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Conserved domains on  [gi|1519313635|ref|NP_003633|]
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histone acetyltransferase type B catalytic subunit [Homo sapiens]

Protein Classification

histone acetyltransferase type B catalytic subunit( domain architecture ID 10564067)

histone acetyltransferase type B catalytic subunit is the active component of the histone acetylase B (HAT-B) complex that acetylates 'Lys-14' of histone H4 which is required for telomeric silencing

CATH:  1.10.10.390|3.40.630.30|3.90.360.10
EC:  2.3.1.48
Gene Ontology:  GO:0004402|GO:0042393|GO:0031509
PubMed:  17694075|33016232
SCOP:  4001800

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Hat1_N pfam10394
Histone acetyl transferase HAT1 N-terminus; This domain is the N-terminal half of the ...
 25-187 1.87e-62

Histone acetyl transferase HAT1 N-terminus; This domain is the N-terminal half of the structure of histone acetyl transferase HAT1. It is often found in association with the C-terminal part of the GNAT Acetyltransf_1 (pfam00583) domain. It seems to be motifs C and D of the structure. Histone acetyltransferases (HATs) catalyze the transfer of an acetyl group from acetyl-CoA to the lysine E-amino groups on the N-terminal tails of histones. HATs are involved in transcription since histones tend to be hyper-acetylated in actively transcribed regions of chromatin, whereas in transcriptionally silent regions histones are hypo-acetylated.


:

Pssm-ID: 463071  Cd Length: 158  Bit Score: 198.54  E-value: 1.87e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313635  25 YKCNTNTAIELKLVRFPEDLENDIRTFFPEYTHQLFGDDETAFGYKGLKILLYYIAGSLSTMFRVEYASKVDENFDCvEA 104
Cdd:pfam10394   1 WTSDANEALKISLVRPEEDVESDDTSFHPEFTYQIFGEEETIFGYKDLKINLYFSAGSLRPYLDISYSEKLDSVGDT-GA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313635 105 DDVEGKIRQIIPPGFCTNTNDFLS-LLEKEVDFKPFGTLLHTYsvlspTGGENFTFQIYKADMTCRGFREYHERLQTFLM 183
Cdd:pfam10394  80 DDVEKKLKEFLPEDLFTDKDEFLKaLEEKEKSFKPPGELIHSY-----TREGKSTFEIYKGSLADPAFRELHRRLQIFVL 154


                  ....
gi 1519313635 184 WFIE 187
Cdd:pfam10394 155 LFIE 158
 
Name Accession Description Interval E-value
Hat1_N pfam10394
Histone acetyl transferase HAT1 N-terminus; This domain is the N-terminal half of the ...
 25-187 1.87e-62

Histone acetyl transferase HAT1 N-terminus; This domain is the N-terminal half of the structure of histone acetyl transferase HAT1. It is often found in association with the C-terminal part of the GNAT Acetyltransf_1 (pfam00583) domain. It seems to be motifs C and D of the structure. Histone acetyltransferases (HATs) catalyze the transfer of an acetyl group from acetyl-CoA to the lysine E-amino groups on the N-terminal tails of histones. HATs are involved in transcription since histones tend to be hyper-acetylated in actively transcribed regions of chromatin, whereas in transcriptionally silent regions histones are hypo-acetylated.


Pssm-ID: 463071  Cd Length: 158  Bit Score: 198.54  E-value: 1.87e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313635  25 YKCNTNTAIELKLVRFPEDLENDIRTFFPEYTHQLFGDDETAFGYKGLKILLYYIAGSLSTMFRVEYASKVDENFDCvEA 104
Cdd:pfam10394   1 WTSDANEALKISLVRPEEDVESDDTSFHPEFTYQIFGEEETIFGYKDLKINLYFSAGSLRPYLDISYSEKLDSVGDT-GA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313635 105 DDVEGKIRQIIPPGFCTNTNDFLS-LLEKEVDFKPFGTLLHTYsvlspTGGENFTFQIYKADMTCRGFREYHERLQTFLM 183
Cdd:pfam10394  80 DDVEKKLKEFLPEDLFTDKDEFLKaLEEKEKSFKPPGELIHSY-----TREGKSTFEIYKGSLADPAFRELHRRLQIFVL 154


                  ....
gi 1519313635 184 WFIE 187
Cdd:pfam10394 155 LFIE 158
 
Name Accession Description Interval E-value
Hat1_N pfam10394
Histone acetyl transferase HAT1 N-terminus; This domain is the N-terminal half of the ...
 25-187 1.87e-62

Histone acetyl transferase HAT1 N-terminus; This domain is the N-terminal half of the structure of histone acetyl transferase HAT1. It is often found in association with the C-terminal part of the GNAT Acetyltransf_1 (pfam00583) domain. It seems to be motifs C and D of the structure. Histone acetyltransferases (HATs) catalyze the transfer of an acetyl group from acetyl-CoA to the lysine E-amino groups on the N-terminal tails of histones. HATs are involved in transcription since histones tend to be hyper-acetylated in actively transcribed regions of chromatin, whereas in transcriptionally silent regions histones are hypo-acetylated.


Pssm-ID: 463071  Cd Length: 158  Bit Score: 198.54  E-value: 1.87e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313635  25 YKCNTNTAIELKLVRFPEDLENDIRTFFPEYTHQLFGDDETAFGYKGLKILLYYIAGSLSTMFRVEYASKVDENFDCvEA 104
Cdd:pfam10394   1 WTSDANEALKISLVRPEEDVESDDTSFHPEFTYQIFGEEETIFGYKDLKINLYFSAGSLRPYLDISYSEKLDSVGDT-GA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313635 105 DDVEGKIRQIIPPGFCTNTNDFLS-LLEKEVDFKPFGTLLHTYsvlspTGGENFTFQIYKADMTCRGFREYHERLQTFLM 183
Cdd:pfam10394  80 DDVEKKLKEFLPEDLFTDKDEFLKaLEEKEKSFKPPGELIHSY-----TREGKSTFEIYKGSLADPAFRELHRRLQIFVL 154


                  ....
gi 1519313635 184 WFIE 187
Cdd:pfam10394 155 LFIE 158
 
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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