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Conserved domains on  [gi|255546221|ref|XP_002514170|]
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histone acetyltransferase type B catalytic subunit [Ricinus communis]

Protein Classification

histone acetyltransferase type B catalytic subunit( domain architecture ID 10564069)

histone acetyltransferase type B (HAT-B) catalytic subunit (HAT1) which acetylates K5 and K12 of histone H4, and is involved in telomeric silencing and DNA double-strand break repair; similar to Cryptococcus neoformans HAT1

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 ...
 29-197 2.04e-36

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: 131.51  E-value: 2.04e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255546221   29 GIEANECITIYMVSSREQVGaSDSFCISPVDLNGFFDEAGKIYGYQGLKITIWISSLTFHAYADITYESTSD--GGKGIT 106
Cdd:pfam10394   2 TSDANEALKISLVRPEEDVE-SDDTSFHPEFTYQIFGEEETIFGYKDLKINLYFSAGSLRPYLDISYSEKLDsvGDTGAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255546221  107 DLKNALQRIFAETLVENKDDFLRSFSaESHLIRSIVstGEIFHHKASNGyigeshlgepTSDMKVFRMAIGNTGAGHLYS 186
Cdd:pfam10394  81 DVEKKLKEFLPEDLFTDKDEFLKALE-EKEKSFKPP--GELIHSYTREG----------KSTFEIYKGSLADPAFRELHR 147

                         170
                  ....*....|.
gi 255546221  187 RLIPLVLLLID 197
Cdd:pfam10394 148 RLQIFVLLFIE 158
MOZ_SAS super family cl38061
MOZ/SAS family; This region of these proteins has been suggested to be homologous to ...
 249-269 1.12e-04

MOZ/SAS family; This region of these proteins has been suggested to be homologous to acetyltransferases.


The actual alignment was detected with superfamily member pfam01853:

Pssm-ID: 460362 [Multi-domain]  Cd Length: 179  Bit Score: 42.80  E-value: 1.12e-04
                          10        20
                  ....*....|....*....|.
gi 255546221  249 LSQILVLPPYQHKGYGRQLVE 269
Cdd:pfam01853  80 LACILTLPPYQRKGYGKLLIE 100
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 224-269 9.93e-04

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


:

Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 37.26  E-value: 9.93e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 255546221 224 DIQHRLLGFTAVYRFYHYPDktRLRLSQILVLPPYQHKGYGRQLVE 269
Cdd:cd04301    5 EDDGEIVGFASLSPDGSGGD--TAYIGDLAVLPEYRGKGIGSALLE 48
 
Name Accession Description Interval E-value
Hat1_N pfam10394
Histone acetyl transferase HAT1 N-terminus; This domain is the N-terminal half of the ...
 29-197 2.04e-36

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: 131.51  E-value: 2.04e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255546221   29 GIEANECITIYMVSSREQVGaSDSFCISPVDLNGFFDEAGKIYGYQGLKITIWISSLTFHAYADITYESTSD--GGKGIT 106
Cdd:pfam10394   2 TSDANEALKISLVRPEEDVE-SDDTSFHPEFTYQIFGEEETIFGYKDLKINLYFSAGSLRPYLDISYSEKLDsvGDTGAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255546221  107 DLKNALQRIFAETLVENKDDFLRSFSaESHLIRSIVstGEIFHHKASNGyigeshlgepTSDMKVFRMAIGNTGAGHLYS 186
Cdd:pfam10394  81 DVEKKLKEFLPEDLFTDKDEFLKALE-EKEKSFKPP--GELIHSYTREG----------KSTFEIYKGSLADPAFRELHR 147

                         170
                  ....*....|.
gi 255546221  187 RLIPLVLLLID 197
Cdd:pfam10394 148 RLQIFVLLFIE 158
MOZ_SAS pfam01853
MOZ/SAS family; This region of these proteins has been suggested to be homologous to ...
 249-269 1.12e-04

MOZ/SAS family; This region of these proteins has been suggested to be homologous to acetyltransferases.


Pssm-ID: 460362 [Multi-domain]  Cd Length: 179  Bit Score: 42.80  E-value: 1.12e-04
                          10        20
                  ....*....|....*....|.
gi 255546221  249 LSQILVLPPYQHKGYGRQLVE 269
Cdd:pfam01853  80 LACILTLPPYQRKGYGKLLIE 100
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 224-269 9.93e-04

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 37.26  E-value: 9.93e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 255546221 224 DIQHRLLGFTAVYRFYHYPDktRLRLSQILVLPPYQHKGYGRQLVE 269
Cdd:cd04301    5 EDDGEIVGFASLSPDGSGGD--TAYIGDLAVLPEYRGKGIGSALLE 48
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
228-269 1.03e-03

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 39.30  E-value: 1.03e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 255546221 228 RLLGFTAVYRFYHYPDKTRLRLSQILVLPPYQHKGYGRQLVE 269
Cdd:COG3153   49 EIVGHVALSPVDIDGEGPALLLGPLAVDPEYRGQGIGRALMR 90
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 226-286 1.32e-03

