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Conserved domains on  [gi|2462552449|ref|XP_054170714|]
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retinoic acid-induced protein 1 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ePHD_RAI1 cd15700
Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant ...
 1686-1901 2.05e-52

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


:

Pssm-ID: 277170  Cd Length: 104  Bit Score: 179.30  E-value: 2.05e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1686 CCLCQNPANFKDLGDLCGPYYPEHclpkkkpklkekvrpegtceeaslplertlkgpecaaaatagkpprpdgpadpakq 1765
Cdd:cd15700      1 CCLCRNPANYKDLGDLCGPYYPEH-------------------------------------------------------- 24

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1766 gplrtsarglsrrlqscyccdgredggeeaapadkgrkhecskeapaepggeaqehWVHEACAVWTGGVYLVAGKLFGLQ 1845
Cdd:cd15700     25 --------------------------------------------------------WVHEACAVWTTGVYLVAGKLFGLQ 48

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462552449 1846 EAMKVAVDMMCSSCQEAGATIGCCHKGCLHTYHYPCASDAGCIFIEENFSLKCPKH 1901
Cdd:cd15700     49 EAVQKAADAKCSSCQGAGATVGCCHKGCTQSYHYICAVEAGCLFEEENFSLRCPKH 104
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 959-1324 1.32e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449  959 RAPGDSTTSDASLAQKPNKPAVPEAPIAKKEPvPRGKSLRSRRVHRGLPEAEDSPCRAPVlPKDLLLPESCTGPPQGQME 1038
Cdd:PHA03247  2576 RPSEPAVTSRARRPDAPPQSARPRAPVDDRGD-PRGPAPPSPLPPDTHAPDPPPPSPSPA-ANEPDPHPPPTVPPPERPR 2653

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1039 GAGAPGRGASEGLPRMCTRSLTALSEPRTPGPPGLTTTPAPPDKLggkqrAAFKSGKRVGKPSPKAASS----PSNPAAL 1114
Cdd:PHA03247  2654 DDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSL-----ADPPPPPPTPEPAPHALVSatplPPGPAAA 2728

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1115 PVASDSSPMGSKTKET-DSPSTPGKDQRsmilRSRTKTQeifhSKRRRPSEGRLPNCRATKKLLDNSHLPATFKVSSSPQ 1193
Cdd:PHA03247  2729 RQASPALPAAPAPPAVpAGPATPGGPAR----PARPPTT----AGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPS 2800

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1194 KEGRVSQRARVPKPGAGSKLSDRPLHALKRKSAFMAPVPTKKRNLVlrSRSSSSSNASGNGGDGKEERPEGSPTL----- 1268
Cdd:PHA03247  2801 PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPP--PPSLPLGGSVAPGGDVRRRPPSRSPAAkpaap 2878

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1269 ----FKRMSSPKKAKPTKGNGEPATKLPPPETPDACLKLASRAAFQGAMKTKVLPPRKGR 1324
Cdd:PHA03247  2879 arppVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR 2938
 
Name Accession Description Interval E-value
ePHD_RAI1 cd15700
Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant ...
 1686-1901 2.05e-52

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


Pssm-ID: 277170  Cd Length: 104  Bit Score: 179.30  E-value: 2.05e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1686 CCLCQNPANFKDLGDLCGPYYPEHclpkkkpklkekvrpegtceeaslplertlkgpecaaaatagkpprpdgpadpakq 1765
Cdd:cd15700      1 CCLCRNPANYKDLGDLCGPYYPEH-------------------------------------------------------- 24

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1766 gplrtsarglsrrlqscyccdgredggeeaapadkgrkhecskeapaepggeaqehWVHEACAVWTGGVYLVAGKLFGLQ 1845
Cdd:cd15700     25 --------------------------------------------------------WVHEACAVWTTGVYLVAGKLFGLQ 48

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462552449 1846 EAMKVAVDMMCSSCQEAGATIGCCHKGCLHTYHYPCASDAGCIFIEENFSLKCPKH 1901
Cdd:cd15700     49 EAVQKAADAKCSSCQGAGATVGCCHKGCTQSYHYICAVEAGCLFEEENFSLRCPKH 104
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
 1824-1901 2.56e-13

