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Conserved domains on  [gi|4504313|ref|NP_003535.1|]
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histone H4 [Homo sapiens]

Protein Classification

H4 domain-containing protein (domain architecture ID 10050499)

H4 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
H4 cd00076
Histone H4, one of the four histones, along with H2A, H2B and H3, which forms the eukaryotic ...
18-101 3.80e-42

Histone H4, one of the four histones, along with H2A, H2B and H3, which forms the eukaryotic nucleosome core; along with H3, it plays a central role in nucleosome formation; histones bind to DNA and wrap the genetic material into "beads on a string" in which DNA (the string) is wrapped around small blobs of histones (the beads) at regular intervals; play a role in the inheritance of specialized chromosome structures and the control of gene activity; defects in the establishment of proper chromosome structure by histones may activate or silence genes aberrantly and thus lead to disease; the sequence of histone H4 has remained almost invariant in more than 2 billion years of evolution


:

Pssm-ID: 238031  Cd Length: 85  Bit Score: 135.32  E-value: 3.80e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504313   18 RHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRT 97
Cdd:cd00076   2 RHRKVLRDNIKGITKPAIRRLARRGGVKRISGGVYDEVRNVLKSYLEDVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRT 81

                ....
gi 4504313   98 LYGF 101
Cdd:cd00076  82 LYGY 85
PLN00035 PLN00035
histone H4; Provisional
1-103 4.71e-53

histone H4; Provisional


:

Pssm-ID: 177669 [Multi-domain]  Cd Length: 103  Bit Score: 163.46  E-value: 4.71e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504313     1 MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRK 80
Cdd:PLN00035   1 MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKIFLENVIRDAVTYTEHARRK 80
                         90       100
                 ....*....|....*....|...
gi 4504313    81 TVTAMDVVYALKRQGRTLYGFGG 103
Cdd:PLN00035  81 TVTAMDVVYALKRQGRTLYGFGG 103
 
Name Accession Description Interval E-value
H4 cd00076
Histone H4, one of the four histones, along with H2A, H2B and H3, which forms the eukaryotic ...
18-101 3.80e-42

Histone H4, one of the four histones, along with H2A, H2B and H3, which forms the eukaryotic nucleosome core; along with H3, it plays a central role in nucleosome formation; histones bind to DNA and wrap the genetic material into "beads on a string" in which DNA (the string) is wrapped around small blobs of histones (the beads) at regular intervals; play a role in the inheritance of specialized chromosome structures and the control of gene activity; defects in the establishment of proper chromosome structure by histones may activate or silence genes aberrantly and thus lead to disease; the sequence of histone H4 has remained almost invariant in more than 2 billion years of evolution


Pssm-ID: 238031  Cd Length: 85  Bit Score: 135.32  E-value: 3.80e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504313   18 RHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRT 97
Cdd:cd00076   2 RHRKVLRDNIKGITKPAIRRLARRGGVKRISGGVYDEVRNVLKSYLEDVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRT 81

                ....
gi 4504313   98 LYGF 101
Cdd:cd00076  82 LYGY 85
H4 smart00417
Histone H4;
18-90 4.88e-36

Histone H4;


Pssm-ID: 128694  Cd Length: 74  Bit Score: 119.18  E-value: 4.88e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4504313      18 RHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYA 90
Cdd:smart00417   2 RHKKVLRDNIQGITKPAIRRLARRGGVKRISGLIYDETRNVLKSFLENVVRDAVTYTEHARRKTVTAMDVVYA 74
HHT1 COG2036
Archaeal histone H3/H4 [Chromatin structure and dynamics];
18-101 4.02e-25

Archaeal histone H3/H4 [Chromatin structure and dynamics];


Pssm-ID: 224947  Cd Length: 91  Bit Score: 91.62  E-value: 4.02e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504313   18 RHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRT 97
Cdd:COG2036   8 EIRRYQRSTDLLLPKAPVRRILRKAGAERVSSSAIEELQEALEEYLEEIAEDAVELAEHAKRKTVKAEDIKLALKRLGRR 87

                ....
gi 4504313   98 LYGF 101
Cdd:COG2036  88 IYGE 91
PLN00163 PLN00163
histone H4; Provisional
1-59 3.43e-17

histone H4; Provisional


Pssm-ID: 165730  Cd Length: 59  Bit Score: 70.10  E-value: 3.43e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 4504313     1 MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVL 59
Cdd:PLN00163   1 MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRTVL 59
CENP-T_C pfam15511
Centromere kinetochore component CENP-T histone fold; CENP-T is a family of vertebral ...
32-95 2.22e-06

Centromere kinetochore component CENP-T histone fold; CENP-T is a family of vertebral kinetochore proteins that associates directly with CENP-W. The N-terminus of CENP-T proteins interacts directly with the Ndc80 complex in the outer kinetochore. Importantly, the CENP-T-W complex does not directly associate with CENP-A, but with histone H3 in the centromere region. CENP-T and -W form a hetero-tetramer with CENP-S and -X and bind to a ~100 bp region of nucleosome-free DNA forming a nucleosome-like structure. The DNA-CENP-T-W-S-X complex is likely to be associated with histone H3-containing nucleosomes rather than with CENP-nucleosomes. This domain is the C-terminal histone fold domain of CENP-T, which associates with chromatin.


Pssm-ID: 292149  Cd Length: 108  Bit Score: 41.25  E-value: 2.22e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4504313     32 KPAIRRLA----RRGGVK-RISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQG 95
Cdd:pfam15511  10 TAVVKRLAkrfsFYSGAKmKLSKEALAALEQASDWFFEQMGDDLEAYAKHAGRKTIDESDVILLMRRQR 78
PLN00035 PLN00035
histone H4; Provisional
1-103 4.71e-53

histone H4; Provisional


Pssm-ID: 177669 [Multi-domain]  Cd Length: 103  Bit Score: 163.46  E-value: 4.71e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504313     1 MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRK 80
Cdd:PLN00035   1 MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKIFLENVIRDAVTYTEHARRK 80
                         90       100
                 ....*....|....*....|...
gi 4504313    81 TVTAMDVVYALKRQGRTLYGFGG 103
Cdd:PLN00035  81 TVTAMDVVYALKRQGRTLYGFGG 103
 
Name Accession Description Interval E-value
H4 cd00076
Histone H4, one of the four histones, along with H2A, H2B and H3, which forms the eukaryotic ...
18-101 3.80e-42

Histone H4, one of the four histones, along with H2A, H2B and H3, which forms the eukaryotic nucleosome core; along with H3, it plays a central role in nucleosome formation; histones bind to DNA and wrap the genetic material into "beads on a string" in which DNA (the string) is wrapped around small blobs of histones (the beads) at regular intervals; play a role in the inheritance of specialized chromosome structures and the control of gene activity; defects in the establishment of proper chromosome structure by histones may activate or silence genes aberrantly and thus lead to disease; the sequence of histone H4 has remained almost invariant in more than 2 billion years of evolution


Pssm-ID: 238031  Cd Length: 85  Bit Score: 135.32  E-value: 3.80e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504313   18 RHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRT 97
Cdd:cd00076   2 RHRKVLRDNIKGITKPAIRRLARRGGVKRISGGVYDEVRNVLKSYLEDVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRT 81

                ....
gi 4504313   98 LYGF 101
Cdd:cd00076  82 LYGY 85
H4 smart00417
Histone H4;
18-90 4.88e-36

Histone H4;


Pssm-ID: 128694  Cd Length: 74  Bit Score: 119.18  E-value: 4.88e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4504313      18 RHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYA 90
Cdd:smart00417   2 RHKKVLRDNIQGITKPAIRRLARRGGVKRISGLIYDETRNVLKSFLENVVRDAVTYTEHARRKTVTAMDVVYA 74
HHT1 COG2036
Archaeal histone H3/H4 [Chromatin structure and dynamics];
18-101 4.02e-25

Archaeal histone H3/H4 [Chromatin structure and dynamics];


Pssm-ID: 224947  Cd Length: 91  Bit Score: 91.62  E-value: 4.02e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504313   18 RHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRT 97
Cdd:COG2036   8 EIRRYQRSTDLLLPKAPVRRILRKAGAERVSSSAIEELQEALEEYLEEIAEDAVELAEHAKRKTVKAEDIKLALKRLGRR 87

