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Conserved domains on  [gi|1907162496|ref|XP_036020904|]
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histone-lysine N-methyltransferase 2C isoform X26 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
3318-3470 5.18e-118

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: 369.84  E-value: 5.18e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3318 KSSQYRRMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRMDNDHVIDA 3397
Cdd:cd19171      1 KSSQYRKLKTEWRSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNRGIYMFRIDNDWVIDA 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907162496 3398 TLTGGPARYINHSCAPNCVAEVVTFERGHKIIISSNRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWM 3470
Cdd:cd19171     81 TMTGGPARYINHSCNPNCVAEVVTFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDQHKIPCLCGAPNCRKWM 153
ePHD2_KMT2C cd15697
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
2962-3066 1.45e-73

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: 240.72  E-value: 1.45e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2962 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTN 3041
Cdd:cd15697      1 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRLRCTN 80
                           90       100
                   ....*....|....*....|....*
gi 1907162496 3042 IYHFTCATKAQCMFFKDKTMLCPMH 3066
Cdd:cd15697     81 VYHFTCAIKAQCMFFKDKTMLCPMH 105
HMG-box_KMT2C cd22026
high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2C (KMT2C) and ...
135-215 1.39e-53

high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2C (KMT2C) and similar proteins; KMT2C, also called 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.


:

Pssm-ID: 438835  Cd Length: 81  Bit Score: 182.68  E-value: 1.39e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  135 QRSTLKWEKEEALGEMATVAPVLYTNINFPNLKEEFPDWTTRVKQIAKLWRKASSQERAPYVQKARDNRAALRINKVQMS 214
Cdd:cd22026      1 QRSTLKWEKEEALGEMATVAPVLYTNINFPNLKEEFPDWTTRVKQIAKLWRKASSQERAPYVQKARDNRAALRINKVQMS 80

                   .
gi 1907162496  215 N 215
Cdd:cd22026     81 N 81
FYRC pfam05965
F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
3168-3252 6.36e-25

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: 100.76  E-value: 6.36e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3168 RPVFVIRIVEqgHEDLVLSDSSPKDVWDKILEPVACVRKKSEMLQLFPAYLKGEDLFGLTVSAVARIAESLPGVEACENY 3247
Cdd:pfam05965    1 GPLFRVTVEE--DPDESFEGSSPTKCWSMVLERVQELRREAGLKLKLPESISGEDMFGLTHPAVVRLIESLPGAEKCTNY 78

                   ....*
gi 1907162496 3248 TFRYG 3252
Cdd:pfam05965   79 KFRYG 83
PHA03247 super family cl33720
large tegument protein UL36; Provisional
375-865 1.67e-19

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 97.32  E-value: 1.67e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  375 ESLSQSQNSQPP---SPQMFSPGSSHSRPPSPVdpyakmvgTPRPP-PGGHSFPRRNSVTPvencvplssvprpihmnet 450
Cdd:PHA03247  2541 EELASDDAGDPPpplPPAAPPAAPDRSVPPPRP--------APRPSePAVTSRARRPDAPP------------------- 2593
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  451 SATRPSPARDLCASSMTNSDPYAKPPDTPRPmmtdqfsKPFSLPRSPVISEQSTKGPLTTGTSDHFTKPS--PRTDAFQR 528
Cdd:PHA03247  2594 QSARPRAPVDDRGDPRGPAPPSPLPPDTHAP-------DPPPPSPSPAANEPDPHPPPTVPPPERPRDDPapGRVSRPRR 2666
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  529 QRLPDPYAGPSLTPaplgNGPfktplHPPPSQDPYGSVSQTSRRLSVDPYERPA------LTPRPVDNFSHSQSNDPYSH 602
Cdd:PHA03247  2667 ARRLGRAAQASSPP----QRP-----RRRAARPTVGSLTSLADPPPPPPTPEPAphalvsATPLPPGPAAARQASPALPA 2737
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  603 PPLTPHPAMTESFTHASRAFPQPGTISRSASQDPYSQPPGTP-----RPLIDSYSQTSGTARSNPDPYSQPPGTPRPNTI 677
Cdd:PHA03247  2738 APAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPprrltRPAVASLSESRESLPSPWDPADPPAAVLAPAAA 2817
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  678 DPYSQQPPTPRPSPQTDMFVSSVANQRHTDPYT------------HHLGPPRPGISVPYSQP---------PAVPRPRTS 736
Cdd:PHA03247  2818 LPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLplggsvapggdvRRRPPSRSPAAKPAAPArppvrrlarPAVSRSTES 2897
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  737 EGFTRPSSARPALMPNQDPFLQAAQNRVPGLPGPLIRPPdtcsqtPRPPGPGRIDTFTHAS---SSAVRDPYDQPPVTPR 813
Cdd:PHA03247  2898 FALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP------PRPQPPLAPTTDPAGAgepSGAVPQPWLGALVPGR 2971
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907162496  814 PHSESFGTSQvvhDLVDRPVPGSEGNFSTSSNLP-VSSQGQQFS-SVSQLPGPV 865
Cdd:PHA03247  2972 VAVPRFRVPQ---PAPSREAPASSTPPLTGHSLSrVSSWASSLAlHEETDPPPV 3022
FYRN pfam05964
F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
3111-3162 3.29e-18

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: 80.63  E-value: 3.29e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907162496 3111 GSLIFHTIGQLLPQQMqAFHSPKALFPVGYEASRLYWSTRYANRRCRYLCSI 3162
Cdd:pfam05964    1 GSLTVLSLGEIVPDRP-AFHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCEI 51
PHA03247 super family cl33720
large tegument protein UL36; Provisional
641-1248 5.57e-11

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 69.20  E-value: 5.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  641 PGTPRPLIDSYSQTSGTARSNPDPYSQPPgtPRPNTIDPYSQQPPTPRPSPQTDMFV-----------SSVANQRHTDPy 709
Cdd:PHA03247  2475 PGAPVYRRPAEARFPFAAGAAPDPGGGGP--PDPDAPPAPSRLAPAILPDEPVGEPVhprmltwirglEELASDDAGDP- 2551
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  710 THHLGPPRPGISVPYSQPPAVPRPRTSEGFTRPSSARPALMPnqdpflQAAQNRVPGlpGPLIRPPDTCSQTPRPPGPgr 789
Cdd:PHA03247  2552 PPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPP------QSARPRAPV--DDRGDPRGPAPPSPLPPDT-- 2621
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  790 idtfthasssavrDPYDQPPVTPRPH-SESFGTSQVVHDLVDRPVPGSEGNfSTSSNLPVSSQGQQFSSVSQLPGPVPTS 868
Cdd:PHA03247  2622 -------------HAPDPPPPSPSPAaNEPDPHPPPTVPPPERPRDDPAPG-RVSRPRRARRLGRAAQASSPPQRPRRRA 2687
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  869 GGTDTQNTVNMSQA-DTEKLRQRQKLREIILQQQQQKKIASRQEKGPQDTAVVPHPVPLPHWQPESINQAFTRPPPPYPG 947
Cdd:PHA03247  2688 ARPTVGSLTSLADPpPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPP 2767
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  948 STRSPVIPPLGPRyavfpkdQRGPYPPEVAGMGMRPHGFRFGFPGAGHGPMPSQDRFHVPQQIQGSGIPPhirrPMSMem 1027
Cdd:PHA03247  2768 APAPPAAPAAGPP-------RRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP----PTSA-- 2834
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 1028 prpsnnpplnnpvgLPQHFPPQGLPVQQHNILGQAFielrhrAPDGR-SRLPFAASPSSVIESPSHPRHGNF----LPRP 1102
Cdd:PHA03247  2835 --------------QPTAPPPPPGPPPPSLPLGGSV------APGGDvRRRPPSRSPAAKPAAPARPPVRRLarpaVSRS 2894
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 1103 DFPGPRHTDPIRQPSQCLSNQLPVHPNLEQVPPSQQEQGHPAHQSSIVMRP------------------LNHPLSGEFS- 1163
Cdd:PHA03247  2895 TESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPttdpagagepsgavpqpwLGALVPGRVAv 2974
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 1164 ------------EAPLSTSTPAETSPDNLEIAGQSSAGLEEKLDSDDPSVKE-LDVKDlegvevkDLDDEDLENLNL-DT 1229
Cdd:PHA03247  2975 prfrvpqpapsrEAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQtLWPPD-------DTEDSDADSLFDsDS 3047
                          650
                   ....*....|....*....
gi 1907162496 1230 EDGKGDDLDTLDNlETNDP 1248
Cdd:PHA03247  3048 ERSDLEALDPLPP-EPHDP 3065
Myosin_tail_1 super family cl37647
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
1687-1769 6.92e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


The actual alignment was detected with superfamily member pfam01576:

Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.55  E-value: 6.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 1687 EEWLQETQQLLQmqqkylEEQigahrKSKKALSAKQRT--AKKAG-REFPEEDAEQLKHVTEQQSMVQKQLEQIRKQQKE 1763
Cdd:pfam01576  467 ESQLQDTQELLQ------EET-----RQKLNLSTRLRQleDERNSlQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEE 535

                   ....*.
gi 1907162496 1764 HAELIE 1769
Cdd:pfam01576  536 DAGTLE 541
Tma16 super family cl12725
Translation machinery-associated protein 16; Proteins in this family localize to the nucleus. ...
194-277 8.45e-03

Translation machinery-associated protein 16; Proteins in this family localize to the nucleus. Their function is not clear.


The actual alignment was detected with superfamily member pfam11176:

Pssm-ID: 463236  Cd Length: 146  Bit Score: 39.42  E-value: 8.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  194 PYVQKA-RDNRAALRINKVQMSNDSMKRQQQ---------QDSIDPSSRIDS-----DLFKDPLKQRESEHEQEWKFRQQ 258
Cdd:pfam11176    7 PNSRKAkQLRRAALRDEKLEKLKAARAKKKNpllerlaffQEALDEDKKPLTleelhELIERYLHRFDEELEELKKERRP 86
                           90
                   ....*....|....*....
gi 1907162496  259 MRQKSKQQAKIEATQKLEQ 277
Cdd:pfam11176   87 GRPPSSREDLLEQKIEREE 105
 
Name Accession Description Interval E-value
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
3318-3470 5.18e-118

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: 369.84  E-value: 5.18e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3318 KSSQYRRMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRMDNDHVIDA 3397
Cdd:cd19171      1 KSSQYRKLKTEWRSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNRGIYMFRIDNDWVIDA 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907162496 3398 TLTGGPARYINHSCAPNCVAEVVTFERGHKIIISSNRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWM 3470
Cdd:cd19171     81 TMTGGPARYINHSCNPNCVAEVVTFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDQHKIPCLCGAPNCRKWM 153
ePHD2_KMT2C cd15697
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
2962-3066 1.45e-73

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: 240.72  E-value: 1.45e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2962 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTN 3041
Cdd:cd15697      1 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRLRCTN 80
                           90       100
                   ....*....|....*....|....*
gi 1907162496 3042 IYHFTCATKAQCMFFKDKTMLCPMH 3066
Cdd:cd15697     81 VYHFTCAIKAQCMFFKDKTMLCPMH 105
HMG-box_KMT2C cd22026
high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2C (KMT2C) and ...
135-215 1.39e-53

high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2C (KMT2C) and similar proteins; KMT2C, also called 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.


Pssm-ID: 438835  Cd Length: 81  Bit Score: 182.68  E-value: 1.39e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  135 QRSTLKWEKEEALGEMATVAPVLYTNINFPNLKEEFPDWTTRVKQIAKLWRKASSQERAPYVQKARDNRAALRINKVQMS 214
Cdd:cd22026      1 QRSTLKWEKEEALGEMATVAPVLYTNINFPNLKEEFPDWTTRVKQIAKLWRKASSQERAPYVQKARDNRAALRINKVQMS 80

                   .
gi 1907162496  215 N 215
Cdd:cd22026     81 N 81
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
3330-3469 3.48e-38

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 140.48  E-value: 3.48e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3330 KSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRgvYMFRMDNDHVIDATLTGGPARYINH 3409
Cdd:COG2940      5 HPRIEVRPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKEPLHT--YLFELDDDGVIDGALGGNPARFINH 82
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3410 SCAPNCVAEvvtfERGHKIIISSNRRIQKGEELCYDYKFDFEDDQHkiPCHCGavNCRKW 3469
Cdd:COG2940     83 SCDPNCEAD----EEDGRIFIVALRDIAAGEELTYDYGLDYDEEEY--PCRCP--NCRGT 134
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
3332-3453 8.23e-36

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: 133.61  E-value: 8.23e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  3332 NVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNR-GVYMFRMDNDHVIDATLTGGPARYINHS 3410
Cdd:smart00317    2 KLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkAFYLFDIDSDLCIDARRKGNLARFINHS 81
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 1907162496  3411 CAPNCVAEVVTFERGHKIIISSNRRIQKGEELCYDYKFDFEDD 3453
Cdd:smart00317   82 CEPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
3342-3447 2.73e-29

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


Pssm-ID: 459965 [Multi-domain]  Cd Length: 115  Bit Score: 114.54  E-value: 2.73e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3342 GLGLYAARDIEKHTMVIEYIGT-IIRNEVANRKEKLYESQNR----GVYMFRMDND--HVIDATLT--GGPARYINHSCA 3412
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLElrlwGPYLFTLDEDseYCIDARALyyGNWARFINHSCD 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1907162496 3413 PNCVAEVVTFERGHKIIISSNRRIQKGEELCYDYK 3447
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115
FYRC pfam05965
F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
3168-3252 6.36e-25

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: 100.76  E-value: 6.36e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3168 RPVFVIRIVEqgHEDLVLSDSSPKDVWDKILEPVACVRKKSEMLQLFPAYLKGEDLFGLTVSAVARIAESLPGVEACENY 3247
Cdd:pfam05965    1 GPLFRVTVEE--DPDESFEGSSPTKCWSMVLERVQELRREAGLKLKLPESISGEDMFGLTHPAVVRLIESLPGAEKCTNY 78

                   ....*
gi 1907162496 3248 TFRYG 3252
Cdd:pfam05965   79 KFRYG 83
FYRC smart00542
FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region ...
3170-3257 1.07e-24

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: 100.06  E-value: 1.07e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  3170 VFVIRIVEQGheDLVLSDSSPKDVWDKILEPVACVRKKSEMLQLFPAYLKGEDLFGLTVSAVARIAESLPGVEACENYTF 3249
Cdd:smart00542    1 LFRVEIESDP--GEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEGVSGEEMFGLSSPAVVKLIEALPGVHQCTNYWF 78

                    ....*...
gi 1907162496  3250 RYGRNPLM 3257
Cdd:smart00542   79 RYHRSPLL 86
PHA03247 PHA03247
large tegument protein UL36; Provisional
375-865 1.67e-19

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 97.32  E-value: 1.67e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  375 ESLSQSQNSQPP---SPQMFSPGSSHSRPPSPVdpyakmvgTPRPP-PGGHSFPRRNSVTPvencvplssvprpihmnet 450
Cdd:PHA03247  2541 EELASDDAGDPPpplPPAAPPAAPDRSVPPPRP--------APRPSePAVTSRARRPDAPP------------------- 2593
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  451 SATRPSPARDLCASSMTNSDPYAKPPDTPRPmmtdqfsKPFSLPRSPVISEQSTKGPLTTGTSDHFTKPS--PRTDAFQR 528
Cdd:PHA03247  2594 QSARPRAPVDDRGDPRGPAPPSPLPPDTHAP-------DPPPPSPSPAANEPDPHPPPTVPPPERPRDDPapGRVSRPRR 2666
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  529 QRLPDPYAGPSLTPaplgNGPfktplHPPPSQDPYGSVSQTSRRLSVDPYERPA------LTPRPVDNFSHSQSNDPYSH 602
Cdd:PHA03247  2667 ARRLGRAAQASSPP----QRP-----RRRAARPTVGSLTSLADPPPPPPTPEPAphalvsATPLPPGPAAARQASPALPA 2737
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  603 PPLTPHPAMTESFTHASRAFPQPGTISRSASQDPYSQPPGTP-----RPLIDSYSQTSGTARSNPDPYSQPPGTPRPNTI 677
Cdd:PHA03247  2738 APAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPprrltRPAVASLSESRESLPSPWDPADPPAAVLAPAAA 2817
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  678 DPYSQQPPTPRPSPQTDMFVSSVANQRHTDPYT------------HHLGPPRPGISVPYSQP---------PAVPRPRTS 736
Cdd:PHA03247  2818 LPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLplggsvapggdvRRRPPSRSPAAKPAAPArppvrrlarPAVSRSTES 2897
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  737 EGFTRPSSARPALMPNQDPFLQAAQNRVPGLPGPLIRPPdtcsqtPRPPGPGRIDTFTHAS---SSAVRDPYDQPPVTPR 813
Cdd:PHA03247  2898 FALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP------PRPQPPLAPTTDPAGAgepSGAVPQPWLGALVPGR 2971
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907162496  814 PHSESFGTSQvvhDLVDRPVPGSEGNFSTSSNLP-VSSQGQQFS-SVSQLPGPV 865
Cdd:PHA03247  2972 VAVPRFRVPQ---PAPSREAPASSTPPLTGHSLSrVSSWASSLAlHEETDPPPV 3022
FYRN pfam05964
F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
3111-3162 3.29e-18

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: 80.63  E-value: 3.29e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907162496 3111 GSLIFHTIGQLLPQQMqAFHSPKALFPVGYEASRLYWSTRYANRRCRYLCSI 3162
Cdd:pfam05964    1 GSLTVLSLGEIVPDRP-AFHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCEI 51
FYRN smart00541
FY-rich domain, N-terminal region; is sometimes closely juxtaposed with the C-terminal region ...
3121-3164 5.24e-17

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: 76.94  E-value: 5.24e-17
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1907162496  3121 LLPQQMQAFHSPKALFPVGYEASRLYWSTRYANRRCRYLCSIEE 3164
Cdd:smart00541    1 LLPIQGKLFHSESAIFPVGYKSTRKYWSVKDPNRRCLYSCVIDE 44
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
2989-3066 2.80e-15

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: 73.52  E-value: 2.80e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2989 HLNCALWSTEVYetQAGA------LINVELALRRGLQMKCVFCH-KTGATSGCHRFRCTNIYHFTCATKAQCMF-FKDKT 3060
Cdd:pfam13771    1 HVVCALWSPELV--QRGNdsmgfpIEDIEKIPKRRWKLKCYLCKkKGGACIQCSKKNCRRAFHVTCALEAGLLMqFDEDN 78
                           90
                   ....*....|
gi 1907162496 3061 ----MLCPMH 3066
Cdd:pfam13771   79 gtfkSYCKKH 88
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
379-800 2.51e-11

