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Conserved domains on  [gi|2464208148|ref|XP_054416569|]
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inactive histone-lysine N-methyltransferase 2E isoform X1 [Pongo abelii]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SET_KMT2E cd19182
SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...
323-451 4.76e-91

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: 291.03  E-value: 4.76e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  323 TNNLLFKPPVESHIQKNKKILKSAKDLPPDALIIEYRGKFMLREQFEANGYFFKRPYPFVLFYSKFHGLEMCVDARTFGN 402
Cdd:cd19182      1 TSNLLFKPPVESHVQKNKKILKAAKDLPPDTLIIEYRGKFMLREQFEANGYFFKRPYPFVLFYSKFHGLEMCVDARTFGN 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2464208148  403 EARFIRRSCTPNAEVRHEIQDGTIHLYIYSIHSIPKGTEITIAFDFDYG 451
Cdd:cd19182     81 EARFIRRSCTPNAEVRHVIEDGTIHLYIYSIRSIPKGTEITIAFDFDYG 129
PHD_MLL5 cd15550
PHD finger found in mixed lineage leukemia 5 (MLL5); MLL5 is a histone methyltransferase that ...
120-163 6.86e-31

PHD finger found in mixed lineage leukemia 5 (MLL5); MLL5 is a histone methyltransferase that plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. It contains a single plant homeodomain (PHD) finger followed by a catalytic SET domain. MLL5 can be recruited to E2F1-responsive promoters to stimulate H3K4 trimethylation and transcriptional activation by binding to the cell cycle regulator host cell factor (HCF-1), thereby facilitating the cell cycle G1 to S phase transition. It is also involved in mitotic fidelity and genomic integrity by modulating the stability of the chromosomal passenger complex (CPC) via the interaction with Borealin. Moreover, MLL5 is a component of a complex associated with retinoic acid receptor that requires GlcN Acylation of its SET domain in order to activate its histone lysine methyltransferase activity. It also participates in the camptothecin (CPT)-induced p53 activation. Furthermore, MLL5 indirectly regulates H3K4 methylation, represses cyclin A2 (CycA) expression, and promotes myogenic differentiation.


:

Pssm-ID: 277025 [Multi-domain]  Cd Length: 44  Bit Score: 115.88  E-value: 6.86e-31
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2464208148  120 RCICGFTHDDGYMICCDKCSVWQHIDCMGIDRQHIPDTYLCERC 163
Cdd:cd15550      1 RCICGFEHDDGFMICCDKCSVWQHGDCMGIDRENIPDSYLCEQC 44
Herpes_TAF50 super family cl25754
Herpesvirus transcription activation factor (transactivator); This family includes EBV BRLF1 ...
1288-1524 2.41e-05

Herpesvirus transcription activation factor (transactivator); This family includes EBV BRLF1 and similar ORF 50 proteins from other herpesviruses.


The actual alignment was detected with superfamily member pfam03326:

Pssm-ID: 308764 [Multi-domain]  Cd Length: 568  Bit Score: 49.31  E-value: 2.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1288 VSCSPSHVQSSPSSHSNHIPQLQAKGPVPSFSELMEDPDPENPEPTTTNECPSPDTSQNTCKSPSKMSKPGSPGSVIPAQ 1367
Cdd:pfam03326  302 VSLFPSTATLVPIAGSTGVTEVVSYGHNSTSPSSTPCPSTAVTEADHQTEPEVPWIATAHQESDQRPIGPGPEKPTFLPP 381
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1368 AHGKIFTKPDPQWDSTVSASEAENGVhlkteLQQKQLSNTNQALSKNHPPQThvrnsseqlsqkLPSAPTKLHCPPSPHL 1447
Cdd:pfam03326  382 VGGKQFFQGLRDSRSTSFLTAPEATS-----AISDVFQGTEVCQPKRIRALH------------PPGSPSANRPLPSSLA 444
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1448 ENPpkSSTPHTPVqhGYLSPKPPSQQL-----GSPYRPHHSQSPQVGTPQREPQRNFYPAAQNLQANTQQATSGTLFTQT 1522
Cdd:pfam03326  445 PTP--TGPVHEPG--SSLTPATVPQPLdaapvATPEASHELQPPDEETPQPLDEDQALCGQQDASHPPPRGQLDELTTTL 520

                   ..
gi 2464208148 1523 PS 1524
Cdd:pfam03326  521 ES 522
PHA03247 super family cl33720
large tegument protein UL36; Provisional
1740-1845 2.19e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 2.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1740 HPPHQ---GPPLFPSSAHPAVPPYPSQATHHTTLGPGPQHQPSGTGPHCPLPVTGPHLQPQGPnsiPTPTasgfcPHPGS 1816
Cdd:PHA03247  2880 RPPVRrlaRPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPP---LAPT-----TDPAG 2951
                           90       100       110
                   ....*....|....*....|....*....|
gi 2464208148 1817 VALPHG-VQGPQQASPVPGQIPIHRAQVPP 1845
Cdd:PHA03247  2952 AGEPSGaVPQPWLGALVPGRVAVPRFRVPQ 2981
TPH super family cl38442
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
561-669 4.21e-04

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.


The actual alignment was detected with superfamily member pfam13868:

Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.52  E-value: 4.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  561 MESEEQIAERKRKMTREERKMEAILQAFARL-EKREKRREQALERISTAKTEVKT-------ECKDTQIVSD---AEVIQ 629
Cdd:pfam13868  133 DEFNEEQAEWKELEKEEEREEDERILEYLKEkAEREEEREAEREEIEEEKEREIArlraqqeKAQDEKAERDelrAKLYQ 212
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2464208148  630 EQAKEENASKPTPAKVNRTKQRKSFSRSRTHIGQQRRRHR 669
Cdd:pfam13868  213 EEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRL 252
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1463-1828 2.86e-03

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 42.69  E-value: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1463 GYLSPKPPSQQLGSPYRPHHSQSP-QVGTPQREPQRnfypaaqnlQANTQQATSGTLFTQTPSGQSSATYSQFNQQSLNS 1541
Cdd:pfam09606  157 GMMQPSSGQPGSGTPNQMGPNGGPgQGQAGGMNGGQ---------QGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANG 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1542 TAPPPPPPPPPSSYYQNQQPSanfqnynqlkGSLSQQTVFTSGPNQAlpgttsQQTVPGHHVTPGHFLPSQNPTIHHQTA 1621
Cdd:pfam09606  228 GMNPQQMGGAPNQVAMQQQQP----------QQQGQQSQLGMGINQM------QQMPQGVGGGAGQGGPGQPMGPPGQQP 291
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1622 AAVVPPPPPPPPAPGPHLVQQPNSHQQ---HSVAHVVGPVHAVTPGSHIHSQTAGHHLPppppppgpaphhhppphpsTG 1698
Cdd:pfam09606  292 GAMPNVMSIGDQNNYQQQQTRQQQQQQggnHPAAHQQQMNQSVGQGGQVVALGGLNHLE-------------------TW 352
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1699 LQGLQAQHQhvVNSAPPPPPPPPPSSVLASGHHTTSAQALHHPPHQGPPLFPSSAHPavppypsqathhttlgpGPQHQP 1778
Cdd:pfam09606  353 NPGNFGGLG--ANPMQRGQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGP-----------------GSQPPQ 413
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2464208148 1779 SGTGPHCPLPVTGPHLQPQ---GPNS---IPTPTASGFCPHPGSVALPHGVqGPQQ 1828
Cdd:pfam09606  414 SHPGGMIPSPALIPSPSPQmsqQPAQqrtIGQDSPGGSLNTPGQSAVNSPL-NPQE 468
 
Name Accession Description Interval E-value
SET_KMT2E cd19182
SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...
323-451 4.76e-91

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: 291.03  E-value: 4.76e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  323 TNNLLFKPPVESHIQKNKKILKSAKDLPPDALIIEYRGKFMLREQFEANGYFFKRPYPFVLFYSKFHGLEMCVDARTFGN 402
Cdd:cd19182      1 TSNLLFKPPVESHVQKNKKILKAAKDLPPDTLIIEYRGKFMLREQFEANGYFFKRPYPFVLFYSKFHGLEMCVDARTFGN 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2464208148  403 EARFIRRSCTPNAEVRHEIQDGTIHLYIYSIHSIPKGTEITIAFDFDYG 451
Cdd:cd19182     81 EARFIRRSCTPNAEVRHVIEDGTIHLYIYSIRSIPKGTEITIAFDFDYG 129
PHD_MLL5 cd15550
PHD finger found in mixed lineage leukemia 5 (MLL5); MLL5 is a histone methyltransferase that ...
120-163 6.86e-31

PHD finger found in mixed lineage leukemia 5 (MLL5); MLL5 is a histone methyltransferase that plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. It contains a single plant homeodomain (PHD) finger followed by a catalytic SET domain. MLL5 can be recruited to E2F1-responsive promoters to stimulate H3K4 trimethylation and transcriptional activation by binding to the cell cycle regulator host cell factor (HCF-1), thereby facilitating the cell cycle G1 to S phase transition. It is also involved in mitotic fidelity and genomic integrity by modulating the stability of the chromosomal passenger complex (CPC) via the interaction with Borealin. Moreover, MLL5 is a component of a complex associated with retinoic acid receptor that requires GlcN Acylation of its SET domain in order to activate its histone lysine methyltransferase activity. It also participates in the camptothecin (CPT)-induced p53 activation. Furthermore, MLL5 indirectly regulates H3K4 methylation, represses cyclin A2 (CycA) expression, and promotes myogenic differentiation.


Pssm-ID: 277025 [Multi-domain]  Cd Length: 44  Bit Score: 115.88  E-value: 6.86e-31
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2464208148  120 RCICGFTHDDGYMICCDKCSVWQHIDCMGIDRQHIPDTYLCERC 163
Cdd:cd15550      1 RCICGFEHDDGFMICCDKCSVWQHGDCMGIDRENIPDSYLCEQC 44
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
343-452 5.76e-29

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: 113.20  E-value: 5.76e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148   343 LKSAKDLPPDALIIEYRGKFMLREQFEANGYFFKR--PYPFVLFYSKFHgleMCVDARTFGNEARFIRRSCTPNAEVRHE 420
Cdd:smart00317   15 VRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTdgAKAFYLFDIDSD---LCIDARRKGNLARFINHSCEPNCELLFV 91
                            90       100       110
                    ....*....|....*....|....*....|..
gi 2464208148   421 IQDGTIHLYIYSIHSIPKGTEITIAFDFDYGN 452
Cdd:smart00317   92 EVNGDDRIVIFALRDIKPGEELTIDYGSDYAN 123
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
343-451 6.25e-17

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: 78.33  E-value: 6.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  343 LKSAKDLPPDALIIEYRGKFML-------REQFEANGYFFKRPYPFVLFYSKFHglEMCVDARTF--GNEARFIRRSCTP 413
Cdd:pfam00856    4 LFATEDIPKGEFIGEYVEVLLItkeeadkRELLYYDKLELRLWGPYLFTLDEDS--EYCIDARALyyGNWARFINHSCDP 81
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2464208148  414 NAEVRHEIQDGTIHLYIYSIHSIPKGTEITIafdfDYG 451
Cdd:pfam00856   82 NCEVRVVYVNGGPRIVIFALRDIKPGEELTI----DYG 115
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
346-451 1.70e-14

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 71.92  E-value: 1.70e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  346 AKDLPPDALIIEYRGKFMLREQFEANGYFFKRPYPFVLFYSKFHGlemcVDARTFGNEARFIRRSCTPNAEVRHEiqDGT 425
Cdd:COG2940     23 TRDIPKGTLIGEYPGEVITWAEAERREPHKEPLHTYLFELDDDGV----IDGALGGNPARFINHSCDPNCEADEE--DGR 96
                           90       100
                   ....*....|....*....|....*.
gi 2464208148  426 IhlYIYSIHSIPKGTEITIafdfDYG 451
Cdd:COG2940     97 I--FIVALRDIAAGEELTY----DYG 116
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
120-166 1.73e-12

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


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 63.67  E-value: 1.73e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2464208148  120 RC-ICGFTHDDGYMICCDKCSVWQHIDCMGI---DRQHIPDTYLCERCQPR 166
Cdd:pfam00628    1 YCaVCGKSDDGGELVQCDGCDDWFHLACLGPpldPAEIPSGEWLCPECKPK 51
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
121-163 4.29e-11

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: 59.53  E-value: 4.29e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 2464208148   121 CICGFTHDDGYMICCDKCSVWQHIDCMGI-DRQHIPD-TYLCERC 163
Cdd:smart00249    3 SVCGKPDDGGELLQCDGCDRWYHQTCLGPpLLEEEPDgKWYCPKC 47
Herpes_TAF50 pfam03326
Herpesvirus transcription activation factor (transactivator); This family includes EBV BRLF1 ...
1288-1524 2.41e-05

Herpesvirus transcription activation factor (transactivator); This family includes EBV BRLF1 and similar ORF 50 proteins from other herpesviruses.