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


Pssm-ID: 463977 [Multi-domain]  Cd Length: 88  Bit Score: 67.35  E-value: 2.56e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1824 HEACAVWTGGVYLVAGK-----LFGLQEAMKVAVDMMCSSC-QEAGATIGCCHKGCLHTYHYPCASDAGCIFIEEN---- 1893
Cdd:pfam13771    1 HVVCALWSPELVQRGNDsmgfpIEDIEKIPKRRWKLKCYLCkKKGGACIQCSKKNCRRAFHVTCALEAGLLMQFDEdngt 80


                   ....*...
gi 2462552449 1894 FSLKCPKH 1901
Cdd:pfam13771   81 FKSYCKKH 88
PHA03247 PHA03247
large tegument protein UL36; Provisional
 959-1324 1.32e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449  959 RAPGDSTTSDASLAQKPNKPAVPEAPIAKKEPvPRGKSLRSRRVHRGLPEAEDSPCRAPVlPKDLLLPESCTGPPQGQME 1038
Cdd:PHA03247  2576 RPSEPAVTSRARRPDAPPQSARPRAPVDDRGD-PRGPAPPSPLPPDTHAPDPPPPSPSPA-ANEPDPHPPPTVPPPERPR 2653

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1039 GAGAPGRGASEGLPRMCTRSLTALSEPRTPGPPGLTTTPAPPDKLggkqrAAFKSGKRVGKPSPKAASS----PSNPAAL 1114
Cdd:PHA03247  2654 DDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSL-----ADPPPPPPTPEPAPHALVSatplPPGPAAA 2728

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1115 PVASDSSPMGSKTKET-DSPSTPGKDQRsmilRSRTKTQeifhSKRRRPSEGRLPNCRATKKLLDNSHLPATFKVSSSPQ 1193
Cdd:PHA03247  2729 RQASPALPAAPAPPAVpAGPATPGGPAR----PARPPTT----AGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPS 2800

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1194 KEGRVSQRARVPKPGAGSKLSDRPLHALKRKSAFMAPVPTKKRNLVlrSRSSSSSNASGNGGDGKEERPEGSPTL----- 1268
Cdd:PHA03247  2801 PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPP--PPSLPLGGSVAPGGDVRRRPPSRSPAAkpaap 2878

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1269 ----FKRMSSPKKAKPTKGNGEPATKLPPPETPDACLKLASRAAFQGAMKTKVLPPRKGR 1324
Cdd:PHA03247  2879 arppVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR 2938
 
Name Accession Description Interval E-value
ePHD_RAI1 cd15700
Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant ...
 1686-1901 2.05e-52

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


Pssm-ID: 277170  Cd Length: 104  Bit Score: 179.30  E-value: 2.05e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1686 CCLCQNPANFKDLGDLCGPYYPEHclpkkkpklkekvrpegtceeaslplertlkgpecaaaatagkpprpdgpadpakq 1765
Cdd:cd15700      1 CCLCRNPANYKDLGDLCGPYYPEH-------------------------------------------------------- 24

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1766 gplrtsarglsrrlqscyccdgredggeeaapadkgrkhecskeapaepggeaqehWVHEACAVWTGGVYLVAGKLFGLQ 1845
Cdd:cd15700     25 --------------------------------------------------------WVHEACAVWTTGVYLVAGKLFGLQ 48

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462552449 1846 EAMKVAVDMMCSSCQEAGATIGCCHKGCLHTYHYPCASDAGCIFIEENFSLKCPKH 1901
Cdd:cd15700     49 EAVQKAADAKCSSCQGAGATVGCCHKGCTQSYHYICAVEAGCLFEEENFSLRCPKH 104
ePHD_RAI1_like cd15668
Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 ...
 1820-1901 2.31e-49

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


Pssm-ID: 277138  Cd Length: 103  Bit Score: 170.57  E-value: 2.31e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1820 EHWVHEACAVWTGGVYLVAGKLFGLQEAMKVAVDMMCSSCQEAGATIGCCHKGCLHTYHYPCASDAGCIFIEENFSLKCP 1899
Cdd:cd15668     22 EVWVHEDCAVWAPGVYLVGGKLYGLEEAVWVAKQSVCSSCQQTGATIGCLHKGCKAKYHYPCAVESGCQLDEENFSLLCP 101