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: 70.18  E-value: 2.51e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  379 QSQNSQPPSPQMFSPGSShsrPPSPVDPYAKMVGTPRPPPGGHSFPrrnsvtpvencvplssvprpihmnetsatrpspa 458
Cdd:pfam03154  165 QILQTQPPVLQAQSGAAS---PPSPPPPGTTQAATAGPTPSAPSVP---------------------------------- 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  459 rdlcassmtnsdPYAKPPDTPRPMMTDQFSKPFSLPRSpviseqstkgplttgtsdhftkpsprTDAFQRQRLPDPYagP 538
Cdd:pfam03154  208 ------------PQGSPATSQPPNQTQSTAAPHTLIQQ--------------------------TPTLHPQRLPSPH--P 247
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  539 SLTPAPLGNGPFKTPLHPPPSQDPYGSVSQTSRRLSVDPYERP-ALTPRPVDNFSH-SQSNDPYSHPPLTPHPAMTESFT 616
Cdd:pfam03154  248 PLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQhPVPPQPFPLTPQsSQSQVPPGPSPAAPGQSQQRIHT 327
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  617 HASRAFPQPGTISRSASQDP-------YSQPPGTPRP-LIDSYSQTSGTARSNPDPYSQPPGTPRPNTIDPYS----QQP 684
Cdd:pfam03154  328 PPSQSQLQSQQPPREQPLPPaplsmphIKPPPTTPIPqLPNPQSHKHPPHLSGPSPFQMNSNLPPPPALKPLSslstHHP 407
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  685 PTPRPSPQTDMFVSS----------VANQRHTDPYTHHLGPPRPGISVPYSQPPAVPRPRTSEGFTR--PSSARPALMPN 752
Cdd:pfam03154  408 PSAHPPPLQLMPQSQqlppppaqppVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPitPPSGPPTSTSS 487
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  753 QDPFLQAAQNRVPGLPGPLI--------------RPPDTCSQTPRPPGPGR--------IDTFTHASSSA 800
Cdd:pfam03154  488 AMPGIQPPSSASVSSSGPVPaavscplppvqikeEALDEAEEPESPPPPPRspspeptvVNTPSHASQSA 557
PHA03247 PHA03247
large tegument protein UL36; Provisional
641-1248 5.57e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 69.20  E-value: 5.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  641 PGTPRPLIDSYSQTSGTARSNPDPYSQPPgtPRPNTIDPYSQQPPTPRPSPQTDMFV-----------SSVANQRHTDPy 709
Cdd:PHA03247  2475 PGAPVYRRPAEARFPFAAGAAPDPGGGGP--PDPDAPPAPSRLAPAILPDEPVGEPVhprmltwirglEELASDDAGDP- 2551
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  710 THHLGPPRPGISVPYSQPPAVPRPRTSEGFTRPSSARPALMPnqdpflQAAQNRVPGlpGPLIRPPDTCSQTPRPPGPgr 789
Cdd:PHA03247  2552 PPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPP------QSARPRAPV--DDRGDPRGPAPPSPLPPDT-- 2621
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  790 idtfthasssavrDPYDQPPVTPRPH-SESFGTSQVVHDLVDRPVPGSEGNfSTSSNLPVSSQGQQFSSVSQLPGPVPTS 868
Cdd:PHA03247  2622 -------------HAPDPPPPSPSPAaNEPDPHPPPTVPPPERPRDDPAPG-RVSRPRRARRLGRAAQASSPPQRPRRRA 2687
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  869 GGTDTQNTVNMSQA-DTEKLRQRQKLREIILQQQQQKKIASRQEKGPQDTAVVPHPVPLPHWQPESINQAFTRPPPPYPG 947
Cdd:PHA03247  2688 ARPTVGSLTSLADPpPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPP 2767
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  948 STRSPVIPPLGPRyavfpkdQRGPYPPEVAGMGMRPHGFRFGFPGAGHGPMPSQDRFHVPQQIQGSGIPPhirrPMSMem 1027
Cdd:PHA03247  2768 APAPPAAPAAGPP-------RRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP----PTSA-- 2834
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 1028 prpsnnpplnnpvgLPQHFPPQGLPVQQHNILGQAFielrhrAPDGR-SRLPFAASPSSVIESPSHPRHGNF----LPRP 1102
Cdd:PHA03247  2835 --------------QPTAPPPPPGPPPPSLPLGGSV------APGGDvRRRPPSRSPAAKPAAPARPPVRRLarpaVSRS 2894
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 1103 DFPGPRHTDPIRQPSQCLSNQLPVHPNLEQVPPSQQEQGHPAHQSSIVMRP------------------LNHPLSGEFS- 1163
Cdd:PHA03247  2895 TESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPttdpagagepsgavpqpwLGALVPGRVAv 2974
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 1164 ------------EAPLSTSTPAETSPDNLEIAGQSSAGLEEKLDSDDPSVKE-LDVKDlegvevkDLDDEDLENLNL-DT 1229
Cdd:PHA03247  2975 prfrvpqpapsrEAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQtLWPPD-------DTEDSDADSLFDsDS 3047
                          650
                   ....*....|....*....
gi 1907162496 1230 EDGKGDDLDTLDNlETNDP 1248
Cdd:PHA03247  3048 ERSDLEALDPLPP-EPHDP 3065
HMG smart00398
high mobility group;
154-207 1.06e-05

high mobility group;


Pssm-ID: 197700 [Multi-domain]  Cd Length: 70  Bit Score: 45.77  E-value: 1.06e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162496   154 APVLYTNINFPNLKEEFPDWTT--RVKQIAKLWRKASSQERAPYVQKARDNRAALR 207
Cdd:smart00398    8 AFMLFSQENRAKIKAENPDLSNaeISKKLGERWKLLSEEEKAPYEEKAKKDKERYE 63
HMG_box pfam00505
HMG (high mobility group) box;
156-207 1.33e-05

HMG (high mobility group) box;


Pssm-ID: 459837 [Multi-domain]  Cd Length: 68  Bit Score: 45.29  E-value: 1.33e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907162496  156 VLYTNINFPNLKEEFPDWTTR--VKQIAKLWRKASSQERAPYVQKARDNRAALR 207
Cdd:pfam00505    9 FLFSKEQRAKLKAENPGLKNAeiSKILGEKWKALSEEEKKPYEEKAEKEKARYE 62
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
3022-3066 1.14e-04

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: 42.20  E-value: 1.14e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1907162496  3022 CVFCHKTGATS---GCHRfrCTNIYHFTCATKAQCMFFKDKTMLCPMH 3066
Cdd:smart00249    2 CSVCGKPDDGGellQCDG--CDRWYHQTCLGPPLLEEEPDGKWYCPKC 47
COG5141 COG5141
PHD zinc finger-containing protein [General function prediction only];
2987-3070 5.23e-04

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


Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 45.74  E-value: 5.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2987 WVHLNCALWSTEVY--ETQAGALINVELALRRGL-QMKCVFCHKTGATS-GCHRFRCTNIYHFTCATKAqCMFFK----- 3057
Cdd:COG5141    268 WGHVICAMFNPELSfgHLLSKDPIDNIASVSSSRwKLGCLICKEFGGTCiQCSYFNCTRAYHVTCARRA-GYFDLniysh 346
                           90       100
                   ....*....|....*....|
gi 1907162496 3058 -------DKTMLCPMHKPKG 3070
Cdd:COG5141    347 ngisyciDHEPLCRKHYPLG 366
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
1687-1769 6.92e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.55  E-value: 6.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 1687 EEWLQETQQLLQmqqkylEEQigahrKSKKALSAKQRT--AKKAG-REFPEEDAEQLKHVTEQQSMVQKQLEQIRKQQKE 1763
Cdd:pfam01576  467 ESQLQDTQELLQ------EET-----RQKLNLSTRLRQleDERNSlQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEE 535

                   ....*.
gi 1907162496 1764 HAELIE 1769
Cdd:pfam01576  536 DAGTLE 541
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
670-1092 9.87e-04

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: 45.14  E-value: 9.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  670 GTPRPNTIDPYSQQPPTPRPSPQ---TDMFVSSVANQRHTDP-----YTHHLGPPRPGISVPYSQPPAVPRPRTSEGFTR 741
Cdd:pfam03154  130 GSSDPKDIDQDNRSTSPSIPSPQdneSDSDSSAQQQILQTQPpvlqaQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQ 209
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  742 PSSarPALMPNQDPFLQAA-----QNRVPGLPGPLIRPPDTCSQTPRPPGPGRIdtfthaSSSAVRDPYDQPPVTPRPHS 816
Cdd:pfam03154  210 GSP--ATSQPPNQTQSTAAphtliQQTPTLHPQRLPSPHPPLQPMTQPPPPSQV------SPQPLPQPSLHGQMPPMPHS 281
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  817 ESFGTSQVVHDLVDRPVPGSegnfstssnlPVSSQGQQfssvsqLPGPVPTSGGTDTQNTvnMSQADTEKLRQRQKLREI 896
Cdd:pfam03154  282 LQTGPSHMQHPVPPQPFPLT----------PQSSQSQV------PPGPSPAAPGQSQQRI--HTPPSQSQLQSQQPPREQ 343
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  897 ILQQQQqkkIASRQEKGPQDTAVVPHPVPLPHWQPESINQAF------TRPPPPY--PGSTRSPVIPPLG--PRYAVFPK 966
Cdd:pfam03154  344 PLPPAP---LSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSpfqmnsNLPPPPAlkPLSSLSTHHPPSAhpPPLQLMPQ 420
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  967 DQRGPYPPE-----VAGMGMRPHGFRFGFPGAGHgPMPSQDRFhvPQQIQGSGIPPHIRRPMSmemprpsnnPPLNNPVG 1041
Cdd:pfam03154  421 SQQLPPPPAqppvlTQSQSLPPPAASHPPTSGLH-QVPSQSPF--PQHPFVPGGPPPITPPSG---------PPTSTSSA 488
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907162496 1042 LPQHFPPQGLPVQQHNILGQAF------IELRHRAPDG----RSRLPFAASPS---SVIESPSH 1092
Cdd:pfam03154  489 MPGIQPPSSASVSSSGPVPAAVscplppVQIKEEALDEaeepESPPPPPRSPSpepTVVNTPSH 552
mukB PRK04863
chromosome partition protein MukB;
1684-1774 3.82e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.41  E-value: 3.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 1684 KQYEEWLQETQQLLQMQQKY--LEEQIGAHRKSKKALsakQRTAKKAGREFPEEDA---------EQLKHVTEQQSMVQK 1752
Cdd:PRK04863   503 RRLREQRHLAEQLQQLRMRLseLEQRLRQQQRAERLL---AEFCKRLGKNLDDEDEleqlqeeleARLESLSESVSEARE 579
                           90       100
                   ....*....|....*....|..
gi 1907162496 1753 QLEQIRKQQKEHAELIEDYRIK 1774
Cdd:PRK04863   580 RRMALRQQLEQLQARIQRLAAR 601
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1678-1802 3.93e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 3.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 1678 VNDSQRKQYEEwLQETQQLLQMQQKYLEEQigahRKSKKALSAKQRTAKKAGREFPEEDAEQLKHVTEQQSMVQKQLEQI 1757
Cdd:COG4942    144 LAPARREQAEE-LRADLAELAALRAELEAE----RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1907162496 1758 RKQQKEHAELIEDYRIKQQQQQQQCALAPPILMPGVQPQPplVPG 1802
Cdd:COG4942    219 QQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLPWP--VSG 261
Tma16 pfam11176
Translation machinery-associated protein 16; Proteins in this family localize to the nucleus. ...
194-277 8.45e-03

Translation machinery-associated protein 16; Proteins in this family localize to the nucleus. Their function is not clear.


Pssm-ID: 463236  Cd Length: 146  Bit Score: 39.42  E-value: 8.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  194 PYVQKA-RDNRAALRINKVQMSNDSMKRQQQ---------QDSIDPSSRIDS-----DLFKDPLKQRESEHEQEWKFRQQ 258
Cdd:pfam11176    7 PNSRKAkQLRRAALRDEKLEKLKAARAKKKNpllerlaffQEALDEDKKPLTleelhELIERYLHRFDEELEELKKERRP 86
                           90
                   ....*....|....*....
gi 1907162496  259 MRQKSKQQAKIEATQKLEQ 277
Cdd:pfam11176   87 GRPPSSREDLLEQKIEREE 105
 
Name Accession Description Interval E-value
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
3318-3470 5.18e-118

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: 369.84  E-value: 5.18e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3318 KSSQYRRMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRMDNDHVIDA 3397
Cdd:cd19171      1 KSSQYRKLKTEWRSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNRGIYMFRIDNDWVIDA 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907162496 3398 TLTGGPARYINHSCAPNCVAEVVTFERGHKIIISSNRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWM 3470
Cdd:cd19171     81 TMTGGPARYINHSCNPNCVAEVVTFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDQHKIPCLCGAPNCRKWM 153
SET_KMT2C cd19208
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) ...
3317-3470 6.56e-108

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: 340.84  E-value: 6.56e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3317 SKSSQYRRMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRMDNDHVID 3396
Cdd:cd19208      1 SKSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRIDNDHVID 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907162496 3397 ATLTGGPARYINHSCAPNCVAEVVTFERGHKIIISSNRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWM 3470
Cdd:cd19208     81 ATLTGGPARYINHSCAPNCVAEVVTFEKGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWM 154
SET_KMT2D cd19209
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...
3316-3470 3.70e-95

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: 304.70  E-value: 3.70e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3316 HSKSSQYRRMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRMDNDHVI 3395
Cdd:cd19209      1 HSKSSQYRRLKTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINNEHVI 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907162496 3396 DATLTGGPARYINHSCAPNCVAEVVTFERGHKIIISSNRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWM 3470
Cdd:cd19209     81 DATLTGGPARYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIPCHCGAWNCRKWM 155
ePHD2_KMT2C cd15697
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
2962-3066 1.45e-73

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: 240.72  E-value: 1.45e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2962 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTN 3041
Cdd:cd15697      1 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRLRCTN 80
                           90       100
                   ....*....|....*....|....*
gi 1907162496 3042 IYHFTCATKAQCMFFKDKTMLCPMH 3066
Cdd:cd15697     81 VYHFTCAIKAQCMFFKDKTMLCPMH 105
SET_SETD1-like cd10518
SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...
3319-3467 9.82e-73

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: 240.19  E-value: 9.82e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3319 SSQYRRMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQN-RGVYMFRMDNDHVIDA 3397
Cdd:cd10518      2 SKRFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKRYDEEGgGGTYMFRIDEDLVIDA 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3398 TLTGGPARYINHSCAPNCVAEVVTFERGHKIIISSNRRIQKGEELCYDYKFDFEDDQhKIPCHCGAVNCR 3467
Cdd:cd10518     82 TKKGNIARFINHSCDPNCYAKIITVDGEKHIVIFAKRDIAPGEELTYDYKFPIEDEE-KIPCLCGAPNCR 150
ePHD2_KMT2C_like cd15666
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
2962-3066 5.34e-70

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: 230.27  E-value: 5.34e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2962 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTN 3041
Cdd:cd15666      1 CVLCGGEGDGDTDGPGRLLNLDVDKWVHLNCALWSYEVYETQNGALMNVEEALRRALTTTCSHCGRTGATVPCFKPRCAN 80
                           90       100
                   ....*....|....*....|....*
gi 1907162496 3042 IYHFTCATKAQCMFFKDKTMLCPMH 3066
Cdd:cd15666     81 VYHLPCAIKDGCMFFKDKTMLCPSH 105
ePHD2_KMT2D cd15698
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...
2962-3067 3.74e-65

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: 216.84  E-value: 3.74e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2962 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTN 3041
Cdd:cd15698      1 CCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQKTGATNSCNRLRCPN 80
                           90       100
                   ....*....|....*....|....*.
gi 1907162496 3042 IYHFTCATKAQCMFFKDKTMLCPMHK 3067
Cdd:cd15698     81 VYHFACAIRAKCMFFKDKTMLCPMHK 106
SET_KMT2A_2B cd19170
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...
3319-3471 2.67e-59

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


Pssm-ID: 380947 [Multi-domain]  Cd Length: 152  Bit Score: 201.85  E-value: 2.67e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3319 SSQYRRMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRMDNDHVIDAT 3398
Cdd:cd19170      2 AMRFRHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKYYESKGIGCYMFRIDDDEVVDAT 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907162496 3399 LTGGPARYINHSCAPNCVAEVVTFERGHKIIISSNRRIQKGEELCYDYKFDFEDDqhKIPCHCGAVNCRKWMN 3471
Cdd:cd19170     82 MHGNAARFINHSCEPNCYSRVVNIDGKKHIVIFALRRILRGEELTYDYKFPIEDV--KIPCTCGSKKCRKYLN 152
SET_SETD1 cd19169
SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...
3330-3467 2.01e-54

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: 187.54  E-value: 2.01e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3330 KSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRG-VYMFRMDNDHVIDATLTGGPARYIN 3408
Cdd:cd19169     12 KKQLKFAKSRIHDWGLFALEPIAADEMVIEYVGQVIRQSVADEREKRYEAIGIGsSYLFRVDDDTIIDATKCGNLARFIN 91
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162496 3409 HSCAPNCVAEVVTFERGHKIIISSNRRIQKGEELCYDYKFDFEDDqhKIPCHCGAVNCR 3467
Cdd:cd19169     92 HSCNPNCYAKIITVESQKKIVIYSKRPIAVNEEITYDYKFPIEDE--KIPCLCGAPQCR 148
HMG-box_KMT2C cd22026
high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2C (KMT2C) and ...
135-215 1.39e-53

high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2C (KMT2C) and similar proteins; KMT2C, also called 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.


Pssm-ID: 438835  Cd Length: 81  Bit Score: 182.68  E-value: 1.39e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  135 QRSTLKWEKEEALGEMATVAPVLYTNINFPNLKEEFPDWTTRVKQIAKLWRKASSQERAPYVQKARDNRAALRINKVQMS 214
Cdd:cd22026      1 QRSTLKWEKEEALGEMATVAPVLYTNINFPNLKEEFPDWTTRVKQIAKLWRKASSQERAPYVQKARDNRAALRINKVQMS 80

                   .
gi 1907162496  215 N 215
Cdd:cd22026     81 N 81
SET_SET1 cd20072
SET domain (including post-SET domain) found in catalytic component of the Saccharomyces ...
3330-3467 4.86e-49

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: 172.22  E-value: 4.86e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3330 KSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRG-VYMFRMDNDHVIDATLTGGPARYIN 3408
Cdd:cd20072     12 KKQLKFARSAIHNWGLYAMENISAKDMVIEYVGEVIRQQVADEREKRYLRQGIGsSYLFRIDDDTVVDATKKGNIARFIN 91
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162496 3409 HSCAPNCVAEVVTFERGHKIIISSNRRIQKGEELCYDYKFDFEDDqhKIPCHCGAVNCR 3467
Cdd:cd20072     92 HCCDPNCTAKIIKVEGEKRIVIYAKRDIAAGEELTYDYKFPREED--KIPCLCGAPNCR 148
SET_KMT2A cd19206
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...
3321-3471 4.67e-47

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: 166.74  E-value: 4.67e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3321 QYRRMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRMDNDHVIDATLT 3400
Cdd:cd19206      4 RFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREKYYDSKGIGCYMFRIDDSEVVDATMH 83
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162496 3401 GGPARYINHSCAPNCVAEVVTFERGHKIIISSNRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWMN 3471
Cdd:cd19206     84 GNAARFINHSCEPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKFPIEDASNKLPCNCGAKKCRKFLN 154
SET_KMT2B cd19207
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...
3321-3471 3.29e-44

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: 158.65  E-value: 3.29e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3321 QYRRMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRMDNDHVIDATLT 3400
Cdd:cd19207      4 RFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDSKGIGCYMFRIDDFDVVDATMH 83
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162496 3401 GGPARYINHSCAPNCVAEVVTFERGHKIIISSNRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWMN 3471
Cdd:cd19207     84 GNAARFINHSCEPNCYSRVIHVEGQKHIVIFALRKIYRGEELTYDYKFPIEDASNKLPCNCGAKRCRRFLN 154
HMG_KMT2C-like cd21997
high mobility group (HMG)-box found in histone-lysine N-methyltransferases KMT2C, KMT2D and ...
140-206 1.53e-41

high mobility group (HMG)-box found in histone-lysine N-methyltransferases KMT2C, KMT2D and similar proteins; This subfamily includes KMT2C and KMT2D. KMT2C, also called myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3) or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) 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, and 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 called 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. All subfamily members contain one HMG-box domain.


Pssm-ID: 438813  Cd Length: 67  Bit Score: 147.50  E-value: 1.53e-41
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162496  140 KWEKEEALGEMATVAPVLYTNINFPNLKEEFPDWTTRVKQIAKLWRKASSQERAPYVQKARDNRAAL 206
Cdd:cd21997      1 KWEKDEPLGDMATISPVLYANINHPNLKQEYPDWTDRAKQIAKLWRKLSAEERAPYLQKARENRAAL 67
HMG-box_KMT2D cd22027
high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2D (KMT2D) and ...
131-212 5.85e-40

high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2D (KMT2D) and similar proteins; KMT2D, also called 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.