Pssm-ID: 308764 [Multi-domain]  Cd Length: 568  Bit Score: 49.31  E-value: 2.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1288 VSCSPSHVQSSPSSHSNHIPQLQAKGPVPSFSELMEDPDPENPEPTTTNECPSPDTSQNTCKSPSKMSKPGSPGSVIPAQ 1367
Cdd:pfam03326  302 VSLFPSTATLVPIAGSTGVTEVVSYGHNSTSPSSTPCPSTAVTEADHQTEPEVPWIATAHQESDQRPIGPGPEKPTFLPP 381
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1368 AHGKIFTKPDPQWDSTVSASEAENGVhlkteLQQKQLSNTNQALSKNHPPQThvrnsseqlsqkLPSAPTKLHCPPSPHL 1447
Cdd:pfam03326  382 VGGKQFFQGLRDSRSTSFLTAPEATS-----AISDVFQGTEVCQPKRIRALH------------PPGSPSANRPLPSSLA 444
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1448 ENPpkSSTPHTPVqhGYLSPKPPSQQL-----GSPYRPHHSQSPQVGTPQREPQRNFYPAAQNLQANTQQATSGTLFTQT 1522
Cdd:pfam03326  445 PTP--TGPVHEPG--SSLTPATVPQPLdaapvATPEASHELQPPDEETPQPLDEDQALCGQQDASHPPPRGQLDELTTTL 520

                   ..
gi 2464208148 1523 PS 1524
Cdd:pfam03326  521 ES 522
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
1310-1502 3.15e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 48.92  E-value: 3.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1310 QAKGPVPSFSElmEDPD-----PENPEPTTTN-ECPSPDTSQNTCKSPSKMSKP----GSPGSVipaqAHGKIFTKPDPQ 1379
Cdd:PTZ00449   491 KSKKKLAPIEE--EDSDkhdepPEGPEASGLPpKAPGDKEGEEGEHEDSKESDEpkegGKPGET----KEGEVGKKPGPA 564
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1380 WDSTVSaseaengvhlKTELQQKQLSNTNQAlskNHPpqthvRNSSEQLSQKLPSAPTKLHCPPSPHLenPPKSSTPHTP 1459
Cdd:PTZ00449   565 KEHKPS----------KIPTLSKKPEFPKDP---KHP-----KDPEEPKKPKRPRSAQRPTRPKSPKL--PELLDIPKSP 624
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2464208148 1460 VQ-HGYLSPK--PPSQQLGSPYRPHHSQSPQVGTPQREPQRNFYPA 1502
Cdd:PTZ00449   625 KRpESPKSPKrpPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFDPK 670
PHA03247 PHA03247
large tegument protein UL36; Provisional
1740-1845 2.19e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 2.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1740 HPPHQ---GPPLFPSSAHPAVPPYPSQATHHTTLGPGPQHQPSGTGPHCPLPVTGPHLQPQGPnsiPTPTasgfcPHPGS 1816
Cdd:PHA03247  2880 RPPVRrlaRPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPP---LAPT-----TDPAG 2951
                           90       100       110
                   ....*....|....*....|....*....|
gi 2464208148 1817 VALPHG-VQGPQQASPVPGQIPIHRAQVPP 1845
Cdd:PHA03247  2952 AGEPSGaVPQPWLGALVPGRVAVPRFRVPQ 2981
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
561-669 4.21e-04

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: 44.52  E-value: 4.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  561 MESEEQIAERKRKMTREERKMEAILQAFARL-EKREKRREQALERISTAKTEVKT-------ECKDTQIVSD---AEVIQ 629
Cdd:pfam13868  133 DEFNEEQAEWKELEKEEEREEDERILEYLKEkAEREEEREAEREEIEEEKEREIArlraqqeKAQDEKAERDelrAKLYQ 212
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2464208148  630 EQAKEENASKPTPAKVNRTKQRKSFSRSRTHIGQQRRRHR 669
Cdd:pfam13868  213 EEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRL 252
Pro-rich_NTERM NF040555
AAA family ATPase Pro-rich N-terminal domain; This HMM describes an extremely rich N-terminal ...
1727-1805 6.32e-04

AAA family ATPase Pro-rich N-terminal domain; This HMM describes an extremely rich N-terminal domain that is well-conserved for a family of AAA family ATPases seen in Streptomyces. The HMM was built to support correct structural annotation of this unusual, low-complexity domain.


Pssm-ID: 468532 [Multi-domain]  Cd Length: 93  Bit Score: 40.71  E-value: 6.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1727 ASGHHTTSAQALHHP----PHQGPPLFPSSAHPAVPPYPSQATHhttlGPGPQHQPSGTGP----HCPLPvtgphlqPQG 1798
Cdd:NF040555    16 GHGPAAGWSPAAHHPgpphPQGPAPVPPPAPGFPAPPGPQPGWH----PPAPQHAPAPPAPdttgHVQLP-------PGG 84

                   ....*..
gi 2464208148 1799 PNSIPTP 1805
Cdd:NF040555    85 PVPMPSP 91
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
561-652 2.77e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.45  E-value: 2.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  561 MESEEQIAERKRKMTREE--RKMEAILQAFARLEKREKRREQALERISTAKTEVKTECKDTqivsDAEVIQEQAKEENAS 638
Cdd:COG1579     94 LQKEIESLKRRISDLEDEilELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL----EAELEELEAEREELA 169
                           90
                   ....*....|....*...
gi 2464208148  639 KPTPAKV----NRTKQRK 652
Cdd:COG1579    170 AKIPPELlalyERIRKRK 187
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1463-1828 2.86e-03

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 42.69  E-value: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1463 GYLSPKPPSQQLGSPYRPHHSQSP-QVGTPQREPQRnfypaaqnlQANTQQATSGTLFTQTPSGQSSATYSQFNQQSLNS 1541
Cdd:pfam09606  157 GMMQPSSGQPGSGTPNQMGPNGGPgQGQAGGMNGGQ---------QGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANG 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1542 TAPPPPPPPPPSSYYQNQQPSanfqnynqlkGSLSQQTVFTSGPNQAlpgttsQQTVPGHHVTPGHFLPSQNPTIHHQTA 1621
Cdd:pfam09606  228 GMNPQQMGGAPNQVAMQQQQP----------QQQGQQSQLGMGINQM------QQMPQGVGGGAGQGGPGQPMGPPGQQP 291
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1622 AAVVPPPPPPPPAPGPHLVQQPNSHQQ---HSVAHVVGPVHAVTPGSHIHSQTAGHHLPppppppgpaphhhppphpsTG 1698
Cdd:pfam09606  292 GAMPNVMSIGDQNNYQQQQTRQQQQQQggnHPAAHQQQMNQSVGQGGQVVALGGLNHLE-------------------TW 352
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1699 LQGLQAQHQhvVNSAPPPPPPPPPSSVLASGHHTTSAQALHHPPHQGPPLFPSSAHPavppypsqathhttlgpGPQHQP 1778
Cdd:pfam09606  353 NPGNFGGLG--ANPMQRGQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGP-----------------GSQPPQ 413
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2464208148 1779 SGTGPHCPLPVTGPHLQPQ---GPNS---IPTPTASGFCPHPGSVALPHGVqGPQQ 1828
Cdd:pfam09606  414 SHPGGMIPSPALIPSPSPQmsqQPAQqrtIGQDSPGGSLNTPGQSAVNSPL-NPQE 468
KLF10_N cd21572
N-terminal domain of Kruppel-like factor 10; Kruppel-like factor 10 (KLF10; also known as ...
1731-1845 4.27e-03

N-terminal domain of Kruppel-like factor 10; Kruppel-like factor 10 (KLF10; also known as Krueppel-like factor 10; early growth response(EGR)-alpha/EGRA; TGFbeta inducible early gene-1/TIEG1) is a protein that in humans is encoded by the KLF10 gene. KLF10 was first identified in human osteoblasts and plays a role in mediating estrogen (E2) signaling in bone and skeletal homeostasis and a regulatory role in tumor formation and metastasis. It may also play a role in adipocyte differentiation and adipose tissue function. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved a-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF10 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF10.


Pssm-ID: 409241 [Multi-domain]  Cd Length: 245  Bit Score: 41.13  E-value: 4.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1731 HTTSAQALHHPPHQGPPLFPSSAHPAVPPYPSQAT---HHTTLGpgpqhQPSGTGPHCPLPVTGPHLQPQGPNSIPTPTA 1807
Cdd:cd21572     71 HPPSAATLHPPAAQPPEEQHLSAETAASQQRFQCTsviRHTADA-----QPCSCSSCPSSPSVVPSVPAGVAGVSPVPVY 145
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2464208148 1808 SGFCP----HPGSVALPHGVQGPQQASPVPGQIPIHRAQVPP 1845
Cdd:cd21572    146 CQILPvsssSTTVVAAQAPLPQPQQQAASPAQVFLMGGQVPK 187
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1743-1845 4.42e-03

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: 42.06  E-value: 4.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1743 HQGPPLFPSSAHPAVPPYPSQATHHTTLGPGPQHQPSGTGPHCPLPVTGPHLQPQGPNSIPTPTASGFCPHPGSVALPHG 1822
Cdd:pfam03154  168 QTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHP 247
                           90       100       110
                   ....*....|....*....|....*....|
gi 2464208148 1823 -VQG------PQQASPVPGQIPIHRAQVPP 1845
Cdd:pfam03154  248 pLQPmtqpppPSQVSPQPLPQPSLHGQMPP 277
 
Name Accession Description Interval E-value
SET_KMT2E cd19182
SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...
323-451 4.76e-91

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: 291.03  E-value: 4.76e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  323 TNNLLFKPPVESHIQKNKKILKSAKDLPPDALIIEYRGKFMLREQFEANGYFFKRPYPFVLFYSKFHGLEMCVDARTFGN 402
Cdd:cd19182      1 TSNLLFKPPVESHVQKNKKILKAAKDLPPDTLIIEYRGKFMLREQFEANGYFFKRPYPFVLFYSKFHGLEMCVDARTFGN 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2464208148  403 EARFIRRSCTPNAEVRHEIQDGTIHLYIYSIHSIPKGTEITIAFDFDYG 451
Cdd:cd19182     81 EARFIRRSCTPNAEVRHVIEDGTIHLYIYSIRSIPKGTEITIAFDFDYG 129
SET_SETD5 cd19181
SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...
334-472 1.33e-77

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: 253.39  E-value: 1.33e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  334 SHIQKNKKILKSAKDLPPDALIIEYRGKFMLREQFEANGYFFKRPYPFVLFYSKFHGLEMCVDARTFGNEARFIRRSCTP 413
Cdd:cd19181     12 TRVQKHRKILRAARDLALDTLIIEYRGKVMLRQQFEVNGHFFKRPYPFVLFYSKFNGVEMCVDARTFGNDARFIRRSCTP 91
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2464208148  414 NAEVRHEIQDGTIHLYIYSIHSIPKGTEITIAFDFDYGNCKYKVDCACLKENPECPVLK 472
Cdd:cd19181     92 NAEVRHMIADGMIHLCIYAVAAIAKDAEVTIAFDYEYSNCNYKVDCACHKGNRNCPVQK 150
SET_SETD5-like cd10529
SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...
325-450 1.81e-57

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: 194.80  E-value: 1.81e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  325 NLLFKPPVESHIQKNKKILKSAKDLPPDALIIEYRGKFMLREQFEANGYFFKRPYPFVLFYSKFHGLEMCVDARTFGNEA 404
Cdd:cd10529      1 RKLTSRTVEKVVGKNRKGLVATEDISPGEPILEYKGEVSLRSEFKEDNGFFKRPSPFVFFYDGFEGLPLCVDARKYGNEA 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2464208148  405 RFIRRSCTPNAEVRHEI-QDGTIHLYIYSIHSIPKGTEITIAFDFDY 450
Cdd:cd10529     81 RFIRRSCRPNAELRHVVvSNGELRLFIFALKDIRKGTEITIPFDYDY 127
PHD_MLL5 cd15550
PHD finger found in mixed lineage leukemia 5 (MLL5); MLL5 is a histone methyltransferase that ...
120-163 6.86e-31

PHD finger found in mixed lineage leukemia 5 (MLL5); MLL5 is a histone methyltransferase that plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. It contains a single plant homeodomain (PHD) finger followed by a catalytic SET domain. MLL5 can be recruited to E2F1-responsive promoters to stimulate H3K4 trimethylation and transcriptional activation by binding to the cell cycle regulator host cell factor (HCF-1), thereby facilitating the cell cycle G1 to S phase transition. It is also involved in mitotic fidelity and genomic integrity by modulating the stability of the chromosomal passenger complex (CPC) via the interaction with Borealin. Moreover, MLL5 is a component of a complex associated with retinoic acid receptor that requires GlcN Acylation of its SET domain in order to activate its histone lysine methyltransferase activity. It also participates in the camptothecin (CPT)-induced p53 activation. Furthermore, MLL5 indirectly regulates H3K4 methylation, represses cyclin A2 (CycA) expression, and promotes myogenic differentiation.


