NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2738407852|ref|WP_348330999|]
View 

GNAT family N-acetyltransferase [Parvibaculum sp.]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11441181)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

CATH:  3.40.630.30
EC:  2.3.-.-
Gene Ontology:  GO:0016746|GO:0008080
PubMed:  27367672|26818562|15581578|10940244
SCOP:  3000403

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
46-158 1.88e-14

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 66.56  E-value: 1.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738407852  46 DAQREETVWSDALGRG-IAWMAEQAGVPVGFGHMEG----------AEVTtLYIRKEDHGQGVGAALLTHLFDEISCLGR 114
Cdd:COG1247    36 SEEEREAWFAAILAPGrPVLVAEEDGEVVGFASLGPfrprpayrgtAEES-IYVDPDARGRGIGRALLEALIERARARGY 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2738407852 115 REAFLWVLEKNAKARGFYERMGGRLVARRPVGFARHPEIMEVRY 158
Cdd:COG1247   115 RRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVL 158
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
46-158 1.88e-14

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 66.56  E-value: 1.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738407852  46 DAQREETVWSDALGRG-IAWMAEQAGVPVGFGHMEG----------AEVTtLYIRKEDHGQGVGAALLTHLFDEISCLGR 114
Cdd:COG1247    36 SEEEREAWFAAILAPGrPVLVAEEDGEVVGFASLGPfrprpayrgtAEES-IYVDPDARGRGIGRALLEALIERARARGY 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2738407852 115 REAFLWVLEKNAKARGFYERMGGRLVARRPVGFARHPEIMEVRY 158
Cdd:COG1247   115 RRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVL 158
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 65-144 1.54e-11

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 58.49  E-value: 1.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738407852  65 MAEQAGVPVGFGHME----GAEVTTLYIRKEDHGQGVGAALLTHLFDEISCLGRREAFLWVLEKNAKARGFYERMGGRLV 140
Cdd:TIGR01575  35 LARIGGKVVGYAGVQivldEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEI 114


                  ....
gi 2738407852 141 ARRP 144
Cdd:TIGR01575 115 AIRR 118
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 29-136 1.57e-10

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: 55.22  E-value: 1.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738407852  29 WREAYPGLLPQPLLDKLDAQREETVWSDALGRGIAWMAEQAGVPVGFG-------HMEGAEVTTLYIRKEDHGQGVGAAL 101
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFAslsiiddEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2738407852 102 LTHLFDEISCLGRREAFLWVLEKNAKARGFYERMG 136
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
PRK10514 PRK10514
putative acetyltransferase; Provisional
 72-145 2.42e-07

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 47.30  E-value: 2.42e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2738407852  72 PVGF-----GHMEGaevttLYIRKEDHGQGVGAALLTHLFDEISCLGRReaflwVLEKNAKARGFYERMGGRLVARRPV 145
Cdd:PRK10514   61 PVGFmllsgGHMEA-----LFVDPDVRGCGVGRMLVEHALSLHPELTTD-----VNEQNEQAVGFYKKMGFKVTGRSEV 129
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 64-120 7.73e-05

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: 38.80  E-value: 7.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2738407852  64 WMAEQAGVPVGFGHM-------EGAEVTTLYIRKEDHGQGVGAALLTHLFDEISCLGRREAFLW 120
Cdd:cd04301     2 LVAEDDGEIVGFASLspdgsggDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
46-158 1.88e-14

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 66.56  E-value: 1.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738407852  46 DAQREETVWSDALGRG-IAWMAEQAGVPVGFGHMEG----------AEVTtLYIRKEDHGQGVGAALLTHLFDEISCLGR 114
Cdd:COG1247    36 SEEEREAWFAAILAPGrPVLVAEEDGEVVGFASLGPfrprpayrgtAEES-IYVDPDARGRGIGRALLEALIERARARGY 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2738407852 115 REAFLWVLEKNAKARGFYERMGGRLVARRPVGFARHPEIMEVRY 158
Cdd:COG1247   115 RRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVL 158
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 81-155 9.23e-13

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 60.44  E-value: 9.23e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2738407852  81 AEVTTLYIRKEDHGQGVGAALLTHLFDEISCLGRREAFLWVLEKNAKARGFYERMGGRLVARRPVGFARHPEIME 155
Cdd:COG0456    14 AEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDALVME 88
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 65-144 1.54e-11

