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Conserved domains on  [gi|802793223|ref|XP_012092288|]
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protein HUA2-LIKE 2 isoform X2 [Jatropha curcas]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 1447-1599 1.56e-83

Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.


:

Pssm-ID: 238207 [Multi-domain]  Cd Length: 152  Bit Score: 270.16  E-value: 1.56e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223 1447 SIHEFTVKDARGQEVDLSVYKGKVLLVVNVASKCGFTdSNYTQLTELYKKYKDQGLEILAFPCNQFLKQEPGSSENAQEF 1526
Cdd:cd00340     1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 802793223 1527 ACTRYKAEYPIFQKVRVNGPNTAPVYKFLKASKFGFMGSSIKWNFTKFLINREGQVINRYGPTTNPLSFEDHI 1599
Cdd:cd00340    80 CETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
PWWP_HULK cd20147
PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family; The HULK family ...
 25-113 6.63e-41

PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family; The HULK family includes HUA2-like proteins 1-3 (HULK1-3), which are probable transcription factors that act with partial redundancy with each other. They may play diverse and essential roles in the control of plant development, physiology and flowering time. The PWWP domain specifically recognizes DNA and histone methylated lysines.


:

Pssm-ID: 438975 [Multi-domain]  Cd Length: 92  Bit Score: 145.71  E-value: 6.63e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223   25 GDLVLAKVKGFPAWPATVSEPEKWGYSADWKKVLVYFFGTQQIAFCNPADVEAFTEEKKQSLLVK--RQGKGADFVRAVQ 102
Cdd:cd20147     1 GDLVLAKVKGFPAWPAQVSEPEDWGSAPDPKKVFVHFFGTQQIGFCNPGELSEFTEEIKQSLLARtlKKKKGSDFSRAVK 80

                          90
                  ....*....|.
gi 802793223  103 EIIDSYEKSKK 113
Cdd:cd20147    81 EICELYEERKG 91
RPR smart00582
domain present in proteins, which are involved in regulation of nuclear pre-mRNA;
899-1030 3.98e-30

domain present in proteins, which are involved in regulation of nuclear pre-mRNA;


:

Pssm-ID: 214731  Cd Length: 124  Bit Score: 116.22  E-value: 3.98e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223    899 SFEGTLGSLTRTKESIGRATRIAIDCAKFGIsnKVVEILARHLESESSlHRRVDLFFLVDSITQCSRGLKG-DVGGIYPS 977
Cdd:smart00582    1 AFEQKLESLNNSQESIQTLTKWAIEHASHAK--EIVELWEKYIKKAPV-PRKLPLLYLLDSIVQNSKRKYGsEFGDELGP 77

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 802793223    978 AIQAVLPRLLsaaappGSFAQENRRQCLKVLRLWLERRILPESVIRHHMRELD 1030
Cdd:smart00582   78 VFQDALRRVL------GAAPEELKKKIRRLLNIWEERGIFPPEVLRPLREKLN 124
DUF3824 pfam12868
Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It ...
 1323-1422 1.37e-05

Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It is proline-rich, and the function is not known.


:

Pssm-ID: 372351 [Multi-domain]  Cd Length: 145  Bit Score: 46.66  E-value: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223  1323 RRENPPPYEHRYHPSHNGDGGNFYYnhERMRPAPYEPS-------------ESWRYPAPPFSGPR-----YPDKGRTPYS 1384
Cdd:pfam12868   29 RRERKKAERERERRRYEDDYRDYYE--DPYSPSPYPPSpagpyasqgqyypETNYFPPPPGSTPQppvdpQPNAPPPPYN 106

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 802793223  1385 PGPYGGPPreQTRIPHQGWSFPPREMHHrnfmPFRPPP 1422
Cdd:pfam12868  107 PADYPPPP--GAAPPPQPYQYPPPPGPD----PYAPRP 138
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 1447-1599 1.56e-83

Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.


Pssm-ID: 238207 [Multi-domain]  Cd Length: 152  Bit Score: 270.16  E-value: 1.56e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223 1447 SIHEFTVKDARGQEVDLSVYKGKVLLVVNVASKCGFTdSNYTQLTELYKKYKDQGLEILAFPCNQFLKQEPGSSENAQEF 1526
Cdd:cd00340     1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 802793223 1527 ACTRYKAEYPIFQKVRVNGPNTAPVYKFLKASKFGFMGSSIKWNFTKFLINREGQVINRYGPTTNPLSFEDHI 1599
Cdd:cd00340    80 CETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
PLN02412 PLN02412
probable glutathione peroxidase
 1446-1603 1.80e-79

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 259.15  E-value: 1.80e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223 1446 KSIHEFTVKDARGQEVDLSVYKGKVLLVVNVASKCGFTDSNYTQLTELYKKYKDQGLEILAFPCNQFLKQEPGSSENAQE 1525
Cdd:PLN02412    7 KSIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQ 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 802793223 1526 FACTRYKAEYPIFQKVRVNGPNTAPVYKFLKASKFGFMGSSIKWNFTKFLINREGQVINRYGPTTNPLSFEDHIKKAL 1603
Cdd:PLN02412   87 TVCTRFKAEFPIFDKVDVNGKNTAPLYKYLKAEKGGLFGDAIKWNFTKFLVSKEGKVVQRYAPTTSPLKIEKDIQNLL 164
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 1447-1603 2.05e-77

Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 253.08  E-value: 2.05e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223 1447 SIHEFTVKDARGQEVDLSVYKGKVLLVVNVASKCGFTdSNYTQLTELYKKYKDQGLEILAFPCNQFLKQEPGSSENAQEF 1526
Cdd:COG0386     3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223 1527 ACTRYKAEYPIFQKVRVNGPNTAPVYKFLK-ASKFGFMGSSIKWNFTKFLINREGQVINRYGPTTNPLS--FEDHIKKAL 1603
Cdd:COG0386    82 CSLNYGVTFPMFAKIDVNGPNAHPLYKYLKeEAPGLLGGGDIKWNFTKFLIDRDGNVVARFAPTTKPEDpeLEAAIEKLL 161
GSHPx pfam00255
Glutathione peroxidase;
1448-1556 6.61e-45

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 157.90  E-value: 6.61e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223  1448 IHEFTVKDARGQEVDLSVYKGKVLLVVNVASKCGFTDsNYTQLTELYKKYKDQGLEILAFPCNQFLKQEPGSSENAQEFA 1527
Cdd:pfam00255    1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79

                           90       100
                   ....*....|....*....|....*....
gi 802793223  1528 CTRYKAEYPIFQKVRVNGPNTAPVYKFLK 1556
Cdd:pfam00255   80 PGGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 1447-1589 4.10e-42

putative glutathione peroxidase Gpx7; This model represents one of several families of known and probable glutathione peroxidases. This family is restricted to animals and designated GPX7.