Pssm-ID: 277025 [Multi-domain]  Cd Length: 44  Bit Score: 115.88  E-value: 6.86e-31
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2464208148  120 RCICGFTHDDGYMICCDKCSVWQHIDCMGIDRQHIPDTYLCERC 163
Cdd:cd15550      1 RCICGFEHDDGFMICCDKCSVWQHGDCMGIDRENIPDSYLCEQC 44
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
343-452 5.76e-29

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: 113.20  E-value: 5.76e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148   343 LKSAKDLPPDALIIEYRGKFMLREQFEANGYFFKR--PYPFVLFYSKFHgleMCVDARTFGNEARFIRRSCTPNAEVRHE 420
Cdd:smart00317   15 VRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTdgAKAFYLFDIDSD---LCIDARRKGNLARFINHSCEPNCELLFV 91
                            90       100       110
                    ....*....|....*....|....*....|..
gi 2464208148   421 IQDGTIHLYIYSIHSIPKGTEITIAFDFDYGN 452
Cdd:smart00317   92 EVNGDDRIVIFALRDIKPGEELTIDYGSDYAN 123
SET_SpSET3-like cd19183
SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...
343-449 1.22e-19

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: 88.23  E-value: 1.22e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  343 LKSAKDLPPDALIIEYRGKFMLREQFEA---NGY-FFKRPYPFVLFYSKfhgLEMCVDARTFGNEARFIRRSCTPNAE-V 417
Cdd:cd19183     16 LFADRPIPAGDPIQELLGEIGLQSEYIAdpeNQYqILGAPKPHVFFHPQ---SPLYIDTRRSGSVARFIRRSCRPNAElV 92
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2464208148  418 RHEIQDGT-IHLYIYSIHSIPKGTEITIAFDFD 449
Cdd:cd19183     93 TVASDSGSvLKFVLYASRDISPGEEITIGWDWD 125
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
343-451 6.25e-17

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: 78.33  E-value: 6.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  343 LKSAKDLPPDALIIEYRGKFML-------REQFEANGYFFKRPYPFVLFYSKFHglEMCVDARTF--GNEARFIRRSCTP 413
Cdd:pfam00856    4 LFATEDIPKGEFIGEYVEVLLItkeeadkRELLYYDKLELRLWGPYLFTLDEDS--EYCIDARALyyGNWARFINHSCDP 81
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2464208148  414 NAEVRHEIQDGTIHLYIYSIHSIPKGTEITIafdfDYG 451
Cdd:pfam00856   82 NCEVRVVYVNGGPRIVIFALRDIKPGEELTI----DYG 115
PHD_MMD1_like cd15556
PHD finger found in Arabidopsis thaliana PHD finger protein MALE MEIOCYTE DEATH 1 (MMD1), PHD ...
121-163 1.20e-15

PHD finger found in Arabidopsis thaliana PHD finger protein MALE MEIOCYTE DEATH 1 (MMD1), PHD finger protein MALE STERILITY 1 (MS1), and similar proteins; MMD1 is a plant homeodomain (PHD) finger protein expressed in male meiocytes. It is encoded by the gene DUET, which is required for male meiotic chromosome organization and progression. MMD1 has been implicated in the regulation of gene expression during meiosis. The mmd1 mutation triggers cell death in male meiocytes. MS1 is a nuclear transcriptional activator that is important for tapetal development and pollen wall biosynthesis. It contains a Leu zipper-like domain and a PHD finger motif, both of which are essential for its function.


Pssm-ID: 277031 [Multi-domain]  Cd Length: 46  Bit Score: 72.41  E-value: 1.20e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2464208148  121 CICGFTHDDG-YMICCDKCSVWQHIDCMGI-DRQHIPDTYLCERC 163
Cdd:cd15556      2 CSCGTRDDDGeRMIACDVCEVWQHTRCVGIaDNEEPPDHFLCRRC 46
PHD_ASH1L cd15548
PHD finger found in histone-lysine N-methyltransferase ASH1L; ASH1L, also termed ASH1-like ...
120-163 5.86e-15

PHD finger found in histone-lysine N-methyltransferase ASH1L; ASH1L, also termed ASH1-like protein, or absent small and homeotic disks protein 1 homolog, or lysine N-methyltransferase 2H, is a protein belonging to the Trithorax family. It methylates Lys36 of histone H3 independently of transcriptional elongation to promote the establishment of Hox gene expression by counteracting Polycomb silencing. It can suppress interleukin-6 (IL-6), and tumor necrosis factor (TNF) production in Toll-like receptor (TLR)-triggered macrophages, and inflammatory autoimmune diseases by inducing the ubiquitin-editing enzyme A20. ASH1L contains an associated with SET domain (AWS), a SET domain, a post-SET domain, a bromodomain, a bromo-adjacent homology domain (BAH), and a plant homeodomain (PHD) finger.


Pssm-ID: 277023  Cd Length: 43  Bit Score: 70.19  E-value: 5.86e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2464208148  120 RCICGFTHDDGYMICCDKCSVWQHIDCMGIDRQhiPDTYLCERC 163
Cdd:cd15548      2 RCICGLYKDEGLMIQCEKCMVWQHCDCMGVNDD--VEHYLCEQC 43
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
346-451 1.70e-14

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 71.92  E-value: 1.70e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  346 AKDLPPDALIIEYRGKFMLREQFEANGYFFKRPYPFVLFYSKFHGlemcVDARTFGNEARFIRRSCTPNAEVRHEiqDGT 425
Cdd:COG2940     23 TRDIPKGTLIGEYPGEVITWAEAERREPHKEPLHTYLFELDDDGV----IDGALGGNPARFINHSCDPNCEADEE--DGR 96
                           90       100
                   ....*....|....*....|....*.
gi 2464208148  426 IhlYIYSIHSIPKGTEITIafdfDYG 451
Cdd:COG2940     97 I--FIVALRDIAAGEELTY----DYG 116
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
343-465 5.11e-14

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: 70.75  E-value: 5.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  343 LKSAKDLPPDALIIEYRG--------KFMLREQFEANGYFFkrpYPFVLfyskfhGLEMCVDARTFGNEARFIRRSCTPN 414
Cdd:cd10531     14 VKAKEDIQKGEFIIEYVGevidkkefKERLDEYEELGKSNF---YILSL------SDDVVIDATRKGNLSRFINHSCEPN 84
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2464208148  415 AEVRHEIQDGTIHLYIYSIHSIPKGTEITiaFDFDYGNCKY-KVDCACLKEN 465
Cdd:cd10531     85 CETQKWIVNGEYRIGIFALRDIPAGEELT--FDYNFVNYNEaKQVCLCGAQN 134
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
346-451 3.17e-13

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: 68.14  E-value: 3.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  346 AKDLPPDALIIEYRGKFMLREQFEANGYFfkrpYPFVLFYSKFHGLEMCVDARTFGNEARFIRRSCTPNAEVRHEIQDGT 425
Cdd:cd10522     20 AETIAKGEFVGEYTGEVLDRWEEDRDSVY----HYDPLYPFDLNGDILVIDAGKKGNLTRFINHSDQPNLELIVRTLKGE 95
                           90       100
                   ....*....|....*....|....*.
gi 2464208148  426 IHLYIYSIHSIPKGTEITIafdfDYG 451
Cdd:cd10522     96 QHIGFVAIRDIKPGEELFI----SYG 117
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
120-166 1.73e-12

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


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 63.67  E-value: 1.73e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2464208148  120 RC-ICGFTHDDGYMICCDKCSVWQHIDCMGI---DRQHIPDTYLCERCQPR 166
Cdd:pfam00628    1 YCaVCGKSDDGGELVQCDGCDDWFHLACLGPpldPAEIPSGEWLCPECKPK 51
PHD_Bye1p_SIZ1_like cd15570
PHD domain found in Saccharomyces cerevisiae bypass of ESS1 protein 1 (Bye1p), the E3 Sumo ...
120-163 2.58e-12

PHD domain found in Saccharomyces cerevisiae bypass of ESS1 protein 1 (Bye1p), the E3 Sumo Ligase SIZ1, and similar proteins; Yeast Bye1p is a nuclear transcription factor with a domain resembling the central domain in the transcription elongation factor TFIIS and plays an inhibitory role during transcription elongation. It functions as a multicopy suppressor of Ess1, a peptidyl-prolyl cis-trans isomerase involved in proline isomerization of the C-terminal domain (CTD) of RNA polymerase II (Pol II). Bye1p contains an N-terminal plant homeodomain (PHD) finger, a central Pol II-binding TFIIS-like domain (TLD) domain, and a C-terminal Spen paralogue and orthologue C-terminal (SPOC) domain. The PHD domain binds to a histone H3 tail peptide containing trimethylated lysine 4 (H3K4me3). The TLD domain is responsible for the association with chromatin. Plant SIZ1 protein is a SUMO (small ubiquitin-related modifier) E3 ligase that facilitates conjugation of SUMO to substrate target proteins (sumoylation) and belongs to the protein inhibitor of activated STAT (PIAS) protein family. It negatively regulates abscisic acid (ABA) signaling, which is dependent on the bZIP transcripton factor ABI5. It also modulates plant growth and plays a role in drought stress response likely through the regulation of gene expression. SIZ1 functions as a floral repressor that not only represses the salicylic acid (SA)-dependent pathway, but also promotes FLOWERING LOCUS C (FLC) expression by repressing FLOWERING LOCUS D (FLD) activity through sumoylation. SIZ1 contains a PHD finger, which specifically binds methylated histone H3 at lysine 4 and arginine 2.


Pssm-ID: 277045  Cd Length: 50  Bit Score: 62.86  E-value: 2.58e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2464208148  120 RCICGFTHDDGYMICCDKCSVWQHIDCMGI------DRQHIPDTYLCERC 163
Cdd:cd15570      1 RCPCGSSMEDGSMIQCEGCKTWQHMDCVLIpdkpadGLPELPSKFYCELC 50
SET_SETD2 cd19172
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...
343-468 4.95e-12

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: 65.29  E-value: 4.95e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  343 LKSAKDLPPDALIIEYRGKFMLREQFEANgyffKRPYPFVL---FYskFHGL--EMCVDARTFGNEARFIRRSCTPNAEV 417
Cdd:cd19172     16 LRAAEDLPKGTFVIEYVGEVLDEKEFKRR----MKEYAREGnrhYY--FMALksDEIIDATKKGNLSRFINHSCEPNCET 89
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2464208148  418 RHEIQDGTIHLYIYSIHSIPKGTEITIAFDFD-YGncKYKVDCAClkENPEC 468
Cdd:cd19172     90 QKWTVNGELRVGFFAKRDIPAGEELTFDYQFErYG--KEAQKCYC--GSPNC 137
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
121-163 4.29e-11

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: 59.53  E-value: 4.29e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 2464208148   121 CICGFTHDDGYMICCDKCSVWQHIDCMGI-DRQHIPD-TYLCERC 163
Cdd:smart00249    3 SVCGKPDDGGELLQCDGCDRWYHQTCLGPpLLEEEPDgKWYCPKC 47
PHD_Hop1p_like cd15558
PHD finger found in Schizosaccharomyces pombe meiosis-specific protein hop1 (Hop1p) and ...
120-163 4.91e-11

PHD finger found in Schizosaccharomyces pombe meiosis-specific protein hop1 (Hop1p) and similar proteins; Fission yeast Hop1p, also termed linear element-associated protein hop1, is an S. pombe homolog of the synaptonemal complex (SC)-associated protein Hop1 in Saccharomyces cerevisiae. In contrast to S. cerevisiae, S. pombe forms thin threads, known as linear elements (LinEs), in meiotic nuclei, instead of a canonical synaptonemal complex. LinEs contain Rec10 protein and are evolutionary relics of SC axial elements. Fission yeast Hop1p is a linear element (LinE)-associated protein. It also associates with Rec10, which plays a role in recruiting the recombination machinery to chromatin. Hop1p contains an N-terminal HORMA (for Hop1p, Rev7p, and MAD2) domain and a C-terminal plant homeodomain (PHD) finger.


