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Conserved domains on  [gi|568920205|ref|XP_006500671|]
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death-inducer obliterator 1 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SPOC_DIDO1-like cd21547
SPOC (Spen paralog and ortholog C-terminal) domain found in some death-inducer obliterator ...
1051-1193 5.03e-102

SPOC (Spen paralog and ortholog C-terminal) domain found in some death-inducer obliterator variants; The Dido/DIDO1 gene has been implicated in several cellular processes such as apoptosis and chromosomal segregation, particularly in the hematopoietic system. It encodes alternative splicing variants, including Dido1, 2, and 3, with Dido3 being the longest isoform and Dido1 being the shortest. Dido3 is ubiquitously expressed in all human tissues, is dispensable for embryonic stem (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. Dido2 and Dido1 are truncated at the C-terminus relative to Dido3, with Dido2 containing a partial SPOC domain whereas Dido1 is missing it completely. Dido1, also called DIO-1, or death-associated transcription factor 1 (DATF-1), is important for maintaining ES cells and directly regulates the expression of pluripotency factors. The conserved plant homeodomain (PHD) finger is responsible for the binding of histone H3 with a higher affinity for trimethylated lysine 4 (H3K4me3). The Dido/DIDO1 gene is a bone morphogenetic protein (BMP) target gene, which promotes BMP-induced melanoma progression. It also triggers apoptosis after nuclear translocation and caspase upregulation. This model corresponds to the SPOC domain which is involved in developmental signaling and has also been proposed to be a phosphorylation binding module.


:

Pssm-ID: 439210  Cd Length: 143  Bit Score: 323.03  E-value: 5.03e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1051 IWKGFINMQSVAKFVTKAYPVSGCLDYLSEDLPDTIHIGGRIAPKTVWDYVGKLKSSVSKELCLIRFHPATEEEEVAYIS 1130
Cdd:cd21547     1 IWKGFINMQSVAKFVTKAYPVSGSFDYLSEDLPDTIHIGGRISPKTVWDYVGKLKSSLSKELCLIRFHPATEEEEVAYIS 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568920205 1131 LYSYFSSRGRFGVVANNNRHVKDLYLIPLSAKDPVPSKLLPFEGPGLESPRPNIILGLVICQK 1193
Cdd:cd21547    81 LYSYFSSRGRFGVVANNNRHVKDLYLIPLSAKDPIPSKLLPFEGPGLESTRPNIILGLVICQK 143
TFS2M smart00510
Domain in the central regions of transcription elongation factor S-II (and elsewhere);
669-770 5.31e-40

Domain in the central regions of transcription elongation factor S-II (and elsewhere);


:

Pssm-ID: 128786 [Multi-domain]  Cd Length: 102  Bit Score: 143.99  E-value: 5.31e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205    669 QNIRRSLKEILWKRVNDSDDLIMTENEVGKIALHIEKEMFNLFQVTDNRYKSKYRSIMFNLKDPKNQGLFHRVLREEISL 748
Cdd:smart00510    1 DKVRDKCQEMLYKALQKISDPEEIELDPTELAVQIEAEMFSEFGTTDKKYKNKYRSLYFNLKDKKNPDLRRKVLNGEITP 80
                            90       100
                    ....*....|....*....|..
gi 568920205    749 AKLVRMKPEELVSKELSMWTEK 770
Cdd:smart00510   81 EKLATMTAEELASAELKEKREK 102
PHD_DIDO1_like cd15639
PHD finger found in death-inducer obliterator variants Dido1, Dido2, and Dido3; This family ...
263-316 2.57e-39

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: 140.49  E-value: 2.57e-39
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568920205  263 PNALYCICRQPHNNRFMICCDRCEEWFHGDCVGISEARGRLLERNGEDYICPNC 316
Cdd:cd15639     1 PNALYCICRQPHNNRFMICCDRCEEWFHGDCVGITEARGRLLERNGEDYICPNC 54
PHA03247 super family cl33720
large tegument protein UL36; Provisional
1571-2083 1.13e-10

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 67.66  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1571 LPRAPTGSTPGPQGTlPARETPAGTAVVQGPGLAAEAkesmAVPWAPGEnavlrpehDIQKCEHPGNPVSLPLDTShlpt 1650
Cdd:PHA03247 2560 PPAAPDRSVPPPRPA-PRPSEPAVTSRARRPDAPPQS----ARPRAPVD--------DRGDPRGPAPPSPLPPDTH---- 2622
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1651 agdgAARPAPPrrvllptppsttfppsfplQPKAQNFSSGSREPFSGPTFMSQETSLGSSQYEDPRGAQSAGKNDSPVAD 1730
Cdd:PHA03247 2623 ----APDPPPP-------------------SPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSP 2679
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1731 MEDSREPQPRPG-ESTTSFPQPGQRGGGPQPQFPGQREPAPRTFGMSGHHGPSFPGPRGPVPPYSEEN-LVPNSDGPRGP 1808
Cdd:PHA03247 2680 PQRPRRRAARPTvGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGpATPGGPARPAR 2759
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1809 PPARFGaqkPPIPSLFSGQHGPPPygdnrglspsylggPRGGAPAQfedrkDPHGEKREFQDTPYNEmTGAPAQCEGPDQ 1888
Cdd:PHA03247 2760 PPTTAG---PPAPAPPAAPAAGPP--------------RRLTRPAV-----ASLSESRESLPSPWDP-ADPPAAVLAPAA 2816
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1889 AqfmgnrapfqfggqrrplLTQMKGPRGGPPPSQFGAQRGPPPghfvgPRGPHPSQFENSRGTHPGQFEGARGQapgfmP 1968
Cdd:PHA03247 2817 A------------------LPPAASPAGPLPPPTSAQPTAPPP-----PPGPPPPSLPLGGSVAPGGDVRRRPP-----S 2868
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1969 GPRGIQPQQFEEQRVNSPPRFAGQRASAPLPYggprgPAPFPEKNEQPPSRFHFQGPSSQPVKPPPRPLLELPSHPPQHR 2048
Cdd:PHA03247 2869 RSPAAKPAAPARPPVRRLARPAVSRSTESFAL-----PPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPL 2943
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 568920205 2049 KDRWDEAGPATALPSSAGPGQGHEADGQWATSEFR 2083
Cdd:PHA03247 2944 APTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFR 2978
TNG2 super family cl34876
Chromatin remodeling protein, contains PhD zinc finger [Chromatin structure and dynamics];
157-299 7.69e-08

Chromatin remodeling protein, contains PhD zinc finger [Chromatin structure and dynamics];


The actual alignment was detected with superfamily member COG5034:

Pssm-ID: 227367 [Multi-domain]  Cd Length: 271  Bit Score: 56.10  E-value: 7.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  157 TLKELQNRLRRKREQEPVERSlrgSQNRLRKKRREEDSAETGSVQI---------GSAEQDRPLCKQEpEASQGPVSQSE 227
Cdd:COG5034   115 VAARIENCHDAVSRLERNSYS---SAARRSSGEHRSAASSQGSRHTklkkrknihNLKRRSPELSSKR-EVSFTLESPSV 190
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568920205  228 TDDIENQLEGKATQGNTEENPREAGKPKPEcevydpnALYCICRQPHNNRfMICCD--RCE-EWFHGDCVGISEA 299
Cdd:COG5034   191 PDTATRVKEGNNGGSTKSRGVSSEDNSEGE-------ELYCFCQQVSYGQ-MVACDnaNCKrEWFHLECVGLKEP 257
SF-CC1 super family cl36939
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
2142-2180 1.53e-04

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


The actual alignment was detected with superfamily member TIGR01622:

Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 46.84  E-value: 1.53e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 568920205  2142 SRERDWERSRDWDRHREWDKGRDRSSNRDRERDNDRAKE 2180
Cdd:TIGR01622    6 ERERLRDSSSAGDRDRRRDKGRERSRDRSRDRERSRSRR 44
PRK14954 super family cl33039
DNA polymerase III subunits gamma and tau; Provisional
600-665 2.65e-03

DNA polymerase III subunits gamma and tau; Provisional


The actual alignment was detected with superfamily member PRK14954:

Pssm-ID: 184918 [Multi-domain]  Cd Length: 620  Bit Score: 43.01  E-value: 2.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568920205  600 WPSATLSGTSARQAGPTPMTAASKKlPGSAAVVGVTRKPMSANVPAASPAPGRLGPVSPAPSQPNS 665
Cdd:PRK14954  381 APSPAGSPDVKKKAPEPDLPQPDRH-PGPAKPEAPGARPAELPSPASAPTPEQQPPVARSAPLPPS 445
SWIRM-assoc_1 super family cl24910
SWIRM-associated region 1; Much of the higher eukaryote SWI/SNF complex subunit SMARCC2 ...
1462-1499 3.11e-03

SWIRM-associated region 1; Much of the higher eukaryote SWI/SNF complex subunit SMARCC2 proteins is of low-complexity and or disordered. However, there are several short regions that are quite highly conserved. This is one of these regions. The function of the individual regions is not known.


The actual alignment was detected with superfamily member pfam16495:

Pssm-ID: 465142 [Multi-domain]  Cd Length: 84  Bit Score: 38.65  E-value: 3.11e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 568920205  1462 ASLVEQQ--------KMLEELNKQIEEQKRQLEEQEEALRQQRAAV 1499
Cdd:pfam16495   27 ALLVETQlkklelklKQFEELEKLLERERRQLERQRQQLFLERLAF 72
 
Name Accession Description Interval E-value
SPOC_DIDO1-like cd21547
SPOC (Spen paralog and ortholog C-terminal) domain found in some death-inducer obliterator ...
1051-1193 5.03e-102

SPOC (Spen paralog and ortholog C-terminal) domain found in some death-inducer obliterator variants; The Dido/DIDO1 gene has been implicated in several cellular processes such as apoptosis and chromosomal segregation, particularly in the hematopoietic system. It encodes alternative splicing variants, including Dido1, 2, and 3, with Dido3 being the longest isoform and Dido1 being the shortest. Dido3 is ubiquitously expressed in all human tissues, is dispensable for embryonic stem (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. Dido2 and Dido1 are truncated at the C-terminus relative to Dido3, with Dido2 containing a partial SPOC domain whereas Dido1 is missing it completely. Dido1, also called DIO-1, or death-associated transcription factor 1 (DATF-1), is important for maintaining ES cells and directly regulates the expression of pluripotency factors. The conserved plant homeodomain (PHD) finger is responsible for the binding of histone H3 with a higher affinity for trimethylated lysine 4 (H3K4me3). The Dido/DIDO1 gene is a bone morphogenetic protein (BMP) target gene, which promotes BMP-induced melanoma progression. It also triggers apoptosis after nuclear translocation and caspase upregulation. This model corresponds to the SPOC domain which is involved in developmental signaling and has also been proposed to be a phosphorylation binding module.


Pssm-ID: 439210  Cd Length: 143  Bit Score: 323.03  E-value: 5.03e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1051 IWKGFINMQSVAKFVTKAYPVSGCLDYLSEDLPDTIHIGGRIAPKTVWDYVGKLKSSVSKELCLIRFHPATEEEEVAYIS 1130
Cdd:cd21547     1 IWKGFINMQSVAKFVTKAYPVSGSFDYLSEDLPDTIHIGGRISPKTVWDYVGKLKSSLSKELCLIRFHPATEEEEVAYIS 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568920205 1131 LYSYFSSRGRFGVVANNNRHVKDLYLIPLSAKDPVPSKLLPFEGPGLESPRPNIILGLVICQK 1193
Cdd:cd21547    81 LYSYFSSRGRFGVVANNNRHVKDLYLIPLSAKDPIPSKLLPFEGPGLESTRPNIILGLVICQK 143
SPOC pfam07744
SPOC domain; The SPOC (Spen paralogue and orthologue C-terminal) domain is involved in ...
1044-1192 3.53e-41

SPOC domain; The SPOC (Spen paralogue and orthologue C-terminal) domain is involved in developmental signalling.


Pssm-ID: 400205  Cd Length: 142  Bit Score: 149.04  E-value: 3.53e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1044 FLSRLNTIWKGFINMQSVAKFVTKAYPVSGCLDYLsedLPDTIHIGGRIAPKTVWDYVGKLKSSVSKELCLIRFHPATEE 1123
Cdd:pfam07744    1 SLQDLEVIWQGTLAMKGVAEFSVRAHLVSGDIDSL---LPSLLRITGRIRLDAVWKYLDEVRRSITRDVLVVRFFPSSES 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568920205  1124 EEVAYISLYSYFSSRGRFGVVANNNRHVKDLYLIPLSakdPVPSKLLPfEGPGLESPRPNIILGLVICQ 1192
Cdd:pfam07744   78 DESAFDELIDYLQSKQRAGVIHAKSADVKDLYLFPPC---EFLELLLP-VGLSLEVSEPNLLLGVVVRK 142
TFS2M smart00510
Domain in the central regions of transcription elongation factor S-II (and elsewhere);
669-770 5.31e-40

Domain in the central regions of transcription elongation factor S-II (and elsewhere);


Pssm-ID: 128786 [Multi-domain]  Cd Length: 102  Bit Score: 143.99  E-value: 5.31e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205    669 QNIRRSLKEILWKRVNDSDDLIMTENEVGKIALHIEKEMFNLFQVTDNRYKSKYRSIMFNLKDPKNQGLFHRVLREEISL 748
Cdd:smart00510    1 DKVRDKCQEMLYKALQKISDPEEIELDPTELAVQIEAEMFSEFGTTDKKYKNKYRSLYFNLKDKKNPDLRRKVLNGEITP 80
                            90       100
                    ....*....|....*....|..
gi 568920205    749 AKLVRMKPEELVSKELSMWTEK 770
Cdd:smart00510   81 EKLATMTAEELASAELKEKREK 102
PHD_DIDO1_like cd15639
PHD finger found in death-inducer obliterator variants Dido1, Dido2, and Dido3; This family ...
263-316 2.57e-39

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: 140.49  E-value: 2.57e-39
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568920205  263 PNALYCICRQPHNNRFMICCDRCEEWFHGDCVGISEARGRLLERNGEDYICPNC 316
Cdd:cd15639     1 PNALYCICRQPHNNRFMICCDRCEEWFHGDCVGITEARGRLLERNGEDYICPNC 54
TFIIS_M pfam07500
Transcription factor S-II (TFIIS), central domain; Transcription elongation by RNA polymerase ...
664-777 4.22e-33

Transcription factor S-II (TFIIS), central domain; Transcription elongation by RNA polymerase II is regulated by the general elongation factor TFIIS. This factor stimulates RNA polymerase II to transcribe through regions of DNA that promote the formation of stalled ternary complexes. TFIIS is composed of three structural domains, termed I, II, and III. The two C-terminal domains (II and III), this domain and pfam01096 are required for transcription activity.