                ....
gi 4504313   98 LYGF 101
Cdd:COG2036  88 IYGE 91
PLN00163 PLN00163
histone H4; Provisional
1-59 3.43e-17

histone H4; Provisional


Pssm-ID: 165730  Cd Length: 59  Bit Score: 70.10  E-value: 3.43e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 4504313     1 MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVL 59
Cdd:PLN00163   1 MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRTVL 59
CENP-T_C pfam15511
Centromere kinetochore component CENP-T histone fold; CENP-T is a family of vertebral ...
32-95 2.22e-06

Centromere kinetochore component CENP-T histone fold; CENP-T is a family of vertebral kinetochore proteins that associates directly with CENP-W. The N-terminus of CENP-T proteins interacts directly with the Ndc80 complex in the outer kinetochore. Importantly, the CENP-T-W complex does not directly associate with CENP-A, but with histone H3 in the centromere region. CENP-T and -W form a hetero-tetramer with CENP-S and -X and bind to a ~100 bp region of nucleosome-free DNA forming a nucleosome-like structure. The DNA-CENP-T-W-S-X complex is likely to be associated with histone H3-containing nucleosomes rather than with CENP-nucleosomes. This domain is the C-terminal histone fold domain of CENP-T, which associates with chromatin.


Pssm-ID: 292149  Cd Length: 108  Bit Score: 41.25  E-value: 2.22e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4504313     32 KPAIRRLA----RRGGVK-RISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQG 95
Cdd:pfam15511  10 TAVVKRLAkrfsFYSGAKmKLSKEALAALEQASDWFFEQMGDDLEAYAKHAGRKTIDESDVILLMRRQR 78
TAF smart00803
TATA box binding protein associated factor; TAFs (TATA box binding protein associated factors) ...
35-92 9.86e-06

TATA box binding protein associated factor; TAFs (TATA box binding protein associated factors) are part of the transcription initiation factor TFIID multimeric protein complex. TFIID is composed of the TATA box binding protein (TBP) and a number of TAFs. The TAFs provide binding sites for many different transcriptional activators and co-activators that modulate transcription initiation by Pol II. TAF proteins adopt a histone-like fold.


Pssm-ID: 129039  Cd Length: 65  Bit Score: 38.76  E-value: 9.86e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 4504313      35 IRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALK 92
Cdd:smart00803   8 IKDVAESLGIGNLSDEAAKLLAEDVEYRIKEIVQEALKFMRHSKRTTLTTSDIDSALR 65
TAF6 cd08050
TATA Binding Protein (TBP) Associated Factor 6 (TAF6) is one of several TAFs that bind TBP and ...
63-102 5.30e-05

TATA Binding Protein (TBP) Associated Factor 6 (TAF6) is one of several TAFs that bind TBP and is involved in forming Transcription Factor IID (TFIID) complex; The TATA Binding Protein (TBP) Associated Factor 6 (TAF6) is one of several TAFs that bind TBP and are involved in forming Transcription Factor IID (TFIID) complex. TFIID is one of seven General Transcription Factors (GTFs) (TFIIA, TFIIB, TFIID, TFIIE, TFIIF, and TFIID) that are involved in accurate initiation of transcription by RNA polymerase II in eukaryotes. TFIID plays an important role in the recognition of promoter DNA and assembly of the pre-initiation complex. TFIID complex is composed of the TBP and at least 13 TAFs. TAFs are named after their electrophoretic mobility in polyacrylamide gels in different species. A new, unified nomenclature has been suggested for the pol II TAFs to show the relationship between TAF orthologs and paralogs. Several hypotheses are proposed for TAFs functions such as serving as activator-binding sites, core-promoter recognition or a role in essential catalytic activity. These TAFs, with the help of specific activators, are required only for expression of a subset of genes and are not universally involved for transcription as are GTFs. In yeast and human cells, TAFs have been found as components of other complexes besides TFIID. Several TAFs interact via histone-fold (HFD) motifs; the HFD is the interaction motif involved in heterodimerization of the core histones and their assembly into nucleosome octamers. The minimal HFD contains three alpha-helices linked by two loops and is found in core histones, TAFs and many other transcription factors. TFIID has a histone octamer-like substructure. TAF6 is a shared subunit of histone acetyltransferase complex SAGA and TFIID complexes. TAF6 domain interacts with TAF9 and makes a novel histone-like heterodimer that is structurally related to histones H4 and H3. TAF6 may also interact with the downstream core promoter element (DPE).