Pssm-ID: 277033  Cd Length: 47  Bit Score: 59.38  E-value: 4.91e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2464208148  120 RCICGFTHDDGYMICCDKCSVWQHIDCMG---IDRQHIPDTYLCERC 163
Cdd:cd15558      1 RCECGDWGEDGAMIQCAFCDTWQHLLCYGfesAKDPRIPDIHVCYRC 47
PHD_PHF3_like cd15552
PHD finger found in PHD finger protein 3 (PHF3), and death-inducer obliterator variants Dido1, ...
121-163 6.77e-11

PHD finger found in PHD finger protein 3 (PHF3), and death-inducer obliterator variants Dido1, Dido2, and Dido3; PHF3 is a human homolog of yeast protein bypass of Ess1 (Bye1), a nuclear protein with a domain resembling the central domain in the transcription elongation factor TFIIS. It is ubiquitously expressed in normal tissues including brain, but its expression is significantly reduced or lost in glioblastomas. PHF3 contains an N-terminal plant homeodomain (PHD) finger, a central RNA polymerase II (Pol II)-binding TFIIS-like domain (TLD) domain, and a C-terminal Spen paralogue and orthologue C-terminal (SPOC) domain. This family also includes Dido gene encoding three alternative splicing variants (Dido1, 2, and 3), which have been implicated in a number of cellular processes such as apoptosis and chromosomal segregation, particularly in the hematopoietic system. Dido1 is important for maintaining embryonic stem (ES) cells and directly regulates the expression of pluripotency factors. It is the shortest isoform that contains only a highly conserved PHD finger responsible for the binding of histone H3 with a higher affinity for trimethylated lysine4 (H3K4me3). Gene Dido1 is a Bone morphogenetic protein (BMP) target gene and promotes BMP-induced melanoma progression. It also triggers apoptosis after nuclear translocation and caspase upregulation. Dido3 is the largest isoform and is ubiquitously expressed in all human tissues. It is dispensable for ES cell self-renewal and pluripotency, but is involved in the maintenance of stem cell genomic stability and tumorigenesis. Dido3 contains a PHD finger, a transcription elongation factor S-II subunit M (TFSIIM) domain, a SPOC module, and a long C-terminal region (CT) of unknown homology.


Pssm-ID: 277027  Cd Length: 50  Bit Score: 58.95  E-value: 6.77e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2464208148  121 CICGFTHDDGYMICCDKCSVWQHIDCMGIDRQHIPD------TYLCERC 163
Cdd:cd15552      2 CICRKPHNNRFMICCDRCEEWFHGDCVGITEAQGKEmeenieEYVCPKC 50
PHD_PHF20L1 cd15633
PHD finger found in PHD finger protein 20-like protein 1 (P20L1); P20L1 is an active malignant ...
120-164 8.14e-11

PHD finger found in PHD finger protein 20-like protein 1 (P20L1); P20L1 is an active malignant brain tumor (MBT) domain-containing protein that binds to monomethylated lysine 142 on DNA (Cytosine-5) Methyltransferase 1 (DNMT1) (DNMT1K142me1) and colocalizes at the perinucleolar space in a SET7-dependent manner. Its MBT domain reads and controls enzyme levels of methylated DNMT1 in cells, thus representing a novel antagonist of DNMT1 proteasomal degradation. In addition to the MBT domain, PHF20L1 also contains two Tudor domains, a plant homeodomain (PHD) finger and the putative DNA-binding domains, AT hook and Cys2His2-type zinc finger.


Pssm-ID: 277103  Cd Length: 46  Bit Score: 58.88  E-value: 8.14e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2464208148  120 RCICGFTHDDGYMICCDKCSVWQHIDCMGIDRQHIPDTYLCERCQ 164
Cdd:cd15633      1 RCICEMDEENGFMIQCEECLCWQHSVCMGLLEESIPEQYICYICR 45
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
343-465 8.59e-11

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: 61.54  E-value: 8.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  343 LKSAKDLPPDALIIEYRGKFMLREQFEANgyfFKRPYpfvLFYSKFHGLEMC----VDARTFGNEARFIRRSCTPNAEVR 418
Cdd:cd19174     14 VRTKEPIKAGQFIIEYVGEVVSEQEFRRR---MIEQY---HNHSHHYCLNLDsgmvIDGYRMGNEARFVNHSCDPNCEMQ 87
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2464208148  419 HEIQDGTIHLYIYSIHSIPKGTEITIAFDFDYGNCKYKVDCACLKEN 465
Cdd:cd19174     88 KWSVNGVYRIGLFALKDIPAGEELTYDYNFHSFNVEKQQPCKCGSPN 134
SET_ASHR3-like cd19175
SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...
343-461 1.23e-10

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: 61.28  E-value: 1.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  343 LKSAKDLPPDALIIEYRGK-----------FMLREQFEANgyffkrpypfvlFYSKFHGLEMCVDARTFGNEARFIRRSC 411
Cdd:cd19175     14 LVADEDINAGEFIIEYVGEviddktceerlWDMKHKGEKN------------FYMCEIDKDMVIDATFKGNLSRFINHSC 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2464208148  412 TPNAEVRHEIQDGTIHLYIYSIHSIPKGTEITIAFDF-DYGNckyKVDCAC 461
Cdd:cd19175     82 DPNCELQKWQVDGETRIGVFAIRDIKKGEELTYDYQFvQFGA---DQDCHC 129
PHD_PHF20_like cd15549
PHD finger found in PHD finger protein 20 (PHF20) and PHD finger protein 20-like protein 1 ...
120-163 2.72e-10

PHD finger found in PHD finger protein 20 (PHF20) and PHD finger protein 20-like protein 1 (P20L1); PHF20, also termed Glioma-expressed antigen 2, or hepatocellular carcinoma-associated antigen 58, or novel zinc finger protein, or transcription factor TZP (referring to Tudor and zinc finger domain containing protein), is a regulator of NF-kappaB activation by disrupting recruitment of PP2A to p65. It also functions as a transcription factor that binds Akt and plays a role in Akt cell survival/growth signaling. Moreover, it transcriptionally regulates p53. The phosphorylation of PHF20 on Ser291 mediated by protein kinase B (PKB) is essential in tumorigenesis via the regulation of p53 mediated signaling. P20L1 is an active malignant brain tumor (MBT) domain-containing protein that binds to monomethylated lysine 142 on DNA (Cytosine-5) Methyltransferase 1 (DNMT1) (DNMT1K142me1) and colocalizes at the perinucleolar space in a SET7-dependent manner. Its MBT domain reads and controls enzyme levels of methylated DNMT1 in cells, thus representing a novel antagonist of DNMT1 proteasomal degradation. Both PHF20 and PHF20L1 contain an N-terminal MBT domain, two Tudor domains, a plant homeodomain (PHD) finger and the putative DNA-binding domains, AT hook and Cys2His2-type zinc finger.


Pssm-ID: 277024  Cd Length: 45  Bit Score: 57.10  E-value: 2.72e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2464208148  120 RCICGFTHDDGYMICCDKCSVWQHIDCMGIDRQ-HIPDTYLCERC 163
Cdd:cd15549      1 HCICGVNEENGLMIQCELCLCWQHGVCMGIEEEeSVPERYVCYVC 45
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
403-451 5.78e-10

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: 56.88  E-value: 5.78e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2464208148  403 EARFIRRSCTPNAEVRHEIQDGTIHLYIYSIHSIPKGTEITiafdFDYG 451
Cdd:cd08161     28 LARFINHSCEPNCEFEEVYVGGKPRVFIVALRDIKAGEELT----VDYG 72
SET_SETDB-like cd10538
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
343-451 1.11e-09

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: 60.46  E-value: 1.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  343 LKSAKDLPPDALIIEYRGKFMLREQFEANGYFFKRP---YPFVL---FYSKFHGLEMCVDARTFGNEARFIRRSCTPN-- 414
Cdd:cd10538    103 VRSLEFIPKGSFVCEYVGEVITTSEADRRGKIYDKSggsYLFDLdefSDSDGDGEELCVDATFCGNVSRFINHSCDPNlf 182
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2464208148  415 -AEVRHEIQDGTIH-LYIYSIHSIPKGTEITiafdFDYG 451
Cdd:cd10538    183 pFNVVIDHDDLRYPrIALFATRDILPGEELT----FDYG 217
PHD_PHF20 cd15634
PHD finger found in PHD finger protein 20 (PHF20); PHF20, also termed Glioma-expressed antigen ...
120-163 1.23e-09

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


Pssm-ID: 277104  Cd Length: 44  Bit Score: 55.34  E-value: 1.23e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2464208148  120 RCICGFTHDDGYMICCDKCSVWQHIDCMGIDRQHIPDTYLCERC 163
Cdd:cd15634      1 RCICEVQEENDFMIQCEECLCWQHGVCMGLLEDNVPEKYTCYIC 44
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
343-461 8.13e-09

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: 56.28  E-value: 8.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  343 LKSAKDLPPDALIIEYRGKfMLREQFeANgyffKRPypfVLFYSKFHGLEM-------CVDARTFGNEARFIRRSCTPN- 414
Cdd:cd19171     28 LYAARDIEKHTMVIEYIGE-IIRNEV-AN----RRE---KIYESQNRGIYMfridndwVIDATMTGGPARYINHSCNPNc 98
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2464208148  415 -AEVRHeiQDGTIHLYIYSIHSIPKGTEITIAFDFDYGNCKYKVDCAC 461
Cdd:cd19171     99 vAEVVT--FDKEKKIIIISNRRIAKGEELTYDYKFDFEDDQHKIPCLC 144
SET_SETD1-like cd10518
SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...
345-468 1.21e-08

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: 55.68  E-value: 1.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  345 SAKDLPPDALIIEYRGKFM------LREQ-FEANG----YFFKrpypfvlfYSKFHglemCVDArTF-GNEARFIRRSCT 412
Cdd:cd10518     30 AKRPIAAGEMVIEYVGEVIrpivadKREKrYDEEGgggtYMFR--------IDEDL----VIDA-TKkGNIARFINHSCD 96
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2464208148  413 PNAEVRHEIQDGTIHLYIYSIHSIPKGTEITIAFDFDYGNCKyKVDCAClkENPEC 468
Cdd:cd10518     97 PNCYAKIITVDGEKHIVIFAKRDIAPGEELTYDYKFPIEDEE-KIPCLC--GAPNC 149
SET_KMT2A cd19206
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...
347-461 5.06e-08

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: 54.26  E-value: 5.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  347 KDLPPDALIIEYRGKFMLREQFEANGYFFKrpypfvlfySKFHGLEM-------CVDARTFGNEARFIRRSCTPNAEVRH 419
Cdd:cd19206     32 RNIDAGEMVIEYSGNVIRSILTDKREKYYD---------SKGIGCYMfriddseVVDATMHGNAARFINHSCEPNCYSRV 102
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2464208148  420 EIQDGTIHLYIYSIHSIPKGTEITIAFDFDYGNCKYKVDCAC 461
Cdd:cd19206    103 INIDGQKHIVIFAMRKIYRGEELTYDYKFPIEDASNKLPCNC 144
SET_SETD1 cd19169
SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...
340-465 5.85e-08