Pssm-ID: 462184  Cd Length: 112  Bit Score: 124.62  E-value: 4.22e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205   664 NSQIRQNIRRSLKEILWKRVNDSDdlimtENEVGKIALHIEKEMFNLFQVTDNRYKSKYRSIMFNLKDPKNQGLFHRVLR 743
Cdd:pfam07500    2 GDKVRDKCRELLYDALAKDSTEAS-----EEDALELAVEIEEALFKKFGGTNKKYKNKIRSLLFNLKDKKNPDLRRRVLS 76
                           90       100       110
                   ....*....|....*....|....*....|....
gi 568920205   744 EEISLAKLVRMKPEELVSKELSMWTEKPTKSVIE 777
Cdd:pfam07500   77 GEISPEKLVTMSPEEMASEELKKEREKIEKEALK 110
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
267-317 2.68e-14

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: 69.06  E-value: 2.68e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568920205   267 YC-ICRQPHNNRFMICCDRCEEWFHGDCVGISEARGRLLErngEDYICPNCT 317
Cdd:pfam00628    1 YCaVCGKSDDGGELVQCDGCDDWFHLACLGPPLDPAEIPS---GEWLCPECK 49
TFSII TIGR01385
transcription elongation factor S-II; This model represents eukaryotic transcription ...
626-776 4.92e-14

transcription elongation factor S-II; This model represents eukaryotic transcription elongation factor S-II. This protein allows stalled RNA transcription complexes to perform a cleavage of the nascent RNA and restart at the newly generated 3-prime end.


Pssm-ID: 273592 [Multi-domain]  Cd Length: 299  Bit Score: 75.26  E-value: 4.92e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205   626 PGSAAVVGVTRKPM--SANVPAASPAPGRLGPVSPAPSQPNS------------QIRQNIRRSLKEILWKRVNDSDDLIM 691
Cdd:TIGR01385   83 PGGNPEDKTTVGESvnSVKQEAKSQSDKIEQPKYVSSSPRNAkndfvptavtndKVRDKCRELLYDALAKDSDHPPQSID 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205   692 TEnevgKIALHIEKEMFNLFQVTDNRYKSKYRSIMFNLKDPKNQGLFHRVLREEISLAKLVRMKPEELVSKELSMWTEKP 771
Cdd:TIGR01385  163 PE----AKAIQIEELKFNNLGTTEAAYKARYRSIYSNLRDKNNPDLRHNVLTGEITPEKLATMTAEEMASAELKQEREEI 238

                   ....*
gi 568920205   772 TKSVI 776
Cdd:TIGR01385  239 TKENL 243
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
267-316 8.37e-13

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: 64.54  E-value: 8.37e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 568920205    267 YC-ICRQPHNNRFMICCDRCEEWFHGDCVGISEargrLLERNGEDYICPNC 316
Cdd:smart00249    1 YCsVCGKPDDGGELLQCDGCDRWYHQTCLGPPL----LEEEPDGKWYCPKC 47
PHA03247 PHA03247
large tegument protein UL36; Provisional
1571-2083 1.13e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 67.66  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1571 LPRAPTGSTPGPQGTlPARETPAGTAVVQGPGLAAEAkesmAVPWAPGEnavlrpehDIQKCEHPGNPVSLPLDTShlpt 1650
Cdd:PHA03247 2560 PPAAPDRSVPPPRPA-PRPSEPAVTSRARRPDAPPQS----ARPRAPVD--------DRGDPRGPAPPSPLPPDTH---- 2622
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1651 agdgAARPAPPrrvllptppsttfppsfplQPKAQNFSSGSREPFSGPTFMSQETSLGSSQYEDPRGAQSAGKNDSPVAD 1730
Cdd:PHA03247 2623 ----APDPPPP-------------------SPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSP 2679
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1731 MEDSREPQPRPG-ESTTSFPQPGQRGGGPQPQFPGQREPAPRTFGMSGHHGPSFPGPRGPVPPYSEEN-LVPNSDGPRGP 1808
Cdd:PHA03247 2680 PQRPRRRAARPTvGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGpATPGGPARPAR 2759
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1809 PPARFGaqkPPIPSLFSGQHGPPPygdnrglspsylggPRGGAPAQfedrkDPHGEKREFQDTPYNEmTGAPAQCEGPDQ 1888
Cdd:PHA03247 2760 PPTTAG---PPAPAPPAAPAAGPP--------------RRLTRPAV-----ASLSESRESLPSPWDP-ADPPAAVLAPAA 2816
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1889 AqfmgnrapfqfggqrrplLTQMKGPRGGPPPSQFGAQRGPPPghfvgPRGPHPSQFENSRGTHPGQFEGARGQapgfmP 1968
Cdd:PHA03247 2817 A------------------LPPAASPAGPLPPPTSAQPTAPPP-----PPGPPPPSLPLGGSVAPGGDVRRRPP-----S 2868
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1969 GPRGIQPQQFEEQRVNSPPRFAGQRASAPLPYggprgPAPFPEKNEQPPSRFHFQGPSSQPVKPPPRPLLELPSHPPQHR 2048
Cdd:PHA03247 2869 RSPAAKPAAPARPPVRRLARPAVSRSTESFAL-----PPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPL 2943
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 568920205 2049 KDRWDEAGPATALPSSAGPGQGHEADGQWATSEFR 2083
Cdd:PHA03247 2944 APTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFR 2978
TNG2 COG5034
Chromatin remodeling protein, contains PhD zinc finger [Chromatin structure and dynamics];
157-299 7.69e-08

Chromatin remodeling protein, contains PhD zinc finger [Chromatin structure and dynamics];


Pssm-ID: 227367 [Multi-domain]  Cd Length: 271  Bit Score: 56.10  E-value: 7.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  157 TLKELQNRLRRKREQEPVERSlrgSQNRLRKKRREEDSAETGSVQI---------GSAEQDRPLCKQEpEASQGPVSQSE 227
Cdd:COG5034   115 VAARIENCHDAVSRLERNSYS---SAARRSSGEHRSAASSQGSRHTklkkrknihNLKRRSPELSSKR-EVSFTLESPSV 190
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568920205  228 TDDIENQLEGKATQGNTEENPREAGKPKPEcevydpnALYCICRQPHNNRfMICCD--RCE-EWFHGDCVGISEA 299
Cdd:COG5034   191 PDTATRVKEGNNGGSTKSRGVSSEDNSEGE-------ELYCFCQQVSYGQ-MVACDnaNCKrEWFHLECVGLKEP 257
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1684-2078 1.80e-07

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: 56.56  E-value: 1.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1684 AQNFSS-GSREPFSGPtfMSQETSLGSSQYEDPRGAQSAGKNDSPVADMEDSREPQPRPGESTTSFPQPGQRGGGPQPQF 1762
Cdd:pfam09606   86 LQNLAGqGTRPQMMGP--MGPGPGGPMGQQMGGPGTASNLLASLGRPQMPMGGAGFPSQMSRVGRMQPGGQAGGMMQPSS 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1763 PGQREPAPRTfgMSGHHGPSFPGPRGPVPPyseenlvpNSDGPRGPPPARFGAQKPPIPSLfSGQHGPPPYGDNRGLSPs 1842
Cdd:pfam09606  164 GQPGSGTPNQ--MGPNGGPGQGQAGGMNGG--------QQGPMGGQMPPQMGVPGMPGPAD-AGAQMGQQAQANGGMNP- 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1843 ylgGPRGGAPAQFEdrkdphgekrefqdtpyneMTGAPAQCEGPDQAQFMGNRAPFQF-GGQRRPLLTQMKGPRGGPPPS 1921
Cdd:pfam09606  232 ---QQMGGAPNQVA-------------------MQQQQPQQQGQQSQLGMGINQMQQMpQGVGGGAGQGGPGQPMGPPGQ 289
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1922 QFGAQ------RGPPPGHFVGPRGPHPSQFENSRGTHPGQF-----EGARGQAPGFMPGPRGIQPQQFEEQRVNSPPRFA 1990
Cdd:pfam09606  290 QPGAMpnvmsiGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMnqsvgQGGQVVALGGLNHLETWNPGNFGGLGANPMQRGQ 369
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1991 GQRASAPLPYGGPRGPAPFPEKNEQPPSRFHF---QGPSSQPVKPPPRPLLELPSHPPQHRKDRWDEAgPATALPSSAGP 2067
Cdd:pfam09606  370 PGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVpspQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQP-AQQRTIGQDSP 448
                          410
                   ....*....|.
gi 568920205  2068 GQGHEADGQWA 2078
Cdd:pfam09606  449 GGSLNTPGQSA 459
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
2142-2180 1.53e-04

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 46.84  E-value: 1.53e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 568920205  2142 SRERDWERSRDWDRHREWDKGRDRSSNRDRERDNDRAKE 2180
Cdd:TIGR01622    6 ERERLRDSSSAGDRDRRRDKGRERSRDRSRDRERSRSRR 44
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
1888-2049 4.41e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 45.57  E-value: 4.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1888 QAQFMgnrapfqfggQRRPLLTQMkgprggPPPSQFGAQRGPPPGHFVGPRGPHPSQFENsrgtHPGQFEGARGQAPGFM 1967
Cdd:TIGR01628  372 QDQFM----------QLQPRMRQL------PMGSPMGGAMGQPPYYGQGPQQQFNGQPLG----WPRMSMMPTPMGPGGP 431
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1968 PGPRGIQP----QQFEEQRVNSPPRfagqRASAPLPYGGPRGPAPFPEKNEQPPSRFHFQGPSSQpvkppprPLLELPSH 2043
Cdd:TIGR01628  432 LRPNGLAPmnavRAPSRNAQNAAQK----PPMQPVMYPPNYQSLPLSQDLPQPQSTASQGGQNKK-------LAQVLASA 500

                   ....*.
gi 568920205  2044 PPQHRK 2049
Cdd:TIGR01628  501 TPQMQK 506
PRK14954 PRK14954
DNA polymerase III subunits gamma and tau; Provisional
600-665 2.65e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184918 [Multi-domain]  Cd Length: 620  Bit Score: 43.01  E-value: 2.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568920205  600 WPSATLSGTSARQAGPTPMTAASKKlPGSAAVVGVTRKPMSANVPAASPAPGRLGPVSPAPSQPNS 665
Cdd:PRK14954  381 APSPAGSPDVKKKAPEPDLPQPDRH-PGPAKPEAPGARPAELPSPASAPTPEQQPPVARSAPLPPS 445
SWIRM-assoc_1 pfam16495
SWIRM-associated region 1; Much of the higher eukaryote SWI/SNF complex subunit SMARCC2 ...
1462-1499 3.11e-03

SWIRM-associated region 1; Much of the higher eukaryote SWI/SNF complex subunit SMARCC2 proteins is of low-complexity and or disordered. However, there are several short regions that are quite highly conserved. This is one of these regions. The function of the individual regions is not known.


Pssm-ID: 465142 [Multi-domain]  Cd Length: 84  Bit Score: 38.65  E-value: 3.11e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 568920205  1462 ASLVEQQ--------KMLEELNKQIEEQKRQLEEQEEALRQQRAAV 1499
Cdd:pfam16495   27 ALLVETQlkklelklKQFEELEKLLERERRQLERQRQQLFLERLAF 72
 
Name Accession Description Interval E-value
SPOC_DIDO1-like cd21547
SPOC (Spen paralog and ortholog C-terminal) domain found in some death-inducer obliterator ...
1051-1193 5.03e-102

SPOC (Spen paralog and ortholog C-terminal) domain found in some death-inducer obliterator variants; The Dido/DIDO1 gene has been implicated in several cellular processes such as apoptosis and chromosomal segregation, particularly in the hematopoietic system. It encodes alternative splicing variants, including Dido1, 2, and 3, with Dido3 being the longest isoform and Dido1 being the shortest. Dido3 is ubiquitously expressed in all human tissues, is dispensable for embryonic stem (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. Dido2 and Dido1 are truncated at the C-terminus relative to Dido3, with Dido2 containing a partial SPOC domain whereas Dido1 is missing it completely. Dido1, also called DIO-1, or death-associated transcription factor 1 (DATF-1), is important for maintaining ES cells and directly regulates the expression of pluripotency factors. The conserved plant homeodomain (PHD) finger is responsible for the binding of histone H3 with a higher affinity for trimethylated lysine 4 (H3K4me3). The Dido/DIDO1 gene is a bone morphogenetic protein (BMP) target gene, which promotes BMP-induced melanoma progression. It also triggers apoptosis after nuclear translocation and caspase upregulation. This model corresponds to the SPOC domain which is involved in developmental signaling and has also been proposed to be a phosphorylation binding module.