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 37.82  E-value: 1.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255546221  226 QHRLLGFTAVYRFYHYPDKTRLRLSqilVLPPYQHKGYGRQLVEVVNKVAISEDVYDFTVE 286
Cdd:pfam13508  11 DGKIVGFAALLPLDDEGALAELRLA---VHPEYRGQGIGRALLEAAEAAAKEGGIKLLELE 68
PRK13688 PRK13688
N-acetyltransferase;
235-269 2.35e-03

N-acetyltransferase;


Pssm-ID: 237470  Cd Length: 156  Bit Score: 38.46  E-value: 2.35e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 255546221 235 VYRFYHYPDKTRLRLSQILVLPPYQHKGYGRQLVE 269
Cdd:PRK13688  68 VEEPYFEDTQDYLELWKLEVLPKYQNRGYGEMLVD 102
 
Name Accession Description Interval E-value
Hat1_N pfam10394
Histone acetyl transferase HAT1 N-terminus; This domain is the N-terminal half of the ...
 29-197 2.04e-36

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: 131.51  E-value: 2.04e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255546221   29 GIEANECITIYMVSSREQVGaSDSFCISPVDLNGFFDEAGKIYGYQGLKITIWISSLTFHAYADITYESTSD--GGKGIT 106
Cdd:pfam10394   2 TSDANEALKISLVRPEEDVE-SDDTSFHPEFTYQIFGEEETIFGYKDLKINLYFSAGSLRPYLDISYSEKLDsvGDTGAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255546221  107 DLKNALQRIFAETLVENKDDFLRSFSaESHLIRSIVstGEIFHHKASNGyigeshlgepTSDMKVFRMAIGNTGAGHLYS 186
Cdd:pfam10394  81 DVEKKLKEFLPEDLFTDKDEFLKALE-EKEKSFKPP--GELIHSYTREG----------KSTFEIYKGSLADPAFRELHR 147

                         170
                  ....*....|.
gi 255546221  187 RLIPLVLLLID 197
Cdd:pfam10394 148 RLQIFVLLFIE 158
MOZ_SAS pfam01853
MOZ/SAS family; This region of these proteins has been suggested to be homologous to ...
 249-269 1.12e-04

MOZ/SAS family; This region of these proteins has been suggested to be homologous to acetyltransferases.


Pssm-ID: 460362 [Multi-domain]  Cd Length: 179  Bit Score: 42.80  E-value: 1.12e-04
                          10        20
                  ....*....|....*....|.
gi 255546221  249 LSQILVLPPYQHKGYGRQLVE 269
Cdd:pfam01853  80 LACILTLPPYQRKGYGKLLIE 100
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 224-269 9.93e-04

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 37.26  E-value: 9.93e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 255546221 224 DIQHRLLGFTAVYRFYHYPDktRLRLSQILVLPPYQHKGYGRQLVE 269
Cdd:cd04301    5 EDDGEIVGFASLSPDGSGGD--TAYIGDLAVLPEYRGKGIGSALLE 48
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
228-269 1.03e-03

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 39.30  E-value: 1.03e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 255546221 228 RLLGFTAVYRFYHYPDKTRLRLSQILVLPPYQHKGYGRQLVE 269
Cdd:COG3153   49 EIVGHVALSPVDIDGEGPALLLGPLAVDPEYRGQGIGRALMR 90
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 226-286 1.32e-03

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 37.82  E-value: 1.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255546221  226 QHRLLGFTAVYRFYHYPDKTRLRLSqilVLPPYQHKGYGRQLVEVVNKVAISEDVYDFTVE 286
Cdd:pfam13508  11 DGKIVGFAALLPLDDEGALAELRLA---VHPEYRGQGIGRALLEAAEAAAKEGGIKLLELE 68
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 223-286 1.66e-03

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 38.50  E-value: 1.66e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255546221 223 GDIQHRLLGFtavYRFYHYPDKTrLRLSQILVLPPYQHKGYGRQLVEVVNKVAISEDVYDFTVE 286
Cdd:COG0454   39 VDDKGEPIGF---AGLRRLDDKV-LELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELD 98
PRK13688 PRK13688
N-acetyltransferase;
235-269 2.35e-03

N-acetyltransferase;


Pssm-ID: 237470  Cd Length: 156  Bit Score: 38.46  E-value: 2.35e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 255546221 235 VYRFYHYPDKTRLRLSQILVLPPYQHKGYGRQLVE 269
Cdd:PRK13688  68 VEEPYFEDTQDYLELWKLEVLPKYQNRGYGEMLVD 102
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 228-281 3.45e-03

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 37.50  E-value: 3.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 255546221  228 RLLGFTAVYRFYHYPDktRLRLSQILVLPPYQHKGYGRQLVEVVNKVAISEDVY 281
Cdd:pfam00583  43 ELVGFASLSIIDDEPP--VGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCE 94
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
203-269 4.53e-03

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 37.67  E-value: 4.53e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255546221 203 DVADPGWELFVLiheknDEQGDIqhrlLGFTAVYRFYHYPDKTRLRLSQILVLPPYQHKGYGRQLVE 269
Cdd:COG1247   46 AILAPGRPVLVA-----EEDGEV----VGFASLGPFRPRPAYRGTAEESIYVDPDARGRGIGRALLE 103
 
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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