NCBI Conserved Domain Search

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...

970-1020

8.55e-04

Pssm-ID: 276966 [Multi-domain] Cd Length: 48 Bit Score: 39.61 E-value: 8.55e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 817208853  970 RCTVCQTCHLRAGPKLSCIRCRQSFHHSCLsksGVSARLYSPDRPYVCQSC 1020
Cdd:cd15489     1 SCIVCGKGGDLGGELLQCDGCGKWFHADCL---GPPLSSFVPNGKWICPVC 48

Name

Accession

Description

Interval

E-value

SET_KMT2A_2B

cd19170

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...

3294-3445

6.95e-111

Pssm-ID: 380947 [Multi-domain] Cd Length: 152 Bit Score: 349.38 E-value: 6.95e-111

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3294 MAMRFRILKETSKESVGVYHSHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNIGCYMFKIDDHLVVDA 3373
Cdd:cd19170     1 MAMRFRHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKYYESKGIGCYMFRIDDDEVVDA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 817208853 3374 TMKGNAARFINHSCEPNCYSRVVDILGKKHILIFALRRIVQGEELTYDYKFPFEDIKIPCTCGSRRCRKYLN 3445
Cdd:cd19170    81 TMHGNAARFINHSCEPNCYSRVVNIDGKKHIVIFALRRILRGEELTYDYKFPIEDVKIPCTCGSKKCRKYLN 152

ePHD_KMT2A_like

cd15664

Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The ...

1407-1511

1.01e-57

Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of histone-lysine N-methyltransferase trithorax (Trx) like proteins, KMT2A/MLL1 and KMT2B/MLL2. KMT2A and KMT2B comprise the mammalian Trx branch of COMPASS family, and are both essential for mammalian embryonic development. KMT2A regulates chromatin-mediated transcription through the catalysis of methylation of histone 3 lysine 4 (H3K4), and is frequently rearranged in acute leukemia. KMT2A functions as the catalytic subunit in the MLL1 complex. KMT2B is a second human homolog of Drosophila trithorax, located on chromosome 19 and functions as the catalytic subunit in the MLL2 complex. It plays a critical role in memory formation by mediating hippocampal H3K4 di- and trimethylation. It is also required for RNA polymerase II association and protection from DNA methylation at the MagohB CpG island promoter. Both KMT2A and KMT2B contain a CxxC (x for any residue) zinc finger domain, three PHD fingers, this extended PHD (ePHD) finger, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain.

Pssm-ID: 277134 Cd Length: 105 Bit Score: 195.32 E-value: 1.01e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCKGLGDGYEMKEGRLLYCGQNEWVHANCALWSNEVFEEIDGSLQNVHSAISRGRLIRCTECGKKGASVGCCSRNCNS 1486
Cdd:cd15664     1 CALCGVYGDDEPNDAGRLLYCGQDEWVHINCALWSAEVFEEDDGSLQNVHSAVSRGRMMKCELCGKPGATVGCCLKSCPA 80

                          90       100
                  ....*....|....*....|....*
gi 817208853 1487 TFHYPCARAIGLAFNDDKTVFCSLH 1511
Cdd:cd15664    81 NYHFMCARKAECVFQDDKKVFCPAH 105

SET

smart00317

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

3307-3428

2.67e-44

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: 157.50 E-value: 2.67e-44

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853   3307 ESVGVYHSHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNI-GCYMFKIDDHLVVDATMKGNAARFINH 3385
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkAFYLFDIDSDLCIDARRKGNLARFINH 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 817208853   3386 SCEPNCYSRVVDILGKKHILIFALRRIVQGEELTYDYKFPFED 3428
Cdd:smart00317   81 SCEPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYAN 123

SET

COG2940

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

3314-3442

2.04e-37

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

Pssm-ID: 442183 [Multi-domain] Cd Length: 134 Bit Score: 138.56 E-value: 2.04e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3314 SHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNIgcYMFKIDDHLVVDATMKGNAARFINHSCEPNCYS 3393
Cdd:COG2940    13 SPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKEPLHT--YLFELDDDGVIDGALGGNPARFINHSCDPNCEA 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 817208853 3394 RVVDilgkKHILIFALRRIVQGEELTYDYKFPFEDIKIPCTCGSrrCRK 3442
Cdd:COG2940    91 DEED----GRIFIVALRDIAAGEELTYDYGLDYDEEEYPCRCPN--CRG 133

PHD3_KMT2A_like

cd15508

PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...

1053-1109

3.59e-34

Pssm-ID: 276983 Cd Length: 57 Bit Score: 126.41 E-value: 3.59e-34

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 817208853 1053 YCPLCQRCYNENDFDTKMMECNECSCWVHARCEGLSDERYQVLSYLPDSIEFTCRQC 1109
Cdd:cd15508     1 YCPLCEKCYDDDDYDSKMMQCSQCDHWVHAKCEGLSDEMYEILSYLPESIEYTCSLC 57

SET

pfam00856

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...

3318-3423

3.39e-33

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: 125.71 E-value: 3.39e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  3318 GRGLFCLRDIEAGEMVIEYAGE-VIRASLTDKREKYYDSKNI----GCYMFKIDDH--LVVDAT--MKGNAARFINHSCE 3388
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLElrlwGPYLFTLDEDseYCIDARalYYGNWARFINHSCD 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 817208853  3389 PNCYSRVVDILGKKHILIFALRRIVQGEELTYDYK 3423
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115

FYRC

pfam05965

F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...

3146-3226

1.13e-22

F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It is similar to SMART:SM00542.

Pssm-ID: 461788 Cd Length: 83 Bit Score: 94.21 E-value: 1.13e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  3146 GPSLMYEIKSQDGFTHTASSMSEIWDTVFKAVQAARRAHNLPPLPHNPLT--ENLGLDNNATVYLVEQLPGVNRCTKYKP 3223
Cdd:pfam05965    1 GPLFRVTVEEDPDESFEGSSPTKCWSMVLERVQELRREAGLKLKLPESISgeDMFGLTHPAVVRLIESLPGAEKCTNYKF 80


                   ...
gi 817208853  3224 RFH 3226
Cdd:pfam05965   81 RYG 83

FYRC

smart00542

FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region ...

3149-3226

1.68e-17

FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region (FYRN), but sometimes is far distant. Unknown function, but occurs frequently in chromatin-associated proteins.

Pssm-ID: 197781 Cd Length: 86 Bit Score: 79.65 E-value: 1.68e-17

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853   3149 LMYEIKSQDGFTHTASSMSEIWDTVFKAVQAARRAHNLPPLPHNPL--TENLGLDNNATVYLVEQLPGVNRCTKYKPRFH 3226
Cdd:smart00542    2 FRVEIESDPGEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEGVsgEEMFGLSSPAVVKLIEALPGVHQCTNYWFRYH 81

PHD1_KMT2A_like

cd15506

PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...

926-971

6.25e-17

Pssm-ID: 276981 Cd Length: 47 Bit Score: 76.63 E-value: 6.25e-17

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 817208853  926 VCYLCGSAGKEPLIHCQCCCEPYHVFCLEPSEWSAC-AQSNWSCPRC 971
Cdd:cd15506     1 LCFLCGSAGLNELLYCSVCCEPYHTFCLEEAERPLNiNKDNWCCRRC 47

zf-HC5HC2H

pfam13771

PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...

1434-1511

1.57e-13

PHD-like zinc-binding domain; The members of this family are annotated as containing PHD domain, but the zinc-binding region here is not typical of PHD domains. The conformation here is a well-conserved cysteine-histidine rich region spanning 90 residues, where the Cys and His are arranged as HxxC(31)CxxC(6)CxxCxxxxCxxxxHxxC (21)CxxH.

Pssm-ID: 463977 [Multi-domain] Cd Length: 88 Bit Score: 68.51 E-value: 1.57e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  1434 HANCALWSNEV-FEEIDG---SLQNVHSAISRGRLIRCTECGKK-GASVGCCSRNCNSTFHYPCARAIGLAF-----NDD 1503
Cdd:pfam13771    1 HVVCALWSPELvQRGNDSmgfPIEDIEKIPKRRWKLKCYLCKKKgGACIQCSKKNCRRAFHVTCALEAGLLMqfdedNGT 80


                   ....*...
gi 817208853  1504 KTVFCSLH 1511
Cdd:pfam13771   81 FKSYCKKH 88

FYRN

pfam05964

F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...

1554-1601

1.10e-11

F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It is similar to SMART:SM00541.

Pssm-ID: 461787 Cd Length: 51 Bit Score: 62.14 E-value: 1.10e-11

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 817208853  1554 GSLTIDCLGTVVPQ--FSDTPEKIIPSDYKCSRLYWSTVNPLKIVKYYIR 1601
Cdd:pfam05964    1 GSLTVLSLGEIVPDrpAFHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCE 50

SP2_N

cd22540

N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...

2452-2768

8.04e-11

N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.

Pssm-ID: 411776 [Multi-domain] Cd Length: 511 Bit Score: 67.64 E-value: 8.04e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2452 GTIIQQQPGAIQCGVISSEQLVLSSTPTLEMFTDSTGSmfvSSQPMYYGLETIVSNTVMS-SSQFMAG-AVPQVLASSYQ 2529
Cdd:cd22540    83 GNIIQLQGSQLSSSAPGGQQVFAIQNPTMIIKGSQTRS---STNQQYQISPQIQAAGQINnSGQIQIIpGTNQAIITPVQ 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2530 TTTQVFQASKLME----PIVDVQAVSAVPGVPAvpTVPTVQAVQNVPGVQPVQN--VPAVPSIQTVPGVQPV-------- 2595
Cdd:cd22540   160 VLQQPQQAHKPVPikpaPLQTSNTNSASLQVPG--NVIKLQSGGNVALTLPVNNlvGTQDGATQLQLAAAPSkpskkirk 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2596 QSLPGVQSGVQVQsvagmQAVQGVPgVQSVQSVTGAQGiRNLSGVQAvpavPPGQNVPTVQPVQGLPGVQAVQSV----- 2670
Cdd:cd22540   238 KSAQAAQPAVTVA-----EQVETVL-IETTADNIIQAG-NNLLIVQS----PGTGQPAVLQQVQVLQPKQEQQVVqipqq 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2671 --RGVTNQHAGYI------LMN-QQPAPAPEPKRVaaprVTMQPPPEQQTyasIGCDAVPPPAPCRPSVEAVRPVRVPPe 2741
Cdd:cd22540   307 alRVVQAASATLPtvpqkpLQNiQIQNSEPTPTQV----YIKTPSGEVQT---VLLQEAPAATATPSSSTSTVQQQVTA- 378

                         330       340
                  ....*....|....*....|....*..
gi 817208853 2742 aslvSSGPTTTSPKPLQHATPTIPRVA 2768
Cdd:cd22540   379 ----NNGTGTSKPNYNVRKERTLPKIA 401

PHA03247

large tegument protein UL36; Provisional

2549-2843

3.90e-10

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 66.50 E-value: 3.90e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2549 AVSAVPGVPAVPTVPTVQAVQNVPGVQPVQNVPAVPSIQTVPGVQPVQSLPgvQSGVQVQSVAGMQAVQGVPGVQSVQSV 2628
Cdd:PHA03247 2734 ALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLT--RPAVASLSESRESLPSPWDPADPPAAV 2811

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2629 TGAQGIRNLSGVQAVPAVPPGQNVPTVQPVQGLPGVQAVQSVRGVTnqhAGYILMNQQPAPAPEPKRVAAPRVTM----Q 2704
Cdd:PHA03247 2812 LAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA---PGGDVRRRPPSRSPAAKPAAPARPPVrrlaR 2888

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2705 PPPEQQTYASigcdAVPPPAPCRPSVEAVRPVRVPPEASLVSSGPT---------------TTSPKPLQHATPTIP---- 2765
Cdd:PHA03247 2889 PAVSRSTESF----ALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQppppppprpqpplapTTDPAGAGEPSGAVPqpwl 2964

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2766 ------RVAV-----------RPSPAShATPHVTAHVTSHVTPHATS---HVTATPhqlhPPWKVSEALFGAEQPVDGGA 2825
Cdd:PHA03247 2965 galvpgRVAVprfrvpqpapsREAPAS-STPPLTGHSLSRVSSWASSlalHEETDP----PPVSLKQTLWPPDDTEDSDA 3039

                         330
                  ....*....|....*...
gi 817208853 2826 RPYFDSKHVSENTSMIKP 2843
Cdd:PHA03247 3040 DSLFDSDSERSDLEALDP 3057

PHD

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...

1053-1112

4.38e-07

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains. Several PHD fingers have been identified as binding modules of methylated histone H3.

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 49.03 E-value: 4.38e-07

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  1053 YCPLCQRcyneNDFDTKMMECNECSCWVHARCEGLSDERYQVLSYlpdsiEFTCRQCSPD 1112
Cdd:pfam00628    1 YCAVCGK----SDDGGELVQCDGCDDWFHLACLGPPLDPAEIPSG-----EWLCPECKPK 51

Glutenin_hmw

pfam03157

High molecular weight glutenin subunit; Members of this family include high molecular weight ...

2246-2712

5.45e-06

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.

Pssm-ID: 367362 [Multi-domain] Cd Length: 786 Bit Score: 52.64 E-value: 5.45e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  2246 PSLCSDSGlQRSNPAASVPLTIPEGINAPSTPSPQVSPTFSSTGVQTATNESPQSMQSPKAAKprspraprpraKGIKPH 2325
Cdd:pfam03157  167 PTSPQQSG-QRQQPGQGQQLRQGQQGQQSGQGQPGYYPTSSQQPGQLQQTGQGQQGQQPERGQ-----------QGQQPG 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  2326 LLKSPAQAHPGHVRFQPMQSAtpviQLQQAQRPAGPTVILQQVASPNILSAYVETLQQQSGQQNLQYIAAIGGQHEAGFK 2405
Cdd:pfam03157  235 QGQQPGQGQQGQQPGQPQQLG----QGQQGYYPISPQQPRQWQQSGQGQQGYYPTSLQQPGQGQSGYYPTSQQQAGQLQQ 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  2406 PQfiaanQIVPGAYIQASSDNLLALQNG----GISVLPGVQIAQPQPTVLGTIiQQQPGAIQCGV--ISSEQLVLSSTPT 2479
Cdd:pfam03157  311 EQ-----QLGQEQQDQQPGQGRQGQQPGqgqqGQQPAQGQQPGQGQPGYYPTS-PQQPGQGQPGYypTSQQQPQQGQQPE 384

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  2480 LEMFTDSTGSMFVSSQPMY-----YGLETIVSNTVMSSSQFMAGAVPqvlaSSYQTTTQVFQASKLMEPIVDVQAVSAVP 2554
Cdd:pfam03157  385 QGQQGQQQGQGQQGQQPGQgqqpgQGQPGYYPTSPQQSGQGQPGYYP----TSPQQSGQGQQPGQGQQPGQEQPGQGQQP 460

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  2555 GvpavptvptvQAVQNVPGVQPVQnvpavpsiqtvpGVQPVQSLPGV------QSGVQVQSVAGMQAVQGVPGVQSVQSV 2628
Cdd:pfam03157  461 G----------QGQQGQQPGQPEQ------------GQQPGQGQPGYyptspqQSGQGQQLGQWQQQGQGQPGYYPTSPL 518

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  2629 TGAQGIRNLSgvqavPAVP--PGQNVPTVQPVQGLPGVQAVQSVRGVTNQHAGYILMNQQPApapEPKRVAAPRVTMQPP 2706
Cdd:pfam03157  519 QPGQGQPGYY-----PTSPqqPGQGQQLGQLQQPTQGQQGQQSGQGQQGQQPGQGQQGQQPG---QGQQGQQPGQGQQPG 590


                   ....*.
gi 817208853  2707 PEQQTY 2712
Cdd:pfam03157  591 QGQPGY 596

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

926-971

7.19e-06

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in epigenetics and chromatin-mediated transcriptional regulation. The PHD finger binds two zinc ions using the so-called 'cross-brace' motif and is thus structurally related to the RING finger and the FYVE finger. It is not yet known if PHD fingers have a common molecular function. Several reports suggest that it can function as a protein-protein interacton domain and it was recently demonstrated that the PHD finger of p300 can cooperate with the adjacent BROMO domain in nucleosome binding in vitro. Other reports suggesting that the PHD finger is a ubiquitin ligase have been refuted as these domains were RING fingers misidentified as PHD fingers.

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 45.28 E-value: 7.19e-06

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 817208853    926 VCYLCGSA-GKEPLIHCQCCCEPYHVFCLEPSEWSACAQSNWSCPRC 971
Cdd:smart00249    1 YCSVCGKPdDGGELLQCDGCDRWYHQTCLGPPLLEEEPDGKWYCPKC 47

FYRN

smart00541

FY-rich domain, N-terminal region; is sometimes closely juxtaposed with the C-terminal region ...

1561-1598

2.81e-05

FY-rich domain, N-terminal region; is sometimes closely juxtaposed with the C-terminal region (FYRC), but sometimes is far distant. Unknown function, but occurs frequently in chromatin-associated proteins.

Pssm-ID: 128814 Cd Length: 44 Bit Score: 43.81 E-value: 2.81e-05

                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 817208853   1561 LGTVVPQFSDTPEKIIPSDYKCSRLYWSTVNPLKIVKY 1598
Cdd:smart00541    1 LLPIQGKLFHSESAIFPVGYKSTRKYWSVKDPNRRCLY 38

PHD

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...

926-974

2.95e-05

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 44.02 E-value: 2.95e-05

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 817208853   926 VCYLCGSAGK-EPLIHCQCCCEPYHVFCLEPSEWSACAQSN-WSCPRCTVC 974
Cdd:pfam00628    1 YCAVCGKSDDgGELVQCDGCDDWFHLACLGPPLDPAEIPSGeWLCPECKPK 51

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

1053-1109

3.89e-05

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 43.35 E-value: 3.89e-05

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 817208853   1053 YCPLCQRCYNENDfdtkMMECNECSCWVHARCEGLSDEryqvlSYLPDSiEFTCRQC 1109
Cdd:smart00249    1 YCSVCGKPDDGGE----LLQCDGCDRWYHQTCLGPPLL-----EEEPDG-KWYCPKC 47

PHA03247

large tegument protein UL36; Provisional

2638-2985

5.20e-05

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.55 E-value: 5.20e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2638 SGVQAVPAVPPGQNVPTVQPVQGLPGVQAVQSVRGVTnqhAGyilmnqQPAPAPEPKRVAAPRVTMQPPPeqqtYASIGC 2717
Cdd:PHA03247 2727 AARQASPALPAAPAPPAVPAGPATPGGPARPARPPTT---AG------PPAPAPPAAPAAGPPRRLTRPA----VASLSE 2793

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2718 DAVPPPAPCRPSVEAVrPVRVPPEASLVSSGPTTTSPKPLQhATPTIPRVAVRPSPASHATPHVTA---HVTSHVTPHAT 2794
Cdd:PHA03247 2794 SRESLPSPWDPADPPA-AVLAPAAALPPAASPAGPLPPPTS-AQPTAPPPPPGPPPPSLPLGGSVApggDVRRRPPSRSP 2871

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2795 SHVTATPHqlHPPWK------VSEALFGAEQPVDGGARPYFDSKHVSENTSMIKPSISSKIPPLPDHCITQrnvdvNKLS 2868
Cdd:PHA03247 2872 AAKPAAPA--RPPVRrlarpaVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQ-----PPLA 2944

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2869 HDVNIVHNSysniMPSGNAGSV-NGNGANANVSVA-NKISMPMSNAPT---SRPMNRVLPMQAVAPKQDSLEPVEKPDIV 2943
Cdd:PHA03247 2945 PTTDPAGAG----EPSGAVPQPwLGALVPGRVAVPrFRVPQPAPSREApasSTPPLTGHSLSRVSSWASSLALHEETDPP 3020

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 817208853 2944 EEPLKPEAESPkEELEDSKKRIVEIADPvKRVEVEA-DEVPAE 2985
Cdd:PHA03247 3021 PVSLKQTLWPP-DDTEDSDADSLFDSDS-ERSDLEAlDPLPPE 3061

COG5141

PHD zinc finger-containing protein [General function prediction only];

1430-1498

6.86e-04

PHD zinc finger-containing protein [General function prediction only];

Pssm-ID: 227470 [Multi-domain] Cd Length: 669 Bit Score: 45.36 E-value: 6.86e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 817208853 1430 NEWVHANCALWSNEVF-------EEIDGsLQNVHSaiSRGRLIrCTECGKK-GASVGCCSRNCNSTFHYPCARAIGL 1498
Cdd:COG5141   266 GRWGHVICAMFNPELSfghllskDPIDN-IASVSS--SRWKLG-CLICKEFgGTCIQCSYFNCTRAYHVTCARRAGY 338

PHD_SF

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...

970-1020

8.55e-04

Pssm-ID: 276966 [Multi-domain] Cd Length: 48 Bit Score: 39.61 E-value: 8.55e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 817208853  970 RCTVCQTCHLRAGPKLSCIRCRQSFHHSCLsksGVSARLYSPDRPYVCQSC 1020
Cdd:cd15489     1 SCIVCGKGGDLGGELLQCDGCGKWFHADCL---GPPLSSFVPNGKWICPVC 48

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

970-1020

1.16e-03

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 39.12 E-value: 1.16e-03

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 817208853    970 RCTVCQTCHLrAGPKLSCIRCRQSFHHSCLsksGVSARLYSPDRPYVCQSC 1020
Cdd:smart00249    1 YCSVCGKPDD-GGELLQCDGCDRWYHQTCL---GPPLLEEEPDGKWYCPKC 47

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

1466-1511

6.89e-03

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 37.19 E-value: 6.89e-03

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 817208853   1466 RCTECGKK---GASVGCCsrNCNSTFHYPCARAIGLAFNDDKTVFCSLH 1511
Cdd:smart00249    1 YCSVCGKPddgGELLQCD--GCDRWYHQTCLGPPLLEEEPDGKWYCPKC 47

Name

Accession

Description

Interval

E-value

SET_KMT2A_2B

cd19170

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...

3294-3445

6.95e-111

Pssm-ID: 380947 [Multi-domain] Cd Length: 152 Bit Score: 349.38 E-value: 6.95e-111

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3294 MAMRFRILKETSKESVGVYHSHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNIGCYMFKIDDHLVVDA 3373
Cdd:cd19170     1 MAMRFRHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKYYESKGIGCYMFRIDDDEVVDA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 817208853 3374 TMKGNAARFINHSCEPNCYSRVVDILGKKHILIFALRRIVQGEELTYDYKFPFEDIKIPCTCGSRRCRKYLN 3445
Cdd:cd19170    81 TMHGNAARFINHSCEPNCYSRVVNIDGKKHIVIFALRRILRGEELTYDYKFPIEDVKIPCTCGSKKCRKYLN 152

SET_KMT2A

cd19206

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...