Pssm-ID: 439210  Cd Length: 143  Bit Score: 323.03  E-value: 5.03e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1051 IWKGFINMQSVAKFVTKAYPVSGCLDYLSEDLPDTIHIGGRIAPKTVWDYVGKLKSSVSKELCLIRFHPATEEEEVAYIS 1130
Cdd:cd21547     1 IWKGFINMQSVAKFVTKAYPVSGSFDYLSEDLPDTIHIGGRISPKTVWDYVGKLKSSLSKELCLIRFHPATEEEEVAYIS 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568920205 1131 LYSYFSSRGRFGVVANNNRHVKDLYLIPLSAKDPVPSKLLPFEGPGLESPRPNIILGLVICQK 1193
Cdd:cd21547    81 LYSYFSSRGRFGVVANNNRHVKDLYLIPLSAKDPIPSKLLPFEGPGLESTRPNIILGLVICQK 143
SPOC_PHF3-like cd21541
SPOC (Spen paralog and ortholog C-terminal) domain found in PHD finger protein 3 (PHF3), ...
1051-1191 2.77e-84

SPOC (Spen paralog and ortholog C-terminal) domain found in PHD finger protein 3 (PHF3), death-inducer obliterator (Dido) variants, and similar proteins; 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. This group also includes the protein products of the Dido gene that encodes three alternative splicing variants (Dido1, 2, and 3), which have been implicated in several cellular processes such as apoptosis and chromosomal segregation, particularly in the hematopoietic system. The Dido gene is a bone morphogenetic protein (BMP) target gene and promotes BMP-induced melanoma progression. 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). 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. This model corresponds to the SPOC domain of the PHF3-like group; the SPOC domain is involved in developmental signaling and has also been proposed to be a phosphorylation binding module.


Pssm-ID: 439204  Cd Length: 141  Bit Score: 272.19  E-value: 2.77e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1051 IWKGFINMQSVAKFVTKAYPVSGCLDYLSEDLPDTIHIGGRIAPKTVWDYVGKLKSSVSKELCLIRFHPATEEEEVAYIS 1130
Cdd:cd21541     1 VWKGFISMQEVAKFVASAYHVSGPCEDLSEDLPDTLEVCGRISPEQVWDYLSKLKQSGTKEIIVIRFHPANEEEKVSYIS 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568920205 1131 LYSYFSSRGRFGVVANNNRHVKDLYLIPLSAKDPVPSKLLPFEGPGLESPRPNIILGLVIC 1191
Cdd:cd21541    81 LYSYLSSRKRCGVVGNNSKHVKDMYLIPLASHQPIPQVLLPFDGPGLEETRPHMLLGIIVR 141
SPOC_PHF3 cd21548
SPOC (Spen paralog and ortholog C-terminal) domain found in PHD finger protein 3 (PHF3); PHF3 ...
1051-1190 1.83e-71

SPOC (Spen paralog and ortholog C-terminal) domain 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 SPOC domain. This model corresponds to the SPOC domain which is involved in developmental signaling and has also been proposed to be a phosphorylation binding module.


Pssm-ID: 439211  Cd Length: 141  Bit Score: 235.53  E-value: 1.83e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1051 IWKGFINMQSVAKFVTKAYPVSGCLDYLSEDLPDTIHIGGRIAPKTVWDYVGKLKSSVSKELCLIRFHPATEEEEVAYIS 1130
Cdd:cd21548     1 IWKGFINMPSVAKFVTKAYPVSGSLEYLTEDLPDSIQVGGRISPQTVWDYVEKIKASGTKEICVVRFSPVTEEDQISYTL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1131 LYSYFSSRGRFGVVANNNRHVKDLYLIPLSAKDPVPSKLLPFEGPGLESPRPNIILGLVI 1190
Cdd:cd21548    81 LYAYFSSRKRYGVVANNMKQVKDMYLIPLGASEKIPHHLVPFDGPGLELHRPNLLLGLII 140
SPOC_PPS-like cd22581
SPOC (Spen paralog and ortholog C-terminal) domain found in Drosophila melanogaster protein ...
1051-1190 1.61e-51

SPOC (Spen paralog and ortholog C-terminal) domain found in Drosophila melanogaster protein partner of Sans-fille and similar proteins; Drosophila melanogaster protein partner of Sans-fille (PPS), also called protein partner of Snf, is a homolog of human DIDO. It mediates diverse chromatin activities, including the regulation of stemness genes in embryonic stem cells and splicing. PPS associates with spliceosomal RNAs including the U1 snRNP protein Sans-fille (Snf) to mediate sex determination gene Sex-lethal (Sxl) splicing autoregulation. Alternative splicing of the Sxl pre-mRNA determines gender during development in Drosophila, producing protein-encoding mRNAs in females but yielding inactive and truncated mRNAs in males. PPS contains a plant homeodomain (PHD) finger, Brahma and Kismet (BRK), a transcription elongation factor S-II subunit M (TFSIIM) domain, and a SPOC domain. This model corresponds to the SPOC domain that is involved in developmental signaling and has also been proposed to be a phosphorylation binding module.


Pssm-ID: 439214  Cd Length: 142  Bit Score: 178.56  E-value: 1.61e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1051 IWKGFINMQSVAKFVTKAYPVSGCLDYLSEDLPDTIHIGGRIAPKTVWDYVGKLKSSVSKELCLIRFHPATEEEEVAYIS 1130
Cdd:cd22581     1 VWKGTINMPDVAKFNVSAQVVSGNSDDLSLDLPKVLDVVGRIAPETVWDYIGKLKKSPTKEIVVVRLTPASEEDEMSYNT 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568920205 1131 LYSYFSSRGRFGVVANNNRHVKDLYLIPLSAKDPVPSKLLPFEGPGL-ESPRPNIILGLVI 1190
Cdd:cd22581    81 FFEYLSSRNRLGVIGSVSKAIKDFYILPLPKESPIPEVLLPLDGPGLfENRRPNLLLGIIV 141
SPOC_TFIIS cd21538
SPOC (Spen paralog and ortholog C-terminal) domain found in the transcription factor S-II ...
1051-1191 6.93e-43

SPOC (Spen paralog and ortholog C-terminal) domain found in the transcription factor S-II (TFIIS) family; The transcription factor S-II (TFIIS) family includes SPOC domain-containing protein 1 (SPOCD1), yeast bypass of ESS1 protein 1 (Bye1p), PHD finger protein 3 (PHF3), and death-inducer obliterator (Dido) splicing variants, among others. They are characterized by having both a central RNA polymerase II (Pol II)-binding TFIIS-like domain (TLD) domain, and a C-terminal SPOC domain. This model corresponds to the SPOC domain that is involved in developmental signaling. SPOCD1 acts as a tumor-related factor that promotes cell proliferation and metastasis. Yeast Bye1p is a nuclear transcription factor with a domain resembling the central domain in 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). PHF3 is a human homolog of the yeast protein Bye1p. It is ubiquitously expressed in normal tissues including brain, but its expression is significantly reduced or lost in glioblastomas. The Dido/DIDO1 gene is implicated in several cellular processes such as apoptosis and chromosomal segregation, particularly in the hematopoietic system. This model corresponds to the SPOC domain that is involved in developmental signaling and has also been proposed to be a phosphorylation binding module.


Pssm-ID: 439201  Cd Length: 146  Bit Score: 153.96  E-value: 6.93e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1051 IWKGFINMQSVAKFVTKAYPVSGCLDYLSED---LPDTIHIGGRIAPKTVWDYVGKLKSSVSKELCLIRFHPATE-EEEV 1126
Cdd:cd21538     1 VWSGKLTMPGVASFPASARQVGGPDLSSTWWtdlLPSTLEIKGRIPLDKAEKYLCELRFSSSRDVVVVSLEPPDSsSDKA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568920205 1127 AYISLYSYFSSRGRFGVVANNNRHVKDLYLIPLSAKDPVPSKLLPFEGPGLESPRP-NIILGLVIC 1191
Cdd:cd21538    81 AFDELFDYFVSRDRYGVVGPKGLAVKDLYLVPLPAGDPLPPFLLLLDDGPGPEPRDeDLLLGVIVL 146
SPOC pfam07744
SPOC domain; The SPOC (Spen paralogue and orthologue C-terminal) domain is involved in ...
1044-1192 3.53e-41

SPOC domain; The SPOC (Spen paralogue and orthologue C-terminal) domain is involved in developmental signalling.


Pssm-ID: 400205  Cd Length: 142  Bit Score: 149.04  E-value: 3.53e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1044 FLSRLNTIWKGFINMQSVAKFVTKAYPVSGCLDYLsedLPDTIHIGGRIAPKTVWDYVGKLKSSVSKELCLIRFHPATEE 1123
Cdd:pfam07744    1 SLQDLEVIWQGTLAMKGVAEFSVRAHLVSGDIDSL---LPSLLRITGRIRLDAVWKYLDEVRRSITRDVLVVRFFPSSES 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568920205  1124 EEVAYISLYSYFSSRGRFGVVANNNRHVKDLYLIPLSakdPVPSKLLPfEGPGLESPRPNIILGLVICQ 1192
Cdd:pfam07744   78 DESAFDELIDYLQSKQRAGVIHAKSADVKDLYLFPPC---EFLELLLP-VGLSLEVSEPNLLLGVVVRK 142
TFS2M smart00510
Domain in the central regions of transcription elongation factor S-II (and elsewhere);
669-770 5.31e-40

Domain in the central regions of transcription elongation factor S-II (and elsewhere);


Pssm-ID: 128786 [Multi-domain]  Cd Length: 102  Bit Score: 143.99  E-value: 5.31e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205    669 QNIRRSLKEILWKRVNDSDDLIMTENEVGKIALHIEKEMFNLFQVTDNRYKSKYRSIMFNLKDPKNQGLFHRVLREEISL 748
Cdd:smart00510    1 DKVRDKCQEMLYKALQKISDPEEIELDPTELAVQIEAEMFSEFGTTDKKYKNKYRSLYFNLKDKKNPDLRRKVLNGEITP 80
                            90       100
                    ....*....|....*....|..
gi 568920205    749 AKLVRMKPEELVSKELSMWTEK 770
Cdd:smart00510   81 EKLATMTAEELASAELKEKREK 102
PHD_DIDO1_like cd15639
PHD finger found in death-inducer obliterator variants Dido1, Dido2, and Dido3; This family ...
263-316 2.57e-39

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: 140.49  E-value: 2.57e-39
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568920205  263 PNALYCICRQPHNNRFMICCDRCEEWFHGDCVGISEARGRLLERNGEDYICPNC 316
Cdd:cd15639     1 PNALYCICRQPHNNRFMICCDRCEEWFHGDCVGITEARGRLLERNGEDYICPNC 54
SPOC_SPOCD1 cd21540
SPOC (Spen paralog and ortholog C-terminal) domain found in SPOC domain-containing protein 1 ...
1051-1190 1.80e-38

SPOC (Spen paralog and ortholog C-terminal) domain found in SPOC domain-containing protein 1 (SPOCD1) and similar proteins; SPOCD1 is a protein belonging to the transcription factor S-II (TFIIS) family of transcription factors. It acts as a tumor-related factor that promotes cell proliferation and metastasis. SPOCD1 was initially found to interact with testis protein phosphatase 1, which is a major eukaryotic serine/threonine-specific phosphatase that regulates cellular signaling. The model corresponds to the SPOC domain of SPOCD1; the SPOC domain is involved in developmental signaling and has also been proposed to be a phosphorylation binding module.


Pssm-ID: 439203  Cd Length: 138  Bit Score: 141.03  E-value: 1.80e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1051 IWKGFINMQSVAKFVTKAYPVSGCLDYLSEDLPDTIHIGGRIAPKTVWDYVGKLKSSVSKELCLIRFHPATEEEEVAYIS 1130
Cdd:cd21540     1 LWEGAIQMFSIKQFGAKAYLVSGHSSQLIQALPAVIRSRGCILPESVWDYLDSIWPAEAKEMCLVRFAPAGARDSQNYRM 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1131 LYSYFSSRGRFGVVannNRHVKDLYLIPLSAKDPVPSKLLPFEGPGLESPRPNIILGLVI 1190
Cdd:cd21540    81 LYSYLNNKQRYGIV---DSEKMDMFLIPLPAFQPVPAKLRPLGGPGLEATHSSLLLALIL 137
PHD_PHF3_like cd15552
PHD finger found in PHD finger protein 3 (PHF3), and death-inducer obliterator variants Dido1, ...
267-316 2.79e-34

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: 125.97  E-value: 2.79e-34
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568920205  267 YCICRQPHNNRFMICCDRCEEWFHGDCVGISEARGRLLERNGEDYICPNC 316
Cdd:cd15552     1 YCICRKPHNNRFMICCDRCEEWFHGDCVGITEAQGKEMEENIEEYVCPKC 50
TFIIS_M pfam07500
Transcription factor S-II (TFIIS), central domain; Transcription elongation by RNA polymerase ...
664-777 4.22e-33

Transcription factor S-II (TFIIS), central domain; Transcription elongation by RNA polymerase II is regulated by the general elongation factor TFIIS. This factor stimulates RNA polymerase II to transcribe through regions of DNA that promote the formation of stalled ternary complexes. TFIIS is composed of three structural domains, termed I, II, and III. The two C-terminal domains (II and III), this domain and pfam01096 are required for transcription activity.