Pssm-ID: 131592 [Multi-domain]  Cd Length: 153  Bit Score: 151.53  E-value: 4.10e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223  1447 SIHEFTVKDARGQEVDLSVYKGKVLLVVNVASKCGFTDSNYTQLTELYKKYKDQGLEILAFPCNQFLKQEPGSSENAQEF 1526
Cdd:TIGR02540    1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 802793223  1527 ACTRYKAEYPIFQKVRVNGPNTAPVYKFLKASKfgfmGSSIKWNFTKFLINREGQVINRYGPT 1589
Cdd:TIGR02540   81 ARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSS----KKEPRWNFWKYLVNPEGQVVKFWRPE 139
PWWP_HULK cd20147
PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family; The HULK family ...
 25-113 6.63e-41

PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family; The HULK family includes HUA2-like proteins 1-3 (HULK1-3), which are probable transcription factors that act with partial redundancy with each other. They may play diverse and essential roles in the control of plant development, physiology and flowering time. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438975 [Multi-domain]  Cd Length: 92  Bit Score: 145.71  E-value: 6.63e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223   25 GDLVLAKVKGFPAWPATVSEPEKWGYSADWKKVLVYFFGTQQIAFCNPADVEAFTEEKKQSLLVK--RQGKGADFVRAVQ 102
Cdd:cd20147     1 GDLVLAKVKGFPAWPAQVSEPEDWGSAPDPKKVFVHFFGTQQIGFCNPGELSEFTEEIKQSLLARtlKKKKGSDFSRAVK 80

                          90
                  ....*....|.
gi 802793223  103 EIIDSYEKSKK 113
Cdd:cd20147    81 EICELYEERKG 91
RPR smart00582
domain present in proteins, which are involved in regulation of nuclear pre-mRNA;
899-1030 3.98e-30

domain present in proteins, which are involved in regulation of nuclear pre-mRNA;


Pssm-ID: 214731  Cd Length: 124  Bit Score: 116.22  E-value: 3.98e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223    899 SFEGTLGSLTRTKESIGRATRIAIDCAKFGIsnKVVEILARHLESESSlHRRVDLFFLVDSITQCSRGLKG-DVGGIYPS 977
Cdd:smart00582    1 AFEQKLESLNNSQESIQTLTKWAIEHASHAK--EIVELWEKYIKKAPV-PRKLPLLYLLDSIVQNSKRKYGsEFGDELGP 77

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 802793223    978 AIQAVLPRLLsaaappGSFAQENRRQCLKVLRLWLERRILPESVIRHHMRELD 1030
Cdd:smart00582   78 VFQDALRRVL------GAAPEELKKKIRRLLNIWEERGIFPPEVLRPLREKLN 124
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 25-109 3.22e-20

PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain binds to Histone-4 methylated at lysine-20, H4K20me, suggesting that it is methyl-lysine recognition motif. Removal of two conserved aromatic residues in a hydrophobic cavity created by this domain within the full-length protein, Pdp1, abolishes the interaction o f the protein with H4K20me3. In fission yeast, Set9 is the sole enzyme that catalyzes all three states of H4K20me, and Set9-mediated H4K20me is required for efficient recruitment of checkpoint protein Crb2 to sites of DNA damage. The methylation of H4K20 is involved in a diverse array of cellular processes, such as organizing higher-order chromatin, maintaining genome stability, and regulating cell-cycle progression.


Pssm-ID: 459964 [Multi-domain]  Cd Length: 92  Bit Score: 86.71  E-value: 3.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223    25 GDLVLAKVKGFPAWPATVSEPEKWG-----YSADWKKVLVYFFGTQQIAFCNPADVEAFTEEKKQSLL--VKRQGKGADF 97
Cdd:pfam00855    1 GDLVWAKLKGYPWWPARVVDPEELPenvlkPKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEFEYLkkKKKKKKKKAF 80

                           90
                   ....*....|..
gi 802793223    98 VRAVQEIIDSYE 109
Cdd:pfam00855   81 KKALEEAEEALK 92
CID pfam04818
CID domain; This domain binds to the phosphorylated C-terminal domain (CTD) of RNA polymerase ...
 898-1022 1.55e-14

CID domain; This domain binds to the phosphorylated C-terminal domain (CTD) of RNA polymerase II. This domain is known as the CTD-interacting domain (CID).


Pssm-ID: 461442  Cd Length: 117  Bit Score: 71.47  E-value: 1.55e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223   898 SSFEGTLGSLTRTKESIGRATRIAIDCAKFgiSNKVVEILARHLeSESSLHRRVDLFFLVDSITQCSRGLKGDVggiYPS 977
Cdd:pfam04818    1 EALEKKLSSLNNSQESIQTLSKWILFHRKH--AKAIVEVWEKYL-KKAKPEKKLHLLYLANDVLQNSRKKGKSE---FAD 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 802793223   978 AIQAVLPRLLSAAAPPGSfaQENRRQCLKVLRLWLERRILPESVI 1022
Cdd:pfam04818   75 AFEPVLPEAFASAYKKCD--EKLKKKLERLLNIWEERNVFSPEVI 117
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 23-75 1.17e-07

domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 50.04  E-value: 1.17e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 802793223     23 KVGDLVLAKVKGFPAWPATVSEPEKWGYS-----ADWKKVLVYFFGTQQIAFCNPADV 75
Cdd:smart00293    2 KPGDLVWAKMKGFPWWPALVISPKMTPDNimkrkSDENLYPVLFFGDKDTAWIPSSKL 59
DUF3824 pfam12868
Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It ...
 1323-1422 1.37e-05

Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It is proline-rich, and the function is not known.


Pssm-ID: 372351 [Multi-domain]  Cd Length: 145  Bit Score: 46.66  E-value: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223  1323 RRENPPPYEHRYHPSHNGDGGNFYYnhERMRPAPYEPS-------------ESWRYPAPPFSGPR-----YPDKGRTPYS 1384
Cdd:pfam12868   29 RRERKKAERERERRRYEDDYRDYYE--DPYSPSPYPPSpagpyasqgqyypETNYFPPPPGSTPQppvdpQPNAPPPPYN 106

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 802793223  1385 PGPYGGPPreQTRIPHQGWSFPPREMHHrnfmPFRPPP 1422
Cdd:pfam12868  107 PADYPPPP--GAAPPPQPYQYPPPPGPD----PYAPRP 138
CID_RPRD_like cd16981
CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing proteins; ...
 898-1023 2.03e-04

CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing proteins; This family is composed of Regulation of nuclear pre-mRNA domain-containing proteins 1A (RPRD1A), 1B (RPRD1B), 2 (RPRD2), yeast Rtt103, and similar proteins. RPRD1A, RPRD1B, and RPRD2 are CID (CTD-Interacting Domain) containing proteins that co-purify with RNA polymerase (Pol) II (RNAP II) and three other RNAP II-associated proteins, RPAP2, GRINL1A and RECQL5, but not with the Mediator complex. Yeast transcription termination factor Rtt103 is a CID containing protein that functions in DNA damage response. CID binds tightly to the carboxy-terminal domain (CTD) of RNAP II. During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices.


Pssm-ID: 340778  Cd Length: 125  Bit Score: 42.57  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223  898 SSFEGTLGSLTRTKESIGRATRIAIDCAKFgiSNKVVEILARHLESeSSLHRRVDLFFLVDSITQCSRGlKGdvGGIYPS 977
Cdd:cd16981     2 EALEKKLRSLNNTQQSIQTLSLWCLFHKKH--AKQIVKIWLKELKK-AKPERKLTLLYLANDVLQNSRR-KG--APEFVE 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 802793223  978 AIQAVLPRLLSAAAPPGSfaQENRRQCLKVLRLWLERRILPESVIR 1023
Cdd:cd16981    76 AFKKVLPEALALVRSEGD--ESVRKKVLRVLNIWEERNVFGSEFLA 119
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 1447-1599 1.56e-83

Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.