3294-3445

2.19e-84

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: 273.82 E-value: 2.19e-84

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3294 MAMRFRILKETSKESVGVYHSHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNIGCYMFKIDDHLVVDA 3373
Cdd:cd19206     1 MPMRFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREKYYDSKGIGCYMFRIDDSEVVDA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 817208853 3374 TMKGNAARFINHSCEPNCYSRVVDILGKKHILIFALRRIVQGEELTYDYKFPFEDI--KIPCTCGSRRCRKYLN 3445
Cdd:cd19206    81 TMHGNAARFINHSCEPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKFPIEDAsnKLPCNCGAKKCRKFLN 154

SET_SETD1-like

cd10518

SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...

3294-3441

1.13e-82

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: 268.70 E-value: 1.13e-82

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3294 MAMRFRILKETSKESVGVYHSHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNI-GCYMFKIDDHLVVD 3372
Cdd:cd10518     1 MSKRFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKRYDEEGGgGTYMFRIDEDLVID 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3373 ATMKGNAARFINHSCEPNCYSRVVDILGKKHILIFALRRIVQGEELTYDYKFPFEDI-KIPCTCGSRRCR 3441
Cdd:cd10518    81 ATKKGNIARFINHSCDPNCYAKIITVDGEKHIVIFAKRDIAPGEELTYDYKFPIEDEeKIPCLCGAPNCR 150

SET_KMT2B

cd19207

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...

3294-3445

2.85e-77

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: 253.41 E-value: 2.85e-77

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3294 MAMRFRILKETSKESVGVYHSHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNIGCYMFKIDDHLVVDA 3373
Cdd:cd19207     1 MAMRFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDSKGIGCYMFRIDDFDVVDA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 817208853 3374 TMKGNAARFINHSCEPNCYSRVVDILGKKHILIFALRRIVQGEELTYDYKFPFEDI--KIPCTCGSRRCRKYLN 3445
Cdd:cd19207    81 TMHGNAARFINHSCEPNCYSRVIHVEGQKHIVIFALRKIYRGEELTYDYKFPIEDAsnKLPCNCGAKRCRRFLN 154

SET_SETD1

cd19169

SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...

3296-3441

1.22e-60

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: 205.26 E-value: 1.22e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3296 MRFRILKeTSKESVGVYHSHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNIG-CYMFKIDDHLVVDAT 3374
Cdd:cd19169     3 LKFNQLK-FRKKQLKFAKSRIHDWGLFALEPIAADEMVIEYVGQVIRQSVADEREKRYEAIGIGsSYLFRVDDDTIIDAT 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 817208853 3375 MKGNAARFINHSCEPNCYSRVVDILGKKHILIFALRRIVQGEELTYDYKFPFEDIKIPCTCGSRRCR 3441
Cdd:cd19169    82 KCGNLARFINHSCNPNCYAKIITVESQKKIVIYSKRPIAVNEEITYDYKFPIEDEKIPCLCGAPQCR 148

SET_KMT2C_2D

cd19171

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...

3298-3444

1.25e-59

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: 202.66 E-value: 1.25e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3298 FRILKETSKESVGVYHSHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNIGCYMFKIDDHLVVDATMKG 3377
Cdd:cd19171     5 YRKLKTEWRSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNRGIYMFRIDNDWVIDATMTG 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 817208853 3378 NAARFINHSCEPNCYSRVVDILGKKHILIFALRRIVQGEELTYDYKFPFEDI--KIPCTCGSRRCRKYL 3444
Cdd:cd19171    85 GPARYINHSCNPNCVAEVVTFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDqhKIPCLCGAPNCRKWM 153

ePHD_KMT2A_like

cd15664

Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The ...

1407-1511

1.01e-57

Pssm-ID: 277134 Cd Length: 105 Bit Score: 195.32 E-value: 1.01e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCKGLGDGYEMKEGRLLYCGQNEWVHANCALWSNEVFEEIDGSLQNVHSAISRGRLIRCTECGKKGASVGCCSRNCNS 1486
Cdd:cd15664     1 CALCGVYGDDEPNDAGRLLYCGQDEWVHINCALWSAEVFEEDDGSLQNVHSAVSRGRMMKCELCGKPGATVGCCLKSCPA 80

                          90       100
                  ....*....|....*....|....*
gi 817208853 1487 TFHYPCARAIGLAFNDDKTVFCSLH 1511
Cdd:cd15664    81 NYHFMCARKAECVFQDDKKVFCPAH 105

SET_SET1

cd20072

SET domain (including post-SET domain) found in catalytic component of the Saccharomyces ...

3296-3441

4.30e-55

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: 189.56 E-value: 4.30e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3296 MRFRILKeTSKESVGVYHSHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNIG-CYMFKIDDHLVVDAT 3374
Cdd:cd20072     3 LRFNQLK-KRKKQLKFARSAIHNWGLYAMENISAKDMVIEYVGEVIRQQVADEREKRYLRQGIGsSYLFRIDDDTVVDAT 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 817208853 3375 MKGNAARFINHSCEPNCYSRVVDILGKKHILIFALRRIVQGEELTYDYKFPFEDIKIPCTCGSRRCR 3441
Cdd:cd20072    82 KKGNIARFINHCCDPNCTAKIIKVEGEKRIVIYAKRDIAAGEELTYDYKFPREEDKIPCLCGAPNCR 148

SET

smart00317

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

3307-3428

2.67e-44

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: 157.50 E-value: 2.67e-44

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853   3307 ESVGVYHSHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNI-GCYMFKIDDHLVVDATMKGNAARFINH 3385
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkAFYLFDIDSDLCIDARRKGNLARFINH 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 817208853   3386 SCEPNCYSRVVDILGKKHILIFALRRIVQGEELTYDYKFPFED 3428
Cdd:smart00317   81 SCEPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYAN 123

SET_SETD1A

cd19204

SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...

3314-3445

2.92e-44

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: 158.65 E-value: 2.92e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3314 SHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNIGC-YMFKIDDHLVVDATMKGNAARFINHSCEPNCY 3392
Cdd:cd19204    21 SRIHEWGLFAMEPIAADEMVIEYVGQNIRQVVADMREKRYVQEGIGSsYLFRVDHDTIIDATKCGNLARFINHCCTPNCY 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 817208853 3393 SRVVDILGKKHILIFALRRIVQGEELTYDYKFPFEDIKIPCTCGSRRCRKYLN 3445
Cdd:cd19204   101 AKVITIESQKKIVIYSKQPIGVNEEITYDYKFPIEDNKIPCLCGTENCRGTLN 153

SET_KMT2C

cd19208

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) ...

3297-3444

1.10e-43

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: 157.10 E-value: 1.10e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3297 RFRILKETSKESVGVYHSHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNIGCYMFKIDDHLVVDATMK 3376
Cdd:cd19208     5 QYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRIDNDHVIDATLT 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3377 GNAARFINHSCEPNCYSRVVDILGKKHILIFALRRIVQGEELTYDYKFPFEDI--KIPCTCGSRRCRKYL 3444
Cdd:cd19208    85 GGPARYINHSCAPNCVAEVVTFEKGHKIIISSSRRIQKGEELCYDYKFDFEDDqhKIPCHCGAVNCRKWM 154

SET_SETD1B

cd19205

SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...

3296-3445

7.62e-43

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: 154.83 E-value: 7.62e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3296 MRFRILKeTSKESVGVYHSHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNIGC-YMFKIDDHLVVDAT 3374
Cdd:cd19205     4 LKFNQLK-FRKKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKRYEDEGIGSsYMFRVDHDTIIDAT 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 817208853 3375 MKGNAARFINHSCEPNCYSRVVDILGKKHILIFALRRIVQGEELTYDYKFPFEDIKIPCTCGSRRCRKYLN 3445
Cdd:cd19205    83 KCGNFARFINHSCNPNCYAKVITVESQKKIVIYSKQHINVNEEITYDYKFPIEDVKIPCLCGSENCRGTLN 153

ePHD_KMT2B

cd15694

Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B); The extended plant ...

1407-1511

2.66e-42

Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of KMT2B. KMT2B is also called trithorax homolog 2 or WW domain-binding protein 7 (WBP-7). KMT2B is encoded by the gene that was first named myeloid/lymphoid or mixed-lineage leukemia 2 (MLL2), a second human homolog of Drosophila trithorax, located on chromosome 19. It belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2) and is vital for normal mammalian embryonic development. KMT2B functions as the catalytic subunit in the MLL2 complex, which contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL2 complex is highly active and specific for histone 3 lysine 4 (H3K4) methylation, which stimulates chromatin transcription in a SAM- and H3K4-dependent manner. Moreover, KMT2B plays a critical role in memory formation by mediating hippocampal H3K4 di- and trimethylation. It is also required for RNA polymerase II association and protection from DNA methylation at the MagohB CpG island promoter. KMT2B contains a CxxC (x for any residue) zinc finger domain, three PHD fingers, this ePHD finger, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain.

Pssm-ID: 277164 Cd Length: 105 Bit Score: 151.35 E-value: 2.66e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCKGLGDGYEMKEGRLLYCGQNEWVHANCALWSNEVFEEIDGSLQNVHSAISRGRLIRCTECGKKGASVGCCSRNCNS 1486
Cdd:cd15694     1 CALCLKYGDADSKDAGRLLYIGQNEWTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCEHCQKIGATVGCCLSACLS 80

                          90       100
                  ....*....|....*....|....*
gi 817208853 1487 TFHYPCARAIGLAFNDDKTVFCSLH 1511
Cdd:cd15694    81 NFHFMCARASRCCFQDDKKVFCQKH 105

SET_KMT2D

cd19209

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...

3297-3444

1.25e-41

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: 151.39 E-value: 1.25e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3297 RFRILKETSKESVGVYHSHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNIGCYMFKIDDHLVVDATMK 3376
Cdd:cd19209     6 QYRRLKTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINNEHVIDATLT 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3377 GNAARFINHSCEPNCYSRVVDILGKKHILIFALRRIVQGEELTYDYKFPFEDIK--IPCTCGSRRCRKYL 3444
Cdd:cd19209    86 GGPARYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQhkIPCHCGAWNCRKWM 155

ePHD_KMT2A

cd15693

Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant ...

1405-1511

5.29e-41

Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of KMT2A. KMT2A also termed ALL-1, or CXXC-type zinc finger protein 7, or myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), or trithorax-like protein (Htrx), or zinc finger protein HRX, is a histone methyltransferase that belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2). It regulates chromatin-mediated transcription through the catalysis of methylation of histone 3 lysine 4 (H3K4), and is frequently rearranged in acute leukemia. KMT2A functions as the catalytic subunit in the MLL1 complex, which also contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL1 complex is highly active and specific for H3K4methylation. KMT2A contains a CxxC (x for any residue) zinc finger domain, three PHD fingers, a Bromodomain domain, this extended PHD finger, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain.

Pssm-ID: 277163 Cd Length: 113 Bit Score: 147.84 E-value: 5.29e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1405 RTCCLCKGLGDGYEMKEGRLLYCGQNEWVHANCALWSNEVFEEIDGSLQNVHSAISRGRLIRCTECGKKGASVGCCSRNC 1484
Cdd:cd15693     1 RQCALCLKYGDDSANDAGRLLYIGQNEWTHVNCALWSAEVFEDDDGSLKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSC 80

                          90       100
                  ....*....|....*....|....*..
gi 817208853 1485 NSTFHYPCARAIGLAFNDDKTVFCSLH 1511
Cdd:cd15693    81 TSNYHFMCSRAKNCVFLEDKKVYCQRH 107

SET_SETD2-like

cd10531

SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...

3318-3441

7.31e-41

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: 148.17 E-value: 7.31e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3318 GRGLFCLRDIEAGEMVIEYAGEVIRASLTDKR-EKYYDSKNIGCYMFKIDDHLVVDATMKGNAARFINHSCEPNCYSRVV 3396
Cdd:cd10531    11 GWGVKAKEDIQKGEFIIEYVGEVIDKKEFKERlDEYEELGKSNFYILSLSDDVVIDATRKGNLSRFINHSCEPNCETQKW 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 817208853 3397 DILGKKHILIFALRRIVQGEELTYDYKFPFE-DIKIPCTCGSRRCR 3441
Cdd:cd10531    91 IVNGEYRIGIFALRDIPAGEELTFDYNFVNYnEAKQVCLCGAQNCR 136

SET

COG2940

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

3314-3442

2.04e-37

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

Pssm-ID: 442183 [Multi-domain] Cd Length: 134 Bit Score: 138.56 E-value: 2.04e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3314 SHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNIgcYMFKIDDHLVVDATMKGNAARFINHSCEPNCYS 3393
Cdd:COG2940    13 SPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKEPLHT--YLFELDDDGVIDGALGGNPARFINHSCDPNCEA 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 817208853 3394 RVVDilgkKHILIFALRRIVQGEELTYDYKFPFEDIKIPCTCGSrrCRK 3442
Cdd:COG2940    91 DEED----GRIFIVALRDIAAGEELTYDYGLDYDEEEYPCRCPN--CRG 133

ePHD2_KMT2C_like

cd15666

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...

1407-1511

3.82e-37

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the second ePHD finger of KMT2C, and KMT2D. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named MLL4, a fourth human homolog of Drosophila trithorax, located on chromosome 12. It enzymatically generates trimethylated histone H3 Lysine 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. KMT2D is also a part of ASCOM. Both KMT2C and KMT2D contain the catalytic domain SET, five PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobilitygroup)-binding motif, and two FY-rich regions.

Pssm-ID: 277136 Cd Length: 105 Bit Score: 136.66 E-value: 3.82e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCKGLGDGYEMKEGRLLYCGQNEWVHANCALWSNEVFEEIDGSLQNVHSAISRGRLIRCTECGKKGASVGCCSRNCNS 1486
Cdd:cd15666     1 CVLCGGEGDGDTDGPGRLLNLDVDKWVHLNCALWSYEVYETQNGALMNVEEALRRALTTTCSHCGRTGATVPCFKPRCAN 80

                          90       100
                  ....*....|....*....|....*
gi 817208853 1487 TFHYPCARAIGLAFNDDKTVFCSLH 1511
Cdd:cd15666    81 VYHLPCAIKDGCMFFKDKTMLCPSH 105

SET_ASHR3-like

cd19175

SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...

3318-3444

3.83e-36

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: 134.85 E-value: 3.83e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3318 GRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSK-NIGCYMFKIDDHLVVDATMKGNAARFINHSCEPNCYSRVV 3396
Cdd:cd19175    11 GWGLVADEDINAGEFIIEYVGEVIDDKTCEERLWDMKHKgEKNFYMCEIDKDMVIDATFKGNLSRFINHSCDPNCELQKW 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 817208853 3397 DILGKKHILIFALRRIVQGEELTYDYKFPFEDIKIPCTCGSRRCRKYL 3444
Cdd:cd19175    91 QVDGETRIGVFAIRDIKKGEELTYDYQFVQFGADQDCHCGSKNCRGKL 138

SET_EZH

cd10519

SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...

3314-3422

1.62e-35

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: 132.37 E-value: 1.62e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3314 SHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNIGcYMFKIDDHLVVDATMKGNAARFINHSCEPNCYS 3393
Cdd:cd10519     8 SDVAGWGLFLKEPIKKDEFIGEYTGELISQDEADRRGKIYDKYNSS-YLFNLNDQFVVDATRKGNKIRFANHSSNPNCYA 86

                          90       100
                  ....*....|....*....|....*....
gi 817208853 3394 RVVDILGKKHILIFALRRIVQGEELTYDY 3422
Cdd:cd10519    87 KVMMVNGDHRIGIFAKRDIEAGEELFFDY 115

SET_ASH1L

cd19174

SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...

3318-3445

1.67e-34

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: 130.49 E-value: 1.67e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3318 GRGLFCLRDIEAGEMVIEYAGEVIRASLTDKR--EKYYDSKNIgcYMFKIDDHLVVDATMKGNAARFINHSCEPNCYSRV 3395
Cdd:cd19174    11 GWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRmiEQYHNHSHH--YCLNLDSGMVIDGYRMGNEARFVNHSCDPNCEMQK 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 817208853 3396 VDILGKKHILIFALRRIVQGEELTYDYKF-PF-EDIKIPCTCGSRRCRKYLN 3445
Cdd:cd19174    89 WSVNGVYRIGLFALKDIPAGEELTYDYNFhSFnVEKQQPCKCGSPNCRGVIG 140

SET_SETD2

cd19172

SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...

3318-3444

1.67e-34

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: 130.39 E-value: 1.67e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3318 GRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNIGCYMF-KIDDHLVVDATMKGNAARFINHSCEPNCYSR-- 3394
Cdd:cd19172    13 GWGLRAAEDLPKGTFVIEYVGEVLDEKEFKRRMKEYAREGNRHYYFmALKSDEIIDATKKGNLSRFINHSCEPNCETQkw 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 817208853 3395 VVDilGKKHILIFALRRIVQGEELTYDYKFP-FEDIKIPCTCGSRRCRKYL 3444
Cdd:cd19172    93 TVN--GELRVGFFAKRDIPAGEELTFDYQFErYGKEAQKCYCGSPNCRGYI 141

PHD3_KMT2A_like

cd15508

PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...

1053-1109

3.59e-34

Pssm-ID: 276983 Cd Length: 57 Bit Score: 126.41 E-value: 3.59e-34

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 817208853 1053 YCPLCQRCYNENDFDTKMMECNECSCWVHARCEGLSDERYQVLSYLPDSIEFTCRQC 1109
Cdd:cd15508     1 YCPLCEKCYDDDDYDSKMMQCSQCDHWVHAKCEGLSDEMYEILSYLPESIEYTCSLC 57

SET

pfam00856

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...

3318-3423

3.39e-33

Pssm-ID: 459965 [Multi-domain] Cd Length: 115 Bit Score: 125.71 E-value: 3.39e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  3318 GRGLFCLRDIEAGEMVIEYAGE-VIRASLTDKREKYYDSKNI----GCYMFKIDDH--LVVDAT--MKGNAARFINHSCE 3388
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLElrlwGPYLFTLDEDseYCIDARalYYGNWARFINHSCD 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 817208853  3389 PNCYSRVVDILGKKHILIFALRRIVQGEELTYDYK 3423
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115

SET_NSD

cd19173

SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...

3318-3444

2.17e-30

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: 118.57 E-value: 2.17e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3318 GRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNI-GCYMFKIDDHLVVDATMKGNAARFINHSCEPNCYSRVV 3396
Cdd:cd19173    13 GWGLRTKRDIKKGDFVIEYVGELIDEEECRRRLKKAHENNItNFYMLTLDKDRIIDAGPKGNLSRFMNHSCQPNCETQKW 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 817208853 3397 DILGKKHILIFALRRIVQGEELTYDYKFPFE-DIKIPCTCGSRRCRKYL 3444
Cdd:cd19173    93 TVNGDTRVGLFAVRDIPAGEELTFNYNLDCLgNEKKVCRCGAPNCSGFL 141

SET_SUV39H

cd10542

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...

3318-3444

1.50e-29

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: 119.71 E-value: 1.50e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3318 GRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNIgCYMF-----KIDDHLVVDATMKGNAARFINHSCEPN-- 3390
Cdd:cd10542    99 GWGVKTLEDIKKGTFVMEYVGEIITSEEAERRGKIYDANGR-TYLFdldynDDDCEYTVDAAYYGNISHFINHSCDPNla 177

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 817208853 3391 CYSRVVDILGKK--HILIFALRRIVQGEELTYDYKF------------PFEDIKIPCTCGSRRCRKYL 3444
Cdd:cd10542   178 VYAVWINHLDPRlpRIAFFAKRDIKAGEELTFDYLMtgtggssestipKPKDVRVPCLCGSKNCRKYL 245

SET_SETDB-like

cd10538

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...

3311-3422

3.55e-29

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: 117.86 E-value: 3.55e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3311 VYHSHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNiGCYMFKIDDH---------LVVDATMKGNAAR 3381
Cdd:cd10538    93 VFRTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRGKIYDKSG-GSYLFDLDEFsdsdgdgeeLCVDATFCGNVSR 171

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 817208853 3382 FINHSCEPNC--YSRVVDILGKK--HILIFALRRIVQGEELTYDY 3422
Cdd:cd10538   172 FINHSCDPNLfpFNVVIDHDDLRypRIALFATRDILPGEELTFDY 216

SET_LegAS4-like

cd10522

SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...

3313-3422

7.74e-29

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: 113.59 E-value: 7.74e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3313 HSHIhGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNigcYMFKID-DHLVVDATMKGNAARFINHSCEPNC 3391
Cdd:cd10522    10 LSHN-GLGLFAAETIAKGEFVGEYTGEVLDRWEEDRDSVYHYDPL---YPFDLNgDILVIDAGKKGNLTRFINHSDQPNL 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 817208853 3392 YSRVVDILGKKHILIFALRRIVQGEELTYDY 3422
Cdd:cd10522    86 ELIVRTLKGEQHIGFVAIRDIKPGEELFISY 116

ePHD

cd15571

Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is ...

1407-1511

1.76e-26

Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. The extended PHD finger is characterized as Cys2HisCys5HisCys2His, which has been found in a variety of eukaryotic proteins involved in the control of gene transcription and chromatin dynamics. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. They also function as epigenome readers controlling gene expression through molecular recruitment of multi-protein complexes of chromatin regulators and transcription factors.

Pssm-ID: 277046 [Multi-domain] Cd Length: 112 Bit Score: 106.52 E-value: 1.76e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCkGLGDGYEMKEGRLLYCGQNEWVHANCALWSNEVFEEIDGSLQ--NVHSAISRGRLIRCTECGKK-GASVGCCSRN 1483
Cdd:cd15571     1 CALC-PRSGGALKGGGALKTTSDGLWVHVVCALWSPEVYFDDGTLLEveGVSKIPKRRKKLKCSICGKRgGACIQCSYPG 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 817208853 1484 CNSTFHYPCARAIGLAF-----NDDKTVFCSLH 1511
Cdd:cd15571    80 CPRSFHVSCAIRAGCLFefedgPGNFVVYCPKH 112

SET_SETD8

cd10528

SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2. ...

3311-3422

2.35e-26

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: 106.89 E-value: 2.35e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3311 VYHSHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKRE-KYYDSKNIGCYMFKIDDH---LVVDATM-KGNAARFINH 3385
Cdd:cd10528    21 VIEIDGKGRGVIATRPFEKGDFVVEYHGDLITITEAKKREaLYAKDPSTGCYMYYFQYKgktYCVDATKeSGRLGRLINH 100

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 817208853 3386 SC-EPNCYSRVVDILGKKHILIFALRRIVQGEELTYDY 3422
Cdd:cd10528   101 SKkKPNLKTKLLVIDGVPHLILVAKRDIKPGEELLYDY 138

SET_EZH2

cd19218

SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...

3314-3424

6.12e-25

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: 102.30 E-value: 6.12e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3314 SHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDsKNIGCYMFKIDDHLVVDATMKGNAARFINHSCEPNCYS 3393
Cdd:cd19218    11 SDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYD-KYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYA 89

                          90       100       110
                  ....*....|....*....|....*....|.
gi 817208853 3394 RVVDILGKKHILIFALRRIVQGEELTYDYKF 3424
Cdd:cd19218    90 KVMMVNGDHRIGIFAKRAIQTGEELFFDYRY 120

ePHD2_KMT2C

cd15697

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...

1407-1511

2.18e-24

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the second ePHD finger of KMT2C. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2C contains PHD fingers, two ePHD fingers, an ATPase alpha beta signature, a high mobility group (HMG)-1 box, a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain and two FY (phenylalanine tyrosine)-rich domains.

Pssm-ID: 277167 Cd Length: 105 Bit Score: 100.12 E-value: 2.18e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCKGLGDGYEMKEGRLLYCGQNEWVHANCALWSNEVFEEIDGSLQNVHSAISRGRLIRCTECGKKGASVGCCSRNCNS 1486
Cdd:cd15697     1 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRLRCTN 80

                          90       100
                  ....*....|....*....|....*
gi 817208853 1487 TFHYPCARAIGLAFNDDKTVFCSLH 1511
Cdd:cd15697    81 VYHFTCAIKAQCMFFKDKTMLCPMH 105

PHD3_KMT2B

cd15593

PHD finger 3 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...

1053-1109

3.29e-24

PHD finger 3 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed trithorax homolog 2 or WW domain-binding protein 7 (WBP-7), is encoded by the gene that was first named myeloid/lymphoid or mixed-lineage leukemia 2 (MLL2), a second human homolog of Drosophila trithorax, located on chromosome 19. It belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2) and is vital for normal mammalian embryonic development. KMT2B functions as the catalytic subunit in the MLL2 complex, which contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL2 complex is highly active and specific for histone 3 lysine 4 (H3K4) methylation, which stimulates chromatin transcription in a SAM- and H3K4-dependent manner. Moreover, KMT2B plays a critical role in memory formation through mediating hippocampal H3K4 di- and trimethylation. It is also required for RNA polymerase II association and protection from DNA methylation at the MagohB CpG island promoter. KMT2B contains a CxxC (x for any residue) zinc finger domain, three plant homeodomain (PHD) fingers, an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the third PHD finger.

Pssm-ID: 277068 Cd Length: 57 Bit Score: 98.00 E-value: 3.29e-24

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 817208853 1053 YCPLCQRCYNENDFDTKMMECNECSCWVHARCEGLSDERYQVLSYLPDSIEFTCRQC 1109
Cdd:cd15593     1 YCPICLKCYEDNDYESKMMQCAKCDHWVHAKCEGLSDELYEILSSLPDSVVYSCAPC 57

SET_EZH1

cd19217

SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43) ...

3314-3428

4.53e-24

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: 100.53 E-value: 4.53e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3314 SHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDsKNIGCYMFKIDDHLVVDATMKGNAARFINHSCEPNCYS 3393
Cdd:cd19217    13 SDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYD-KYMSSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYA 91

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 817208853 3394 RVVDILGKKHILIFALRRIVQGEELTYDYKFPFED 3428
Cdd:cd19217    92 KVVMVNGDHRIGIFAKRAIQQGEELFFDYRYSQAD 126

ePHD2_KMT2D

cd15698

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...

1407-1511

9.70e-24

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the second ePHD finger of KMT2D. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named myeloid/lymphoid or mixed-lineage leukemia 4 (MLL4), a fourth human homolog of Drosophila trithorax, located on chromosome 12. KMT2D enzymatically generates trimethylated histone H3 Lys 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. It is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and KMT2D. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D contains the catalytic domain SET, five PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions.

Pssm-ID: 277168 Cd Length: 107 Bit Score: 98.20 E-value: 9.70e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCKGLGDGYEMKEGRLLYCGQNEWVHANCALWSNEVFEEIDGSLQNVHSAISRGRLIRCTECGKKGASVGCCSRNCNS 1486
Cdd:cd15698     1 CCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQKTGATNSCNRLRCPN 80

                          90       100
                  ....*....|....*....|....*
gi 817208853 1487 TFHYPCARAIGLAFNDDKTVFCSLH 1511
Cdd:cd15698    81 VYHFACAIRAKCMFFKDKTMLCPMH 105

SET_NSD1

cd19210

SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...

3309-3444

1.38e-23

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: 99.23 E-value: 1.38e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3309 VGVYHSHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNI-GCYMFKIDDHLVVDATMKGNAARFINHSC 3387
Cdd:cd19210     4 VEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDItNFYMLTLDKDRIIDAGPKGNYARFMNHCC 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 817208853 3388 EPNCYSRVVDILGKKHILIFALRRIVQGEELTYDYKFP-FEDIKIPCTCGSRRCRKYL 3444
Cdd:cd19210    84 QPNCETQKWTVNGDTRVGLFALCDIKAGTELTFNYNLEcLGNGKTVCKCGAPNCSGFL 141

SET_NSD2

cd19211

SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...

3318-3444

3.32e-23

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: 98.14 E-value: 3.32e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3318 GRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNIG-CYMFKIDDHLVVDATMKGNAARFINHSCEPNCYSRVV 3396
Cdd:cd19211    13 GWGLIAKRDIKKGEFVNEYVGELIDEEECMARIKHAHENDIThFYMLTIDKDRIIDAGPKGNYSRFMNHSCQPNCETQKW 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 817208853 3397 DILGKKHILIFALRRIVQGEELTYDYKFP-FEDIKIPCTCGSRRCRKYL 3444
Cdd:cd19211    93 TVNGDTRVGLFAVCDIPAGTELTFNYNLDcLGNEKTVCRCGAPNCSGFL 141

FYRC

pfam05965

F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...

3146-3226

1.13e-22

F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It is similar to SMART:SM00542.

Pssm-ID: 461788 Cd Length: 83 Bit Score: 94.21 E-value: 1.13e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  3146 GPSLMYEIKSQDGFTHTASSMSEIWDTVFKAVQAARRAHNLPPLPHNPLT--ENLGLDNNATVYLVEQLPGVNRCTKYKP 3223
Cdd:pfam05965    1 GPLFRVTVEEDPDESFEGSSPTKCWSMVLERVQELRREAGLKLKLPESISgeDMFGLTHPAVVRLIESLPGAEKCTNYKF 80


                   ...
gi 817208853  3224 RFH 3226
Cdd:pfam05965   81 RYG 83

SET_SETMAR

cd10544

SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...

3311-3444

3.01e-22

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: 98.91 E-value: 3.01e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3311 VYHSHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYyDSKNIGCYMFKIDDHL--------VVDATMKGNAARF 3382
Cdd:cd10544    94 VFKTPKKGWGLRTLEFIPKGRFVCEYAGEVIGFEEARRRTKS-QTKGDMNYIIVLREHLssgkvletFVDPTYIGNIGRF 172

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 817208853 3383 INHSCEPNCYS---RVVDILGKkhILIFALRRIVQGEELTYDY------------KFPFEDIKI--PCTCGSRRCRKYL 3444
Cdd:cd10544   173 LNHSCEPNLFMvpvRVDSMVPK--LALFAARDIVAGEELSFDYsgefsnsvesvtLARQDESKSrkPCLCGAENCRGFL 249

PHD3_KMT2A

cd15592

PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, ...

1053-1109

1.40e-21

PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, CXXC-type zinc finger protein 7, myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), trithorax-like protein (Htrx), or zinc finger protein HRX) is a histone methyltransferase that belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2). It regulates chromatin-mediated transcription through the catalysis of methylation of histone 3 lysine 4 (H3K4), and is frequently rearranged in acute leukemia. KMT2A functions as the catalytic subunit in the MLL1 complex, which also contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL1 complex is highly active and specific for H3K4 methylation. KMT2A contains a CxxC (x for any residue) zinc finger domain, three plant homeodomain (PHD) fingers, a Bromodomain domain, an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the third PHD finger.

Pssm-ID: 277067 Cd Length: 57 Bit Score: 90.43 E-value: 1.40e-21

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 817208853 1053 YCPLCQRCYNENDFDTKMMECNECSCWVHARCEGLSDERYQVLSYLPDSIEFTCRQC 1109
Cdd:cd15592     1 FCPLCDKCYDDDDYESKMMQCGKCDRWVHSKCENLSDEMYEILSNLPESVAYTCINC 57

SET_SUV39H2

cd10532

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...

3266-3444

5.77e-21

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: 94.96 E-value: 5.77e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3266 LASRHRQQPKM---VPMTETESRRTASTNLPMamrfRILKETSKESVGVYH-SHIHGRGLFCLRDIEAGEMVIEYAGEVI 3341
Cdd:cd10532    44 FAYNEHGQLKIppgTPIYECNSRCKCGPDCPN----RVVQKGTQYSLCIFRtSNGRGWGVKTLQKIKKNSFVMEYVGEVI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3342 RASLTDKREKYYDSKNIgCYMFKID---DHLVVDATMKGNAARFINHSCEPN--CYSRVVDILGKK--HILIFALRRIVQ 3414
Cdd:cd10532   120 TSEEAERRGQFYDSKGI-TYLFDLDyesDEFTVDAARYGNVSHFVNHSCDPNlqVFNVFIDNLDTRlpRIALFSTRTIKA 198

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 817208853 3415 GEELTYDYKF---------------PFEDIKIPCTCGSRRCRKYL 3444
Cdd:cd10532   199 GEELTFDYQMkgsgdlssdsidnspAKKRVRTVCKCGAVTCRGYL 243

SET_SETD5-like

cd10529

SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...

3319-3426

3.18e-20

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: 88.87 E-value: 3.18e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3319 RGLFCLRDIEAGEMVIEYAGEVirASLTDKREKYYDSKNIGCYMF----KIDDHLVVDATMKGNAARFINHSCEPNCYSR 3394
Cdd:cd10529    17 KGLVATEDISPGEPILEYKGEV--SLRSEFKEDNGFFKRPSPFVFfydgFEGLPLCVDARKYGNEARFIRRSCRPNAELR 94

                          90       100       110
                  ....*....|....*....|....*....|...
gi 817208853 3395 -VVDILGKKHILIFALRRIVQGEELTYDYKFPF 3426
Cdd:cd10529    95 hVVVSNGELRLFIFALKDIRKGTEITIPFDYDY 127

SET_SUV39H_Clr4-like

cd20073

SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 ...

3299-3444

3.62e-20

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: 93.02 E-value: 3.62e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3299 RILKETSKESVGVYHSHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNIgCYMFKID-------DHLVV 3371
Cdd:cd20073    85 RVVQRGRKLPLEIFKTKHKGWGLRCPRFIKAGTFIGVYLGEVITQSEAEIRGKKYDNVGV-TYLFDLDlfedqvdEYYTV 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3372 DATMKGNAARFINHSCEPN--CYSRVVDILGKK--HILIFALRRIVQGEELTYDY------------------KFPFEDI 3429
Cdd:cd20073   164 DAQYCGDVTRFINHSCDPNlaIYSVLRDKSDSKiyDLAFFAIKDIPALEELTFDYsgrnnfdqlgfignrsnsKYINLKN 243

                         170
                  ....*....|....*
gi 817208853 3430 KIPCTCGSRRCRKYL 3444
Cdd:cd20073   244 KRPCYCGSANCRGWL 258

SET_NSD3

cd19212

SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...

3318-3444

1.01e-19

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: 88.06 E-value: 1.01e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3318 GRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNI-GCYMFKIDDHLVVDATMKGNAARFINHSCEPNCYSRVV 3396
Cdd:cd19212    13 GWGLRTKRSIKKGEFVNEYVGELIDEEECRLRIKRAHENSVtNFYMLTVTKDRIIDAGPKGNYSRFMNHSCNPNCETQKW 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 817208853 3397 DILGKKHILIFALRRIVQGEELTYDYKFP-FEDIKIPCTCGSRRCRKYL 3444
Cdd:cd19212    93 TVNGDVRVGLFALCDIPAGMELTFNYNLDcLGNGRTECHCGADNCSGFL 141

SET_EHMT

cd10543

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...

3318-3441

1.69e-19

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: 90.48 E-value: 1.69e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3318 GRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKyyDSknigcYMFKIDDHLV----VDATMKGNAARFINHSCEPNCYS 3393
Cdd:cd10543   102 GWGVRALQDIPKGTFVCEYIGELISDSEADSRED--DS-----YLFDLDNKDGetycIDARRYGNISRFINHLCEPNLIP 174

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 817208853 3394 RVVDI----LGKKHILIFALRRIVQGEELTYDYKFPFEDIK---IPCTCGSRRCR 3441
Cdd:cd10543   175 VRVFVehqdLRFPRIAFFASRDIKAGEELGFDYGEKFWRIKgkyFTCRCGSPKCK 229

SET_SUV39H1

cd10525

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...

3318-3444

1.96e-19

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: 90.72 E-value: 1.96e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3318 GRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNIgCYMFKID---DHLVVDATMKGNAARFINHSCEPN--CY 3392
Cdd:cd10525    98 GWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGA-TYLFDLDyveDVYTVDAAYYGNISHFVNHSCDPNlqVY 176

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 817208853 3393 SRVVDILGKK--HILIFALRRIVQGEELTYDYKF------------------------PFEDIKIPCTCGSRRCRKYL 3444
Cdd:cd10525   177 NVFIDNLDERlpRIALFATRTIRAGEELTFDYNMqvdpvdaestkmdsnfglaglpgsPKKRVRIECKCGVRSCRKYL 254

ePHD_RAI1_like

cd15668

Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 ...

1407-1511

3.03e-19

Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 (TCF-20) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the C-terminal ePHD/ADD (ATRX-DNMT3-DNMT3L) domain of RAI1 and TCF-20. RAI1, a homolog of stromelysin-1 PDGF (platelet-derived growth factor)-responsive element-binding protein (SPBP, also termed TCF-20), is a chromatin-binding protein implicated in the regulation of gene expression. TCF-20 is involved in transcriptional activation of the MMP3 (matrix metalloprotease 3) promoter. It also functions as a transcriptional co-regulator that enhances or represses the transcriptional activity of certain transcription factors/cofactors, such as specificity protein 1 (Sp1), E twenty-six 1 (Ets1), paired box protein 6 (Pax6), small nuclear RING-finger (SNURF)/RNF4, c-Jun, androgen receptor (AR) and estrogen receptor alpha (ERalpha). Both RAI1 and TCF-20 are strongly enriched in chromatin in interphase HeLa cells, and display low nuclear mobility, and have been implicated in Smith-Magenis syndrome and Potocki-Lupski syndrome.

Pssm-ID: 277138 Cd Length: 103 Bit Score: 85.44 E-value: 3.03e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCK------GLGD--G--YEMkegrllycgqneWVHANCALWSNEVFEeIDGSLQNVHSAISRGRLIRCTECGKKGAS 1476
Cdd:cd15668     1 CVFCKrgphykGLGDlfGpyYEV------------WVHEDCAVWAPGVYL-VGGKLYGLEEAVWVAKQSVCSSCQQTGAT 67

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 817208853 1477 VGCCSRNCNSTFHYPCARAIGLAFNDDK-TVFCSLH 1511
Cdd:cd15668    68 IGCLHKGCKAKYHYPCAVESGCQLDEENfSLLCPKH 103

SET_EZH-like

cd19168

SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb ...

3307-3422

6.92e-19

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: 84.93 E-value: 6.92e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3307 ESVGVYHSHIH-GRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNiGCYMFKIDDHLVVDATMKGNAARFINH 3385
Cdd:cd19168     1 KAVVLGKSQLEcGLGLFAAEDIKEGEFVIEYTGELISHDEGVRREHRRGDVS-YLYLFEEQEGIWVDAAIYGNLSRYINH 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 817208853 3386 SCEP----NCYSRVVDILGKKHILIFALRRIVQGEELTYDY 3422
Cdd:cd19168    80 ATDKvktgNCMPKIMYVNHEWRIKFTAIKDIKIGEELFFNY 120

SET

cd08161

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...

3314-3422

1.55e-18

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: 82.30 E-value: 1.55e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3314 SHIHGRGLFCLRDIEAGEMVIEyagevirasltdkrekyydsknigcymfkiddhlvvdatmkgnaARFINHSCEPNCYS 3393
Cdd:cd08161     7 IPGAGFGLFATRDIPKGEVIGL--------------------------------------------ARFINHSCEPNCEF 42

                          90       100
                  ....*....|....*....|....*....
gi 817208853 3394 RVVDILGKKHILIFALRRIVQGEELTYDY 3422
Cdd:cd08161    43 EEVYVGGKPRVFIVALRDIKAGEELTVDY 71

ePHD1_KMT2C_like

cd15665

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...

1407-1511

1.71e-18

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the first ePHD finger of KMTC2C and KMTC2D. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named MLL4, a fourth human homolog of Drosophila trithorax, located on chromosome 12. It enzymatically generates trimethylated histone H3 Lysine 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. KMT2D is also a part of ASCOM. Both KMT2C and KMT2D contain the catalytic domain SET, five plant PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobilitygroup)-binding motif, and two FY-rich regions.

Pssm-ID: 277135 Cd Length: 90 Bit Score: 82.75 E-value: 1.71e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCkglgdgyemkegrllYCGQNeWVHANCALWSNEVFEEIDGSLQNVHSAISRGRLIRCTECGKKGASVGCCSRNCNS 1486
Cdd:cd15665     1 CALC---------------NLGEV-YAHHCCAAWSEGVCQTEDGALENVDKAVAKALSQKCSFCLRYGASISCRMPSCSK 64

                          90       100
                  ....*....|....*....|....*..
gi 817208853 1487 TFHYPCARAIGlAFNDDKT--VFCSLH 1511
Cdd:cd15665    65 SFHFPCAAAAG-CFQDIKTltLFCPEH 90

SET_EHMT1

cd10535

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...

3297-3441

2.03e-18

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: 87.30 E-value: 2.03e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3297 RFRILKETSKESVGVYHSHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKyyDSknigcYMFKIDDH----LVVD 3372
Cdd:cd10535    81 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--DS-----YLFDLDNKdgevYCID 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 817208853 3373 ATMKGNAARFINHSCEPNCYSRVVDI----LGKKHILIFALRRIVQGEELTYDYKFPFEDIK---IPCTCGSRRCR 3441
Cdd:cd10535   154 ARFYGNVSRFINHHCEPNLVPVRVFMahqdLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKgklFSCRCGSPKCR 229

SET_EHMT2

cd10533

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...

3299-3441

2.43e-18

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: 87.38 E-value: 2.43e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3299 RILKETSKESVGVYHSHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKyyDSknigcYMFKIDDH----LVVDAT 3374
Cdd:cd10533    83 RVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED--DS-----YLFDLDNKdgevYCIDAR 155

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 817208853 3375 MKGNAARFINHSCEPNCYSRVVDILGKK----HILIFALRRIVQGEELTYDYKFPFEDIK---IPCTCGSRRCR 3441
Cdd:cd10533   156 YYGNISRFINHLCDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWDIKskyFTCQCGSEKCK 229

SET_SUV39H_DIM5-like

cd19473

SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...

3318-3444

2.60e-18

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: 88.14 E-value: 2.60e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3318 GRGLFCLRDIEAGEMVIEYAGEVIRASLTD-KREKYYDSKNIGCYMFKID--------------DHLVVDATMKGNAARF 3382
Cdd:cd19473   117 GWGVRSTVDIKRGQFVDCYVGEIITPEEAQrRRDAATIAQRKDVYLFALDkfsdpdsldprlrgDPYEIDGEFMSGPTRF 196

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 817208853 3383 INHSCEPNC--YSRVVDiLGKKHI---LIFALRRIVQGEELTYDY-----------KFPFEDI-KIPCTCGSRRCRKYL 3444
Cdd:cd19473   197 INHSCDPNLriFARVGD-HADKHIhdlAFFAIKDIPRGTELTFDYvdgvtgldddaGDEEKEKeMTKCLCGSPKCRGYL 274

FYRC

smart00542

FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region ...

3149-3226

1.68e-17

Pssm-ID: 197781 Cd Length: 86 Bit Score: 79.65 E-value: 1.68e-17

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853   3149 LMYEIKSQDGFTHTASSMSEIWDTVFKAVQAARRAHNLPPLPHNPL--TENLGLDNNATVYLVEQLPGVNRCTKYKPRFH 3226
Cdd:smart00542    2 FRVEIESDPGEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEGVsgEEMFGLSSPAVVKLIEALPGVHQCTNYWFRYH 81

PHD1_KMT2A_like

cd15506

PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...

926-971

6.25e-17

Pssm-ID: 276981 Cd Length: 47 Bit Score: 76.63 E-value: 6.25e-17

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 817208853  926 VCYLCGSAGKEPLIHCQCCCEPYHVFCLEPSEWSAC-AQSNWSCPRC 971
Cdd:cd15506     1 LCFLCGSAGLNELLYCSVCCEPYHTFCLEEAERPLNiNKDNWCCRRC 47

SET_SETDB

cd10541

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...

3318-3444

2.01e-16

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: 81.44 E-value: 2.01e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3318 GRGLFCLRDIEAGEMVIEYAGEVIRASLTDKrEKYYDSKNIGCYMFKIDDHL-VVDATMKGNAARFINHSCEPNCYsrVV 3396
Cdd:cd10541   103 GWGIRCLDDIAKGTFVCIYAGKILTDDFADK-EGLEMGDEYFANLDHIEESCyIIDAKLEGNLGRYLNHSCSPNLF--VQ 179

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 817208853 3397 DILGKKH------ILIFALRRIVQGEELTYDYKF---PFEDIKIPCTCGSRRCRKYL 3444
Cdd:cd10541   180 NVFVDTHdlrfpwVAFFASKRIKAGTELTWDYNYevgSVEGKELLCCCGSNECRGRL 236

SET_SETDB1

cd10517

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...

3318-3444

3.11e-16

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: 81.95 E-value: 3.11e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3318 GRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDS-------------KNIGCYMFKIDDHL-VVDATMKGNAARFI 3383
Cdd:cd10517   140 GWGIRCLDDIPKGSFVCIYAGQILTEDEANEEGLQYGDeyfaeldyievveKLKEGYESDVEEHCyIIDAKSEGNLGRYL 219

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3384 NHSCEPNCYsrVVDILGKKHIL------IFALRRIVQGEELTYDYKFPF---EDIKIPCTCGSRRCRKYL 3444
Cdd:cd10517   220 NHSCSPNLF--VQNVFVDTHDLrfpwvaFFASRYIRAGTELTWDYNYEVgsvPGKVLYCYCGSSNCRGRL 287

ePHD_PHF6_like

cd15673

Extended PHD finger found in PHD finger protein 6 (PHF6) and PHD finger protein 11 (PHF11); ...