Pssm-ID: 462184  Cd Length: 112  Bit Score: 124.62  E-value: 4.22e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205   664 NSQIRQNIRRSLKEILWKRVNDSDdlimtENEVGKIALHIEKEMFNLFQVTDNRYKSKYRSIMFNLKDPKNQGLFHRVLR 743
Cdd:pfam07500    2 GDKVRDKCRELLYDALAKDSTEAS-----EEDALELAVEIEEALFKKFGGTNKKYKNKIRSLLFNLKDKKNPDLRRRVLS 76
                           90       100       110
                   ....*....|....*....|....*....|....
gi 568920205   744 EEISLAKLVRMKPEELVSKELSMWTEKPTKSVIE 777
Cdd:pfam07500   77 GEISPEKLVTMSPEEMASEELKKEREKIEKEALK 110
PHD2_3_BPTF cd15560
PHD finger 2 and 3 found in bromodomain and PHD finger-containing transcription factor (BPTF); ...
267-316 4.25e-20

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: 85.09  E-value: 4.25e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568920205  267 YCICRQPHN-NRFMICCDRCEEWFHGDCVGISEARGrlleRNGEDYICPNC 316
Cdd:cd15560     1 YCICRTPYDeSQFYIGCDRCQDWFHGRCVGILQSEA----EKIDEYVCPQC 47
PHD_PHF2_like cd15554
PHD finger found in PHF2, PHF8 and KDM7; This family includes PHF2, PHF8, KDM7, and similar ...
267-316 4.84e-20

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: 85.13  E-value: 4.84e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568920205  267 YCICRQPHN-NRFMICCDRCEEWFHGDCVGISEARGRLLERngedYICPNC 316
Cdd:cd15554     1 YCICRQPYDvTRFMIECDVCKDWFHGSCVGVEEHQANDIER----YHCPNC 47
PHD_Cfp1 cd15553
PHD finger found in CXXC-type zinc finger protein 1 (Cfp1); Cfp1, also termed CpG-binding ...
267-316 6.02e-18

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: 78.96  E-value: 6.02e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568920205  267 YCICRQPHNNRFMICCDRCEEWFHGDCVGISEARGRLLERngedYICPNC 316
Cdd:cd15553     1 YCICRSSDISRFMIGCDNCEEWYHGDCINITEKEAKAIKE----WYCQQC 46
PHD_PHF3 cd15638
PHD finger found in PHD finger protein 3 (PHF3); PHF3 is a human homolog of yeast protein ...
269-316 1.48e-17

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: 78.04  E-value: 1.48e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568920205  269 ICRQPHNNRFMICCDRCEEWFHGDCVGISEARGRLLERNGEDYICPNC 316
Cdd:cd15638     4 FCKKPHGNRFMVGCGRCDDWFHGDCVGLSLSQAQQMEEEDKEYVCVKC 51
PHD_SPP1 cd16039
PHD finger found in Set1 complex component SPP1; Set1C component SPP1, also called COMPASS ...
267-316 4.26e-16

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: 74.05  E-value: 4.26e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568920205  267 YCICRQPHNNRFMICCDRCEEWFHGDCVGISEARGRLLERngedYICPNC 316
Cdd:cd16039     1 YCICQKPDDGRWMIACDGCDEWYHFTCVNIPEADVELVDS----FFCPPC 46
PHD_KDM7 cd15640
PHD finger found in lysine-specific demethylase 7 (KDM7); KDM7, also termed JmjC ...
267-319 4.86e-15

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: 71.17  E-value: 4.86e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568920205  267 YCICRQPHN-NRFMICCDRCEEWFHGDCVGISEARGRLLERngedYICPNCTIL 319
Cdd:cd15640     1 YCVCRQPYDvNRFMIECDICKDWFHGSCVQVEEHHAADIDL----YHCPNCEVL 50
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
267-317 2.68e-14

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: 69.06  E-value: 2.68e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568920205   267 YC-ICRQPHNNRFMICCDRCEEWFHGDCVGISEARGRLLErngEDYICPNCT 317
Cdd:pfam00628    1 YCaVCGKSDDGGELVQCDGCDDWFHLACLGPPLDPAEIPS---GEWLCPECK 49
SPOC_SF cd21520
SPOC (Spen paralog and ortholog C-terminal) domain superfamily; The SPOC domain is involved in ...
1051-1190 3.69e-14

SPOC (Spen paralog and ortholog C-terminal) domain superfamily; The SPOC domain is involved in developmental signalling and has also been proposed to be a phosphorylation binding module. It has been found mainly in two protein families: transcription factor S-II (TFIIS) and Spen (split end). The TFIIS family includes SPOC domain-containing protein 1 (SPOCD1), yeast bypass of ESS1 protein 1 (Bye1p), PHD finger protein 3 (PHF3), and death-inducer obliterator (Dido) splicing variants, among others. They are characterized by having both a central RNA polymerase II (Pol II)-binding TFIIS-like domain (TLD) domain, and a C-terminal SPOC domain. The Spen protein family includes SMART/HDAC1-associated repressor protein (SHARP) and RNA binding motif protein 15 (RBM15)-like proteins from metazoans, as well as plant flowering time control protein FPA and yeast chromo domain-containing protein 1 (Chp1p). They are characterized by containing RNA recognition motifs (RRMs) and a SPOC domain.


Pssm-ID: 439200  Cd Length: 138  Bit Score: 71.55  E-value: 3.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1051 IWKGFINMQSVAKFVTKAYPVSGCLDYLSEDLPDTIHIGGRIAPKTVWDYVGKLKSSVSKELCLIRFHPATEEEEVAYIS 1130
Cdd:cd21520     1 VWQGLLALKNDPTAAARLHFVSGNNVLALSELPPVLRIAQRMRLNATQLEGVARRMAVATDYCLVLALPCGRDDESLKAA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568920205 1131 LYSYFSSRGRFGVVANNNRHVkdlYLIPLSAKDPVPSKLLPF-EGPGLESPRPNIILGLVI 1190
Cdd:cd21520    81 FITYLQAKQRAGIASNQPAYV---LQLFPPCEFSESHLSRLApDLLASIVTISPHLMIVIL 138
TFSII TIGR01385
transcription elongation factor S-II; This model represents eukaryotic transcription ...
626-776 4.92e-14

transcription elongation factor S-II; This model represents eukaryotic transcription elongation factor S-II. This protein allows stalled RNA transcription complexes to perform a cleavage of the nascent RNA and restart at the newly generated 3-prime end.


Pssm-ID: 273592 [Multi-domain]  Cd Length: 299  Bit Score: 75.26  E-value: 4.92e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205   626 PGSAAVVGVTRKPM--SANVPAASPAPGRLGPVSPAPSQPNS------------QIRQNIRRSLKEILWKRVNDSDDLIM 691
Cdd:TIGR01385   83 PGGNPEDKTTVGESvnSVKQEAKSQSDKIEQPKYVSSSPRNAkndfvptavtndKVRDKCRELLYDALAKDSDHPPQSID 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205   692 TEnevgKIALHIEKEMFNLFQVTDNRYKSKYRSIMFNLKDPKNQGLFHRVLREEISLAKLVRMKPEELVSKELSMWTEKP 771
Cdd:TIGR01385  163 PE----AKAIQIEELKFNNLGTTEAAYKARYRSIYSNLRDKNNPDLRHNVLTGEITPEKLATMTAEEMASAELKQEREEI 238

                   ....*
gi 568920205   772 TKSVI 776
Cdd:TIGR01385  239 TKENL 243
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
267-316 8.37e-13

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: 64.54  E-value: 8.37e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 568920205    267 YC-ICRQPHNNRFMICCDRCEEWFHGDCVGISEargrLLERNGEDYICPNC 316
Cdd:smart00249    1 YCsVCGKPDDGGELLQCDGCDRWYHQTCLGPPL----LEEEPDGKWYCPKC 47
PHD_PHF8 cd15642
PHD finger found in histone lysine demethylase PHF8; PHF8, also termed PHD finger protein 8, ...
266-320 2.36e-12

PHD finger found in histone lysine demethylase PHF8; 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. PHF8 contains an N-terminal plant homeodomain (PHD) finger followed by a JmjC domain. The PHD finger mediates binding to nucleosomes at active gene promoters and the JmjC domain catalyzes the demethylation of mono- or dimethyl-lysines.


Pssm-ID: 277112  Cd Length: 52  Bit Score: 63.50  E-value: 2.36e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568920205  266 LYCICRQPHN-NRFMICCDRCEEWFHGDCVGISEARGRLLERngedYICPNCTILQ 320
Cdd:cd15642     1 VYCLCRLPYDvTRFMIECDVCQDWFHGSCVGVEEEKAAEIDL----YHCPNCQVTH 52
SPOC_Bye1p-like cd21542
SPOC (Spen paralog and ortholog C-terminal) domain found in Saccharomyces cerevisiae bypass of ...
1051-1181 2.52e-11

SPOC (Spen paralog and ortholog C-terminal) domain found in Saccharomyces cerevisiae bypass of ESS1 protein 1 (Bye1p) and similar proteins; Yeast Bye1p is a nuclear transcription factor with a domain resembling the central domain in the transcription elongation factor TFIIS. It 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 SPOC domain. This model corresponds to the SPOC domain which is involved in developmental signaling and has also been proposed to be a phosphorylation binding module.


Pssm-ID: 439205  Cd Length: 153  Bit Score: 63.85  E-value: 2.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1051 IWKGFINMQSV-AKFVTKAYPVSGCL--------DYLSEDLPDTIHIGGRIAPKTVWDYVGKLKSSvsKELCLIRFHP-A 1120
Cdd:cd21542     1 VWKGTLEYPEInAEFSGKIKFVGSSTklskqnvkEQQDALGDKKLEVEGRLSAETADKYLNQIMSS--RDLLVYELEPnE 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568920205 1121 TEEEEVAYISLYSYFSSRGRFGVVANNNRHVKDLYLIPLSAKDPVPSKLLPFEGPGLESPR 1181
Cdd:cd21542    79 SSEDKTNFDKLFDYLHSRERYGVLKNKPSYVKDAYLIPLSAGDKPPILFIILNPISILEEE 139
PHD_MLL5 cd15550
PHD finger found in mixed lineage leukemia 5 (MLL5); MLL5 is a histone methyltransferase that ...
268-316 3.72e-11

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: 59.64  E-value: 3.72e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568920205  268 CICRQPHNNRFMICCDRCEEWFHGDCVGISEargrllERNGEDYICPNC 316
Cdd:cd15550     2 CICGFEHDDGFMICCDKCSVWQHGDCMGIDR------ENIPDSYLCEQC 44
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
267-316 6.04e-11

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: 59.25  E-value: 6.04e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568920205  267 YC-ICRQPHN-NRFMICCDRCEEWFHGDCVGISEARGRLlernGEDYICPNC 316
Cdd:cd15489     1 SCiVCGKGGDlGGELLQCDGCGKWFHADCLGPPLSSFVP----NGKWICPVC 48
PHD_PHF2 cd15641
PHD finger found in lysine-specific demethylase PHF2; PHF2, also termed GRC5, or PHD finger ...
267-316 7.10e-11

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: 59.26  E-value: 7.10e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568920205  267 YCICRQPHN-NRFMICCDRCEEWFHGDCVGISEARGRLLERngedYICPNC 316
Cdd:cd15641     1 YCICRLPYDvTRFMIECDACKDWFHGSCVGVEEEEAPDIDI----YHCPNC 47
PHA03247 PHA03247
large tegument protein UL36; Provisional
1571-2083 1.13e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 67.66  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1571 LPRAPTGSTPGPQGTlPARETPAGTAVVQGPGLAAEAkesmAVPWAPGEnavlrpehDIQKCEHPGNPVSLPLDTShlpt 1650
Cdd:PHA03247 2560 PPAAPDRSVPPPRPA-PRPSEPAVTSRARRPDAPPQS----ARPRAPVD--------DRGDPRGPAPPSPLPPDTH---- 2622
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1651 agdgAARPAPPrrvllptppsttfppsfplQPKAQNFSSGSREPFSGPTFMSQETSLGSSQYEDPRGAQSAGKNDSPVAD 1730
Cdd:PHA03247 2623 ----APDPPPP-------------------SPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSP 2679
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1731 MEDSREPQPRPG-ESTTSFPQPGQRGGGPQPQFPGQREPAPRTFGMSGHHGPSFPGPRGPVPPYSEEN-LVPNSDGPRGP 1808
Cdd:PHA03247 2680 PQRPRRRAARPTvGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGpATPGGPARPAR 2759
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1809 PPARFGaqkPPIPSLFSGQHGPPPygdnrglspsylggPRGGAPAQfedrkDPHGEKREFQDTPYNEmTGAPAQCEGPDQ 1888
Cdd:PHA03247 2760 PPTTAG---PPAPAPPAAPAAGPP--------------RRLTRPAV-----ASLSESRESLPSPWDP-ADPPAAVLAPAA 2816
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1889 AqfmgnrapfqfggqrrplLTQMKGPRGGPPPSQFGAQRGPPPghfvgPRGPHPSQFENSRGTHPGQFEGARGQapgfmP 1968
Cdd:PHA03247 2817 A------------------LPPAASPAGPLPPPTSAQPTAPPP-----PPGPPPPSLPLGGSVAPGGDVRRRPP-----S 2868
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1969 GPRGIQPQQFEEQRVNSPPRFAGQRASAPLPYggprgPAPFPEKNEQPPSRFHFQGPSSQPVKPPPRPLLELPSHPPQHR 2048
Cdd:PHA03247 2869 RSPAAKPAAPARPPVRRLARPAVSRSTESFAL-----PPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPL 2943
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 568920205 2049 KDRWDEAGPATALPSSAGPGQGHEADGQWATSEFR 2083
Cdd:PHA03247 2944 APTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFR 2978
PHD_Ecm5p_Lid2p_like cd15518
PHD finger found in Saccharomyces cerevisiae extracellular matrix protein 5 (Ecm5p), ...
267-316 1.66e-09