                   ..
gi 2462552449 1900 KH 1901
Cdd:cd15668    102 KH 103
ePHD_TCF20 cd15699
Extended PHD finger (ePHD) found in transcription factor 20 (TCF-20); The extended plant ...
 1816-1901 2.17e-38

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


Pssm-ID: 277169  Cd Length: 103  Bit Score: 139.28  E-value: 2.17e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1816 GEAQEHWVHEACAVWTGGVYLVAGKLFGLQEAMKVAVDMMCSSCQEAGATIGCCHKGCLHTYHYPCASDAGCIFIEENFS 1895
Cdd:cd15699     18 GPFYEFWVHEGCILWANGIYLVCGRLYGLQEALDIAREMKCSHCQEAGATLGCYNKGCSFRYHYPCAIDADCLLNEENFS 97


                   ....*.
gi 2462552449 1896 LKCPKH 1901
Cdd:cd15699     98 VRCPKH 103
ePHD_KMT2A_like cd15664
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The ...
 1806-1901 7.31e-22

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


Pssm-ID: 277134  Cd Length: 105  Bit Score: 92.08  E-value: 7.31e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1806 CSKEAPAEPGGEA------QEHWVHEACAVWTGGVYL-VAGKLFGLQEAMKVAVDMMCSSCQEAGATIGCCHKGCLHTYH 1878
Cdd:cd15664      4 CGVYGDDEPNDAGrllycgQDEWVHINCALWSAEVFEeDDGSLQNVHSAVSRGRMMKCELCGKPGATVGCCLKSCPANYH 83

                           90       100
                   ....*....|....*....|...
gi 2462552449 1879 YPCASDAGCIFIEENfSLKCPKH 1901
Cdd:cd15664     84 FMCARKAECVFQDDK-KVFCPAH 105
ePHD cd15571
Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is ...
 1806-1901 1.08e-19

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


Pssm-ID: 277046 [Multi-domain]  Cd Length: 112  Bit Score: 86.10  E-value: 1.08e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1806 CSKEAPAEPGGEAQEH-----WVHEACAVWTGGVYLVAG---KLFGLQEAMKVAVDMMCSSCQEA-GATIGCCHKGCLHT 1876
Cdd:cd15571      4 CPRSGGALKGGGALKTtsdglWVHVVCALWSPEVYFDDGtllEVEGVSKIPKRRKKLKCSICGKRgGACIQCSYPGCPRS 83

                           90       100
                   ....*....|....*....|....*....
gi 2462552449 1877 YHYPCASDAGCIFIE----ENFSLKCPKH 1901
Cdd:cd15571     84 FHVSCAIRAGCLFEFedgpGNFVVYCPKH 112
ePHD2_KMT2C_like cd15666
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
 1822-1901 2.37e-17

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


Pssm-ID: 277136  Cd Length: 105  Bit Score: 79.27  E-value: 2.37e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1822 WVHEACAVWTGGVY-LVAGKLFGLQEAMKVAVDMMCSSCQEAGATIGCcHKG-CLHTYHYPCASDAGCIFIeENFSLKCP 1899
Cdd:cd15666     26 WVHLNCALWSYEVYeTQNGALMNVEEALRRALTTTCSHCGRTGATVPC-FKPrCANVYHLPCAIKDGCMFF-KDKTMLCP 103


                   ..
gi 2462552449 1900 KH 1901
Cdd:cd15666    104 SH 105
ePHD1_KMT2C_like cd15665
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
 1820-1901 6.62e-16

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


Pssm-ID: 277135  Cd Length: 90  Bit Score: 74.66  E-value: 6.62e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1820 EHWVHEACAVWTGGVY-LVAGKLFGLQEAMKVAVDMMCSSCQEAGATIGCCHKGCLHTYHYPCASDAGCIFIEENFSLKC 1898
Cdd:cd15665      8 EVYAHHCCAAWSEGVCqTEDGALENVDKAVAKALSQKCSFCLRYGASISCRMPSCSKSFHFPCAAAAGCFQDIKTLTLFC 87


                   ...
gi 2462552449 1899 PKH 1901
Cdd:cd15665     88 PEH 90
ePHD_KMT2A cd15693
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant ...
 1819-1904 7.57e-15

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


Pssm-ID: 277163  Cd Length: 113  Bit Score: 72.34  E-value: 7.57e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1819 QEHWVHEACAVWTGGVYL-VAGKLFGLQEAMKVAVDMMCSSCQEAGATIGCCHKGCLHTYHYPCASDAGCIFIEENfSLK 1897
Cdd:cd15693     25 QNEWTHVNCALWSAEVFEdDDGSLKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSCTSNYHFMCSRAKNCVFLEDK-KVY 103


                   ....*..
gi 2462552449 1898 CPKHKRL 1904
Cdd:cd15693    104 CQRHKDL 110
ePHD1_KMT2D cd15695
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...
 1820-1901 1.14e-14

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


Pssm-ID: 277165  Cd Length: 90  Bit Score: 71.10  E-value: 1.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1820 EHWVHEACAVWTGGVYLVAG-KLFGLQEAMKVAVDMMCSSCQEAGATIGCCHKGCLHTYHYPCASDAGCIFIEENFSLKC 1898
Cdd:cd15695      8 ECWVHHWCAAWSAGVKQHEGdGLIGVDKAVFSGISQKCEHCKRLGATIQCHAEGCPRFYHFPCAAASGSFQSMKTLLLLC 87


                   ...
gi 2462552449 1899 PKH 1901
Cdd:cd15695     88 PEH 90
ePHD_KMT2B cd15694
Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B); The extended plant ...
 1809-1901 4.08e-14

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


Pssm-ID: 277164  Cd Length: 105  Bit Score: 70.07  E-value: 4.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1809 EAPAEPGGE----AQEHWVHEACAVWTGGVYLVA-GKLFGLQEAMKVAVDMMCSSCQEAGATIGCCHKGCLHTYHYPCAS 1883
Cdd:cd15694      9 DADSKDAGRllyiGQNEWTHVNCAIWSAEVFEENdGSLKNVHAAVARGRQMRCEHCQKIGATVGCCLSACLSNFHFMCAR 88

                           90
                   ....*....|....*...
gi 2462552449 1884 DAGCIFiEENFSLKCPKH 1901
Cdd:cd15694     89 ASRCCF-QDDKKVFCQKH 105
ePHD2_KMT2C cd15697
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
 1822-1901 1.87e-13

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


Pssm-ID: 277167  Cd Length: 105  Bit Score: 68.15  E-value: 1.87e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1822 WVHEACAVWTGGVYLV-AGKLFGLQEAMKVAVDMMCSSCQEAGATIGCCHKGCLHTYHYPCASDAGCIFIEENfSLKCPK 1900
Cdd:cd15697     26 WVHLNCALWSTEVYETqAGALINVELALRRGLQMKCVFCHKTGATSGCHRLRCTNVYHFTCAIKAQCMFFKDK-TMLCPM 104


                   .
gi 2462552449 1901 H 1901
Cdd:cd15697    105 H 105
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
 1824-1901 2.56e-13

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


Pssm-ID: 463977 [Multi-domain]  Cd Length: 88  Bit Score: 67.35  E-value: 2.56e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1824 HEACAVWTGGVYLVAGK-----LFGLQEAMKVAVDMMCSSC-QEAGATIGCCHKGCLHTYHYPCASDAGCIFIEEN---- 1893
Cdd:pfam13771    1 HVVCALWSPELVQRGNDsmgfpIEDIEKIPKRRWKLKCYLCkKKGGACIQCSKKNCRRAFHVTCALEAGLLMQFDEdngt 80


                   ....*...
gi 2462552449 1894 FSLKCPKH 1901
Cdd:pfam13771   81 FKSYCKKH 88
ePHD1_KMT2C cd15696
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
 1820-1901 8.73e-13

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


Pssm-ID: 277166  Cd Length: 90  Bit Score: 65.74  E-value: 8.73e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1820 EHWVHEACAVWTGGVYLVAGK-LFGLQEAMKVAVDMMCSSCQEAGATIGCCHKGCLHTYHYPCASDAGCIFIEENFSLKC 1898
Cdd:cd15696      8 ECWAHLRCAEWSLGVCQGEEQlLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQDFSRRLLLC 87


                   ...
gi 2462552449 1899 PKH 1901
Cdd:cd15696     88 PTH 90
ePHD2_KMT2D cd15698
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...
 1822-1902 9.51e-13