1407-1511

1.63e-15

Extended PHD finger found in PHD finger protein 6 (PHF6) and PHD finger protein 11 (PHF11); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the two ePHD fingers of PFH6 and the single ePHD finger of PFH11. PHF6, also termed the X-linked mental retardation disorder Borjeson-Forssman-Lehmann syndrome-associated protein, is a nucleolus, ribosomal RNA promoter-associated protein that regulates cell cycle progression by suppressing ribosomal RNA synthesis. It has been implicated in cell cycle control, genomic maintenance, and tumor suppression. PHF6 shows transcriptional repression activity through directly interacting with the nucleosome remodeling and deacetylation complex component RBBP4. PHF6 contains two non-canonical ePHD fingers. PHF11, also termed BRCA1 C-terminus-associated protein, or renal carcinoma antigen NY-REN-34, is a transcriptional co-activator of the Th1 effector cytokine genes, interleukin-2 (IL2) and interferon-gamma (IFNG), co-operating with nuclear factor kappa B (NF-kappaB). It is involved in T-cell activation and viability. Polymorphisms within PHF11 are associated with total IgE, allergic asthma and eczema.

Pssm-ID: 277143 Cd Length: 116 Bit Score: 75.12 E-value: 1.63e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCKgLGDGYEmKEGRLLYCGQNEWVHANCALWSNEVFEEIDGS--------LQNVHSAISRGRLIRCTECGKKGASVG 1478
Cdd:cd15673     1 CGFCK-SGEENK-ETGGKLASGEKIAAHHNCMLFSSGLVQYVSPNendfggfdIEDVKKEIKRGRKLKCNLCKKTGATIG 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 817208853 1479 CCSRNCNSTFHYPCARAIGLAFNDDK-----TVFCSLH 1511
Cdd:cd15673    79 CDVKQCKKTYHYHCAKKDDAKIIERNsqgiyRVYCKNH 116

ePHD_PHF7_G2E3_like

cd15669

Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ...

1407-1494

1.83e-14

Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ubiquitin-protein ligase (G2E3); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of PHF7 and G2E3. PHF7, also termed testis development protein NYD-SP6, is a testis-specific PHD finger-containing protein that associates with chromatin and binds histone H3 N-terminal tails with a preference for dimethyl lysine 4 (H3K4me2). It may play an important role in stimulating transcription involved in testicular development and/or spermatogenesis. PHF7 contains a PHD finger and a non-canonical ePHD finger, both of which may be involved in activating transcriptional regulation. G2E3 is a dual function ubiquitin ligase (E3) that may play a possible role in cell cycle regulation and the cellular response to DNA damage. It is essential for prevention of apoptosis in early embryogenesis. It is also a nucleo-cytoplasmic shuttling protein with DNA damage responsive localization. G2E3 contains two distinct RING-like ubiquitin ligase domains that catalyze lysine 48-linked polyubiquitination, and a C-terminal catalytic HECT domain that plays an important role in ubiquitin ligase activity and in the dynamic subcellular localization of the protein. The RING-like ubiquitin ligase domains consist of a PHD finger and an ePHD finger.

Pssm-ID: 277139 [Multi-domain] Cd Length: 112 Bit Score: 71.90 E-value: 1.83e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCkGLGDGYEMKEGRLLYCGqNEWVHANCALWSNEVF------EEIDGSL-QNVHSAISRGRLIRCTECGKKGASVGC 1479
Cdd:cd15669     1 CVLC-GRSDDDPDKYGEKLQKD-GICAHYFCLLFSSGLPqrgednEGIYGFLpEDIRKEVRRASRLRCFYCKKKGASIGC 78

                          90
                  ....*....|....*
gi 817208853 1480 CSRNCNSTFHYPCAR 1494
Cdd:cd15669    79 AVKGCRRSFHFPCGL 93

zf-HC5HC2H

pfam13771

PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...

1434-1511

1.57e-13

Pssm-ID: 463977 [Multi-domain] Cd Length: 88 Bit Score: 68.51 E-value: 1.57e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  1434 HANCALWSNEV-FEEIDG---SLQNVHSAISRGRLIRCTECGKK-GASVGCCSRNCNSTFHYPCARAIGLAF-----NDD 1503
Cdd:pfam13771    1 HVVCALWSPELvQRGNDSmgfPIEDIEKIPKRRWKLKCYLCKKKgGACIQCSKKNCRRAFHVTCALEAGLLMqfdedNGT 80


                   ....*...
gi 817208853  1504 KTVFCSLH 1511
Cdd:pfam13771   81 FKSYCKKH 88

ePHD_TCF20

cd15699

Extended PHD finger (ePHD) found in transcription factor 20 (TCF-20); The extended plant ...

1407-1521

2.20e-13

Extended PHD finger (ePHD) found in transcription factor 20 (TCF-20); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the C-terminal ePHD/ADD (ATRX-DNMT3-DNMT3L) domain of TCF-20. TCF-20, also termed nuclear factor SPBP, or protein AR1, or stromelysin-1 PDGF (platelet-derived growth factor)-responsive element-binding protein (SPRE-binding protein), is involved in transcriptional activation of the MMP3 (matrix metalloprotease 3) promoter. It is strongly enriched on chromatin in interphase HeLa cells, and displays low nuclear mobility, and has been implicated in Smith-Magenis syndrome and Potocki-Lupski syndrome. As a chromatin-binding protein, TCF-20 plays a role in the regulation of gene expression. It also functions as a transcriptional co-regulator that enhances or represses the transcriptional activity of certain transcription factors/cofactors, such as specificity protein 1 (Sp1), E twenty-six 1 (Ets1), paired box protein 6 (Pax6), small nuclear RING-finger (SNURF)/RNF4, c-Jun, androgen receptor (AR) and estrogen receptor alpha (ERalpha). TCF-20 contains an N-terminal transactivation domain, a novel DNA-binding domain with an AT-hook motif, three nuclear localization signals (NLSs) and a C-terminal ePHD/ADD domain.

Pssm-ID: 277169 Cd Length: 103 Bit Score: 68.79 E-value: 2.20e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLC------KGLGD----GYEMkegrllycgqneWVHANCALWSNEVFEeIDGSLQNVHSAISRGRLIRCTECGKKGAS 1476
Cdd:cd15699     1 CCLCgkwanyRNLGDlfgpFYEF------------WVHEGCILWANGIYL-VCGRLYGLQEALDIAREMKCSHCQEAGAT 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 817208853 1477 VGCCSRNCNSTFHYPCaraiglAFNDDktvfCSLHLANCAERTPQ 1521
Cdd:cd15699    68 LGCYNKGCSFRYHYPC------AIDAD----CLLNEENFSVRCPK 102

ePHD_RAI1

cd15700

Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant ...

1407-1503

3.82e-13

Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the C-terminal ePHD/ADD (ATRX-DNMT3-DNMT3L) domain of RAI1. RAI1, a homolog of stromelysin-1 PDGF (platelet-derived growth factor)-responsive element-binding protein (SPBP, also termed TCF-20), is a chromatin-binding protein implicated in the regulation of gene expression. It is strongly enriched on chromatin in interphase HeLa cells, and displays low nuclear mobility, and has been implicated in Smith-Magenis syndrome, Potocki-Lupski syndrome, and non-syndromic autism. RAI1 contains a region with homology to the novel nucleosome-binding region SPBP and an ePHD/ADD domain with ability to bind nucleosomes.

Pssm-ID: 277170 Cd Length: 104 Bit Score: 67.98 E-value: 3.82e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLC------KGLGDgyemkegrllYCGQ---NEWVHANCALWSNEVFEeIDGSLQNVHSAISRGRLIRCTECGKKGASV 1477
Cdd:cd15700     1 CCLCrnpanyKDLGD----------LCGPyypEHWVHEACAVWTTGVYL-VAGKLFGLQEAVQKAADAKCSSCQGAGATV 69

                          90       100
                  ....*....|....*....|....*.
gi 817208853 1478 GCCSRNCNSTFHYPCARAIGLAFNDD 1503
Cdd:cd15700    70 GCCHKGCTQSYHYICAVEAGCLFEEE 95

SET_AtSUVH-like

cd10545

SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...

3311-3422

5.70e-13

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: 71.28 E-value: 5.70e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3311 VYHSHIHGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDsknigcYMFKIDDH---------------------- 3368
Cdd:cd10545    90 VFKTAERGWGVRSWDSIPAGSFICEYVGELLDTSEADTRSGNDD------YLFDIDNRqtnrgwdggqrldvgmsdgers 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 817208853 3369 ---------LVVDATMKGNAARFINHSCEPNCYSRVV-----DILgKKHILIFALRRIVQGEELTYDY 3422
Cdd:cd10545   164 saedeesseFTIDAGSFGNVARFINHSCSPNLFVQCVlydhnDLR-LPRVMLFAADNIPPLQELTYDY 230

SET_SETDB2

cd10523

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...

3311-3444

1.07e-12

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: 71.02 E-value: 1.07e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3311 VYHSHIHGRGLFCLRDIEAGEMVIEYAGEV-IRAS-----LTDKREKYYD-------SKNIGCYMFKIDDHL-VVDATMK 3376
Cdd:cd10523   112 VFKTEKKGWGVRCLDDIDKGTFVCIYAGRVlSRARsptepLPPKLELPSEnevevvtSWLILSKKRKLRENVcFLDASKE 191

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 817208853 3377 GNAARFINHSCEPNCYsrVVDILGKKH------ILIFALRRIVQGEELTYDYKF---PFEDIKIPCTCGSRRCRKYL 3444
Cdd:cd10523   192 GNVGRFLNHSCCPNLF--VQNVFVDTHdknfpwVAFFTNRVVKAGTELTWDYSYdagTSPEQEIPCLCGVNKCQKKI 266

ePHD1_KMT2C

cd15696

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...

1426-1511

2.11e-12

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the first ePHD finger of KMT2C. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2C contains several PHD fingers, two ePHD fingers, an ATPase alpha beta signature, a high mobility group (HMG)-1 box, a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain and two FY (phenylalanine tyrosine)-rich domains.

Pssm-ID: 277166 Cd Length: 90 Bit Score: 65.35 E-value: 2.11e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1426 YCGQNeWVHANCALWSNEVFEEIDGSLQNVHSAISRGRLIRCTECGKKGASVGCCSRNCNSTFHYPCARAIGlAFND--D 1503
Cdd:cd15696     5 YCGEC-WAHLRCAEWSLGVCQGEEQLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAG-TFQDfsR 82


                  ....*...
gi 817208853 1504 KTVFCSLH 1511
Cdd:cd15696    83 RLLLCPTH 90

SET_SpSET3-like

cd19183

SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...

3320-3426

5.84e-12

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: 66.66 E-value: 5.84e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3320 GLFCLRDIEAGEMVIEYAGEVIRAS--LTDKREKYYDSKNIGCYMFkIDDH--LVVDATMKGNAARFINHSCEPNC--YS 3393
Cdd:cd19183    15 GLFADRPIPAGDPIQELLGEIGLQSeyIADPENQYQILGAPKPHVF-FHPQspLYIDTRRSGSVARFIRRSCRPNAelVT 93

                          90       100       110
                  ....*....|....*....|....*....|...
gi 817208853 3394 RVVDILGKKHILIFALRRIVQGEELTYDYKFPF 3426
Cdd:cd19183    94 VASDSGSVLKFVLYASRDISPGEEITIGWDWDN 126

PHD1_KMT2A

cd15588

PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, ...

926-971

6.19e-12

PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, CXXC-type zinc finger protein 7, myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), trithorax-like protein (Htrx), or zinc finger protein HRX) is a histone methyltransferase that belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2). It regulates chromatin-mediated transcription through the catalysis of methylation of histone 3 lysine 4 (H3K4), and is frequently rearranged in acute leukemia. KMT2A functions as the catalytic subunit in MLL1 complex, which also contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL1 complex is highly active and specific for H3K4 methylation. KMT2A contains a CxxC (x for any residue) zinc finger domain, three plant homeodomain (PHD) fingers, a Bromodomain domain, an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the first PHD finger.

Pssm-ID: 277063 Cd Length: 47 Bit Score: 62.66 E-value: 6.19e-12

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 817208853  926 VCYLCGSAGKEPLIHCQCCCEPYHVFCLEPSEWSACAQ-SNWSCPRC 971
Cdd:cd15588     1 VCFLCASSGHVEFVYCQVCCEPFHKFCLEEAERPLEDQlENWCCRRC 47

FYRN

pfam05964

F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...

1554-1601

1.10e-11

F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It is similar to SMART:SM00541.

Pssm-ID: 461787 Cd Length: 51 Bit Score: 62.14 E-value: 1.10e-11

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 817208853  1554 GSLTIDCLGTVVPQ--FSDTPEKIIPSDYKCSRLYWSTVNPLKIVKYYIR 1601
Cdd:pfam05964    1 GSLTVLSLGEIVPDrpAFHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCE 50

SET_SMYD

cd20071

SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...

3313-3422

1.52e-11

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: 63.94 E-value: 1.52e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3313 HSHIHGRGLFCLRDIEAGEMVIEYAGEVIraSLTDKREKYYDSKNIGCYMFKIddhlvvdatmkgnaARFINHSCEPNCy 3392
Cdd:cd20071     5 SEGSKGRGLVATRDIEPGELILVEKPLVS--VPSNSFSLTDGLNEIGVGLFPL--------------ASLLNHSCDPNA- 67

                          90       100       110
                  ....*....|....*....|....*....|
gi 817208853 3393 srVVDILGKKHILIFALRRIVQGEELTYDY 3422
Cdd:cd20071    68 --VVVFDGNGTLRVRALRDIKAGEELTISY 95

PHD1_KMT2B

cd15589

PHD finger 1 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...

926-971

2.22e-11

PHD finger 1 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed trithorax homolog 2 or WW domain-binding protein 7 (WBP-7), is encoded by the gene that was first named myeloid/lymphoid or mixed-lineage leukemia 2 (MLL2), a second human homolog of Drosophila trithorax, located on chromosome 19. It belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2) and is vital for normal mammalian embryonic development. KMT2B functions as the catalytic subunit in the MLL2 complex, which contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL2 complex is highly active and specific for histone 3 lysine 4 (H3K4) methylation, which stimulates chromatin transcription in a SAM- and H3K4-dependent manner. Moreover, KMT2B plays a critical role in memory formation through mediating hippocampal H3K4 di- and trimethylation. It is also required for RNA polymerase II association and protection from DNA methylation at the MagohB CpG island promoter. KMT2B contains a CxxC (x for any residue) zinc finger domain, three plant homeodomain (PHD) fingers, an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the first PHD finger.

Pssm-ID: 277064 Cd Length: 47 Bit Score: 61.03 E-value: 2.22e-11

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 817208853  926 VCYLCGSAGKEPLIHCQCCCEPYHVFCLEPSEWSACAQ-SNWSCPRC 971
Cdd:cd15589     1 VCLLCASKGQHELLFCQVCCEPFHRFCLEESERPLPEQeENWCCRRC 47

ePHD_PHF11

cd15712

Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain ...

1407-1511

5.72e-11

Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of PHF11. PHF11, also termed BRCA1 C-terminus-associated protein, or renal carcinoma antigen NY-REN-34, is a transcriptional co-activator of the Th1 effector cytokine genes, interleukin-2 (IL2) and interferon-gamma (IFNG), co-operating with nuclear factor kappa B (NF-kappaB). It is involved in T-cell activation and viability. Polymorphisms within PHF11 are associated with total IgE, allergic asthma and eczema.

Pssm-ID: 277182 [Multi-domain] Cd Length: 115 Bit Score: 62.22 E-value: 5.72e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCKglgdgyEMKEGRLLYCG--QNEWVHANCALWSNEVFE---------EIDGSLQNVHSAISRGRLIRCTECGKKGA 1475
Cdd:cd15712     1 CAFCP------KGEEYSIMYFAqeQNIAAHQNCLLYSSGFVEseeynplnlDRRFDVESVLNEIKRGKRLKCNFCRKKGA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 817208853 1476 SVGCCSRNCNSTFHYPCARAIGLAFNDDKT-----VFCSLH 1511
Cdd:cd15712    75 TVGCEERACRRSYHYFCALCDDAAIETDEVrgiyrVFCQKH 115

SP2_N

cd22540

N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...

2452-2768

8.04e-11

Pssm-ID: 411776 [Multi-domain] Cd Length: 511 Bit Score: 67.64 E-value: 8.04e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2452 GTIIQQQPGAIQCGVISSEQLVLSSTPTLEMFTDSTGSmfvSSQPMYYGLETIVSNTVMS-SSQFMAG-AVPQVLASSYQ 2529
Cdd:cd22540    83 GNIIQLQGSQLSSSAPGGQQVFAIQNPTMIIKGSQTRS---STNQQYQISPQIQAAGQINnSGQIQIIpGTNQAIITPVQ 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2530 TTTQVFQASKLME----PIVDVQAVSAVPGVPAvpTVPTVQAVQNVPGVQPVQN--VPAVPSIQTVPGVQPV-------- 2595
Cdd:cd22540   160 VLQQPQQAHKPVPikpaPLQTSNTNSASLQVPG--NVIKLQSGGNVALTLPVNNlvGTQDGATQLQLAAAPSkpskkirk 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2596 QSLPGVQSGVQVQsvagmQAVQGVPgVQSVQSVTGAQGiRNLSGVQAvpavPPGQNVPTVQPVQGLPGVQAVQSV----- 2670
Cdd:cd22540   238 KSAQAAQPAVTVA-----EQVETVL-IETTADNIIQAG-NNLLIVQS----PGTGQPAVLQQVQVLQPKQEQQVVqipqq 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2671 --RGVTNQHAGYI------LMN-QQPAPAPEPKRVaaprVTMQPPPEQQTyasIGCDAVPPPAPCRPSVEAVRPVRVPPe 2741
Cdd:cd22540   307 alRVVQAASATLPtvpqkpLQNiQIQNSEPTPTQV----YIKTPSGEVQT---VLLQEAPAATATPSSSTSTVQQQVTA- 378

                         330       340
                  ....*....|....*....|....*..
gi 817208853 2742 aslvSSGPTTTSPKPLQHATPTIPRVA 2768
Cdd:cd22540   379 ----NNGTGTSKPNYNVRKERTLPKIA 401

PHA03247

large tegument protein UL36; Provisional

2549-2843

3.90e-10

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 66.50 E-value: 3.90e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2549 AVSAVPGVPAVPTVPTVQAVQNVPGVQPVQNVPAVPSIQTVPGVQPVQSLPgvQSGVQVQSVAGMQAVQGVPGVQSVQSV 2628
Cdd:PHA03247 2734 ALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLT--RPAVASLSESRESLPSPWDPADPPAAV 2811

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2629 TGAQGIRNLSGVQAVPAVPPGQNVPTVQPVQGLPGVQAVQSVRGVTnqhAGYILMNQQPAPAPEPKRVAAPRVTM----Q 2704
Cdd:PHA03247 2812 LAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA---PGGDVRRRPPSRSPAAKPAAPARPPVrrlaR 2888

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2705 PPPEQQTYASigcdAVPPPAPCRPSVEAVRPVRVPPEASLVSSGPT---------------TTSPKPLQHATPTIP---- 2765
Cdd:PHA03247 2889 PAVSRSTESF----ALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQppppppprpqpplapTTDPAGAGEPSGAVPqpwl 2964

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2766 ------RVAV-----------RPSPAShATPHVTAHVTSHVTPHATS---HVTATPhqlhPPWKVSEALFGAEQPVDGGA 2825
Cdd:PHA03247 2965 galvpgRVAVprfrvpqpapsREAPAS-STPPLTGHSLSRVSSWASSlalHEETDP----PPVSLKQTLWPPDDTEDSDA 3039

                         330
                  ....*....|....*...
gi 817208853 2826 RPYFDSKHVSENTSMIKP 2843
Cdd:PHA03247 3040 DSLFDSDSERSDLEALDP 3057

ePHD1_KMT2D

cd15695

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...

1424-1511

1.62e-09

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the first ePHD finger of KMT2D. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named myeloid/lymphoid or mixed-lineage leukemia 4 (MLL4), a fourth human homolog of Drosophila trithorax, located on chromosome 12. KMT2D enzymatically generates trimethylated histone H3 at Lys 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. It is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and KMT2D. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D contains the catalytic domain SET, five PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions.

Pssm-ID: 277165 Cd Length: 90 Bit Score: 57.23 E-value: 1.62e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1424 LLYCGQNeWVHANCALWSNEVFEEIDGSLQNVHSAISRGRLIRCTECGKKGASVGCCSRNCNSTFHYPCARAIGlAFNDD 1503
Cdd:cd15695     3 LCNCGEC-WVHHWCAAWSAGVKQHEGDGLIGVDKAVFSGISQKCEHCKRLGATIQCHAEGCPRFYHFPCAAASG-SFQSM 80

                          90
                  ....*....|
gi 817208853 1504 KT--VFCSLH 1511
Cdd:cd15695    81 KTllLLCPEH 90

ePHD_BRPF

cd15670

Extended PHD finger found in BRPF proteins; The extended plant homeodomain (ePHD) zinc finger ...

1430-1511

5.93e-09

Extended PHD finger found in BRPF proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the ePHD finger of the family of BRPF proteins, which includes BRPF1, BRD1/BRPF2, and BRPF3. These are scaffold proteins that form monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complexes with other regulatory subunits, such as inhibitor of growth 5 (ING5) and Esa1-associated factor 6 ortholog (EAF6). BRPF proteins have multiple domains, including a plant homeodomain (PHD) zinc finger followed by a non-canonical ePHD finger, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. This PHD finger binds to lysine 4 of histone H3 (K4H3), the bromodomain interacts with acetylated lysines on N-terminal tails of histones and other proteins, and the PWWP domain shows histone-binding and chromatin association properties.

Pssm-ID: 277140 Cd Length: 116 Bit Score: 56.57 E-value: 5.93e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1430 NEWVHANCALW------SNEVF-EEIDGsLQNVHSAisRGRLIrCTECGKK-GASVGCCSRNCNSTFHYPCARAIGL--- 1498
Cdd:cd15670    17 GRWAHVVCALWipevsfANTVFlEPIDG-IQNIPKA--RWKLT-CYICKKRmGACIQCHKKNCYTAFHVTCAQQAGLymk 92

                          90       100
                  ....*....|....*....|....
gi 817208853 1499 ---------AFNDD--KTVFCSLH 1511
Cdd:cd15670    93 iepvkdpgnGTSDSvrKEAYCDKH 116

SET_SpSet7-like

cd10540

SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...

3318-3422

7.73e-09

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: 56.11 E-value: 7.73e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3318 GRGLFCLRDIEAGEmVIEYAGeVIRasLTDKREKYYDSKNIGCYMFkiddhlVVDATMKGNAARF---INHSCEPNCysR 3394
Cdd:cd10540    11 GRGVFATRPIKKGE-VIEEAP-VIV--LPKEEYQHLCKTVLDHYVF------SWGDGCLALALGYgsmFNHSYTPNA--E 78

                          90       100
                  ....*....|....*....|....*...
gi 817208853 3395 VVDILGKKHILIFALRRIVQGEELTYDY 3422
Cdd:cd10540    79 YEIDFENQTIVFYALRDIEAGEELTINY 106

SET_SETD5

cd19181

SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...