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: 55.05  E-value: 1.66e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568920205  267 YCICRQPHNNrFMICCDRCEEWFHGDCVGISeaRGRLleRNGEDYICPNC 316
Cdd:cd15518     1 YCFCRQGEGG-TMIECEICKEWYHVKCIKNG--RWKL--DDDDKFVCPIC 45
PHD2_KDM5A cd15606
PHD finger 2 found in Lysine-specific demethylase 5A (KDM5A); KDM5A (also termed Histone ...
267-316 3.42e-09

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


Pssm-ID: 277079  Cd Length: 56  Bit Score: 54.75  E-value: 3.42e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568920205  267 YCICRQPHNNrFMICCDRCEEWFHGDCVGISEARGRLLERNGED-------YICPNC 316
Cdd:cd15606     1 YCICRKPFSG-FMLQCELCKDWFHSSCVPLPKSSSQKKGGNGSGqgakelkFLCPLC 56
PHD_ING cd15505
PHD finger found in the inhibitor of growth (ING) protein family; The ING family includes a ...
267-316 4.10e-09

PHD finger found in the inhibitor of growth (ING) protein family; The ING family includes a group of tumor suppressors, ING1-5, which act as readers and writers of the histone epigenetic code, affecting DNA damage response, chromatin remodeling, cellular senescence, differentiation, cell cycle regulation and apoptosis. They may have a general role in mediating the cellular response to genotoxic stress through binding to and regulating the activities of histone acetyltransferase (HAT) and histone deacetylase (HDAC) chromatin remodeling complexes. All ING proteins contain an N-terminal ING domain and a C-terminal plant homeodomain (PHD) finger.


Pssm-ID: 276980 [Multi-domain]  Cd Length: 45  Bit Score: 53.84  E-value: 4.10e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568920205  267 YCICRQPHNNRfMICCD--RCE-EWFHGDCVGISEArgrlleRNGEDYiCPNC 316
Cdd:cd15505     1 YCICNQVSYGE-MVACDnpNCPiEWFHFECVGLTAK------PKGKWY-CPEC 45
PHD_TCF19_like cd15517
PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and ...
280-316 4.45e-09

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: 54.09  E-value: 4.45e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 568920205  280 ICCDRCEEWFHGDCVGISEARGRLlernGEDYICPNC 316
Cdd:cd15517    17 VQCDGCDKWFHQFCLGLSNERYAD----EDKFKCPNC 49
PHD3_KDM5A_like cd15610
PHD finger 3 found in Lysine-specific demethylase 5A (KDM5A), 5B (KDM5B), and similar proteins; ...
282-316 4.64e-09

PHD finger 3 found in Lysine-specific demethylase 5A (KDM5A), 5B (KDM5B), and similar proteins; The family includes KDM5A and KDM5B, both of which belong to the JARID subfamily within the JmjC proteins. KDM5A, also termed Histone demethylase JARID1A, or Jumonji/ARID domain-containing protein 1A, or Retinoblastoma-binding protein 2 (RBBP-2 or RBP2), was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK and BMAL1. KDM5A functions as the trimethylated histone H3 lysine 4 (H3K4me3) demethylase. It also displays DNA-binding activities that can recognize the specific DNA sequence CCGCCC. KDM5B, also termed Cancer/testis antigen 31 (CT31), or Histone demethylase JARID1B, or Jumonji/ARID domain-containing protein 1B (JARID1B), or PLU-1, or retinoblastoma-binding protein 2 homolog 1 (RBP2-H1 or RBBP2H1A), 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. KDM5B acts as a histone demethylase that catalyzes the removal of trimethylation of lysine 4 on histone H3 (H3K4me3), induced by polychlorinated biphenyls (PCBs). It also mediates demethylation of H3K4me2 and H3K4me1. Moreover, KDM5B functions as a negative regulator of hematopoietic stem cell (HSC) self-renewal and progenitor cell activity. KDM5B has also been shown to interact with the DNA binding transcription factors BF-1 and PAX9, as well asTIEG1/KLF10 (transforming growth factor-beta inducible early gene-1/Kruppel-like transcription factor 10), and possibly function as a transcriptional corepressor. The family also includes the Drosophila melanogaster protein little imaginal discs (Lid) that functions as a JmjC-dependent trimethyl histone H3K4 (H3K4me3) demethylase, which is required for dMyc-induced cell growth. It positively regulates Hox gene expression in S2 cells. Members in this family contain the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the third PHD finger.


Pssm-ID: 277083 [Multi-domain]  Cd Length: 50  Bit Score: 53.87  E-value: 4.64e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568920205  282 CDRCEEWFHGDCVGISEargrLLERNGEDYICPNC 316
Cdd:cd15610    20 CDGCEEWFHLLCVGLSP----EEVAEDEDYICPSC 50
PHD_TAF3 cd15522
PHD finger found in transcription initiation factor TFIID subunit 3 (TAF3); TAF3 (also termed ...
267-316 2.26e-08

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: 51.90  E-value: 2.26e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568920205  267 YC-ICRQPHNNRFMICCDRCEEWFHGDCVGISEArgrllERNGEDYICPNC 316
Cdd:cd15522     1 ICpICKKPDDGSPMIGCDECDDWYHWECVGITDE-----PPEEDDWFCPKC 46
PHD_AL_plant cd15613
PHD finger found in plant Alfin1-like (AL) proteins; AL proteins are ubiquitously expressed ...
275-317 6.13e-08

PHD finger found in plant Alfin1-like (AL) proteins; AL proteins are ubiquitously expressed nuclear proteins existing only in plants. They are involved in chromatin regulation by binding to tri- and dimethylated histone H3 at lysine 4 (H3K4me3/2), the active histone markers, through their plant homeodomain (PHD) fingers.


Pssm-ID: 277085  Cd Length: 51  Bit Score: 50.96  E-value: 6.13e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568920205  275 NNRFMICCDRCEEWFHGDCVGISEARGRLLERngedYICPNCT 317
Cdd:cd15613    11 ADEFWICCDVCEKWYHGKCVKITPAKAEHIKQ----YKCPSCS 49
TNG2 COG5034
Chromatin remodeling protein, contains PhD zinc finger [Chromatin structure and dynamics];
157-299 7.69e-08

Chromatin remodeling protein, contains PhD zinc finger [Chromatin structure and dynamics];


Pssm-ID: 227367 [Multi-domain]  Cd Length: 271  Bit Score: 56.10  E-value: 7.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  157 TLKELQNRLRRKREQEPVERSlrgSQNRLRKKRREEDSAETGSVQI---------GSAEQDRPLCKQEpEASQGPVSQSE 227
Cdd:COG5034   115 VAARIENCHDAVSRLERNSYS---SAARRSSGEHRSAASSQGSRHTklkkrknihNLKRRSPELSSKR-EVSFTLESPSV 190
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568920205  228 TDDIENQLEGKATQGNTEENPREAGKPKPEcevydpnALYCICRQPHNNRfMICCD--RCE-EWFHGDCVGISEA 299
Cdd:COG5034   191 PDTATRVKEGNNGGSTKSRGVSSEDNSEGE-------ELYCFCQQVSYGQ-MVACDnaNCKrEWFHLECVGLKEP 257
PHD_UBR7 cd15542
PHD finger found in putative E3 ubiquitin-protein ligase UBR7; UBR7, also termed N-recognin-7, ...
267-316 1.45e-07

PHD finger found in putative E3 ubiquitin-protein ligase UBR7; UBR7, also termed N-recognin-7, is a UBR box-containing protein that belongs to the E3 ubiquitin ligase family that recognizes N-degrons or structurally related molecules for ubiquitin-dependent proteolysis or related processes through the UBR box motif. In addition to the UBR box, UBR7 also harbors a plant homeodomain (PHD) finger. The biochemical properties of UBR7 remain unclear.


Pssm-ID: 277017  Cd Length: 54  Bit Score: 50.06  E-value: 1.45e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568920205  267 YCICRQPHN------NRFMICCDRCEEWFHGDCVGISEArgRLLERNGEDYICPNC 316
Cdd:cd15542     1 YCTCDRPYPdpedevEDEMIQCVLCEDWFHGRHLGLTPP--EPDPDEFDEMICSGC 54
PHD_MMD1_like cd15556
PHD finger found in Arabidopsis thaliana PHD finger protein MALE MEIOCYTE DEATH 1 (MMD1), PHD ...
268-316 1.64e-07

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: 49.69  E-value: 1.64e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568920205  268 CICRQPHNN--RfMICCDRCEEWFHGDCVGISEArgrllERNGEDYICPNC 316
Cdd:cd15556     2 CSCGTRDDDgeR-MIACDVCEVWQHTRCVGIADN-----EEPPDHFLCRRC 46
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1684-2078 1.80e-07

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: 56.56  E-value: 1.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1684 AQNFSS-GSREPFSGPtfMSQETSLGSSQYEDPRGAQSAGKNDSPVADMEDSREPQPRPGESTTSFPQPGQRGGGPQPQF 1762
Cdd:pfam09606   86 LQNLAGqGTRPQMMGP--MGPGPGGPMGQQMGGPGTASNLLASLGRPQMPMGGAGFPSQMSRVGRMQPGGQAGGMMQPSS 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1763 PGQREPAPRTfgMSGHHGPSFPGPRGPVPPyseenlvpNSDGPRGPPPARFGAQKPPIPSLfSGQHGPPPYGDNRGLSPs 1842
Cdd:pfam09606  164 GQPGSGTPNQ--MGPNGGPGQGQAGGMNGG--------QQGPMGGQMPPQMGVPGMPGPAD-AGAQMGQQAQANGGMNP- 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1843 ylgGPRGGAPAQFEdrkdphgekrefqdtpyneMTGAPAQCEGPDQAQFMGNRAPFQF-GGQRRPLLTQMKGPRGGPPPS 1921
Cdd:pfam09606  232 ---QQMGGAPNQVA-------------------MQQQQPQQQGQQSQLGMGINQMQQMpQGVGGGAGQGGPGQPMGPPGQ 289
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1922 QFGAQ------RGPPPGHFVGPRGPHPSQFENSRGTHPGQF-----EGARGQAPGFMPGPRGIQPQQFEEQRVNSPPRFA 1990
Cdd:pfam09606  290 QPGAMpnvmsiGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMnqsvgQGGQVVALGGLNHLETWNPGNFGGLGANPMQRGQ 369
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1991 GQRASAPLPYGGPRGPAPFPEKNEQPPSRFHF---QGPSSQPVKPPPRPLLELPSHPPQHRKDRWDEAgPATALPSSAGP 2067
Cdd:pfam09606  370 PGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVpspQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQP-AQQRTIGQDSP 448
                          410
                   ....*....|.
gi 568920205  2068 GQGHEADGQWA 2078
Cdd:pfam09606  449 GGSLNTPGQSA 459
PHD_ING3 cd15585
PHD finger found in inhibitor of growth protein 3 (ING3) and similar proteins; ING3, also ...
267-316 1.56e-06

PHD finger found in inhibitor of growth protein 3 (ING3) and similar proteins; ING3, also termed p47ING3, is one member of the inhibitor of growth (ING) family of type II tumor suppressors. It is ubiquitously expressed and has been implicated in transcription modulation, cell cycle control, and the induction of apoptosis. It is an important subunit of human NuA4 histone acetyltransferase complex, which regulates the acetylation of histones H2A and H4. Moreover, ING3 promotes ultraviolet (UV)-induced apoptosis through the Fas/caspase-8-dependent pathway in melanoma cells. It physically interacts with subunits of E3 ligase Skp1-Cullin-F-boxprotein complex (SCF complex) and is degraded by the SCF (F-box protein S-phase kinase-associated protein 2, Skp2)-mediated ubiquitin-proteasome system. It also acts as a suppression factor during tumorigenesis and progression of hepatocellular carcinoma (HCC). ING3 contains an N-terminal ING domain and a C-terminal plant homeodomain (PHD) finger.


Pssm-ID: 277060 [Multi-domain]  Cd Length: 45  Bit Score: 46.68  E-value: 1.56e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568920205  267 YCICRQPHNNRfMICCD--RCE-EWFHGDCVGISEA-RGRllerngedYICPNC 316
Cdd:cd15585     1 YCICNQVSYGE-MVGCDndDCPiEWFHYGCVGLTEApKGK--------WYCPQC 45
PHD3_Lid2p_like cd15520
PHD finger 3 found in Schizosaccharomyces pombe Lid2 complex component Lid2p and similar ...
268-316 4.17e-06

PHD finger 3 found in Schizosaccharomyces pombe Lid2 complex component Lid2p and similar proteins; 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. The family corresponds to the third PHD finger.