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


Pssm-ID: 277168  Cd Length: 107  Bit Score: 66.23  E-value: 9.51e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1822 WVHEACAVWTGGVYLV-AGKLFGLQEAMKVAVDMMCSSCQEAGATIGCCHKGCLHTYHYPCASDAGCIFIEENfSLKCPK 1900
Cdd:cd15698     26 WVHLNCALWSTEVYETqGGALMNVEVALHRGLLTKCSLCQKTGATNSCNRLRCPNVYHFACAIRAKCMFFKDK-TMLCPM 104


                   ..
gi 2462552449 1901 HK 1902
Cdd:cd15698    105 HK 106
ePHD_PHF7_G2E3_like cd15669
Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ...
 1855-1901 2.60e-12

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


Pssm-ID: 277139 [Multi-domain]  Cd Length: 112  Bit Score: 64.96  E-value: 2.60e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2462552449 1855 MCSSCQEAGATIGCCHKGCLHTYHYPCASDAGCI--FIEENFSLkCPKH 1901
Cdd:cd15669     65 RCFYCKKKGASIGCAVKGCRRSFHFPCGLENGCVtqFFGEYRSF-CWEH 112
ePHD_PHF6_like cd15673
Extended PHD finger found in PHD finger protein 6 (PHF6) and PHD finger protein 11 (PHF11); ...
 1854-1901 7.56e-08

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


Pssm-ID: 277143  Cd Length: 116  Bit Score: 52.39  E-value: 7.56e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462552449 1854 MMCSSCQEAGATIGCCHKGCLHTYHYPCA-SDAGCI---FIEENFSLKCPKH 1901
Cdd:cd15673     65 LKCNLCKKTGATIGCDVKQCKKTYHYHCAkKDDAKIierNSQGIYRVYCKNH 116
ePHD1_PHF6 cd15710
Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
 1844-1882 1.54e-06

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


Pssm-ID: 277180  Cd Length: 115  Bit Score: 48.80  E-value: 1.54e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462552449 1844 LQEAMKVAVDMMCSSCQEAGATIGCCHKGCLHTYHYPCA 1882
Cdd:cd15710     54 VQKEIKRGTKLMCSLCHCPGATIGCDVKTCHRTYHYYCA 92
zf-HC5HC2H_2 pfam13832
PHD-zinc-finger like domain;
1822-1901 2.80e-06

PHD-zinc-finger like domain;


Pssm-ID: 463991 [Multi-domain]  Cd Length: 109  Bit Score: 47.72  E-value: 2.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1822 WVHEACAVWTGGVYLVAGK---LFGLQEAMKVAVDMMCSSCQE-AGATIGCCHKGCLHTYHYPCASDAGCIF-IEENFSL 1896
Cdd:pfam13832   21 WVHVLCAIFVPEVRFGNVAtmePIDVSRIPPERWKLKCVFCKKrSGACIQCSKGRCTTAFHVTCAQAAGVYMePEDWPNV 100


                   ....*....
gi 2462552449 1897 K----CPKH 1901
Cdd:pfam13832  101 VviayCQKH 109
ePHD2_PHF6 cd15711
Extended PHD finger 2 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
 1844-1901 5.20e-06

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


Pssm-ID: 277181  Cd Length: 118  Bit Score: 47.39  E-value: 5.20e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462552449 1844 LQEaMKVAVDMMCSSCQEAGATIGCCHKGCLHTYHYPCASDAGCIFIEEN----FSLKCPKH 1901
Cdd:cd15711     58 IQE-IKRGKRMKCTLCSQLGATIGCEIKACVKTYHYHCGVQDKAKYIENMsrgiYKLYCKNH 118
ePHD_JADE cd15671
Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended ...
 1821-1901 5.31e-05

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


Pssm-ID: 277141  Cd Length: 112  Bit Score: 44.36  E-value: 5.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1821 HWVHEACAVWTGGVYlvagklFGLQEAMKVAV----------DMMCSSCQE-AGATIGCCHKGCLHTYHYPCASDAG--- 1886
Cdd:cd15671     19 KWVHVSCALWIPEVS------IGCPEKMEPITkishipmsrwALVCVLCKEkTGACIQCSVKSCKTAFHVTCAFQHGlem 92