Pssm-ID: 438836  Cd Length: 84  Bit Score: 143.69  E-value: 5.85e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  131 LSNAQRSTLKWEKEEALGEMATVAPVLYTNINFPNLKEEFPDWTTRVKQIAKLWRKASSQERAPYVQKARDNRAALRINK 210
Cdd:cd22027      2 LSYNQRSLQRWEKDEELGELSTISPVLYANINFPNLKQDYPDWSSRCKQIMKLWRKVPAADKAPYLQKAKDNRAAHRINK 81

                   ..
gi 1907162496  211 VQ 212
Cdd:cd22027     82 VQ 83
SET_SETD1A cd19204
SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...
3330-3471 8.38e-40

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: 145.94  E-value: 8.38e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3330 KSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGV-YMFRMDNDHVIDATLTGGPARYIN 3408
Cdd:cd19204     13 KKKLRFGRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQVVADMREKRYVQEGIGSsYLFRVDHDTIIDATKCGNLARFIN 92
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907162496 3409 HSCAPNCVAEVVTFERGHKIIISSNRRIQKGEELCYDYKFDFEDDqhKIPCHCGAVNCRKWMN 3471
Cdd:cd19204     93 HCCTPNCYAKVITIESQKKIVIYSKQPIGVNEEITYDYKFPIEDN--KIPCLCGTENCRGTLN 153
SET_SETD1B cd19205
SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...
3330-3471 1.54e-38

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: 142.50  E-value: 1.54e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3330 KSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGV-YMFRMDNDHVIDATLTGGPARYIN 3408
Cdd:cd19205     13 KKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKRYEDEGIGSsYMFRVDHDTIIDATKCGNFARFIN 92
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907162496 3409 HSCAPNCVAEVVTFERGHKIIISSNRRIQKGEELCYDYKFDFEDDqhKIPCHCGAVNCRKWMN 3471
Cdd:cd19205     93 HSCNPNCYAKVITVESQKKIVIYSKQHINVNEEITYDYKFPIEDV--KIPCLCGSENCRGTLN 153
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
3330-3469 3.48e-38

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 140.48  E-value: 3.48e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3330 KSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRgvYMFRMDNDHVIDATLTGGPARYINH 3409
Cdd:COG2940      5 HPRIEVRPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKEPLHT--YLFELDDDGVIDGALGGNPARFINH 82
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3410 SCAPNCVAEvvtfERGHKIIISSNRRIQKGEELCYDYKFDFEDDQHkiPCHCGavNCRKW 3469
Cdd:COG2940     83 SCDPNCEAD----EEDGRIFIVALRDIAAGEELTYDYGLDYDEEEY--PCRCP--NCRGT 134
ePHD_KMT2A_like cd15664
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The ...
2962-3066 1.03e-37

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: 138.31  E-value: 1.03e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2962 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTN 3041
Cdd:cd15664      1 CALCGVYGDDEPNDAGRLLYCGQDEWVHINCALWSAEVFEEDDGSLQNVHSAVSRGRMMKCELCGKPGATVGCCLKSCPA 80
                           90       100
                   ....*....|....*....|....*
gi 1907162496 3042 IYHFTCATKAQCMFFKDKTMLCPMH 3066
Cdd:cd15664     81 NYHFMCARKAECVFQDDKKVFCPAH 105
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
3332-3453 8.23e-36

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: 133.61  E-value: 8.23e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  3332 NVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNR-GVYMFRMDNDHVIDATLTGGPARYINHS 3410
Cdd:smart00317    2 KLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkAFYLFDIDSDLCIDARRKGNLARFINHS 81
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 1907162496  3411 CAPNCVAEVVTFERGHKIIISSNRRIQKGEELCYDYKFDFEDD 3453
Cdd:smart00317   82 CEPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
ePHD_KMT2A cd15693
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant ...
2960-3067 2.80e-34

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: 128.58  E-value: 2.80e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2960 RKCCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRC 3039
Cdd:cd15693      1 RQCALCLKYGDDSANDAGRLLYIGQNEWTHVNCALWSAEVFEDDDGSLKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSC 80
                           90       100
                   ....*....|....*....|....*...
gi 1907162496 3040 TNIYHFTCATKAQCMFFKDKTMLCPMHK 3067
Cdd:cd15693     81 TSNYHFMCSRAKNCVFLEDKKVYCQRHK 108
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
3332-3467 4.50e-32

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: 123.13  E-value: 4.50e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3332 NVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQN-RGVYMFRMDNDHVIDATLTGGPARYINHS 3410
Cdd:cd10531      1 KLELFRTEKKGWGVKAKEDIQKGEFIIEYVGEVIDKKEFKERLDEYEELGkSNFYILSLSDDVVIDATRKGNLSRFINHS 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907162496 3411 CAPNCVAEvVTFERGHKII-ISSNRRIQKGEELCYDYKFDFEDDQhKIPCHCGAVNCR 3467
Cdd:cd10531     81 CEPNCETQ-KWIVNGEYRIgIFALRDIPAGEELTFDYNFVNYNEA-KQVCLCGAQNCR 136
SET_SETD2 cd19172
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...
3331-3470 4.74e-32

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: 123.46  E-value: 4.74e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3331 SNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRM-DNDHVIDATLTGGPARYINH 3409
Cdd:cd19172      2 AKVEVFRTEKKGWGLRAAEDLPKGTFVIEYVGEVLDEKEFKRRMKEYAREGNRHYYFMAlKSDEIIDATKKGNLSRFINH 81
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907162496 3410 SCAPNCVAEVVTFERGHKIIISSNRRIQKGEELCYDYKFD--FEDDQhkiPCHCGAVNCRKWM 3470
Cdd:cd19172     82 SCEPNCETQKWTVNGELRVGFFAKRDIPAGEELTFDYQFEryGKEAQ---KCYCGSPNCRGYI 141
SET_ASHR3-like cd19175
SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...
3342-3470 1.92e-31

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: 121.37  E-value: 1.92e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3342 GLGLYAARDIEKHTMVIEYIGTIIRNEVAnrKEKLYESQNRG---VYMFRMDNDHVIDATLTGGPARYINHSCAPNCVAE 3418
Cdd:cd19175     11 GWGLVADEDINAGEFIIEYVGEVIDDKTC--EERLWDMKHKGeknFYMCEIDKDMVIDATFKGNLSRFINHSCDPNCELQ 88
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907162496 3419 VVTFERGHKIIISSNRRIQKGEELCYDYKF-DFEDDQHkipCHCGAVNCRKWM 3470
Cdd:cd19175     89 KWQVDGETRIGVFAIRDIKKGEELTYDYQFvQFGADQD---CHCGSKNCRGKL 138
SET_EZH cd10519
SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...
3333-3446 2.52e-31

SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar proteins; The family includes EZH1 and EZH2. EZH1 (EC 2.1.1.43; also termed ENX-2, or histone-lysine N-methyltransferase EZH1) is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. EZH2 (EC 2.1.1.43; also termed lysine N-methyltransferase 6, ENX-1, or histone-lysine N-methyltransferase EZH2) is a catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Both, EZH1 and EZH2, can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively.


Pssm-ID: 380917  Cd Length: 117  Bit Score: 120.43  E-value: 2.52e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3333 VYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGvYMFRMDNDHVIDATLTGGPARYINHSCA 3412
Cdd:cd10519      3 LLLGKSDVAGWGLFLKEPIKKDEFIGEYTGELISQDEADRRGKIYDKYNSS-YLFNLNDQFVVDATRKGNKIRFANHSSN 81
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1907162496 3413 PNCVAEVVTFERGHKIIISSNRRIQKGEELCYDY 3446
Cdd:cd10519     82 PNCYAKVMMVNGDHRIGIFAKRDIEAGEELFFDY 115
SET_NSD cd19173
SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...
3342-3466 3.34e-31

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: 120.88  E-value: 3.34e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3342 GLGLYAARDIEKHTMVIEYIGTII-RNEVANRKEKLYESQNRGVYMFRMDNDHVIDATLTGGPARYINHSCAPNCVAEVV 3420
Cdd:cd19173     13 GWGLRTKRDIKKGDFVIEYVGELIdEEECRRRLKKAHENNITNFYMLTLDKDRIIDAGPKGNLSRFMNHSCQPNCETQKW 92
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1907162496 3421 TFERGHKIIISSNRRIQKGEELCYDYKFDFEDDQhKIPCHCGAVNC 3466
Cdd:cd19173     93 TVNGDTRVGLFAVRDIPAGEELTFNYNLDCLGNE-KKVCRCGAPNC 137
SET_SUV39H cd10542
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
3342-3470 1.23e-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: 120.09  E-value: 1.23e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3342 GLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRgVYMFRMD-----NDHVIDATLTGGPARYINHSCAPN-- 3414
Cdd:cd10542     99 GWGVKTLEDIKKGTFVMEYVGEIITSEEAERRGKIYDANGR-TYLFDLDyndddCEYTVDAAYYGNISHFINHSCDPNla 177
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162496 3415 ---CVAEVVtFERGHKIIISSNRRIQKGEELCYDYKFDFEDDQH----------KIPCHCGAVNCRKWM 3470
Cdd:cd10542    178 vyaVWINHL-DPRLPRIAFFAKRDIKAGEELTFDYLMTGTGGSSestipkpkdvRVPCLCGSKNCRKYL 245
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
3342-3447 2.73e-29

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


Pssm-ID: 459965 [Multi-domain]  Cd Length: 115  Bit Score: 114.54  E-value: 2.73e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3342 GLGLYAARDIEKHTMVIEYIGT-IIRNEVANRKEKLYESQNR----GVYMFRMDND--HVIDATLT--GGPARYINHSCA 3412
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLElrlwGPYLFTLDEDseYCIDARALyyGNWARFINHSCD 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1907162496 3413 PNCVAEVVTFERGHKIIISSNRRIQKGEELCYDYK 3447
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115
ePHD cd15571
Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is ...
2962-3066 3.99e-29

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: 113.83  E-value: 3.99e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2962 CCFCHEEGDGLTDGPArLLNLDLDLWVHLNCALWSTEVYETQAGAL--INVELALRRGLQMKCVFCHKT-GATSGCHRFR 3038
Cdd:cd15571      1 CALCPRSGGALKGGGA-LKTTSDGLWVHVVCALWSPEVYFDDGTLLevEGVSKIPKRRKKLKCSICGKRgGACIQCSYPG 79
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1907162496 3039 CTNIYHFTCATKAQCMF-----FKDKTMLCPMH 3066
Cdd:cd15571     80 CPRSFHVSCAIRAGCLFefedgPGNFVVYCPKH 112
ePHD_KMT2B cd15694
Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B); The extended plant ...
2962-3066 2.06e-27

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: 108.59  E-value: 2.06e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2962 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTN 3041
Cdd:cd15694      1 CALCLKYGDADSKDAGRLLYIGQNEWTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCEHCQKIGATVGCCLSACLS 80
                           90       100
                   ....*....|....*....|....*
gi 1907162496 3042 IYHFTCATKAQCMFFKDKTMLCPMH 3066
Cdd:cd15694     81 NFHFMCARASRCCFQDDKKVFCQKH 105
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
3342-3471 4.84e-26

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: 106.22  E-value: 4.84e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3342 GLGLYAARDIEKHTMVIEYIGTII-RNEVANRKEKLYeSQNRGVYMFRMDNDHVIDATLTGGPARYINHSCAPNCvaEVV 3420
Cdd:cd19174     11 GWGVRTKEPIKAGQFIIEYVGEVVsEQEFRRRMIEQY-HNHSHHYCLNLDSGMVIDGYRMGNEARFVNHSCDPNC--EMQ 87
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907162496 3421 TFE-RG-HKIIISSNRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWMN 3471
Cdd:cd19174     88 KWSvNGvYRIGLFALKDIPAGEELTYDYNFHSFNVEKQQPCKCGSPNCRGVIG 140
FYRC pfam05965
F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
3168-3252 6.36e-25

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: 100.76  E-value: 6.36e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3168 RPVFVIRIVEqgHEDLVLSDSSPKDVWDKILEPVACVRKKSEMLQLFPAYLKGEDLFGLTVSAVARIAESLPGVEACENY 3247
Cdd:pfam05965    1 GPLFRVTVEE--DPDESFEGSSPTKCWSMVLERVQELRREAGLKLKLPESISGEDMFGLTHPAVVRLIESLPGAEKCTNY 78

                   ....*
gi 1907162496 3248 TFRYG 3252
Cdd:pfam05965   79 KFRYG 83
FYRC smart00542
FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region ...
3170-3257 1.07e-24

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: 100.06  E-value: 1.07e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  3170 VFVIRIVEQGheDLVLSDSSPKDVWDKILEPVACVRKKSEMLQLFPAYLKGEDLFGLTVSAVARIAESLPGVEACENYTF 3249
Cdd:smart00542    1 LFRVEIESDP--GEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEGVSGEEMFGLSSPAVVKLIEALPGVHQCTNYWF 78

                    ....*...
gi 1907162496  3250 RYGRNPLM 3257
Cdd:smart00542   79 RYHRSPLL 86
SET_EZH2 cd19218
SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...
3329-3448 1.08e-23

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: 98.83  E-value: 1.08e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3329 WKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYEsQNRGVYMFRMDNDHVIDATLTGGPARYIN 3408
Cdd:cd19218      2 SKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYD-KYMCSFLFNLNNDFVVDATRKGNKIRFAN 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1907162496 3409 HSCAPNCVAEVVTFERGHKIIISSNRRIQKGEELCYDYKF 3448
Cdd:cd19218     81 HSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRY 120
SET_EZH1 cd19217
SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43) ...
3330-3452 3.51e-22

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: 95.13  E-value: 3.51e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3330 KSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYEsQNRGVYMFRMDNDHVIDATLTGGPARYINH 3409
Cdd:cd19217      5 KKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYD-KYMSSFLFNLNNDFVVDATRKGNKIRFANH 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1907162496 3410 SCAPNCVAEVVTFERGHKIIISSNRRIQKGEELCYDYKFDFED 3452
Cdd:cd19217     84 SVNPNCYAKVVMVNGDHRIGIFAKRAIQQGEELFFDYRYSQAD 126
SET_SETDB-like cd10538
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
3337-3446 1.12e-20

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: 93.20  E-value: 1.12e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3337 RSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYeSQNRGVYMFRMDND---------HVIDATLTGGPARYI 3407
Cdd:cd10538     95 RTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRGKIY-DKSGGSYLFDLDEFsdsdgdgeeLCVDATFCGNVSRFI 173
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1907162496 3408 NHSCAPN----CVAEVVTFERGHKIIISSNRRIQKGEELCYDY 3446
Cdd:cd10538    174 NHSCDPNlfpfNVVIDHDDLRYPRIALFATRDILPGEELTFDY 216
SET_NSD2 cd19211
SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...
3335-3466 4.38e-20

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: 89.28  E-value: 4.38e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3335 LARSRIQGLGLYAARDIEKHTMVIEYIGTII-RNEVANRKEKLYESQNRGVYMFRMDNDHVIDATLTGGPARYINHSCAP 3413
Cdd:cd19211      6 IIKTEGKGWGLIAKRDIKKGEFVNEYVGELIdEEECMARIKHAHENDITHFYMLTIDKDRIIDAGPKGNYSRFMNHSCQP 85
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907162496 3414 NCVAEVVTFERGHKIIISSNRRIQKGEELCYDYKFDFEDDQHKIpCHCGAVNC 3466
Cdd:cd19211     86 NCETQKWTVNGDTRVGLFAVCDIPAGTELTFNYNLDCLGNEKTV-CRCGAPNC 137
ePHD_RAI1_like cd15668
Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 ...
2962-3066 1.17e-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: 86.59  E-value: 1.17e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2962 CCFC--HEEGDGLTD--GPArllnldLDLWVHLNCALWSTEVYETqAGALINVELALRRGLQMKCVFCHKTGATSGCHRF 3037
Cdd:cd15668      1 CVFCkrGPHYKGLGDlfGPY------YEVWVHEDCAVWAPGVYLV-GGKLYGLEEAVWVAKQSVCSSCQQTGATIGCLHK 73
                           90       100       110
                   ....*....|....*....|....*....|
gi 1907162496 3038 RCTNIYHFTCATKAQCMFFKDK-TMLCPMH 3066
Cdd:cd15668     74 GCKAKYHYPCAVESGCQLDEENfSLLCPKH 103
PHA03247 PHA03247
large tegument protein UL36; Provisional
375-865 1.67e-19

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 97.32  E-value: 1.67e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  375 ESLSQSQNSQPP---SPQMFSPGSSHSRPPSPVdpyakmvgTPRPP-PGGHSFPRRNSVTPvencvplssvprpihmnet 450
Cdd:PHA03247  2541 EELASDDAGDPPpplPPAAPPAAPDRSVPPPRP--------APRPSePAVTSRARRPDAPP------------------- 2593
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  451 SATRPSPARDLCASSMTNSDPYAKPPDTPRPmmtdqfsKPFSLPRSPVISEQSTKGPLTTGTSDHFTKPS--PRTDAFQR 528
Cdd:PHA03247  2594 QSARPRAPVDDRGDPRGPAPPSPLPPDTHAP-------DPPPPSPSPAANEPDPHPPPTVPPPERPRDDPapGRVSRPRR 2666
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  529 QRLPDPYAGPSLTPaplgNGPfktplHPPPSQDPYGSVSQTSRRLSVDPYERPA------LTPRPVDNFSHSQSNDPYSH 602
Cdd:PHA03247  2667 ARRLGRAAQASSPP----QRP-----RRRAARPTVGSLTSLADPPPPPPTPEPAphalvsATPLPPGPAAARQASPALPA 2737
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  603 PPLTPHPAMTESFTHASRAFPQPGTISRSASQDPYSQPPGTP-----RPLIDSYSQTSGTARSNPDPYSQPPGTPRPNTI 677
Cdd:PHA03247  2738 APAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPprrltRPAVASLSESRESLPSPWDPADPPAAVLAPAAA 2817
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  678 DPYSQQPPTPRPSPQTDMFVSSVANQRHTDPYT------------HHLGPPRPGISVPYSQP---------PAVPRPRTS 736
Cdd:PHA03247  2818 LPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLplggsvapggdvRRRPPSRSPAAKPAAPArppvrrlarPAVSRSTES 2897
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  737 EGFTRPSSARPALMPNQDPFLQAAQNRVPGLPGPLIRPPdtcsqtPRPPGPGRIDTFTHAS---SSAVRDPYDQPPVTPR 813
Cdd:PHA03247  2898 FALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP------PRPQPPLAPTTDPAGAgepSGAVPQPWLGALVPGR 2971
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907162496  814 PHSESFGTSQvvhDLVDRPVPGSEGNFSTSSNLP-VSSQGQQFS-SVSQLPGPV 865
Cdd:PHA03247  2972 VAVPRFRVPQ---PAPSREAPASSTPPLTGHSLSrVSSWASSLAlHEETDPPPV 3022
ePHD1_KMT2C_like cd15665
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
2962-3066 5.56e-19

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: 84.29  E-value: 5.56e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2962 CCFCheegdgltdgparllNLDlDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTN 3041
Cdd:cd15665      1 CALC---------------NLG-EVYAHHCCAAWSEGVCQTEDGALENVDKAVAKALSQKCSFCLRYGASISCRMPSCSK 64
                           90       100
                   ....*....|....*....|....*..
gi 1907162496 3042 IYHFTCATKAQCmF--FKDKTMLCPMH 3066
Cdd:cd15665     65 SFHFPCAAAAGC-FqdIKTLTLFCPEH 90
SET_SETD8 cd10528
SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2. ...
3339-3446 7.64e-19

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: 85.71  E-value: 7.64e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3339 RIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYES-QNRGVYM--FRMDN-DHVIDATL-TGGPARYINHSC-A 3412
Cdd:cd10528     25 DGKGRGVIATRPFEKGDFVVEYHGDLITITEAKKREALYAKdPSTGCYMyyFQYKGkTYCVDATKeSGRLGRLINHSKkK 104
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1907162496 3413 PNCVAEVVTFERGHKIIISSNRRIQKGEELCYDY 3446
Cdd:cd10528    105 PNLKTKLLVIDGVPHLILVAKRDIKPGEELLYDY 138
SET_EHMT cd10543
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
3330-3467 1.20e-18

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: 87.78  E-value: 1.20e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3330 KSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKlyESqnrgvYMFRMDND----HVIDATLTGGPAR 3405
Cdd:cd10543     90 RYRLQLFRTRGMGWGVRALQDIPKGTFVCEYIGELISDSEADSRED--DS-----YLFDLDNKdgetYCIDARRYGNISR 162
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162496 3406 YINHSCAPNCVAevVTFERGH------KIIISSNRRIQKGEELCYDYKFDFEDDQHK-IPCHCGAVNCR 3467
Cdd:cd10543    163 FINHLCEPNLIP--VRVFVEHqdlrfpRIAFFASRDIKAGEELGFDYGEKFWRIKGKyFTCRCGSPKCK 229
FYRN pfam05964
F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
3111-3162 3.29e-18

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: 80.63  E-value: 3.29e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907162496 3111 GSLIFHTIGQLLPQQMqAFHSPKALFPVGYEASRLYWSTRYANRRCRYLCSI 3162
Cdd:pfam05964    1 GSLTVLSLGEIVPDRP-AFHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCEI 51
SET_NSD3 cd19212
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
3341-3466 1.02e-17

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


Pssm-ID: 380989 [Multi-domain]  Cd Length: 142  Bit Score: 82.28  E-value: 1.02e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3341 QGLGLYAARDIEKHTMVIEYIGTII-RNEVANRKEKLYESQNRGVYMFRMDNDHVIDATLTGGPARYINHSCAPNCVAEV 3419
Cdd:cd19212     12 RGWGLRTKRSIKKGEFVNEYVGELIdEEECRLRIKRAHENSVTNFYMLTVTKDRIIDAGPKGNYSRFMNHSCNPNCETQK 91
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1907162496 3420 VTFERGHKIIISSNRRIQKGEELCYDYKFDFEDDQHKIpCHCGAVNC 3466
Cdd:cd19212     92 WTVNGDVRVGLFALCDIPAGMELTFNYNLDCLGNGRTE-CHCGADNC 137
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
3342-3470 1.61e-17

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: 85.04  E-value: 1.61e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3342 GLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKlyeSQNRG----VYMFR--MDNDHV----IDATLTGGPARYINHSC 3411
Cdd:cd10544    101 GWGLRTLEFIPKGRFVCEYAGEVIGFEEARRRTK---SQTKGdmnyIIVLRehLSSGKVletfVDPTYIGNIGRFLNHSC 177
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907162496 3412 APNCVAEVVtfeRGH----KIIISSNRRIQKGEELCYDY------------KFDFEDDQHKIPCHCGAVNCRKWM 3470
Cdd:cd10544    178 EPNLFMVPV---RVDsmvpKLALFAARDIVAGEELSFDYsgefsnsvesvtLARQDESKSRKPCLCGAENCRGFL 249
SET_SUV39H_Clr4-like cd20073
SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 ...
3341-3470 2.92e-17