Pssm-ID: 238207 [Multi-domain]  Cd Length: 152  Bit Score: 270.16  E-value: 1.56e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223 1447 SIHEFTVKDARGQEVDLSVYKGKVLLVVNVASKCGFTdSNYTQLTELYKKYKDQGLEILAFPCNQFLKQEPGSSENAQEF 1526
Cdd:cd00340     1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 802793223 1527 ACTRYKAEYPIFQKVRVNGPNTAPVYKFLKASKFGFMGSSIKWNFTKFLINREGQVINRYGPTTNPLSFEDHI 1599
Cdd:cd00340    80 CETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
PLN02412 PLN02412
probable glutathione peroxidase
 1446-1603 1.80e-79

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 259.15  E-value: 1.80e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223 1446 KSIHEFTVKDARGQEVDLSVYKGKVLLVVNVASKCGFTDSNYTQLTELYKKYKDQGLEILAFPCNQFLKQEPGSSENAQE 1525
Cdd:PLN02412    7 KSIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQ 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 802793223 1526 FACTRYKAEYPIFQKVRVNGPNTAPVYKFLKASKFGFMGSSIKWNFTKFLINREGQVINRYGPTTNPLSFEDHIKKAL 1603
Cdd:PLN02412   87 TVCTRFKAEFPIFDKVDVNGKNTAPLYKYLKAEKGGLFGDAIKWNFTKFLVSKEGKVVQRYAPTTSPLKIEKDIQNLL 164
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 1447-1603 2.05e-77

Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 253.08  E-value: 2.05e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223 1447 SIHEFTVKDARGQEVDLSVYKGKVLLVVNVASKCGFTdSNYTQLTELYKKYKDQGLEILAFPCNQFLKQEPGSSENAQEF 1526
Cdd:COG0386     3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223 1527 ACTRYKAEYPIFQKVRVNGPNTAPVYKFLK-ASKFGFMGSSIKWNFTKFLINREGQVINRYGPTTNPLS--FEDHIKKAL 1603
Cdd:COG0386    82 CSLNYGVTFPMFAKIDVNGPNAHPLYKYLKeEAPGLLGGGDIKWNFTKFLIDRDGNVVARFAPTTKPEDpeLEAAIEKLL 161
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 1433-1603 1.23e-75

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 250.97  E-value: 1.23e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223 1433 SRAGMGGSASVPEKSIHEFTVKDARGQEVDLSVYKGKVLLVVNVASKCGFTDSNYTQLTELYKKYKDQGLEILAFPCNQF 1512
Cdd:PLN02399   64 SRSFGVYARAATEKSVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQF 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223 1513 LKQEPGSSENAQEFACTRYKAEYPIFQKVRVNGPNTAPVYKFLKASKFGFMGSSIKWNFTKFLINREGQVINRYGPTTNP 1592
Cdd:PLN02399  144 GGQEPGSNPEIKQFACTRFKAEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLGDLIKWNFEKFLVDKNGKVVERYPPTTSP 223

                         170
                  ....*....|.
gi 802793223 1593 LSFEDHIKKAL 1603
Cdd:PLN02399  224 FQIEKDIQKLL 234
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
 1443-1603 6.74e-59

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 200.76  E-value: 6.74e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223 1443 VPEKSIHEFTVKDARGQEVDLSVYKG-KVLLVVNVASKCGFTDSNYTQLTELYKKYKDQGLEILAFPCNQFLKQEPGSSE 1521
Cdd:PTZ00256   15 PPTKSFFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223 1522 NAQEFACTRYKAEYPIFQKVRVNGPNTAPVYKFLKASKFGFMGSS-----IKWNFTKFLINREGQVINRYGPTTNPLSFE 1596
Cdd:PTZ00256   95 EIKEYVQKKFNVDFPLFQKIEVNGENTHEIYKYLRRNSELFQNNTnearqIPWNFAKFLIDGQGKVVKYFSPKVNPNEMI 174


                  ....*..
gi 802793223 1597 DHIKKAL 1603
Cdd:PTZ00256  175 QDIEKLL 181
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 1444-1606 2.01e-46

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 165.80  E-value: 2.01e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223 1444 PEKSIHEFTVKDARGQEVDLSVYKGKVLLVVNVASKCGFTDSNYTQLTELYKKYKDQGLEILAFPCNQFLKQEPGSSENA 1523
Cdd:PTZ00056   15 LRKSIYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223 1524 QEFAcTRYKAEYPIFQKVRVNGPNTAPVYKFLKAS------KFGFMgSSIKWNFTKFLINREGQVINRYGPTTNPLSFED 1597
Cdd:PTZ00056   95 RKFN-DKNKIKYNFFEPIEVNGENTHELFKFLKANcdsmhdENGTL-KAIGWNFGKFLVNKSGNVVAYFSPRTEPLELEK 172


                  ....*....
gi 802793223 1598 HIKKALEIK 1606
Cdd:PTZ00056  173 KIAELLGVK 181
btuE PRK10606
putative glutathione peroxidase; Provisional
 1447-1603 3.51e-46

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 164.56  E-value: 3.51e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223 1447 SIHEFTVKDARGQEVDLSVYKGKVLLVVNVASKCGFTdSNYTQLTELYKKYKDQGLEILAFPCNQFLKQEPGSSENAQEF 1526
Cdd:PRK10606    4 SILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLT-PQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKTY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223 1527 ACTRYKAEYPIFQKVRVNGPNTAPVYKFLKAS--------KFGF---MGSS---------IKWNFTKFLINREGQVINRY 1586
Cdd:PRK10606   83 CRTTWGVTFPMFSKIEVNGEGRHPLYQKLIAAaptavapeESGFyarMVSKgraplypddILWNFEKFLVGRDGQVIQRF 162

                         170       180
                  ....*....|....*....|..
gi 802793223 1587 GPTTNPlsfED-----HIKKAL 1603
Cdd:PRK10606  163 SPDMTP---EDpivmeSIKLAL 181
GSHPx pfam00255
Glutathione peroxidase;
1448-1556 6.61e-45

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 157.90  E-value: 6.61e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223  1448 IHEFTVKDARGQEVDLSVYKGKVLLVVNVASKCGFTDsNYTQLTELYKKYKDQGLEILAFPCNQFLKQEPGSSENAQEFA 1527
Cdd:pfam00255    1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79

                           90       100
                   ....*....|....*....|....*....
gi 802793223  1528 CTRYKAEYPIFQKVRVNGPNTAPVYKFLK 1556
Cdd:pfam00255   80 PGGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 1447-1589 4.10e-42

putative glutathione peroxidase Gpx7; This model represents one of several families of known and probable glutathione peroxidases. This family is restricted to animals and designated GPX7.


Pssm-ID: 131592 [Multi-domain]  Cd Length: 153  Bit Score: 151.53  E-value: 4.10e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223  1447 SIHEFTVKDARGQEVDLSVYKGKVLLVVNVASKCGFTDSNYTQLTELYKKYKDQGLEILAFPCNQFLKQEPGSSENAQEF 1526
Cdd:TIGR02540    1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 802793223  1527 ACTRYKAEYPIFQKVRVNGPNTAPVYKFLKASKfgfmGSSIKWNFTKFLINREGQVINRYGPT 1589
Cdd:TIGR02540   81 ARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSS----KKEPRWNFWKYLVNPEGQVVKFWRPE 139
PWWP_HULK cd20147
PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family; The HULK family ...
 25-113 6.63e-41

PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family; The HULK family includes HUA2-like proteins 1-3 (HULK1-3), which are probable transcription factors that act with partial redundancy with each other. They may play diverse and essential roles in the control of plant development, physiology and flowering time. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438975 [Multi-domain]  Cd Length: 92  Bit Score: 145.71  E-value: 6.63e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223   25 GDLVLAKVKGFPAWPATVSEPEKWGYSADWKKVLVYFFGTQQIAFCNPADVEAFTEEKKQSLLVK--RQGKGADFVRAVQ 102
Cdd:cd20147     1 GDLVLAKVKGFPAWPAQVSEPEDWGSAPDPKKVFVHFFGTQQIGFCNPGELSEFTEEIKQSLLARtlKKKKGSDFSRAVK 80

                          90
                  ....*....|.
gi 802793223  103 EIIDSYEKSKK 113
Cdd:cd20147    81 EICELYEERKG 91
RPR smart00582
domain present in proteins, which are involved in regulation of nuclear pre-mRNA;
899-1030 3.98e-30

domain present in proteins, which are involved in regulation of nuclear pre-mRNA;


