETHRARMVKHHCCPGCG 498
Cdd:cd20905      1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCsNLPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2049844526  499 YFCTAGTFLECHPDFRVAHRFHKACVSQLNGMVFCPHCGEDAS-EAQEVTIP 549
Cdd:cd20905     81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLP 132
SET_SETDB1 cd10517
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
925-1150 4.59e-63

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: 216.39  E-value: 4.59e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  925 DVARGYENVPIPCVNGVDGEPcPEDYKYISENCETSTMNID---------------RNITHLQDGRLLQEFNKIEPPL-- 987
Cdd:cd10517      8 DISYGKEGVPIPCVNEIDNSS-PPYVEYSKERIPGKGVNINldpdflvgcdctdgcRDKSKCACQQLTIEATAATPGGqi 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  988 ------------------IFECNQACSCWRNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDA 1049
Cdd:cd10517     87 npsagyqyrrlmeklptgVYECNSRCKCDKRCYNRVVQNGLQVRLQVFKTEKKGWGIRCLDDIPKGSFVCIYAGQILTED 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1050 EADVRE---DDSYLFDLD------------NKDGEVYC--IDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAF 1112
Cdd:cd10517    167 EANEEGlqyGDEYFAELDyievveklkegyESDVEEHCyiIDAKSEGNLGRYLNHSCSPNLFVQNVFVDTHDLRFPWVAF 246
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2049844526 1113 FSSRDIRTGEELGFDYGdrfWDIKSKYFT---CQCGSEKCK 1150
Cdd:cd10517    247 FASRYIRAGTELTWDYN---YEVGSVPGKvlyCYCGSSNCR 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
628-887 3.21e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 191.32  E-value: 3.21e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  628 GREALEKALVIQESERRKKLRFHPRQLYLSVKQGELQKVILMLLDNLDPNFQSDQQSkrTPLHAAAQKGSVEICHVLLQA 707
Cdd:COG0666     32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEA 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  708 GANINAVDKQQRTPLMEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWT 787
Cdd:COG0666    110 GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDNDGET 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  788 PIIWAAEHKHIEVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNARCDLHAVNYHGDTPLHIAARESYHDCV 867
Cdd:COG0666    189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
                          250       260
                   ....*....|....*....|
gi 2049844526  868 LLFLSRGANPELRNKEGDTA 887
Cdd:COG0666    269 KLLLLALLLLAAALLDLLTL 288
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
968-1129 7.91e-53

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: 184.91  E-value: 7.91e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  968 ITHLQDGRLlqefnkIEP-PLIFECNQACSCWRNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELI 1046
Cdd:cd10545     47 IPYNFNGRL------IRAkPAIYECGPLCKCPPSCYNRVTQKGLRYRLEVFKTAERGWGVRSWDSIPAGSFICEYVGELL 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1047 SDAEADVR-EDDSYLFDLDNK------DGEV---------------------YCIDARYYGNISRFINHLCDPNIIPVRV 1098
Cdd:cd10545    121 DTSEADTRsGNDDYLFDIDNRqtnrgwDGGQrldvgmsdgerssaedeesseFTIDAGSFGNVARFINHSCSPNLFVQCV 200
                          170       180       190
                   ....*....|....*....|....*....|.
gi 2049844526 1099 FMLHQDLRFPRIAFFSSRDIRTGEELGFDYG 1129
Cdd:cd10545    201 LYDHNDLRLPRVMLFAADNIPPLQELTYDYG 231
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
973-1149 3.42e-52

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: 184.04  E-value: 3.42e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  973 DGRLLQEFNKIEPPlIFECNQACSCWRNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEAD 1052
Cdd:cd10544     52 DGCLLDFDGKYSGP-VFECNSMCKCSESCQNRVVQNGLQFKLQVFKTPKKGWGLRTLEFIPKGRFVCEYAGEVIGFEEAR 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1053 VR------EDDSYLFDLDN--KDGEVY--CIDARYYGNISRFINHLCDPN--IIPVRVfmlhqDLRFPRIAFFSSRDIRT 1120
Cdd:cd10544    131 RRtksqtkGDMNYIIVLREhlSSGKVLetFVDPTYIGNIGRFLNHSCEPNlfMVPVRV-----DSMVPKLALFAARDIVA 205
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2049844526 1121 GEELGFDYGDRFWDIKSKYFT-----------CQCGSEKC 1149
Cdd:cd10544    206 GEELSFDYSGEFSNSVESVTLarqdesksrkpCLCGAENC 245
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
663-921 9.96e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 184.00  E-value: 9.96e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  663 LQKVILMLLDNLDPNFQSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQRGG 742
Cdd:COG0666     32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  743 CVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIEVIRMLLTRGADVTLTDNEENICL 822
Cdd:COG0666    112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  823 HWASFTGSAAIAEVLLNARCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDLTPERSDVWFALQ 902
Cdd:COG0666    191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
                          250
                   ....*....|....*....
gi 2049844526  903 LNRKLRLGVGNRAIRTEKI 921
Cdd:COG0666    271 LLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
667-907 6.88e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 175.91  E-value: 6.88e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  667 ILMLLDNLDPNFQSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQRGGCVYS 746
Cdd:COG0666      3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  747 KEEDGSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIEVIRMLLTRGADVTLTDNEENICLHWAS 826
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  827 FTGSAAIAEVLLNARCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDLTPERSDVWFALQLNRK 906
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                   .
gi 2049844526  907 L 907
Cdd:COG0666    242 G 242
SET_SETDB cd10541
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...
985-1150 8.85e-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: 170.80  E-value: 8.85e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  985 PPLIFECNQACSCWRN-CKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADvRED----DSY 1059
Cdd:cd10541     64 PTGVYECNKLCKCDPNmCQNRLVQHGLQVRLQLFKTQNKGWGIRCLDDIAKGTFVCIYAGKILTDDFAD-KEGlemgDEY 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1060 LFDLDNKDGEVYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKY 1139
Cdd:cd10541    143 FANLDHIEESCYIIDAKLEGNLGRYLNHSCSPNLFVQNVFVDTHDLRFPWVAFFASKRIKAGTELTWDYNYEVGSVEGKE 222
                          170
                   ....*....|.
gi 2049844526 1140 FTCQCGSEKCK 1150
Cdd:cd10541    223 LLCCCGSNECR 233
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
982-1150 1.67e-45

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


Pssm-ID: 380923 [Multi-domain]  Cd Length: 255  Bit Score: 164.68  E-value: 1.67e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  982 KIEPPL-IFECNQACSCWRNCKNRVVQSGIKVRLQLYRTAK-MGWGVRALQTIPQGTFICEYVGELISDAEADVR----- 1054
Cdd:cd10525     55 KVRPGLpIYECNSRCRCGPDCPNRVVQKGIQYDLCIFRTDNgRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRgqiyd 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1055 -EDDSYLFDLDNKDgEVYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDY----- 1128
Cdd:cd10525    135 rQGATYLFDLDYVE-DVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIALFATRTIRAGEELTFDYnmqvd 213
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2049844526 1129 ----------------GDRFWDIKSKYFTCQCGSEKCK 1150
Cdd:cd10525    214 pvdaestkmdsnfglaGLPGSPKKRVRIECKCGVRSCR 251
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
982-1150 3.00e-45

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


Pssm-ID: 380930 [Multi-domain]  Cd Length: 243  Bit Score: 163.52  E-value: 3.00e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  982 KIEPPL-IFECNQACSCWRNCKNRVVQSGIKVRLQLYRTAK-MGWGVRALQTIPQGTFICEYVGELISDAEADVR----- 1054
Cdd:cd10532     53 KIPPGTpIYECNSRCKCGPDCPNRVVQKGTQYSLCIFRTSNgRGWGVKTLQKIKKNSFVMEYVGEVITSEEAERRgqfyd 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1055 -EDDSYLFDLDNKDGEvYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDY----- 1128
Cdd:cd10532    133 sKGITYLFDLDYESDE-FTVDAARYGNVSHFVNHSCDPNLQVFNVFIDNLDTRLPRIALFSTRTIKAGEELTFDYqmkgs 211
                          170       180
                   ....*....|....*....|....*....
gi 2049844526 1129 GDRFWD------IKSKYFT-CQCGSEKCK 1150
Cdd:cd10532    212 GDLSSDsidnspAKKRVRTvCKCGAVTCR 240
SET_SUV39H_Clr4-like cd20073
SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 ...
988-1150 8.40e-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: 162.74  E-value: 8.40e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  988 IFECNQACSCWRNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRE---DD---SYLF 1061
Cdd:cd20073     69 IYECNENCDCGINCPNRVVQRGRKLPLEIFKTKHKGWGLRCPRFIKAGTFIGVYLGEVITQSEAEIRGkkyDNvgvTYLF 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1062 DLDNKDGEV---YCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDR------- 1131
Cdd:cd20073    149 DLDLFEDQVdeyYTVDAQYCGDVTRFINHSCDPNLAIYSVLRDKSDSKIYDLAFFAIKDIPALEELTFDYSGRnnfdqlg 228
                          170       180
                   ....*....|....*....|....*...
gi 2049844526 1132 ---------FWDIKSKyFTCQCGSEKCK 1150
Cdd:cd20073    229 fignrsnskYINLKNK-RPCYCGSANCR 255
SET_SUV39H_DIM5-like cd19473
SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...
988-1150 1.84e-44