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 58.49  E-value: 1.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738407852  65 MAEQAGVPVGFGHME----GAEVTTLYIRKEDHGQGVGAALLTHLFDEISCLGRREAFLWVLEKNAKARGFYERMGGRLV 140
Cdd:TIGR01575  35 LARIGGKVVGYAGVQivldEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEI 114


                  ....
gi 2738407852 141 ARRP 144
Cdd:TIGR01575 115 AIRR 118
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 29-136 1.57e-10

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: 55.22  E-value: 1.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738407852  29 WREAYPGLLPQPLLDKLDAQREETVWSDALGRGIAWMAEQAGVPVGFG-------HMEGAEVTTLYIRKEDHGQGVGAAL 101
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFAslsiiddEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2738407852 102 LTHLFDEISCLGRREAFLWVLEKNAKARGFYERMG 136
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 64-163 2.92e-10

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 55.00  E-value: 2.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738407852  64 WMAEQAGVPVGFGHMEG-----AEVTTLYIRKEDHGQGVGAALLTHLFDEISCLGRREAFLWVlekNAKARGFYERMGGR 138
Cdd:COG1246    31 WVAEEDGEIVGCAALHPldedlAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKLGFE 107

                          90       100
                  ....*....|....*....|....*
gi 2738407852 139 LVARRPVGFARHPEIMEVRYDFMLD 163
Cdd:COG1246   108 EIDKEDLPYAKVWQRDSVVMEKDLE 132
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 41-149 9.54e-10

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 53.52  E-value: 9.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738407852  41 LLDKLDAQREETVWSDALGRGIAwmAEQAGVPVGFGHM-----EGAEVTTLYIRKEDHGQGVGAALLTHLFDEISCLGRR 115
Cdd:COG0454    16 LIEALDAELKAMEGSLAGAEFIA--VDDKGEPIGFAGLrrlddKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCT 93

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2738407852 116 EAFLWVLEKNAKARGFYERMG----GRLVARRPVGFAR 149
Cdd:COG0454    94 ALELDTLDGNPAAIRFYERLGfkeiERYVAYVGGEFEK 131
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 60-136 1.62e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 49.38  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738407852  60 RGIAWMAEQAGVPVGFGHMEGAEVTT------LYIRKEDHGQGVGAALLTHLfdeISCLGRREAFLWVLEKNAKARGFYE 133
Cdd:pfam13508   2 GGRFFVAEDDGKIVGFAALLPLDDEGalaelrLAVHPEYRGQGIGRALLEAA---EAAAKEGGIKLLELETTNRAAAFYE 78


                  ...
gi 2738407852 134 RMG 136
Cdd:pfam13508  79 KLG 81
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
16-155 1.17e-07

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 48.16  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738407852  16 EDEETLARLkvvcWREAYPGLLPQPLLDKLDAQREetvwsdalgRGIAWMAEQAGVPVGF---------GHMEGAEVTTL 86
Cdd:COG3153     7 EDAEAIAAL----LRAAFGPGREAELVDRLREDPA---------AGLSLVAEDDGEIVGHvalspvdidGEGPALLLGPL 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2738407852  87 YIRKEDHGQGVGAALLTHLFDEISCLGRREAFLWVlekNAKARGFYERMGGRLVARRPVGFARHPEIME 155
Cdd:COG3153    74 AVDPEYRGQGIGRALMRAALEAARERGARAVVLLG---DPSLLPFYERFGFRPAGELGLTLGPDEVFLA 139
PRK10514 PRK10514
putative acetyltransferase; Provisional
 72-145 2.42e-07

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 47.30  E-value: 2.42e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2738407852  72 PVGF-----GHMEGaevttLYIRKEDHGQGVGAALLTHLFDEISCLGRReaflwVLEKNAKARGFYERMGGRLVARRPV 145
Cdd:PRK10514   61 PVGFmllsgGHMEA-----LFVDPDVRGCGVGRMLVEHALSLHPELTTD-----VNEQNEQAVGFYKKMGFKVTGRSEV 129
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
81-142 7.92e-07

Predicted acetyltransferase, GNAT family [General function prediction only];


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 44.90  E-value: 7.92e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2738407852  81 AEVTTLYIRKEDHGQGVGAALLTHLFDEISCLGRREAFLWVLEKNAKARGFYERMGGRLVAR 142
Cdd:COG3393    16 AEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGE 77
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 64-136 5.02e-06