Pssm-ID: 214731  Cd Length: 124  Bit Score: 116.22  E-value: 3.98e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223    899 SFEGTLGSLTRTKESIGRATRIAIDCAKFGIsnKVVEILARHLESESSlHRRVDLFFLVDSITQCSRGLKG-DVGGIYPS 977
Cdd:smart00582    1 AFEQKLESLNNSQESIQTLTKWAIEHASHAK--EIVELWEKYIKKAPV-PRKLPLLYLLDSIVQNSKRKYGsEFGDELGP 77

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 802793223    978 AIQAVLPRLLsaaappGSFAQENRRQCLKVLRLWLERRILPESVIRHHMRELD 1030
Cdd:smart00582   78 VFQDALRRVL------GAAPEELKKKIRRLLNIWEERGIFPPEVLRPLREKLN 124
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 25-109 3.22e-20

PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain binds to Histone-4 methylated at lysine-20, H4K20me, suggesting that it is methyl-lysine recognition motif. Removal of two conserved aromatic residues in a hydrophobic cavity created by this domain within the full-length protein, Pdp1, abolishes the interaction o f the protein with H4K20me3. In fission yeast, Set9 is the sole enzyme that catalyzes all three states of H4K20me, and Set9-mediated H4K20me is required for efficient recruitment of checkpoint protein Crb2 to sites of DNA damage. The methylation of H4K20 is involved in a diverse array of cellular processes, such as organizing higher-order chromatin, maintaining genome stability, and regulating cell-cycle progression.


Pssm-ID: 459964 [Multi-domain]  Cd Length: 92  Bit Score: 86.71  E-value: 3.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223    25 GDLVLAKVKGFPAWPATVSEPEKWG-----YSADWKKVLVYFFGTQQIAFCNPADVEAFTEEKKQSLL--VKRQGKGADF 97
Cdd:pfam00855    1 GDLVWAKLKGYPWWPARVVDPEELPenvlkPKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEFEYLkkKKKKKKKKAF 80

                           90
                   ....*....|..
gi 802793223    98 VRAVQEIIDSYE 109
Cdd:pfam00855   81 KKALEEAEEALK 92
PWWP cd05162
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
 25-106 4.40e-17

PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, is a small domain consisting of 100-150 amino acids and is composed of a five-stranded antiparallel beta-barrel followed by a helical region. It is found in numerous proteins that are involved in cell division, growth, and differentiation. Most PWWP-domain proteins seem to be nuclear, often DNA-binding, proteins that function as transcription factors regulating a variety of developmental processes. PWWP domains specifically recognize DNA and histone methylated lysines at the level of the nucleosome. Based on the fact that other regions of PWWP-domain proteins are responsible for nuclear localization and DNA-binding, is likely that the PWWP domain acts as a site for protein-protein binding interactions, influencing chromatin remodeling and thereby regulating transcriptional processes. Some PWWP-domain proteins have been linked to cancer or other diseases; some are known to function as growth factors.


Pssm-ID: 438958 [Multi-domain]  Cd Length: 86  Bit Score: 77.54  E-value: 4.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223   25 GDLVLAKVKGFPAWPATVSEPEK----WGYSADWKKVLVYFFGTQQIAFCNPADVEAFTEEKKQSLLVKRQgKGADFVRA 100
Cdd:cd05162     1 GDLVWAKLKGYPWWPARVVDPEElpeeVGKKKKKGGVLVQFFGDNDYAWVKSKNIKPFEEGFKKEFKKKKK-KSKKFKKA 79


                  ....*.
gi 802793223  101 VQEIID 106
Cdd:cd05162    80 VEEAEE 85
PWWP_HRP cd05834
PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family; The ...
 23-105 3.63e-16

PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family; The HRP family includes hepatoma-derived growth factor (HDGF), and HDGF-related proteins (HRPs). HDGF, also called high mobility group protein 1-like 2 (HMG-1L2), is a heparin-binding protein that acts as a transcriptional repressor with mitogenic activity for fibroblasts. It is a prognostic factor in several types of cancer. HDGFL1 is also called PWWP domain-containing protein 1 (PWWP1). Its biological function remains unclear. HDGFL2, also called HDGF-related protein 2 (HRP-2), or hepatoma-derived growth factor 2 (HDGF-2), is involved in cellular growth control, through the regulation of cyclin D1 expression. HDGFL3, also called HDGF-related protein 3 (HRP-3), enhances DNA synthesis and may play a role in cell proliferation. The family also includes PC4 and SFRS1-interacting protein (PSIP) and similar proteins. PSIP, also called CLL-associated antigen KW-7, dense fine speckles 70 kDa protein (DFS 70), lens epithelium-derived growth factor (LEDGF), or transcriptional coactivator p75/p52, acts as a transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Members of the HRP family contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438959 [Multi-domain]  Cd Length: 82  Bit Score: 74.90  E-value: 3.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223   23 KVGDLVLAKVKGFPAWPATVSEPEKWGYSADwKKVLVYFFGTQQIAFCNPADVEAFTEEK-KQSLLVKRQGkgadFVRAV 101
Cdd:cd05834     2 KPGDLVFAKVKGYPPWPARIDEIPEGAKIPK-NKYPVFFYGTHETAFLKPKDLFPYEENKeKYGKPRKRKG----FNEGL 76


                  ....
gi 802793223  102 QEII 105
Cdd:cd05834    77 WEIE 80
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
 22-106 5.17e-16

PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called 3-hydroxyisobutyrate dehydrogenase-like protein, cytokine-like nuclear factor N-PAC, nuclear protein NP60, or nuclear protein of 60 kDa, is a putative oxidoreductase that is recruited on chromatin and promotes KDM1B demethylase activity. It recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3). GLYR1 enhances the activity of MAP2K4 and MAP2K6 kinases to phosphorylate p38-alpha. In addition to the PWWP domain, GLYR1 also contains an AT-hook and a C-terminal NAD-binding domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438961 [Multi-domain]  Cd Length: 86  Bit Score: 74.56  E-value: 5.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223   22 WKVGDLVLAKVKGFPAWPATVSEPEKwgysaDWKKV-------LVYFFGTQQIAFCNPADVEAFTEEKKQSLLVKrqgKG 94
Cdd:cd05836     1 FKIGDLVWAKMKGFPPWPGKIVNPPP-----DLKKPprkkkmhCVYFFGSENYAWIEDENIKPYEEFKEEMLKSK---KS 72

                          90
                  ....*....|..
gi 802793223   95 ADFVRAVQEIID 106
Cdd:cd05836    73 AGFKDAVEAIEE 84
CID pfam04818
CID domain; This domain binds to the phosphorylated C-terminal domain (CTD) of RNA polymerase ...
 898-1022 1.55e-14

CID domain; This domain binds to the phosphorylated C-terminal domain (CTD) of RNA polymerase II. This domain is known as the CTD-interacting domain (CID).