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: 84.55  E-value: 2.92e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3341 QGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYEsqNRGV-YMFRMD-------NDHVIDATLTGGPARYINHSCA 3412
Cdd:cd20073    103 KGWGLRCPRFIKAGTFIGVYLGEVITQSEAEIRGKKYD--NVGVtYLFDLDlfedqvdEYYTVDAQYCGDVTRFINHSCD 180
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907162496 3413 PNCVAEVV----TFERGHKIIISSNRRIQKGEELCYDYKFDFEDDQ----------------HKIPCHCGAVNCRKWM 3470
Cdd:cd20073    181 PNLAIYSVlrdkSDSKIYDLAFFAIKDIPALEELTFDYSGRNNFDQlgfignrsnskyinlkNKRPCYCGSANCRGWL 258
FYRN smart00541
FY-rich domain, N-terminal region; is sometimes closely juxtaposed with the C-terminal region ...
3121-3164 5.24e-17

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: 76.94  E-value: 5.24e-17
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1907162496  3121 LLPQQMQAFHSPKALFPVGYEASRLYWSTRYANRRCRYLCSIEE 3164
Cdd:smart00541    1 LLPIQGKLFHSESAIFPVGYKSTRKYWSVKDPNRRCLYSCVIDE 44
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
3342-3452 6.53e-17

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: 79.31  E-value: 6.53e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3342 GLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNrgvYMFRMDNDH-VIDATLTGGPARYINHSCAPNCVAEVV 3420
Cdd:cd10522     14 GLGLFAAETIAKGEFVGEYTGEVLDRWEEDRDSVYHYDPL---YPFDLNGDIlVIDAGKKGNLTRFINHSDQPNLELIVR 90
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1907162496 3421 TFERGHKIIISSNRRIQKGEELCYDYKFDFED 3452
Cdd:cd10522     91 TLKGEQHIGFVAIRDIKPGEELFISYGPKYWK 122
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
3318-3467 2.94e-16

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: 80.75  E-value: 2.94e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3318 KSSQYRRMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKlyesqnrGVYMFRMDND----H 3393
Cdd:cd10535     78 RNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE-------DSYLFDLDNKdgevY 150
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162496 3394 VIDATLTGGPARYINHSCAPNCVAEVVTFE----RGHKIIISSNRRIQKGEELCYDYKFDFEDDQHKI-PCHCGAVNCR 3467
Cdd:cd10535    151 CIDARFYGNVSRFINHHCEPNLVPVRVFMAhqdlRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLfSCRCGSPKCR 229
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
3331-3466 5.63e-16

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: 77.27  E-value: 5.63e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3331 SNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTII-RNEVANRKEKLYESQNRGVYMFRMDNDHVIDATLTGGPARYINH 3409
Cdd:cd19210      2 PEVEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIdEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMNH 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162496 3410 SCAPNCVAEVVTFERGHKIIISSNRRIQKGEELCYDYKFDFEDDQhKIPCHCGAVNC 3466
Cdd:cd19210     82 CCQPNCETQKWTVNGDTRVGLFALCDIKAGTELTFNYNLECLGNG-KTVCKCGAPNC 137
SET_SUV39H_DIM5-like cd19473
SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...
3342-3470 5.85e-16

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: 81.21  E-value: 5.85e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3342 GLGLYAARDIEKHTMVIEYIGTIIRNEVAN-RKEKLYESQNRGVYMFRMD---NDHVIDATLTG-----------GPARY 3406
Cdd:cd19473    117 GWGVRSTVDIKRGQFVDCYVGEIITPEEAQrRRDAATIAQRKDVYLFALDkfsDPDSLDPRLRGdpyeidgefmsGPTRF 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3407 INHSCAPNC-VAEVVT------FergHKIIISSNRRIQKGEELCYDY----------KFDFEDDQHKIPCHCGAVNCRKW 3469
Cdd:cd19473    197 INHSCDPNLrIFARVGdhadkhI---HDLAFFAIKDIPRGTELTFDYvdgvtgldddAGDEEKEKEMTKCLCGSPKCRGY 273

                   .
gi 1907162496 3470 M 3470
Cdd:cd19473    274 L 274
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
3341-3470 8.44e-16

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: 79.93  E-value: 8.44e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3341 QGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRgVYMFRMD---NDHVIDATLTGGPARYINHSCAPNCVA 3417
Cdd:cd10532     95 RGWGVKTLQKIKKNSFVMEYVGEVITSEEAERRGQFYDSKGI-TYLFDLDyesDEFTVDAARYGNVSHFVNHSCDPNLQV 173
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3418 EVVTFE----RGHKIIISSNRRIQKGEELCYDYKFDFEDD-------------QHKIPCHCGAVNCRKWM 3470
Cdd:cd10532    174 FNVFIDnldtRLPRIALFSTRTIKAGEELTFDYQMKGSGDlssdsidnspakkRVRTVCKCGAVTCRGYL 243
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
3332-3446 1.33e-15

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: 73.82  E-value: 1.33e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3332 NVYLARSRIQGLGLYAARDIEKhtmvieyiGTIIrnevanrkeklyesqnrgvymfrmdndhvidatltgGPARYINHSC 3411
Cdd:cd08161      1 EIRPSTIPGAGFGLFATRDIPK--------GEVI------------------------------------GLARFINHSC 36
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1907162496 3412 APNCVAEVVTFERGHKIIISSNRRIQKGEELCYDY 3446
Cdd:cd08161     37 EPNCEFEEVYVGGKPRVFIVALRDIKAGEELTVDY 71
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
3341-3470 1.42e-15

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: 79.55  E-value: 1.42e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3341 QGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNrGVYMFRMD---NDHVIDATLTGGPARYINHSCAPNCVA 3417
Cdd:cd10525     97 RGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQG-ATYLFDLDyveDVYTVDAAYYGNISHFVNHSCDPNLQV 175
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162496 3418 EVVTF----ERGHKIIISSNRRIQKGEELCYDYKF-----DFEDDQH-----------------KIPCHCGAVNCRKWM 3470
Cdd:cd10525    176 YNVFIdnldERLPRIALFATRTIRAGEELTFDYNMqvdpvDAESTKMdsnfglaglpgspkkrvRIECKCGVRSCRKYL 254
SET_EZH-like cd19168
SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb ...
3333-3450 1.62e-15

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: 75.30  E-value: 1.62e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3333 VYLARSRIQ-GLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRgVYMFRMDNDHVIDATLTGGPARYINH-- 3409
Cdd:cd19168      3 VVLGKSQLEcGLGLFAAEDIKEGEFVIEYTGELISHDEGVRREHRRGDVSY-LYLFEEQEGIWVDAAIYGNLSRYINHat 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1907162496 3410 --SCAPNCVAEVVTFERGHKIIISSNRRIQKGEELCYDYKFDF 3450
Cdd:cd19168     82 dkVKTGNCMPKIMYVNHEWRIKFTAIKDIKIGEELFFNYGDNF 124
SET_SETD5-like cd10529
SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...
3344-3450 2.42e-15

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


Pssm-ID: 380927  Cd Length: 127  Bit Score: 75.00  E-value: 2.42e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3344 GLYAARDIEKHTMVIEYIGTI-IRNEVANRKEKLYESQNRgVYMF--RMDNDHVIDATLTGGPARYINHSCAPNCVAEVV 3420
Cdd:cd10529     18 GLVATEDISPGEPILEYKGEVsLRSEFKEDNGFFKRPSPF-VFFYdgFEGLPLCVDARKYGNEARFIRRSCRPNAELRHV 96
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1907162496 3421 TFERG-HKIIISSNRRIQKGEELCYDYKFDF 3450
Cdd:cd10529     97 VVSNGeLRLFIFALKDIRKGTEITIPFDYDY 127
PHA03247 PHA03247
large tegument protein UL36; Provisional
343-868 2.75e-15

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 83.45  E-value: 2.75e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  343 LPGTPASTPSDGVFVKPQPPPPPSTPSRIPVQESLS-QSQNSQPPSPQMFSPGSSHSRPPSPVDPYAKmvgTPRPPPGGH 421
Cdd:PHA03247  2555 LPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDaPPQSARPRAPVDDRGDPRGPAPPSPLPPDTH---APDPPPPSP 2631
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  422 SfPRRNSVTPVEncvPLSSVPRPIHMNETSATRPSPARDlcASSMTNSDPYAKPPDTPRPMMTDQFSKP---FSLPRSPV 498
Cdd:PHA03247  2632 S-PAANEPDPHP---PPTVPPPERPRDDPAPGRVSRPRR--ARRLGRAAQASSPPQRPRRRAARPTVGSltsLADPPPPP 2705
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  499 ISEQSTKGPLTTGTsdhftkPSPRTDAFQRQRLPDPYAGPSLTPAPLGNGPFKTPLHPPPSQDPYGSVSQTSRRLSVDPy 578
Cdd:PHA03247  2706 PTPEPAPHALVSAT------PLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAG- 2778
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  579 ERPALTPRPVDNFSHSQSN-----DPYSHPPLTPHPAMTESFTHASRAFPQPGTISRSASQDPYSQPPGTPRPLIDSYSQ 653
Cdd:PHA03247  2779 PPRRLTRPAVASLSESRESlpspwDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAP 2858
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  654 TSGTARSNP--DPYSQPPGTPRP-----------NTIDPYSQQPPTPRPSPQTDMFVSSVANQRHTDPYTHHLGPPRPGI 720
Cdd:PHA03247  2859 GGDVRRRPPsrSPAAKPAAPARPpvrrlarpavsRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR 2938
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  721 SVPYSQPPAVPRPRTSEGFTRPSSARPALMPNQDPflqAAQNRVPGlPGPLIRPPDTCSQTPRPPGPGRIDTFthASSSA 800
Cdd:PHA03247  2939 PQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVA---VPRFRVPQ-PAPSREAPASSTPPLTGHSLSRVSSW--ASSLA 3012
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  801 VRDPYDQPPVT-------PRPHSESFGTSQVVHDLVDR------PVPGSEGNFSTSSNLPVSSQGQQFSSVSQLPGPVPT 867
Cdd:PHA03247  3013 LHEETDPPPVSlkqtlwpPDDTEDSDADSLFDSDSERSdlealdPLPPEPHDPFAHEPDPATPEAGARESPSSQFGPPPL 3092

                   .
gi 1907162496  868 S 868
Cdd:PHA03247  3093 S 3093
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
2989-3066 2.80e-15

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: 73.52  E-value: 2.80e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2989 HLNCALWSTEVYetQAGA------LINVELALRRGLQMKCVFCH-KTGATSGCHRFRCTNIYHFTCATKAQCMF-FKDKT 3060
Cdd:pfam13771    1 HVVCALWSPELV--QRGNdsmgfpIEDIEKIPKRRWKLKCYLCKkKGGACIQCSKKNCRRAFHVTCALEAGLLMqFDEDN 78
                           90
                   ....*....|
gi 1907162496 3061 ----MLCPMH 3066
Cdd:pfam13771   79 gtfkSYCKKH 88
PHA03247 PHA03247
large tegument protein UL36; Provisional
529-1101 8.44e-15

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 81.91  E-value: 8.44e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  529 QRLPD---PYAgPSLTPAPLGNGPFKTPLHPPPSQDPYGSVSQTSRRLSVDPyeRPALTPRPVDNFSHSQSNDPYSHPPL 605
Cdd:PHA03247  2481 RRPAEarfPFA-AGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPVHP--RMLTWIRGLEELASDDAGDPPPPLPP 2557
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  606 TPHPAMTESFTHASRAFPQPGTISRSASQDPYSQPPGTPRPlidsysqtsgtaRSNPDPYSQPPGTPRPNTIDPYSQQPP 685
Cdd:PHA03247  2558 AAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARP------------RAPVDDRGDPRGPAPPSPLPPDTHAPD 2625
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  686 TPRPSPqtdmfvSSVANQRhtdPYTHHLGPPRPGISVPYSQPPAVPRPRTSEGFTRPSSA--------RPALMPNQDPFL 757
Cdd:PHA03247  2626 PPPPSP------SPAANEP---DPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQAssppqrprRRAARPTVGSLT 2696
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  758 QAAQNRVPGlPGPLIRPPDTCSQTPRPPGPgridtfthassSAVRDPYDQPPVTPRPHSESFGTSqvvhdlvdrpVPGSE 837
Cdd:PHA03247  2697 SLADPPPPP-PTPEPAPHALVSATPLPPGP-----------AAARQASPALPAAPAPPAVPAGPA----------TPGGP 2754
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  838 GnfstssnlPVSSQGQQFSSVSQLPGPVPTSGGTdtqntvnmsqadteklrqrqklREIILQQQQQKKIASRQEKGPQDT 917
Cdd:PHA03247  2755 A--------RPARPPTTAGPPAPAPPAAPAAGPP----------------------RRLTRPAVASLSESRESLPSPWDP 2804
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  918 AVVPHPVPLPH-WQPESINQAFTRPPPPY-----PGSTRSPVIPPLGPRYAVFPK---DQRGP--YPPEVAGMGMRPHGF 986
Cdd:PHA03247  2805 ADPPAAVLAPAaALPPAASPAGPLPPPTSaqptaPPPPPGPPPPSLPLGGSVAPGgdvRRRPPsrSPAAKPAAPARPPVR 2884
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  987 RFGFPGaghgPMPSQDRFHVPQ-QIQGSGIPPHIRRPMSMEMPRPSNNPPLNNPV-GLPQ-HFPPQGLPVQQHNILGQA- 1062
Cdd:PHA03247  2885 RLARPA----VSRSTESFALPPdQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPpPRPQpPLAPTTDPAGAGEPSGAVp 2960
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|...
gi 1907162496 1063 FIELRHRAPDG----RSRLPFAASPSSVIESPSHPRHGNFLPR 1101
Cdd:PHA03247  2961 QPWLGALVPGRvavpRFRVPQPAPSREAPASSTPPLTGHSLSR 3003
PHA03247 PHA03247
large tegument protein UL36; Provisional
305-837 1.01e-14

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 81.52  E-value: 1.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  305 APGSDTPSSGAQSPLTPqagngnvSPAQTfhkdlfskHLPGTPASTPSDGVFVKPQPPPPPSTPSRIPVQE------SLS 378
Cdd:PHA03247  2600 APVDDRGDPRGPAPPSP-------LPPDT--------HAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDpapgrvSRP 2664
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  379 QSQNSQPPSPQMFSPGSSHSRP--PSPVDPYAKMVGTPRPPPGGHSFPRRNSVTPVENCVPLSSVPRPIHMNETSATRPS 456
Cdd:PHA03247  2665 RRARRLGRAAQASSPPQRPRRRaaRPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAV 2744
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  457 PARDLCASSMT--NSDPYAKPPDTPRPMMTDQFSKPFSLPRSPV--ISEQSTKGPLTTGTSDHFTKPSPRTDAFQRQRLP 532
Cdd:PHA03247  2745 PAGPATPGGPArpARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVasLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  533 DPYAGPSLTPAPLgnGPFKTPLHPPPSQDPYGSVSQTSrrlsvDPYERPalTPRPvdnfshsqsndPYSHPPLTPHPAMt 612
Cdd:PHA03247  2825 AGPLPPPTSAQPT--APPPPPGPPPPSLPLGGSVAPGG-----DVRRRP--PSRS-----------PAAKPAAPARPPV- 2883
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  613 esfthasRAFPQPGTisrSASQDPYSQPPGTPRPLIDSYSQTSgtarsnPDPYSQPPGTPRPNTIDPYSQQPPTPrPSPQ 692
Cdd:PHA03247  2884 -------RRLARPAV---SRSTESFALPPDQPERPPQPQAPPP------PQPQPQPPPPPQPQPPPPPPPRPQPP-LAPT 2946
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  693 TDMFVSSVANQRHTDPYTHHLGPPRpgisvpysqpPAVPRPRTSEgftrPSSARPALMPNQDPFLQAAQNRVPGLPGPLI 772
Cdd:PHA03247  2947 TDPAGAGEPSGAVPQPWLGALVPGR----------VAVPRFRVPQ----PAPSREAPASSTPPLTGHSLSRVSSWASSLA 3012
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907162496  773 ------RPPDTCSQTPRPP-------GPGRIDTFTHASSSAVRDPYDQPPVTPRPHSESFGTSQVVHdlvdRPVPGSE 837
Cdd:PHA03247  3013 lheetdPPPVSLKQTLWPPddtedsdADSLFDSDSERSDLEALDPLPPEPHDPFAHEPDPATPEAGA----RESPSSQ 3086
ePHD1_KMT2D cd15695
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...
2985-3066 1.36e-14

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: 71.49  E-value: 1.36e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2985 DLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTNIYHFTCATkAQCMFFKDKT--ML 3062
Cdd:cd15695      8 ECWVHHWCAAWSAGVKQHEGDGLIGVDKAVFSGISQKCEHCKRLGATIQCHAEGCPRFYHFPCAA-ASGSFQSMKTllLL 86

                   ....
gi 1907162496 3063 CPMH 3066
Cdd:cd15695     87 CPEH 90
ePHD_RAI1 cd15700
Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant ...
2962-3066 1.65e-14

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: 71.83  E-value: 1.65e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2962 CCFCHEegdgltdgPARLLNL-DL------DLWVHLNCALWSTEVYETqAGALINVELALRRGLQMKCVFCHKTGATSGC 3034
Cdd:cd15700      1 CCLCRN--------PANYKDLgDLcgpyypEHWVHEACAVWTTGVYLV-AGKLFGLQEAVQKAADAKCSSCQGAGATVGC 71
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1907162496 3035 HRFRCTNIYHFTCATKAQCMFFKDK-TMLCPMH 3066
Cdd:cd15700     72 CHKGCTQSYHYICAVEAGCLFEEENfSLRCPKH 104
ePHD_TCF20 cd15699
Extended PHD finger (ePHD) found in transcription factor 20 (TCF-20); The extended plant ...
2962-3066 2.87e-14

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: 71.10  E-value: 2.87e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2962 CCFCHEEGD----GLTDGPArllnldLDLWVHLNCALWSTEVYETqAGALINVELALRRGLQMKCVFCHKTGATSGCHRF 3037
Cdd:cd15699      1 CCLCGKWANyrnlGDLFGPF------YEFWVHEGCILWANGIYLV-CGRLYGLQEALDIAREMKCSHCQEAGATLGCYNK 73
                           90       100       110
                   ....*....|....*....|....*....|
gi 1907162496 3038 RCTNIYHFTCATKAQCMFFKDK-TMLCPMH 3066
Cdd:cd15699     74 GCSFRYHYPCAIDADCLLNEENfSVRCPKH 103
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
3318-3467 3.43e-14

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: 75.05  E-value: 3.43e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3318 KSSQYRRMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKlyesqnrGVYMFRMDND----H 3393
Cdd:cd10533     78 RNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED-------DSYLFDLDNKdgevY 150
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162496 3394 VIDATLTGGPARYINHSCAPNCVAEVVTFE----RGHKIIISSNRRIQKGEELCYDYKFDFEDDQHK-IPCHCGAVNCR 3467
Cdd:cd10533    151 CIDARYYGNISRFINHLCDPNIIPVRVFMLhqdlRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKyFTCQCGSEKCK 229
ePHD1_KMT2C cd15696
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
2985-3066 3.45e-14

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: 70.36  E-value: 3.45e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2985 DLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTNIYHFTCATKAQCMF-FKDKTMLC 3063
Cdd:cd15696      8 ECWAHLRCAEWSLGVCQGEEQLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQdFSRRLLLC 87

                   ...
gi 1907162496 3064 PMH 3066
Cdd:cd15696     88 PTH 90
ePHD_PHF6_like cd15673
Extended PHD finger found in PHD finger protein 6 (PHF6) and PHD finger protein 11 (PHF11); ...
2962-3066 3.19e-13

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: 68.57  E-value: 3.19e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2962 CCFCHEEGDGLTDGParLLNLDLDLWVHLNCALWSTEVYETQ-------AGALIN-VELALRRGLQMKCVFCHKTGATSG 3033
Cdd:cd15673      1 CGFCKSGEENKETGG--KLASGEKIAAHHNCMLFSSGLVQYVspnendfGGFDIEdVKKEIKRGRKLKCNLCKKTGATIG 78
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907162496 3034 CHRFRCTNIYHFTCATKAQCMFFKDK-----TMLCPMH 3066
Cdd:cd15673     79 CDVKQCKKTYHYHCAKKDDAKIIERNsqgiyRVYCKNH 116
SET_SETDB1 cd10517
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
3342-3468 8.48e-13

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: 71.94  E-value: 8.48e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3342 GLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLY--------------ESQNRGVYMFRMDNDHVIDATLTGGPARYI 3407
Cdd:cd10517    140 GWGIRCLDDIPKGSFVCIYAGQILTEDEANEEGLQYgdeyfaeldyievvEKLKEGYESDVEEHCYIIDAKSEGNLGRYL 219
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162496 3408 NHSCAPNCVAEVVtFERGHKIIIS-----SNRRIQKGEELCYDYKFDFEDDQHKI-PCHCGAVNCRK 3468
Cdd:cd10517    220 NHSCSPNLFVQNV-FVDTHDLRFPwvaffASRYIRAGTELTWDYNYEVGSVPGKVlYCYCGSSNCRG 285
zf-HC5HC2H_2 pfam13832
PHD-zinc-finger like domain;
2960-3055 8.57e-13

PHD-zinc-finger like domain;


Pssm-ID: 463991 [Multi-domain]  Cd Length: 109  Bit Score: 66.98  E-value: 8.57e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2960 RKCCFCHEEGDGL---TDGparllnldldLWVHLNCALWSTEVY--ETQAGALINVELALRRGLQMKCVFCHK-TGATSG 3033
Cdd:pfam13832    1 VRCCLCPLRGGALkqtSDG----------RWVHVLCAIFVPEVRfgNVATMEPIDVSRIPPERWKLKCVFCKKrSGACIQ 70
                           90       100
                   ....*....|....*....|..
gi 1907162496 3034 CHRFRCTNIYHFTCATKAQCMF 3055
Cdd:pfam13832   71 CSKGRCTTAFHVTCAQAAGVYM 92
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
3341-3470 2.77e-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: 69.86  E-value: 2.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3341 QGLGLYAARDIEKHTMVIEYIGTI---IRNEVANRKEKLYESQNRGVYMFRM-----------DNDHVIDATLTGGPARY 3406
Cdd:cd10523    118 KGWGVRCLDDIDKGTFVCIYAGRVlsrARSPTEPLPPKLELPSENEVEVVTSwlilskkrklrENVCFLDASKEGNVGRF 197
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162496 3407 INHSCAPNCVAEVVTFERGHK----IIISSNRRIQKGEELCYDYKFDFEDDQHK-IPCHCGAVNCRKWM 3470
Cdd:cd10523    198 LNHSCCPNLFVQNVFVDTHDKnfpwVAFFTNRVVKAGTELTWDYSYDAGTSPEQeIPCLCGVNKCQKKI 266
SET_SETDB cd10541
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...
3341-3468 5.24e-12

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: 68.34  E-value: 5.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3341 QGLGLYAARDIEKHTMVIEYIGTIIRNEVANrKEKLYESQNrgvYMFRMD----NDHVIDATLTGGPARYINHSCAPNCV 3416
Cdd:cd10541    102 KGWGIRCLDDIAKGTFVCIYAGKILTDDFAD-KEGLEMGDE---YFANLDhieeSCYIIDAKLEGNLGRYLNHSCSPNLF 177
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907162496 3417 AEVVtFERGHK-----IIISSNRRIQKGEELCYDYKFDFED-DQHKIPCHCGAVNCRK 3468
Cdd:cd10541    178 VQNV-FVDTHDlrfpwVAFFASKRIKAGTELTWDYNYEVGSvEGKELLCCCGSNECRG 234
ePHD_PHF7_G2E3_like cd15669
Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ...
2962-3066 1.07e-11

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: 64.19  E-value: 1.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2962 CCFCHEEGDGlTDGPARLLNLDlDLWVHLNCALWSTEVYETQ------AGALIN-VELALRRGLQMKCVFCHKTGATSGC 3034
Cdd:cd15669      1 CVLCGRSDDD-PDKYGEKLQKD-GICAHYFCLLFSSGLPQRGednegiYGFLPEdIRKEVRRASRLRCFYCKKKGASIGC 78
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1907162496 3035 HRFRCTNIYHFTCATKAQC--MFFKDKTMLCPMH 3066
Cdd:cd15669     79 AVKGCRRSFHFPCGLENGCvtQFFGEYRSFCWEH 112
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
379-800 2.51e-11

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: 70.18  E-value: 2.51e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  379 QSQNSQPPSPQMFSPGSShsrPPSPVDPYAKMVGTPRPPPGGHSFPrrnsvtpvencvplssvprpihmnetsatrpspa 458
Cdd:pfam03154  165 QILQTQPPVLQAQSGAAS---PPSPPPPGTTQAATAGPTPSAPSVP---------------------------------- 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  459 rdlcassmtnsdPYAKPPDTPRPMMTDQFSKPFSLPRSpviseqstkgplttgtsdhftkpsprTDAFQRQRLPDPYagP 538
Cdd:pfam03154  208 ------------PQGSPATSQPPNQTQSTAAPHTLIQQ--------------------------TPTLHPQRLPSPH--P 247
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  539 SLTPAPLGNGPFKTPLHPPPSQDPYGSVSQTSRRLSVDPYERP-ALTPRPVDNFSH-SQSNDPYSHPPLTPHPAMTESFT 616
Cdd:pfam03154  248 PLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQhPVPPQPFPLTPQsSQSQVPPGPSPAAPGQSQQRIHT 327
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  617 HASRAFPQPGTISRSASQDP-------YSQPPGTPRP-LIDSYSQTSGTARSNPDPYSQPPGTPRPNTIDPYS----QQP 684
Cdd:pfam03154  328 PPSQSQLQSQQPPREQPLPPaplsmphIKPPPTTPIPqLPNPQSHKHPPHLSGPSPFQMNSNLPPPPALKPLSslstHHP 407
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  685 PTPRPSPQTDMFVSS----------VANQRHTDPYTHHLGPPRPGISVPYSQPPAVPRPRTSEGFTR--PSSARPALMPN 752
Cdd:pfam03154  408 PSAHPPPLQLMPQSQqlppppaqppVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPitPPSGPPTSTSS 487
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  753 QDPFLQAAQNRVPGLPGPLI--------------RPPDTCSQTPRPPGPGR--------IDTFTHASSSA 800
Cdd:pfam03154  488 AMPGIQPPSSASVSSSGPVPaavscplppvqikeEALDEAEEPESPPPPPRspspeptvVNTPSHASQSA 557
PHA03247 PHA03247
large tegument protein UL36; Provisional
641-1248 5.57e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 69.20  E-value: 5.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  641 PGTPRPLIDSYSQTSGTARSNPDPYSQPPgtPRPNTIDPYSQQPPTPRPSPQTDMFV-----------SSVANQRHTDPy 709
Cdd:PHA03247  2475 PGAPVYRRPAEARFPFAAGAAPDPGGGGP--PDPDAPPAPSRLAPAILPDEPVGEPVhprmltwirglEELASDDAGDP- 2551
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  710 THHLGPPRPGISVPYSQPPAVPRPRTSEGFTRPSSARPALMPnqdpflQAAQNRVPGlpGPLIRPPDTCSQTPRPPGPgr 789
Cdd:PHA03247  2552 PPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPP------QSARPRAPV--DDRGDPRGPAPPSPLPPDT-- 2621
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  790 idtfthasssavrDPYDQPPVTPRPH-SESFGTSQVVHDLVDRPVPGSEGNfSTSSNLPVSSQGQQFSSVSQLPGPVPTS 868
Cdd:PHA03247  2622 -------------HAPDPPPPSPSPAaNEPDPHPPPTVPPPERPRDDPAPG-RVSRPRRARRLGRAAQASSPPQRPRRRA 2687
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  869 GGTDTQNTVNMSQA-DTEKLRQRQKLREIILQQQQQKKIASRQEKGPQDTAVVPHPVPLPHWQPESINQAFTRPPPPYPG 947
Cdd:PHA03247  2688 ARPTVGSLTSLADPpPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPP 2767
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  948 STRSPVIPPLGPRyavfpkdQRGPYPPEVAGMGMRPHGFRFGFPGAGHGPMPSQDRFHVPQQIQGSGIPPhirrPMSMem 1027
Cdd:PHA03247  2768 APAPPAAPAAGPP-------RRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP----PTSA-- 2834
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 1028 prpsnnpplnnpvgLPQHFPPQGLPVQQHNILGQAFielrhrAPDGR-SRLPFAASPSSVIESPSHPRHGNF----LPRP 1102
Cdd:PHA03247  2835 --------------QPTAPPPPPGPPPPSLPLGGSV------APGGDvRRRPPSRSPAAKPAAPARPPVRRLarpaVSRS 2894
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 1103 DFPGPRHTDPIRQPSQCLSNQLPVHPNLEQVPPSQQEQGHPAHQSSIVMRP------------------LNHPLSGEFS- 1163
Cdd:PHA03247  2895 TESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPttdpagagepsgavpqpwLGALVPGRVAv 2974
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 1164 ------------EAPLSTSTPAETSPDNLEIAGQSSAGLEEKLDSDDPSVKE-LDVKDlegvevkDLDDEDLENLNL-DT 1229
Cdd:PHA03247  2975 prfrvpqpapsrEAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQtLWPPD-------DTEDSDADSLFDsDS 3047
                          650
                   ....*....|....*....
gi 1907162496 1230 EDGKGDDLDTLDNlETNDP 1248
Cdd:PHA03247  3048 ERSDLEALDPLPP-EPHDP 3065
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
3342-3446 8.19e-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: 62.01  E-value: 8.19e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3342 GLGLYAARDIEKhtmvieyiGTIIRNE------VANRKEKLYESQNRGVYMFRMdndhvidatltggpARYINHSCAPNC 3415
Cdd:cd20071     10 GRGLVATRDIEP--------GELILVEkplvsvPSNSFSLTDGLNEIGVGLFPL--------------ASLLNHSCDPNA 67
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1907162496 3416 VaevVTFERGHKIIISSNRRIQKGEELCYDY 3446
Cdd:cd20071     68 V---VVFDGNGTLRVRALRDIKAGEELTISY 95
SET_SpSET3-like cd19183
SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...
3343-3457 2.81e-10

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: 62.04  E-value: 2.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3343 LGLYAARDIEKHTMVIEYIGtiirnEVANRKEKLYESQNRgvY----------MFRMDNDHVIDATLTGGPARYINHSCA 3412
Cdd:cd19183     14 FGLFADRPIPAGDPIQELLG-----EIGLQSEYIADPENQ--YqilgapkphvFFHPQSPLYIDTRRSGSVARFIRRSCR 86
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1907162496 3413 PNCVAEVVTFERGH--KIIISSNRRIQKGEELCYDYKFDFEDDQHKI 3457
Cdd:cd19183     87 PNAELVTVASDSGSvlKFVLYASRDISPGEEITIGWDWDNPHPFRRF 133
ePHD_PHF11 cd15712
Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain ...
2985-3066 1.14e-09

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: 58.37  E-value: 1.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2985 DLWVHLNCALWSTEVYETQAGALINVELA---------LRRGLQMKCVFCHKTGATSGCHRFRCTNIYHFTCATKAQCMF 3055
Cdd:cd15712     20 NIAAHQNCLLYSSGFVESEEYNPLNLDRRfdvesvlneIKRGKRLKCNFCRKKGATVGCEERACRRSYHYFCALCDDAAI 99
                           90
                   ....*....|....*.
gi 1907162496 3056 FKDKT-----MLCPMH 3066
Cdd:cd15712    100 ETDEVrgiyrVFCQKH 115
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
299-778 1.69e-08

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 60.96  E-value: 1.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  299 SQHLLVAPGSD---TPSSGAQSPLTPQAGNGNVSPAQTFHKDLFSKHLPGTPASTPSDGVFVKPQPPPPpstpsripvqe 375
Cdd:PHA03307    46 DSAELAAVTVVagaAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSP----------- 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  376 slsqsqnsqPPSPQMFSPGSSHSRPPSPVDPYAKMVGTPRPPPGG--------HSFPRRNSVTPVENCVPLSSVPrpihm 447
Cdd:PHA03307   115 ---------DPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAAsppaagasPAAVASDAASSRQAALPLSSPE----- 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  448 nETSATRPSPArdlcASSMTNSDPYAKPPDTPRPMMTDQFSKPFSLPRSPviseQSTKGPLTTGTSDHFTKPSPRTDAFQ 527
Cdd:PHA03307   181 -ETARAPSSPP----AEPPPSTPPAAASPRPPRRSSPISASASSPAPAPG----RSAADDAGASSSDSSSSESSGCGWGP 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  528 RQRLPDPYAGPSLTPAPLGNGpfKTPLHPPPSQDPYGSVSQTSRRlsvdpyerpalTPRPvdnfshsQSNDPYSHPPLTP 607
Cdd:PHA03307   252 ENECPLPRPAPITLPTRIWEA--SGWNGPSSRPGPASSSSSPRER-----------SPSP-------SPSSPGSGPAPSS 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  608 HPAMtesfthASRAFPQPGTISRSASQDPYSQPPGTPRPLIDSYSQTSGTARSNPDPySQPPGTPRPNTIDPYSQQPPTP 687
Cdd:PHA03307   312 PRAS------SSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADP-SSPRKRPRPSRAPSSPAASAGR 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  688 RPSPQTDMFVSSVANQRHTdpythhlGPPRPGisvpySQPPAVPrPRTSEGFTRPSSARPALMPNQDPFlqaaqnrvPGL 767
Cdd:PHA03307   385 PTRRRARAAVAGRARRRDA-------TGRFPA-----GRPRPSP-LDAGAASGAFYARYPLLTPSGEPW--------PGS 443
                          490
                   ....*....|.
gi 1907162496  768 PGPlirPPDTC 778
Cdd:PHA03307   444 PPP---PPGRV 451
SET_Suv4-20-like cd10524
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
3329-3468 6.40e-08

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: 54.21  E-value: 6.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3329 WKSNVYLARSRiQGLGLYAARDIEKHTMVIEYIGTIIRNEVAnrkEKLYESQNRG----VYMFRMDNDHVIDatltgGPA 3404
Cdd:cd10524      7 CPCNRYSLENH-YGAKIIATKPIKKGEKIHELCGCIAELSEE---EEALLRPGGNdfsvMYSSRKKCSQLWL-----GPA 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907162496 3405 RYINHSCAPNCvaEVVTFERGhKIIISSNRRIQKGEELCYDYKFDFEDDQHkipCHCGAVNCRK 3468
Cdd:cd10524     78 AFINHDCRPNC--KFVPTGKS-TACVKVLRDIEPGEEITVYYGDNYFGENN---EECECETCER 135
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
305-692 6.90e-08

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: 58.63  E-value: 6.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  305 APGSDTPSSGAQ-SPLTPQAGNGNVSPA----------QTFHKDLFSKHLPGTPASTPSdgvfvkpqppPPPSTPSRIPV 373
Cdd:pfam03154  198 GPTPSAPSVPPQgSPATSQPPNQTQSTAaphtliqqtpTLHPQRLPSPHPPLQPMTQPP----------PPSQVSPQPLP 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  374 QESLsqsQNSQPPSPQMFSPGSSHSRPPSPVDPYakmvgtPRPPPGGHSfprrnsvtpveNCVPLSSVPRPIHMNETSAT 453
Cdd:pfam03154  268 QPSL---HGQMPPMPHSLQTGPSHMQHPVPPQPF------PLTPQSSQS-----------QVPPGPSPAAPGQSQQRIHT 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  454 RPSpardlcASSMTNSDPYAKPPDTPRPMMTDQFSKPFSLPRSPVISEQSTKGPLTTGTSDHFTKPS--PRTDAFQRQRL 531
Cdd:pfam03154  328 PPS------QSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSnlPPPPALKPLSS 401
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  532 PDPYAGPSLTPAPLGNGPFKTPLHPPPSQDPYGSVSQTsrrlsvdpyerpaLTPRPVDNFSHSQSNDPYSHPPLTPHPAM 611
Cdd:pfam03154  402 LSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQS-------------LPPPAASHPPTSGLHQVPSQSPFPQHPFV 468
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  612 TESfthASRAFPQPGTISRSASQDPYSQPPGTPRPlidSYSQTSGTARSNPDPYSQPPGTPRPNTIDPYSQQPPTPRPSP 691
Cdd:pfam03154  469 PGG---PPPITPPSGPPTSTSSAMPGIQPPSSASV---SSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSP 542

                   .
gi 1907162496  692 Q 692
Cdd:pfam03154  543 E 543
PHA03247 PHA03247
large tegument protein UL36; Provisional
304-641 9.84e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.41  E-value: 9.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  304 VAPGSDTPssgaqsPLTPQAGNGNVSPAQtfhkdlfskhlPGTPASTPSDGVFVKPQPPPPPSTPSRIPVQESLSQSQNS 383
Cdd:PHA03247  2749 ATPGGPAR------PARPPTTAGPPAPAP-----------PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAV 2811
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  384 QPPSPQMfspgSSHSRPPSPVDPYAKMVGTPRPPPGGhsfPRRNSVTPVENCVPLSSV-----PRPIHMNETSATRPsPA 458
Cdd:PHA03247  2812 LAPAAAL----PPAASPAGPLPPPTSAQPTAPPPPPG---PPPPSLPLGGSVAPGGDVrrrppSRSPAAKPAAPARP-PV 2883
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  459 RDLCASSMTNS-DPYAKPPDTPRPMMTDQFSKPFSLPRSPVISEQSTKGPLTTGTSDHFTKPSPRTDAFQRQR--LPDPY 535
Cdd:PHA03247  2884 RRLARPAVSRStESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSgaVPQPW 2963
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  536 AGP----------SLTPAPLGNGPFKTPLHPPPSQDPYGSVSQ--TSRRLSVDPYERPA---LTPRPVDN---------- 590
Cdd:PHA03247  2964 LGAlvpgrvavprFRVPQPAPSREAPASSTPPLTGHSLSRVSSwaSSLALHEETDPPPVslkQTLWPPDDtedsdadslf 3043
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907162496  591 FSHSQSNDPYSHPPLTPHPamTESFTHAsrafPQPGTISRSASQDPYSQ--PP 641
Cdd:PHA03247  3044 DSDSERSDLEALDPLPPEP--HDPFAHE----PDPATPEAGARESPSSQfgPP 3090
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
613-956 1.24e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 58.26  E-value: 1.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  613 ESFTHASRAFPQPGTISRSASQDPYSQPPG----TPRPLIDSYSQTSGTARSNPDPYSQPPGTPRPNTIDPYSQQPPTPR 688
Cdd:PHA03307    12 EAAAEGGEFFPRPPATPGDAADDLLSGSQGqlvsDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWS 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  689 PSPQTdmfVSSVANQRHTDPYTHHLGPPRPGISVPYSQPP-----AVPRPRTSEGFTRPSSARPALMPNQDPFLQAAQNR 763
Cdd:PHA03307    92 LSTLA---PASPAREGSPTPPGPSSPDPPPPTPPPASPPPspapdLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAAS 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  764 VPGLPGPLIRPPDT--CSQTPRPPGPGRIDTFTHASSSAVRDPYDQPPV---TPRP----------------HSESFGTS 822
Cdd:PHA03307   169 SRQAALPLSSPEETarAPSSPPAEPPPSTPPAAASPRPPRRSSPISASAsspAPAPgrsaaddagasssdssSSESSGCG 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  823 QVVHDLVDRPVP-----------GSEGNFSTSSNLPVSSqgqqfSSVSQLPGPVPTSGGTDTQNTVNMSQADTEKLRQRq 891
Cdd:PHA03307   249 WGPENECPLPRPapitlptriweASGWNGPSSRPGPASS-----SSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSR- 322
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907162496  892 klreiilqqqqQKKIASRQEKGPQDTAVVPHPVPLPHWQPESinqafTRPPPPYPGSTRSPVIPP 956
Cdd:PHA03307   323 -----------ESSSSSTSSSSESSRGAAVSPGPSPSRSPSP-----SRPPPPADPSSPRKRPRP 371
GGN pfam15685
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ...
385-872 1.76e-07

Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the maturation of sperm and is expressed virtually only in the testis. It is found to be associated with the intracellular membrane, binds with GGNBP1 and may be involved in vesicular trafficking.