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


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 43.41  E-value: 5.02e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2738407852  64 WMAEQAGVPVGFGHM-EGAEVTTLYIRKEDHGQGVGAALLTHLFDEISclgRREAFLWVLEKNA--KARGFYERMG 136
Cdd:pfam13673  34 FVAFEGGQIVGVIALrDRGHISLLFVDPDYQGQGIGKALLEAVEDYAE---KDGIKLSELTVNAspYAVPFYEKLG 106
PRK10562 PRK10562
putative acetyltransferase; Provisional
 58-142 2.86e-05

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 41.59  E-value: 2.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738407852  58 LGRGIAWMAEQAGVPVGF-GHMEGAEVTTLYIRKEDHGQGVGAALLTHL---FDEISclgrreafLWVLEKNAKARGFYE 133
Cdd:PRK10562   45 LPAAQTWVWEEDGKLLGFvSVLEGRFVGALFVAPKAVRRGIGKALMQHVqqrYPHLS--------LEVYQKNQRAVNFYH 116


                  ....*....
gi 2738407852 134 RMGGRLVAR 142
Cdd:PRK10562  117 AQGFRIVDS 125
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 64-120 7.73e-05

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: 38.80  E-value: 7.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2738407852  64 WMAEQAGVPVGFGHM-------EGAEVTTLYIRKEDHGQGVGAALLTHLFDEISCLGRREAFLW 120
Cdd:cd04301     2 LVAEDDGEIVGFASLspdgsggDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PRK09831 PRK09831
GNAT family N-acetyltransferase;
47-145 4.74e-04

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 38.40  E-value: 4.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738407852  47 AQREETVWSDALGRGIAWMAEQAGVPVGFGHMEGAEVTTLYIRKEDHGQGVGAALLTHLFDEISCLgrreaflwVLEKNA 126
Cdd:PRK09831   39 AQIDESRWKEKLAKSQVRVAVINAQPVGFITCIEHYIDMLFVDPEYTRRGVASALLKPLIKSESEL--------TVDASI 110

                          90
                  ....*....|....*....
gi 2738407852 127 KARGFYERMGGRLVARRPV 145
Cdd:PRK09831  111 TAKPFFERYGFQTVKQQRV 129
PRK07757 PRK07757
N-acetyltransferase;
64-142 7.17e-04

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 37.87  E-value: 7.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738407852  64 WMAEQAGVPVGFG--HMEG---AEVTTLYIRKEDHGQGVGAALLTHLFDEISCLGRREAFLWVLEknakaRGFYERMGGR 138
Cdd:PRK07757   44 YVAEEEGEIVGCCalHILWedlAEIRSLAVSEDYRGQGIGRMLVEACLEEARELGVKRVFALTYQ-----PEFFEKLGFR 118


                  ....
gi 2738407852 139 LVAR 142
Cdd:PRK07757  119 EVDK 122
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 94-143 1.05e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 37.22  E-value: 1.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2738407852  94 GQGVGAALLTHLFDEIscLGRREAFLW--VLEKNAKARGFYERMGGRLVARR 143
Cdd:PRK09491   77 RQGLGRALLEHLIDEL--EKRGVATLWleVRASNAAAIALYESLGFNEVTIR 126
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 87-144 3.74e-03

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 36.13  E-value: 3.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2738407852  87 YIRKEDHGQGVG----AALLTHLFDEiscLGRREAFLWVLEKNAKARGFYERMGGRLVARRP 144
Cdd:COG1670    94 WLAPAYWGKGYAtealRALLDYAFEE---LGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLR 152
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 57-139 3.75e-03

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 34.61  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738407852  57 ALGRGIAWMAeqagvpvgfgHMEGAEVTTLYIRKEDHGQGVGAALLTHLFDEISCLGRrEAFLWVLEKNAKARGFYERMG 136
Cdd:pfam08445   8 DTGELAAWCL----------RLPGGELGALQTLPEHRRRGLGSRLVAALARGIAERGI-TPFAVVVAGNTPSRRLYEKLG 76


                  ...
gi 2738407852 137 GRL 139
Cdd:pfam08445  77 FRK 79
PRK03624 PRK03624
putative acetyltransferase; Provisional
 94-142 3.81e-03

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 35.67  E-value: 3.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2738407852  94 GQGVGAALLTHLFDEISCLGRREAFLWVLEKNAKARGFYERMGGRLVAR 142
Cdd:PRK03624   82 GRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQDR 130
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH