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Conserved domains on  [gi|2049092012|gb|QWF13620|]
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GNAT family N-acetyltransferase (plasmid) [Ralstonia solanacearum]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10003213)

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

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List of domain hits

 Name Accession Description Interval E-value
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 7-129 4.18e-22

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: 85.43  E-value: 4.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049092012   7 VQLRQASRADCNEVAALLRrcglpADDIHDIIDAFQIALEKGRVIGCAAMEQGGKSIV-VRSVAVDPVCRDRGIASRLIE 85
Cdd:COG1246     1 MTIRPATPDDVPAILELIR-----PYALEEEIGEFWVAEEDGEIVGCAALHPLDEDLAeLRSLAVHPDYRGRGIGRRLLE 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2049092012  86 TLLLRAHGAGAREAYLLSTS-APSYFARWGFSLFPADKAPAEVRA 129
Cdd:COG1246    76 ALLAEARELGLKRLFLLTTSaAIHFYEKLGFEEIDKEDLPYAKVW 120
 
Name Accession Description Interval E-value
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 7-129 4.18e-22

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: 85.43  E-value: 4.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049092012   7 VQLRQASRADCNEVAALLRrcglpADDIHDIIDAFQIALEKGRVIGCAAMEQGGKSIV-VRSVAVDPVCRDRGIASRLIE 85
Cdd:COG1246     1 MTIRPATPDDVPAILELIR-----PYALEEEIGEFWVAEEDGEIVGCAALHPLDEDLAeLRSLAVHPDYRGRGIGRRLLE 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2049092012  86 TLLLRAHGAGAREAYLLSTS-APSYFARWGFSLFPADKAPAEVRA 129
Cdd:COG1246    76 ALLAEARELGLKRLFLLTTSaAIHFYEKLGFEEIDKEDLPYAKVW 120
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 43-115 8.68e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 49.76  E-value: 8.68e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2049092012  43 IALEKGRVIGCAAM--EQGGKSIVVRSVAVDPVCRDRGIASRLIETLLLRAHGAGAREAYLLST-SAPSYFARWGF 115
Cdd:pfam13508   7 VAEDDGKIVGFAALlpLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTnRAAAFYEKLGF 82
PRK07757 PRK07757
N-acetyltransferase;
6-124 1.08e-08

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 50.96  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049092012   6 DVQLRQASRADCNEVAALLRRC---GL----PADDIHDIIDAFQIALEKGRVIGCAAMeqggkSIV------VRSVAVDP 72
Cdd:PRK07757    1 MMEIRKARLSDVKAIHALINVYakkGLmlprSLDELYENIRDFYVAEEEGEIVGCCAL-----HILwedlaeIRSLAVSE 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2049092012  73 VCRDRGIASRLIETLLLRAHGAGAREAYLLsTSAPSYFARWGFSLFPADKAP 124
Cdd:PRK07757   76 DYRGQGIGRMLVEACLEEARELGVKRVFAL-TYQPEFFEKLGFREVDKEALP 126
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 43-101 1.17e-07

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: 46.11  E-value: 1.17e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2049092012  43 IALEKGRVIGCAAM---EQGGKSIVVRSVAVDPVCRDRGIASRLIETLLLRAHGAGAREAYL 101
Cdd:cd04301     3 VAEDDGEIVGFASLspdGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 41-101 1.23e-06

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: 45.01  E-value: 1.23e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2049092012  41 FQIALEKGRVIGCAAMEQGGKSIVVRSVAVDPVCRDRGIASRLIETLLLRAHGAGAREAYL 101
Cdd:TIGR01575  33 YLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFL 93
 
Name Accession Description Interval E-value
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 7-129 4.18e-22

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: 85.43  E-value: 4.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049092012   7 VQLRQASRADCNEVAALLRrcglpADDIHDIIDAFQIALEKGRVIGCAAMEQGGKSIV-VRSVAVDPVCRDRGIASRLIE 85
Cdd:COG1246     1 MTIRPATPDDVPAILELIR-----PYALEEEIGEFWVAEEDGEIVGCAALHPLDEDLAeLRSLAVHPDYRGRGIGRRLLE 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2049092012  86 TLLLRAHGAGAREAYLLSTS-APSYFARWGFSLFPADKAPAEVRA 129
Cdd:COG1246    76 ALLAEARELGLKRLFLLTTSaAIHFYEKLGFEEIDKEDLPYAKVW 120
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
9-115 2.38e-13

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 62.80  E-value: 2.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049092012   9 LRQASRADCNEVAALLRRCgLPADDIHDIIDAFQ---------IALEKGRVIGCAAM-----EQGGKSIVVRSVAVDPVC 74
Cdd:COG3153     1 IRPATPEDAEAIAALLRAA-FGPGREAELVDRLRedpaaglslVAEDDGEIVGHVALspvdiDGEGPALLLGPLAVDPEY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2049092012  75 RDRGIASRLIETLLLRAHGAGAREAYLLST-SAPSYFARWGF 115
Cdd:COG3153    80 RGQGIGRALMRAALEAARERGARAVVLLGDpSLLPFYERFGF 121
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 43-115 8.68e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 49.76  E-value: 8.68e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2049092012  43 IALEKGRVIGCAAM--EQGGKSIVVRSVAVDPVCRDRGIASRLIETLLLRAHGAGAREAYLLST-SAPSYFARWGF 115
Cdd:pfam13508   7 VAEDDGKIVGFAALlpLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTnRAAAFYEKLGF 82
PRK07757 PRK07757
N-acetyltransferase;
6-124 1.08e-08

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 50.96  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049092012   6 DVQLRQASRADCNEVAALLRRC---GL----PADDIHDIIDAFQIALEKGRVIGCAAMeqggkSIV------VRSVAVDP 72
Cdd:PRK07757    1 MMEIRKARLSDVKAIHALINVYakkGLmlprSLDELYENIRDFYVAEEEGEIVGCCAL-----HILwedlaeIRSLAVSE 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2049092012  73 VCRDRGIASRLIETLLLRAHGAGAREAYLLsTSAPSYFARWGFSLFPADKAP 124
Cdd:PRK07757   76 DYRGQGIGRMLVEACLEEARELGVKRVFAL-TYQPEFFEKLGFREVDKEALP 126
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 43-101 1.17e-07

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: 46.11  E-value: 1.17e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2049092012  43 IALEKGRVIGCAAM---EQGGKSIVVRSVAVDPVCRDRGIASRLIETLLLRAHGAGAREAYL 101
Cdd:cd04301     3 VAEDDGEIVGFASLspdGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
PRK07922 PRK07922
amino-acid N-acetyltransferase;
41-129 1.68e-07

amino-acid N-acetyltransferase;


Pssm-ID: 236132 [Multi-domain]  Cd Length: 169  Bit Score: 47.99  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049092012  41 FQIA-LEKGRVIGCAAM----EQGGKsivVRSVAVDPVCRDRGIASRLIETLLLRAHGAGAREAYLLsTSAPSYFARWGF 115
Cdd:PRK07922   47 FWVAeHLDGEVVGCGALhvmwEDLAE---IRTVAVDPAARGRGVGHAIVERLLDVARELGLSRVFVL-TFEVEFFARHGF 122

                          90
                  ....*....|....
gi 2049092012 116 SLFPADKAPAEVRA 129
Cdd:PRK07922  123 VEIDGTPVTPEVYA 136
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 31-115 4.90e-07

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: 45.59  E-value: 4.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049092012  31 ADDIHDIIDAFQIALEKGRVIGCAAM---EQGGKSIVVRSVAVDPVCRDRGIASRLIETLL--LRAHGAGAREAYLLSTS 105
Cdd:pfam00583  25 EDWDEDASEGFFVAEEDGELVGFASLsiiDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLewARERGCERIFLEVAADN 104

                          90
                  ....*....|..
gi 2049092012 106 APS--YFARWGF 115
Cdd:pfam00583 105 LAAiaLYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
6-115 7.76e-07

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 46.14  E-value: 7.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049092012   6 DVQLRQASRADCNEVAALLRRC--------GLPADDIHDIIDAFQ----------IALEKGRVIGCAAMEQ-----GGKS 62
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNEAiaegtatfETEPPSEEEREAWFAailapgrpvlVAEEDGEVVGFASLGPfrprpAYRG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2049092012  63 IVVRSVAVDPVCRDRGIASRLIETLLLRAHGAGAREAYL--LSTSAPS--YFARWGF 115
Cdd:COG1247    81 TAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAvvLADNEASiaLYEKLGF 137
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 41-101 1.23e-06

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: 45.01  E-value: 1.23e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2049092012  41 FQIALEKGRVIGCAAMEQGGKSIVVRSVAVDPVCRDRGIASRLIETLLLRAHGAGAREAYL 101
Cdd:TIGR01575  33 YLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFL 93
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
43-115 1.43e-06

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 44.79  E-value: 1.43e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2049092012  43 IALEKGRVIGCAAM-EQGGKSIVVRSVAVDPVCRDRGIASRLIETLLLRAHGAGAREAYLLS-TSAPSYFARWGF 115
Cdd:COG2153    38 LAYDDGELVATARLlPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAqAHAVGFYEKLGF 112
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 9-109 1.44e-06

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 44.48  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049092012   9 LRQASRADCNEVAALLRRCgLPADDIHDIIDAFQIALEKGRVIGCaamEQGGK----------SIVVR----------SV 68
Cdd:pfam13527   1 IRPLTEDEFDEVLRLLEYA-FQDEDSPELREYFRPLLEEGRVLGA---FDDGElvstlalypfELNVPgktlpaagitGV 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2049092012  69 AVDPVCRDRGIASRLIETLLLRAHGAGAREAYLLSTSAPSY 109
Cdd:pfam13527  77 ATYPEYRGRGVMSRLLRRSLEEMRERGVPLSFLYPSSYPIY 117
PLN02825 PLN02825
amino-acid N-acetyltransferase
 1-129 1.46e-06

amino-acid N-acetyltransferase


Pssm-ID: 215441 [Multi-domain]  Cd Length: 515  Bit Score: 46.30  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049092012   1 MQITEDVQ-LRQASRAdCNEVAALLRRCglpADDIHDIIDAFQIALEKGRVIGCAAM-----EQGGKsivVRSVAVDPVC 74
Cdd:PLN02825  372 MARVEDLAgIRQIIRP-LEESGILVRRT---DEELLRALDSFVVVEREGSIIACAALfpffeEKCGE---VAAIAVSPEC 444

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2049092012  75 RDRGIASRLIETLLLRAHGAGAREAYLLSTSAPSYFARWGFSLFPADKAPAEVRA 129
Cdd:PLN02825  445 RGQGQGDKLLDYIEKKAASLGLEKLFLLTTRTADWFVRRGFSECSIESLPEARRK 499
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 36-101 1.15e-05

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 42.35  E-value: 1.15e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2049092012  36 DIIDAFQIALEKGRVIGCAAMEQ-GGKSIVVRSVAVDPVCRDRGIASRLIETLLLRAHGAGAREAYL 101
Cdd:COG0454    31 LAGAEFIAVDDKGEPIGFAGLRRlDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALEL 97
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 53-149 2.18e-05

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 40.79  E-value: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049092012  53 CAAMEQGGKSIVVRSVAVDPVCRDRGIASRLIETLLLRAHGAGAREAYLL----STSAPSYFARWGFslfpadkapaevR 128
Cdd:COG0456     4 LLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEvredNEAAIALYEKLGF------------E 71

                          90       100
                  ....*....|....*....|.
gi 2049092012 129 ASATFRNAERSSALCMRCDLR 149
Cdd:COG0456    72 EVGERPNYYGDDALVMEKELA 92
Eis COG4552
Predicted acetyltransferase [General function prediction only];
8-141 4.71e-05

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 41.81  E-value: 4.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049092012   8 QLRQASRADCNEVAALLRRC-GLPADDihDIIDAFQIALEKGRVIGCA------------AMEQ--GGKSIV---VRSVA 69
Cdd:COG4552     2 EIRPLTEDDLDAFARLLAYAfGPEPDD--EELEAYRPLLEPGRVLGVFddgelvgtlalyPFTLnvGGARVPmagITGVA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049092012  70 VDPVCRDRGIASRLIETLLLRAHGAGAREAYLLSTSaPSYFARWGFSL--------FPADKAPAEVRASATFRNAERSSA 141
Cdd:COG4552    80 VAPEHRRRGVARALLREALAELRERGQPLSALYPFE-PGFYRRFGYELagdrrrytIPPESLPLRPDAPGRVRRVDPDDA 158
PRK03624 PRK03624
putative acetyltransferase; Provisional
 5-93 8.43e-05

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 39.91  E-value: 8.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049092012   5 EDVQLRQASRADCNEVAALLRRCGL------PADDI-----HDIiDAFQIALEKGRVIGCAAMEQGGKSIVVRSVAVDPV 73
Cdd:PRK03624    1 DAMEIRVFRQADFEAVIALWERCDLtrpwndPEMDIerklnHDP-SLFLVAEVGGEVVGTVMGGYDGHRGWAYYLAVHPD 79

                          90       100
                  ....*....|....*....|..
gi 2049092012  74 CRDRGIASRLIETL--LLRAHG 93
Cdd:PRK03624   80 FRGRGIGRALVARLekKLIARG 101
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 29-115 5.56e-04

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: 37.64  E-value: 5.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049092012  29 LPADDIHDIIDA----FQIALEKGRVIGCAAMEQGGKsivVRSVAVDPVCRDRGIASRLIETLLLRAHGAGAREAYLLST 104
Cdd:pfam13673  17 ISPEALRERIDQgeyfFFVAFEGGQIVGVIALRDRGH---ISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVN 93

                          90
                  ....*....|....
gi 2049092012 105 SAPS---YFARWGF 115
Cdd:pfam13673  94 ASPYavpFYEKLGF 107
PRK12308 PRK12308
argininosuccinate lyase;
32-127 1.02e-03

argininosuccinate lyase;


Pssm-ID: 183425 [Multi-domain]  Cd Length: 614  Bit Score: 38.23  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049092012  32 DDIHDIiDAFQIALEKGRVIGCAAM---EQGGKSIvvRSVAVDPVCRDRGIASRLIETLLLRAHGAGAREAYLLsTSAPS 108
Cdd:PRK12308  497 ELVRDI-GSFAVAEHHGEVTGCASLyiyDSGLAEI--RSLGVEAGWQVQGQGSALVQYLVEKARQMAIKKVFVL-TRVPE 572

                          90
                  ....*....|....*....
gi 2049092012 109 YFARWGFSLFPADKAPAEV 127
Cdd:PRK12308  573 FFMKQGFSPTSKSLLPEKV 591
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
49-101 3.09e-03

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 34.88  E-value: 3.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2049092012  49 RVIGCAAME-QGGKSIVVRSVAVDPVCRDRGIASRLIETLLLRAHGAGAREAYL 101
Cdd:COG3393     1 ELVAMAGVRaESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFL 54
PRK05279 PRK05279
N-acetylglutamate synthase; Validated
 38-129 3.67e-03

N-acetylglutamate synthase; Validated


Pssm-ID: 235386 [Multi-domain]  Cd Length: 441  Bit Score: 36.28  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049092012  38 IDAFQIALEKGRVIGCAAM-----EQGGKsivVRSVAVDPVCRDRGIASRLIETLLLRAHGAGAREAYLLSTSAPSYFAR 112
Cdd:PRK05279  333 IDKFTVIERDGLIIGCAALypfpeEKMGE---MACLAVHPDYRGSGRGERLLKRIEQRARQLGLKRLFVLTTRTAHWFLE 409

                          90
                  ....*....|....*..
gi 2049092012 113 WGFSLFPADKAPAEVRA 129
Cdd:PRK05279  410 RGFVPVDVDDLPEAKRQ 426
 
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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