Pssm-ID: 461442  Cd Length: 117  Bit Score: 71.47  E-value: 1.55e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223   898 SSFEGTLGSLTRTKESIGRATRIAIDCAKFgiSNKVVEILARHLeSESSLHRRVDLFFLVDSITQCSRGLKGDVggiYPS 977
Cdd:pfam04818    1 EALEKKLSSLNNSQESIQTLSKWILFHRKH--AKAIVEVWEKYL-KKAKPEKKLHLLYLANDVLQNSRKKGKSE---FAD 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 802793223   978 AIQAVLPRLLSAAAPPGSfaQENRRQCLKVLRLWLERRILPESVI 1022
Cdd:pfam04818   75 AFEPVLPEAFASAYKKCD--EKLKKKLERLLNIWEERNVFSPEVI 117
PWWP_HDGF cd20148
PWWP domain found in Hepatoma-derived growth factor (HDGF); HDGF, also called high mobility ...
 22-84 1.92e-11

PWWP domain found in Hepatoma-derived growth factor (HDGF); HDGF, also called high mobility group protein 1-like 2 (HMG-1L2), is a heparin-binding protein that acts as a transcriptional repressor with mitogenic activity for fibroblasts. It contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438976 [Multi-domain]  Cd Length: 87  Bit Score: 61.58  E-value: 1.92e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 802793223   22 WKVGDLVLAKVKGFPAWPATVSEPEKWGYSADWKKVLVYFFGTQQIAFCNPADVEAFTEEKKQ 84
Cdd:cd20148     1 YKCGDLVFAKMKGYPHWPARIDEMPEAAVKSTANKYQVFFFGTHETAFLGPKDLFPYEESKEK 63
PWWP_PSIP cd20151
PWWP domain found in PC4 and SFRS1-interacting protein (PSIP); PSIP, also called ...
 22-92 3.43e-11

PWWP domain found in PC4 and SFRS1-interacting protein (PSIP); PSIP, also called CLL-associated antigen KW-7, dense fine speckles 70 kDa protein (DFS 70), lens epithelium-derived growth factor (LEDGF), or transcriptional coactivator p75/p52, acts as a transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. It contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438979 [Multi-domain]  Cd Length: 88  Bit Score: 60.77  E-value: 3.43e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 802793223   22 WKVGDLVLAKVKGFPAWPATVSEPEKWGYSADWKKVLVYFFGTQQIAFCNPADVEAFTEEK-KQSLLVKRQG 92
Cdd:cd20151     1 FKPGDLIFAKMKGYPHWPARVDEVPDGAVKPPTNKLPIFFFGTHETAFLGPKDIFPYSENKeKYGKPNKRKG 72
PWWP_HDGFL3 cd20150
PWWP domain found in Hepatoma-derived growth factor-related protein 3 (HDGFL3); HDGFL3, also ...
 21-84 1.88e-10

PWWP domain found in Hepatoma-derived growth factor-related protein 3 (HDGFL3); HDGFL3, also called HDGF-related protein 3 (HRP-3), is the only hepatoma-derived growth factor (HDGF)-related protein (HRP) family member whose expression is almost restricted to the nervous tissue. It enhances DNA synthesis and may play a role in cell proliferation. It contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438978 [Multi-domain]  Cd Length: 93  Bit Score: 58.92  E-value: 1.88e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 802793223   21 QWKVGDLVLAKVKGFPAWPATVSEPEKWGYSADWKKVLVYFFGTQQIAFCNPADVEAFTEEKKQ 84
Cdd:cd20150     5 EYKAGDLVFAKMKGYPHWPARIDELPEGAVKPPANKYPIFFFGTHETAFLGPKDLFPYKEYKDK 68
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
1450-1604 9.64e-10

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 58.34  E-value: 9.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223 1450 EFTVKDARGQEVDLSVYKGKVLLVVNVASKCGF-TDSNyTQLTELYKKYKDQGLEILAFpcnqflkqEPGSSENAQEFAc 1528
Cdd:COG1225     3 DFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGcTAEL-PELRDLYEEFKDKGVEVLGV--------SSDSDEAHKKFA- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223 1529 TRYKAEYPIF----QKVrvngpntapvykflkASKFGfmgssIKWNFTKFLINREGQVINRYgptTNPLSFEDHIKKALE 1604
Cdd:COG1225    73 EKYGLPFPLLsdpdGEV---------------AKAYG-----VRGTPTTFLIDPDGKIRYVW---VGPVDPRPHLEEVLE 129
PWWP_HDGFL2 cd20149
PWWP domain found in Hepatoma-derived growth factor-related protein 2 (HDGFL2); HDGFL2, also ...
 22-84 1.35e-09

PWWP domain found in Hepatoma-derived growth factor-related protein 2 (HDGFL2); HDGFL2, also called HDGF-related protein 2 (HRP-2), or Hepatoma-derived growth factor 2 (HDGF-2), is involved in cellular growth control, through the regulation of cyclin D1 expression. It contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438977 [Multi-domain]  Cd Length: 84  Bit Score: 56.45  E-value: 1.35e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 802793223   22 WKVGDLVLAKVKGFPAWPATVSEPEKWGYSADWKKVLVYFFGTQQIAFCNPADVEAFTEEKKQ 84
Cdd:cd20149     1 FKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKYKDK 63
PWWP_AtATX3-like cd20143
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
 25-110 2.53e-09

PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like protein ATX3, ATX4, ATX5, and similar proteins; The family includes A. thaliana ATX3 (also called protein SET domain group 14, or trithorax-homolog protein 3), ATX4 (also called protein SET domain group 16, or trithorax-homolog protein 4) and ATX5 (also called protein SET domain group 29, or trithorax-homolog protein 5), which belong to the histone-lysine methyltransferase family. They show distinct phylogenetic origins from the family of ATX1 and ATX2. They are multi-domain containing protein that consists of an N-terminal PWWP domain, a canonical plant homeodomain (PHD) domain, a non-canonical extended PHD (ePHD) domain, and a C-terminal SET domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438971 [Multi-domain]  Cd Length: 100  Bit Score: 55.84  E-value: 2.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223   25 GDLVLAKVKGFPAWPATVSEPEKWG----YSADWKKVLVYFFG---TQQIAFCNPADVEAFTEE--KKQSLLVKRQGKGA 95
Cdd:cd20143     3 GDLVWAKVGTHPFWPARVVEPAEQAeevrRRCVPGSLCVYFFGpggSRDYGWVRRSMIFPFTDDlaRFQTQKIKNKKRPQ 82

                          90
                  ....*....|....*
gi 802793223   96 DFVRAVQEIIDSYEK 110
Cdd:cd20143    83 EFQEALEEAKLADAG 97
PWWP_ScIOC4-like cd05840
PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar ...
 25-113 2.91e-09

PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar proteins; ScIOC4 functions as a component of the ISW1B complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW1B complex acts within coding regions to control the amount of RNA polymerase II released into productive elongation and to coordinate elongation with termination and pre-mRNA processing. The family also includes Schizosaccharomyces pombe PWWP domain-containing proteins 1 and 2 (SpPDP1 and SpPDP2). SpPDP1 associates with Set9 to regulate its chromatin localization and methyltransferase activity towards H4K20. Members of this family contain a PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438965  Cd Length: 94  Bit Score: 55.77  E-value: 2.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223   25 GDLVLAKVKGFPAWPATVSEPEKWGYSADWKKVL----------VYFFGTQQIAFCNPADVEAFTEEKKQSLLVKRQGKG 94
Cdd:cd05840     1 GDLVLAKVKGYPPWPAMVLPEELLPKNVLKAKKRkpkskktvypVQFFPDNEYYWVSPSSLKPLTKEEIDKFLSKSKRKN 80

                          90
                  ....*....|....*....
gi 802793223   95 adfvravQEIIDSYEKSKK 113
Cdd:cd05840    81 -------KDLIEAYEVALE 92
PWWP_AtATX1-like cd20142
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
 24-113 1.66e-08

PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like proteins ATX1, ATX2, and similar proteins; This family includes A. thaliana ATX1 and ATX2, which 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 called 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 called protein SET domain group 30, or trithorax-homolog protein 2 (TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). Both ATX1 and ATX2 are multi-domain containing proteins that consist of an N-terminal PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical plant homeodomain (PHD) domain, a non-canonical extended PHD (ePHD) domain, and a C-terminal SET domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438970 [Multi-domain]  Cd Length: 97  Bit Score: 53.51  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223   24 VGDLVLAKVKGFPAWPATV---SEPEKWGYSADWKK----VLVYFFGTQQIAFCNPADVEAFTEEKKQSLLVKRqgKGAD 96
Cdd:cd20142     2 PGDVVWAKVKGYPMWPALVideEHAERCGLEANRPGkkgtVPVQFFGTYEVARLNPKKVVGFSKGLDLKYHSKC--KAPV 79