Pssm-ID: 434857 [Multi-domain]  Cd Length: 668  Bit Score: 57.08  E-value: 1.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  385 PPSPQMF-SPGSSHSRPPSPVDP-----YAKMVGTPRPPPGGhsfprrnsvtpvencvplSSVPRPIHMNETSATRPSPA 458
Cdd:pfam15685   64 PPEPQASpSPLPLTLELPLPVTPppeeaAAAAVSTAPPPAVG------------------SLLPAPSKWRKPTGTAVARI 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  459 RDLC-ASSMTNSDPYAKPPDTprPMMTDQFSKPFSLPRSPViseqstkGPLTTGTSDHFTKPSPRTDAFQRQRLPDPYAG 537
Cdd:pfam15685  126 RGLLeASHRGQGDPLSLRPLL--PLLPRQLIEKDPAPGAPA-------PPPPTPLEPRKPPPLPPSDRQPPNRGITPALA 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  538 PSLTPaplgngpfktplhPPPSQDPYGSVSQTSRrlSVDPYERPALTPRPVDNFSHSQSNDPY-------SHPPLTPHPA 610
Cdd:pfam15685  197 TSATS-------------PTDSQAKHIAEGKTAG--GACGGAPPQAGEGEMARFAASESGLSLlckvtfkSAAPLCPAAA 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  611 MTESFTHASRAFPQPGTISRSASQDPYSQ-------PPGTPRPL--IDSYSQTSGTARSNPDPYSQPPGTPRPNTidpYS 681
Cdd:pfam15685  262 SGPLAAKASLGGGGGGGLFAASGAISCAEvlkqgplAPGAARPLgeVPRAALETEGGEGDGEGCSGGPAAPASHA---RA 338
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  682 QQPPT----PRPSPQTDMFVSSVANQRH--TDPYTHHLGPPR---PGISVPYSQPPavPRPRTSEGFTRPSSARPALMPN 752
Cdd:pfam15685  339 LPPPAyttfPGSKPKFDWVSPPDGPERHfrFNGAGGGIGAPRrraAALSGPWGSPP--PPPGKAHPIPGPRRPAPALLAP 416
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  753 QDPFLQAAQNRVPGLPGplirPPDTCSQTPRPPGPGRIDTFTHASSSAVRDPYDQPPVTP--RPHSESFGTSQVVHDLVD 830
Cdd:pfam15685  417 PMFIFPAPTNGEPVRPG----PPAPQALLPRPPPPTPPATPPPVPPPIPQLPALQPMPLAaaRPPTPRPCPGHGESALAP 492
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1907162496  831 RPVPgsegnfSTSSNLPVSSQGQQFSSVSQLPGPVPTSGGTD 872
Cdd:pfam15685  493 APTA------PLPPALAADQAPAPALAAAPAPSPAPAPATAD 528
HMG-box_SF cd00084
high mobility group (HMG)-box domain superfamily; The High Mobility Group (HMG)-box is found ...
157-204 1.40e-06

high mobility group (HMG)-box domain superfamily; The High Mobility Group (HMG)-box is found in a variety of eukaryotic chromosomal proteins and transcription factors. HMGs bind to the minor groove of DNA and have been classified by DNA binding preferences. Two phylogenetically distinct groups of Class I proteins bind DNA in a sequence specific fashion and contain a single HMG box. One group (SOX-TCF) includes transcription factors, TCF-1, -3, -4, and also SRY and LEF-1, which bind four-way DNA junctions and duplex DNA targets. The second group (MATA) includes fungal mating type gene products MC, MATA1 and Ste11. Class II and III proteins (HMGB-UBF) bind DNA in a non-sequence specific fashion and contain two or more tandem HMG boxes. Class II members include non-histone chromosomal proteins, HMG1 and HMG2, which bind to bent or distorted DNA such as four-way DNA junctions, synthetic DNA cruciforms, kinked cisplatin-modified DNA, DNA bulges, cross-overs in supercoiled DNA, and can cause looping of linear DNA. Class III members include nucleolar and mitochondrial transcription factors, UBF and mtTF1, which bind four-way DNA junctions.


Pssm-ID: 438789 [Multi-domain]  Cd Length: 59  Bit Score: 47.90  E-value: 1.40e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907162496  157 LYTNINFPNLKEEFPDWTTR--VKQIAKLWRKASSQERAPYVQKARDNRA 204
Cdd:cd00084      8 LFSKEKRPKLKKENPDLSFTeiSKLLGERWKELSEEEKQPYEEKAKEDKE 57
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
3333-3452 2.47e-06

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: 48.79  E-value: 2.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3333 VYLARSRIQGLGLYAARDIEKHTmVIEYIGTIIrneVANRKEKLYESQNRGVYMFRMDNDHVidATLTGGPARYiNHSCA 3412
Cdd:cd10540      2 LEVKPSTLKGRGVFATRPIKKGE-VIEEAPVIV---LPKEEYQHLCKTVLDHYVFSWGDGCL--ALALGYGSMF-NHSYT 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1907162496 3413 PNcvAEVVTFERGHKIIISSNRRIQKGEELCYDYKFDFED 3452
Cdd:cd10540     75 PN--AEYEIDFENQTIVFYALRDIEAGEELTINYGDDLWD 112
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
3357-3446 3.53e-06

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: 51.25  E-value: 3.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3357 VIEYIGTIIRNEVANRKEKlyesqnRGVYMFRMDN-------------------------------DHVIDATLTGGPAR 3405
Cdd:cd10545    112 ICEYVGELLDTSEADTRSG------NDDYLFDIDNrqtnrgwdggqrldvgmsdgerssaedeessEFTIDAGSFGNVAR 185
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1907162496 3406 YINHSCAPNCVAEVVTFE----RGHKIIISSNRRIQKGEELCYDY 3446
Cdd:cd10545    186 FINHSCSPNLFVQCVLYDhndlRLPRVMLFAADNIPPLQELTYDY 230
ePHD_JMJD2 cd15675
Extended PHD finger found in Jumonji domain-containing protein 2 (JMJD2) family of histone ...
2962-3055 5.23e-06

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: 47.74  E-value: 5.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2962 CCFCHEEGDGL---TDGparllnldldLWVHLNCALWSTEVY--ETQAGALINV-ELALRRgLQMKCVFCHK-------T 3028
Cdd:cd15675      1 CCLCCLRGGALkptTDG----------RWAHVVCAIAIPEVRfsNVPERGPIDIsKIPPAR-LKLKCIYCSKitksmshM 69
                           90       100
                   ....*....|....*....|....*..
gi 1907162496 3029 GATSGCHRFRCTNIYHFTCATKAQCMF 3055
Cdd:cd15675     70 GACIQCSTGKCTTSFHVTCAHAAGVQM 96
ePHD1_PHF6 cd15710
Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
2989-3052 5.36e-06

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: 48.03  E-value: 5.36e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907162496 2989 HLNCALWSTEVYETQAG-------ALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTNIYHFTCA--TKAQ 3052
Cdd:cd15710     26 HHKCMLFSSALVSSHSDsenlggfSIEDVQKEIKRGTKLMCSLCHCPGATIGCDVKTCHRTYHYYCAlhDKAQ 98
SET_SETD5 cd19181
SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...
3345-3466 5.69e-06

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: 48.85  E-value: 5.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3345 LYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRMDN--DHVIDATLTGGPARYINHSCAPNCVAEVVTF 3422
Cdd:cd19181     21 LRAARDLALDTLIIEYRGKVMLRQQFEVNGHFFKRPYPFVLFYSKFNgvEMCVDARTFGNDARFIRRSCTPNAEVRHMIA 100
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1907162496 3423 ERGHKIIISSNRRIQKGEELCYDYKFDFEDDQHKIPCHC--GAVNC 3466
Cdd:cd19181    101 DGMIHLCIYAVAAIAKDAEVTIAFDYEYSNCNYKVDCAChkGNRNC 146
PHA03377 PHA03377
EBNA-3C; Provisional
306-688 1.06e-05

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 51.59  E-value: 1.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  306 PGSDTPSSGAQSPLTPQAGNGNVSPAQTFHKDLfSKHLPGTPASTPSDgvfvKPQPPPPPSTPSRIPVQESLSQSQNSQP 385
Cdd:PHA03377   568 PVMAPPSTGPRVMATPSTGPRDMAPPSTGPRQQ-AKCKDGPPASGPHE----KQPPSSAPRDMAPSVVRMFLRERLLEQS 642
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  386 --PSPQMF------SPGSSHSRPPSPVDPYAKMVGTPRPP--PGGHSFPRRNSVTP----VENCVPLSSVPRPIHMNETS 451
Cdd:PHA03377   643 tgPKPKSFwemragRDGSGIQQEPSSRRQPATQSTPPRPSwlPSVFVLPSVDAGRAqpseESHLSSMSPTQPISHEEQPR 722
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  452 ATRPSPARDLCASSMTNSDPYAKPPDTPR--PMMTDQFSKPFSLPRSPVISEQSTKGPLTTGTSDH----FTKPSPRTDA 525
Cdd:PHA03377   723 YEDPDDPLDLSLHPDQAPPPSHQAPYSGHeePQAQQAPYPGYWEPRPPQAPYLGYQEPQAQGVQVSsypgYAGPWGLRAQ 802
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  526 FQRQRLP------DPYAGPSLTPAPlgngpfKTPLHPPPSQDPYGSVSQTSrrlsvdpyerpaltprpVDNFSHSQSNDP 599
Cdd:PHA03377   803 HPRYRHSwaywsqYPGHGHPQGPWA------PRPPHLPPQWDGSAGHGQDQ-----------------VSQFPHLQSETG 859
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  600 YSHPPLTPHPAMTESFTHASRAFPQPGTISRSASQDPY-SQPPGTPRPLIDSYS---QTSGTARSN---PDPYSQPPGTP 672
Cdd:PHA03377   860 PPRLQLSQVPQLPYSQTLVSSSAPSWSSPQPRAPIRPIpTRFPPPPMPLQDSMAvgcDSSGTACPSmpfASDYSQGAFTP 939
                          410
                   ....*....|....*.
gi 1907162496  673 rpntIDPYSQQPPTPR 688
Cdd:PHA03377   940 ----LDINAQTPKRPR 951
HMG smart00398
high mobility group;
154-207 1.06e-05

high mobility group;


Pssm-ID: 197700 [Multi-domain]  Cd Length: 70  Bit Score: 45.77  E-value: 1.06e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162496   154 APVLYTNINFPNLKEEFPDWTT--RVKQIAKLWRKASSQERAPYVQKARDNRAALR 207
Cdd:smart00398    8 AFMLFSQENRAKIKAENPDLSNaeISKKLGERWKLLSEEEKAPYEEKAKKDKERYE 63
ePHD_JMJD2A cd15713
Extended PHD finger (ePHD) found in Jumonji domain-containing protein 2A (JMJD2A); The ...
2962-3058 1.24e-05

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: 46.89  E-value: 1.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2962 CCFCHEEGDGLTDGparllnlDLDLWVHLNCALWSTEVYETQAGALINVELA---LRRgLQMKCVFCHK-----TGATSG 3033
Cdd:cd15713      1 CCLCSLRGGALQRA-------NDDKWVHVMCAVAVLEARFVNIAERSPVDVSkipLQR-FKLKCIFCKKrrkrtAGCCVQ 72
                           90       100
                   ....*....|....*....|....*
gi 1907162496 3034 CHRFRCTNIYHFTCATKAQCMFFKD 3058
Cdd:cd15713     73 CSHGRCPTSFHASCAQAAGVMMQPD 97
HMG_box pfam00505
HMG (high mobility group) box;
156-207 1.33e-05

HMG (high mobility group) box;


Pssm-ID: 459837 [Multi-domain]  Cd Length: 68  Bit Score: 45.29  E-value: 1.33e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907162496  156 VLYTNINFPNLKEEFPDWTTR--VKQIAKLWRKASSQERAPYVQKARDNRAALR 207
Cdd:pfam00505    9 FLFSKEQRAKLKAENPGLKNAeiSKILGEKWKALSEEEKKPYEEKAEKEKARYE 62
SET_SETD7 cd10530
SET domain found in SET domain-containing protein 7 (SETD7) and similar proteins; SETD7 (EC 2. ...
3333-3446 1.72e-05

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: 46.91  E-value: 1.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3333 VYLARSRIQ--GLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESqnrgvYMFRMDNDHVID------------AT 3398
Cdd:cd10530      9 VYVAESLIPsaGEGLFAKVAVGPNTVMSFYNGVRITHQEVDSRDWSLNG-----NTISLDEETVIDvpepynsvskycAS 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1907162496 3399 LtGGPAryiNHSCAPNCVAEVVTFER-GHKIIISSNRRIQKGEELCYDY 3446
Cdd:cd10530     84 L-GHKA---NHSFTPNCIYDPFVHPRfGPIKCIRTLRAVEAGEELTVAY 128
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
585-814 1.84e-05

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: 50.92  E-value: 1.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  585 PRPVDNFSHSQSNDPYS------------HPPLTPHPAMTESFTHASRAFPQPGTISRSASQDP-YSQPPGTPRPLIDSY 651
Cdd:pfam03154  149 PSPQDNESDSDSSAQQQilqtqppvlqaqSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPaTSQPPNQTQSTAAPH 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  652 SQTSGTarsnpdPYSQPPGTPRPNT-------IDPYSQQPPTPRPSPQTDMFVSSVANQRHTDP-YTHHLGPPRPGISVP 723
Cdd:pfam03154  229 TLIQQT------PTLHPQRLPSPHPplqpmtqPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPsHMQHPVPPQPFPLTP 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  724 YSQPPAVPrPRTSEGFTRPSSARPALMPNQDPFLQAAQNRVPGLPG-----PLIRPPDTcsqTPRPPGPGRiDTFTHASS 798
Cdd:pfam03154  303 QSSQSQVP-PGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPaplsmPHIKPPPT---TPIPQLPNP-QSHKHPPH 377
                          250
                   ....*....|....*.
gi 1907162496  799 SAVRDPYDQPPVTPRP 814
Cdd:pfam03154  378 LSGPSPFQMNSNLPPP 393
PHA03378 PHA03378
EBNA-3B; Provisional
496-883 2.49e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 50.45  E-value: 2.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  496 SPVISEQSTKGPLTTGTSDHFTKPSPRTDAFQRQRLPDPYAGPSLTPAPLGNGPFKTPLHPPPSQDPYGSVSQTSRRLSV 575
Cdd:PHA03378   579 SPTTSQLASSAPSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFPTPHQPPQVE 658
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  576 DPYERPALTPRPVDNFSHSQSNDPYSH-----------PPLTPHPAMTESFTHASRAFPQ--PGTISRSASQDPYSQPPG 642
Cdd:PHA03378   659 ITPYKPTWTQIGHIPYQPSPTGANTMLpiqwapgtmqpPPRAPTPMRPPAAPPGRAQRPAaaTGRARPPAAAPGRARPPA 738
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  643 TPRPLIDSYSQTSGTAR---SNPDPYSQPPGTPRPNTIDPYSQQPPTPRPSPQTdmfVSSVANQRHTDPYTHHLGPPRPg 719
Cdd:PHA03378   739 AAPGRARPPAAAPGRARppaAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRG---APTPQPPPQAGPTSMQLMPRAA- 814
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  720 isvPYSQPPA--VPRPRTSEGFT--RPSSARPALMPNQDPflqAAQNRVPG-------LPGPLIRPP-DTCSQTPRPPGP 787
Cdd:PHA03378   815 ---PGQQGPTkqILRQLLTGGVKrgRPSLKKPAALERQAA---AGPTPSPGsgtsdkiVQAPVFYPPvLQPIQVMRQLGS 888
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  788 GRIDTFTHASSSAVRDPYDQPPVTPRPHSESFGTSQVVHD-LVDRPVPGSEGNFSTSSNLPVSSQGQQfssvsqlpgPVP 866
Cdd:PHA03378   889 VRAAAASTVTQAPTEYTGERRGVGPMHPTDIPPSKRAKTDaYVESQPPHGGQSHSFSVIWENVSQGQQ---------QTL 959
                          410
                   ....*....|....*..
gi 1907162496  867 TSGGTDTQNTVNMSQAD 883
Cdd:PHA03378   960 ECGGTTKQERAMLGTGD 976
ePHD2_PHF6 cd15711
Extended PHD finger 2 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
2962-3058 2.66e-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: 46.23  E-value: 2.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2962 CCFCHE-EGDGLTDGPARLLNLDlDLWVHLNCALWST---EVYETQAGALINVELA-----LRRGLQMKCVFCHKTGATS 3032
Cdd:cd15711      1 CGFCHAgEEENETRGKLHIFNAK-KAAAHYKCMLFSSgtvQLTTTSRAEFGDFDIKtviqeIKRGKRMKCTLCSQLGATI 79
                           90       100
                   ....*....|....*....|....*.
gi 1907162496 3033 GCHRFRCTNIYHFTCATKAQCMFFKD 3058
Cdd:cd15711     80 GCEIKACVKTYHYHCGVQDKAKYIEN 105
dnaA PRK14086
chromosomal replication initiator protein DnaA;
533-763 3.01e-05

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 49.82  E-value: 3.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  533 DPYAGPSLTPAPlgngpfktplHPPPSQDPYGSvsqTSRRLSVDPYERPALTPRPvdnfshsQSNDPYSHPPlTPHPAMT 612
Cdd:PRK14086    89 DPSAGEPAPPPP----------HARRTSEPELP---RPGRRPYEGYGGPRADDRP-------PGLPRQDQLP-TARPAYP 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  613 eSFTHASRAFPQPGT-ISRSASQDPYSQPPGTPRPLIDSYS-------QTSGTARSNPDPYSQPPGTPRPNTIDPYSQQP 684
Cdd:PRK14086   148 -AYQQRPEPGAWPRAaDDYGWQQQRLGFPPRAPYASPASYApeqerdrEPYDAGRPEYDQRRRDYDHPRPDWDRPRRDRT 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  685 PTPRPSPQTdmfvssvanqrHTDPYTHHLGPPRPGISVPYSQPPAvPRPRTSEGFTRPSSARPALMPNQ----DPFLQAA 760
Cdd:PRK14086   227 DRPEPPPGA-----------GHVHRGGPGPPERDDAPVVPIRPSA-PGPLAAQPAPAPGPGEPTARLNPkytfDTFVIGA 294

                   ...
gi 1907162496  761 QNR 763
Cdd:PRK14086   295 SNR 297
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
532-773 3.32e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 49.87  E-value: 3.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  532 PDPYAGPSLTP------APLGNGPFKTPlhPPPSQDPYGSVSQTSRRLSVDPYERPALTPRPVDNFSHSQSNDPYSHPPL 605
Cdd:PRK12323   347 PDEYAGFTMTLlrmlafRPGQSGGGAGP--ATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPA 424
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  606 TPHPAMTESFTHASRAFPQPGTISRSASQdPYSQPPGTPRPLIDSysqtsgtARSNPDPYSQPP--------GTPRPNTI 677
Cdd:PRK12323   425 RRSPAPEALAAARQASARGPGGAPAPAPA-PAAAPAAAARPAAAG-------PRPVAAAAAAAParaapaaaPAPADDDP 496
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  678 DPYSQQPPT-PRPSP-QTDMFVSSVANQRHTDPYTHHLGPPRPGISVPYSQPPAVPRPRTSEGF---TRPSSARPALMPN 752
Cdd:PRK12323   497 PPWEELPPEfASPAPaQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVvapRPPRASASGLPDM 576
                          250       260
                   ....*....|....*....|....
gi 1907162496  753 QD---PFLqAAQNRVPGLPGPLIR 773
Cdd:PRK12323   577 FDgdwPAL-AARLPVRGLAQQLAR 599
ePHD_JMJD2B cd15714
Extended PHD finger found in Jumonji domain-containing protein 2B (JMJD2B); The extended plant ...
2962-3051 4.46e-05

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: 45.31  E-value: 4.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2962 CCFCHEEGDGL---TDgparllnldlDLWVHLNCALWSTEVYETQA--GALINVELALRRGLQMKCVFCHKT-----GAT 3031
Cdd:cd15714      1 CCLCNLRGGALqmtTD----------ERWVHVICAIAVPEARFLNVieRHPVDVSAIPEQRWKLKCVYCRKRmkkvsGAC 70
                           90       100
                   ....*....|....*....|
gi 1907162496 3032 SGCHRFRCTNIYHFTCATKA 3051
Cdd:cd15714     71 IQCSYDHCSTSFHVTCAHAA 90
HMG-box_BHMG1 cd21977
high mobility group (HMG)-box found in basic helix-loop-helix and HMG box domain-containing ...
156-210 5.76e-05

high mobility group (HMG)-box found in basic helix-loop-helix and HMG box domain-containing protein 1 (BHMG1) and similar proteins; BHMG1 is an uncharacterized HMG-box containing protein that contains a degenerate basic motif not likely to bind DNA.