Pssm-ID: 276995  Cd Length: 47  Bit Score: 45.67  E-value: 4.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568920205  268 CICRQPHNNR-FMICCDRCEEWFHGDCVGISEArgrlLERNGEDYICPNC 316
Cdd:cd15520     2 CGCGEGFNIAdRMIFCDRCERTVHLDCVGLSDR----IVDSPSEFFCPEC 47
SPOC_FPA-like cd21546
SPOC (Spen paralog and ortholog C-terminal) domain found in Arabidopsis thaliana flowering ...
1051-1189 4.86e-06

SPOC (Spen paralog and ortholog C-terminal) domain found in Arabidopsis thaliana flowering time control protein FPA and similar proteins; FPA plays a role in the regulation of flowering time in the autonomous flowering pathway by decreasing FLOWERING LOCUS C mRNA levels. It is required for RNA-mediated chromatin silencing of a range of loci in the genome. FPA cotranscriptionally recognizes aberrant RNA and marks it for silencing. It controls alternative cleavage and polyadenylation on pre-mRNAs and antisense RNAs. FPA functions redundantly with FCA to prevent the expression of distally polyadenylated antisense RNAs at the FLC locus. FPA belongs to the Spen (split end) protein family, whose members contain three N-terminal RNA recognition motifs (RRMs), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal SPOC domain. This model corresponds to the SPOC domain that is involved in developmental signaling and has also been proposed to be a phosphorylation binding module.


Pssm-ID: 439209  Cd Length: 125  Bit Score: 47.67  E-value: 4.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1051 IWKGFINMQSvaKFVTK--AYPVSGclDYLSED--LPDTIHIGGRiapkTVWDYVgKLKSSVSKELCLIrFHPATEEEEV 1126
Cdd:cd21546     1 KWSGTLAKSG--KPRCNvvAHPVSG--DVAREPvsLPEVLNVSHR----TDLEEV-AHKPVARAVLVLL-FAPENESDRG 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568920205 1127 AYISLYSYFSSRGRFGVVA-NNNRHvkdLYLIPLSakDPVPSKLLPFegpgleSPRPNIILGLV 1189
Cdd:cd21546    71 AFDEFIDYLSSKDRAGVVKlPDNRT---LYLVPPS--EELFSQLLLN------VIRQNCLLGIV 123
PHA03247 PHA03247
large tegument protein UL36; Provisional
1515-1861 5.38e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.25  E-value: 5.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1515 PPPKSSLGKTELFSQEQ-QAPDPSQGAPNTNHNLDSRQSRDPRQARRLAAENTENESLPRA---PTGST-----PGPQGT 1585
Cdd:PHA03247 2627 PPPSPSPAANEPDPHPPpTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAarpTVGSLtsladPPPPPP 2706
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1586 LPA-RETPAGTAVVQGPGLAAEAKESMAVPWAPgenaVLRPEHDIQKCEHPGNPVSLPLDTSHLPTAGDGAARPAPPRRV 1664
Cdd:PHA03247 2707 TPEpAPHALVSATPLPPGPAAARQASPALPAAP----APPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR 2782
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1665 LLPTPPSTTFPPSFPL-------------------QPKAQNFSSGSREPFSGPTFMSQETSLGSSQYEDPRGAQSAGknd 1725
Cdd:PHA03247 2783 LTRPAVASLSESRESLpspwdpadppaavlapaaaLPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPG--- 2859
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1726 SPVADMEDSREPQPRPGEST----TSFPQPG-QRGGGPQPQFPGQREPAPRTfgmsghhgpsfPGPRGPVPPYSEEnlVP 1800
Cdd:PHA03247 2860 GDVRRRPPSRSPAAKPAAPArppvRRLARPAvSRSTESFALPPDQPERPPQP-----------QAPPPPQPQPQPP--PP 2926
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568920205 1801 NSDGPRGPPPARFGAQKPPI--PSLFSGQHGPPPYGDNRGLSPSYLGGPRGGAPAQFEDRKDP 1861
Cdd:PHA03247 2927 PQPQPPPPPPPRPQPPLAPTtdPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAP 2989
PHD_Bye1p_SIZ1_like cd15570
PHD domain found in Saccharomyces cerevisiae bypass of ESS1 protein 1 (Bye1p), the E3 Sumo ...
268-316 1.11e-05

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: 44.37  E-value: 1.11e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568920205  268 CICRQPHNNRFMICCDRCEEWFHGDCVGISEARGRLLERNGEDYICPNC 316
Cdd:cd15570     2 CPCGSSMEDGSMIQCEGCKTWQHMDCVLIPDKPADGLPELPSKFYCELC 50
PHD2_KDM5A_like cd15516
PHD finger 2 found in Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D, and similar ...
267-316 2.04e-05

PHD finger 2 found in Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D, and similar proteins; The JARID subfamily within the JmjC proteins includes Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and a Drosophila homolog protein, little imaginal discs (Lid). 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 interacting 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. KDM5C is a H3K4 trimethyl-histone demethylase that catalyzes demethylation of H3K4me3 and H3K4me2 to H3K4me1. It plays a role in neuronal survival and dendrite development. KDM5C defects are associated with X-linked mental retardation (XLMR). KDM5D is a male-specific antigen that shows a demethylase activity specific for di- and tri-methylated histone H3K4 (H3K4me3 and H3K4me2), and has a male-specific function as a histone H3K4 demethylase by recruiting a meiosis-regulatory protein, MSH5, to condensed DNA. KDM5D directly interacts with a polycomb-like protein Ring6a/MBLR, and plays a role in regulation of transcriptional initiation through H3K4 demethylation. The family also includes Drosophila melanogaster protein little imaginal discs (Lid) that functions as a JmjC-dependent trimethyl histone H3K4 (H3K4me3) demethylase, which is required for dMyc-induced cell growth. It positively regulates Hox gene expression in S2 cells. Members in this family contain the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as two or three plant homeodomain (PHD) fingers. This model corresponds to the second PHD finger.


Pssm-ID: 276991  Cd Length: 53  Bit Score: 43.84  E-value: 2.04e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568920205  267 YCICRQPHNNrFMICCDRCEEWFHGDCVGI----SEARGRLLERNGEDYICPNC 316
Cdd:cd15516     1 ICLCGKALAA-GMLQCELCQDWFHGSCVAVprisSSPRPLAWWEGDRKFLCPLC 53
PHD_PHF20 cd15634
PHD finger found in PHD finger protein 20 (PHF20); PHF20, also termed Glioma-expressed antigen ...
268-316 2.39e-05

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: 43.40  E-value: 2.39e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568920205  268 CICRQPHNNRFMICCDRCEEWFHGDCVGiseargrLLERN-GEDYICPNC 316
Cdd:cd15634     2 CICEVQEENDFMIQCEECLCWQHGVCMG-------LLEDNvPEKYTCYIC 44
PHD_PHF20_like cd15549
PHD finger found in PHD finger protein 20 (PHF20) and PHD finger protein 20-like protein 1 ...
268-316 3.76e-05

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: 42.85  E-value: 3.76e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568920205  268 CICRQPHNNRFMICCDRCEEWFHGDCVGISEArgrllERNGEDYICPNC 316
Cdd:cd15549     2 CICGVNEENGLMIQCELCLCWQHGVCMGIEEE-----ESVPERYVCYVC 45
PHD1_KMT2A_like cd15506
PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...
279-316 5.36e-05

PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This family includes histone-lysine N-methyltransferase trithorax (Trx) like proteins, KMT2A (MLL1) and KMT2B (MLL2), which comprise the mammalian Trx branch of the COMPASS family, and are both essential for mammalian embryonic development. KMT2A regulates chromatin-mediated transcription through the catalysis of methylation of histone 3 lysine 4 (H3K4), and is frequently rearranged in acute leukemia. KMT2A functions as the catalytic subunit in the MLL1 complex. KMT2B is a second human homolog of Drosophila trithorax, located on chromosome 19 and functions as the catalytic subunit in the MLL2 complex. It plays a critical role in memory formation through mediating hippocampal H3K4 di- and trimethylation. It is also required for RNA polymerase II association and protection from DNA methylation at the MagohB CpG island promoter. Both KMT2A and KMT2B contain a CxxC (x for any residue) zinc finger domain, three plant homeodomain (PHD) fingers, an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the first PHD finger.


Pssm-ID: 276981  Cd Length: 47  Bit Score: 42.35  E-value: 5.36e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568920205  279 MICCDRCEEWFHGDCVgisEARGRLLERNGEDYICPNC 316
Cdd:cd15506    13 LLYCSVCCEPYHTFCL---EEAERPLNINKDNWCCRRC 47
PHD_ING1_2 cd15584
PHD finger found in inhibitor of growth protein 1 (ING1) and 2 (ING2); ING1 is an epigenetic ...
267-316 1.19e-04

PHD finger found in inhibitor of growth protein 1 (ING1) and 2 (ING2); ING1 is an epigenetic regulator and a type II tumor suppressor that impacts cell growth, aging, apoptosis, and DNA repair, by affecting chromatin conformation and gene expression. It acts as a reader of the active chromatin mark, the trimethylation of histone H3 lysine 4 (H3K4me3). It binds and directs Growth arrest and DNA damage inducible protein 45 a (Gadd45a) to target sites, thus linking the histone code with DNA demethylation. It interacts with the proliferating cell nuclear antigen (PCNA) via the PCNA-interacting protein (PIP) domain in a UV-inducible manner. It also interacts with a PCNA-interacting protein, p15 (PAF). Moreover, ING1 associates with members of the 14-3-3 family, which is necessary for cytoplasmic relocalization. Endogenous ING1 protein specifically interacts with the pro-apoptotic BCL2 family member BAX and colocalizes with BAX in a UV-inducible manner. It stabilizes the p53 tumor suppressor by inhibiting polyubiquitination of multi-monoubiquitinated forms via interaction with and colocalization of the herpesvirus-associated ubiquitin-specific protease (HAUSP)-deubiquitinase with p53. It is also involved in trichostatin A-induced apoptosis and caspase 3 signaling in p53-deficient glioblastoma cells. In addition, tyrosine kinase Src can bind and phosphorylate ING1 and further regulates its activity. ING2, also termed inhibitor of growth 1-like protein (ING1Lp), or p32, or p33ING2, belongs to the inhibitor of growth (ING) family of type II tumor suppressors. It is a core component of a multi-factor chromatin-modifying complex containing the transcriptional co-repressor SIN3A and histone deacetylase 1 (HDAC1). It has been implicated in the control of cell cycle, in genome stability, and in muscle differentiation. ING2 independently interacts with H3K4me3 (Histone H3 trimethylated on lysine 4) and PtdIns(5)P, and modulates crosstalk between lysine methylation and lysine acetylation on histone proteins through association with chromatin in the presence of DNA damage. It collaborates with SnoN to mediate transforming growth factor (TGF)-beta-induced Smad-dependent transcription and cellular responses. It is upregulated in colon cancer and increases invasion by enhanced MMP13 expression. It also acts as a cofactor of p300 for p53 acetylation and plays a positive regulatory role during p53-mediated replicative senescence. Both ING1 and ING2 contain an N-terminal ING domain and a C-terminal plant homeodomain (PHD) finger.


Pssm-ID: 277059 [Multi-domain]  Cd Length: 45  Bit Score: 41.28  E-value: 1.19e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568920205  267 YCICRQPHNNRfMICCD--RCE-EWFHGDCVGIS-EARGRllerngedYICPNC 316
Cdd:cd15584     1 YCLCNQVSYGE-MIGCDndECPiEWFHFSCVGLThKPKGK--------WYCPKC 45
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
2142-2180 1.53e-04

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 46.84  E-value: 1.53e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 568920205  2142 SRERDWERSRDWDRHREWDKGRDRSSNRDRERDNDRAKE 2180
Cdd:TIGR01622    6 ERERLRDSSSAGDRDRRRDKGRERSRDRSRDRERSRSRR 44
PHD2_PHF10 cd15529
PHD finger 2 found in PHD finger protein 10 (PHF10) and similar proteins; PHF10, also termed ...
268-316 1.67e-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: 41.14  E-value: 1.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568920205  268 CICRQPHNNRFMICCDRCEEWFHGDCVGISE-ARGRllerngedYICPNC 316
Cdd:cd15529     3 TKCGDPHDEDKMMFCDQCDRGYHTFCVGLRSiPDGR--------WICPLC 44
PHD3_KDM5A cd15686
PHD finger 3 found in Lysine-specific demethylase 5A (KDM5A); KDM5A, also termed Histone ...
270-317 2.28e-04

PHD finger 3 found in Lysine-specific demethylase 5A (KDM5A); KDM5A, also termed Histone demethylase JARID1A, or Jumonji/ARID domain-containing protein 1A, or Retinoblastoma-binding protein 2 (RBBP-2 or RBP2), was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK and BMAL1. KDM5A functions as a trimethylated histone H3 lysine 4 (H3K4me3) demethylase that belongs to the JARID subfamily within the JmjC proteins. It also displays DNA-binding activities that can recognize the specific DNA sequence CCGCCC. KDM5A contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the third PHD finger.