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


Pssm-ID: 380996 [Multi-domain]  Cd Length: 274  Bit Score: 162.49  E-value: 1.84e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  988 IFECNQACSCWRNCKNRVVQSGIKVRLQLYRTA-KMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDS-------- 1058
Cdd:cd19473     81 IYECHEGCACSDDCPNRVVERGRKVPLQIFRTSdGRGWGVRSTVDIKRGQFVDCYVGEIITPEEAQRRRDAAtiaqrkdv 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1059 YLFDLDN----------KDGEVYCIDARYYGNISRFINHLCDPNIipvRVFML---HQDLRFPRIAFFSSRDIRTGEELG 1125
Cdd:cd19473    161 YLFALDKfsdpdsldprLRGDPYEIDGEFMSGPTRFINHSCDPNL---RIFARvgdHADKHIHDLAFFAIKDIPRGTELT 237
                          170       180       190
                   ....*....|....*....|....*....|....
gi 2049844526 1126 FDY--------GDRFWDIKSKYFT-CQCGSEKCK 1150
Cdd:cd19473    238 FDYvdgvtgldDDAGDEEKEKEMTkCLCGSPKCR 271
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
954-1150 8.61e-41

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: 151.52  E-value: 8.61e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  954 SENCETSTMNIDRNITHLQDGRLLQEFnkiePPLIFECNQACSCWRN-CKNRVVQSGIKVRLQLYRTAKMGWGVRALQTI 1032
Cdd:cd10523     53 ARAFSKSESSPSKGGRGYKYKRLQEPI----PSGLYECNVSCKCNRMlCQNRVVQHGLQVRLQVFKTEKKGWGVRCLDDI 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1033 PQGTFICEYVGELIS-----------------DAEADVREDDSYLFDLDNKDGEVYCIDARYYGNISRFINHLCDPNIIP 1095
Cdd:cd10523    129 DKGTFVCIYAGRVLSrarspteplppklelpsENEVEVVTSWLILSKKRKLRENVCFLDASKEGNVGRFLNHSCCPNLFV 208
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2049844526 1096 VRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCK 1150
Cdd:cd10523    209 QNVFVDTHDKNFPWVAFFTNRVVKAGTELTWDYSYDAGTSPEQEIPCLCGVNKCQ 263
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
1012-1134 1.34e-40

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on outlier plant homologues


Pssm-ID: 214614 [Multi-domain]  Cd Length: 124  Bit Score: 145.56  E-value: 1.34e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  1012 VRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRE--------DDSYLFDLDNKdgevYCIDARYYGNISR 1083
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPkaydtdgaKAFYLFDIDSD----LCIDARRKGNLAR 76
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 2049844526  1084 FINHLCDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWD 1134
Cdd:smart00317   77 FINHSCEPNCELLFVEVNGDD----RIVIFALRDIKPGEELTIDYGSDYAN 123
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
1014-1150 3.66e-36

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


Pssm-ID: 380929  Cd Length: 136  Bit Score: 133.53  E-value: 3.66e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1014 LQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED--------DSYLFDLdnKDGEVycIDARYYGNISRFI 1085
Cdd:cd10531      2 LELFRTEKKGWGVKAKEDIQKGEFIIEYVGEVIDKKEFKERLDeyeelgksNFYILSL--SDDVV--IDATRKGNLSRFI 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2049844526 1086 NHLCDPNIIPVRVFMLHQdlrfPRIAFFSSRDIRTGEELGFDYG-DRFWDIKSKyftCQCGSEKCK 1150
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), ...
1002-1150 6.68e-34

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


Pssm-ID: 380916  Cd Length: 150  Bit Score: 127.71  E-value: 6.68e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1002 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED--------DSYLFDLDNKdgevYCI 1073
Cdd:cd10518      4 RFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKrydeegggGTYMFRIDED----LVI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1074 DARYYGNISRFINHLCDPN----IIPVRVFMlhqdlrfpRIAFFSSRDIRTGEELGFDYgdRFWDIKSKYFTCQCGSEKC 1149
Cdd:cd10518     80 DATKKGNIARFINHSCDPNcyakIITVDGEK--------HIVIFAKRDIAPGEELTYDY--KFPIEDEEKIPCLCGAPNC 149

                   .
gi 2049844526 1150 K 1150
Cdd:cd10518    150 R 150
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
1014-1150 5.28e-32

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


Pssm-ID: 380951 [Multi-domain]  Cd Length: 141  Bit Score: 121.63  E-value: 5.28e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1014 LQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNkdgevYC--------IDARYYGNISRFI 1085
Cdd:cd19174      2 LERFRTEDKGWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRMIEQYHNHSHH-----YClnldsgmvIDGYRMGNEARFV 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2049844526 1086 NHLCDPNIIPVRVFMLHQdlrfPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYfTCQCGSEKCK 1150
Cdd:cd19174     77 NHSCDPNCEMQKWSVNGV----YRIGLFALKDIPAGEELTYDYNFHSFNVEKQQ-PCKCGSPNCR 136
SET_EZH cd10519
SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...
1013-1130 1.58e-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: 1.58e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1013 RLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRE---DD---SYLFDLDNKdgevYCIDARYYGNISRFIN 1086
Cdd:cd10519      2 RLLLGKSDVAGWGLFLKEPIKKDEFIGEYTGELISQDEADRRGkiyDKynsSYLFNLNDQ----FVVDATRKGNKIRFAN 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2049844526 1087 HLCDPNIIPvRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDYGD 1130
Cdd:cd10519     78 HSSNPNCYA-KVMMVNGD---HRIGIFAKRDIEAGEELFFDYGY 117
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
1023-1129 1.21e-30

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


Pssm-ID: 459965 [Multi-domain]  Cd Length: 115  Bit Score: 116.85  E-value: 1.21e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1023 GWGVRALQTIPQGTFICEYVGE-LISDAEADVRED-----------DSYLFDLDNKDGevYCIDAR--YYGNISRFINHL 1088
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELlyydklelrlwGPYLFTLDEDSE--YCIDARalYYGNWARFINHS 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2049844526 1089 CDPNIIPVRVFMlhqdLRFPRIAFFSSRDIRTGEELGFDYG 1129
Cdd:pfam00856   79 CDPNCEVRVVYV----NGGPRIVIFALRDIKPGEELTIDYG 115
SET_SETD2 cd19172
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...
1013-1150 2.16e-30

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


Pssm-ID: 380949 [Multi-domain]  Cd Length: 142  Bit Score: 117.30  E-value: 2.16e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1013 RLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAE--------ADVREDDSYLFDLDNKDgevyCIDARYYGNISRF 1084
Cdd:cd19172      3 KVEVFRTEKKGWGLRAAEDLPKGTFVIEYVGEVLDEKEfkrrmkeyAREGNRHYYFMALKSDE----IIDATKKGNLSRF 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2049844526 1085 INHLCDPNIIpVRVFMLHQDLrfpRIAFFSSRDIRTGEELGFDYG-DRFWDIKSKyftCQCGSEKCK 1150
Cdd:cd19172     79 INHSCEPNCE-TQKWTVNGEL---RVGFFAKRDIPAGEELTFDYQfERYGKEAQK---CYCGSPNCR 138
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
1010-1151 5.29e-29

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 113.13  E-value: 5.29e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1010 IKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDS-----YLFDLDnkDGEVycIDARYYGNISRF 1084
Cdd:COG2940      4 LHPRIEVRPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKeplhtYLFELD--DDGV--IDGALGGNPARF 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2049844526 1085 INHLCDPNIIPVRvfmlhqdlRFPRIAFFSSRDIRTGEELGFDYGDRFWDiksKYFTCQCGseKCKH 1151
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, ...
1012-1149 1.11e-25

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


Pssm-ID: 380950 [Multi-domain]  Cd Length: 142  Bit Score: 103.93  E-value: 1.11e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1012 VRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR------EDDS--YLFDLDNKdgevYCIDARYYGNISR 1083
Cdd:cd19173      2 PPTEPFKTGDRGWGLRTKRDIKKGDFVIEYVGELIDEEECRRRlkkaheNNITnfYMLTLDKD----RIIDAGPKGNLSR 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2049844526 1084 FINHLCDPNiIPVRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDYG-DRFWDIKSKyftCQCGSEKC 1149
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 ...
1013-1150 2.42e-25

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


Pssm-ID: 380952 [Multi-domain]  Cd Length: 139  Bit Score: 102.88  E-value: 2.42e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1013 RLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR--------EDDSYLFDLDnKDgevYCIDARYYGNISRF 1084
Cdd:cd19175      1 KMKLVKTEKCGWGLVADEDINAGEFIIEYVGEVIDDKTCEERlwdmkhkgEKNFYMCEID-KD---MVIDATFKGNLSRF 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2049844526 1085 INHLCDPNIIpVRVFMLHQDLrfpRIAFFSSRDIRTGEELGFDYgdRFWDIKSKYfTCQCGSEKCK 1150
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 ...
1011-1150 6.52e-25

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


Pssm-ID: 380998  Cd Length: 148  Bit Score: 101.73  E-value: 6.52e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1011 KVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED--------DSYLFDLDnkdgEVYCIDARYYGNIS 1082
Cdd:cd20072     12 KKQLKFARSAIHNWGLYAMENISAKDMVIEYVGEVIRQQVADEREKrylrqgigSSYLFRID----DDTVVDATKKGNIA 87
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2049844526 1083 RFINHLCDPNIIpVRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDYgdRFwDIKSKYFTCQCGSEKCK 1150
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. ...
1004-1131 2.34e-24

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


Pssm-ID: 380926 [Multi-domain]  Cd Length: 141  Bit Score: 99.96  E-value: 2.34e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1004 RVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRE--------DDSYLFDLDNKdGEVYCIDA 1075
Cdd:cd10528      9 ELILSGKEEGLKVIEIDGKGRGVIATRPFEKGDFVVEYHGDLITITEAKKREalyakdpsTGCYMYYFQYK-GKTYCVDA 87
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2049844526 1076 -RYYGNISRFINHLC-DPNIIPVRVFMlhQDLrfPRIAFFSSRDIRTGEELGFDYGDR 1131
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 ...
1023-1132 6.20e-24

SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb repressive complex 2 (PRC2), and similar proteins; The family includes EZH1 and EZH2. EZH1 (EC 2.1.1.43; also termed ENX-2, or histone-lysine N-methyltransferase EZH1) is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. EZH2 (EC 2.1.1.43; also termed lysine N-methyltransferase 6, ENX-1, or histone-lysine N-methyltransferase EZH2) is a catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Both EZH1 and EZH2 can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. PRC2 is involved in several cancers; EZH2 is overexpressed in breast, liver and prostate cancer, while point mutations in EZH2 alter the substrate preference and product specificity of PRC2 in Non-Hodgkin lymphomas (NHLs). Thus, PRC2 is a popular target for cancer therapeutics.