Pssm-ID: 173968 [Multi-domain]  Cd Length: 343  Bit Score: 39.23  E-value: 5.30e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 4504313   63 LENVIRDAVTYTEHAKRKTVTAMDVVYALK-RQGRTLYGFG 102
Cdd:cd08050  33 LREIIQEAAKFMRHSKRRKLTTSDVNHALRlRNVEPLYGFS 73
TFIID-31kDa pfam02291
Transcription initiation factor IID, 31kD subunit; This family represents the N-terminus of ...
52-103 1.15e-04

Transcription initiation factor IID, 31kD subunit; This family represents the N-terminus of the 31kD subunit (42kD in drosophila) of transcription initiation factor IID (TAFII31). TAFII31 binds to p53, and is an essential requirement for p53 mediated transcription activation.


Pssm-ID: 280456  Cd Length: 121  Bit Score: 36.70  E-value: 1.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 4504313     52 YEEtrGVLKVFLE-------NVIRDAVTYTEHAKRKTVTAMDVVYALkrQGRTLYGFGG 103
Cdd:pfam02291  23 YEP--RVPLQLLDfayryttSVLEDALVYAEHAGRKTIDLDDVRLAI--QSRLNYQFTG 77
TAF12 cd07981
TATA Binding Protein (TBP) Associated Factor 12 (TAF12) is one of several TAFs that bind TBP ...
62-94 9.06e-04

TATA Binding Protein (TBP) Associated Factor 12 (TAF12) is one of several TAFs that bind TBP and is involved in forming Transcription Factor IID (TFIID) complex; The TATA Binding Protein (TBP) Associated Factor 12 (TAF12) is one of several TAFs that bind TBP and are involved in forming the TFIID complex. TFIID is one of the seven General Transcription Factors (GTFs) (TFIIA, TFIIB, TFIID, TFIIE, TFIIF, and TFIID) that are involved in accurate initiation of transcription by RNA polymerase II in eukaryotes. TFIID plays an important role in the recognition of promoter DNA and assembly of the pre-initiation complex. TFIID complex is composed of the TBP and at least 13 TAFs. TAFs are named after their electrophoretic mobility in polyacrylamide gels in different species. A new, unified nomenclature has been suggested for the pol II TAFs to show the relationship between TAF orthologs and paralogs. Several hypotheses are proposed for TAFs function such as serving as activator-binding sites, core-promoter recognition or a role in essential catalytic activity. These TAFs, with the help of specific activators, are required only for expression of a subset of genes and are not universally involved for transcription as are GTFs. In yeast and human cells, TAFs have been found as components of other complexes besides TFIID. Several TAFs interact via histone-fold (HFD) motifs; the HFD is the interaction motif involved in heterodimerization of the core histones and their assembly into nucleosome octamers. The minimal HFD contains three alpha-helices linked by two loops and is found in core histones, TAFs and many other transcription factors. TFIID has a histone octamer-like substructure. TAF12 domain interacts with TAF4 and makes a novel histone-like heterodimer that binds DNA and has a core promoter function of a subset of genes.


Pssm-ID: 173964  Cd Length: 72  Bit Score: 33.73  E-value: 9.06e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 4504313   62 FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQ 94
Cdd:cd07981  35 FVDDVVEDACRLAKHRKSDTLEVKDVQLHLERN 67
TAF9 cd07979
TATA Binding Protein (TBP) Associated Factor 9 (TAF9) is one of several TAFs that bind TBP and ...
66-92 9.35e-04

TATA Binding Protein (TBP) Associated Factor 9 (TAF9) is one of several TAFs that bind TBP and is involved in forming Transcription Factor IID (TFIID) complex; The TATA Binding Protein (TBP) Associated Factor 9 (TAF9) is one of several TAFs that bind TBP and are involved in forming the TFIID complex. TFIID is one of seven General Transcription Factors (GTF) (TFIIA, TFIIB, TFIID, TFIIE, TFIIF, and TFIID) that are involved in accurate initiation of transcription by RNA polymerase II in eukaryotes. TFIID plays an important role in the recognition of promoter DNA and assembly of the pre-initiation complex. The TFIID complex is composed of the TBP and at least 13 TAFs. TAFs from various species were originally named by their predicted molecular weight or their electrophoretic mobility in polyacrylamide gels. A new, unified nomenclature for the pol II TAFs has been suggested to show the relationship between TAFs orthologs and paralogs. Human TAF9 has a paralogue gene (TAF9L) which has a redundant function. Several hypotheses are proposed for TAF function such as serving as activator-binding sites, in core-promoter recognition or a role in essential catalytic activity. It has been shown that TAF9 interacts directly with different transcription factors such as p53, herpes simplex virus activator vp16 and the basal transcription factor TFIIB. Each TAF, with the help of a specific activator, is required only for expression of subset of genes and are not universally involved for transcription as are GTFs. In yeast and human cells, TAFs have been found as components of other complexes besides TFIID. TAF9 is a component of TFIID in multiple organisms as well as different TBP-free TAF complexes containing the GCN5-type histone acetyltransferase. Several TAFs interact via histone-fold (HFD) motifs; HFD is the interaction motif involved in heterodimerization of the core histones and their assembly into nucleosome octamers. The minimal HFD contains three alpha-helices linked by two loops and is found in core histones, TAFS and many other transcription factors. TFIID has a histone octamer-like substructure. TFIID has a histone octamer-like substructure. TAF9 is a shared subunit of both, histone acetyltransferase complex (SAGA) and TFIID complexes. TAF9 domain interacts with TAF6 to form a novel histone-like heterodimer that is structurally related to the histone H3 and H4 oligomer.


Pssm-ID: 173963  Cd Length: 117  Bit Score: 34.51  E-value: 9.35e-04
                        10        20
                ....*....|....*....|....*..
gi 4504313   66 VIRDAVTYTEHAKRKTVTAMDVVYALK 92
Cdd:cd07979  38 VLDDAKVYSEHAGKANIDADDVKLAIQ 64
TAF pfam02969
TATA box binding protein associated factor (TAF); TAF proteins adopt a histone-like fold.
63-92 3.70e-03

TATA box binding protein associated factor (TAF); TAF proteins adopt a histone-like fold.


Pssm-ID: 281032  Cd Length: 66  Bit Score: 31.98  E-value: 3.70e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 4504313     63 LENVIRDAVTYTEHAKRKTVTAMDVVYALK 92
Cdd:pfam02969  37 LKEIVQDAAKFMRHSKRQKLTVADVDSALR 66
CENP-S pfam15630
Kinetochore component CENP-S; CENP-S is a family of vertebral and fungal kinetochore component ...
62-93 6.75e-03

Kinetochore component CENP-S; CENP-S is a family of vertebral and fungal kinetochore component proteins. CENP-S complexes with CENP-X to form a stable CENP-T-W-S-X heterotetramer.


Pssm-ID: 292263  Cd Length: 76  Bit Score: 31.37  E-value: 6.75e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 4504313     62 FLENVIRDAVTYTEHAKRKTVTAMDVVYALKR 93
Cdd:pfam15630  41 QLENLAKDLEAFAKHAKRSTITTDDVKLLARR 72
PLN00035 PLN00035
histone H4; Provisional
1-103 4.71e-53

histone H4; Provisional


Pssm-ID: 177669 [Multi-domain]  Cd Length: 103  Bit Score: 163.46  E-value: 4.71e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504313     1 MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRK 80
Cdd:PLN00035   1 MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKIFLENVIRDAVTYTEHARRK 80
                         90       100
                 ....*....|....*....|...
gi 4504313    81 TVTAMDVVYALKRQGRTLYGFGG 103
Cdd:PLN00035  81 TVTAMDVVYALKRQGRTLYGFGG 103
PTZ00015 PTZ00015
histone H4; Provisional
18-101 2.91e-46

histone H4; Provisional


Pssm-ID: 185397 [Multi-domain]  Cd Length: 102  Bit Score: 146.04  E-value: 2.91e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504313    18 RHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRT 97
Cdd:PTZ00015  19 RQKKVLRDNIRGITKGAIRRLARRGGVKRISGDIYEEVRGVLKAFLENVVRDSTAYTEYARRKTVTAMDVVYALKRQGRT 98

                 ....
gi 4504313    98 LYGF 101
Cdd:PTZ00015  99 LYGF 102
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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