                           90       100
                   ....*....|....*....|
gi 2462552449 1887 -CIFIEENFSLK----CPKH 1901
Cdd:cd15671     93 kTILEDEDDEVKfksyCPKH 112
ePHD_ATX1_2_like cd15662
Extended PHD finger found in Arabidopsis thaliana ATX1, -2, and similar proteins; The extended ...
 1822-1886 1.21e-04

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


Pssm-ID: 277132  Cd Length: 115  Bit Score: 43.23  E-value: 1.21e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1822 WVHEACAVWTGGVYLV----AGKLFGLQEAMKVAVDMMCSSC-QEAGATIGCCHKGCLHTYHYPCASDAG 1886
Cdd:cd15662     19 WAHLACAIWIPETCLLdvktMEPVDGINAISKERWELSCTICkQRYGACIQCSNNSCRVAYHPLCARAAG 88
PHA03247 PHA03247
large tegument protein UL36; Provisional
 959-1324 1.32e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449  959 RAPGDSTTSDASLAQKPNKPAVPEAPIAKKEPvPRGKSLRSRRVHRGLPEAEDSPCRAPVlPKDLLLPESCTGPPQGQME 1038
Cdd:PHA03247  2576 RPSEPAVTSRARRPDAPPQSARPRAPVDDRGD-PRGPAPPSPLPPDTHAPDPPPPSPSPA-ANEPDPHPPPTVPPPERPR 2653

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1039 GAGAPGRGASEGLPRMCTRSLTALSEPRTPGPPGLTTTPAPPDKLggkqrAAFKSGKRVGKPSPKAASS----PSNPAAL 1114
Cdd:PHA03247  2654 DDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSL-----ADPPPPPPTPEPAPHALVSatplPPGPAAA 2728

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1115 PVASDSSPMGSKTKET-DSPSTPGKDQRsmilRSRTKTQeifhSKRRRPSEGRLPNCRATKKLLDNSHLPATFKVSSSPQ 1193
Cdd:PHA03247  2729 RQASPALPAAPAPPAVpAGPATPGGPAR----PARPPTT----AGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPS 2800

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1194 KEGRVSQRARVPKPGAGSKLSDRPLHALKRKSAFMAPVPTKKRNLVlrSRSSSSSNASGNGGDGKEERPEGSPTL----- 1268
Cdd:PHA03247  2801 PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPP--PPSLPLGGSVAPGGDVRRRPPSRSPAAkpaap 2878

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1269 ----FKRMSSPKKAKPTKGNGEPATKLPPPETPDACLKLASRAAFQGAMKTKVLPPRKGR 1324
Cdd:PHA03247  2879 arppVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR 2938
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 859-1279 1.44e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 46.99  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449  859 SRKEDLEAEEEYSslcELLGSPEQRPGmQDPLSPKAPLICTKEEVE-----EVLDSKAGWGSPCHLSGESVILLGPT--- 930
Cdd:PTZ00449   492 SKKKLAPIEEEDS---DKHDEPPEGPE-ASGLPPKAPGDKEGEEGEhedskESDEPKEGGKPGETKEGEVGKKPGPAkeh 567

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449  931 ----VGTESKVQSWFESSLSHMKPGE-EGPDGERAPGDSTTSDA----SLAQKPNKPAVPEAPIAKKEPVPRGKSLRSRR 1001
Cdd:PTZ00449   568 kpskIPTLSKKPEFPKDPKHPKDPEEpKKPKRPRSAQRPTRPKSpklpELLDIPKSPKRPESPKSPKRPPPPQRPSSPER 647

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1002 vhrglPEAEDSP--CRAPVLPKDLLLPESCTGPPQGQMEGAGAPGRGASEGLPRMCTRSLTALSEPRTPGPPGLTTTPAP 1079
Cdd:PTZ00449   648 -----PEGPKIIksPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTPRPLP 722

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1080 PdKLGGKQRAAFKSGKRVGKPSPKAASSPSNPAALPVASDSSPMGSK--------------TKETDSPSTPGKDQRSMIL 1145
Cdd:PTZ00449   723 P-KLPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTFFHETPADTPlpdilaeefkeediHAETGEPDEAMKRPDSPSE 801

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1146 RSRTKTQEI--FHSKRRRPSEGRLPNC----RATKKLLDNSHLPATFKVSSS-------PQKEGRVSQRARVPKPGAGSK 1212
Cdd:PTZ00449   802 HEDKPPGDHpsLPKKRHRLDGLALSTTdlesDAGRIAKDASGKIVKLKRSKSfddlttvEEAEEMGAEARKIVVDDDGTE 881

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462552449 1213 LSDRPLHalkrksafmapvPTKKRNLvlrsrsssssnasgngGDGKEERPEGSPTLFKRMSSPKKAK 1279
Cdd:PTZ00449   882 ADDEDTH------------PPEEKHK----------------SEVRRRRPPKKPSKPKKPSKPKKPK 920
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 948-1232 1.58e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.09  E-value: 1.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449  948 MKPGEEGPDGERAPGDSTTSDASLAQKPNKPAVPEAPIAKKEPVPRGKSLRSRRVH-RGLPEAEDSPCRAPVLPKDlllp 1026
Cdd:PHA03307   152 PPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPrRSSPISASASSPAPAPGRS---- 227

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1027 eSCTGPPQGQMEGAGAPGRGASEGLPRMCTRSLTALSepRTPGPPGLTTTPAPPDKLGGKQRAAFKSGKRVGKPSPKAAS 1106
Cdd:PHA03307   228 -AADDAGASSSDSSSSESSGCGWGPENECPLPRPAPI--TLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPG 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1107 SPSNPAALPVASDSSPMGSKTKETDSPSTPGKDQRSMilrSRTKTqeifHSKRRRPSEGRLPNCRATKKLLDNSHLPATF 1186
Cdd:PHA03307   305 SGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAV---SPGPS----PSRSPSPSRPPPPADPSSPRKRPRPSRAPSS 377

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462552449 1187 KVSSSPQKEGRVSQRARV--------PKPGAGSKLSDRPLHALKRKSAFMAPVP 1232
Cdd:PHA03307   378 PAASAGRPTRRRARAAVAgrarrrdaTGRFPAGRPRPSPLDAGAASGAFYARYP 431
ePHD_PHF11 cd15712
Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain ...
 1854-1901 2.32e-04

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


Pssm-ID: 277182 [Multi-domain]  Cd Length: 115  Bit Score: 42.58  E-value: 2.32e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462552449 1854 MMCSSCQEAGATIGCCHKGCLHTYHYPCA-SDAGCIFIEEN---FSLKCPKH 1901
Cdd:cd15712     64 LKCNFCRKKGATVGCEERACRRSYHYFCAlCDDAAIETDEVrgiYRVFCQKH 115
PHA03247 PHA03247
large tegument protein UL36; Provisional
 955-1361 4.60e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 4.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449  955 PDGERAPGDSttSDASLAQKPNKPAVPEAPiaKKEPVPRGKSLRSRRVHRGLPEAEDSPCRAPVLPKDLLLPESCTGPPQ 1034
Cdd:PHA03247  2595 SARPRAPVDD--RGDPRGPAPPSPLPPDTH--APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRL 2670

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1035 GQMEGAGAPGRGASEGLPRMCTRSLTALSEPRTPGP-------PGLTTTPAPPDKLGGKQRAAFKSGKRVGKPSPKAASS 1107
Cdd:PHA03247  2671 GRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPtpepaphALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAT 2750

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1108 PSNPAALPVASDSSPMGSKTKETDSPSTPGKDQRSMILRSRTKTQEIFHSKRRrPSEGRLPNCRATKKLLDNSHLPATFK 1187
Cdd:PHA03247  2751 PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWD-PADPPAAVLAPAAALPPAASPAGPLP 2829

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1188 VSSSPQKEGRVSQRARVPKPGA-------GSKLSDRPLhalKRKSAFMAPVPTKKRNLVLRSRSSSSSNASGNGGDGKEE 1260
Cdd:PHA03247  2830 PPTSAQPTAPPPPPGPPPPSLPlggsvapGGDVRRRPP---SRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPE 2906

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1261 RPEGSPTlfkrMSSPKKAKPTKGNGEPATKLPPPETPDACLKLASRAAFQGAMKTKVLPPRKGRGLKLEAIVQKITSPSL 1340
Cdd:PHA03247  2907 RPPQPQA----PPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQP 2982