                          90
                  ....*....|....*..
gi 802793223   97 FVRAVQEiIDSYEKSKK 113
Cdd:cd20142    80 FRQALEE-AERYLKEGK 95
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 1450-1586 7.34e-08

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 52.24  E-value: 7.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223 1450 EFTVKDARGQEVDLSVYKGKVlLVVNV-ASKCGFTDSNYTQLTELYKKYKDQGLEILAfpcnqfLKQEPGSSENAQEFAc 1528
Cdd:cd02966     1 DFSLPDLDGKPVSLSDLKGKV-VLVNFwASWCPPCRAEMPELEALAKEYKDDGVEVVG------VNVDDDDPAAVKAFL- 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 802793223 1529 TRYKAEYPIFQkvrvngpntAPVYKFLKAskFGFMGssikWNFTkFLINREGQVINRY 1586
Cdd:cd02966    73 KKYGITFPVLL---------DPDGELAKA--YGVRG----LPTT-FLIDRDGRIRARH 114
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 23-75 1.17e-07

domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 50.04  E-value: 1.17e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 802793223     23 KVGDLVLAKVKGFPAWPATVSEPEKWGYS-----ADWKKVLVYFFGTQQIAFCNPADV 75
Cdd:smart00293    2 KPGDLVWAKMKGFPWWPALVISPKMTPDNimkrkSDENLYPVLFFGDKDTAWIPSSKL 59
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 1450-1604 9.40e-07

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 49.69  E-value: 9.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223 1450 EFTVKDARGQEVDLSVYKGKVLLvVNV-ASKCGFTDSNYTQLTELYKKYKdqGLEILAFPCNQflkqepgSSENAQEFAc 1528
Cdd:COG0526    10 DFTLTDLDGKPLSLADLKGKPVL-VNFwATWCPPCRAEMPVLKELAEEYG--GVVFVGVDVDE-------NPEAVKAFL- 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 802793223 1529 TRYKAEYPIFQkvrvngpntAPVYKFlkASKFGFMGSSikwnfTKFLINREGQVINRYGPTTNPLSFEDHIKKALE 1604
Cdd:COG0526    79 KELGLPYPVLL---------DPDGEL--AKAYGVRGIP-----TTVLIDKDGKIVARHVGPLSPEELEEALEKLLA 138
DUF3824 pfam12868
Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It ...
 1323-1422 1.37e-05

Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It is proline-rich, and the function is not known.


Pssm-ID: 372351 [Multi-domain]  Cd Length: 145  Bit Score: 46.66  E-value: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223  1323 RRENPPPYEHRYHPSHNGDGGNFYYnhERMRPAPYEPS-------------ESWRYPAPPFSGPR-----YPDKGRTPYS 1384
Cdd:pfam12868   29 RRERKKAERERERRRYEDDYRDYYE--DPYSPSPYPPSpagpyasqgqyypETNYFPPPPGSTPQppvdpQPNAPPPPYN 106

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 802793223  1385 PGPYGGPPreQTRIPHQGWSFPPREMHHrnfmPFRPPP 1422
Cdd:pfam12868  107 PADYPPPP--GAAPPPQPYQYPPPPGPD----PYAPRP 138
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 1450-1538 2.14e-05

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 45.68  E-value: 2.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223  1450 EFTVKDARGQEVDLSVYKGKVLLVVNVASK-CGFTDSNYTQLTELYKKYKDQGLEILAFPCNqflkqepgSSENAQEFAc 1528
Cdd:pfam00578    7 DFELPDGDGGTVSLSDYRGKWVVLFFYPADwTPVCTTELPALADLYEEFKKLGVEVLGVSVD--------SPESHKAFA- 77

                           90
                   ....*....|
gi 802793223  1529 TRYKAEYPIF 1538
Cdd:pfam00578   78 EKYGLPFPLL 87
PWWP_PRKCBP1 cd20160
PWWP domain found in protein kinase C-binding protein 1 (PRKCBP1) and similar proteins; ...
 27-104 2.21e-05

PWWP domain found in protein kinase C-binding protein 1 (PRKCBP1) and similar proteins; PRKCBP1, also called cutaneous T-cell lymphoma-associated antigen se14-3 (CTCL-associated antigen se14-3), Rack7, or zinc finger MYND domain-containing protein 8 (ZMYND8), is a novel receptor for activated C-kinase (RACK)-like protein that may play an important role in the activation and regulation of PKC-beta I, and the PKC signaling cascade. It also has been identified as a formin homology-2-domain containing protein 1 (FHOD1)-binding protein that may be involved in FHOD1-regulated actin polymerization and transcription. Moreover, PRKCBP1 may function as a REST co-repressor 2 (RCOR2) interacting factor. They form a RCOR2/ZMYND8 complex which might be involved in the regulation of neural differentiation. PRKCBP1 contains a plant homeodomain (PHD) finger, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438988  Cd Length: 91  Bit Score: 44.48  E-value: 2.21e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 802793223   27 LVLAKVKGFPAWPATVsepekwgYSADWKKVLVYFFGTQQIAFCNPADVEAFTEEKKQSLLVKRQgkgaDFVRAVQEI 104
Cdd:cd20160     9 LVWAKLKGFPFWPAKA-------LRVNNGQVDVRFFGAHDRAWVPVKDCYLYSKEPPTSVKKKKS----GLDEAMEEL 75
PWWP_MUM1-like cd06080
PWWP domain found in mutated melanoma-associated antigen 1 (MUM-1) and similar proteins; MUM-1, ...
 23-110 2.59e-05

PWWP domain found in mutated melanoma-associated antigen 1 (MUM-1) and similar proteins; MUM-1, also called PWWP domain-containing DNA repair factor 3A (PWWP3A), or protein expandere (EXPAND1), is a melanoma-associated antigen (MAA) that belongs to the mutated or aberrantly expressed type of MAAs, along with antigens such as CDK4, beta-catenin, gp100-in4, p15, and N-acetylglucosaminyltransferase V. It is highly expressed in several types of human cancers and involved in the DNA damage response pathway by contributing to the maintenance of chromatin architecture. MUM-1 is recruited to the vicinity of DNA breaks by TP53BP1 and plays an accessory role to facilitate damage-induced chromatin changes and promoting chromatin relaxation. It is required for efficient DNA repair and cell survival following DNA damage. This subfamily also includes mutated melanoma-associated antigen 1-like protein 1 (MUM1L1), also called MUM1-like protein 1, or PWWP domain-containing DNA repair factor 3B (PWWP3B). Its biological function remains unclear. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438967  Cd Length: 90  Bit Score: 44.17  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223   23 KVGDLVLAKVKGFPAWPATVsepekwgYSADW--KKVLVYFFGT--QQIAFCNPAD-VEAFTEEKKQSLL--VKRQGKGA 95
Cdd:cd06080     2 SKGDIVWAKYRKYPYWPAVV-------KSVYKkpKKASVLFLELppEKKGIKVSLKkLKPFDCKEKEELLeeGKESPYSE 74

                          90
                  ....*....|....*
gi 802793223   96 DFVRAVQEIIDSYEK 110
Cdd:cd06080    75 DFKEAVELAEDYLIK 89
PWWP_NSD_rpt2 cd05838
second PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
 24-103 2.62e-05

second PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein family consists of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1, that are critical in maintaining chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising in suppressing cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play nonredundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (C5HCH). This model corresponds to the second PWWP domain. The family also includes Drosophila melanogaster maternal-effect sterile 4 (dMes4) that may act as a histone-lysine N-methyltransferase required for wing morphogenesis. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438963 [Multi-domain]  Cd Length: 96  Bit Score: 44.54  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223   24 VGDLVLAKVKGFPAWPATVSEPEK-----WGYSADWKKVLVYFFGTQQIAFCNPADVEAFTEEKKQSLLVKRQGKGADFV 98
Cdd:cd05838     2 YGDIVWVKLGNYRWWPAEILHPREvpdniQSLPHPPGEFPVRFFGSHDYYWVHRGRVFLFEEGDKGSKEKSKKSLDKSFK 81