Pssm-ID: 380945  Cd Length: 124  Bit Score: 98.03  E-value: 6.20e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1023 GWGVRALQTIPQGTFICEYVGELISDAEADVRE------DDSYLFDLDNKdgevYCIDARYYGNISRFINHLCDP----N 1092
Cdd:cd19168     13 GLGLFAAEDIKEGEFVIEYTGELISHDEGVRREhrrgdvSYLYLFEEQEG----IWVDAAIYGNLSRYINHATDKvktgN 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2049844526 1093 IIPVRVFMLHQdlrfPRIAFFSSRDIRTGEELGFDYGDRF 1132
Cdd:cd19168     89 CMPKIMYVNHE----WRIKFTAIKDIKIGEELFFNYGDNF 124
SET_SETD1 cd19169
SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...
1011-1150 1.26e-23

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


Pssm-ID: 380946  Cd Length: 148  Bit Score: 98.18  E-value: 1.26e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1011 KVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED--------DSYLFDLDnkdgEVYCIDARYYGNIS 1082
Cdd:cd19169     12 KKQLKFAKSRIHDWGLFALEPIAADEMVIEYVGQVIRQSVADEREKryeaigigSSYLFRVD----DDTIIDATKCGNLA 87
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2049844526 1083 RFINHLCDPN----IIPVRvfmlhqdlRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKskyFTCQCGSEKCK 1150
Cdd:cd19169     88 RFINHSCNPNcyakIITVE--------SQKKIVIYSKRPIAVNEEITYDYKFPIEDEK---IPCLCGAPQCR 148
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
1023-1134 1.73e-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: 1.73e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1023 GWGVRALQTIPQGTFICEYVGELISDAEADVR----EDDSYLFDLDnkDGEVYcIDARYYGNISRFINHLCDPNIIPVrv 1098
Cdd:cd10522     14 GLGLFAAETIAKGEFVGEYTGEVLDRWEEDRDsvyhYDPLYPFDLN--GDILV-IDAGKKGNLTRFINHSDQPNLELI-- 88
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2049844526 1099 FMLHQDLrfPRIAFFSSRDIRTGEELGFDYGDRFWD 1134
Cdd:cd10522     89 VRTLKGE--QHIGFVAIRDIKPGEELFISYGPKYWK 122
Ank_2 pfam12796
Ankyrin repeats (3 copies);
722-815 1.95e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 1.95e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  722 LMEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLStgQVDVNAQDSGgWTPIIWAAEHKHIEVI 801
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNG-RTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 2049844526  802 RMLLTRGADVTLTD 815
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
654-876 1.09e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 99.35  E-value: 1.09e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  654 LYLSVKQGELQKVILMLLDNLDPNFQSDQQSkrTPLHAAAQKGSV-----EICHVLLQAGANINAVDKQQRTPLMEAVVN 728
Cdd:PHA03100    39 LYLAKEARNIDVVKILLDNGADINSSTKNNS--TPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISK 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  729 --NHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIG--NLEMVSLLLSTGqVDVNAQDSggwtpiiwaaehkhievIRML 804
Cdd:PHA03100   117 ksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNkiDLKILKLLIDKG-VDINAKNR-----------------VNYL 178
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2049844526  805 LTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNARCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGAN 876
Cdd:PHA03100   179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
SET_KMT2A_2B cd19170
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...
1004-1150 1.26e-21

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


Pssm-ID: 380947 [Multi-domain]  Cd Length: 152  Bit Score: 92.45  E-value: 1.26e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1004 RVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED--DS-----YLFDLDnkdgEVYCIDAR 1076
Cdd:cd19170      6 RHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKyyESkgigcYMFRID----DDEVVDAT 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2049844526 1077 YYGNISRFINHLCDPN----IIPVrvfmlhqDLRfPRIAFFSSRDIRTGEELGFDYGDRFWDIKskyFTCQCGSEKCK 1150
Cdd:cd19170     82 MHGNAARFINHSCEPNcysrVVNI-------DGK-KHIVIFALRRILRGEELTYDYKFPIEDVK---IPCTCGSKKCR 148
Ank_2 pfam12796
Ankyrin repeats (3 copies);
689-782 1.30e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.48  E-value: 1.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  689 LHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQRGGCvySKEEDGSTCLHHAAKIGNLEMVS 768
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|....
gi 2049844526  769 LLLSTGqVDVNAQD 782
Cdd:pfam12796   79 LLLEKG-ADINVKD 91
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
1011-1150 2.31e-19

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), 2D (KMT2D) and similar proteins; This family includes KMT2C and KMT2D. Both, KMT2C (also termed HALR or MLL3) and KMT2D (also termed ALR or MLL2), act as histone methyltransferases that methylate 'Lys-4' of histone H3 (H3K4me). They are subunits of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation.


Pssm-ID: 380948 [Multi-domain]  Cd Length: 153  Bit Score: 85.94  E-value: 2.31e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1011 KVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDS-------YLFDLDNKdgevYCIDARYYGNISR 1083
Cdd:cd19171     13 RSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYesqnrgiYMFRIDND----WVIDATMTGGPAR 88
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2049844526 1084 FINHLCDPNIIpVRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKyFTCQCGSEKCK 1150
Cdd:cd19171     89 YINHSCNPNCV-AEVVTFDKE---KKIIIISNRRIAKGEELTYDYKFDFEDDQHK-IPCLCGAPNCR 150
PHA03100 PHA03100
ankyrin repeat protein; Provisional
662-886 6.81e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.88  E-value: 6.81e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  662 ELQKVILMLLDNLDPNFQSdqqsKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNH-----LEVARY 736
Cdd:PHA03100    16 KNIKYIIMEDDLNDYSYKK----PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  737 MVQRGGCVYSKEEDGSTCLHHAA--KIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHI--EVIRMLLTRGADVT 812
Cdd:PHA03100    92 LLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDIN 170
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2049844526  813 LTDNeeniclhwasftgsaaiAEVLLNARCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDT 886
Cdd:PHA03100   171 AKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
SET_NSD2 cd19211
SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...
1015-1149 1.68e-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: 1.68e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1015 QLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR-----EDDS---YLFDLDnKDgevYCIDARYYGNISRFIN 1086
Cdd:cd19211      5 KIIKTEGKGWGLIAKRDIKKGEFVNEYVGELIDEEECMARikhahENDIthfYMLTID-KD---RIIDAGPKGNYSRFMN 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2049844526 1087 HLCDPNiIPVRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDYG-DRFWDIKSkyfTCQCGSEKC 1149
Cdd:cd19211     81 HSCQPN-CETQKWTVNGD---TRVGLFAVCDIPAGTELTFNYNlDCLGNEKT---VCRCGAPNC 137
SET_SETD5-like cd10529
SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...
1025-1128 6.26e-18

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


Pssm-ID: 380927  Cd Length: 127  Bit Score: 81.17  E-value: 6.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1025 GVRALQTIPQGTFICEYVGE--LISDAEADVRED---DSYLFDLDNKDGEVYCIDARYYGNISRFINHLCDPNiipVRV- 1098
Cdd:cd10529     18 GLVATEDISPGEPILEYKGEvsLRSEFKEDNGFFkrpSPFVFFYDGFEGLPLCVDARKYGNEARFIRRSCRPN---AELr 94
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2049844526 1099 FMLHQDLRFpRIAFFSSRDIRTGEE--LGFDY 1128
Cdd:cd10529     95 HVVVSNGEL-RLFIFALKDIRKGTEitIPFDY 125
SET_EZH2 cd19218
SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...
1009-1128 9.44e-18

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


Pssm-ID: 380995  Cd Length: 120  Bit Score: 80.34  E-value: 9.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1009 GIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDD------SYLFDLDNKdgevYCIDARYYGNIS 1082
Cdd:cd19218      1 GSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVydkymcSFLFNLNND----FVVDATRKGNKI 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2049844526 1083 RFINHLCDPNIIpVRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDY 1128
Cdd:cd19218     77 RFANHSVNPNCY-AKVMMVNGD---HRIGIFAKRAIQTGEELFFDY 118
SET_EZH1 cd19217
SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43) ...
1007-1128 1.98e-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: 1.98e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1007 QSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED------DSYLFDLDNKdgevYCIDARYYGN 1080
Cdd:cd19217      1 QRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKvydkymSSFLFNLNND----FVVDATRKGN 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2049844526 1081 ISRFINHLCDPNIIpVRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDY 1128
Cdd:cd19217     77 KIRFANHSVNPNCY-AKVVMVNGD---HRIGIFAKRAIQQGEELFFDY 120
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
1014-1149 2.01e-17