Pssm-ID: 438793 [Multi-domain]  Cd Length: 66  Bit Score: 43.46  E-value: 5.76e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907162496  156 VLYTNINFPNLKEEFPDWTTRV--KQIAKLWRKASSQERAPYVQKARD-NRAALRINK 210
Cdd:cd21977      9 IMFCRLNRKNYIDKHPGLASTEltKELGQLWRELSAEEKKPYCVRARElSQLHNRKVK 66
PHA03377 PHA03377
EBNA-3C; Provisional
577-1018 7.69e-05

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 48.90  E-value: 7.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  577 PYERPALTP---RPVDNFSHSQSNDPYSHPPLTP--HPAMTESFTHASRAFPQPGTISRSASQDPYSQPPGTPRPLIDSY 651
Cdd:PHA03377   391 PYIDPNMEPvqqRPVMFVSRVPWRKPRTLPWPTPktHPVKRTLVKTSGRSDEAEQAQSTPERPGPSDQPSVPVEPAHLTP 470
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  652 SQTSGTArsnpdpYSQPPGTPRPNTIDPYSQ--------------------------------QPPTPRPSPQTDMFVSS 699
Cdd:PHA03377   471 VEHTTVI------LHQPPQSPPTVAIKPAPPpsrrrrgacvvydddiievidvetteeeesvtQPAKPHRKVQDGFQRSG 544
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  700 VANQRHTDPYTHHLGPPRPGISVPYSQPPAVPRPRTSEGFTRPSSARPalmPNQDPFLQAAQNRVPGLPGPLIRPPDtcS 779
Cdd:PHA03377   545 RRQKRATPPKVSPSDRGPPKASPPVMAPPSTGPRVMATPSTGPRDMAP---PSTGPRQQAKCKDGPPASGPHEKQPP--S 619
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  780 QTPRPPGPGRIDTFThasssavRDPYDQPPVTPRPhsESFGTSQVVHDLVD-RPVPGSEGNFSTSSNLPVSSqgqQFSSV 858
Cdd:PHA03377   620 SAPRDMAPSVVRMFL-------RERLLEQSTGPKP--KSFWEMRAGRDGSGiQQEPSSRRQPATQSTPPRPS---WLPSV 687
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  859 SQLPGpVPTSGGTDTQNTVNMSQADTEKLRQRQKLReiilqqqqqkkiaSRQEKGPQDTAVVPHPVPLP-HWQPESINQA 937
Cdd:PHA03377   688 FVLPS-VDAGRAQPSEESHLSSMSPTQPISHEEQPR-------------YEDPDDPLDLSLHPDQAPPPsHQAPYSGHEE 753
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  938 FTRPPPPYPG--STRSPVIPPLGPRYAVFPKDQRGPYPPEVAGMGMRPHGFRF--------GFPGAGHGPMPSQDRF-HV 1006
Cdd:PHA03377   754 PQAQQAPYPGywEPRPPQAPYLGYQEPQAQGVQVSSYPGYAGPWGLRAQHPRYrhswaywsQYPGHGHPQGPWAPRPpHL 833
                          490
                   ....*....|..
gi 1907162496 1007 PQQIQGSGIPPH 1018
Cdd:PHA03377   834 PPQWDGSAGHGQ 845
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
594-818 7.81e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.83  E-value: 7.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  594 SQSNDPYSHPPLTPHPAmtesfthaSRAFPQPGTISRSASQDPYSQPPGTPrplidsYSQTSGTARSNPDPYSQPPGTPR 673
Cdd:PRK07764   606 SGPPEEAARPAAPAAPA--------APAAPAPAGAAAAPAEASAAPAPGVA------APEHHPKHVAVPDASDGGDGWPA 671
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  674 PNTIDPYSQQPPTPRPSPQtdmfvssVANQRHTDPYTHHLGPPRPGiSVPYSQPPAVPRPRTSEGFTRPSSARPALMPNQ 753
Cdd:PRK07764   672 KAGGAAPAAPPPAPAPAAP-------AAPAGAAPAQPAPAPAATPP-AGQADDPAAQPPQAAQGASAPSPAADDPVPLPP 743
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907162496  754 DPFLQAAQNRVPGLPGPlIRPPDTCSQTPRPPGPgridtfTHASSSAVRDPYDQPPVTPRPHSES 818
Cdd:PRK07764   744 EPDDPPDPAGAPAQPPP-PPAPAPAAAPAAAPPP------SPPSEEEEMAEDDAPSMDDEDRRDA 801
PostSET smart00508
Cysteine-rich motif following a subset of SET domains;
3455-3471 8.94e-05

Cysteine-rich motif following a subset of SET domains;


Pssm-ID: 214703  Cd Length: 17  Bit Score: 41.62  E-value: 8.94e-05
                            10
                    ....*....|....*..
gi 1907162496  3455 HKIPCHCGAVNCRKWMN 3471
Cdd:smart00508    1 KKQPCLCGAPNCRGFLG 17
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
3022-3066 1.14e-04

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: 42.20  E-value: 1.14e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1907162496  3022 CVFCHKTGATS---GCHRfrCTNIYHFTCATKAQCMFFKDKTMLCPMH 3066
Cdd:smart00249    2 CSVCGKPDDGGellQCDG--CDRWYHQTCLGPPLLEEEPDGKWYCPKC 47
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
556-748 1.20e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.06  E-value: 1.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  556 PPPSQDPYGSVSQTSRRLSVDPYERPALTPRPVDnfshsqsnDPYSHPPLTPHPAMTESFTHASRAFPQPGTISRSASQD 635
Cdd:PRK07764   590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAA--------PAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPD 661
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  636 PYSQPPGTPRPLID-----------SYSQTSGTARSNPDPYSQPPGTPRPntiDPYSQQPPTPRPSPQTDMFVSSVANQR 704
Cdd:PRK07764   662 ASDGGDGWPAKAGGaapaapppapaPAAPAAPAGAAPAQPAPAPAATPPA---GQADDPAAQPPQAAQGASAPSPAADDP 738
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1907162496  705 HTDPYTHHLgPPRPGISVPYSQPPAVPRPRTSEGFTRPSSARPA 748
Cdd:PRK07764   739 VPLPPEPDD-PPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSE 781
ePHD_JADE cd15671
Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended ...
2987-3050 1.30e-04

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: 43.97  E-value: 1.30e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162496 2987 WVHLNCALWSTEV-------YEtqagALINVELALRRGLQMKCVFCH-KTGATSGCHRFRCTNIYHFTCATK 3050
Cdd:cd15671     20 WVHVSCALWIPEVsigcpekME----PITKISHIPMSRWALVCVLCKeKTGACIQCSVKSCKTAFHVTCAFQ 87
ePHD_JMJD2C cd15715
Extended PHD finger found in Jumonji domain-containing protein 2C (JMJD2C); The extended plant ...
2962-3051 1.32e-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: 43.79  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2962 CCFCHEEGDGLTDGPArllnldlDLWVHLNCALWSTEVYETQAGALINVELA---LRRgLQMKCVFCHK-----TGATSG 3033
Cdd:cd15715      1 CCLCNLRGGALKQTSD-------DKWAHVMCAVALPEVRFINVVERTPIDISripLQR-LKLKCIFCRNrikrvSGACIQ 72
                           90
                   ....*....|....*...
gi 1907162496 3034 CHRFRCTNIYHFTCATKA 3051
Cdd:cd15715     73 CSYGRCPASFHVTCAHAA 90
SET_KMT2E cd19182
SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...
3345-3450 1.50e-04

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


Pssm-ID: 380959  Cd Length: 129  Bit Score: 44.11  E-value: 1.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 3345 LYAARDIEKHTMVIEYIGTIIRNEV--AN-----RKEK--LYESQNRGVYMfrmdndhVIDATLTGGPARYINHSCAPNC 3415
Cdd:cd19182     21 LKAAKDLPPDTLIIEYRGKFMLREQfeANgyffkRPYPfvLFYSKFHGLEM-------CVDARTFGNEARFIRRSCTPNA 93
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1907162496 3416 VAEVVTFERGHKIIISSNRRIQKGEELCYDYKFDF 3450
Cdd:cd19182     94 EVRHVIEDGTIHLYIYSIRSIPKGTEITIAFDFDY 128
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
3022-3066 1.93e-04

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) finger typically characterized as Cys4HisCys3, and a non-canonical extended PHD finger, characterized as Cys2HisCys5HisCys2His. Variations include the RAG2 PHD finger characterized by Cys3His2Cys2His and the PHD finger 5 found in nuclear receptor-binding SET domain-containing proteins characterized by Cys4HisCys2His. The PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. Single or multiple copies of PHD fingers have 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. The PHD finger domain SF is structurally similar to the RING and FYVE_like superfamilies.


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 41.53  E-value: 1.93e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1907162496 3022 CVFCHKTGATSG----CHRfrCTNIYHFTCATKAQCMFFKDKTMLCPMH 3066
Cdd:cd15489      2 CIVCGKGGDLGGellqCDG--CGKWFHADCLGPPLSSFVPNGKWICPVC 48
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
494-735 2.28e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 46.84  E-value: 2.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  494 PRSPVISEQSTKGPLTTGTSDHFTKPSPRTDAFQRQRLP---DPYAG-------PSLTPAPLGNGPFKTP----LHPPPS 559
Cdd:PLN03209   330 PKESDAADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPrplSPYTAyedlkppTSPIPTPPSSSPASSKsvdaVAKPAE 409
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  560 QDPYGSVSQTSRRLSVDPYERPALTPRPVDNFSHSQSNDPYSHPPLTPHPAMTESFTHASRAFPQPGTISRSASQDPYSQ 639
Cdd:PLN03209   410 PDVVPSPGSASNVPEVEPAQVEAKKTRPLSPYARYEDLKPPTSPSPTAPTGVSPSVSSTSSVPAVPDTAPATAATDAAAP 489
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  640 PPGTPRPLIDSYSQTSGTARSNPDPYSQPPGTPRPNTidpySQQPPTPRPSPQTdmfvSSVANQRHTDPythhlgPPRPg 719
Cdd:PLN03209   490 PPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSST----NEVVKVGNSAPPT----ALADEQHHAQP------KPRP- 554
                          250       260
                   ....*....|....*....|.
gi 1907162496  720 ISvPYS-----QPPAVPRPRT 735
Cdd:PLN03209   555 LS-PYTmyedlKPPTSPTPSP 574
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
309-752 2.52e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 46.99  E-value: 2.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  309 DTPSSGAQSPLTPQAGNGNVSPAQTFHKDLFSKHLP---GTPASTPSDGVFVKPQPPPPPSTPSRIPV-------QESLS 378
Cdd:PTZ00449   508 DEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPkegGKPGETKEGEVGKKPGPAKEHKPSKIPTLskkpefpKDPKH 587
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  379 QSQNSQPPSPQMFSPGSSHSRPPSPVDPYAKMVGTPRPPPGGHSFPRRnsvtPVencvplssvprpihmnetSATRP-SP 457
Cdd:PTZ00449   588 PKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKR----PP------------------PPQRPsSP 645
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  458 ARDLCASSMTNSdpyaKPPDTPRPMMTDQFSKPFSLPRSPVISEqsTKGPLTTGTSDHftkpspRTDAFQRQRLPDPYAG 537
Cdd:PTZ00449   646 ERPEGPKIIKSP----KPPKSPKPPFDPKFKEKFYDDYLDAAAK--SKETKTTVVLDE------SFESILKETLPETPGT 713
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  538 PSLTPAPLgngPFKTPLHPPPSQDPygsvsqtsrrlsvdPYERPALTPRPVDNFSHSQSNDPYSH--PPLTPHPAMT--- 612
Cdd:PTZ00449   714 PFTTPRPL---PPKLPRDEEFPFEP--------------IGDPDAEQPDDIEFFTPPEEERTFFHetPADTPLPDILaee 776
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  613 --ESFTHASRAFPQPgTISRSASQDPYS-QPPGT------PRPLIDSYSQTSGTARSNP-----DPYSQPPGTPRPNTID 678
Cdd:PTZ00449   777 fkEEDIHAETGEPDE-AMKRPDSPSEHEdKPPGDhpslpkKRHRLDGLALSTTDLESDAgriakDASGKIVKLKRSKSFD 855
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162496  679 PYSQQPPTPRPSPQTDMFVSSVANQRHTDPYTHhlgPP--RPGISVPYSQPPAVP-RPRTSEGFTRPSSARPALMPN 752
Cdd:PTZ00449   856 DLTTVEEAEEMGAEARKIVVDDDGTEADDEDTH---PPeeKHKSEVRRRRPPKKPsKPKKPSKPKKPKKPDSAFIPS 929
SET_SMYD4 cd10536
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
3407-3463 3.22e-04

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


Pssm-ID: 380934 [Multi-domain]  Cd Length: 218  Bit Score: 44.98  E-value: 3.22e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907162496 3407 INHSCAPNCvaeVVTFErGHKIIISSNRRIQKGEEL--CYDYKF---DFED------DQHKIPCHCGA 3463
Cdd:cd10536    154 LNHSCDPNT---IRSFY-GNTIVVRATRPIKKGEEItiCYGPHFsrmKRSErqrllkEQYFFDCSCEA 217
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
498-785 3.32e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 46.46  E-value: 3.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  498 VISEqsTKGPLTTgTSDHFTK-PSprtdafQRQRLPDPYAGPSLTPAPLGNGPFKTPLhPPPSQDPYGSVSQTSRRLSvd 576
Cdd:PLN03209   305 VIAE--TTAPLTP-MEELLAKiPS------QRVPPKESDAADGPKPVPTKPVTPEAPS-PPIEEEPPQPKAVVPRPLS-- 372
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  577 PYE-----RPALTPRPVdnfshsqsndPYSHPPLTPHPAMTESFTHASRAFPQPGTISRSASQDPYSQPPGTPRPLidsy 651
Cdd:PLN03209   373 PYTayedlKPPTSPIPT----------PPSSSPASSKSVDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPL---- 438
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  652 sqtsgtarsnpDPYS-----QPPGTPRPNTIDPY----------SQQPPTPRPSPQTDMFVSSVANQRHTDPYTHHLGPP 716
Cdd:PLN03209   439 -----------SPYAryedlKPPTSPSPTAPTGVspsvsstssvPAVPDTAPATAATDAAAPPPANMRPLSPYAVYDDLK 507
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907162496  717 RPGISVPYSQPPAVPRPRTSEGFTRPSSARP-ALMPNQDpflQAAQNRVPGLPGPL---IRPPdtCSQTPRPP 785
Cdd:PLN03209   508 PPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPtALADEQH---HAQPKPRPLSPYTMyedLKPP--TSPTPSPV 575
SET_SMYD3 cd19203
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 ...
3408-3446 3.39e-04

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: 44.66  E-value: 3.39e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1907162496 3408 NHSCAPNCVAevvTFErGHKIIISSNRRIQKGEELCYDY 3446
Cdd:cd19203    147 NHSCDPNCVI---VFN-GPHLLLRAIREIEVGEELTISY 181
ePHD_BRPF cd15670
Extended PHD finger found in BRPF proteins; The extended plant homeodomain (ePHD) zinc finger ...
2987-3051 3.70e-04

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: 42.71  E-value: 3.70e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907162496 2987 WVHLNCALWSTEVYetqagaLIN-VELALRRGLQ--------MKCVFC-HKTGATSGCHRFRCTNIYHFTCATKA 3051
Cdd:cd15670     19 WAHVVCALWIPEVS------FANtVFLEPIDGIQnipkarwkLTCYICkKRMGACIQCHKKNCYTAFHVTCAQQA 87
PHA03379 PHA03379
EBNA-3A; Provisional
381-838 5.03e-04

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 46.20  E-value: 5.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  381 QNSQPPSPQMFSPGSSHSR-----------PPSPVDPYAKMVGTPRPPPGGhsfprRNSVTPVEncVPLSSVPRPIHMNE 449
Cdd:PHA03379   441 QVPEPPPVHDLEPGPLHDQhsmapcpvaqlPPGPLQDLEPGDQLPGVVQDG-----RPACAPVP--APAGPIVRPWEASL 513
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  450 TSATRPSPArdlcassMTNSDPYAKPPDtPRPmmtdqfSKPFSLPRSPVISEQSTKGPLTTGTSdhftkpsprtdafqrQ 529
Cdd:PHA03379   514 SQVPGVAFA-------PVMPQPMPVEPV-PVP------TVALERPVCPAPPLIAMQGPGETSGI---------------V 564
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  530 RLPDPYAGPSLTPAPLgNGPFKTPLHPPPSQ-DPYGSVSQTSrrLSVDPYERPALTPRpvdnfshsqsnDPYSHpPLTPH 608
Cdd:PHA03379   565 RVRERWRPAPWTPNPP-RSPSQMSVRDRLARlRAEAQPYQAS--VEVQPPQLTQVSPQ-----------QPMEY-PLEPE 629
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  609 PAMtesftHASRAFPQPGTISRsASQDPYSQPPGTPRPLIDSYSQTSGTArsnPDPYSQPPGTPRPNTIDPYSQQPPTPR 688
Cdd:PHA03379   630 QQM-----FPGSPFSQVADVMR-AGGVPAMQPQYFDLPLQQPISQGAPLA---PLRASMGPVPPVPATQPQYFDIPLTEP 700
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  689 PSPQTDMFvssvanqrhtdpythHLGPPRPgisvpySQPPAVPRPRTSEGFTRPSSARPALMPNQD---PFLQAAQNRVP 765
Cdd:PHA03379   701 INQGASAA---------------HFLPQQP------MEGPLVPERWMFQGATLSQSVRPGVAQSQYfdlPLTQPINHGAP 759
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907162496  766 GLPGPlirppdtcsqtPRPPGPGRIdtfthassSAVRDPYDQPPVTPR----PHS-ESFGtsQVVHDLVDRPVPGSEG 838
Cdd:PHA03379   760 AAHFL-----------HQPPMEGPW--------VPEQWMFQGAPPSQGtdvvQHQlDALG--YVLHVLNHPGVPVSPA 816
COG5141 COG5141
PHD zinc finger-containing protein [General function prediction only];
2987-3070 5.23e-04

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


Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 45.74  E-value: 5.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2987 WVHLNCALWSTEVY--ETQAGALINVELALRRGL-QMKCVFCHKTGATS-GCHRFRCTNIYHFTCATKAqCMFFK----- 3057
Cdd:COG5141    268 WGHVICAMFNPELSfgHLLSKDPIDNIASVSSSRwKLGCLICKEFGGTCiQCSYFNCTRAYHVTCARRA-GYFDLniysh 346
                           90       100
                   ....*....|....*....|
gi 1907162496 3058 -------DKTMLCPMHKPKG 3070
Cdd:COG5141    347 ngisyciDHEPLCRKHYPLG 366
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
1687-1769 6.92e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.55  E-value: 6.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 1687 EEWLQETQQLLQmqqkylEEQigahrKSKKALSAKQRT--AKKAG-REFPEEDAEQLKHVTEQQSMVQKQLEQIRKQQKE 1763
Cdd:pfam01576  467 ESQLQDTQELLQ------EET-----RQKLNLSTRLRQleDERNSlQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEE 535

                   ....*.
gi 1907162496 1764 HAELIE 1769
Cdd:pfam01576  536 DAGTLE 541
PTZ00395 PTZ00395
Sec24-related protein; Provisional
534-673 7.00e-04

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 45.84  E-value: 7.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  534 PYAGPSLTPAPLGNGPFKtplHPPPSQDPYgsvsqtsrrlSVDPYERPALTPRPVDNFSHsqSNDPYSHPP---LTPHPA 610
Cdd:PTZ00395   418 GNSNPGYNNAPNSNTPYN---NPPNSNTPY----------SNPPNSNPPYSNLPYSNTPY--SNAPLSNAPpssAKDHHS 482
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162496  611 MTESfTHASRAFPQPG----TISRSASQDPYSQPPGTPRPLIDSYSQTSGTARSNPDPYSQPPGTPR 673
Cdd:PTZ00395   483 AYHA-AYQHRAANQPAanlpTANQPAANNFHGAAGNSVGNPFASRPFGSAPYGGNAATTADPNGIAK 548
dnaA PRK14086
chromosomal replication initiator protein DnaA;
676-874 8.36e-04

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 45.20  E-value: 8.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  676 TIDPYSQQPPTPRPSPQtdmfvssvanqRHTDPYTHHLGP-PRPGisvpYSQPPAVPRPRTSEGFTRPSSARPALMPNQD 754
Cdd:PRK14086    87 TVDPSAGEPAPPPPHAR-----------RTSEPELPRPGRrPYEG----YGGPRADDRPPGLPRQDQLPTARPAYPAYQQ 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  755 PflqaaqnrvpGLPGPLIRPPDTCSQTPRPPGPGRIDTFTHASSSA-----VRDPYD----------QPPVTPRPHSEsf 819
Cdd:PRK14086   152 R----------PEPGAWPRAADDYGWQQQRLGFPPRAPYASPASYApeqerDREPYDagrpeydqrrRDYDHPRPDWD-- 219
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907162496  820 gtsQVVHDLVDRPV--PGSEGNFSTSSNLPVSSQGQQFSSVSQLPG-------PVPTSGGTDTQ 874
Cdd:PRK14086   220 ---RPRRDRTDRPEppPGAGHVHRGGPGPPERDDAPVVPIRPSAPGplaaqpaPAPGPGEPTAR 280
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
670-1092 9.87e-04