3317-3440

1.12e-08

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: 56.55 E-value: 1.12e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3317 HGRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKnigcYMF-----KIDD-HLVVDATMKGNAARFINHSCEPN 3390
Cdd:cd19181    17 HRKILRAARDLALDTLIIEYRGKVMLRQQFEVNGHFFKRP----YPFvlfysKFNGvEMCVDARTFGNDARFIRRSCTPN 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 817208853 3391 CYSRVVDILGKKHILIFALRRIVQGEELT--YDYKFPFEDIKIPCTC--GSRRC 3440
Cdd:cd19181    93 AEVRHMIADGMIHLCIYAVAAIAKDAEVTiaFDYEYSNCNYKVDCAChkGNRNC 146

PRK10263

DNA translocase FtsK; Provisional

2521-2779

2.20e-08

DNA translocase FtsK; Provisional

Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 60.48 E-value: 2.20e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2521 PQVLASSYQTTTQVFQAsklmePIVDVQAVSAVPGVPAVPTVPTVQAvQNVPGVQ--------------PVQNVPAVPSI 2586
Cdd:PRK10263  319 PVAVAAAATTATQSWAA-----PVEPVTQTPPVASVDVPPAQPTVAW-QPVPGPQtgepviapapegypQQSQYAQPAVQ 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2587 QTVPGVQPVQSLPGVQSGVQVQSVAGMQ-AVQGVPGVQSVQSVTGAQGIRNLSGVQAVPAVPPGQNVPT-------VQPV 2658
Cdd:PRK10263  393 YNEPLQQPVQPQQPYYAPAAEQPAQQPYyAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTyqteqtyQQPA 472

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2659 QGLPGVQAVQSVRGVTNQHAGYILMNQQPAPAP-------EPKRvAAPRVTM----QPPPEqqtyasigcdAVPPPAPCR 2727
Cdd:PRK10263  473 AQEPLYQQPQPVEQQPVVEPEPVVEETKPARPPlyyfeevEEKR-AREREQLaawyQPIPE----------PVKEPEPIK 541

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 817208853 2728 PSVEAVRPVRVPPEASLVSSGPTTTSPKPLQHATPTIPRVAVrP--SPASHATP 2779
Cdd:PRK10263  542 SSLKAPSVAAVPPVEAAAAVSPLASGVKKATLATGAAATVAA-PvfSLANSGGP 594

zf-HC5HC2H_2

pfam13832

PHD-zinc-finger like domain;

1405-1511

2.49e-08

PHD-zinc-finger like domain;

Pssm-ID: 463991 [Multi-domain] Cd Length: 109 Bit Score: 54.27 E-value: 2.49e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  1405 RTCCLCKGLGdgyemkeGRLLYCGQNEWVHANCALWSNEVF-------EEIDgsLQNVHSAISRGRlirCTECGKK-GAS 1476
Cdd:pfam13832    1 VRCCLCPLRG-------GALKQTSDGRWVHVLCAIFVPEVRfgnvatmEPID--VSRIPPERWKLK---CVFCKKRsGAC 68

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 817208853  1477 VGCCSRNCNSTFHYPCARAIGLAF------NDDKTVFCSLH 1511
Cdd:pfam13832   69 IQCSKGRCTTAFHVTCAQAAGVYMepedwpNVVVIAYCQKH 109

ePHD_BRPF3

cd15703

Extended PHD finger found in bromodomain and PHD finger-containing protein 3 (BRPF3) and ...

1407-1511

7.58e-08

Extended PHD finger found in bromodomain and PHD finger-containing protein 3 (BRPF3) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of BRPF3. BRF3 is a homolog of BRPF1 and BRPF2. It is a scaffold protein that forms a novel monocytic leukemic zinc finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complex with other regulatory subunits. BRPF3 contains a plant homeodomain (PHD) finger followed by this non-canonical ePHD finger, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain.

Pssm-ID: 277173 [Multi-domain] Cd Length: 118 Bit Score: 53.52 E-value: 7.58e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCKGLGDGY-EMKEGRllycgqneWVHANCALW------SNEVFEEIDGSLQNVHSAisRGRLIrCTECGKKG--ASV 1477
Cdd:cd15703     1 CVLCPNKGGAFkQTSDGR--------WAHVVCAIWipevcfANTVFLEPVEGVNNIPPA--RWKLT-CYLCKQKGrgAAI 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 817208853 1478 GCCSRNCNSTFHYPCARAIGL---------------AFNDDKTVFCSLH 1511
Cdd:cd15703    70 QCHKVNCYTAFHVTCAQRAGLfmkiepvretglngtTFTVRKTAYCENH 118

rne

PRK10811

ribonuclease E; Reviewed

2640-2801

1.17e-07

ribonuclease E; Reviewed

Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 58.13 E-value: 1.17e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2640 VQAVPAVPPGQNVPTVQPVQGLPGVQAVQSVRGVTNQHAGYILMNQQPAPAPEPKRVAAPrVTMQPPPEQQTYASIGCDA 2719
Cdd:PRK10811  864 VQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAP-VTEQPQVITESDVAVAQEV 942

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2720 VPPPAPCRPSVEAVRPVRVPPEAS--LVSSGPTTTSPKPLQHATPTIPRVAVRPSPASHATPHVTAHVTSHVtpHATSHV 2797
Cdd:PRK10811  943 AEHAEPVVEPQDETADIEEAAETAevVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATVEHN--HATAPM 1020


                  ....
gi 817208853 2798 TATP 2801
Cdd:PRK10811 1021 TRAP 1024

ePHD_JMJD2

cd15675

Extended PHD finger found in Jumonji domain-containing protein 2 (JMJD2) family of histone ...

1407-1500

1.62e-07

Extended PHD finger found in Jumonji domain-containing protein 2 (JMJD2) family of histone demethylases; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of JMJD2 proteins. JMJD2 proteins, also termed lysine-specific demethylase 4 histone demethylases (KDM4), have been implicated in various cellular processes including DNA damage response, transcription, cell cycle regulation, cellular differentiation, senescence, and carcinogenesis. They selectively catalyze the demethylation of di- and trimethylated H3K9 and H3K36. This model contains three JMJD2 proteins, JMJD2A-C, which all contain jmjN and jmjC domains in the N-terminal region, followed by a canonical PHD finger, this non-canonical ePHD finger, and a Tudor domain. JMJD2D is not included in this family, since it lacks both PHD and Tudor domains and has a different substrate specificity. JMJD2A-C are required for efficient cancer cell growth.

Pssm-ID: 277145 [Multi-domain] Cd Length: 112 Bit Score: 52.36 E-value: 1.62e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCKglgdgyeMKEGRLLYCGQNEWVHANCALWSNEV-FEEIDGSLQNVHSAISRGRL-IRCTECGKK-------GASV 1477
Cdd:cd15675     1 CCLCC-------LRGGALKPTTDGRWAHVVCAIAIPEVrFSNVPERGPIDISKIPPARLkLKCIYCSKItksmshmGACI 73

                          90       100
                  ....*....|....*....|...
gi 817208853 1478 GCCSRNCNSTFHYPCARAIGLAF 1500
Cdd:cd15675    74 QCSTGKCTTSFHVTCAHAAGVQM 96

ePHD_ATX1_2_like

cd15662

Extended PHD finger found in Arabidopsis thaliana ATX1, -2, and similar proteins; The extended ...

1407-1498

3.15e-07

Extended PHD finger found in Arabidopsis thaliana ATX1, -2, and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of A. thaliana histone-lysine N-methyltransferase arabidopsis trithorax-like proteins ATX1, -2, and similar proteins. ATX1 and -2 are sister paralogs originating from a segmental chromosomal duplication; they are plant counterparts of the Drosophila melanogaster trithorax (TRX) and mammalian mixed-lineage leukemia (MLL1) proteins. ATX1 (also known as protein SET domain group 27, or trithorax-homolog protein 1/TRX-homolog protein 1), is a methyltransferase that trimethylates histone H3 at lysine 4 (H3K4me3). It also acts as a histone modifier and as a positive effector of gene expression. ATX1 regulates transcription from diverse classes of genes implicated in biotic and abiotic stress responses. It is involved in dehydration stress signaling in both abscisic acid (ABA)-dependent and ABA-independent pathways. ATX2 (also known as protein SET domain group 30, or trithorax-homolog protein 2/TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). ATX1 and ATX2 are multi-domain proteins that consist of an N-terminal PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical PHD finger, this non-canonical ePHD finger, and a C-terminal SET domain.

Pssm-ID: 277132 Cd Length: 115 Bit Score: 51.32 E-value: 3.15e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCKGLGdgyemkeGRLLYCGQNEWVHANCALWSNE--VFEEIDGSLQNVHSAISRGRL-IRCTECGKK-GASVGCCSR 1482
Cdd:cd15662     1 CCLCPVVG-------GALKPTTDGRWAHLACAIWIPEtcLLDVKTMEPVDGINAISKERWeLSCTICKQRyGACIQCSNN 73

                          90
                  ....*....|....*.
gi 817208853 1483 NCNSTFHYPCARAIGL 1498
Cdd:cd15662    74 SCRVAYHPLCARAAGL 89

ePHD1_PHF6

cd15710

Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...

1407-1493

3.87e-07

Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. PHF6 contains two non-canonical ePHD fingers, this model corresponds to the first ePHD finger. PHF6, also termed the X-linked mental retardation disorder Borjeson-Forssman-Lehmann syndrome-associated protein, is a nucleolus, ribosomal RNA promoter-associated protein that regulates cell cycle progression by suppressing ribosomal RNA synthesis. It has been implicated in cell cycle control, genomic maintenance, and tumor suppression. PHF6 shows transcriptional repression activity through directly interacting with the nucleosome remodeling and deacetylation complex component RBBP4. .

Pssm-ID: 277180 Cd Length: 115 Bit Score: 51.11 E-value: 3.87e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCKGLGDgyemKEGRLLYCGQNEWV--HANCALWSNEVF------EEIDG-SLQNVHSAISRGRLIRCTECGKKGASV 1477
Cdd:cd15710     1 CGFCRSNRE----KECGQLLISENQKVaaHHKCMLFSSALVsshsdsENLGGfSIEDVQKEIKRGTKLMCSLCHCPGATI 76

                          90
                  ....*....|....*.
gi 817208853 1478 GCCSRNCNSTFHYPCA 1493
Cdd:cd15710    77 GCDVKTCHRTYHYYCA 92

PHD

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...

1053-1112

4.38e-07

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 49.03 E-value: 4.38e-07

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  1053 YCPLCQRcyneNDFDTKMMECNECSCWVHARCEGLSDERYQVLSYlpdsiEFTCRQCSPD 1112
Cdd:pfam00628    1 YCAVCGK----SDDGGELVQCDGCDDWFHLACLGPPLDPAEIPSG-----EWLCPECKPK 51

PHA03247

large tegument protein UL36; Provisional

2476-2824

6.71e-07

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 55.71 E-value: 6.71e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2476 STPTLEMFTDSTGSMFVSSQPMYY--GLETIVSNTVMSSSQFMAGAVPQVLASSYQTTTQvfQASKLMEPIVdvQAVSAV 2553
Cdd:PHA03247 2513 SRLAPAILPDEPVGEPVHPRMLTWirGLEELASDDAGDPPPPLPPAAPPAAPDRSVPPPR--PAPRPSEPAV--TSRARR 2588

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2554 PGVPAVPTVPTVQAVQNVPGVQPVQNVPAVPSIQTVPGVQPVQSLPGVQSGVQVQSVA-GMQAVQGVPGVQSVQSVTGAQ 2632
Cdd:PHA03247 2589 PDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVpPPERPRDDPAPGRVSRPRRAR 2668

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2633 GIRNLSGVQAVPAVP-PGQNVPTVQPVQGL---------------PGVQAVQSVRGVTNQHAGYILMNQQPAPAPEPKRV 2696
Cdd:PHA03247 2669 RLGRAAQASSPPQRPrRRAARPTVGSLTSLadpppppptpepaphALVSATPLPPGPAAARQASPALPAAPAPPAVPAGP 2748

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2697 AAPrVTMQPPPEQQTYASigcdavpPPAPCRPSVEAVRPVR---VPPEASLVSSGPTTTSPK-PLQHATPTIPRVAVRPS 2772
Cdd:PHA03247 2749 ATP-GGPARPARPPTTAG-------PPAPAPPAAPAAGPPRrltRPAVASLSESRESLPSPWdPADPPAAVLAPAAALPP 2820

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 817208853 2773 PASHATPhvtahvtshvTPHATSHVTATPHQLHPPWKVSEALFGAEQPvdGG 2824
Cdd:PHA03247 2821 AASPAGP----------LPPPTSAQPTAPPPPPGPPPPSLPLGGSVAP--GG 2860

ePHD_BRPF1

cd15701

Extended PHD finger found in bromodomain and PHD finger-containing protein 1 (BRPF1) and ...

1407-1511

1.10e-06

Extended PHD finger found in bromodomain and PHD finger-containing protein 1 (BRPF1) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of BRPF1. BRPF1, also termed peregrin, or protein Br140, is a multi-domain protein that binds histones, mediates monocytic leukemic zinc-finger protein (MOZ) -dependent histone acetylation, and is required for Hox gene expression and segmental identity. It is a close partner of the MOZ histone acetyltransferase (HAT) complex and a novel Trithorax group (TrxG) member with a central role during development. BRPF1 is primarily a nuclear protein that has a broad tissue distribution and is abundant in testes and spermatogonia. It contains a plant homeodomain (PHD) zinc finger followed by a non-canonical ePHD finger, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. This PHD finger binds to methylated lysine 4 of histone H3 (H3K4me), the bromodomain interacts with acetylated lysines on N-terminal tails of histones and other proteins, and the PWWP domain shows histone-binding and chromatin association properties. BRPF1 may be involved in chromatin remodeling.

Pssm-ID: 277171 [Multi-domain] Cd Length: 121 Bit Score: 50.08 E-value: 1.10e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCKGLGDGYEMKEgrllycgQNEWVHANCALW------SNEVFEEIDGSLQNVHSAisRGRLIrCTECGKKG--ASVG 1478
Cdd:cd15701     1 CALCPNKGGAFKQTD-------DGRWAHVVCALWipevcfANTVFLEPIDSIEHIPPA--RWKLT-CYICKQRGsgACIQ 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 817208853 1479 CCSRNCNSTFHYPCARAIGL---------------AFNDDKTVFCSLH 1511
Cdd:cd15701    71 CHKANCYTAFHVTCAQQAGLymkmepvretgangtSFSVRKTAYCDIH 118

ePHD_BRPF2

cd15702

Extended PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and ...

1407-1511

1.19e-06

Extended PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of BRPF2. BRPF2 also termed bromodomain-containing protein 1 (BRD1), or BR140-likeprotein, is encoded by BRL (BR140 Like gene). It is responsible for the bulk of the acetylation of H3K14 and forms a novel monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complex with HBO1 and ING4. The complex is required for full transcriptional activation of the erythroid-specific regulator genes essential for terminal differentiation and survival of erythroblasts in fetal liver. BRPF2 shows widespread expression and localizes to the nucleus within spermatocytes. It contains a cysteine rich region harboring a plant homeodomain (PHD) finger followed by a non-canonical ePHD finger, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain.

Pssm-ID: 277172 Cd Length: 118 Bit Score: 50.04 E-value: 1.19e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCKGLGDGYEMKEgrllycgQNEWVHANCALW------SNEVF-EEIDGsLQNVHSAisRGRLIrCTECGKKG--ASV 1477
Cdd:cd15702     1 CVLCPNKGGAFKKTD-------DDRWGHVVCALWipevgfANTVFiEPIDG-VRNIPPA--RWKLT-CYLCKQKGvgACI 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 817208853 1478 GCCSRNCNSTFHYPCARAIGL---------------AFNDDKTVFCSLH 1511
Cdd:cd15702    70 QCHKANCYTAFHVTCAQKAGLymkmepvkevtgggtTFSVRKTAYCDAH 118

ePHD_JADE

cd15671

Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended ...

1407-1511

1.50e-06

Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-1 (PHF17), Jade-2 (PHF15), and Jade-3 (PHF16); each of these proteins is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and EAF6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, has reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. This family also contains Drosophila melanogaster PHD finger protein rhinoceros (RNO). It is a novel plant homeodomain (PHD)-containing nuclear protein that may function as a transcription factor that antagonizes Ras signaling by regulating transcription of key EGFR/Ras pathway regulators in the Drosophila eye. All Jade proteins contain a canonical PHD finger followed by this non-canonical ePHD finger, both of which are zinc-binding motifs.

Pssm-ID: 277141 Cd Length: 112 Bit Score: 49.36 E-value: 1.50e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCKGLGDGyeMKEGRllycGQNEWVHANCALWSNEV-------FEEIDgslqNV-HSAISRGRLIrCTECG-KKGASV 1477
Cdd:cd15671     1 CVLCPKKGGA--MKSTK----SGTKWVHVSCALWIPEVsigcpekMEPIT----KIsHIPMSRWALV-CVLCKeKTGACI 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 817208853 1478 GCCSRNCNSTFHYPCARAIGLAF-----NDDKTV----FCSLH 1511
Cdd:cd15671    70 QCSVKSCKTAFHVTCAFQHGLEMktileDEDDEVkfksYCPKH 112

SET_ATXR5_6-like

cd10539

SET domain found in fungal protein lysine methyltransferase SET5 and similar protein; The ...

3325-3422

1.99e-06

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

Pssm-ID: 380937 Cd Length: 138 Bit Score: 49.72 E-value: 1.99e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3325 RDIEAGEMVIEYAGEVIraslTDKREKYYDSKNIGCYMFKID--DHLVVDATMKGNAARFI----NHSCE----PNCYSR 3394
Cdd:cd10539    22 GFIKDLTIIAEYTGDVD----YIRNREFDDNDSIMTLLLAGDpsKSLVICPDKRGNIARFIsginNHTKDgkkkQNCKCV 97

                          90       100
                  ....*....|....*....|....*...
gi 817208853 3395 VVDILGKKHILIFALRRIVQGEELTYDY 3422
Cdd:cd10539    98 RYSINGEARVLLVATRDIAKGERLYYDY 125

SP2_N

cd22540

N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...

2506-2801

2.08e-06

Pssm-ID: 411776 [Multi-domain] Cd Length: 511 Bit Score: 53.39 E-value: 2.08e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2506 SNTVMSSSQfmaGAVPQV----LASSYQTTTQVFQASKLMEPIVDVQAVSAvpgvpavptvpTVQAVQNVPGVQPVQNVP 2581
Cdd:cd22540    74 NSIGFLSAK---GNIIQLqgsqLSSSAPGGQQVFAIQNPTMIIKGSQTRSS-----------TNQQYQISPQIQAAGQIN 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2582 AVPSIQTVPG-----VQPVQSLPGVQSGVQVQ--SVAGMQAVQGVPGVQSVQ---------SVTGAQGIRNLSGVQAVPA 2645
Cdd:cd22540   140 NSGQIQIIPGtnqaiITPVQVLQQPQQAHKPVpiKPAPLQTSNTNSASLQVPgnviklqsgGNVALTLPVNNLVGTQDGA 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2646 VP-----------------PGQNVPTVQPVQGLPGVQAVQSVRGVTNQHAGYILMNQQPAPAPEPkrVAAPRVTMQPPPE 2708
Cdd:cd22540   220 TQlqlaaapskpskkirkkSAQAAQPAVTVAEQVETVLIETTADNIIQAGNNLLIVQSPGTGQPA--VLQQVQVLQPKQE 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2709 QQTYASI--------GCDAVPPPAPCRPSVEavrpvrvppeaslVSSGPTTTSPKPLQHATPT--IPRVAVRPSPASHAT 2778
Cdd:cd22540   298 QQVVQIPqqalrvvqAASATLPTVPQKPLQN-------------IQIQNSEPTPTQVYIKTPSgeVQTVLLQEAPAATAT 364

                         330       340
                  ....*....|....*....|...
gi 817208853 2779 PHVTAHVTSHVTPHATSHVTATP 2801
Cdd:cd22540   365 PSSSTSTVQQQVTANNGTGTSKP 387

rne

PRK10811

ribonuclease E; Reviewed

2516-2798

2.26e-06

ribonuclease E; Reviewed

Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 53.89 E-value: 2.26e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2516 MAGAVPQvLAS-----SYqTTTQVFQASklMEPIVDVQAVSAVPGVPAVPTVPTVQAVQNVPGVQPVQNVPAVPSIQTVP 2590
Cdd:PRK10811  829 VACASPE-MASgkvwiRY-PVVRPQDVQ--VEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEP 904

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2591 GVQPVQSLPGVQSGVQVQSVAGMQAVQGVPGVQSVQSVTgaqgirnlsgVQAVPAVPPGQNVPTVQPVQglpgvqavqsv 2670
Cdd:PRK10811  905 QPEEVVVVETTHPEVIAAPVTEQPQVITESDVAVAQEVA----------EHAEPVVEPQDETADIEEAA----------- 963

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2671 rgvtnqhagyilmNQQPAPAPEPKRVAAPRVTMQPPPEQQTyasigcdAVPPPApcrPSVEAVRPVRVPPEASLVSSGPT 2750
Cdd:PRK10811  964 -------------ETAEVVVAEPEVVAQPAAPVVAEVAAEV-------ETVTAV---EPEVAPAQVPEATVEHNHATAPM 1020

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 817208853 2751 TTSPKPLQHATPTIPRVAVRPSPASHATPHVTAHVTSHvtpHATSHVT 2798
Cdd:PRK10811 1021 TRAPAPEYVPEAPRHSDWQRPTFAFEGKGAAGGHSATH---HASAPAT 1065

SET_KMT2E

cd19182

SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...

3325-3426

2.27e-06

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

Pssm-ID: 380959 Cd Length: 129 Bit Score: 49.51 E-value: 2.27e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3325 RDIEAGEMVIEYAGEVIrasLTDKREK--YYDSKNIGCYMFKIDDH---LVVDATMKGNAARFINHSCEPNCYSRVVDIL 3399
Cdd:cd19182    25 KDLPPDTLIIEYRGKFM---LREQFEAngYFFKRPYPFVLFYSKFHgleMCVDARTFGNEARFIRRSCTPNAEVRHVIED 101

                          90       100
                  ....*....|....*....|....*..
gi 817208853 3400 GKKHILIFALRRIVQGEELTYDYKFPF 3426
Cdd:cd19182   102 GTIHLYIYSIRSIPKGTEITIAFDFDY 128

SET_Suv4-20-like

cd10524

SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...

3380-3442

3.03e-06

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

Pssm-ID: 380922 [Multi-domain] Cd Length: 141 Bit Score: 49.20 E-value: 3.03e-06

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 817208853 3380 ARFINHSCEPNCysrVVDILGKKHILIFALRRIVQGEELTYDY--KFpFEDIKIPCTCgsRRCRK 3442
Cdd:cd10524    77 AAFINHDCRPNC---KFVPTGKSTACVKVLRDIEPGEEITVYYgdNY-FGENNEECEC--ETCER 135

PHD_SF

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...