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


Pssm-ID: 380987 [Multi-domain]  Cd Length: 142  Bit Score: 79.97  E-value: 2.01e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1014 LQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR-----EDD---SYLFDLDnKDgevYCIDARYYGNISRFI 1085
Cdd:cd19210      4 VEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIDEEECRARiryaqEHDitnFYMLTLD-KD---RIIDAGPKGNYARFM 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2049844526 1086 NHLCDPNiIPVRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDYgdRFWDIKSKYFTCQCGSEKC 1149
Cdd:cd19210     80 NHCCQPN-CETQKWTVNGD---TRVGLFALCDIKAGTELTFNY--NLECLGNGKTVCKCGAPNC 137
PreSET smart00468
N-terminal to some SET domains; A Cys-rich putative Zn2+-binding domain that occurs N-terminal ...
923-996 2.63e-17

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: 78.23  E-value: 2.63e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526   923 CRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCETSTMNIDRNITHL----------------------------QDG 974
Cdd:smart00468    1 CLDISNGKENVPVPLVNEVDEDPPPPDFEYISEYIYGQGVPIDRSPSPLvgcscsgdcsssnkcecarknggefayeLNG 80
                            90       100
                    ....*....|....*....|..
gi 2049844526   975 RllqeFNKIEPPLIFECNQACS 996
Cdd:smart00468   81 G----LRLKRKPLIYECNSRCS 98
SET_KMT2A cd19206
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...
1016-1150 3.70e-17

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


Pssm-ID: 380983 [Multi-domain]  Cd Length: 154  Bit Score: 79.68  E-value: 3.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1016 LYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRE---DDS----YLFDLDnkDGEVycIDARYYGNISRFINHL 1088
Cdd:cd19206     18 VYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREkyyDSKgigcYMFRID--DSEV--VDATMHGNAARFINHS 93
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2049844526 1089 CDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWDIKSKyFTCQCGSEKCK 1150
Cdd:cd19206     94 CEPNCYSRVINIDGQK----HIVIFAMRKIYRGEELTYDYKFPIEDASNK-LPCNCGAKKCR 150
Ank_2 pfam12796
Ankyrin repeats (3 copies);
789-881 7.09e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 7.09e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  789 IIWAAEHKHIEVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLN-ARCDlhaVNYHGDTPLHIAARESYHDCV 867
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEhADVN---LKDNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 2049844526  868 LLFLSRGANPELRN 881
Cdd:pfam12796   78 KLLLEKGADINVKD 91
SET_NSD3 cd19212
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
1015-1149 7.24e-17

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


Pssm-ID: 380989 [Multi-domain]  Cd Length: 142  Bit Score: 78.43  E-value: 7.24e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1015 QLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDN-------KDgevYCIDARYYGNISRFINH 1087
Cdd:cd19212      5 EIIKTERRGWGLRTKRSIKKGEFVNEYVGELIDEEECRLRIKRAHENSVTNfymltvtKD---RIIDAGPKGNYSRFMNH 81
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2049844526 1088 LCDPNiIPVRVFMLHQDLrfpRIAFFSSRDIRTGEELGFDYG-DRFWDIKSKyftCQCGSEKC 1149
Cdd:cd19212     82 SCNPN-CETQKWTVNGDV---RVGLFALCDIPAGMELTFNYNlDCLGNGRTE---CHCGADNC 137
SET_SETD1A cd19204
SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...
1011-1150 8.59e-17

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


Pssm-ID: 380981 [Multi-domain]  Cd Length: 153  Bit Score: 78.91  E-value: 8.59e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1011 KVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED--------DSYLFDLDNKDgevyCIDARYYGNIS 1082
Cdd:cd19204     13 KKKLRFGRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQVVADMREKryvqegigSSYLFRVDHDT----IIDATKCGNLA 88
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2049844526 1083 RFINHLCDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGdrfWDIKSKYFTCQCGSEKCK 1150
Cdd:cd19204     89 RFINHCCTPNCYAKVITIESQK----KIVIYSKQPIGVNEEITYDYK---FPIEDNKIPCLCGTENCR 149
PHA02874 PHA02874
ankyrin repeat protein; Provisional
687-921 3.00e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 82.70  E-value: 3.00e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  687 TPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQRGgcvyskeEDGST----CLhhaakig 762
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG-------VDTSIlpipCI------- 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  763 NLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIEVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNARC 842
Cdd:PHA02874   103 EKDMIKTILDCG-IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  843 DLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGdtawdLTPERSdvwfALQLNRK-LRLGVGNRAIRTEKI 921
Cdd:PHA02874   182 YANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNG-----FTPLHN----AIIHNRSaIELLINNASINDQDI 252
PHA03095 PHA03095
ankyrin-like protein; Provisional
686-879 3.33e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 82.77  E-value: 3.33e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  686 RTPLHA-----AAQKGSVEIchvLLQAGANINAVDKQQRTPLMEAVVNNH--LEVARYMVQRGGCVYSKEEDGSTCLHHA 758
Cdd:PHA03095   118 RTPLHVylsgfNINPKVIRL---LLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHHH 194
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  759 A---KIGNlEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEH---KHIeVIRMLLTRGADVTLTDNEENICLHWASFTGSAA 832
Cdd:PHA03095   195 LqsfKPRA-RIVRELIRAG-CDPAATDMLGNTPLHSMATGsscKRS-LVLPLLIAGISINARNRYGQTPLHYAAVFNNPR 271
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2049844526  833 IAEVLLNARCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPEL 879
Cdd:PHA03095   272 ACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAET 318
PHA03095 PHA03095
ankyrin-like protein; Provisional
651-887 3.67e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 82.77  E-value: 3.67e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  651 PRQLYLSVKQGELQKVILMLLDN-LDPNFQSdqQSKRTPLHAAAQKGSVE-ICHVLLQAGANINAVDKQQRTPLME--AV 726
Cdd:PHA03095    50 PLHLYLHYSSEKVKDIVRLLLEAgADVNAPE--RCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVylSG 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  727 VNNHLEVARYMVQRGGCVYSKEEDGSTCLH-----HAAkigNLEMVSLLLSTGqVDVNAQDSGGWTPIiwaaeHKHIE-- 799
Cdd:PHA03095   128 FNINPKVIRLLLRKGADVNALDLYGMTPLAvllksRNA---NVELLRLLIDAG-ADVYAVDDRFRSLL-----HHHLQsf 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  800 -----VIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEV--LLNARCDLHAVNYHGDTPLHIAARESYHDCVLLFLS 872
Cdd:PHA03095   199 kprarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIA 278
                          250
                   ....*....|....*
gi 2049844526  873 RGANPELRNKEGDTA 887
Cdd:PHA03095   279 LGADINAVSSDGNTP 293
PHA02876 PHA02876
ankyrin repeat protein; Provisional
658-887 4.09e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 83.57  E-value: 4.09e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  658 VKQGELQKVILMLLDNLDPNfqSDQQSKRTPLHAAAQKGSVEICHVLLQAGANIN------------AVD---------- 715
Cdd:PHA02876   153 IQQDELLIAEMLLEGGADVN--AKDIYCITPIHYAAERGNAKMVNLLLSYGADVNiialddlsvlecAVDsknidtikai 230
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  716 -------KQQRTPLMEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIGNL-EMVSLLLSTGqVDVNAQDSGGWT 787
Cdd:PHA02876   231 idnrsniNKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERG-ADVNAKNIKGET 309
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  788 PIIWAAEHKH-IEVIRMLLTRGADVTLTDNEENICLHWAS-FTGSAAIAEVLLNARCDLHAVNYHGDTPLHIAARESYHD 865
Cdd:PHA02876   310 PLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVV 389
                          250       260
                   ....*....|....*....|..
gi 2049844526  866 CVLLFLSRGANPELRNKEGDTA 887
Cdd:PHA02876   390 IINTLLDYGADIEALSQKIGTA 411
Pre-SET pfam05033
Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines ...
926-1004 5.95e-16

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: 74.38  E-value: 5.95e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  926 VARGYENVPIPCVNGVDGEPCPEDYKYI-----------------------SENCETSTMNIDRNITHLQDGRLLQEfnk 982
Cdd:pfam05033    1 ISKGKENVPIPVVNEVDDEPPPPDFTYItsyiypkeflliipqgcdcgdcsSEKCSCAQLNGGEFRFPYDKDGLLVP--- 77
                           90       100
                   ....*....|....*....|..
gi 2049844526  983 IEPPLIFECNQACSCWRNCKNR 1004
Cdd:pfam05033   78 ESKPPIYECNPLCGCPPSCPNR 99
SET_SETD1B cd19205
SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...
1011-1150 3.56e-15

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


Pssm-ID: 380982 [Multi-domain]  Cd Length: 153  Bit Score: 73.94  E-value: 3.56e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1011 KVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED--------DSYLFDLDNKDgevyCIDARYYGNIS 1082
Cdd:cd19205     13 KKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKryedegigSSYMFRVDHDT----IIDATKCGNFA 88
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2049844526 1083 RFINHLCDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGdrfWDIKSKYFTCQCGSEKCK 1150
Cdd:cd19205     89 RFINHSCNPNCYAKVITVESQK----KIVIYSKQHINVNEEITYDYK---FPIEDVKIPCLCGSENCR 149
SET_KMT2C cd19208
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) ...
999-1150 1.12e-14