                  ....*
gi 802793223   99 RAVQE 103
Cdd:cd05838    82 RALKE 86
PWWP_BS69 cd20159
PWWP domain found in protein BS69 and similar proteins; Protein BS69, also called zinc finger ...
 26-103 6.83e-05

PWWP domain found in protein BS69 and similar proteins; Protein BS69, also called zinc finger MYND domain-containing protein 11 (ZMYND11 or ZMY11), is a ubiquitously expressed nuclear protein acting as a transcriptional co-repressor in association with various transcription factors. It was originally identified as an adenovirus 5 E1A-binding protein that inhibits E1A transactivation, as well as c-Myb transcription. It also mediates repression, at least in part, through interaction with the co-repressor N-CoR. Moreover, it interacts with Toll-interleukin 1 receptor domain (TIR)-containing adaptor molecule-1 (TICAM-1, also named TRIF) to facilitate NF-kappaB activation and type I IFN induction. It associates with PIAS1, a SUMO E3 enzyme, and Ubc9, a SUMO E2 enzyme, and plays an inhibitory role in muscle and neuronal differentiation. Moreover, BS69 regulates Epstein-Barr virus (EBV) latent membrane protein 1 (LMP1)/C-terminal activation region 2 (CTAR2)-mediated NF-kappaB activation by interfering with the complex formation between TNFR-associated death domain protein (TRADD) and LMP1/CTAR2. It also cooperates with tumor necrosis factor receptor (TNFR)-associated factor 3 (TRAF3) in the regulation of EBV-derived LMP1/CTAR1-induced NF-kappaB activation. Furthermore, BS69 is involved in the p53-p21Cip1-mediated senescence pathway. BS69 contains a plant homeodomain (PHD) finger, a bromodomain, a proline-tryptophan-tryptophan-proline (PWWP) domain, and a MYeloid translocation protein 8, Nervy and DEAF-1 (MYND) domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438987  Cd Length: 85  Bit Score: 42.97  E-value: 6.83e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 802793223   26 DLVLAKVKGFPAWPATVSEPEKwgysadwKKVLVYFFG-TQQIAFCNPADVEAFTeEKKQSLLVKRqgkGADFVRAVQE 103
Cdd:cd20159     8 ELVWAKQKGFPYWPAKVIQKED-------NQYDVRFFGgHHQRAWIPKENIKPIT-TSPKQLKVKR---TAGWNKACEE 75
PWWP_MBD5 cd20141
PWWP domain found in methyl-CpG-binding domain protein 5 (MBD5) and similar proteins; MBD5, is ...
 23-103 7.27e-05

PWWP domain found in methyl-CpG-binding domain protein 5 (MBD5) and similar proteins; MBD5, is a methyl-CpG-binding protein that binds to heterochromatin. It does not interact with either methylated or unmethylated DNA. MBD5 acts as a transcriptional regulator responsible for 2q23.1 deletion syndrome. It belongs to the MBD family proteins, which play central roles in transcriptional regulation and development. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438969  Cd Length: 92  Bit Score: 43.07  E-value: 7.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223   23 KVGDLVLAKVKGFPAWPAT-VSEPEKWGYSADwkKVLVYFFGTQQIAFCNPADVEAFTE-----EKKQsllvKRQGKG-- 94
Cdd:cd20141     2 NVGDLVWGQIRGFPSWPGKlVSENDVGKTNEG--KVWVSWFGDHSFGQVEPDKLKTLSEgleahHRAR----KRTRKGrk 75

                          90
                  ....*....|.
gi 802793223   95 --ADFVRAVQE 103
Cdd:cd20141    76 lnNHLEAAIQE 86
PWWP_ZCWPW2 cd20146
PWWP domain found in zinc finger CW-type PWWP domain protein 2 (ZCWPW2) and similar proteins; ...
 21-64 8.68e-05

PWWP domain found in zinc finger CW-type PWWP domain protein 2 (ZCWPW2) and similar proteins; ZCWPW2 is a histone H3K4me3 reader. In addition to the PWWP domain, ZCWPW2 contains a zinc finger CW (zf-CW) domain that is a histone modification reader for the histone H3 tail with trimethylated K4. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438974  Cd Length: 113  Bit Score: 43.44  E-value: 8.68e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 802793223   21 QWKVGDLVLAKVKGFPAWPATVSE-PEKWGYsADWKK---VLVY---FFGT 64
Cdd:cd20146     8 QLPLGSLVWAKMTGYPRWPAILTPdPICGEY-VDYDEdgeVEKYhveFLGK 57
PWWP_PWWP2B cd20153
PWWP domain found in PWWP domain-containing protein 2B (PWWP2B); PWWP2B is a paralog of PWWP2A, ...
 24-103 1.57e-04

PWWP domain found in PWWP domain-containing protein 2B (PWWP2B); PWWP2B is a paralog of PWWP2A, a H2A.Z-specific chromatin binding protein which may play an important role in the neural crest stem cell migration and differentiation during early development. PWWP2A and PWWP2B form a stable complex with NuRD subunits MTA1/2/3:HDAC1/2:RBBP4/7, but not with MBD2/3, p66alpha/beta, and CHD3/4. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438981  Cd Length: 116  Bit Score: 43.02  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223   24 VGDLVLAKVKGFPAWPA---TVSEPEKWGYSADWKKVLVYFFGTQQIAFCNPADVEAFTEEKKqsLLVKRQGKGAdFVRA 100
Cdd:cd20153    16 VGDIVWGKIHGFPWWPArvlSISLSQKEDGEPSWQEAKVSWFGSPTTSLLSVSKLSPFSEFFK--LRFNRKKKGM-YRKA 92


                  ...
gi 802793223  101 VQE 103
Cdd:cd20153    93 ITE 95
CID_RPRD_like cd16981
CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing proteins; ...
 898-1023 2.03e-04

CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing proteins; This family is composed of Regulation of nuclear pre-mRNA domain-containing proteins 1A (RPRD1A), 1B (RPRD1B), 2 (RPRD2), yeast Rtt103, and similar proteins. RPRD1A, RPRD1B, and RPRD2 are CID (CTD-Interacting Domain) containing proteins that co-purify with RNA polymerase (Pol) II (RNAP II) and three other RNAP II-associated proteins, RPAP2, GRINL1A and RECQL5, but not with the Mediator complex. Yeast transcription termination factor Rtt103 is a CID containing protein that functions in DNA damage response. CID binds tightly to the carboxy-terminal domain (CTD) of RNAP II. During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices.