1053-1109

3.03e-06

Pssm-ID: 276966 [Multi-domain] Cd Length: 48 Bit Score: 46.54 E-value: 3.03e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 817208853 1053 YCPLCQRCYNENDfdtKMMECNECSCWVHARCEGLSDERYQvlsylpDSIEFTCRQC 1109
Cdd:cd15489     1 SCIVCGKGGDLGG---ELLQCDGCGKWFHADCLGPPLSSFV------PNGKWICPVC 48

Glutenin_hmw

pfam03157

High molecular weight glutenin subunit; Members of this family include high molecular weight ...

2246-2712

5.45e-06

Pssm-ID: 367362 [Multi-domain] Cd Length: 786 Bit Score: 52.64 E-value: 5.45e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  2246 PSLCSDSGlQRSNPAASVPLTIPEGINAPSTPSPQVSPTFSSTGVQTATNESPQSMQSPKAAKprspraprpraKGIKPH 2325
Cdd:pfam03157  167 PTSPQQSG-QRQQPGQGQQLRQGQQGQQSGQGQPGYYPTSSQQPGQLQQTGQGQQGQQPERGQ-----------QGQQPG 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  2326 LLKSPAQAHPGHVRFQPMQSAtpviQLQQAQRPAGPTVILQQVASPNILSAYVETLQQQSGQQNLQYIAAIGGQHEAGFK 2405
Cdd:pfam03157  235 QGQQPGQGQQGQQPGQPQQLG----QGQQGYYPISPQQPRQWQQSGQGQQGYYPTSLQQPGQGQSGYYPTSQQQAGQLQQ 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  2406 PQfiaanQIVPGAYIQASSDNLLALQNG----GISVLPGVQIAQPQPTVLGTIiQQQPGAIQCGV--ISSEQLVLSSTPT 2479
Cdd:pfam03157  311 EQ-----QLGQEQQDQQPGQGRQGQQPGqgqqGQQPAQGQQPGQGQPGYYPTS-PQQPGQGQPGYypTSQQQPQQGQQPE 384

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  2480 LEMFTDSTGSMFVSSQPMY-----YGLETIVSNTVMSSSQFMAGAVPqvlaSSYQTTTQVFQASKLMEPIVDVQAVSAVP 2554
Cdd:pfam03157  385 QGQQGQQQGQGQQGQQPGQgqqpgQGQPGYYPTSPQQSGQGQPGYYP----TSPQQSGQGQQPGQGQQPGQEQPGQGQQP 460

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  2555 GvpavptvptvQAVQNVPGVQPVQnvpavpsiqtvpGVQPVQSLPGV------QSGVQVQSVAGMQAVQGVPGVQSVQSV 2628
Cdd:pfam03157  461 G----------QGQQGQQPGQPEQ------------GQQPGQGQPGYyptspqQSGQGQQLGQWQQQGQGQPGYYPTSPL 518

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  2629 TGAQGIRNLSgvqavPAVP--PGQNVPTVQPVQGLPGVQAVQSVRGVTNQHAGYILMNQQPApapEPKRVAAPRVTMQPP 2706
Cdd:pfam03157  519 QPGQGQPGYY-----PTSPqqPGQGQQLGQLQQPTQGQQGQQSGQGQQGQQPGQGQQGQQPG---QGQQGQQPGQGQQPG 590


                   ....*.
gi 817208853  2707 PEQQTY 2712
Cdd:pfam03157  591 QGQPGY 596

Atrophin-1

pfam03154

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...

2543-2961

5.80e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.

Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 52.46 E-value: 5.80e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  2543 PIVDVQAVSAVPgVPAVPTVPT-VQAVQNVPGVQPVQNVPAVPSIQTVPGVQPvQSLPGVQSGVQvqsvagmqavqgvpg 2621
Cdd:pfam03154  188 PPGTTQAATAGP-TPSAPSVPPqGSPATSQPPNQTQSTAAPHTLIQQTPTLHP-QRLPSPHPPLQ--------------- 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  2622 vqsvqsvtgaqgirnlsgvQAVPAVPPGQNVPTVQPVQGLPGvqavqsvrgvtnqhagyilmnqQPAPAPEPKRVAAPRV 2701
Cdd:pfam03154  251 -------------------PMTQPPPPSQVSPQPLPQPSLHG----------------------QMPPMPHSLQTGPSHM 289

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  2702 TMQPPPE--QQTYASIGCDAVPPPAPCRPSVEAVRPVRVPPEASLVSSGPTTTSPKP-----LQH--ATPTIPrVAVRPS 2772
Cdd:pfam03154  290 QHPVPPQpfPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPpaplsMPHikPPPTTP-IPQLPN 368

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  2773 PASHATP-HVTA----HVTSHVTPHA-----TSHVTATPHQLHPP----WKVSEALFG--AEQPV--DGGARPYFDSKHV 2834
Cdd:pfam03154  369 PQSHKHPpHLSGpspfQMNSNLPPPPalkplSSLSTHHPPSAHPPplqlMPQSQQLPPppAQPPVltQSQSLPPPAASHP 448

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  2835 SENTSMIKPSisskIPPLPDHCItqrnvdvnklshdvnIVHNSYSNIMPSGNAGSVN--GNGANANVSVANKISMPMSNA 2912
Cdd:pfam03154  449 PTSGLHQVPS----QSPFPQHPF---------------VPGGPPPITPPSGPPTSTSsaMPGIQPPSSASVSSSGPVPAA 509

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 817208853  2913 PTSrpmnrvlPMQAVAPKQDSLEPVEKPDivEEPLKPEAESPKEELEDS 2961
Cdd:pfam03154  510 VSC-------PLPPVQIKEEALDEAEEPE--SPPPPPRSPSPEPTVVNT 549

PHD6_KMT2C_like

cd15514

PHD finger 6 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 5 found in ...

1053-1090

6.16e-06

PHD finger 6 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 5 found in KMT2D; KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named MLL4, a fourth human homolog of Drosophila trithorax, located on chromosome 12. It enzymatically generates trimethylated histone H3 Lysine 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. KMT2D is also a part of ASCOM. Both KMT2C and KMT2D contain the catalytic domain SET, several plant homeodomain (PHD) fingers, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions. This model corresponds to the sixth PHD finger of KMT2C and the fifth PHD finger of KMT2D.

Pssm-ID: 276989 Cd Length: 51 Bit Score: 45.74 E-value: 6.16e-06

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 817208853 1053 YCPLCQRCYNENDfdtKMMECNECSCWVHARCEGLSDE 1090
Cdd:cd15514     1 KCPVCSRSYNEGE---LIIQCSQCERWLHGACDSLRTE 35

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

926-971

7.19e-06

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 45.28 E-value: 7.19e-06

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 817208853    926 VCYLCGSA-GKEPLIHCQCCCEPYHVFCLEPSEWSACAQSNWSCPRC 971
Cdd:smart00249    1 YCSVCGKPdDGGELLQCDGCDRWYHQTCLGPPLLEEEPDGKWYCPKC 47

PHD_ARID4_like

cd15615

PHD finger found in Arabidopsis thaliana AT-rich interactive domain-containing protein 4 ...

1053-1109

1.52e-05

PHD finger found in Arabidopsis thaliana AT-rich interactive domain-containing protein 4 (ARID4) and similar proteins; This family includes A. thaliana ARID4 (ARID domain-containing protein 4) and similar proteins. Their biological roles remain unclear, but they all contain an AT-rich interactive domain (ARID) and a plant homeodomain (PHD) finger at the C-terminus. ARID is a helix-turn-helix motif-based DNA-binding domain conserved in all eukaryotes. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins.

Pssm-ID: 277087 Cd Length: 57 Bit Score: 44.78 E-value: 1.52e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 817208853 1053 YCPLCQRCYNENDFDTK-MMECNECSCWVHARCE---GLSDERYqvlsYLPDSIEFTCRQC 1109
Cdd:cd15615     1 FCILCGQVYEENEGDEKeWVQCDSCSEWVHFECDgrtGLGAFKY----AKSDGLQYVCPRC 57

FYRN

smart00541

FY-rich domain, N-terminal region; is sometimes closely juxtaposed with the C-terminal region ...

1561-1598

2.81e-05

Pssm-ID: 128814 Cd Length: 44 Bit Score: 43.81 E-value: 2.81e-05

                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 817208853   1561 LGTVVPQFSDTPEKIIPSDYKCSRLYWSTVNPLKIVKY 1598
Cdd:smart00541    1 LLPIQGKLFHSESAIFPVGYKSTRKYWSVKDPNRRCLY 38

PHD

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...

926-974

2.95e-05

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 44.02 E-value: 2.95e-05

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 817208853   926 VCYLCGSAGK-EPLIHCQCCCEPYHVFCLEPSEWSACAQSN-WSCPRCTVC 974
Cdd:pfam00628    1 YCAVCGKSDDgGELVQCDGCDDWFHLACLGPPLDPAEIPSGeWLCPECKPK 51

ePHD2_PHF6

cd15711

Extended PHD finger 2 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...

1434-1493

3.56e-05

Extended PHD finger 2 found in PHD finger protein 6 (PHF6); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. PHF6 contains two non-canonical ePHD fingers, this model corresponds to the second ePHD finger. PHF6, also termed the X-linked mental retardation disorder Borjeson-Forssman-Lehmann syndrome-associated protein, is a nucleolus, ribosomal RNA promoter-associated protein that regulates cell cycle progression by suppressing ribosomal RNA synthesis. It has been implicated in cell cycle control, genomic maintenance, and tumor suppression. PHF6 shows transcriptional repression activity through directly interacting with the nucleosome remodeling and deacetylation complex component RBBP4.

Pssm-ID: 277181 Cd Length: 118 Bit Score: 45.85 E-value: 3.56e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 817208853 1434 HANCALWSNEVFEEIDGS--------LQNVHSAISRGRLIRCTECGKKGASVGCCSRNCNSTFHYPCA 1493
Cdd:cd15711    28 HYKCMLFSSGTVQLTTTSraefgdfdIKTVIQEIKRGKRMKCTLCSQLGATIGCEIKACVKTYHYHCG 95

PRK07003

DNA polymerase III subunit gamma/tau;

2552-2831

3.74e-05

DNA polymerase III subunit gamma/tau;

Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 49.85 E-value: 3.74e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2552 AVPGVPAVPTVPTVQAVQNVPGVQPVQNvPAVPSIQTVPGVQPVQSLPGVQSGVQVQSVAGMQAVQGvpgvqsvqsvTGA 2631
Cdd:PRK07003  386 RAAAAVGASAVPAVTAVTGAAGAALAPK-AAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPA----------KAN 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2632 QGIRNLSGVQAVPAVPPGQNVPTVQPVQGLPGVQAVQS---VRGVTNQHAGYILMNQQPAPAPEPKRVAAPRvtmQPPPE 2708
Cdd:PRK07003  455 ARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPaprAAAPSAATPAAVPDARAPAAASREDAPAAAA---PPAPE 531

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2709 QqtyasigcdAVPPPAPCRPSVEA---------VRP--VRVPPEASLVSSGPTTTSPKPLQHATPTIPRVAVR-PSP-AS 2775
Cdd:PRK07003  532 A---------RPPTPAAAAPAARAggaaaaldvLRNagMRVSSDRGARAAAAAKPAAAPAAAPKPAAPRVAVQvPTPrAR 602

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 817208853 2776 HATPHVTAHVTSHVTPHATShvtatpHQLHPPWK----------VSEALFGaeqPVDGGARPYFDS 2831
Cdd:PRK07003  603 AATGDAPPNGAARAEQAAES------RGAPPPWEdippddyvplSADEGFG---GPDDGFVPVFDS 659

PAT1

pfam09770

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...

2497-2729

3.84e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.

Pssm-ID: 401645 [Multi-domain] Cd Length: 846 Bit Score: 49.65 E-value: 3.84e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  2497 MYYGLETIVSNTVMSSSQFMAGAVPQVLASSYQTTTQVFQAS------KLMEPIVDVQAVSAVPGVP-----AVPTVPTV 2565
Cdd:pfam09770  100 VRFNRQQPAARAAQSSAQPPASSLPQYQYASQQSQQPSKPVRtgyekyKEPEPIPDLQVDASLWGVApkkaaAPAPAPQP 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  2566 QAVQNVPG-----VQPVQNVPAVPSIQTVPGVQPVQSLPgvqsgvqVQSVAGMQAVQGVPGVQSVQSVTGAQgirnlsgV 2640
Cdd:pfam09770  180 AAQPASLPapsrkMMSLEEVEAAMRAQAKKPAQQPAPAP-------AQPPAAPPAQQAQQQQQFPPQIQQQQ-------Q 245

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  2641 QAVPAVPPGQNVPTVQPVQGLPGVQAVQSVRGVTNQHAGYILMNQQPAPAPE--------PKRVAAPRVTM--------Q 2704
Cdd:pfam09770  246 PQQQPQQPQQHPGQGHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVqptqilqnPNRLSAARVGYpqnpqpgvQ 325

                          250       260
                   ....*....|....*....|....*
gi 817208853  2705 PPPEQQTYASIGCDAVPPPAPCRPS 2729
Cdd:pfam09770  326 PAPAHQAHRQQGSFGRQAPIITHPQ 350

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

1053-1109

3.89e-05

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 43.35 E-value: 3.89e-05

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 817208853   1053 YCPLCQRCYNENDfdtkMMECNECSCWVHARCEGLSDEryqvlSYLPDSiEFTCRQC 1109
Cdd:smart00249    1 YCSVCGKPDDGGE----LLQCDGCDRWYHQTCLGPPLL-----EEEPDG-KWYCPKC 47

ePHD_JADE1

cd15704

Extended PHD finger found in protein Jade-1 and similar proteins; The extended plant ...

1407-1498

5.09e-05

Extended PHD finger found in protein Jade-1 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-1. Jade-1, also termed PHD finger protein 17 (PHF17), is a novel binding partner of von Hippel-Lindau (VHL) tumor suppressor Pvhl, a key regulator of cellular oxygen sensing pathway. It is highly expressed in renal proximal tubules. Jade-1 functions as an essential regulator of multiple cell signaling pathways. It may be involved in the Serine/threonine kinase AKT/AKT1 pathway during renal cancer pathogenesis and normally prevents renal epithelial cell proliferation and transformation. It also acts as a pro-apoptotic and growth suppressive ubiquitin ligase to inhibit canonical Wnt downstream effector beta-catenin for proteasomal degradation and ASA transcription factor associated with histone acetyltransferase activity and with increased abundance of cyclin-dependent kinase inhibitor p21. Moreover, Jade-1 is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and Eaf6 to form a HBO1 complex, and plays a role in epithelial cell regeneration. It has also been identified as a novel component of the nephrocystin protein (NPHP) complex and interacts with the ciliary protein nephrocystin-4 (NPHP4). Jade-1 contains a canonical plant homeodomain (PHD) finger followed by this non-canonical ePHD finger, both of which are zinc-binding motifs.

Pssm-ID: 277174 Cd Length: 118 Bit Score: 45.45 E-value: 5.09e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCKGLGDGyeMKEGRllycGQNEWVHANCALWSNEVF----EEIDGSLQNVHSAISRGRLIrCTECGKK-GASVGCCS 1481
Cdd:cd15704     4 CLLCPKKGGA--MKPTR----SGTKWVHVSCALWIPEVSigspEKMEPITKVSHIPSSRWALV-CSLCNEKvGASIQCSV 76

                          90
                  ....*....|....*..
gi 817208853 1482 RNCNSTFHYPCARAIGL 1498
Cdd:cd15704    77 KNCRTAFHVTCAFDRGL 93

PHA03247

large tegument protein UL36; Provisional

2638-2985

5.20e-05

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.55 E-value: 5.20e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2638 SGVQAVPAVPPGQNVPTVQPVQGLPGVQAVQSVRGVTnqhAGyilmnqQPAPAPEPKRVAAPRVTMQPPPeqqtYASIGC 2717
Cdd:PHA03247 2727 AARQASPALPAAPAPPAVPAGPATPGGPARPARPPTT---AG------PPAPAPPAAPAAGPPRRLTRPA----VASLSE 2793

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2718 DAVPPPAPCRPSVEAVrPVRVPPEASLVSSGPTTTSPKPLQhATPTIPRVAVRPSPASHATPHVTA---HVTSHVTPHAT 2794
Cdd:PHA03247 2794 SRESLPSPWDPADPPA-AVLAPAAALPPAASPAGPLPPPTS-AQPTAPPPPPGPPPPSLPLGGSVApggDVRRRPPSRSP 2871

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2795 SHVTATPHqlHPPWK------VSEALFGAEQPVDGGARPYFDSKHVSENTSMIKPSISSKIPPLPDHCITQrnvdvNKLS 2868
Cdd:PHA03247 2872 AAKPAAPA--RPPVRrlarpaVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQ-----PPLA 2944

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2869 HDVNIVHNSysniMPSGNAGSV-NGNGANANVSVA-NKISMPMSNAPT---SRPMNRVLPMQAVAPKQDSLEPVEKPDIV 2943
Cdd:PHA03247 2945 PTTDPAGAG----EPSGAVPQPwLGALVPGRVAVPrFRVPQPAPSREApasSTPPLTGHSLSRVSSWASSLALHEETDPP 3020

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 817208853 2944 EEPLKPEAESPkEELEDSKKRIVEIADPvKRVEVEA-DEVPAE 2985
Cdd:PHA03247 3021 PVSLKQTLWPP-DDTEDSDADSLFDSDS-ERSDLEAlDPLPPE 3061

ePHD_JADE3

cd15706

Extended PHD finger found in protein Jade-3 and similar proteins; The extended plant ...

1407-1498

6.05e-05

Extended PHD finger found in protein Jade-3 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-3. Jade-3, also termed PHD finger protein 16 (PHF16), is a plant homeodomain (PHD) zinc finger protein that is close related to Jade-1, which functions as an essential regulator of multiple cell signaling pathways. Like Jade-1, Jade-3 is required for ING4 and ING5 to associate with histone acetyl transferase (HAT) HBO1 and Eaf6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. Jade-3 contains a canonical PHD domain followed by this non-canonical ePHD domain, both of which are zinc-binding motifs.

Pssm-ID: 277176 Cd Length: 111 Bit Score: 44.71 E-value: 6.05e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCKGLGDGyeMKEGRllycGQNEWVHANCALWSNEVF----EEIDGSLQNVHSAISRGRLIrCTECG-KKGASVGCCS 1481
Cdd:cd15706     1 CLLCPKTGGA--MKATR----TGTKWAHVSCALWIPEVSiacpERMEPITKVSHIPPSRWALV-CSLCKlKTGACIQCSV 73

                          90
                  ....*....|....*..
gi 817208853 1482 RNCNSTFHYPCARAIGL 1498
Cdd:cd15706    74 KSCITAFHVTCAFEHSL 90

SP1-4_arthropods_N

cd22553

N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ...

2396-2693

8.52e-05

N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. One SP is clade SP1-4, which is expressed ubiquitously throughout development. SP1-4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. This model represents the N-terminal domain of SP1-4 from arthropods.

Pssm-ID: 411778 [Multi-domain] Cd Length: 384 Bit Score: 48.10 E-value: 8.52e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2396 IGGQHEAGFKPQFIAANQIVPGAYIQASSDNLLALQNGG------ISVLPGVQIAqpqpTVLG---TIIQQQPGAIQCGV 2466
Cdd:cd22553    22 IGGQQKQAQSDSSETHDPLILSPPLSQPQQIITAQSSGSaaggvaYSVSPAVQTV----TVDGheaIFIPANSGLLQTNN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2467 ISSEQLvlSSTPTLEMFTDstgsmfvssqpmyyGLETIVSNTVMSSSQfmAGAVPQVLASSYQTTTQVFQASKLMEPIVD 2546
Cdd:cd22553    98 QQAIQL--APGGTQAILAN--------------QQTLIRPNTVQGQAN--ASNVLQNIAQIASGGNAVQLPLNNMTQTIP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2547 VQA-VSAVPGVPAVPT--VPtVQAVQNVP---GVQPVQnVPAVPSIQTVPGVQPVQsLPGVQSGVQVQSVAGMQAVQGVP 2620
Cdd:cd22553   160 VQVpVSTANGQTVYQTiqVP-IQAIQSGNaggGNQALQ-AQVIPQLAQAAQLQPQQ-LAQVSSQGYIQQIPANASQQQPQ 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2621 GVQSVQSVTGAQGIRNLSGVQAVPAVPP------------GQNVPTVQPVQGLPGVQAVQSVRGVTNQHAGYILMNQQPA 2688
Cdd:cd22553   237 MVQQGPNQSGQIIGQVASASSIQAAAIPltvytgalagqnGSNQQQVGQIVTSPIQGMTQGLTAPASSSIPTVVQQQAIQ 316


                  ....*
gi 817208853 2689 PAPEP 2693
Cdd:cd22553   317 GNPLP 321

PRK07764

DNA polymerase III subunits gamma and tau; Validated

2547-2784

1.01e-04

DNA polymerase III subunits gamma and tau; Validated

Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 48.44 E-value: 1.01e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2547 VQAVSAVPGVPAVPTVPTVQAVQNVPGVQPVQNVPAVPSIQTVPGVQPVQSLPGVQSGVQVQSVAGMQAVQGVPGVQSVQ 2626
Cdd:PRK07764  584 VEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDAS 663

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2627 SVTGAQGIRNLSGVQAVPAVPPgqnvPTVQPVQGLPGVQAVQSVRGVtnqhagyilmnQQPAPAPEPKRVAAPRVTMQPP 2706
Cdd:PRK07764  664 DGGDGWPAKAGGAAPAAPPPAP----APAAPAAPAGAAPAQPAPAPA-----------ATPPAGQADDPAAQPPQAAQGA 728

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2707 PEQQTYASigcDAVP-PPAPCRPSVEAVRPVRVPPEASLVSSGPTTTSPKPLQHATPTIPRVAVRPSPA--SHATPHVTA 2783
Cdd:PRK07764  729 SAPSPAAD---DPVPlPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDdeDRRDAEEVA 805


                  .
gi 817208853 2784 H 2784
Cdd:PRK07764  806 M 806

ePHD_JMJD2C

cd15715

Extended PHD finger found in Jumonji domain-containing protein 2C (JMJD2C); The extended plant ...

1407-1503

1.19e-04

Extended PHD finger found in Jumonji domain-containing protein 2C (JMJD2C); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of JMJD2C. JMJD2C, also termed lysine-specific demethylase 4C (KDM4C), or gene amplified in squamous cell carcinoma 1 protein (GASC-1 protein), or JmjC domain-containing histone demethylation protein 3C (JHDM3C), is an epigenetic factor that catalyzes the demethylation of di- and trimethylated H3K9 and H3K36, and may be involved in the development and/or progression of various types of cancer including esophageal squamous cell carcinoma (ESC) and breast cancer. It selectively interacts with hypoxia-inducible factor 1alpha (HIF1alpha) and plays a role in breast cancer progression. Moreover, JMJD2C may play an important role in the treatment of obesity and its complications by modulating the regulation of adipogenesis by nuclear receptor peroxisome proliferator-activated receptor gamma (PPARgamma). JMJD2C contains jmjN and jmjC domains in the N-terminal region, followed by a canonical plant homeodomain (PHD) finger, this non-canonical ePHD finger, and a Tudor domain.