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: 72.74  E-value: 1.12e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  999 RNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED-------DSYLFDLDNKdgevY 1071
Cdd:cd19208      2 KSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKlyesqnrGVYMFRIDND----H 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2049844526 1072 CIDARYYGNISRFINHLCDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWDIKSKyFTCQCGSEKCK 1150
Cdd:cd19208     78 VIDATLTGGPARYINHSCAPNCVAEVVTFEKGH----KIIISSSRRIQKGEELCYDYKFDFEDDQHK-IPCHCGAVNCR 151
SET_SpSET3-like cd19183
SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...
1014-1176 1.65e-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: 72.82  E-value: 1.65e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1014 LQLYRTAKMGW-GVRALQTIPQGTFICEYVGELISDAEADVREDDSY----------LFDldnkDGEVYCIDARYYGNIS 1082
Cdd:cd19183      3 ISSIGLANASRfGLFADRPIPAGDPIQELLGEIGLQSEYIADPENQYqilgapkphvFFH----PQSPLYIDTRRSGSVA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1083 RFINHLCDPN--IIPVRVfmlhQDLRFPRIAFFSSRDIRTGEELGFDYGdrfWDIkskyftcqcgsekcKHSAEAIALEQ 1160
Cdd:cd19183     79 RFIRRSCRPNaeLVTVAS----DSGSVLKFVLYASRDISPGEEITIGWD---WDN--------------PHPFRRFALGE 137
                          170
                   ....*....|....*.
gi 2049844526 1161 SRLARLDPHPELLPEL 1176
Cdd:cd19183    138 LVPSNLDLEQHLLSFL 153
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
1013-1129 2.93e-14

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, Enhancer-of-zeste, Trithorax (SET) domain superfamily corresponds to SET domain-containing lysine methyltransferases, which catalyze site and state-specific methylation of lysine residues in histones that are fundamental in epigenetic regulation of gene activation and silencing in eukaryotic organisms. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains has been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as N-SET and C-SET. C-SET forms an unusual and conserved knot-like structure of probable functional importance. In addition to N-SET and C-SET, an insert region (I-SET) and flanking regions of high structural variability form part of the overall structure. Some family members contain a pre-SET domain, which is found in a number of histone methyltransferases (HMTase), and a post-SET domain, which harbors a zinc-binding site.


Pssm-ID: 380914 [Multi-domain]  Cd Length: 72  Bit Score: 68.82  E-value: 2.93e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1013 RLQLYRTAKMGWGVRALQTIPQGTFICeyvgelisdaeadvreddsylfdldnkdgevycidaryygnISRFINHLCDPN 1092
Cdd:cd08161      1 EIRPSTIPGAGFGLFATRDIPKGEVIG-----------------------------------------LARFINHSCEPN 39
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2049844526 1093 IIPVRVFmlhqDLRFPRIAFFSSRDIRTGEELGFDYG 1129
Cdd:cd08161     40 CEFEEVY----VGGKPRVFIVALRDIKAGEELTVDYG 72
Ank_2 pfam12796
Ankyrin repeats (3 copies);
654-741 3.90e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.99  E-value: 3.90e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  654 LYLSVKQGELQKVILMLLDNLDPNFQSdqQSKRTPLHAAAQKGSVEICHVLLQaGANINAVDkQQRTPLMEAVVNNHLEV 733
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQD--KNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEI 76

                   ....*...
gi 2049844526  734 ARYMVQRG 741
Cdd:pfam12796   77 VKLLLEKG 84
PHA02878 PHA02878
ankyrin repeat protein; Provisional
641-884 4.14e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 76.46  E-value: 4.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  641 SERRKKLRFHPRQLYLSvkqgelqKVILmlLDNLDPNFQSDQQSKRTPLHAAAQKgsVEICHVLLQAGANINAVDKQQ-R 719
Cdd:PHA02878   101 TLVAIKDAFNNRNVEIF-------KIIL--TNRYKNIQTIDLVYIDKKSKDDIIE--AEITKLLLSYGADINMKDRHKgN 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  720 TPLMEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGQvDVNAQDSGGWTPIIWAAEH-KHI 798
Cdd:PHA02878   170 TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA-STDARDKCGNTPLHISVGYcKDY 248
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  799 EVIRMLLTRGADVTLTDNEENIC-LHWAsfTGSAAIAEVLLNARCDLHAVNYHGDTPLHIAARESY----------HDCV 867
Cdd:PHA02878   249 DILKLLLEHGVDVNAKSYILGLTaLHSS--IKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLcinigrilisNICL 326
                          250
                   ....*....|....*..
gi 2049844526  868 LLFLsrgaNPELRNKEG 884
Cdd:PHA02878   327 LKRI----KPDIKNSEG 339
SET_KMT2B cd19207
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...
1016-1150 4.54e-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: 70.82  E-value: 4.54e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1016 LYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED-------DSYLFDLDNKDgevyCIDARYYGNISRFINHL 1088
Cdd:cd19207     18 VYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKfydskgiGCYMFRIDDFD----VVDATMHGNAARFINHS 93
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2049844526 1089 CDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWDIKSKyFTCQCGSEKCK 1150
Cdd:cd19207     94 CEPNCYSRVIHVEGQK----HIVIFALRKIYRGEELTYDYKFPIEDASNK-LPCNCGAKRCR 150
SET_KMT2D cd19209
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...
999-1150 5.85e-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: 70.50  E-value: 5.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  999 RNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED-------DSYLFDLDNKdgevY 1071
Cdd:cd19209      3 KSSQYRRLKTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKiyeeqnrGIYMFRINNE----H 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2049844526 1072 CIDARYYGNISRFINHLCDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWDIKSKyFTCQCGSEKCK 1150
Cdd:cd19209     79 VIDATLTGGPARYINHSCAPNCVAEVVTFDKED----KIIIISSRRIPKGEELTYDYQFDFEDDQHK-IPCHCGAWNCR 152
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
686-812 1.14e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 75.67  E-value: 1.14e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  686 RTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQRGGCvySKEEDGSTCLHHAAKIGNLE 765
Cdd:PLN03192   559 RTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASI--SDPHAAGDLLCTAAKRNDLT 636
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2049844526  766 MVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIEVIRMLLTRGADVT 812
Cdd:PLN03192   637 AMKELLKQG-LNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVD 682
PHA02876 PHA02876
ankyrin repeat protein; Provisional
685-876 2.68e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 74.33  E-value: 2.68e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  685 KRTPLHAAAQKGSV-EICHVLLQAGANINAVDKQQRTPLMEAVVNNH-LEVARYMVQRGGCVYSKEEDGSTCLHHAAKIG 762
Cdd:PHA02876   273 KNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLD 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  763 -NLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIEVIRMLLTRGADVTLTDNEENICLHWASF-TGSAAIAEVLLNA 840
Cdd:PHA02876   353 rNKDIVITLLELG-ANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCgTNPYMSVKTLIDR 431
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2049844526  841 RCDLHAVNYHGDTPLHIAARESYH-DCVLLFLSRGAN 876
Cdd:PHA02876   432 GANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGAD 468
PHA02874 PHA02874
ankyrin repeat protein; Provisional
654-817 2.92e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.46  E-value: 2.92e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  654 LYLSVKQGELQKVILMLLDNLDPNFQSDQQSkrTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEV 733
Cdd:PHA02874   128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGC--YPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  734 ARYMVQRGGCVYSKEEDGSTCLHHAAkIGNLEMVSLLLSTGQvdVNAQDSGGWTPIIWAAEHK-HIEVIRMLLTRGADVT 812
Cdd:PHA02874   206 IKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLINNAS--INDQDIDGSTPLHHAINPPcDIDIIDILLYHKADIS 282

                   ....*
gi 2049844526  813 LTDNE 817
Cdd:PHA02874   283 IKDNK 287
PHA03095 PHA03095
ankyrin-like protein; Provisional
697-887 3.64e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.14  E-value: 3.64e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  697 SVEICHVLLQAGANINAVDKQQRTPL---MEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIGN-LEMVSLLLS 772
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIK 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  773 TGqVDVNAQDSGGWTPIiwaaeHKHI-------EVIRMLLTRGADVTLTDNEENICLH-WASFTG-SAAIAEVLLNARCD 843
Cdd:PHA03095   106 AG-ADVNAKDKVGRTPL-----HVYLsgfninpKVIRLLLRKGADVNALDLYGMTPLAvLLKSRNaNVELLRLLIDAGAD 179
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2049844526  844 LHAVNYHGDTPLHIAAR--ESYHDCVLLFLSRGANPELRNKEGDTA 887
Cdd:PHA03095   180 VYAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTP 225
PHA02875 PHA02875
ankyrin repeat protein; Provisional
654-838 4.84e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.25  E-value: 4.84e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  654 LYLSVKQGELQKVILMLLDNLDPNFQsdQQSKRTPLHAAAQKGSVEICHVLLQAGANINAV-DKQQRTPLMEAVVNNHLE 732
Cdd:PHA02875    39 IKLAMKFRDSEAIKLLMKHGAIPDVK--YPDIESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLD 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  733 VARYMVQRGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTgQVDVNAQDSGGWTPIIWAAEHKHIEV------------ 800
Cdd:PHA02875   117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH-KACLDIEDCCGCTPLIIAMAKGDIAIckmlldsganid 195
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2049844526  801 ----------------------IRMLLTRGAD---VTLTDNEE--------NICLHWASFTGSAAIAEVLL 838
Cdd:PHA02875   196 yfgkngcvaalcyaiennkidiVRLFIKRGADcniMFMIEGEEctildmicNMCTNLESEAIDALIADIAI 266
PHA02875 PHA02875
ankyrin repeat protein; Provisional
686-887 1.11e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 68.48  E-value: 1.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  686 RTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIGNLE 765
Cdd:PHA02875     3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  766 MVSLLLSTGQV--DVNAQDsgGWTPIIWAAEHKHIEVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNARCD 843
Cdd:PHA02875    83 AVEELLDLGKFadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2049844526  844 LHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTA 887
Cdd:PHA02875   161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVA 204
Ank_4 pfam13637
Ankyrin repeats (many copies);
751-805 1.14e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.75  E-value: 1.14e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2049844526  751 GSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIEVIRMLL 805
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
686-738 1.74e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 1.74e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2049844526  686 RTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMV 738
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
681-884 2.08e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 67.68  E-value: 2.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  681 DQQSKrTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAK 760
Cdd:PHA02874   121 DAELK-TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  761 IGNLEMVSLLLSTGQvDVNAQDSGGWTPIIWAAEHKHIEVirMLLTRGADVTLTDNEENICLHWA-SFTGSAAIAEVLLN 839
Cdd:PHA02874   200 YGDYACIKLLIDHGN-HIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAiNPPCDIDIIDILLY 276
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2049844526  840 ARCDLHAVNYHGDTPLHIAARESYHDCVLLFLSrgANPELRNKEG 884
Cdd:PHA02874   277 HKADISIKDNKGENPIDTAFKYINKDPVIKDII--ANAVLIKEAD 319
PHA03100 PHA03100
ankyrin repeat protein; Provisional
665-811 1.77e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.69  E-value: 1.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  665 KVILMLLDN-LDPNFQSDQQSkrTPLHAAAQK--GSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNH--LEVARYMVQ 739
Cdd:PHA03100    87 EIVKLLLEYgANVNAPDNNGI--TPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLID 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  740 RG---------------GC-VYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIEVIRM 803
Cdd:PHA03100   165 KGvdinaknrvnyllsyGVpINIKDVYGFTPLHYAVYNNNPEFVKYLLDLG-ANPNLVNKYGDTPLHIAILNNNKEIFKL 243