Pssm-ID: 277156  Cd Length: 52  Bit Score: 40.82  E-value: 2.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568920205  270 CRQPHNNR--FMICCDRCEEWFHGDCVGISEARGRllernGEDYICPNCT 317
Cdd:cd15686     8 CQRPCKDKvdWVQCDGGCDEWFHQVCVGVSPEMAE-----NEDYICINCA 52
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1562-2024 2.68e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1562 AAENTENESLPRAPTGSTP-----GPQGTLPARETPAGTAVVQGPGLAAEAKESMAVPWAPGENAVLRPEHDIQKCEHPG 1636
Cdd:PHA03307   14 AAEGGEFFPRPPATPGDAAddllsGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLS 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1637 NPVSLPLDTSHLPTAGDGAARPAPPRRVLLPTPPSTTFPPSFPLQPKAQNFSSGSREPFSGPtfmsqetslGSSQYEDPR 1716
Cdd:PHA03307   94 TLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAA---------GASPAAVAS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1717 GAQSAGKNDSPVADMEDSREPQPRPGESTTSFPQPGQRGGGPQPQFPGQREPAPRTFGMSGHHGPSFPG--------PRG 1788
Cdd:PHA03307  165 DAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGasssdsssSES 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1789 PVPPYSEENLVPNSDGPRGPPPARFGAQKPPIPSLFSGQHGPPPYGDNRGLSPSYLGGPRGGAPAQfedrkdPHGEKREF 1868
Cdd:PHA03307  245 SGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPS------SPRASSSS 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1869 QDTPYNEMTGAPAQCEGPDQAQFMGNRAPfqfggqrrplltqmkgPRGGPPPSQFGAQRGPPPghfvgPRGPHPSQFENS 1948
Cdd:PHA03307  319 SSSRESSSSSTSSSSESSRGAAVSPGPSP----------------SRSPSPSRPPPPADPSSP-----RKRPRPSRAPSS 377
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568920205 1949 RGTHPGQFEGARGQAPGFMPGPRGIQPQQFEEQRVNSPPRFAGQRASAPLPYGGPRGPA--PFPEKNEQPPSRFHFQG 2024
Cdd:PHA03307  378 PAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYPLLTPSgePWPGSPPPPPGRVRYGG 455
PHD_PHF20L1 cd15633
PHD finger found in PHD finger protein 20-like protein 1 (P20L1); P20L1 is an active malignant ...
268-317 2.68e-04

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: 40.39  E-value: 2.68e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568920205  268 CICRQPHNNRFMICCDRCEEWFHGDCVGISEargrllERNGEDYICPNCT 317
Cdd:cd15633     2 CICEMDEENGFMIQCEECLCWQHSVCMGLLE------ESIPEQYICYICR 45
PHD_SHPRH cd15547
PHD finger found in E3 ubiquitin-protein ligase SHPRH; SHPRH, also termed SNF2, histone-linker, ...
268-316 3.16e-04

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: 40.47  E-value: 3.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568920205  268 CIC--RQPHNNRFMICCDRCEEWFHGDCVGI-SEARGRllerngEDYICPNC 316
Cdd:cd15547     2 CICgeLDEIDNKHRVQCLKCGLWQHAECVNYdEESDKR------EPYLCPHC 47
PHD_ASH1L cd15548
PHD finger found in histone-lysine N-methyltransferase ASH1L; ASH1L, also termed ASH1-like ...
268-316 3.39e-04

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: 40.14  E-value: 3.39e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568920205  268 CICRQPHNNRFMICCDRCEEWFHGDCVGISEargrllerNGEDYICPNC 316
Cdd:cd15548     3 CICGLYKDEGLMIQCEKCMVWQHCDCMGVND--------DVEHYLCEQC 43
PHD_ARID4_like cd15615
PHD finger found in Arabidopsis thaliana AT-rich interactive domain-containing protein 4 ...
280-316 3.42e-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: 40.54  E-value: 3.42e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568920205  280 ICCDRCEEWFHGDCvgisEARGRL-----LERNGEDYICPNC 316
Cdd:cd15615    20 VQCDSCSEWVHFEC----DGRTGLgafkyAKSDGLQYVCPRC 57
PHD_Yng1p_like cd15587
PHD finger found in yeast orthologs of ING tumor suppressor family; The yeast orthologs of the ...
267-317 3.99e-04

PHD finger found in yeast orthologs of ING tumor suppressor family; The yeast orthologs of the plant homeodomain (PHD) finger-containing ING tumor suppressor family consists of chromatin modification-related protein YNG1 (Yng1p), YNG2 (Yng2p), and transcriptional regulatory protein PHO23 (Pho23p). Yng1p, also termed ING1 homolog 1, is one of the components of the NuA3 histone acetyltransferase (HAT) complex. Its PHD finger binding to H3 Trimethylated at K4 (H3K4me3) promotes NuA3 H3 HAT activity at K14 of H3 on chromatin. Yng2p, also termed ESA1-associated factor 4, or ING1 homolog 2, is a subunit of the NuA4 HAT complex. It plays a critical role in intra-S-phase DNA damage response. Pho23p is part of the Rpd3/Sin3 histone deacetylase (HDAC) complex. It is required for the normal function of Rpd3 in the silencing of rDNA, telomeric, and mating-type loci. Yng1p and Pho23p inhibit p53-dependent transcription. In contrast, Yng2p has the opposite effect. All family members contain an N-terminal ING histone-binding domain and a C-terminal PHD finger.


Pssm-ID: 277062 [Multi-domain]  Cd Length: 47  Bit Score: 40.09  E-value: 3.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568920205  267 YCICRQPHNNRfMICCDR--CE-EWFHGDCVGISEA-RGRllerngedYICPNCT 317
Cdd:cd15587     1 YCYCRRVSFGE-MVACDNpdCKiEWFHFECVGLTETpKGK--------WYCSDCK 46
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
1888-2049 4.41e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 45.57  E-value: 4.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1888 QAQFMgnrapfqfggQRRPLLTQMkgprggPPPSQFGAQRGPPPGHFVGPRGPHPSQFENsrgtHPGQFEGARGQAPGFM 1967
Cdd:TIGR01628  372 QDQFM----------QLQPRMRQL------PMGSPMGGAMGQPPYYGQGPQQQFNGQPLG----WPRMSMMPTPMGPGGP 431
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1968 PGPRGIQP----QQFEEQRVNSPPRfagqRASAPLPYGGPRGPAPFPEKNEQPPSRFHFQGPSSQpvkppprPLLELPSH 2043
Cdd:TIGR01628  432 LRPNGLAPmnavRAPSRNAQNAAQK----PPMQPVMYPPNYQSLPLSQDLPQPQSTASQGGQNKK-------LAQVLASA 500

                   ....*.
gi 568920205  2044 PPQHRK 2049
Cdd:TIGR01628  501 TPQMQK 506
PHA03379 PHA03379
EBNA-3A; Provisional
1617-2029 4.57e-04

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 45.43  E-value: 4.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1617 PGENAVLRPEHDIQKCEHPGNPVSLPLDTSHlptagDGAARPAPP------RRVLLPTPPSTTFPPSFPLQPKAQNFSSG 1690
Cdd:PHA03379  341 HDEGATGETREESEDTESDGDDEELPRIVSR-----EGTKRKRPPiflrrlHRLLLMRAGKLTERAREALEKASEPTYGT 415
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1691 SREPFSGP-----TFMSQETSLGSSQYEDPRGAQSA---------GKNDSPVADMEDSREPQPRPGESTTSFPQPGQRGG 1756
Cdd:PHA03379  416 PRPPVEKPrpevpQSLETATSHGSAQVPEPPPVHDLepgplhdqhSMAPCPVAQLPPGPLQDLEPGDQLPGVVQDGRPAC 495
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1757 GPQPQFPGqrePAPRTFGMSGHHGPSF-PGPRGPVPPYSEENLVPNS--DGPRGPPPARFGAQKPPIPS---LFSGQHGP 1830
Cdd:PHA03379  496 APVPAPAG---PIVRPWEASLSQVPGVaFAPVMPQPMPVEPVPVPTValERPVCPAPPLIAMQGPGETSgivRVRERWRP 572
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1831 PPYGDNRGLSPSYLggPRGGAPAQFEDRKDPHGEKREFQDTpynEMTGAPAQC-----EGPDQAQFMGNRAPFQFGGQRR 1905
Cdd:PHA03379  573 APWTPNPPRSPSQM--SVRDRLARLRAEAQPYQASVEVQPP---QLTQVSPQQpmeypLEPEQQMFPGSPFSQVADVMRA 647
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1906 PLLTQMKGPRGGPPPSQFGAQRGP--PPGHFVGPRGPHPSQFEN----------SRGTHPGQFEGARGQAPGFMPgPRGI 1973
Cdd:PHA03379  648 GGVPAMQPQYFDLPLQQPISQGAPlaPLRASMGPVPPVPATQPQyfdipltepiNQGASAAHFLPQQPMEGPLVP-ERWM 726
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568920205 1974 QPQQFEEQRVN---SPPRFAGQRASAPLPYGGPRGPAPFPEKNEQP--PSRFHFQGPSSQP 2029
Cdd:PHA03379  727 FQGATLSQSVRpgvAQSQYFDLPLTQPINHGAPAAHFLHQPPMEGPwvPEQWMFQGAPPSQ 787
PHD3_KMT2C cd15511
PHD finger 3 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...
254-316 5.09e-04

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


Pssm-ID: 276986  Cd Length: 52  Bit Score: 39.78  E-value: 5.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568920205  254 PKPECEvydpnalyCICrQPHNNRFMICCDRCEEWFHGDCVGISEarGRLLERNGEDYICPNC 316
Cdd:cd15511     1 PCPACK--------KNL-DPELQKDMLHCHVCKRWIHLECEKPND--NELLDQLKEDYICSLC 52
PHD3_KDM5B cd15687
PHD finger 3 found in lysine-specific demethylase 5B (KDM5B); KDM5B, also termed Cancer/testis ...
270-316 7.26e-04

PHD finger 3 found in lysine-specific demethylase 5B (KDM5B); KDM5B, also termed Cancer/testis antigen 31 (CT31), or Histone demethylase JARID1B, or Jumonji/ARID domain-containing protein 1B (JARID1B), or PLU-1, or retinoblastoma-binding protein 2 homolog 1 (RBP2-H1 or RBBP2H1A), is a member of the JARID subfamily within the JmjC proteins. It has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. KDM5B acts as a histone demethylase that catalyzes the removal of trimethylation of lysine 4 on histone H3 (H3K4me3), induced by polychlorinated biphenyls (PCBs). It also mediates demethylation of H3K4me2 and H3K4me1. Moreover, KDM5B functions as a negative regulator of hematopoietic stem cell (HSC) self-renewal and progenitor cell activity. KDM5B has also been shown to interact with the DNA binding transcription factors BF-1 and PAX9, as well as TIEG1/KLF10 (transforming growth factor-beta inducible early gene-1/Kruppel-like transcription factor 10), and possibly function as a transcriptional corepressor. KDM5B contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the third PHD finger.


Pssm-ID: 277157  Cd Length: 50  Bit Score: 39.54  E-value: 7.26e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568920205  270 CRQPHNNRF-MICCD-RCEEWFHGDCVGISearGRLLERngEDYICPNC 316
Cdd:cd15687     7 CLQPEGEEVdWVQCDgSCNRWFHQVCVGVS---AEMAEK--EDYICVSC 50
PHD_PHF13_like cd15546
PHD finger found in PHD finger proteins PHF13 and PHF23; PHF13, also termed survival ...
268-316 9.17e-04

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: 38.96  E-value: 9.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568920205  268 CICRQPHNNRFMICCDRCEEWFHGDCVGIseargrllERNG--EDYICPNC 316
Cdd:cd15546     2 CFCGKPFAGRPMIECSECLTWIHLSCAKI--------RKNNvpEVFICQKC 44
PHD_PHF13 cd15632
PHD finger found in PHD finger protein 13 (PHF13); PHF13, also termed survival time-associated ...
268-316 1.94e-03

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: 38.10  E-value: 1.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568920205  268 CICRQPHNNRFMICCDRCEEWFHGDCVGISEArgrlleRNGEDYICPNC 316
Cdd:cd15632     4 CFCMKPFAGRPMIECNECHTWIHLSCAKIRKS------NVPEVYVCQKC 46
PHD_RSF1 cd15543
PHD finger found in Remodeling and spacing factor 1 (Rsf-1); Rsf-1, also termed HBV ...
268-316 2.53e-03

PHD finger found in Remodeling and spacing factor 1 (Rsf-1); Rsf-1, also termed HBV pX-associated protein 8, or Hepatitis B virus X-associated protein alpha (HBxAPalpha), or p325 subunit of RSF chromatin-remodeling complex, is a novel nuclear protein with histone chaperon function. It is a subunit of an ISWI chromatin remodeling complex, remodeling and spacing factor (RSF), and plays a role in mediating ATPase-dependent chromatin remodeling and conferring tumor aggressiveness in common carcinomas. As an ataxia-telangiectasia mutated (ATM)-dependent chromatin remodeler, Rsf-1 facilitates DNA damage checkpoints and homologous recombination repair. It regulates the mitotic spindle checkpoint and chromosome instability through the association with serine/threonine kinase BubR1 (BubR1) and Hepatitis B virus (HBV) X protein (HBx) in the chromatin fraction during mitosis. It also interacts with cyclin E1 and promotes tumor development. Rsf-1 contains a plant homeodomain (PHD) finger.