Pssm-ID: 277185 Cd Length: 110 Bit Score: 44.18 E-value: 1.19e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCKglgdgyeMKEGRLLYCGQNEWVHANCALWSNEV-FEEIDGSLQNVHSAISRGRL-IRCTECGKK-----GASVGC 1479
Cdd:cd15715     1 CCLCN-------LRGGALKQTSDDKWAHVMCAVALPEVrFINVVERTPIDISRIPLQRLkLKCIFCRNRikrvsGACIQC 73

                          90       100
                  ....*....|....*....|....
gi 817208853 1480 CSRNCNSTFHYPCARAIGLAFNDD 1503
Cdd:cd15715    74 SYGRCPASFHVTCAHAAGVLMEPD 97

ePHD_JMJD2B

cd15714

Extended PHD finger found in Jumonji domain-containing protein 2B (JMJD2B); The extended plant ...

1407-1503

1.22e-04

Extended PHD finger found in Jumonji domain-containing protein 2B (JMJD2B); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of JMJD2B. JMJD2B, also termed lysine-specific demethylase 4B (KDM4B), or JmjC domain-containing histone demethylation protein 3B (JHDM3B), specifically antagonizes the trimethyl group from H3K9 in pericentric heterochromatin and reduces H3K36 methylation in mammalian cells. It plays an essential role in the growth regulation of cancer cells by modulating the G1-S transition and promotes cell-cycle progression through the regulation of cyclin-dependent kinase 6 (CDK6). It interacts with heat shock protein 90 (Hsp90) and its stability can be regulated by Hsp90. JMJD2B also functions as a direct transcriptional target of p53, which induces its expression through promoter binding. Moreover, JMJD2B expression can be controlled by hypoxia-inducible factor 1alpha (HIF1alpha) in colorectal cancer and estrogen receptor alpha (ERalpha) in breast cancer. It is also involved in bladder, lung, and gastric cancer. JMJD2B contains jmjN and jmjC domains in the N-terminal region, followed by a canonical PHD finger, this non-canonical ePHD finger, and a Tudor domain.

Pssm-ID: 277184 Cd Length: 110 Bit Score: 44.16 E-value: 1.22e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCKglgdgyeMKEGRLLYCGQNEWVHANCALWSNEV--FEEIDGSLQNVHSAISRGRLIRCTECGKK-----GASVGC 1479
Cdd:cd15714     1 CCLCN-------LRGGALQMTTDERWVHVICAIAVPEArfLNVIERHPVDVSAIPEQRWKLKCVYCRKRmkkvsGACIQC 73

                          90       100
                  ....*....|....*....|....
gi 817208853 1480 CSRNCNSTFHYPCARAIGLAFNDD 1503
Cdd:cd15714    74 SYDHCSTSFHVTCAHAAGVVMEPD 97

PRK12323

DNA polymerase III subunit gamma/tau;

2555-2775

1.49e-04

DNA polymerase III subunit gamma/tau;

Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 47.56 E-value: 1.49e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2555 GVPAVPTVPTVQAVQNVPGVQPVQNVPAVPSIQTVPGVQPVQSLPGVQSgvQVQSVAGMQavqgvPGVQSVQSVTGAQGI 2634
Cdd:PRK12323  370 GGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARA--VAAAPARRS-----PAPEALAAARQASAR 442

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2635 RNlSGVQAVPAVPPGQNVPTVQPvqglpgvqAVQSVRGVTNQHAgyilmnqQPAPAPEPKRVAAPRVTMQPPPEQ--QTY 2712
Cdd:PRK12323  443 GP-GGAPAPAPAPAAAPAAAARP--------AAAGPRPVAAAAA-------AAPARAAPAAAPAPADDDPPPWEElpPEF 506

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 817208853 2713 ASIGCDAVPPPAPCRPSVEAVRPVRVPPEASLVSSGPTTTSPKPLQHATPTIPRVAVRPSPAS 2775
Cdd:PRK12323  507 ASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRAS 569

SET_SETD7

cd10530

SET domain found in SET domain-containing protein 7 (SETD7) and similar proteins; SETD7 (EC 2. ...

3318-3422

1.82e-04

SET domain found in SET domain-containing protein 7 (SETD7) and similar proteins; SETD7 (EC 2.1.1.43; also termed histone H3-K4 methyltransferase SETD7, H3-K4-HMTase SETD7, lysine N-methyltransferase 7 (KMT7) or SET7/9) is a histone-lysine N-methyltransferase that specifically monomethylates 'Lys-4' of histone H3. It plays a central role in the transcriptional activation of genes such as collagenase or insulin. Set7/9 also methylates non-histone proteins, including estrogen receptor alpha (ERa), suggesting it has a role in diverse biological processes. ERa methylation by Set7/9 stabilizes ERa and activates its transcriptional activities, which are involved in the carcinogenesis of breast cancer. In a high-throughput screen, treatment of human breast cancer cells (MCF7 cells) with cyproheptadine, a Set7/9 inhibitor, decreased the expression and transcriptional activity of ERa, thereby inhibiting estrogen-dependent cell growth.

Pssm-ID: 380928 Cd Length: 130 Bit Score: 43.83 E-value: 1.82e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 3318 GRGLFCLRDIEAGEMVIEYAGEVIRASLTDKREKYYDSKNIgcymfKIDDHLVVD------------ATMkGNAArfiNH 3385
Cdd:cd10530    20 GEGLFAKVAVGPNTVMSFYNGVRITHQEVDSRDWSLNGNTI-----SLDEETVIDvpepynsvskycASL-GHKA---NH 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 817208853 3386 SCEPNC-YSRVVD-ILGkkHI-LIFALRRIVQGEELTYDY 3422
Cdd:cd10530    91 SFTPNCiYDPFVHpRFG--PIkCIRTLRAVEAGEELTVAY 128

PHD1_KDM5B

cd15603

PHD finger 1 found in lysine-specific demethylase 5B (KDM5B); KDM5B (also termed Cancer/testis ...

926-971

2.76e-04

PHD finger 1 found in lysine-specific demethylase 5B (KDM5B); KDM5B (also termed Cancer/testis antigen 31 (CT31), Histone demethylase JARID1B, Jumonji/ARID domain-containing protein 1B (JARID1B), PLU-1, or retinoblastoma-binding protein 2 homolog 1 (RBP2-H1 or RBBP2H1A)) is a member of the JARID subfamily within the JmjC proteins. It has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of pregnant females and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. KDM5B acts as a histone demethylase that catalyzes the removal of trimethylation of lysine 4 on histone H3 (H3K4me3), induced by polychlorinated biphenyls (PCBs). It also mediates demethylation of H3K4me2 and H3K4me1. Moreover, KDM5B functions as a negative regulator of hematopoietic stem cell (HSC) self-renewal and progenitor cell activity. KDM5B has also been shown to interact with the DNA binding transcription factors BF-1 and PAX9, as well as TIEG1/KLF10 (transforming growth factor-beta inducible early gene-1/Kruppel-like transcription factor 10), and possibly function as a transcriptional corepressor. KDM5B contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger.

Pssm-ID: 277076 Cd Length: 46 Bit Score: 41.09 E-value: 2.76e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 817208853  926 VCYLCGSAGKEP-LIHCQCCCEPYHVFCLEPSeWSACAQSNWSCPRC 971
Cdd:cd15603     1 VCLVCGSGNDEDrLLLCDGCDDSYHTFCLIPP-LHDVPKGDWRCPKC 46

PHD1_Lid_like

cd15605

PHD finger 1 found in Drosophila melanogaster protein little imaginal discs (Lid) and similar ...

926-971

2.86e-04

PHD finger 1 found in Drosophila melanogaster protein little imaginal discs (Lid) and similar proteins; Drosophila melanogaster Lid, also termed Retinoblastoma-binding protein 2 homolog, is identified genetically as a trithorax group (trxG) protein that is a Drosophila homolog of the human protein JARID1A/kdm5A, a member of the JARID subfamily within the JmjC proteins. Lid functions as a JmjC-dependent trimethyl histone H3K4 (H3K4me3) demethylase, which is required for dMyc-induced cell growth. It positively regulates Hox gene expression in S2 cells. Lid contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger of Lid.

Pssm-ID: 277078 Cd Length: 46 Bit Score: 40.90 E-value: 2.86e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 817208853  926 VCYLCGSA-GKEPLIHCQCCCEPYHVFCLEPSeWSACAQSNWSCPRC 971
Cdd:cd15605     1 VCHTCGRGdGEESMLLCDGCDDSYHTFCLLPP-LSEVPKGDWRCPKC 46

RFX1_trans_act

pfam04589

RFX1 transcription activation region; The RFX family is a family of winged-helix DNA binding ...

2546-2631

3.65e-04

RFX1 transcription activation region; The RFX family is a family of winged-helix DNA binding proteins. RFX1 is a regulatory factor essential for expression of MHC class II genes. This region is to found N terminal to the RFX DNA binding region (pfam02257) in some mammalian RFX proteins, and is thought to activate transcription when associated with DNA. Deletion analysis has identified the region 233-351 in human RFX1 as being required for maximal activation.

Pssm-ID: 461362 [Multi-domain] Cd Length: 163 Bit Score: 43.76 E-value: 3.65e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853  2546 DVQAVSAVPGVPAVPTVPTvQAVQNVPGVQPVQNVPAVPSIQ--------TVPGVQPVQSLPGVQSGVQVQsvagmqaVQ 2617
Cdd:pfam04589    2 DSGSDSAPPAAVLQQLAPT-QVVQPVPASQQRSVVQATPSAPkgghvqqlSVPRLQQVHVTQEVQQLQQVP-------VQ 73

                           90
                   ....*....|....
gi 817208853  2618 GVPGVQsVQSVTGA 2631
Cdd:pfam04589   74 HVYPNQ-VQYVEGG 86

PHD_PHF2_like

cd15554

PHD finger found in PHF2, PHF8 and KDM7; This family includes PHF2, PHF8, KDM7, and similar ...

1053-1109

3.81e-04

PHD finger found in PHF2, PHF8 and KDM7; This family includes PHF2, PHF8, KDM7, and similar proteins. PHF2, also termed GRC5, or PHD finger protein 2, is a histone lysine demethylase ubiquitously expressed in various tissues. PHF8, also termed PHD finger protein 8, or KDM7B, is a monomethylated histone H4 lysine 20(H4K20me1) demethylase that transcriptionally regulates many cell cycle genes. It also preferentially acts on H3K9me2 and H3K9me1. PHF8 is modulated by CDC20-containing anaphase-promoting complex (APC (cdc20)) and plays an important role in the G2/M transition. It acts as a critical molecular sensor for mediating retinoic acid (RA) treatment response in RAR alpha-fusion-induced leukemia. Moreover, PHF8 is essential for cytoskeleton dynamics and is associated with X-linked mental retardation. KDM7, also termed JmjC domain-containing histone demethylation protein 1D (JHDM1D), or KIAA1718, is a dual histone demethylase that catalyzes demethylation of monomethylated and dimethylated H3K9 (H3K9me2/me1) and H3K27 (H3K27me2/me1), which functions as an eraser of silencing marks on chromatin during brain development. It also plays a tumor-suppressive role by regulating angiogenesis. All family members contain a plant homeodomain (PHD) finger and a JmjC domain.

Pssm-ID: 277029 Cd Length: 47 Bit Score: 40.44 E-value: 3.81e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 817208853 1053 YCpLCQRCYNENDFdtkMMECNECSCWVHARCEGLsdERYQVlsylPDSIEFTCRQC 1109
Cdd:cd15554     1 YC-ICRQPYDVTRF---MIECDVCKDWFHGSCVGV--EEHQA----NDIERYHCPNC 47

PRK12323

DNA polymerase III subunit gamma/tau;

2599-2791

4.67e-04

DNA polymerase III subunit gamma/tau;

Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 46.02 E-value: 4.67e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2599 PGVQSG-VQVQSVAGMQAVQGVPGVQSVQSVTGAQgirnlSGVQAVPAVPPGQNVPTVQPVQG----LPGVQAVQSVRGV 2673
Cdd:PRK12323  365 PGQSGGgAGPATAAAAPVAQPAPAAAAPAAAAPAP-----AAPPAAPAAAPAAAAAARAVAAAparrSPAPEALAAARQA 439

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2674 TNQHAGYIL----------MNQQPAPAPEPKRVAAPRVTMQPPPEQQTYASIGCDAVPPPAPCRPSVEAVRPVRVPPEAS 2743
Cdd:PRK12323  440 SARGPGGAPapapapaaapAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPA 519

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 817208853 2744 LVSSGPTttsPKPlQHATPTIPRVAVRPSPASHATPHVTAHVTSHVTP 2791
Cdd:PRK12323  520 GWVAESI---PDP-ATADPDDAFETLAPAPAAAPAPRAAAATEPVVAP 563

PRK12323

DNA polymerase III subunit gamma/tau;

2686-2827

6.07e-04

DNA polymerase III subunit gamma/tau;

Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 45.64 E-value: 6.07e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2686 QPAPAPEPKRVAAPRVTMQPPPEQQTYASIGCDAVPPPAPCR--PSVEAVRPVRVPPEASLVSSGPTTTSPKPlqhatpt 2763
Cdd:PRK12323  384 QPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARrsPAPEALAAARQASARGPGGAPAPAPAPAA------- 456

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 817208853 2764 IPRVAVRPSPASHATPHVTAHVTShvTPHATSHVTATPHQLHPPWKVSEALFGAEQPVDGGARP 2827
Cdd:PRK12323  457 APAAAARPAAAGPRPVAAAAAAAP--ARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAP 518

PHD_PHF20

cd15634

PHD finger found in PHD finger protein 20 (PHF20); PHF20, also termed Glioma-expressed antigen ...

1063-1109

6.26e-04

PHD finger found in PHD finger protein 20 (PHF20); PHF20, also termed Glioma-expressed antigen 2, or hepatocellular carcinoma-associated antigen 58, or novel zinc finger protein, or transcription factor TZP (referring to Tudor and zinc finger domain containing protein), is a regulator of NF-kappaB activation by disrupting recruitment of PP2A to p65. It also functions as a transcription factor that binds Akt and plays a role in Akt cell survival/growth signaling. Moreover, it transcriptionally regulates p53. The phosphorylation of PHF20 on Ser291 mediated by protein kinase B (PKB) is essential in tumorigenesis via the regulation of p53 mediated signaling. PHF20 contains an N-terminal malignant brain tumor (MBT) domain, two Tudor domains, a plant homeodomain (PHD) finger and the putative DNA-binding domains, AT hook and Cys2His2-type zinc finger.

Pssm-ID: 277104 Cd Length: 44 Bit Score: 39.93 E-value: 6.26e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 817208853 1063 ENDFdtkMMECNECSCWVHARCEGLSDERyqvlsyLPDSieFTCRQC 1109
Cdd:cd15634     9 ENDF---MIQCEECLCWQHGVCMGLLEDN------VPEK--YTCYIC 44

COG5141

PHD zinc finger-containing protein [General function prediction only];

1430-1498

6.86e-04

PHD zinc finger-containing protein [General function prediction only];

Pssm-ID: 227470 [Multi-domain] Cd Length: 669 Bit Score: 45.36 E-value: 6.86e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 817208853 1430 NEWVHANCALWSNEVF-------EEIDGsLQNVHSaiSRGRLIrCTECGKK-GASVGCCSRNCNSTFHYPCARAIGL 1498
Cdd:COG5141   266 GRWGHVICAMFNPELSfghllskDPIDN-IASVSS--SRWKLG-CLICKEFgGTCIQCSYFNCTRAYHVTCARRAGY 338

ePHD_JMJD2A

cd15713

Extended PHD finger (ePHD) found in Jumonji domain-containing protein 2A (JMJD2A); The ...

1407-1511

6.87e-04

Extended PHD finger (ePHD) found in Jumonji domain-containing protein 2A (JMJD2A); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of JMJD2A. JMJD2A, also termed lysine-specific demethylase 4A (KDM4A), or JmjC domain-containing histone demethylation protein 3A (JHDM3A), catalyzes the demethylation of di- and trimethylated H3K9 and H3K36. It is involved in carcinogenesis and functions as a transcription regulator that may either stimulate or repress gene transcription. It associates with nuclear receptor co-repressor complex or histone deacetylases. Moreover, JMJD2A forms complexes with both the androgen and estrogen receptor (ER) and plays an essential role in growth of both ER-positive and -negative breast tumors. It is also involved in prostate, colon, and lung cancer progression. JMJD2A contains jmjN and jmjC domains in the N-terminal region, followed by a canonical PHD finger, this non-canonical ePHD finger, and a Tudor domain.

Pssm-ID: 277183 Cd Length: 110 Bit Score: 41.88 E-value: 6.87e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCkglgdgyEMKEGRLLYCGQNEWVHANCALWSNEV-FEEIDGSLQNVHSAISRGRL-IRCTECGKK-----GASVGC 1479
Cdd:cd15713     1 CCLC-------SLRGGALQRANDDKWVHVMCAVAVLEArFVNIAERSPVDVSKIPLQRFkLKCIFCKKRrkrtaGCCVQC 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 817208853 1480 CSRNCNSTFHYPCARAIGLAFNDDKTVF-----CSLH 1511
Cdd:cd15713    74 SHGRCPTSFHASCAQAAGVMMQPDDWPFvvfitCFRH 110

PRK07003

DNA polymerase III subunit gamma/tau;

2581-2779

8.05e-04

DNA polymerase III subunit gamma/tau;

Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 45.23 E-value: 8.05e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2581 PAVPSIQTVPGVQPVQSLPGV-QSGVQVQSVAGMQAVQGVPGVqsvqSVTGAQGIRNLSGVQAVPAVPPGqnvptvqPVQ 2659
Cdd:PRK07003  360 PAVTGGGAPGGGVPARVAGAVpAPGARAAAAVGASAVPAVTAV----TGAAGAALAPKAAAAAAATRAEA-------PPA 428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2660 GLPGVQAVQSVRGVTNQHAGYilmnQQPAPAPEPKRVAAPRVTMQPPPEQQTYASIGCDAvPPPAPCRPSVEAVRPVRVP 2739
Cdd:PRK07003  429 APAPPATADRGDDAADGDAPV----PAKANARASADSRCDERDAQPPADSGSASAPASDA-PPDAAFEPAPRAAAPSAAT 503

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 817208853 2740 PEASLVSSGPTttspkplqhATPTIPRVAVRPSPASHATP 2779
Cdd:PRK07003  504 PAAVPDARAPA---------AASREDAPAAAAPPAPEARP 534

PHD_SF

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...

970-1020

8.55e-04

Pssm-ID: 276966 [Multi-domain] Cd Length: 48 Bit Score: 39.61 E-value: 8.55e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 817208853  970 RCTVCQTCHLRAGPKLSCIRCRQSFHHSCLsksGVSARLYSPDRPYVCQSC 1020
Cdd:cd15489     1 SCIVCGKGGDLGGELLQCDGCGKWFHADCL---GPPLSSFVPNGKWICPVC 48

PHD1_CHD_II

cd15531

PHD finger 1 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...

927-971

9.86e-04

PHD finger 1 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD proteins includes chromodomain-helicase-DNA-binding protein CHD3, CHD4, and CHD5, which are nuclear and ubiquitously expressed chromatin remodelling ATPases generally associated with histone deacetylases (HDACs). They are involved in DNA Double Strand Break (DSB) signaling, DSB repair and/or p53-dependent pathways such as apoptosis and senescence, as well as in the maintenance of genomic stability, and/or cancer prevention. They function as subunits of the Nucleosome Remodelling and Deacetylase (NuRD) complex, which is generally associated with gene repression, heterochromatin formation, and overall chromatin compaction. In contrast to the class I CHD enzymes (CHD1 and CHD2), class II CHD proteins lack identifiable DNA-binding domains, but possess a C-terminal coiled-coil region. Moreover, in addition to the tandem chromodomains and a helicase domain, they all harbor tandem plant homeodomain (PHD) zinc fingers involved in the recognition of methylated histone tails. This model corresponds to the first PHD finger.

Pssm-ID: 277006 [Multi-domain] Cd Length: 43 Bit Score: 39.51 E-value: 9.86e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 817208853  927 CYLCGSAGKepLIHCQCCCEPYHVFCLEPsEWSACAQSNWSCPRC 971
Cdd:cd15531     2 CEVCQQGGE--IILCDTCPRAYHLVCLDP-ELEKAPEGKWSCPHC 43

PHD_TCF19_like

cd15517

PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and ...

1056-1109

1.09e-03

PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and KDM5B, and other similar proteins; TCF-19 was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. KDM5A was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interaction with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK, and BMAL1. KDM5B has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. Both KDM5A and KDM5B function as trimethylated histone H3 lysine 4 (H3K4me3) demethylases. This family also includes Caenorhabditis elegans Lysine-specific demethylase 7 homolog (ceKDM7A). ceKDM7A (also termed JmjC domain-containing protein 1.2, PHD finger protein 8 homolog, or PHF8 homolog) is a plant homeodomain (PHD)- and JmjC domain-containing protein that functions as a histone demethylase specific for H3K9me2 and H3K27me2. The binding of the PHD finger to H3K4me3 guides H3K9me2- and H3K27me2-specific demethylation by its catalytic JmjC domain in a trans-histone regulation mechanism. In addition, this family includes plant protein OBERON 1 and OBERON 2, Alfin1-like (AL) proteins, histone acetyltransferases (HATs) HAC, and AT-rich interactive domain-containing protein 4 (ARID4).

Pssm-ID: 276992 [Multi-domain] Cd Length: 49 Bit Score: 39.45 E-value: 1.09e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 817208853 1056 LCQRCYNENDFDT-KMMECNECSCWVHARCEGLSDERYqvlsYLPDsiEFTCRQC 1109
Cdd:cd15517     1 VCGICNLETAAVDeLWVQCDGCDKWFHQFCLGLSNERY----ADED--KFKCPNC 49

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

970-1020

1.16e-03

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 39.12 E-value: 1.16e-03

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 817208853    970 RCTVCQTCHLrAGPKLSCIRCRQSFHHSCLsksGVSARLYSPDRPYVCQSC 1020
Cdd:smart00249    1 YCSVCGKPDD-GGELLQCDGCDRWYHQTCL---GPPLLEEEPDGKWYCPKC 47

PRK07003

DNA polymerase III subunit gamma/tau;

2644-2827

1.23e-03

DNA polymerase III subunit gamma/tau;

Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 44.84 E-value: 1.23e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2644 PAV----PPGQNVPTVQPvQGLPGVQAVQSVRGVTNQHAGYILMNQQPAPAPEPKRVAAPRVTMQPPPEQQTYASIGCDA 2719
Cdd:PRK07003  360 PAVtgggAPGGGVPARVA-GAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADR 438

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2720 VPPPAPCRPSVEAVRPVRVPPEASLVSSGPTTTSPKPLQHATPTIPRVAVRPSPASHATPhVTAHVTSHVTPHATSHVTA 2799
Cdd:PRK07003  439 GDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAA-PSAATPAAVPDARAPAAAS 517

                         170       180
                  ....*....|....*....|....*...
gi 817208853 2800 TPHQLHPPwkvSEALFGAEQPVDGGARP 2827
Cdd:PRK07003  518 REDAPAAA---APPAPEARPPTPAAAAP 542

PHD1_KDM5A

cd15602

PHD finger 1 found in Lysine-specific demethylase 5A (KDM5A); KDM5A (also termed Histone ...