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: 53.88  E-value: 5.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  340 KKILKSAK------------DLPPDALIIEYRGKFM------LRE-QFEANG----YFFKRPYPFVLfyskfhglemcvD 396
Cdd:cd19169     12 KKQLKFAKsrihdwglfalePIAADEMVIEYVGQVIrqsvadEREkRYEAIGigssYLFRVDDDTII------------D 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2464208148  397 ARTFGNEARFIRRSCTPNAEVRHEIQDGTIHLYIYSIHSIPKGTEITIAFDFDYGNckYKVDCACLKEN 465
Cdd:cd19169     80 ATKCGNLARFINHSCNPNCYAKIITVESQKKIVIYSKRPIAVNEEITYDYKFPIED--EKIPCLCGAPQ 146
SET_KMT2D cd19209
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...
343-461 7.70e-08

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: 53.55  E-value: 7.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  343 LKSAKDLPPDALIIEYRGKFMLREQFEANGYFFKRPYPFVLFYSKFHglEMCVDARTFGNEARFIRRSCTPNAEVRHEIQ 422
Cdd:cd19209     30 LYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINN--EHVIDATLTGGPARYINHSCAPNCVAEVVTF 107
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2464208148  423 DGTIHLYIYSIHSIPKGTEITIAFDFDYGNCKYKVDCAC 461
Cdd:cd19209    108 DKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIPCHC 146
SET_KMT2A_2B cd19170
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...
343-461 1.55e-07

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: 52.78  E-value: 1.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  343 LKSAKDLPPDALIIEYRGKFM------LREQF-EANG---YFFKRPYPFVlfyskfhglemcVDARTFGNEARFIRRSCT 412
Cdd:cd19170     28 LFCKRNIDAGEMVIEYAGEVIrsvltdKREKYyESKGigcYMFRIDDDEV------------VDATMHGNAARFINHSCE 95
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2464208148  413 PNAEVRHEIQDGTIHLYIYSIHSIPKGTEITIAFDFDYGNCkyKVDCAC 461
Cdd:cd19170     96 PNCYSRVVNIDGKKHIVIFALRRILRGEELTYDYKFPIEDV--KIPCTC 142
SET_NSD3 cd19212
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
395-465 3.38e-07

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: 51.46  E-value: 3.38e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2464208148  395 VDARTFGNEARFIRRSCTPNAEVRHEIQDGTIHLYIYSIHSIPKGTEITIAFDFD-YGNCKYKvdCACLKEN 465
Cdd:cd19212     67 IDAGPKGNYSRFMNHSCNPNCETQKWTVNGDVRVGLFALCDIPAGMELTFNYNLDcLGNGRTE--CHCGADN 136
SET_SUV39H cd10542
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
343-450 3.54e-07

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: 53.45  E-value: 3.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  343 LKSAKDLPPDALIIEYRGKFMLREQFEANGYFF---KRPYPFVLFYSKFHGlEMCVDARTFGNEARFIRRSCTPNAEVRH 419
Cdd:cd10542    102 VKTLEDIKKGTFVMEYVGEIITSEEAERRGKIYdanGRTYLFDLDYNDDDC-EYTVDAAYYGNISHFINHSCDPNLAVYA 180
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2464208148  420 ---EIQDGTI-HLYIYSIHSIPKGTEITiafdFDY 450
Cdd:cd10542    181 vwiNHLDPRLpRIAFFAKRDIKAGEELT----FDY 211
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
121-163 3.64e-07

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: 48.47  E-value: 3.64e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2464208148  121 CICGFTHDD-GYMICCDKCSVWQHIDCMGID--RQHIPDTYLCERC 163
Cdd:cd15489      3 IVCGKGGDLgGELLQCDGCGKWFHADCLGPPlsSFVPNGKWICPVC 48
PHD_DIDO1_like cd15639
PHD finger found in death-inducer obliterator variants Dido1, Dido2, and Dido3; This family ...
121-163 4.92e-07

PHD finger found in death-inducer obliterator variants Dido1, Dido2, and Dido3; This family includes three alternative splicing variants (Dido1, 2, and 3) encoded by the Dido gene, which have been implicated in a number of cellular processes such as apoptosis and chromosomal segregation, particularly in the hematopoietic system. Dido1, also termed DIO-1, or death-associated transcription factor 1 (DATF-1), is important for maintaining embryonic stem (ES) cells and directly regulates the expression of pluripotency factors. It is the shortest isoform that contains only a highly conserved plant homeodomain (PHD) finger responsible for the binding of histone H3 with a higher affinity for trimethylated lysine 4 (H3K4me3). Gene Dido is a Bonemorphogenetic protein (BMP) target gene, which promotes BMP-induced melanoma progression. It also triggers apoptosis after nuclear translocation and caspase upregulation. Dido3 is the largest isoform ubiquitously expressed in all human tissues. It is dispensable for ES cell self-renewal and pluripotency, but involved in the maintenance of stem cell genomic stability and tumorigenesis. Dido3 contains a PHD finger, a transcription elongation factor S-II subunit M (TFSIIM) domain, aspen paralog and ortholog (SPOC) module, and a long C-terminal region (CT) of unknown homology. Its PHD finger interacts with H3K4me3.


Pssm-ID: 277109  Cd Length: 54  Bit Score: 48.04  E-value: 4.92e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2464208148  121 CICGFTHDDGYMICCDKCSVWQHIDCMGIDR------QHIPDTYLCERC 163
Cdd:cd15639      6 CICRQPHNNRFMICCDRCEEWFHGDCVGITEargrllERNGEDYICPNC 54
PHD_PHF13 cd15632
PHD finger found in PHD finger protein 13 (PHF13); PHF13, also termed survival time-associated ...
121-164 5.21e-07

PHD finger found in PHD finger protein 13 (PHF13); PHF13, also termed survival time-associated PHD finger protein in ovarian cancer 1 (SPOC1), is a novel plant homeodomain (PHD) finger-containing protein that shows strong expression in spermatogonia and ovarian cancer cells, modulates chromatin structure and mitotic chromosome condensation, and is important for proper cell division. It is also required for spermatogonial stem cell differentiation and sustained spermatogenesis. The overexpression of PHF13 associates with unresectable carcinomas and shorter survival in ovarian cancer.


Pssm-ID: 277102  Cd Length: 47  Bit Score: 48.11  E-value: 5.21e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2464208148  121 CICGFTHDDGYMICCDKCSVWQHIDCMGIDRQHIPDTYLCERCQ 164
Cdd:cd15632      4 CFCMKPFAGRPMIECNECHTWIHLSCAKIRKSNVPEVYVCQKCR 47
PHD_TCF19_like cd15517
PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and ...
122-163 1.18e-06

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


Pssm-ID: 276992 [Multi-domain]  Cd Length: 49  Bit Score: 47.16  E-value: 1.18e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2464208148  122 ICG-FTH-DDGYMICCDKCSVWQHIDCMGID--RQHIPDTYLCERC 163
Cdd:cd15517      4 ICNlETAaVDELWVQCDGCDKWFHQFCLGLSneRYADEDKFKCPNC 49
SET_KMT2B cd19207
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...
395-461 1.99e-06

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: 49.64  E-value: 1.99e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2464208148  395 VDARTFGNEARFIRRSCTPNAEVRHEIQDGTIHLYIYSIHSIPKGTEITIAFDFDYGNCKYKVDCAC 461
Cdd:cd19207     78 VDATMHGNAARFINHSCEPNCYSRVIHVEGQKHIVIFALRKIYRGEELTYDYKFPIEDASNKLPCNC 144
PHD_PHF23 cd15631
PHD finger found in PHD finger protein 23 (PHF23); PHF23, also termed PHD-containing protein ...
121-163 2.23e-06

PHD finger found in PHD finger protein 23 (PHF23); PHF23, also termed PHD-containing protein JUNE-1, is a hypothetical protein with a plant homeodomain (PHD) finger. It is encoded by gene PHF23 that acts as a candidate fusion partner for the nucleoporin gene NUP98. The NUP98-PHF23 fusion results from a cryptic translocation t(11;17)(p15;p13) in acute myeloid leukemia (AML).


Pssm-ID: 277101  Cd Length: 44  Bit Score: 46.06  E-value: 2.23e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2464208148  121 CICGFTHDDGYMICCDKCSVWQHIDCMGIDRQHIPDTYLCERC 163
Cdd:cd15631      2 CYCGKPFAGRPMIECSQCGTWIHLSCAKIKKSNVPDFFYCQKC 44
SET_NSD2 cd19211
SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...
343-465 2.29e-06

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: 48.83  E-value: 2.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  343 LKSAKDLPPDALIIEYRGKFMLREQFEANgYFFKRPYPFVLFYSKFHGLEMCVDARTFGNEARFIRRSCTPNAEVRHEIQ 422
Cdd:cd19211     16 LIAKRDIKKGEFVNEYVGELIDEEECMAR-IKHAHENDITHFYMLTIDKDRIIDAGPKGNYSRFMNHSCQPNCETQKWTV 94
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2464208148  423 DGTIHLYIYSIHSIPKGTEITIAFDFD-YGNckYKVDCACLKEN 465
Cdd:cd19211     95 NGDTRVGLFAVCDIPAGTELTFNYNLDcLGN--EKTVCRCGAPN 136
PHD_PHF13_like cd15546
PHD finger found in PHD finger proteins PHF13 and PHF23; PHF13, also termed survival ...
121-163 2.55e-06

PHD finger found in PHD finger proteins PHF13 and PHF23; PHF13, also termed survival time-associated PHD finger protein in ovarian cancer 1 (SPOC1), is a novel plant homeodomain (PHD) finger-containing protein that shows strong expression in spermatogonia and ovarian cancer cells, modulates chromatin structure and mitotic chromosome condensation, and is important for proper cell division. It is also required for spermatogonial stem cell differentiation and sustained spermatogenesis. The overexpression of PHF13 associates with unresectable carcinomas and shorter survival in ovarian cancer. PHF23, also termed PHD-containing protein JUNE-1, is a hypothetical protein with a PHD finger. It is encoded by gene PHF23 that acts as a candidate fusion partner for the nucleoporin gene NUP98. The NUP98-PHF23 fusion results from a cryptic translocation t(11;17)(p15;p13) in acute myeloid leukemia (AML).


Pssm-ID: 277021  Cd Length: 44  Bit Score: 45.90  E-value: 2.55e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2464208148  121 CICGFTHDDGYMICCDKCSVWQHIDCMGIDRQHIPDTYLCERC 163
Cdd:cd15546      2 CFCGKPFAGRPMIECSECLTWIHLSCAKIRKNNVPEVFICQKC 44
SET_NSD cd19173
SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...
395-465 3.10e-06

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: 48.47  E-value: 3.10e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2464208148  395 VDARTFGNEARFIRRSCTPNAEVRHEIQDGTIHLYIYSIHSIPKGTEITIAFDFD-YGNCKYKvdCACLKEN 465
Cdd:cd19173     67 IDAGPKGNLSRFMNHSCQPNCETQKWTVNGDTRVGLFAVRDIPAGEELTFNYNLDcLGNEKKV--CRCGAPN 136
PHD2_3_BPTF cd15560
PHD finger 2 and 3 found in bromodomain and PHD finger-containing transcription factor (BPTF); ...
121-163 3.47e-06

PHD finger 2 and 3 found in bromodomain and PHD finger-containing transcription factor (BPTF); BPTF, also termed nucleosome-remodeling factor subunit BPTF, or fetal Alz-50 clone 1 protein (FAC1), or fetal Alzheimer antigen, functions as a transcriptional regulator that exhibits altered expression and subcellular localization during neuronal development and neurodegenerative diseases such as Alzheimer's disease. It interacts with the human orthologue of the Kelch-like Ech-associated protein (Keap1). Its function and subcellular localization can be regulated by Keap1. Moreover, BPTF is a novel DNA-binding protein that recognizes the DNA sequence CACAACAC and represses transcription through this site in a phosphorylation-dependent manner. Furthermore, BPTF interacts with the Myc-associated zinc finger protein (ZF87/MAZ) and alters its transcriptional activity, which has been implicated in gene regulation in neurodegeneration. Some family members contain two or three plant homeodomain (PHD) fingers, which may be involved in complex formation with histone H3 trimethylated at K4 (H3K4me3). This family corresponds to the second and third PHD fingers.


Pssm-ID: 277035  Cd Length: 47  Bit Score: 45.41  E-value: 3.47e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2464208148  121 CICGFTHDDG-YMICCDKCSVWQHIDCMGIDRQHIP--DTYLCERC 163
Cdd:cd15560      2 CICRTPYDESqFYIGCDRCQDWFHGRCVGILQSEAEkiDEYVCPQC 47
PHD_SPP1 cd16039
PHD finger found in Set1 complex component SPP1; Set1C component SPP1, also called COMPASS ...
121-163 3.65e-06

PHD finger found in Set1 complex component SPP1; Set1C component SPP1, also called COMPASS component Spp1, or Complex proteins associated with set1 protein Spp1, or Suppressor of PRP protein 1, is a component of the COMPASS complex that links histone methylation to initiation of meiotic recombination. It induces double-strand break (DSB) formation by tethering to recombinationally cold regions. SPP1 interacts with H3K4me3 and Mer2, a protein required for DSB formation, to promote recruitment of potential meiotic DSB sites to the chromosomal axis. SPP1 contains a PHD finger, a zinc binding motif.


Pssm-ID: 277186  Cd Length: 46  Bit Score: 45.55  E-value: 3.65e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2464208148  121 CICGFTHDDGYMICCDKCSVWQHIDCMGIDRQ--HIPDTYLCERC 163
Cdd:cd16039      2 CICQKPDDGRWMIACDGCDEWYHFTCVNIPEAdvELVDSFFCPPC 46
SET_SET1 cd20072
SET domain (including post-SET domain) found in catalytic component of the Saccharomyces ...
336-461 5.82e-06

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: 47.80  E-value: 5.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  336 IQKNKKILKSAK------------DLPPDALIIEYRGKFM------LRE-QFEANG----YFFKRPYPFVlfyskfhgle 392
Cdd:cd20072      8 LKKRKKQLKFARsaihnwglyameNISAKDMVIEYVGEVIrqqvadEREkRYLRQGigssYLFRIDDDTV---------- 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2464208148  393 mcVDARTFGNEARFIRRSCTPNAEVRHEIQDGTIHLYIYSIHSIPKGTEITiaFDFDYGNCKYKVDCAC 461
Cdd:cd20072     78 --VDATKKGNIARFINHCCDPNCTAKIIKVEGEKRIVIYAKRDIAAGEELT--YDYKFPREEDKIPCLC 142
PHD_PHF2_like cd15554
PHD finger found in PHF2, PHF8 and KDM7; This family includes PHF2, PHF8, KDM7, and similar ...
121-163 6.27e-06

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


Pssm-ID: 277029  Cd Length: 47  Bit Score: 44.68  E-value: 6.27e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2464208148  121 CICGFTHDDG-YMICCDKCSVWQHIDCMGIDRQHIPD--TYLCERC 163
Cdd:cd15554      2 CICRQPYDVTrFMIECDVCKDWFHGSCVGVEEHQANDieRYHCPNC 47
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
343-468 1.25e-05

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: 46.84  E-value: 1.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  343 LKSAKDLPPDALIIEYRGKFMLREQFEANgYFFKRPYPFVLFYSKFHGLEMCVDARTFGNEARFIRRSCTPNAEVRHEIQ 422
Cdd:cd19210     16 LRCKTDIKKGEFVNEYVGELIDEEECRAR-IRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMNHCCQPNCETQKWTV 94
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2464208148  423 DGTIHLYIYSIHSIPKGTEITIAFDFD-YGNCKYKVDCAClkenPEC 468
Cdd:cd19210     95 NGDTRVGLFALCDIKAGTELTFNYNLEcLGNGKTVCKCGA----PNC 137
SET_EZH cd10519
SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...
392-451 1.73e-05

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: 45.70  E-value: 1.73e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  392 EMCVDARTFGNEARFIRRSCTPNAEVRHEIQDGTIHLYIYSIHSIPKGTEITiafdFDYG 451
Cdd:cd10519     61 QFVVDATRKGNKIRFANHSSNPNCYAKVMMVNGDHRIGIFAKRDIEAGEELF----FDYG 116
PHD_SHPRH cd15547
PHD finger found in E3 ubiquitin-protein ligase SHPRH; SHPRH, also termed SNF2, histone-linker, ...
121-163 2.02e-05

PHD finger found in E3 ubiquitin-protein ligase SHPRH; SHPRH, also termed SNF2, histone-linker, PHD and RING finger domain-containing helicase, belongs to the SWI2/SNF2 family of ATP-dependent chromatin remodeling enzymes, containing the Cys3HisCys4 RING-finger characteristic of E3 ubiquitin ligases. It plays a key role in the error-free branch of DNA damage tolerance. As functional homologs of Saccharomyces cerevisiae Rad5, SHPRH and its closely-related protein, helicase like transcription factor (HLTF), act as ubiquitin ligases that cooperatively mediate Ubc13-Mms2-dependent polyubiquitination of proliferating cell nuclear antigen (PCNA) and maintain genomic stability. SHPRH contains a SNF2 domain, a H1.5 (linker histone H1 and H5) domain, a plant homeodomain (PHD) finger, a Cys3HisCys4 RING-finger, and a C-terminal helicase domain.


Pssm-ID: 277022 [Multi-domain]  Cd Length: 47  Bit Score: 43.55  E-value: 2.02e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2464208148  121 CICG--FTHDDGYMICCDKCSVWQHIDCMGIDRQHIP-DTYLCERC 163
Cdd:cd15547      2 CICGelDEIDNKHRVQCLKCGLWQHAECVNYDEESDKrEPYLCPHC 47
PHD_Cfp1 cd15553
PHD finger found in CXXC-type zinc finger protein 1 (Cfp1); Cfp1, also termed CpG-binding ...
121-163 2.06e-05

PHD finger found in CXXC-type zinc finger protein 1 (Cfp1); Cfp1, also termed CpG-binding protein, or PHD finger and CXXC domain-containing protein 1 (PCCX1), is a specificity factor that binds to unmethylated CpGs and links H3K4me3 with CpG islands (CGIs). It integrates both promoter CpG content and gene activity for accurate trimethylation of histone H3 Lys 4 (H3K4me3) deposition in embryonic stem cells. Moreover, Cfp1 is an essential component of the SETD1 histone H3K4 methyltransferase complex and functions as a critical regulator of histone methylation, cytosine methylation, cellular differentiation, and vertebrate development. Cfp1 contains a plant homeodomain (PHD) finger, a CXXC domain, and a CpG binding protein zinc finger C-terminal domain. Its CXXC domain selectively binds to non-methylated CpG islands, following by a preference for a guanosine nucleotide.


Pssm-ID: 277028  Cd Length: 46  Bit Score: 43.52  E-value: 2.06e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2464208148  121 CICGFTHDDGYMICCDKCSVWQHIDCMGI---DRQHIPDTYlCERC 163
Cdd:cd15553      2 CICRSSDISRFMIGCDNCEEWYHGDCINItekEAKAIKEWY-CQQC 46
Herpes_TAF50 pfam03326
Herpesvirus transcription activation factor (transactivator); This family includes EBV BRLF1 ...
1288-1524 2.41e-05

Herpesvirus transcription activation factor (transactivator); This family includes EBV BRLF1 and similar ORF 50 proteins from other herpesviruses.


Pssm-ID: 308764 [Multi-domain]  Cd Length: 568  Bit Score: 49.31  E-value: 2.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1288 VSCSPSHVQSSPSSHSNHIPQLQAKGPVPSFSELMEDPDPENPEPTTTNECPSPDTSQNTCKSPSKMSKPGSPGSVIPAQ 1367
Cdd:pfam03326  302 VSLFPSTATLVPIAGSTGVTEVVSYGHNSTSPSSTPCPSTAVTEADHQTEPEVPWIATAHQESDQRPIGPGPEKPTFLPP 381
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1368 AHGKIFTKPDPQWDSTVSASEAENGVhlkteLQQKQLSNTNQALSKNHPPQThvrnsseqlsqkLPSAPTKLHCPPSPHL 1447
Cdd:pfam03326  382 VGGKQFFQGLRDSRSTSFLTAPEATS-----AISDVFQGTEVCQPKRIRALH------------PPGSPSANRPLPSSLA 444
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1448 ENPpkSSTPHTPVqhGYLSPKPPSQQL-----GSPYRPHHSQSPQVGTPQREPQRNFYPAAQNLQANTQQATSGTLFTQT 1522
Cdd:pfam03326  445 PTP--TGPVHEPG--SSLTPATVPQPLdaapvATPEASHELQPPDEETPQPLDEDQALCGQQDASHPPPRGQLDELTTTL 520

                   ..
gi 2464208148 1523 PS 1524
Cdd:pfam03326  521 ES 522
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
391-451 2.75e-05

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: 47.40  E-value: 2.75e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2464208148  391 LEMCVDARTFGNEARFIRRSCTPN---AEVRHEIQDGTI-HLYIYSIHSIPKGTEITiafdFDYG 451
Cdd:cd10545    171 SEFTIDAGSFGNVARFINHSCSPNlfvQCVLYDHNDLRLpRVMLFAADNIPPLQELT----YDYG 231
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
1310-1502 3.15e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 48.92  E-value: 3.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1310 QAKGPVPSFSElmEDPD-----PENPEPTTTN-ECPSPDTSQNTCKSPSKMSKP----GSPGSVipaqAHGKIFTKPDPQ 1379
Cdd:PTZ00449   491 KSKKKLAPIEE--EDSDkhdepPEGPEASGLPpKAPGDKEGEEGEHEDSKESDEpkegGKPGET----KEGEVGKKPGPA 564
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1380 WDSTVSaseaengvhlKTELQQKQLSNTNQAlskNHPpqthvRNSSEQLSQKLPSAPTKLHCPPSPHLenPPKSSTPHTP 1459
Cdd:PTZ00449   565 KEHKPS----------KIPTLSKKPEFPKDP---KHP-----KDPEEPKKPKRPRSAQRPTRPKSPKL--PELLDIPKSP 624
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2464208148 1460 VQ-HGYLSPK--PPSQQLGSPYRPHHSQSPQVGTPQREPQRNFYPA 1502
Cdd:PTZ00449   625 KRpESPKSPKrpPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFDPK 670
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
383-461 4.91e-05

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: 44.68  E-value: 4.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  383 LFYSKFHGLEMCVDARTFGN----EARFIRRSCTPNAEVRHeiqDGTIHLYIYSIHSIPKGTEITIAFDFDYGN------ 452
Cdd:cd20071     31 LVSVPSNSFSLTDGLNEIGVglfpLASLLNHSCDPNAVVVF---DGNGTLRVRALRDIKAGEELTISYIDPLLPrterrr 107
                           90
                   ....*....|..
gi 2464208148  453 ---CKYKVDCAC 461
Cdd:cd20071    108 ellEKYGFTCSC 119
PHD_Ecm5p_Lid2p_like cd15518
PHD finger found in Saccharomyces cerevisiae extracellular matrix protein 5 (Ecm5p), ...
121-163 6.09e-05

PHD finger found in Saccharomyces cerevisiae extracellular matrix protein 5 (Ecm5p), Schizosaccharomyces pombe Lid2 complex component Lid2p, and similar proteins; The family includes Saccharomyces cerevisiae Ecm5p, Schizosaccharomyces pombe Lid2 complex component Lid2p, and similar proteins. Ecm5p is a JmjC domain-containing protein that directly removes histone lysine methylation via a hydroxylation reaction. It associates with the yeast Snt2p and Rpd3 deacetylase, which may play a role in regulating transcription in response to oxidative stress. Ecm5p promotes oxidative stress tolerance, while Snt2p ultimately decreases tolerance. Ecm5p contains an N-terminal ARID domain, a JmjC domain, and a C-terminal plant homeodomain (PHD) finger. Lid2p is a trimethyl H3K4 (H3K4me3) demethylase responsible for H3K4 hypomethylation in heterochromatin. It interacts with the histone lysine-9 methyltransferase, Clr4, through the Dos1/Clr8-Rik1 complex, and mediates H3K9 methylation and small RNA production. It also acts cooperatively with the histone modification enzymes Set1 and Lsd1 and plays an essential role in cross-talk between H3K4 and H3K9 methylation in euchromatin. Lid2p contains a JmjC domain, three PHD fingers and a JmjN domain. This model includes the second PHD finger of Lid2p.