Pssm-ID: 277018 [Multi-domain]  Cd Length: 46  Bit Score: 37.63  E-value: 2.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568920205  268 CICRQPHNNRFMICCDRCEEWFHGDCVgiseaRGRLLERNGEDYICPNC 316
Cdd:cd15543     3 RKCGLSDHPEWILLCDRCDAGYHTACL-----RPPLMIIPDGNWFCPPC 46
PRK14954 PRK14954
DNA polymerase III subunits gamma and tau; Provisional
600-665 2.65e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184918 [Multi-domain]  Cd Length: 620  Bit Score: 43.01  E-value: 2.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568920205  600 WPSATLSGTSARQAGPTPMTAASKKlPGSAAVVGVTRKPMSANVPAASPAPGRLGPVSPAPSQPNS 665
Cdd:PRK14954  381 APSPAGSPDVKKKAPEPDLPQPDRH-PGPAKPEAPGARPAELPSPASAPTPEQQPPVARSAPLPPS 445
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
1877-2029 2.80e-03

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


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 43.10  E-value: 2.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1877 TGAPAQCEGPDQAQFMgnrapfQFGGQRRPLLTQMKGPRGGPPPSQFGAQRGPPPGHFVGPRGPHPSQFENSRGTHPGQF 1956
Cdd:pfam09770  215 APAPAQPPAAPPAQQA------QQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQPDPAQPSIQPQAQQF 288
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568920205  1957 egaRGQAPGFMPGPRGIQPQqfeeqrvnsPPRFAGQRASAPLPYGGPRGPAPFPEKNEQPPSRFHFQGPSSQP 2029
Cdd:pfam09770  289 ---HQQPPPVPVQPTQILQN---------PNRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITHP 349
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1725-1946 2.93e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 2.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1725 DSPVADMEDSREPQPRPGESTTSFPQPGQRGGGPQPQFPGQREPAPRtfGMSGHHGPSFPGPRGPVPPYSEENlvPNSDG 1804
Cdd:PRK07764  591 APGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPA--EASAAPAPGVAAPEHHPKHVAVPD--ASDGG 666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205 1805 PRGPPPARFGAQKPPIPslfSGQHGPPPygdnrglspsylgGPRGGAPAQfEDRKDPHGEKREFQDTPYNEMTGAPAqce 1884
Cdd:PRK07764  667 DGWPAKAGGAAPAAPPP---APAPAAPA-------------APAGAAPAQ-PAPAPAATPPAGQADDPAAQPPQAAQ--- 726
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568920205 1885 gpdqaqfmGNRAPFQFGGQRRPLLTQMKGPRGGPPPSQFGAQRGPPPGHFVGPRGPHPSQFE 1946
Cdd:PRK07764  727 --------GASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPS 780
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1726-2017 3.02e-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: 42.83  E-value: 3.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1726 SPVADMEDSREPQPRPGESTTSFPQPGQRG-----------GGPQPQFPGQREPAPRTFGMSGHHGPSFPGPRGPVPPYS 1794
Cdd:pfam03154  244 SPHPPLQPMTQPPPPSQVSPQPLPQPSLHGqmppmphslqtGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQ 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1795 EENLVPNSDGPRGPPPARfgaQKPPIPSLFSGQH-GPPPYGDNRGLS-------PSYLGGPrggAPAQFEDRKDPHGEKR 1866
Cdd:pfam03154  324 RIHTPPSQSQLQSQQPPR---EQPLPPAPLSMPHiKPPPTTPIPQLPnpqshkhPPHLSGP---SPFQMNSNLPPPPALK 397
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1867 EFQDTPYNEMTGApaqceGPDQAQFMGNRAPFQFGGQRRPLLTQMKGPrggPPPsqfgAQRGPPPG--HFVGPRGPHPsq 1944
Cdd:pfam03154  398 PLSSLSTHHPPSA-----HPPPLQLMPQSQQLPPPPAQPPVLTQSQSL---PPP----AASHPPTSglHQVPSQSPFP-- 463
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568920205  1945 fensrgTHPgqfeGARGQAPGFMPgPRGIQPQQFEEQRVNSPPRFAGQRASAPLPyGGPRGPAPFPEKNEQPP 2017
Cdd:pfam03154  464 ------QHP----FVPGGPPPITP-PSGPPTSTSSAMPGIQPPSSASVSSSGPVP-AAVSCPLPPVQIKEEAL 524
SWIRM-assoc_1 pfam16495
SWIRM-associated region 1; Much of the higher eukaryote SWI/SNF complex subunit SMARCC2 ...
1462-1499 3.11e-03

SWIRM-associated region 1; Much of the higher eukaryote SWI/SNF complex subunit SMARCC2 proteins is of low-complexity and or disordered. However, there are several short regions that are quite highly conserved. This is one of these regions. The function of the individual regions is not known.


Pssm-ID: 465142 [Multi-domain]  Cd Length: 84  Bit Score: 38.65  E-value: 3.11e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 568920205  1462 ASLVEQQ--------KMLEELNKQIEEQKRQLEEQEEALRQQRAAV 1499
Cdd:pfam16495   27 ALLVETQlkklelklKQFEELEKLLERERRQLERQRQQLFLERLAF 72
PHD2_CHD_II cd15532
PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...
267-316 4.10e-03

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


Pssm-ID: 277007 [Multi-domain]  Cd Length: 43  Bit Score: 36.87  E-value: 4.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568920205  267 YC-ICRQPHNnrfMICCDRCEEWFHGDCVGIseargRLLERNGEDYICPNC 316
Cdd:cd15532     1 FCrVCKDGGE---LLCCDGCPSSYHLHCLNP-----PLAEIPDGDWFCPRC 43
PHD2_MTF2_PHF19_like cd15503
PHD finger 2 found in polycomb repressive complex 2 (PRC2)-associated polycomb-like (PCL) ...
267-294 4.31e-03

PHD finger 2 found in polycomb repressive complex 2 (PRC2)-associated polycomb-like (PCL) family proteins MTF2, PHF19, and similar proteins; The PCL family includes PHD finger protein1 (PHF1) and its homologs metal-response element-binding transcription factor 2 (MTF2/PCL2) and PHF19/PCL3, which are accessory components of the Polycomb repressive complex 2 (PRC2) core complex and all contain an N-terminal Tudor domain followed by two plant homeodomain (PHD) fingers, and a C-terminal MTF2 domain. PCL proteins specifically recognize tri-methylated H3K36 (H3K36me3) through their N-terminal Tudor domains. The interaction between their Tudor domains and H3K36me3 is critical for both the targeting and spreading of PRC2 into active chromatin regions and for the maintenance of optimal repression of poised developmental genes where PCL proteins, H3K36me3, and H3K27me3 coexist. Moreover, unlike other PHD finger-containing proteins, the first PHD finger of PCL proteins do not display histone H3K4 binding affinity and they do not affect the Tudor domain binding to histones. This model corresponds to the second PHD finger.


Pssm-ID: 276978  Cd Length: 52  Bit Score: 37.38  E-value: 4.31e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 568920205  267 YCICRQPH--NNRFMICCdRCEEWFHGDCV 294
Cdd:cd15503     1 YCYCGGPGewNLKMLQCC-KCRQWFHEACL 29
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1718-2070 6.36e-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: 41.68  E-value: 6.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1718 AQSAGKNDSPVADMEDSREPQPRPGESTTSFPQPGQRGGGPQPQFPgQREPAPRTFGMSG--HHGPSFPGPRGPVPPYse 1795
Cdd:pfam03154  176 AQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQT-QSTAAPHTLIQQTptLHPQRLPSPHPPLQPM-- 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1796 enlvpnsdgPRGPPPARFGAQKPPIPSLfsgqHGP-PPYGDNRGLSPSYLGGPrgGAPAQFedrkdPHGEKREFQDTPYN 1874
Cdd:pfam03154  253 ---------TQPPPPSQVSPQPLPQPSL----HGQmPPMPHSLQTGPSHMQHP--VPPQPF-----PLTPQSSQSQVPPG 312
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1875 EMTGAPAQCEGPDQAQFMGNRAPFQFGGQRRPLL-TQMKGPRGGPPPSQFGAQRGPPPGHFVGPRGPHPSQFE-NSRGTH 1952
Cdd:pfam03154  313 PSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPpAPLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQmNSNLPP 392
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1953 PGQFEG----ARGQAPGFMPGPRGIQPQQfeeQRVNSPPrfagqrASAPLPYGGPRGPAPfpeKNEQPPSRFHFQGPSSQ 2028
Cdd:pfam03154  393 PPALKPlsslSTHHPPSAHPPPLQLMPQS---QQLPPPP------AQPPVLTQSQSLPPP---AASHPPTSGLHQVPSQS 460
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 568920205  2029 PVKPPPRPLLELPS-HPPQHRKDRWDEAGPATALPSSAGPGQG 2070
Cdd:pfam03154  461 PFPQHPFVPGGPPPiTPPSGPPTSTSSAMPGIQPPSSASVSSS 503
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
1847-1990 6.37e-03

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


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 41.95  E-value: 6.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920205  1847 PRGGAPAQFedrkdPHGEKREFQDTPYNemtgAPAQCEGPDQAQFMGNRAPFQFGG------QRRPLLTQMKGPRGGPPP 1920
Cdd:pfam09770  213 QPAPAPAQP-----PAAPPAQQAQQQQQ----FPPQIQQQQQPQQQPQQPQQHPGQghpvtiLQRPQSPQPDPAQPSIQP 283
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568920205  1921 SQFGAQRGPPPGHfvgprgPHPSQ-FENsrgthPGQFEGARGQAPGFMPGPRGIQPQQFEEQRVNSPPRFA 1990
Cdd:pfam09770  284 QAQQFHQQPPPVP------VQPTQiLQN-----PNRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQA 343
PHD_PYGO cd15551
PHD finger found in PYGO proteins; The family includes Drosophila melanogaster protein pygopus ...
268-316 8.93e-03

PHD finger found in PYGO proteins; The family includes Drosophila melanogaster protein pygopus (dPYGO) and its two homologs, PYGO1 and PYGO2. dPYGO is a fundamental Wnt signaling transcriptional component in Drosophila. PYGO1 is essential for the association with Legless (Lgs)/Bcl9 that acts an adaptor between Pygopus (Pygo) and Arm/beta-catenin. dPYGO and PYGO2 function as context-dependent beta-catenin coactivators, and they bind di- and trimethylated lysine 4 of histone H3 (H3K4me2/3). Moreover, PYGO2 acts as a histone methylation reader, and a chromatin remodeler in a testis-specific and Wnt-unrelated manner. It also mediates chromatin regulation and links Wnt signaling and Notch signaling to suppress the luminal/alveolar differentiation competence of mammary stem and basal cells. PYGO2 also plays a new role in rRNA transcription during cancer cell growth. It regulates mammary tumor initiation and heterogeneity in MMTV-Wnt1 mice. All family members contain a plant homeodomain (PHD) finger.


Pssm-ID: 277026  Cd Length: 54  Bit Score: 36.57  E-value: 8.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568920205  268 CICRQP--HNNRFMICCDRCEEWFHGDCVGISEARGRLL--ERNGEdYICPNC 316
Cdd:cd15551     3 GICNNEvnDDDDAILCESSCNKWFHRTCTGLTESAYDLLtsEESAE-WVCDSC 54
PHD_ING4_5 cd15586
PHD finger found in inhibitor of growth protein 4 (ING4) and 5 (ING5); ING4, also termed ...
267-316 9.40e-03

PHD finger found in inhibitor of growth protein 4 (ING4) and 5 (ING5); ING4, also termed p29ING4, and ING5, also termed p28ING5, belong to the inhibitor of growth (ING) family of type II tumor suppressors. ING4 acts as an E3 ubiquitin ligase to induce ubiquitination of the p65 subunit of NF-kappaB and inhibit the transactivation of NF-kappaB target genes. It also induces apoptosis through a p53 dependent pathway, including increasing p53 acetylation, inhibiting Mdm2-mediated degradation of p53 and enhancing the expression of p53 responsive genes both at the transcriptional and post-translational levels. Moreover, ING4 can inhibit the translation of proto-oncogene MYC by interacting with AUF1. It also regulates other transcription factors, such as hypoxia-inducible factor (HIF). ING5 is a Tip60 cofactor that acetylates p53 at K120 and subsequently activates the expression of p53-dependent apoptotic genes in response to DNA damage. Aberrant ING5 expression may contribute to pathogenesis, growth, and invasion of gastric carcinomas and colorectal cancer. ING5 can physically interact with p300 and p53 in vivo, and its overexpression induces apoptosis in colorectal cancer cells. It also associates with cyclin A1 (INCA1) and functions as a growth suppressor with suppressed expression in Acute Myeloid Leukemia (AML). Moreover, ING5 translocation from the nucleus to the cytoplasm might be a critical event for carcinogenesis and tumor progression in human head and neck squamous cell carcinoma. Both ING4 and ING5 contain an N-terminal ING histone-binding domain and a C-terminal plant homeodomain (PHD) finger. They associate with histone acetyltransferase (HAT) complexes containing MOZ (monocytic leukemia zinc finger protein)/MORF (MOZ-related factor) and HBO1, and further direct the MOZ/MORF and HBO1 complexes to chromatin.


Pssm-ID: 277061 [Multi-domain]  Cd Length: 45  Bit Score: 36.01  E-value: 9.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568920205  267 YCICRQPHNNRfMICCDRCE---EWFHGDCVGI-SEARGRllerngedYICPNC 316
Cdd:cd15586     1 YCLCHQVSYGE-MIGCDNPDcpiEWFHFACVGLtTKPKGK--------WFCPRC 45
 
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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