926-971

1.29e-03

PHD finger 1 found in Lysine-specific demethylase 5A (KDM5A); KDM5A (also termed Histone demethylase JARID1A, Jumonji/ARID domain-containing protein 1A, or Retinoblastoma-binding protein 2 (RBBP-2 or RBP2)) was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK and BMAL1. KDM5A functions as a trimethylated histone H3 lysine 4 (H3K4me3) demethylase that belongs to the JARID subfamily within the JmjC proteins. It also displays DNA-binding activities that can recognize the specific DNA sequence CCGCCC. KDM5A contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger.

Pssm-ID: 277075 Cd Length: 49 Bit Score: 39.16 E-value: 1.29e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 817208853  926 VCYLCGSAGKE-PLIHCQCCCEPYHVFCLEPSeWSACAQSNWSCPRC 971
Cdd:cd15602     1 VCLFCGRGNNEdKLLLCDGCDDSYHTFCLIPP-LPDVPKGDWRCPKC 46

PHD_SF

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...

926-971

1.33e-03

Pssm-ID: 276966 [Multi-domain] Cd Length: 48 Bit Score: 39.22 E-value: 1.33e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 817208853  926 VCYLCGSAGK--EPLIHCQCCCEPYHVFCLEPSEWSACAQSNWSCPRC 971
Cdd:cd15489     1 SCIVCGKGGDlgGELLQCDGCGKWFHADCLGPPLSSFVPNGKWICPVC 48

PRK14951

DNA polymerase III subunits gamma and tau; Provisional

2642-2791

1.37e-03

DNA polymerase III subunits gamma and tau; Provisional

Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 44.32 E-value: 1.37e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2642 AVPAVPPGQNVPTVQPVQGLPGVQAvqsvrgvtnqhagyilmnqQPAPAPEPKRVAAPRVTMQPPPEQQTYAsigcdavP 2721
Cdd:PRK14951  369 AAEAAAPAEKKTPARPEAAAPAAAP-------------------VAQAAAAPAPAAAPAAAASAPAAPPAAA-------P 422

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 817208853 2722 PPAPCRPSVEAVRPvrvPPEASLVSSGPTTTSPKPLQHATPTIP-RVAVRPSPASHATPHVTAHVTSHVTP 2791
Cdd:PRK14951  423 PAPVAAPAAAAPAA---APAAAPAAVALAPAPPAQAAPETVAIPvRVAPEPAVASAAPAPAAAPAAARLTP 490

PRK07764

DNA polymerase III subunits gamma and tau; Validated

2615-2807

1.38e-03

DNA polymerase III subunits gamma and tau; Validated

Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.59 E-value: 1.38e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2615 AVQGVPGVQSVQSVTGAQGIRNLSGVQAVPAVPPGQNVPTVQPVQGLPGVQAVQSVRGVTnqhagyilmnQQPAPAPEPK 2694
Cdd:PRK07764  586 AVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAP----------GVAAPEHHPK 655

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2695 RVAAPRVTMQPPPEqqtyASIGCDAVPPPAPCRPSVEAVRPVRVPPEASLVSSGPTTTSPKPLQHATPTIPRVAVRPSPA 2774
Cdd:PRK07764  656 HVAVPDASDGGDGW----PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAP 731

                         170       180       190
                  ....*....|....*....|....*....|...
gi 817208853 2775 SHATPHVtahVTSHVTPHATSHVTATPHQLHPP 2807
Cdd:PRK07764  732 SPAADDP---VPLPPEPDDPPDPAGAPAQPPPP 761

PHA02030

hypothetical protein

2500-2592

1.53e-03

hypothetical protein

Pssm-ID: 222843 [Multi-domain] Cd Length: 336 Bit Score: 43.81 E-value: 1.53e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2500 GLETIVSNTVMSSSQFMAGAVPQVLASSYQTTTQvfqasklmePIVDVQAVSAvPGVPAVPTVPTVQAVQNVPGVQPVQ- 2578
Cdd:PHA02030  249 GGEDLIIKPKSKAAGSNLPAVPNVAADAGSAAAP---------AVPAAAAAVA-QAAPSVPQVPNVAVLPDVPQVAPVAa 318

                          90
                  ....*....|....*...
gi 817208853 2579 ----NVPAVPSIQTVPGV 2592
Cdd:PHA02030  319 paapEVPAVPVVPAAPQV 336

ePHD_RNO

cd15707

Extended PHD finger found in Drosophila melanogaster PHD finger protein rhinoceros (RNO) and ...

1407-1498

1.61e-03

Extended PHD finger found in Drosophila melanogaster PHD finger protein rhinoceros (RNO) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Drosophila melanogaster RNO. RNO is a novel plant homeodomain (PHD)-containing nuclear protein that may function as a transcription factor that antagonizes Ras signaling by regulating the transcription of key EGFR/Ras pathway regulators in the Drosophila eye. RNO contains a canonical PHD domain followed by this non-canonical ePHD domain, both of which are zinc-binding motifs.

Pssm-ID: 277177 [Multi-domain] Cd Length: 113 Bit Score: 40.66 E-value: 1.61e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCKGLGDGyeMKEGRllycGQNEWVHANCALWSNEV----FEEIDGSLQNVHSAISRGRLIrCTECGKK-GASVGCCS 1481
Cdd:cd15707     1 CILCPNKGGA--MKSTR----SGTKWAHVSCALWIPEVsigcVEKMEPITKISSIPASRWALI-CVLCRERtGACIQCSV 73

                          90
                  ....*....|....*..
gi 817208853 1482 RNCNSTFHYPCARAIGL 1498
Cdd:cd15707    74 KTCKTAYHVTCGFQHGL 90

PHD1_KMT2C_like

cd15509

PHD finger 1 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...

927-971

1.66e-03

PHD finger 1 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3) or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named MLL4, a fourth human homolog of Drosophila trithorax, located on chromosome 12. It enzymatically generates trimethylated histone H3 Lysine 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. KMT2D is also a part of ASCOM. Both KMT2C and KMT2D contain the catalytic domain SET, several plant homeodomain (PHD) fingers, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions. This model corresponds to the first PHD finger.

Pssm-ID: 276984 Cd Length: 48 Bit Score: 38.83 E-value: 1.66e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 817208853  927 CYLCGSAGK-EPLIHCQCCCEPYHVFCLEPS-EWSACAQSNWSCPRC 971
Cdd:cd15509     2 CAVCDSPGDlSDLLFCTSCGQHYHGSCLDPAvRPTPLVRAGWQCPEC 48

PRK12323

DNA polymerase III subunit gamma/tau;

2537-2756

2.15e-03

DNA polymerase III subunit gamma/tau;

Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 43.71 E-value: 2.15e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2537 ASKLMEPIVDVQAVSAVPGVPAVPTVPTVQAVQNVPGVQPVQNVPAVPSiqtvPGVQPVQSLPGVQSGVQVQSVAGMQAV 2616
Cdd:PRK12323  379 AAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRS----PAPEALAAARQASARGPGGAPAPAPAP 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2617 QGVPGVQSVQSVTGAQGIRNLSGVQAVPAVPPGQNVPT---VQPVQGLPGVQAVQsvrGVTNQHAGYILMNQQPAPAPEP 2693
Cdd:PRK12323  455 AAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPAdddPPPWEELPPEFASP---APAQPDAAPAGWVAESIPDPAT 531

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 817208853 2694 KRVAAPRVTMQPPPeqqtyasigcdaVPPPAPCRPSVEAVRPVRVPPEASLVSSGPTTTSPKP 2756
Cdd:PRK12323  532 ADPDDAFETLAPAP------------AAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGDWP 582

PHD1_KDM5C_5D

cd15604

PHD finger 1 found in Lysine-specific demethylase 5C (KDM5C) and 5D (KDM5D); The family ...

926-971

2.72e-03

PHD finger 1 found in Lysine-specific demethylase 5C (KDM5C) and 5D (KDM5D); The family includes KDM5C and KDM5D, both of which belong to the JARID subfamily within the JmjC proteins. KDM5C (also termed Histone demethylase JARID1C, Jumonji/ARID domain-containing protein 1C, SmcX, or Xe169) is a H3K4 trimethyl-histone demethylase that catalyzes demethylation of H3K4me3 and H3K4me2 to H3K4me1. It plays a role in neuronal survival and dendrite development. KDM5C defects are associated with X-linked mental retardation (XLMR). KDM5D (also termed Histocompatibility Y antigen (H-Y), Histone demethylase JARID1D, Jumonji/ARID domain-containing protein 1D, or SmcY) is a male-specific antigen that shows a demethylase activity specific for di- and tri-methylated histone H3K4 (H3K4me3 andH3K4me2), and has a male-specific function as a histone H3K4 demethylase by recruiting a meiosis-regulatory protein, MSH5, to condensed DNA. KDM5D directly interacts with a polycomb-like protein Ring6a/MBLR, and plays a role in regulation of transcriptional initiation through H3K4 demethylation. Both KDM5C and KDM5D contain the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as two plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger.

Pssm-ID: 277077 Cd Length: 46 Bit Score: 38.28 E-value: 2.72e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 817208853  926 VCYLCGSAGK-EPLIHCQCCCEPYHVFCLEPSeWSACAQSNWSCPRC 971
Cdd:cd15604     1 VCRMCSRGDEdDKLLLCDGCDDNYHTFCLLPP-LPEPPKGIWRCPKC 46

SET_SMYD4

cd10536

SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...

3382-3422

2.84e-03

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

Pssm-ID: 380934 [Multi-domain] Cd Length: 218 Bit Score: 41.90 E-value: 2.84e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 817208853 3382 FINHSCEPNCysrVVDILGKKhILIFALRRIVQGEELTYDY 3422
Cdd:cd10536   153 LLNHSCDPNT---IRSFYGNT-IVVRATRPIKKGEEITICY 189

PRK07764

DNA polymerase III subunits gamma and tau; Validated

2685-2806

3.20e-03

DNA polymerase III subunits gamma and tau; Validated

Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.44 E-value: 3.20e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2685 QQPAPAPEPKRVAAPRVTMQPPPEQQTYAsigcdAVPPPAPCRPSVEAVRPVRVPPEASLVSSGPTTTSPKPLQHATPTi 2764
Cdd:PRK07764  402 AAAAPAAAPAPAAAAPAAAAAPAPAAAPQ-----PAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPE- 475

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 817208853 2765 PRVAVRPSPASHATPHVTAHVTSHVTPHATSHVTATPHQLHP 2806
Cdd:PRK07764  476 PTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRERWP 517

SP4_N

cd22536

N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...

2349-2669

3.89e-03

N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. Human SP4 is a risk gene of multiple psychiatric disorders including schizophrenia, bipolar disorder, and major depression. SP4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP4.

Pssm-ID: 411773 [Multi-domain] Cd Length: 623 Bit Score: 42.98 E-value: 3.89e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2349 VIQLQQAQRPAGPtviLQQVASPNIlsayvETLQQQSGQQNLQYIAAIGGQHEagfKPQFIAA--NQIVPGAYIQASSDN 2426
Cdd:cd22536   129 VIQVQNMQNPSGS---VQYQVIPQI-----QTVEGQQIQISPANATALQDLQG---QIQLIPAgnNQAILTTPNRTASGN 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2427 LLA--LQNGGISVL--PGVQIaqpqPTVLGTIiqqqPGAiQCGVISSEQL----VLSSTPTLEMFTDSTGSMFVSsQPMY 2498
Cdd:cd22536   198 IIAqnLANQTVPVQirPGVSI----PLQLQTI----PGA-QAQVVTTLPIniggVTLALPVINNVAAGGGSGQLV-QPSD 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2499 YGLET---IVSNTVMSSSqfmAGAVPQVLASSYQTTTQVFQASklmePIVDVQAVSAVPGVPAVPTVPTVQAVQNVPgvQ 2575
Cdd:cd22536   268 GGVSNgnqLVSTPITTAS---VSTMPESPSSSTTCTTTASTSL----TSSDTLVSSAETGQYASTAASSERTEEEPQ--T 338

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2576 PVQNVPAVPSIQTVP-GVQPVQSLPGVQSGVQVQSVAGMQAVQGVPGVQSVQSVTGAQGIRNLSGVQavPAVPPGQNVPT 2654
Cdd:cd22536   339 SAAESEAQSSSQLQSnGLQNVQDQSNSLQQVQIVGQPILQQIQIQQPQQQIIQAIQPQSFQLQSGQT--IQTIQQQPLQN 416

                         330
                  ....*....|....*
gi 817208853 2655 VQPvqglpgvQAVQS 2669
Cdd:cd22536   417 VQL-------QAVQS 424

ePHD_Snt2p_like

cd15667

Extended PHD finger found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) ...

1407-1494

3.91e-03

Extended PHD finger found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Snt2p. Sntp2 is a yeast protein that may function in multiple stress pathways. It coordinates the transcriptional response to hydrogen peroxide-mediated oxidative stress through interaction with Ecm5 and the Rpd3 deacetylase. Snt2p contains a bromo adjacent homology (BAH) domain, two canonical PHD fingers, a non-canonical ePHD finger, and a SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domain.

Pssm-ID: 277137 Cd Length: 141 Bit Score: 40.44 E-value: 3.91e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLC---KGLGDGYEMKEGRL----LYC-GQNEWVHANCALWSNEVFEEIDGSLQ---NVHSAISRGRLIRCTECGKKGA 1475
Cdd:cd15667     1 CSLCnakESNYELAKKQSPRTrpdaLKCtSNGTWCHVLCALFNEDIKFGNSKSLQpilNTESVLLKGSRQKCEICKVSGG 80

                          90
                  ....*....|....*....
gi 817208853 1476 SVGCCSRnCNSTFHYPCAR 1494
Cdd:cd15667    81 GLVKCEV-CDDRFHVSCAQ 98

SET_SMYD3

cd19203

SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 ...

3384-3422

5.04e-03

SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 (SMYD3) and similar proteins; 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. It is overexpressed in colorectal, breast, prostate, and hepatocellular tumors, and has been implicated as an oncogene in human malignancies. Methylation of MEKK2 by SMYD3 is important for regulation of the MEK/ERK pathway, suggesting the possibility of selectively targeting SMYD3 in RAS-driven cancers.

Pssm-ID: 380980 [Multi-domain] Cd Length: 210 Bit Score: 41.20 E-value: 5.04e-03

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 817208853 3384 NHSCEPNCysrvVDILGKKHILIFALRRIVQGEELTYDY 3422
Cdd:cd19203   147 NHSCDPNC----VIVFNGPHLLLRAIREIEVGEELTISY 181

PHD6_KMT2C

cd15600

PHD finger 6 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...

1054-1090

5.52e-03

PHD finger 6 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2C contains several plant homeodomain (PHD) fingers, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, an ATPase alpha beta signature, a high mobility group (HMG)-1 box, a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain and two FY (phenylalanine tyrosine)-rich domains. This model corresponds to the sixth PHD finger.

Pssm-ID: 277073 Cd Length: 51 Bit Score: 37.60 E-value: 5.52e-03

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 817208853 1054 CPLCQRCYNENDFdtkMMECNECSCWVHARCEGLSDE 1090
Cdd:cd15600     2 CPICYRNYREEEL---ILQCRQCDRWMHASCQNLNTE 35

ePHD_PHF14

cd15674

Extended PHD finger found in PHD finger protein 14 (PHF14) and similar proteins; The extended ...

1407-1511

5.74e-03

Extended PHD finger found in PHD finger protein 14 (PHF14) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of PHF14. PHF14 is a novel nuclear transcription factor that controls the proliferation of mesenchymal cells by directly repressing platelet-derived growth factor receptor-alpha (PDGFRalpha) expression. It also acts as an epigenetic regulator and plays an important role in the development of multiple organs in mammals. PHF14 contains three canonical plant homeodomain (PHD) fingers and this non-canonical ePHD finger. It can interact with histones through its PHD fingers.

Pssm-ID: 277144 Cd Length: 114 Bit Score: 39.29 E-value: 5.74e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 1407 CCLCKGLGDGY-EMKEGRllycgqneWVHANCALWSNEV-FEEIDG----SLQNVHSAISRGRliRCTEC-----GKKGA 1475
Cdd:cd15674     1 CELCPNRGGIFkETDTGR--------WVHLVCALYTPGVaFGDVDKlspvTLTEMNYSKWGAR--ECSLCedprfARTGV 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 817208853 1476 SVGCCSRNCNSTFHYPCARAIGL---AFNDDKTV-----FCSLH 1511
Cdd:cd15674    71 CISCDAGMCKSYFHVTCAQREGLlseATDEEDIAdpfyaYCKQH 114

PRK14950

DNA polymerase III subunits gamma and tau; Provisional

2687-2779

5.80e-03

DNA polymerase III subunits gamma and tau; Provisional

Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 42.49 E-value: 5.80e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817208853 2687 PAPAPEPKRVAAPrvtmQPPPEQQTYASIGcdavPPPAPCRPSVEAVRPVRVPPEASLVSSGPTTTSPKPLQHATPTIPR 2766
Cdd:PRK14950  362 PVPAPQPAKPTAA----APSPVRPTPAPST----RPKAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPESAPKLTR 433

                          90
                  ....*....|...
gi 817208853 2767 VAVRPSPASHATP 2779
Cdd:PRK14950  434 AAIPVDEKPKYTP 446

PHD5_KMT2D

cd15601

PHD finger 5 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...

1054-1090

6.01e-03

PHD finger 5 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named myeloid/lymphoid or mixed-lineage leukemia 4 (MLL4), a fourth human homolog of Drosophila trithorax, located on chromosome 12. KMT2D enzymatically generates trimethylated histone H3 Lys 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such asHOXA1-3 and NESTIN. It is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and KMT2D. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is downregulated in cholestasis. KMT2D contains the catalytic domain SET, five plant homeodomain (PHD) fingers, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions. This model corresponds to the fifth PHD finger.

Pssm-ID: 277074 Cd Length: 51 Bit Score: 37.19 E-value: 6.01e-03

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 817208853 1054 CPLCQRCYNENDFdtkMMECNECSCWVHARCEGLSDE 1090
Cdd:cd15601     2 CPVCRAKYVEEDL---LIQCRHCDRWVHAVCESLFTE 35

PHD_UHRF1_2

cd15525

PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein UHRF1 and ...

927-971

6.24e-03

PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein UHRF1 and UHRF2; UHRF1 is a unique chromatin effector protein that integrates the recognition of both histone PTMs and DNA methylation. It is essential for cell proliferation and plays a critical role in the development and progression of many human carcinomas, such as laryngeal squamous cell carcinoma (LSCC), gastric cancer (GC), esophageal squamous cell carcinoma (ESCC), colorectal cancer, prostate cancer, and breast cancer. UHRF1 acts as a transcriptional repressor through its binding to histone H3 when it is unmodified at Arg2. Its overexpression in human lung fibroblasts results in downregulation of expression of the tumour suppressor pRB. It also plays a role in transcriptional repression of the cell cycle regulator p21. Moreover, UHRF1-dependent repression of transcription factors can facilitate the G1-S transition. It interacts with Tat-interacting protein of 60 kDa (TIP60) and induces degradation-independent ubiquitination of TIP60. It is also an N-methylpurine DNA glycosylase (MPG)-interacting protein that binds MPG in a p53 status-independent manner in the DNA base excision repair (BER) pathway. In addition, UHRF1 functions as an epigenetic regulator that is important for multiple aspects of epigenetic regulation, including maintenance of DNA methylation patterns and recognition of various histone modifications. UHRF2 was originally identified as a ubiquitin ligase acting as a small ubiquitin-like modifier (SUMO) E3 ligase that enhances zinc finger protein 131 (ZNF131) SUMOylation but does not enhance ZNF131 ubiquitination. It also ubiquitinates PCNP, a PEST-containing nuclear protein. Moreover, UHRF2 functions as a nuclear protein involved in cell-cycle regulation and has been implicated in tumorigenesis. It interacts with cyclins, CDKs, p53, pRB, PCNA, HDAC1, DNMTs, G9a, methylated histone H3 lysine 9, and methylated DNA. It interacts with the cyclin E-CDK2 complex, ubiquitinates cyclins D1 and E1, induces G1 arrest, and is involved in the G1/S transition regulation. Furthermore, UHRF2 is a direct transcriptional target of the transcription factor E2F-1 in the induction of apoptosis. It recruits HDAC1 and binds to methyl-CpG. UHRF2 also participates in the maturation of Hepatitis B virus (HBV) by interacting with the HBV core protein and promoting its degradation. Both UHRF1 and UHRF2 contain an N-terminal ubiquitin-like domain (UBL), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a SET- and RING-associated (SRA) domain, and a C-terminal RING finger.

Pssm-ID: 277000 Cd Length: 47 Bit Score: 36.96 E-value: 6.24e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 817208853  927 CYLCGsaGK---EPLIHCQCCCEPYHVFCLEPSEWSACAQSNWSCPRC 971
Cdd:cd15525     2 CHVCG--GKqdpEKQLLCDECDMAYHLYCLDPPLTSLPDDDEWYCPDC 47

PHD2_CHD_II

cd15532

PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...

926-971

6.32e-03

PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD proteins includes chromodomain-helicase-DNA-binding protein CHD3, CHD4, and CHD5, which are nuclear and ubiquitously expressed chromatin remodelling ATPases generally associated with histone deacetylases (HDACs). They are involved in DNA Double Strand Break (DSB) signaling, DSB repair and/or p53-dependent pathways such as apoptosis and senescence, as well as in the maintenance of genomic stability, and/or cancer prevention. They function as subunits of the Nucleosome Remodelling and Deacetylase (NuRD) complex, which is generally associated with gene repression, heterochromatin formation, and overall chromatin compaction. In contrast to the class I CHD enzymes (CHD1 and CHD2), class II CHD proteins lack identifiable DNA-binding domains, but possess a C-terminal coiled-coil region. Moreover, in addition to the tandem chromodomains and a helicase domain, they all harbor tandem plant homeodomain (PHD) zinc fingers involved in the recognition of methylated histone tails. This model corresponds to the second PHD finger.

Pssm-ID: 277007 [Multi-domain] Cd Length: 43 Bit Score: 36.87 E-value: 6.32e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 817208853  926 VCYLCGSAGKepLIHCQCCCEPYHVFCLEPSEWSAcAQSNWSCPRC 971
Cdd:cd15532     1 FCRVCKDGGE--LLCCDGCPSSYHLHCLNPPLAEI-PDGDWFCPRC 43

PHD