                   ....*...
gi 2049844526  804 LLTRGADV 811
Cdd:PHA03100   244 LLNNGPSI 251
PHA02876 PHA02876
ankyrin repeat protein; Provisional
665-811 1.95e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.08  E-value: 1.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  665 KVILMLLDNLDPNFQSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAV--VNNHLEVaRYMVQRGG 742
Cdd:PHA02876   355 KDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALcgTNPYMSV-KTLIDRGA 433
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  743 CVYSKEEDGSTCLHHAAKIG-NLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIevIRMLLTRGADV 811
Cdd:PHA02876   434 NVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNG-ADVNAINIQNQYPLLIALEYHGI--VNILLHYGAEL 500
PHA03100 PHA03100
ankyrin repeat protein; Provisional
727-876 2.32e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.30  E-value: 2.32e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  727 VNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHI-----EVI 801
Cdd:PHA03100    11 RIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNG-ADINSSTKNNSTPLHYLSNIKYNltdvkEIV 89
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2049844526  802 RMLLTRGADVTLTDNEENICLHWASFT--GSAAIAEVLLNARCDLHAVNYHGDTPLHIAARESYHD--CVLLFLSRGAN 876
Cdd:PHA03100    90 KLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVD 168
PHA02798 PHA02798
ankyrin-like protein; Provisional
697-818 3.68e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 63.70  E-value: 3.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  697 SVEICHVLLQAGANINAVDKQQRTPLMEAVVN----NH-LEVARYMVQRGGCVYSKEEDGST---CLHHAAKIGNLEMVS 768
Cdd:PHA02798    50 STDIVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHmLDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILL 129
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2049844526  769 LLLSTGqVDVNAQDSGGWTPI---IWAAEHKHIEVIRMLLTRGADVTLTDNEE 818
Cdd:PHA02798   130 FMIENG-ADTTLLDKDGFTMLqvyLQSNHHIDIEIIKLLLEKGVDINTHNNKE 181
Ank_4 pfam13637
Ankyrin repeats (many copies);
718-771 4.52e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 4.52e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2049844526  718 QRTPLMEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLL 771
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
765-887 4.54e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 62.28  E-value: 4.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  765 EMVSLLLSTGQVDVNAQDSGGWTPIIWAAEHKHIEVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNARCDL 844
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2049844526  845 HAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTA 887
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123
PHA02876 PHA02876
ankyrin repeat protein; Provisional
699-876 1.07e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.77  E-value: 1.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  699 EIC-HVLLQA--GANI--NAVDK--QQRTPLMEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLL 771
Cdd:PHA02876   119 EACiHILKEAisGNDIhyDKINEsiEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLL 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  772 STGqVDVNAQDSGGWTPIIWAAEHKHIEVIR-----------------------------MLLTRGADVTLTDNEENICL 822
Cdd:PHA02876   199 SYG-ADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsninkndlsllkairnedletslLLYDAGFSVNSIDDCKNTPL 277
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2049844526  823 HWASFTGS-AAIAEVLLNARCDLHAVNYHGDTPLHIAARESYH-DCVLLFLSRGAN 876
Cdd:PHA02876   278 HHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGAD 333
PHA02878 PHA02878
ankyrin repeat protein; Provisional
688-886 4.31e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.28  E-value: 4.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  688 PLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQrggcVYSKEEDGST--CLHHAAKIGNLE 765
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR----SINKCSVFYTlvAIKDAFNNRNVE 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  766 MVSLLLSTG-----QVDVNAQDSGGWTPIIWAaehkhiEVIRMLLTRGADVTLTD-NEENICLHWASFTGSAAIAEVLLN 839
Cdd:PHA02878   116 IFKIILTNRykniqTIDLVYIDKKSKDDIIEA------EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLS 189
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2049844526  840 ARCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDT 886
Cdd:PHA02878   190 YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
218-326 6.63e-09

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 60.39  E-value: 6.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  218 GKVTSDLAKRRKLNSGG--GLSEELGSARRSGEVTLTKGDPGSLEEWETVVGDDFSLYYDSYSVDERVDSDSKSEVEalt 295
Cdd:TIGR00927  789 GEMKGDEGAEGKVEHEGetEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDGGDSEE--- 865
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2049844526  296 eqlsEEEEEEEEEEEEEEEEEEEEEEEEDEE 326
Cdd:TIGR00927  866 ----EEEEEEEEEEEEEEEEEEEEEEEENEE 892
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
1021-1149 6.89e-09

SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing protein, and similar proteins; The family includes SET and MYND domain-containing proteins, SMYD1-SYMD5. SMYD1 (EC 2.1.1.43; also termed BOP) is a heart and muscle specific SET-MYND domain containing protein, which functions as a histone methyltransferase and regulates downstream gene transcription. It methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. SMYD2 (also termed HSKM-B, or lysine N-methyltransferase 3C (KMT3C)) functions as a histone methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. It specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). SMYD3 (also termed zinc finger MYND domain-containing protein 1) functions as a histone methyltransferase that specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. It also methylates 'Lys-5' of histone H4. SMYD3 plays an important role in transcriptional activation as a member of an RNA polymerase complex. SMYD4 functions as a potential tumor suppressor that plays a critical role in breast carcinogenesis at least partly through inhibiting the expression of PDGFR-alpha. SMYD5 (also termed protein NN8-4AG, or retinoic acid-induced protein 15) functions as histone lysine methyltransferase that mediates H4K20me3 at heterochromatin regions.


Pssm-ID: 380997 [Multi-domain]  Cd Length: 122  Bit Score: 55.08  E-value: 6.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1021 KMGWGVRALQTIPQGtficeyvgELISDAEADVREDDSYLFDLDNKDGEVYCIdaryYGNISRFiNHLCDPNiipVRVFM 1100
Cdd:cd20071      8 SKGRGLVATRDIEPG--------ELILVEKPLVSVPSNSFSLTDGLNEIGVGL----FPLASLL-NHSCDPN---AVVVF 71
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2049844526 1101 LHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWD--------IKSKYFTCQCgsEKC 1149
Cdd:cd20071     72 DGNG----TLRVRALRDIKAGEELTISYIDPLLPrterrrelLEKYGFTCSC--PRC 122
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
229-327 7.15e-09

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 60.39  E-value: 7.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  229 KLNSGGGLSEELGSARRSGEVTLTKGDPGSLEEWETVVGDDFSLYYDSYSVDERVDSDSKSEVEALTEQLSEEEEEEEEE 308
Cdd:TIGR00927  792 KGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEEEE 871
                           90
                   ....*....|....*....
gi 2049844526  309 EEEEEEEEEEEEEEEDEES 327
Cdd:TIGR00927  872 EEEEEEEEEEEEEEEEEEN 890
PHA03100 PHA03100
ankyrin repeat protein; Provisional
650-774 7.41e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 59.29  E-value: 7.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  650 HPRQLYLSVKQGELqKVILMLLDNlDPNFQSDQQSKRTPLHAAAQ--KGSVEICHVLLQAGANINA-------------- 713
Cdd:PHA03100   108 TPLLYAISKKSNSY-SIVEYLLDN-GANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKGVDINAknrvnyllsygvpi 185
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2049844526  714 --VDKQQRTPLMEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTG 774
Cdd:PHA03100   186 niKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
716-857 9.28e-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: 9.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  716 KQQR---TPLMEAVVNNHLEVARYMVQRGGC-VYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGQVDVNAQDSG----GWT 787
Cdd:cd22192     12 QQKRiseSPLLLAAKENDVQAIKKLLKCPSCdLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSdlyqGET 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  788 PIIWAAEHKHIEVIRMLLTRGADVT--------LTDNEENIC------LHWASFTGSAAIAEVLLNARCDLHAVNYHGDT 853
Cdd:cd22192     92 ALHIAVVNQNLNLVRELIARGADVVspratgtfFRPGPKNLIyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171