Pssm-ID: 276993  Cd Length: 45  Bit Score: 41.95  E-value: 6.09e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2464208148  121 CICGfTHDDGYMICCDKCSVWQHIDCMGIDRQHIP--DTYLCERC 163
Cdd:cd15518      2 CFCR-QGEGGTMIECEICKEWYHVKCIKNGRWKLDddDKFVCPIC 45
SET_EHMT cd10543
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
343-464 8.53e-05

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: 46.18  E-value: 8.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  343 LKSAKDLPPDALIIEYRGKfmLREQFEANgyffKRPYPFVLFYSKFHGLEM-CVDARTFGNEARFIRRSCTPN---AEVR 418
Cdd:cd10543    105 VRALQDIPKGTFVCEYIGE--LISDSEAD----SREDDSYLFDLDNKDGETyCIDARRYGNISRFINHLCEPNlipVRVF 178
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2464208148  419 HEIQDGTI-HLYIYSIHSIPKGTEITiafdFDYGN----CKYK-VDCACLKE 464
Cdd:cd10543    179 VEHQDLRFpRIAFFASRDIKAGEELG----FDYGEkfwrIKGKyFTCRCGSP 226
SET_SETD8 cd10528
SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2. ...
341-451 9.50e-05

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: 44.10  E-value: 9.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  341 KILKSAKDLPPDALIIEYRGKFM------LREQF----EANGYFfkrpypfvLFYSKFHGLEMCVDARTF-GNEARFIRR 409
Cdd:cd10528     29 RGVIATRPFEKGDFVVEYHGDLItiteakKREALyakdPSTGCY--------MYYFQYKGKTYCVDATKEsGRLGRLINH 100
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2464208148  410 SCT-PNAEVRHEIQDGTIHLYIYSIHSIPKGTEITiafdFDYG 451
Cdd:cd10528    101 SKKkPNLKTKLLVIDGVPHLILVAKRDIKPGEELL----YDYG 139
PHD_KDM7 cd15640
PHD finger found in lysine-specific demethylase 7 (KDM7); KDM7, also termed JmjC ...
121-165 2.01e-04

PHD finger found in lysine-specific demethylase 7 (KDM7); KDM7, also termed JmjC domain-containing histone demethylation protein 1D (JHDM1D), or KIAA1718, is a dual histone demethylase that catalyzes demethylation of monomethylated and dimethylated H3K9 (H3K9me2/me1) and H3K27 (H3K27me2/me1), which functions as an eraser of silencing marks on chromatin during brain development. It also plays a tumor-suppressive role by regulating angiogenesis. KDM7 contains a plant homeodomain (PHD) that binds Lys4-trimethylated histone 3 (H3K4me3) and a jumonji domain that demethylates either H3K9me2 or H3K27me2.


Pssm-ID: 277110  Cd Length: 50  Bit Score: 40.74  E-value: 2.01e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2464208148  121 CICGFTHD-DGYMICCDKCSVWQHIDCMGIDRQHIPDT--YLCERCQP 165
Cdd:cd15640      2 CVCRQPYDvNRFMIECDICKDWFHGSCVQVEEHHAADIdlYHCPNCEV 49
PHA03247 PHA03247
large tegument protein UL36; Provisional
1740-1845 2.19e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 2.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1740 HPPHQ---GPPLFPSSAHPAVPPYPSQATHHTTLGPGPQHQPSGTGPHCPLPVTGPHLQPQGPnsiPTPTasgfcPHPGS 1816
Cdd:PHA03247  2880 RPPVRrlaRPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPP---LAPT-----TDPAG 2951
                           90       100       110
                   ....*....|....*....|....*....|
gi 2464208148 1817 VALPHG-VQGPQQASPVPGQIPIHRAQVPP 1845
Cdd:PHA03247  2952 AGEPSGaVPQPWLGALVPGRVAVPRFRVPQ 2981
SET_KMT2C cd19208
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) ...
343-461 3.16e-04

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: 43.08  E-value: 3.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  343 LKSAKDLPPDALIIEYRGKFMLREQFEANGYFFKRPYPFVLFYSKFHglEMCVDARTFGNEARFIRRSCTPNAEVRHEIQ 422
Cdd:cd19208     29 LYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRIDN--DHVIDATLTGGPARYINHSCAPNCVAEVVTF 106
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2464208148  423 DGTIHLYIYSIHSIPKGTEITIAFDFDYGNCKYKVDCAC 461
Cdd:cd19208    107 EKGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIPCHC 145
PHD_PHF2 cd15641
PHD finger found in lysine-specific demethylase PHF2; PHF2, also termed GRC5, or PHD finger ...
121-164 3.80e-04

PHD finger found in lysine-specific demethylase PHF2; PHF2, also termed GRC5, or PHD finger protein 2, is a histone lysine demethylase ubiquitously expressed in various tissues. It contains a plant homeodomain (PHD) finger and a JmjC domain and plays an important role in adipogenesis. The PHD finger domain can recognize trimethylated histone H3 lysine 4 (H3K4me3). PHF2 also has dimethylated histone H3 lysine 9(H3K9me2) demethylase activity and acts as a coactivator of several metabolism-related transcription factors. Moreover, it can demethylate ARID5B and further forms a complex with demethylated ARD5B to bind the promoter regions of target genes. The overexpression of PHF2 is involved in the progression of esophageal squamous cell carcinoma (ESCC).


Pssm-ID: 277111  Cd Length: 50  Bit Score: 40.00  E-value: 3.80e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2464208148  121 CICGFTHD-DGYMICCDKCSVWQHIDCMGIDRQHIP--DTYLCERCQ 164
Cdd:cd15641      2 CICRLPYDvTRFMIECDACKDWFHGSCVGVEEEEAPdiDIYHCPNCE 48
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
561-669 4.21e-04

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: 44.52  E-value: 4.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  561 MESEEQIAERKRKMTREERKMEAILQAFARL-EKREKRREQALERISTAKTEVKT-------ECKDTQIVSD---AEVIQ 629
Cdd:pfam13868  133 DEFNEEQAEWKELEKEEEREEDERILEYLKEkAEREEEREAEREEIEEEKEREIArlraqqeKAQDEKAERDelrAKLYQ 212
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2464208148  630 EQAKEENASKPTPAKVNRTKQRKSFSRSRTHIGQQRRRHR 669
Cdd:pfam13868  213 EEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRL 252
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
343-450 5.40e-04

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: 43.73  E-value: 5.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  343 LKSAKDLPPDALIIEYRGKFMLREQFEANGYFFKRPYPFVLFYSKFHGLEMCVDARTFGNEARFIRRSCTPNAEVRHEIQ 422
Cdd:cd10532     99 VKTLQKIKKNSFVMEYVGEVITSEEAERRGQFYDSKGITYLFDLDYESDEFTVDAARYGNVSHFVNHSCDPNLQVFNVFI 178
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2464208148  423 DG----TIHLYIYSIHSIPKGTEITiafdFDY 450
Cdd:cd10532    179 DNldtrLPRIALFSTRTIKAGEELT----FDY 206
PHD2_PHF10 cd15529
PHD finger 2 found in PHD finger protein 10 (PHF10) and similar proteins; PHF10, also termed ...
121-163 5.82e-04

PHD finger 2 found in PHD finger protein 10 (PHF10) and similar proteins; PHF10, also termed BRG1-associated factor 45a (BAF45a), or XAP135, is a ubiquitously expressed transcriptional regulator that is required for maintaining the undifferentiated status of neuroblasts. It contains a SAY (supporter of activation of yellow) domain and two adjacent plant homeodomain (PHD) fingers. This model corresponds to the second PHD finger.


Pssm-ID: 277004  Cd Length: 44  Bit Score: 39.21  E-value: 5.82e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2464208148  121 CICGFTHDDGYMICCDKCSVWQHIDCMGIDrqHIPD-TYLCERC 163
Cdd:cd15529      3 TKCGDPHDEDKMMFCDQCDRGYHTFCVGLR--SIPDgRWICPLC 44
PHD_ARID4_like cd15615
PHD finger found in Arabidopsis thaliana AT-rich interactive domain-containing protein 4 ...
122-163 6.12e-04

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


Pssm-ID: 277087  Cd Length: 57  Bit Score: 39.39  E-value: 6.12e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2464208148  122 ICG-----FTHDDGYMICCDKCSVWQHIDCMGIDRQHIPDT-------YLCERC 163
Cdd:cd15615      4 LCGqvyeeNEGDEKEWVQCDSCSEWVHFECDGRTGLGAFKYaksdglqYVCPRC 57
Pro-rich_NTERM NF040555
AAA family ATPase Pro-rich N-terminal domain; This HMM describes an extremely rich N-terminal ...
1727-1805 6.32e-04

AAA family ATPase Pro-rich N-terminal domain; This HMM describes an extremely rich N-terminal domain that is well-conserved for a family of AAA family ATPases seen in Streptomyces. The HMM was built to support correct structural annotation of this unusual, low-complexity domain.


Pssm-ID: 468532 [Multi-domain]  Cd Length: 93  Bit Score: 40.71  E-value: 6.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1727 ASGHHTTSAQALHHP----PHQGPPLFPSSAHPAVPPYPSQATHhttlGPGPQHQPSGTGP----HCPLPvtgphlqPQG 1798
Cdd:NF040555    16 GHGPAAGWSPAAHHPgpphPQGPAPVPPPAPGFPAPPGPQPGWH----PPAPQHAPAPPAPdttgHVQLP-------PGG 84

                   ....*..
gi 2464208148 1799 PNSIPTP 1805
Cdd:NF040555    85 PVPMPSP 91
SET_SETD1A cd19204
SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...
395-465 6.46e-04

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: 42.32  E-value: 6.46e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2464208148  395 VDARTFGNEARFIRRSCTPNAEVRHEIQDGTIHLYIYSIHSIPKGTEITiaFDFDYGNCKYKVDCACLKEN 465
Cdd:cd19204     79 IDATKCGNLARFINHCCTPNCYAKVITIESQKKIVIYSKQPIGVNEEIT--YDYKFPIEDNKIPCLCGTEN 147
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
343-468 1.01e-03

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: 42.61  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  343 LKSAKDLPPDALIIEYRGKFMLREQF---EANGYFFKrpypfvlfYSKFHGLEMCVDARTFGNEARFIRRSCTPN---AE 416
Cdd:cd10535    105 VRSLQDIPPGTFVCEYVGELISDSEAdvrEEDSYLFD--------LDNKDGEVYCIDARFYGNVSRFINHHCEPNlvpVR 176
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2464208148  417 VRHEIQDGTI-HLYIYSIHSIPKGTEItiafDFDYGNCKYKV-----DCAClkENPEC 468
Cdd:cd10535    177 VFMAHQDLRFpRIAFFSTRLIEAGEQL----GFDYGERFWDIkgklfSCRC--GSPKC 228
SET_SETD1B cd19205
SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...
343-465 1.22e-03

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: 41.19  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  343 LKSAKDLPPDALIIEYRGKF-------MLREQFEANG----YFFKRPYpfvlfyskfhglEMCVDARTFGNEARFIRRSC 411
Cdd:cd19205     28 LFAMEPIAADEMVIEYVGQNirqviadMREKRYEDEGigssYMFRVDH------------DTIIDATKCGNFARFINHSC 95
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2464208148  412 TPNAEVRHEIQDGTIHLYIYSIHSIPKGTEITiaFDFDYGNCKYKVDCACLKEN 465
Cdd:cd19205     96 NPNCYAKVITVESQKKIVIYSKQHINVNEEIT--YDYKFPIEDVKIPCLCGSEN 147
PHD_TAF3 cd15522
PHD finger found in transcription initiation factor TFIID subunit 3 (TAF3); TAF3 (also termed ...
120-163 1.25e-03

PHD finger found in transcription initiation factor TFIID subunit 3 (TAF3); TAF3 (also termed 140 kDa TATA box-binding protein-associated factor, TBP-associated factor 3, transcription initiation factor TFIID 140 kDa subunit (TAF140), or TAFII-140, is an integral component of TFIID) is a general initiation factor (GTF) that plays a key role in preinitiation complex (PIC) assembly through core promoter recognition. The interaction of H3K4me3 with TAF3 directs global TFIID recruitment to active genes, which regulates gene-selective functions of p53 in response to genotoxic stress. TAF3 is highly enriched in embryonic stem cells and is required for endoderm lineage differentiation and prevents premature specification of neuroectoderm and mesoderm. Moreover, TAF3, along with TRF3, forms a complex that is essential for myogenic differentiation. TAF3 contains a plant homeodomain (PHD) finger. This family also includes Drosophila melanogaster BIP2 (Bric-a-brac interacting protein 2) protein, which functions as an interacting partner of D. melanogaster p53 (Dmp53).