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: 45.14  E-value: 9.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  670 GTPRPNTIDPYSQQPPTPRPSPQ---TDMFVSSVANQRHTDP-----YTHHLGPPRPGISVPYSQPPAVPRPRTSEGFTR 741
Cdd:pfam03154  130 GSSDPKDIDQDNRSTSPSIPSPQdneSDSDSSAQQQILQTQPpvlqaQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQ 209
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  742 PSSarPALMPNQDPFLQAA-----QNRVPGLPGPLIRPPDTCSQTPRPPGPGRIdtfthaSSSAVRDPYDQPPVTPRPHS 816
Cdd:pfam03154  210 GSP--ATSQPPNQTQSTAAphtliQQTPTLHPQRLPSPHPPLQPMTQPPPPSQV------SPQPLPQPSLHGQMPPMPHS 281
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  817 ESFGTSQVVHDLVDRPVPGSegnfstssnlPVSSQGQQfssvsqLPGPVPTSGGTDTQNTvnMSQADTEKLRQRQKLREI 896
Cdd:pfam03154  282 LQTGPSHMQHPVPPQPFPLT----------PQSSQSQV------PPGPSPAAPGQSQQRI--HTPPSQSQLQSQQPPREQ 343
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  897 ILQQQQqkkIASRQEKGPQDTAVVPHPVPLPHWQPESINQAF------TRPPPPY--PGSTRSPVIPPLG--PRYAVFPK 966
Cdd:pfam03154  344 PLPPAP---LSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSpfqmnsNLPPPPAlkPLSSLSTHHPPSAhpPPLQLMPQ 420
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  967 DQRGPYPPE-----VAGMGMRPHGFRFGFPGAGHgPMPSQDRFhvPQQIQGSGIPPHIRRPMSmemprpsnnPPLNNPVG 1041
Cdd:pfam03154  421 SQQLPPPPAqppvlTQSQSLPPPAASHPPTSGLH-QVPSQSPF--PQHPFVPGGPPPITPPSG---------PPTSTSSA 488
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907162496 1042 LPQHFPPQGLPVQQHNILGQAF------IELRHRAPDG----RSRLPFAASPS---SVIESPSH 1092
Cdd:pfam03154  489 MPGIQPPSSASVSSSGPVPAAVscplppVQIKEEALDEaeepESPPPPPRSPSpepTVVNTPSH 552
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1682-1774 1.13e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.14  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 1682 QRKQ--YEEWLQETQQLLQMQQKYLEEQigahrksKKALSAKQRTAKKAGREFPEEDAEQLKHVTEQQSMVQKQLEQIRK 1759
Cdd:pfam13868   87 QKRQeeYEEKLQEREQMDEIVERIQEED-------QAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILE 159
                           90
                   ....*....|....*
gi 1907162496 1760 QQKEHAELIEDYRIK 1774
Cdd:pfam13868  160 YLKEKAEREEEREAE 174
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
517-711 1.25e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  517 TKPSPRTDAFQRQRLPDPYAGPSLTPAPLGNGPFKTPLHPPPSQDPYGSVSQTSRRLSVDPYERPALTPRPVDNFSHSQS 596
Cdd:PRK07764   600 PPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPA 679
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  597 NDPYSHPPLTPHPAMTESFT---HASRAFPQPGTISRSASQDPYSQPPGTPRPLIDSYSQTSGTARSNPDPYSQPPGTPR 673
Cdd:PRK07764   680 APPPAPAPAAPAAPAGAAPAqpaPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPP 759
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1907162496  674 PNTID-PYSQQPPTPRPSPQTDMFVSSVANQRHTDPYTH 711
Cdd:PRK07764   760 PPPAPaPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDR 798
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
609-833 1.38e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.78  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  609 PAMTESFTHASRAFPQPGTISRSASQDPYSQPPGTPRPLidsysqtSGTARSNPDPYSQPPGT----PRPNTIDPYSQQP 684
Cdd:PHA03307   761 PSLVPAKLAEALALLEPAEPQRGAGSSPPVRAEAAFRRP-------GRLRRSGPAADAASRTAskrkSRSHTPDGGSESS 833
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  685 PTPRPSPQTdmFVSSVANQRHTDPYTHHLGPPRPGISVPYSQPPAVPRPRTSEGFTRPSSARPAlmpnqdpflqaaqnRV 764
Cdd:PHA03307   834 GPARPPGAA--ARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAA--------------PP 897
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162496  765 PGLPGPLIRPPDTCSQTPRPPGpGRidtfthASSSAVRDPYDQPPVTPRP---HSESFGTSQVVHDLVDRPV 833
Cdd:PHA03307   898 AGAPAPRPRPAPRVKLGPMPPG-GP------DPRGGFRRVPPGDLHTPAPsaaALAAYCPPEVVAELVDHPL 962
ePHD_BRPF1 cd15701
Extended PHD finger found in bromodomain and PHD finger-containing protein 1 (BRPF1) and ...
2962-3068 1.82e-03

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: 40.83  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2962 CCFCHEEGDGLTdgparllNLDLDLWVHLNCALWSTEVYETQAGAL---INVELALRRGLQMKCVFCHK--TGATSGCHR 3036
Cdd:cd15701      1 CALCPNKGGAFK-------QTDDGRWAHVVCALWIPEVCFANTVFLepiDSIEHIPPARWKLTCYICKQrgSGACIQCHK 73
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1907162496 3037 FRCTNIYHFTCATKAQcMFFK----------------DKTMLCPMHKP 3068
Cdd:cd15701     74 ANCYTAFHVTCAQQAG-LYMKmepvretgangtsfsvRKTAYCDIHTP 120
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
536-761 1.94e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.21  E-value: 1.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  536 AGPSLTPAPLGNGPFKTPLHPPPSQDPYGSVSQtsrrlsvdPYERPALTPRPVDNFSHSQSNDPYSHPPLTPHPAMTESF 615
Cdd:PRK07764   595 AGGEGPPAPASSGPPEEAARPAAPAAPAAPAAP--------APAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGG 666
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  616 THASRAFPQPGTISRSASQDPYSQPPGTPRPLIDSYSQTSGTARSNP--DPYSQPPGTPRPNTIDPYS---QQPPTPRPS 690
Cdd:PRK07764   667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQadDPAAQPPQAAQGASAPSPAaddPVPLPPEPD 746
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162496  691 PQTDmfvssvanqrhtdPYTHHLGPPRPGISVPYSQPPAvpRPRTSEGFTRPSSARPALMPNQDPFLQAAQ 761
Cdd:PRK07764   747 DPPD-------------PAGAPAQPPPPPAPAPAAAPAA--APPPSPPSEEEEMAEDDAPSMDDEDRRDAE 802
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
1680-1773 2.36e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 40.63  E-value: 2.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 1680 DSQRKQYEEW---LQETQQLLQMQQKYLEEQIGAHRKSKKALSAKQRTA-KKAgrefpEEDAEQLKHVTEQQSMVQKQLE 1755
Cdd:pfam13863   16 DAKREEIERLeelLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRAlKKA-----EEETKLKKEKEKEIKKLTAQIE 90
                           90
                   ....*....|....*...
gi 1907162496 1756 QIRKQQKEHAELIEDYRI 1773
Cdd:pfam13863   91 ELKSEISKLEEKLEEYKP 108
ePHD_BRPF3 cd15703
Extended PHD finger found in bromodomain and PHD finger-containing protein 3 (BRPF3) and ...
2987-3051 2.50e-03

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: 40.42  E-value: 2.50e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162496 2987 WVHLNCALWSTEVYETQAGALINVE----LALRRgLQMKCVFCHKTG--ATSGCHRFRCTNIYHFTCATKA 3051
Cdd:cd15703     19 WAHVVCAIWIPEVCFANTVFLEPVEgvnnIPPAR-WKLTCYLCKQKGrgAAIQCHKVNCYTAFHVTCAQRA 88
HMG-box_HMGB_rpt2 cd21979
second high mobility group (HMG)-box found in the high mobility group protein B (HMGB) family; ...
163-199 2.94e-03

second high mobility group (HMG)-box found in the high mobility group protein B (HMGB) family; HMGB proteins are chromatin-associated nuclear proteins that act as architectural factors in nucleoprotein structures, which regulate DNA-dependent processes including transcription. In mammals, four family members are present: HMGB1, HMGB2, HMGB3 and HMGB4. They regulate the expression of a wide range of genes through architectural remodeling of the chromatin structure. HMGB1, also called high mobility group protein 1 (HMG-1), is a prototypical alarmin or damage-associated molecular pattern (DAMP) molecule when released from cells. It plays important roles in the regulation of a wide range of processes, including transcription, replication, DNA repair, and nucleosome formation, in the nucleus. It also plays multiple roles in regulating inflammation and responses to cell and tissue stress. HMGB2, also called high mobility group protein 2 (HMG-2), has been implicated in numerous cellular processes, including proliferation, differentiation, apoptosis, and tumor growth. It acts as a chromatin-associated nonhistone protein involved in transcriptional regulation and nucleic-acid-mediated innate immune responses in mammalian. It binds DNA to stabilize nucleosomes and promote transcription. HMGB3, also called high mobility group protein 2a (HMG-2a), or high mobility group protein 4 (HMG-4), is an X-linked member of HMGB family and functions as a universal sentinel for nucleic acid-mediated innate immune responses. HMGB3 has been implicated in the regulation of cellular proliferation and differentiation, as well as inflammatory response. HMGB4 is expressed by neuronal cells and affects the expression of genes involved in neural differentiation. It is a factor that regulates chromatin and expression of neuronal differentiation markers. The family also includes high mobility group protein B1 pseudogene 1 (HMGB1P1) and nuclear auto-antigen Sp-100. HMGB1P1, also called putative high mobility group protein B1-like 1 (HMGB1L1), or putative high mobility group protein 1-like 1 (HMG-1L1), is an HMG-box containing protein that binds preferentially single-stranded DNA and unwinds double-stranded DNA. Sp-100, also called nuclear dot-associated Sp100 protein, or speckled 100 kDa. It is a tumor suppressor that is a major constituent of the promyelocytic leukemia (PML) bodies, a subnuclear organelle involved in many physiological processes including cell growth, differentiation and apoptosis. Through the regulation of ETS1, Sp-100 may play a role in angiogenesis, controlling endothelial cell motility and invasion. It may also play roles in the regulation of telomeres lengthening, TP53-mediated transcription, FAS-mediated apoptosis, etc. In addition, the family includes Drosophila melanogaster high mobility group protein DSP1 (dDSP1) and similar proteins. dDSP1, also called protein dorsal switch 1, is a Drosophila HMG1 protein that binds preferentially single-stranded DNA and unwinds double-stranded DNA. It converts Dorsal and nuclear factor (NF)-kappa B from transcriptional activators to repressors. Members of the HMGB family contain two HMG-box domains. This model corresponds to the second one.


Pssm-ID: 438795 [Multi-domain]  Cd Length: 71  Bit Score: 38.93  E-value: 2.94e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1907162496  163 FPNLKEEFPDWTtrVKQIAK----LWRKASSQERAPYVQKA 199
Cdd:cd21979     18 RPKIKGEHPGLS--IGDVAKklgeMWNNTSAKDKQPYEKKA 56
PHA03379 PHA03379
EBNA-3A; Provisional
911-1182 2.99e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 43.51  E-value: 2.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  911 EKGPQDTAVVPHP-VPLPHWQ-PESINQAFTRPPP--PYPGSTRSPVIPPLGPRYAVFP----KDQRGPYPPEVAGmGMR 982
Cdd:PHA03379   406 EKASEPTYGTPRPpVEKPRPEvPQSLETATSHGSAqvPEPPPVHDLEPGPLHDQHSMAPcpvaQLPPGPLQDLEPG-DQL 484
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  983 PHGFRFGFPGAGHGPMPSQDRFH----VPQQIQGSGIPPHIRRPMSMEMPRPSNNPPLNNPVGLPQHFPPQGlPVQQHNI 1058
Cdd:PHA03379   485 PGVVQDGRPACAPVPAPAGPIVRpweaSLSQVPGVAFAPVMPQPMPVEPVPVPTVALERPVCPAPPLIAMQG-PGETSGI 563
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 1059 LGqafIELRHRAPDGRSRLPFAASPSSVIESPSHPR-------HGNFLPRPDFPGPRHTDPIRQPSQCLSNQLPVHPnLE 1131
Cdd:PHA03379   564 VR---VRERWRPAPWTPNPPRSPSQMSVRDRLARLRaeaqpyqASVEVQPPQLTQVSPQQPMEYPLEPEQQMFPGSP-FS 639
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162496 1132 QVPPSQQEQGHPAHQSSIVMRPLNHPLSGEFSEAPLSTST-----PAETSPDNLEI 1182
Cdd:PHA03379   640 QVADVMRAGGVPAMQPQYFDLPLQQPISQGAPLAPLRASMgpvppVPATQPQYFDI 695
mukB PRK04863
chromosome partition protein MukB;
1684-1774 3.82e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.41  E-value: 3.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 1684 KQYEEWLQETQQLLQMQQKY--LEEQIGAHRKSKKALsakQRTAKKAGREFPEEDA---------EQLKHVTEQQSMVQK 1752
Cdd:PRK04863   503 RRLREQRHLAEQLQQLRMRLseLEQRLRQQQRAERLL---AEFCKRLGKNLDDEDEleqlqeeleARLESLSESVSEARE 579
                           90       100
                   ....*....|....*....|..
gi 1907162496 1753 QLEQIRKQQKEHAELIEDYRIK 1774
Cdd:PRK04863   580 RRMALRQQLEQLQARIQRLAAR 601
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1678-1802 3.93e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 3.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 1678 VNDSQRKQYEEwLQETQQLLQMQQKYLEEQigahRKSKKALSAKQRTAKKAGREFPEEDAEQLKHVTEQQSMVQKQLEQI 1757
Cdd:COG4942    144 LAPARREQAEE-LRADLAELAALRAELEAE----RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1907162496 1758 RKQQKEHAELIEDYRIKQQQQQQQCALAPPILMPGVQPQPplVPG 1802
Cdd:COG4942    219 QQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLPWP--VSG 261
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
641-838 3.98e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 3.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  641 PGTPRPLIDSYSQTSGTARSNPDPYSQPPGTPRPNTidpysQQPPTPRPSPQTDMFVSSVANQRHTDPYTHHLGPPRPGI 720
Cdd:PRK07764   588 VGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAA-----PAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDA 662
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  721 SVPYSQPPAVPRPRTSEGFTRPSSARPALMPNQDPFLQAAQNRVPGLPGPliRPPDTCSQTPRPPgpgridtftHASSSA 800
Cdd:PRK07764   663 SDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAG--QADDPAAQPPQAA---------QGASAP 731
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1907162496  801 VRDPYDQPPVTPRPHSESFGtSQVVHDLVDRPVPGSEG 838
Cdd:PRK07764   732 SPAADDPVPLPPEPDDPPDP-AGAPAQPPPPPAPAPAA 768
SET_SMYD1 cd10526
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 ...
3407-3461 4.52e-03

SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 (SMYD1) and similar proteins; 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. SMYD1 plays a critical role in cardiomyocyte differentiation, cardiac morphogenesis and myofibril organization, as well as in the regulation of endothelial cells (ECs). It is expressed in vascular endothelial cells, it has beenshown that knockdown of SMYD1 in endothelial cells impairs EC migration and tube formation.


Pssm-ID: 380924 [Multi-domain]  Cd Length: 210  Bit Score: 41.25  E-value: 4.52e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907162496 3407 INHSCAPNCvaeVVTFERGhKIIISSNRRIQKGEELCYDYkFDF----ED------DQHKIPCHC 3461
Cdd:cd10526    146 VNHDCWPNC---TVIFNNG-RIELRALGKISEGDELTVSY-IDFlntsEDrkeqlkKQYYFDCTC 205
ePHD_BRPF2 cd15702
Extended PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and ...
2962-3051 5.41e-03

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: 39.64  E-value: 5.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2962 CCFCHEEGDGLTdgparllNLDLDLWVHLNCALWSTEV------YETQAGALINVELALrrgLQMKCVFCHK--TGATSG 3033
Cdd:cd15702      1 CVLCPNKGGAFK-------KTDDDRWGHVVCALWIPEVgfantvFIEPIDGVRNIPPAR---WKLTCYLCKQkgVGACIQ 70
                           90
                   ....*....|....*...
gi 1907162496 3034 CHRFRCTNIYHFTCATKA 3051
Cdd:cd15702     71 CHKANCYTAFHVTCAQKA 88
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
1681-1769 5.80e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.51  E-value: 5.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 1681 SQRKQYEEWLQETQQLLQMQQKY---LEEQIGAHRKSKKALSAKQ-RTAKKAGREFPEEDAEQLKHVTEQQSMVQ----- 1751
Cdd:PRK00409   527 ELERELEQKAEEAEALLKEAEKLkeeLEEKKEKLQEEEDKLLEEAeKEAQQAIKEAKKEADEIIKELRQLQKGGYasvka 606
                           90
                   ....*....|....*...
gi 1907162496 1752 KQLEQIRKQQKEHAELIE 1769
Cdd:PRK00409   607 HELIEARKRLNKANEKKE 624
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
624-881 6.87e-03

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: 42.33  E-value: 6.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  624 QPGTISRSASQDPYSQPPGTPRPLIDSYSQTSGTARSNPDPYSQPpgTPRPN----------TIDPYSQQPPTPRPSPQT 693
Cdd:pfam09770  106 QPAARAAQSSAQPPASSLPQYQYASQQSQQPSKPVRTGYEKYKEP--EPIPDlqvdaslwgvAPKKAAAPAPAPQPAAQP 183
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  694 DMFVSSV----------ANQRHTDPythhlGPPRPGISVPYSQPPAVPRPRTSEGFTRPSSARPALMPNQDPfLQAAQNR 763
Cdd:pfam09770  184 ASLPAPSrkmmsleeveAAMRAQAK-----KPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQP-QQPQQHP 257
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  764 VPGLP-GPLIRPPdtcSQTPRPPGPgridtftHASSSAVRDPYDQPPVTPRPhsesfgtSQVVHD---LVDRPVPGSEGN 839
Cdd:pfam09770  258 GQGHPvTILQRPQ---SPQPDPAQP-------SIQPQAQQFHQQPPPVPVQP-------TQILQNpnrLSAARVGYPQNP 320
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1907162496  840 FSTSSNLPVSSQGQQFSSVSQLPGPVptsggTDTQNTVNMSQ 881
Cdd:pfam09770  321 QPGVQPAPAHQAHRQQGSFGRQAPII-----THPQQLAQLSE 357
ePHD_ATX3_4_5_like cd15663
Extended PHD finger found in Arabidopsis thaliana ATX3, -4, -5, and similar proteins; The ...
2962-3051 8.45e-03

Extended PHD finger found in Arabidopsis thaliana ATX3, -4, -5, 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 ATX3 (also termed protein SET domain group 14, or trithorax-homolog protein 3), ATX4 (also termed protein SET domain group 16, or trithorax-homolog protein 4) and ATX5 (also termed protein SET domain group 29, or trithorax-homolog protein 5), which belong to the histone-lysine methyltransferase family. These proteins show distinct phylogenetic origins from the family of ATX1 and ATX2. They are multi-domain proteins that consist of an N-terminal PWWP domain, a canonical PHD finger, this non-canonical extended PHD finger, and a C-terminal SET domain.


Pssm-ID: 277133  Cd Length: 112  Bit Score: 38.65  E-value: 8.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496 2962 CCFCHEEGDGLTdgPARLLNLdldlWVHLNCALWSTEV-------YETQAGaLINVELAlrrGLQMKCVFCHKT-GATSG 3033
Cdd:cd15663      1 CCLCPVKGGALK--PTDVEGL----WVHVTCAWFRPEVcfkneekMEPAVG-LLRIPLS---TFLKACVICKQIhGSCTQ 70
                           90
                   ....*....|....*...
gi 1907162496 3034 CHrfRCTNIYHFTCATKA 3051
Cdd:cd15663     71 CC--KCATYFHAMCASRA 86
Tma16 pfam11176
Translation machinery-associated protein 16; Proteins in this family localize to the nucleus. ...
194-277 8.45e-03

Translation machinery-associated protein 16; Proteins in this family localize to the nucleus. Their function is not clear.


Pssm-ID: 463236  Cd Length: 146  Bit Score: 39.42  E-value: 8.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  194 PYVQKA-RDNRAALRINKVQMSNDSMKRQQQ---------QDSIDPSSRIDS-----DLFKDPLKQRESEHEQEWKFRQQ 258
Cdd:pfam11176    7 PNSRKAkQLRRAALRDEKLEKLKAARAKKKNpllerlaffQEALDEDKKPLTleelhELIERYLHRFDEELEELKKERRP 86
                           90
                   ....*....|....*....
gi 1907162496  259 MRQKSKQQAKIEATQKLEQ 277
Cdd:pfam11176   87 GRPPSSREDLLEQKIEREE 105
PLN03188 PLN03188
kinesin-12 family protein; Provisional
489-576 8.58e-03

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 42.23  E-value: 8.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162496  489 KPFSLPRSPVISEQSTKGPLTTGTSDHFTKPSPRTDAFQRQRLPDP---YAGPSLTPAPL-GNGPFKTPLHP-PPSQDPY 563
Cdd:PLN03188     2 KHFMLPRNAILRETSSGEEQSPNPSSHKSKPSSRKLKSSKENAPPPdlnSLTSDLKPDHRsASAKLKSPLPPrPPSSNPL 81
                           90
                   ....*....|...
gi 1907162496  564 gsvsqtSRRLSVD 576
Cdd:PLN03188    82 ------KRKLSAE 88
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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