                          410       420
                   ....*....|....*....|.
gi 2462552449 1341 KKfACKAPGASPGNPLSPSLS 1361
Cdd:PHA03247  2983 AP-SREAPASSTPPLTGHSLS 3002
ePHD_JADE1 cd15704
Extended PHD finger found in protein Jade-1 and similar proteins; The extended plant ...
 1806-1901 7.58e-04

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


Pssm-ID: 277174  Cd Length: 118  Bit Score: 41.21  E-value: 7.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1806 CSKEAPAEPGGEAQEHWVHEACAVWTGGVYLvaGKLFGLQEAMKVA------VDMMCSSCQEA-GATIGCCHKGCLHTYH 1878
Cdd:cd15704      7 CPKKGGAMKPTRSGTKWVHVSCALWIPEVSI--GSPEKMEPITKVShipssrWALVCSLCNEKvGASIQCSVKNCRTAFH 84

                           90       100       110
                   ....*....|....*....|....*....|
gi 2462552449 1879 YPCASDAG----CIFIEEN---FSLKCPKH 1901
Cdd:cd15704     85 VTCAFDRGlemkTILAENDevkFKSYCPKH 114
ePHD_RNO cd15707
Extended PHD finger found in Drosophila melanogaster PHD finger protein rhinoceros (RNO) and ...
 1806-1901 5.86e-03

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


Pssm-ID: 277177 [Multi-domain]  Cd Length: 113  Bit Score: 38.34  E-value: 5.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1806 CSKEAPAEPGGEAQEHWVHEACAVWTGGVYLvaGKLFGLQEAMKVAV------DMMCSSCQE-AGATIGCCHKGCLHTYH 1878
Cdd:cd15707      4 CPNKGGAMKSTRSGTKWAHVSCALWIPEVSI--GCVEKMEPITKISSipasrwALICVLCRErTGACIQCSVKTCKTAYH 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2462552449 1879 YPCASDAGC---IFIEEN------FSLKCPKH 1901
Cdd:cd15707     82 VTCGFQHGLemkTILDEEsedgvkLRSYCQKH 113
PHA03247 PHA03247
large tegument protein UL36; Provisional
 941-1136 7.23e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 7.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449  941 FESSLSHMKPGEEGPDGERAPGDSTTSDASLAQKPNKPAVPEAPiakkepvPRGKSLRSRRVHRGLPEAEDSPCRAPVLP 1020
Cdd:PHA03247  2636 NEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSP-------PQRPRRRAARPTVGSLTSLADPPPPPPTP 2708

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1021 KDLLLPESCTGP-PQGQMEGAGAPGRGASEGLPRMCTRSLTALSEPRTPGPPGLTTTP----APPDKLGGKQRAAFKSGK 1095
Cdd:PHA03247  2709 EPAPHALVSATPlPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPpapaPPAAPAAGPPRRLTRPAV 2788

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2462552449 1096 RVGKPSPKAASSPSNPAALPVAsdSSPMGSKTKETDSPSTP 1136
Cdd:PHA03247  2789 ASLSESRESLPSPWDPADPPAA--VLAPAAALPPAASPAGP 2827
PHA03247 PHA03247
large tegument protein UL36; Provisional
 949-1135 8.13e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 8.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449  949 KPGEEGPDGERAPGDST----TSDASLAQKPNKPAVPEAPIAKKEP----VPRGKSLRSRRVHRGLPEAEDSPcRAPVLP 1020
Cdd:PHA03247  2700 DPPPPPPTPEPAPHALVsatpLPPGPAAARQASPALPAAPAPPAVPagpaTPGGPARPARPPTTAGPPAPAPP-AAPAAG 2778

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552449 1021 KDLLLPESCTGPPQGQMEGAGAPGRGASEGLPRMC-TRSLTALSEPRTPGPPGLTTTPAPPDKLGGKQRAAFKSGKRVGK 1099
Cdd:PHA03247  2779 PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLApAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAP 2858

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2462552449 1100 PSPKAASSPS-NPAALPVASDSSPMGSKTKETDSPST 1135
Cdd:PHA03247  2859 GGDVRRRPPSrSPAAKPAAPARPPVRRLARPAVSRST 2895
 
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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