                   ....
gi 2049844526  854 PLHI 857
Cdd:cd22192    172 VLHI 175
Ank_2 pfam12796
Ankyrin repeats (3 copies);
634-715 1.16e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.58  E-value: 1.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  634 KALVIQESERRKKLRFHPRQLYLSVKQGELQKVILmLLDNLDPNFQSDQqskRTPLHAAAQKGSVEICHVLLQAGANINA 713
Cdd:pfam12796   14 KLLLENGADANLQDKNGRTALHLAAKNGHLEIVKL-LLEHADVNLKDNG---RTALHYAARSGHLEIVKLLLEKGADINV 89

                   ..
gi 2049844526  714 VD 715
Cdd:pfam12796   90 KD 91
Ank_5 pfam13857
Ankyrin repeats (many copies);
770-817 2.00e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.58  E-value: 2.00e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2049844526  770 LLSTGQVDVNAQDSGGWTPIIWAAEHKHIEVIRMLLTRGADVTLTDNE 817
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE 48
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
710-886 2.68e-08

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: 58.17  E-value: 2.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  710 NINAVDKQQRTPLMEAVV-NNHLEVARYMVQRGGCVYSkeedGSTCLHHAAK--IGNLEMVSLLLSTGQVD------VNA 780
Cdd:TIGR00870   44 NINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAV----GDTLLHAISLeyVDAVEAILLHLLAAFRKsgplelAND 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  781 QDSG----GWTPIIWAAEHKHIEVIRMLLTRGADVtltdneeniclhwasftgsaaiaevllNARC--------DLHAVN 848
Cdd:TIGR00870  120 QYTSeftpGITALHLAAHRQNYEIVKLLLERGASV---------------------------PARAcgdffvksQGVDSF 172
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2049844526  849 YHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDT 886
Cdd:TIGR00870  173 YHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNT 210
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
828-889 2.76e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 2.76e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2049844526  828 TGSAAIAEVLLNARCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTA-WD 889
Cdd:PLN03192   535 TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAlWN 597
Ank_4 pfam13637
Ankyrin repeats (many copies);
785-838 2.89e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 2.89e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2049844526  785 GWTPIIWAAEHKHIEVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLL 838
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
822-887 3.40e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 3.40e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2049844526  822 LHWASFTGSAAIAEVLLNARCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRgANPELRNkEGDTA 887
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTA 64
SET_ATXR5_6-like cd10539
SET domain found in fungal protein lysine methyltransferase SET5 and similar protein; The ...
1021-1128 4.28e-08

SET domain found in fungal protein lysine methyltransferase SET5 and similar protein; The family includes Arabidopsis thaliana ATXR5 and ATXR6. Both ATXR5 (also termed protein SET DOMAIN GROUP 15, or TRX-related protein 5) and ATXR6 (also termed protein SET DOMAIN GROUP 34, or TRX-related protein 6) function as histone methyltransferase that specifically monomethylates 'Lys-37' of histone H3 (H3K27me1). They are required for chromatin structure and gene silencing.


Pssm-ID: 380937  Cd Length: 138  Bit Score: 53.18  E-value: 4.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1021 KMGWGVRALQTIPQGTFICEYVGEL--ISDAEADvrEDDSYLFDLDNKDGE---VYCIDARyyGNISRFI----NHLCD- 1090
Cdd:cd10539     13 REGFTVEADGFIKDLTIIAEYTGDVdyIRNREFD--DNDSIMTLLLAGDPSkslVICPDKR--GNIARFIsginNHTKDg 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2049844526 1091 ---PNIIPVRVFMLHQdlrfPRIAFFSSRDIRTGEELGFDY 1128
Cdd:cd10539     89 kkkQNCKCVRYSINGE----ARVLLVATRDIAKGERLYYDY 125
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
686-716 6.40e-07

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 46.90  E-value: 6.40e-07
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2049844526  686 RTPLHAAA-QKGSVEICHVLLQAGANINAVDK 716
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
697-780 8.16e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 8.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  697 SVEICH-----------VLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIGNLE 765
Cdd:PTZ00322    83 TVELCQlaasgdavgarILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFRE 162
                           90
                   ....*....|....*
gi 2049844526  766 MVSLLLSTGQVDVNA 780
Cdd:PTZ00322   163 VVQLLSRHSQCHFEL 177
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
678-865 9.60e-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: 53.16  E-value: 9.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  678 FQSDQqskrTPLHAAAQKGSVEICHVLLQAGANINAvdkqqrtplmeavvnnhlevarymvqRGGCVYSKEEDGSTCLHH 757
Cdd:TIGR00870  125 FTPGI----TALHLAAHRQNYEIVKLLLERGASVPA--------------------------RACGDFFVKSQGVDSFYH 174
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  758 -------AAKIGNLEMVSLLLSTGQvDVNAQDSGGWTPiiwaaehKHIEVIRMLLTrgadvtlTDNEENICL-------H 823
Cdd:TIGR00870  175 gesplnaAACLGSPSIVALLSEDPA-DILTADSLGNTL-------LHLLVMENEFK-------AEYEELSCQmynfalsL 239
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2049844526  824 WASFTGSAAIAEVLlnarcdlhavNYHGDTPLHIAARESYHD 865
Cdd:TIGR00870  240 LDKLRDSKELEVIL----------NHQGLTPLKLAAKEGRIV 271
Ank_5 pfam13857
Ankyrin repeats (many copies);
837-890 1.27e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 1.27e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2049844526  837 LLNAR-CDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDL 890
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PHA02875 PHA02875
ankyrin repeat protein; Provisional
758-897 2.61e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.15  E-value: 2.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  758 AAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIEVIRMLLTRGA--DVTLTDNEENicLHWASFTGSAAIAE 835
Cdd:PHA02875     9 AILFGELDIARRLLDIG-INPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIESE--LHDAVEEGDVKAVE 85
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2049844526  836 VLLNARCDLHAVNYH-GDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDLTPERSDV 897
Cdd:PHA02875    86 ELLDLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
654-861 5.43e-06

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: 50.78  E-value: 5.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  654 LYLSVKQGELQKVILMLLDNLDPNFQSDQQSKrTPLHAAAQKGSVEICHVLLQAGAN-INAVDK----QQRTPLMEAVVN 728
Cdd:cd22192     21 LLLAAKENDVQAIKKLLKCPSCDLFQRGALGE-TALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVVN 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  729 NHLEVARYMVQRGGCVYSKEEDGS------TCLHH--------AAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIiwaae 794
Cdd:cd22192    100 QNLNLVRELIARGADVVSPRATGTffrpgpKNLIYygehplsfAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVL----- 173
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2049844526  795 hkHIevirmlltrgadVTLTDNEENICLhwasftgsaaIAEVLLN--ARCDLHAV----NYHGDTPLHIAARE 861
Cdd:cd22192    174 --HI------------LVLQPNKTFACQ----------MYDLILSydKEDDLQPLdlvpNNQGLTPFKLAAKE 222
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
850-882 7.14e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.82  E-value: 7.14e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2049844526  850 HGDTPLHIAA-RESYHDCVLLFLSRGANPELRNK 882
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02875 PHA02875
ankyrin repeat protein; Provisional
648-741 8.72e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.60  E-value: 8.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  648 RFHPrqLYLSVKQGELQKVILMLLDNLDPNFQSDQQSkrTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLM-EAV 726
Cdd:PHA02875   135 KFSP--LHLAVMMGDIKGIELLIDHKACLDIEDCCGC--TPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAI 210
                           90
                   ....*....|....*
gi 2049844526  727 VNNHLEVARYMVQRG 741
Cdd:PHA02875   211 ENNKIDIVRLFIKRG 225
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
828-893 8.96e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 8.96e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2049844526  828 TGSAAIAEVLLNARCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDLTPE 893
Cdd:PTZ00322    92 SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
Ank_5 pfam13857
Ankyrin repeats (many copies);
737-792 1.06e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 1.06e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2049844526  737 MVQRGGC-VYSKEEDGSTCLHHAAKIGNLEMVSLLLsTGQVDVNAQDSGGWTPIIWA 792
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
225-332 1.13e-05

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 49.99  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  225 AKRRKLNSGGGLSEELGSARRSGEVTL-----TKGDPGSL-----EEWETVVGDDFSLYYDSYSVDERVDSDSKSEVEAL 294
Cdd:TIGR00927  759 GDRKETEHEGETEAEGKEDEDEGEIQAgedgeMKGDEGAEgkvehEGETEAGEKDEHEGQSETQADDTEVKDETGEQELN 838
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2049844526  295 TEQLSEEEEEEE-------------EEEEEEEEEEEEEEEEEDEESGNQSD 332
Cdd:TIGR00927  839 AENQGEAKQDEKgvdggggsdggdsEEEEEEEEEEEEEEEEEEEEEEEEEE 889
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
785-813 1.25e-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: 1.25e-05
                            10        20
                    ....*....|....*....|....*....
gi 2049844526   785 GWTPIIWAAEHKHIEVIRMLLTRGADVTL 813
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
755-838 1.29e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  755 LHHAAKIGNLEMVSLLLSTGqVDVNAQDSGGWTPIIWAAEHKHIEVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIA 834
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164

                   ....
gi 2049844526  835 EVLL 838
Cdd:PTZ00322   165 QLLS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
668-751 1.77e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 1.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  668 LMLLDNLDPNfqSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQRGGCVYSK 747
Cdd:PTZ00322   100 ILLTGGADPN--CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177

                   ....
gi 2049844526  748 EEDG 751
Cdd:PTZ00322   178 GANA 181
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
785-816 1.83e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 1.83e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2049844526  785 GWTPIIWAAEH-KHIEVIRMLLTRGADVTLTDN 816
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
1013-1134 2.23e-05