Pssm-ID: 340778  Cd Length: 125  Bit Score: 42.57  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223  898 SSFEGTLGSLTRTKESIGRATRIAIDCAKFgiSNKVVEILARHLESeSSLHRRVDLFFLVDSITQCSRGlKGdvGGIYPS 977
Cdd:cd16981     2 EALEKKLRSLNNTQQSIQTLSLWCLFHKKH--AKQIVKIWLKELKK-AKPERKLTLLYLANDVLQNSRR-KG--APEFVE 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 802793223  978 AIQAVLPRLLSAAAPPGSfaQENRRQCLKVLRLWLERRILPESVIR 1023
Cdd:cd16981    76 AFKKVLPEALALVRSEGD--ESVRKKVLRVLNIWEERNVFGSEFLA 119
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
1451-1590 2.10e-04

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 43.84  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223 1451 FTVKDARGQEVDLSVYKGKVLLVVNVASKCGFTDSNYTQLTELYKKYKDQGLEILAfpcnqflkqepgssenaqefactr 1530
Cdd:PRK03147   44 FVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIA------------------------ 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 802793223 1531 ykaeypifqkVRVNGPNTApVYKFLKasKFGFmgssikwNFtKFLINREGQVINRYG----PTT 1590
Cdd:PRK03147  100 ----------VNVDETELA-VKNFVN--RYGL-------TF-PVAIDKGRQVIDAYGvgplPTT 142
PWWP_BRPF cd05839
PWWP domain found in the bromodomain and PHD finger-containing (BRPF) protein family; The BRPF ...
 22-113 2.29e-04

PWWP domain found in the bromodomain and PHD finger-containing (BRPF) protein family; The BRPF family of proteins includes BRPF1, BRD1/BRPF2, and BRPF3. They are scaffold proteins that form monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complexes with other regulatory subunits, such as inhibitor of growth 5 (ING5) and Esa1-associated factor 6 ortholog (EAF6). BRPF proteins have multiple domains, including a plant homeodomain (PHD) zinc finger followed by a non-canonical extended PHD (ePHD) finger, C2HC5HC2H, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. The PHD finger binds to lysine 4 of histone H3 (K4H3), the bromodomain interacts with acetylated lysines on N-terminal tails of histones and other proteins, and the PWWP domain shows histone-binding and chromatin association properties.


Pssm-ID: 438964  Cd Length: 106  Bit Score: 41.87  E-value: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223   22 WKVGDLVLAKVKGFPAWPATVSEP----------------EKWGYSADwKKVLVYFFGTQQI-AFCNPADVEAF--TEEK 82
Cdd:cd05839     1 LEPGDLVWAKCRGYPWYPAEIVDPkdpkegngvpipvppdRVLKKSNE-KLYLVLFFDAKRTwGWLPRNKLRPLgvDEEL 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 802793223   83 KQSLLVKRQGKgadfvRAVQEIIDSYEKSKK 113
Cdd:cd05839    80 DKLKLSEAKKS-----KRRKEVRKAYERACK 105
CID_SCAF8_like cd16983
CID (CTD-Interacting Domain) of SR-related and CTD-associated factor 8 and similar proteins; ...
 898-1022 1.85e-03

CID (CTD-Interacting Domain) of SR-related and CTD-associated factor 8 and similar proteins; This subfamily includes SR-related and CTD-associated factors 8 (SCAF8) and 4 (SCAF4), and similar proteins. SCAF4 is also called Splicing factor arginine serine rich 15 (SFRS15). Members may play roles in mRNA processing. Both SCAF4 and SCAF8 contains a CTD-interacting domain (CID) at the amino terminus and a Ser/Arg-rich domain followed by an RNA recognition motif. CID binds tightly to the carboxy-terminal domain (CTD) of RNA polymerase (Pol) II (RNAP II). During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices.


Pssm-ID: 340780  Cd Length: 131  Bit Score: 39.90  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223  898 SSFEGTLGSLTRTKESIGRA-----TRIAIDCAKFgiSNKVVEILARHLESESSLHRrVDLFFLVDSITQCSRGLKGDVG 972
Cdd:cd16983     1 EEFNKELSSLLDSKPPVSKSkinaiTKLAIKAIKF--YKHVVQSVEKFIQKCKPEYK-LPGLYVIDSIIRQSRHQYGKEK 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 802793223  973 GIYpsaiqavLPRL---LSAAAPPGSFA-QENRRQCLKVLRLWLERRILPESVI 1022
Cdd:cd16983    78 DVY-------APRFaknLSKTFLNLLKCpEKDKPKVKRVLNLWQKNGVFPKEII 124
PWWP_DNMT3 cd05835
PWWP domain found in the DNA (cytosine-5)-methyltransferase 3 (DNMT3) family; The DNMT3 family ...
 23-105 1.97e-03

PWWP domain found in the DNA (cytosine-5)-methyltransferase 3 (DNMT3) family; The DNMT3 family includes DNMT3A and DNMT3B, which are required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNMT3A, also called DNA methyltransferase HsaIIIA, DNA MTase HsaIIIA, or M.HsaIIIA, modifies DNA in a non-processive manner and also methylates non-CpG sites. It may preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. DNMT3A is recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. DNMT3B, also called DNA methyltransferase HsaIIIB, DNA MTase HsaIIIB, or M.HsaIIIB, may preferentially methylate nucleosomal DNA within the nucleosome core region. DNMT3B may function as a transcriptional co-repressor by associating with CBX4 and independently of DNA methylation. Members of this family contains a PWWP domain that is responsible for establishing DNA methylation patterns during embryogenesis and gametogenesis. In tumorigenesis, DNA methylation by DNMT3B is known to play a role in the inactivation of tumor suppressor genes. In addition, a point mutation in the PWWP domain of DNMT3B has been identified in patients with ICF (immunodeficiency, centromeric instability, and facial anomalie) syndrome , a rare autosomal recessive disorder characterized by hypomethylation of classical satellite DNA.


Pssm-ID: 438960 [Multi-domain]  Cd Length: 89  Bit Score: 38.78  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802793223   23 KVGDLVLAKVKGFPAWPATVSEPEKWGYS-ADWKKVLVYFFGTQQIAFCNPADVEAFTEEKKQslLVKRQGKGADFVRAV 101
Cdd:cd05835     1 KIGDLVWAKLKGSPWWPGIVVSHKDCGQKpPAEGSVWVFWFGDHKVSEVPLDKILPFAEFFNK--FYISKNSSKLYKKAV 78


                  ....
gi 802793223  102 QEII 105
Cdd:cd05835    79 YEAL 82
PWWP_BS69-like cd05841
PWWP domain found in protein BS69, protein kinase C-binding protein 1 (PRKCBP1) and similar ...
 27-103 3.61e-03

PWWP domain found in protein BS69, protein kinase C-binding protein 1 (PRKCBP1) and similar proteins; Protein BS69, also called zinc finger MYND domain-containing protein 11 (ZMYND11 or ZMY11), is a ubiquitously expressed nuclear protein acting as a transcriptional co-repressor in association with various transcription factors. It was originally identified as an adenovirus 5 E1A-binding protein that inhibits E1A transactivation, as well as c-Myb transcription. BS69 is a multi-domain protein, containing bromo, plant homeodomain (PHD), proline-tryptophan-tryptophan-proline (PWWP), and MYeloid translocation protein 8, Nervy and DEAF-1 (MYND) domains. The specific role of the PWWP domain within BS69 is not clearly identified, but BS69 functions in chromatin remodeling, consistent with other PWWP-containing proteins. PRKCBP1, also called cutaneous T-cell lymphoma-associated antigen se14-3 (CTCL-associated antigen se14-3), Rack7, or zinc finger MYND domain-containing protein 8 (ZMYND8), is a novel receptor for activated C-kinase (RACK)-like protein that may play an important role in the activation and regulation of PKC-beta I, and the PKC signaling cascade. It also has been identified as a formin homology-2-domain containing protein 1 (FHOD1)-binding protein that may be involved in FHOD1-regulated actin polymerization and transcription. Moreover, PRKCBP1 may function as a REST co-repressor 2 (RCOR2) interacting factor. They form a RCOR2/ZMYND8 complex which might be involved in the regulation of neural differentiation. PRKCBP1 contains a PHD finger, a bromodomain, and a PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438966  Cd Length: 89  Bit Score: 38.15  E-value: 3.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 802793223   27 LVLAKVKGFPAWPATVSEPEKwgysadwKKVLVYFFGTQQIAFCNPADVEAFTEEKKQSLLVKRQGK-GADFVRAVQE 103
Cdd:cd05841     9 LVWVKLDGFPFWPAKVMGTKD-------GQVDVRFFGDYDRAWLPSKNVTLHTREIVSTLPDSSESKdKRTLKKAIKE 79
 
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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