Pssm-ID: 276997 [Multi-domain]  Cd Length: 46  Bit Score: 38.42  E-value: 1.25e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2464208148  120 RC-ICGFTHDDGYMICCDKCSVWQHIDCMGIDR-QHIPDTYLCERC 163
Cdd:cd15522      1 ICpICKKPDDGSPMIGCDECDDWYHWECVGITDePPEEDDWFCPKC 46
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
343-478 1.48e-03

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: 42.31  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  343 LKSAKDLPPDALIIEYRGKFMLREQF---EANGYFFKrpypfvlfYSKFHGLEMCVDARTFGNEARFIRRSCTPN---AE 416
Cdd:cd10533    105 VRALQTIPQGTFICEYVGELISDAEAdvrEDDSYLFD--------LDNKDGEVYCIDARYYGNISRFINHLCDPNiipVR 176
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2464208148  417 VRHEIQDGTI-HLYIYSIHSIPKGTEItiafDFDYGN------CKYkVDCACLKEnpECpvlKRSSESM 478
Cdd:cd10533    177 VFMLHQDLRFpRIAFFSSRDIRTGEEL----GFDYGDrfwdikSKY-FTCQCGSE--KC---KHSAEAI 235
PHD1_AIRE cd15539
PHD finger 1 found in autoimmune regulator (AIRE); AIRE, also termed autoimmune ...
122-163 1.87e-03

PHD finger 1 found in autoimmune regulator (AIRE); AIRE, also termed autoimmune polyendocrinopathy candidiasis ectodermal dystrophy (APECED) protein, functions as a regulator of gene transcription in the thymus. It is essential for prevention of autoimmunity. AIRE plays a critical role in the induction of central tolerance. It promotes self-tolerance through tissue-specific antigen (TSA) expression. It also acts as an active regulator of chondrocyte differentiation. AIRE contains a homogeneously-staining region (HSR) or caspase-recruitment domain (CARD), a nuclear localization signal (NLS), a SAND (for Sp100, AIRE, nuclear phosphoprotein 41/75 or NucP41/75, and deformed epidermal auto regulatory factor 1 or Deaf1) domain, two plant homeodomain (PHD) fingers, and four LXXLL (where L stands for leucine) motifs. This model corresponds to the first PHD finger that recognizes the unmethylated tail of histone H3 and targets AIRE-dependent genes.


Pssm-ID: 277014 [Multi-domain]  Cd Length: 43  Bit Score: 37.82  E-value: 1.87e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2464208148  122 ICGfthDDGYMICCDKCSVWQHIDCMGIDRQHIP-DTYLCERC 163
Cdd:cd15539      4 VCG---DGGELLCCDGCPRAFHLACLVPPLTLIPsGTWRCSSC 43
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
561-652 2.77e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.45  E-value: 2.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  561 MESEEQIAERKRKMTREE--RKMEAILQAFARLEKREKRREQALERISTAKTEVKTECKDTqivsDAEVIQEQAKEENAS 638
Cdd:COG1579     94 LQKEIESLKRRISDLEDEilELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL----EAELEELEAEREELA 169
                           90
                   ....*....|....*...
gi 2464208148  639 KPTPAKV----NRTKQRK 652
Cdd:COG1579    170 AKIPPELlalyERIRKRK 187
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1463-1828 2.86e-03

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 42.69  E-value: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1463 GYLSPKPPSQQLGSPYRPHHSQSP-QVGTPQREPQRnfypaaqnlQANTQQATSGTLFTQTPSGQSSATYSQFNQQSLNS 1541
Cdd:pfam09606  157 GMMQPSSGQPGSGTPNQMGPNGGPgQGQAGGMNGGQ---------QGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANG 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1542 TAPPPPPPPPPSSYYQNQQPSanfqnynqlkGSLSQQTVFTSGPNQAlpgttsQQTVPGHHVTPGHFLPSQNPTIHHQTA 1621
Cdd:pfam09606  228 GMNPQQMGGAPNQVAMQQQQP----------QQQGQQSQLGMGINQM------QQMPQGVGGGAGQGGPGQPMGPPGQQP 291
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1622 AAVVPPPPPPPPAPGPHLVQQPNSHQQ---HSVAHVVGPVHAVTPGSHIHSQTAGHHLPppppppgpaphhhppphpsTG 1698
Cdd:pfam09606  292 GAMPNVMSIGDQNNYQQQQTRQQQQQQggnHPAAHQQQMNQSVGQGGQVVALGGLNHLE-------------------TW 352
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1699 LQGLQAQHQhvVNSAPPPPPPPPPSSVLASGHHTTSAQALHHPPHQGPPLFPSSAHPavppypsqathhttlgpGPQHQP 1778
Cdd:pfam09606  353 NPGNFGGLG--ANPMQRGQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGP-----------------GSQPPQ 413
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2464208148 1779 SGTGPHCPLPVTGPHLQPQ---GPNS---IPTPTASGFCPHPGSVALPHGVqGPQQ 1828
Cdd:pfam09606  414 SHPGGMIPSPALIPSPSPQmsqQPAQqrtIGQDSPGGSLNTPGQSAVNSPL-NPQE 468
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
391-451 3.25e-03

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: 41.52  E-value: 3.25e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2464208148  391 LEMCVDARTFGNEARFIRRSCTPNAE---VRheiQDGTI-HLYIYSIHSIPKGTEITiafdFDYG 451
Cdd:cd10544    157 LETFVDPTYIGNIGRFLNHSCEPNLFmvpVR---VDSMVpKLALFAARDIVAGEELS----FDYS 214
KLF10_N cd21572
N-terminal domain of Kruppel-like factor 10; Kruppel-like factor 10 (KLF10; also known as ...
1731-1845 4.27e-03

N-terminal domain of Kruppel-like factor 10; Kruppel-like factor 10 (KLF10; also known as Krueppel-like factor 10; early growth response(EGR)-alpha/EGRA; TGFbeta inducible early gene-1/TIEG1) is a protein that in humans is encoded by the KLF10 gene. KLF10 was first identified in human osteoblasts and plays a role in mediating estrogen (E2) signaling in bone and skeletal homeostasis and a regulatory role in tumor formation and metastasis. It may also play a role in adipocyte differentiation and adipose tissue function. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved a-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF10 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF10.


Pssm-ID: 409241 [Multi-domain]  Cd Length: 245  Bit Score: 41.13  E-value: 4.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1731 HTTSAQALHHPPHQGPPLFPSSAHPAVPPYPSQAT---HHTTLGpgpqhQPSGTGPHCPLPVTGPHLQPQGPNSIPTPTA 1807
Cdd:cd21572     71 HPPSAATLHPPAAQPPEEQHLSAETAASQQRFQCTsviRHTADA-----QPCSCSSCPSSPSVVPSVPAGVAGVSPVPVY 145
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2464208148 1808 SGFCP----HPGSVALPHGVQGPQQASPVPGQIPIHRAQVPP 1845
Cdd:cd21572    146 CQILPvsssSTTVVAAQAPLPQPQQQAASPAQVFLMGGQVPK 187
PHD_UHRF1_2 cd15525
PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein UHRF1 and ...
121-163 4.34e-03

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


Pssm-ID: 277000  Cd Length: 47  Bit Score: 36.96  E-value: 4.34e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2464208148  121 CICGFTHDDGYMICCDKCSVWQHIDCMGIDRQHIP--DTYLCERC 163
Cdd:cd15525      3 HVCGGKQDPEKQLLCDECDMAYHLYCLDPPLTSLPddDEWYCPDC 47
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1743-1845 4.42e-03

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: 42.06  E-value: 4.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148 1743 HQGPPLFPSSAHPAVPPYPSQATHHTTLGPGPQHQPSGTGPHCPLPVTGPHLQPQGPNSIPTPTASGFCPHPGSVALPHG 1822
Cdd:pfam03154  168 QTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHP 247
                           90       100       110
                   ....*....|....*....|....*....|
gi 2464208148 1823 -VQG------PQQASPVPGQIPIHRAQVPP 1845
Cdd:pfam03154  248 pLQPmtqpppPSQVSPQPLPQPSLHGQMPP 277
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
549-669 4.66e-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: 41.44  E-value: 4.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464208148  549 IEEKTPISNEVEMESEEQIAERKRKMTR----------EERKMEAILQ--AFARLEKREKRRE-QALERISTAKTEVKTE 615
Cdd:pfam13868  161 LKEKAEREEEREAEREEIEEEKEREIARlraqqekaqdEKAERDELRAklYQEEQERKERQKErEEAEKKARQRQELQQA 240
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2464208148  616 CKDtQIVSDAEVIQEQAKEENASKPTPAKVNR---TKQRKSFSRSRthigQQRRRHR 669
Cdd:pfam13868  241 REE-QIELKERRLAEEAEREEEEFERMLRKQAedeEIEQEEAEKRR----MKRLEHR 292
PHD_PHF3 cd15638
PHD finger found in PHD finger protein 3 (PHF3); PHF3 is a human homolog of yeast protein ...
122-163 5.17e-03

PHD finger found in PHD finger protein 3 (PHF3); PHF3 is a human homolog of yeast protein bypass of Ess1 (Bye1), a nuclear protein with a domain resembling the central domain in the transcription elongation factor TFIIS. It is ubiquitously expressed in normal tissues including brain, but its expression is significantly reduced or lost in glioblastomas. PHF3 contains an N-terminal plant homeodomain (PHD) finger, a central RNA polymerase II (Pol II)-binding TFIIS-like domain (TLD) domain, and a C-terminal Spen paralogue and orthologue C-terminal (SPOC) domain.


Pssm-ID: 277108  Cd Length: 51  Bit Score: 36.83  E-value: 5.17e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2464208148  122 ICGFTHDDGYMICCDKCSVWQHIDCMGID---RQHIPD---TYLCERC 163
Cdd:cd15638      4 FCKKPHGNRFMVGCGRCDDWFHGDCVGLSlsqAQQMEEedkEYVCVKC 51
PHD_UHRF2 cd15617
PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein 2 (UHRF2); ...
121-163 8.61e-03

PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein 2 (UHRF2); UHRF2 (also termed Np95/ICBP90-like RING finger protein (NIRF), Np95-like RING finger protein, nuclear protein 97, nuclear zinc finger protein Np97, RING finger protein 107, or E3 ubiquitin-protein ligase UHRF2) was originally identified as a ubiquitin ligase acting as a small ubiquitin-like modifier (SUMO) E3 ligase that enhances zinc finger protein 131 (ZNF131) SUMOylation but does not enhance ZNF131 ubiquitination. It also ubiquitinates PCNP, a PEST-containing nuclear protein. Moreover, UHRF2 functions as a nuclear protein involved in cell-cycle regulation and has been implicated in tumorigenesis. It interacts with cyclins, CDKs,p53, pRB, PCNA, HDAC1, DNMTs, G9a, methylated histone H3 lysine 9, and methylated DNA. It interacts with the cyclin E-CDK2 complex, ubiquitinates cyclins D1 and E1, induces G1 arrest, and is involved in the G1/S transition regulation. Furthermore, UHRF2 is a direct transcriptional target of the transcription factor E2F-1 in the induction of apoptosis. It recruits HDAC1 and binds to methyl-CpG. UHRF2 also participates in the maturation of Hepatitis B virus (HBV) by interacting with the HBV core protein and promoting its degradation. UHRF2 contains an N-terminal ubiquitin-like domain (UBL), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a SET- and RING-associated (SRA) domain, and a C-terminal RING finger.


Pssm-ID: 277089  Cd Length: 47  Bit Score: 36.09  E-value: 8.61e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2464208148  121 CICGFTHDDGYMICCDKCSVWQHIDCMGIDRQHIPDT--YLCERC 163
Cdd:cd15617      3 YVCGGKQDAHMQLLCDECNMAYHIYCLNPPLDKIPEDedWYCPSC 47
PHD_2 pfam13831
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
132-163 9.33e-03

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


Pssm-ID: 463990 [Multi-domain]  Cd Length: 35  Bit Score: 35.39  E-value: 9.33e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2464208148  132 MICCDKCSVWQHIDCMGIDRQHIPDTYLCERC 163
Cdd:pfam13831    4 LVYCSKCSVQVHASCYGVPPIPDGDGWKCRRC 35
 
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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