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


Pssm-ID: 380938  Cd Length: 112  Bit Score: 44.55  E-value: 2.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1013 RLQLYRTAKMGWGVRALQTIPQGTFIcEYVGELISDAEADVREDDSYLFDLdnkdgeVYCIDARYY----GNISRFiNHL 1088
Cdd:cd10540      1 RLEVKPSTLKGRGVFATRPIKKGEVI-EEAPVIVLPKEEYQHLCKTVLDHY------VFSWGDGCLalalGYGSMF-NHS 72
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2049844526 1089 CDPNIIPVRVFMLHqdlrfpRIAFFSSRDIRTGEELGFDYGDRFWD 1134
Cdd:cd10540     73 YTPNAEYEIDFENQ------TIVFYALRDIEAGEELTINYGDDLWD 112
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
686-713 2.38e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 2.38e-05
                            10        20
                    ....*....|....*....|....*...
gi 2049844526   686 RTPLHAAAQKGSVEICHVLLQAGANINA 713
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
750-782 2.39e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.28  E-value: 2.39e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2049844526  750 DGSTCLHHAA-KIGNLEMVSLLLSTGqVDVNAQD 782
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKG-ADVNARD 33
PHA02798 PHA02798
ankyrin-like protein; Provisional
667-779 2.48e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 48.29  E-value: 2.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  667 ILMLLDNLDPNFQSDQQSKRTPL-----HAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVN---NHLEVARYMV 738
Cdd:PHA02798    53 IVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMI 132
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2049844526  739 QRGGCVYSKEEDGSTCLHHAAKIGN---LEMVSLLLSTGqVDVN 779
Cdd:PHA02798   133 ENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKG-VDIN 175
Ank_4 pfam13637
Ankyrin repeats (many copies);
821-871 3.31e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 3.31e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2049844526  821 CLHWASFTGSAAIAEVLLNARCDLHAVNYHGDTPLHIAARESYHDCVLLFL 871
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
801-872 5.10e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 5.10e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2049844526  801 IRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNARCDLHAVNYHGDTPLHIAARESYHDCVLLFLS 872
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
850-879 1.12e-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: 1.12e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 2049844526   850 HGDTPLHIAARESYHDCVLLFLSRGANPEL 879
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
670-722 1.17e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 1.17e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2049844526  670 LLDNLDPNFQSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPL 722
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02859 PHA02859
ankyrin repeat protein; Provisional
697-789 1.19e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.81  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  697 SVEICHVLLQAGANINAVDKQQRTPLMEAV--VNNHLEVARYMVQRGGCVYSKEEDGSTCLH-----HAAKignlEMVSL 769
Cdd:PHA02859   102 EPEILKILIDSGSSITEEDEDGKNLLHMYMcnFNVRINVIKLLIDSGVSFLNKDFDNNNILYsyilfHSDK----KIFDF 177
                           90       100
                   ....*....|....*....|
gi 2049844526  770 LLSTGqVDVNAQDSGGWTPI 789
Cdd:PHA02859   178 LTSLG-IDINETNKSGYNCY 196
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
750-780 1.30e-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: 1.30e-04
                            10        20        30
                    ....*....|....*....|....*....|.
gi 2049844526   750 DGSTCLHHAAKIGNLEMVSLLLSTGqVDVNA 780
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKG-ADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
687-749 1.36e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.81  E-value: 1.36e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2049844526  687 TPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQRGGCVYSKEE 749
Cdd:PHA03100   194 TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
1023-1132 1.41e-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: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1023 GWGVRALQTIPQGTFICEYVGELISDAEAdvrEDDSYLFDLDNKDGEVYCIDAR--YYGNISRFIN---HLCDPNIIpvr 1097
Cdd:cd19193     19 GLGVWAEAPIPKGMVFGPYEGEIVEDEEA---ADSGYSWQIYKGGKLSHYIDAKdeSKSNWMRYVNcarNEEEQNLV--- 92
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2049844526 1098 VFMLHQDlrfprIAFFSSRDIRTGEELGFDYGDRF 1132
Cdd:cd19193     93 AFQYRGK-----IYYRTCKDIAPGTELLVWYGDEY 122
PHA03247 PHA03247
large tegument protein UL36; Provisional
42-204 1.98e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526   42 GDTPRSEETLPKATPDSLEPAGPSSPASVTVTVgdegadtPVGATPLIGDESENLEGDGDLRGGRILLGHATKSFPSSPS 121
Cdd:PHA03247  2753 GPARPARPPTTAGPPAPAPPAAPAAGPPRRLTR-------PAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPA 2825
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526  122 kGGSCPSRAKMSMTGAGKSPPSVQSLAMRLLSMPGAQGAAAAGSEPPPATTSPEGQPKVHR-ARKTMSKPGN--GQPPVP 198
Cdd:PHA03247  2826 -GPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRlARPAVSRSTEsfALPPDQ 2904

                   ....*.
gi 2049844526  199 EKRPPE 204
Cdd:PHA03247  2905 PERPPQ 2910
SET_KMT2E cd19182
SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...
1026-1129 3.04e-04

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


Pssm-ID: 380959  Cd Length: 129  Bit Score: 41.80  E-value: 3.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1026 VRALQTIPQGTFICEYVGELISDAEAdvrEDDSYLFD--------LDNKDGEVYCIDARYYGNISRFINHLCDPNIIPVR 1097
Cdd:cd19182     21 LKAAKDLPPDTLIIEYRGKFMLREQF---EANGYFFKrpypfvlfYSKFHGLEMCVDARTFGNEARFIRRSCTPNAEVRH 97
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2049844526 1098 VF---MLHqdlrfprIAFFSSRDIRTGEEL----GFDYG 1129
Cdd:cd19182     98 VIedgTIH-------LYIYSIRSIPKGTEItiafDFDYG 129
Ank_5 pfam13857
Ankyrin repeats (many copies);
704-758 3.80e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 3.80e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2049844526  704 LLQAG-ANINAVDKQQRTPLMEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHA 758
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PR-SET_PRDM6 cd19191
PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 ...
1023-1132 4.77e-04

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


Pssm-ID: 380968  Cd Length: 128  Bit Score: 41.31  E-value: 4.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1023 GWGVRALQTIPQGTFICEYVGELIS-DAEADVREDDSYLFDLDNKDGEV-YCIDAR--YYGNISRFIN---HLCDPNIIP 1095
Cdd:cd19191     16 GYGICAAQRIPQGTWIGPFEGVLVSpEKQIGAVRNTQHLWEIYDQEGTLqHFIDGGdpSKSSWMRYIRcarHCGEQNLTV 95
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2049844526 1096 VRvfmlHQDLRFPRIAffssRDIRTGEELGFDYGDRF 1132
Cdd:cd19191     96 VQ----YRGCIFYRAC----RDIPRGTELLVWYDDSY 124
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
686-713 5.68e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.39  E-value: 5.68e-04
                           10        20
                   ....*....|....*....|....*...
gi 2049844526  686 RTPLHAAAQKGSVEICHVLLQAGANINA 713
Cdd:pfam13606    3 NTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
785-811 7.85e-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: 7.85e-04
                           10        20
                   ....*....|....*....|....*..
gi 2049844526  785 GWTPIIWAAEHKHIEVIRMLLTRGADV 811
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADI 28
SET_SMYD4 cd10536
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
1084-1144 9.98e-04

SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing protein 4 (SMYD4) and similar proteins; SMYD4 functions as a potential tumor suppressor that plays a critical role in breast carcinogenesis at least partly through inhibiting the expression of PDGFR-alpha. In zebrafish, SMYD4 is ubiquitously expressed in early embryos and becomes enriched in the developing heart; mutants show a strong defect in cardiomyocyte proliferation, which lead to a severe cardiac malformation.


Pssm-ID: 380934 [Multi-domain]  Cd Length: 218  Bit Score: 41.90  E-value: 9.98e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2049844526 1084 FINHLCDPNIIpvRVFMLHQdlrfprIAFFSSRDIRTGEELGFDYG------DRFW---DIKSKY-FTCQC 1144
Cdd:cd10536    153 LLNHSCDPNTI--RSFYGNT------IVVRATRPIKKGEEITICYGphfsrmKRSErqrLLKEQYfFDCSC 215
PR-SET_PRDM14 cd19198
PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 ...
1014-1132 1.05e-03

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


Pssm-ID: 380975  Cd Length: 133  Bit Score: 40.46  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1014 LQLYRTAKMG---WGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLdNKDGEV-YCIDAR-YYGNISRFINhl 1088
Cdd:cd19198      7 LRVLQTSFGGtphYGVFCKKTIPKGTRFGPFRGRVVNTSEIKTYDDNSFMWEI-FEDGKLsHFIDGRgSTGNWMSYVN-- 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2049844526 1089 C-----DPNIIPVRvfmlHQDlrfpRIAFFSSRDIRTGEELGFDYGDRF 1132
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 ...
1006-1092 1.71e-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: 1.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049844526 1006 VQSGIKVRLQLYRTAkmgwgVRALQTIPQGTFICEYVGELISDAEADV-----REDDSYLFDLDNKDGEVYCIDARYYGN 1080
Cdd:cd19181      6 LQLGRVTRVQKHRKI-----LRAARDLALDTLIIEYRGKVMLRQQFEVnghffKRPYPFVLFYSKFNGVEMCVDARTFGN 80
                           90
                   ....*....|..
gi 2049844526 1081 ISRFINHLCDPN 1092
Cdd:cd19181     81 DARFIRRSCTPN 92
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
750-780 5.95e-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: 5.95e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2049844526  750 DGSTCLHHAAKIGNLEMVSLLLSTGqVDVNA 780
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENG-ADINA 30
 
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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