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Conserved domains on  [gi|1052974457|emb|SCG95376|]
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Phosphinothricin N-acetyltransferase [uncultured Bacteroides 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

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List of domain hits

 Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-160 1.89e-63

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 191.75  E-value: 1.89e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457   1 MIRKVCKEDAPAITAIYNHYITHTTITFELEPVSEEEMWTRIQTISSQ-YPYFVYEVEGQIAGYCYVHGWKEKAAYNQSV 79
Cdd:COG1247     3 TIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPgRPVLVAEEDGEVVGFASLGPFRPRPAYRGTA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457  80 ETTIYLAPSSTGKGLGTELMQHLIEECRRCGLHALIACITEGNEASYALHEKLGFEKVSSFREVGRKFGKWLGIVDYELI 159
Cdd:COG1247    83 EESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQKR 162


                  .
gi 1052974457 160 L 160
Cdd:COG1247   163 L 163
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-160 1.89e-63

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 191.75  E-value: 1.89e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457   1 MIRKVCKEDAPAITAIYNHYITHTTITFELEPVSEEEMWTRIQTISSQ-YPYFVYEVEGQIAGYCYVHGWKEKAAYNQSV 79
Cdd:COG1247     3 TIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPgRPVLVAEEDGEVVGFASLGPFRPRPAYRGTA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457  80 ETTIYLAPSSTGKGLGTELMQHLIEECRRCGLHALIACITEGNEASYALHEKLGFEKVSSFREVGRKFGKWLGIVDYELI 159
Cdd:COG1247    83 EESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQKR 162


                  .
gi 1052974457 160 L 160
Cdd:COG1247   163 L 163
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 13-134 3.32e-18

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: 75.25  E-value: 3.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457  13 ITAIYNHYITHTTITFELEPVSEEEMWTRIQTissqYPYFVYEVEGQIAGY--CYVHGWKEKAAYnqsvETTIYLAPSST 90
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDAS----EGFFVAEEDGELVGFasLSIIDDEPPVGE----IEGLAVAPEYR 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1052974457  91 GKGLGTELMQHLIEECRRCGLHALIACITEGNEASYALHEKLGF 134
Cdd:pfam00583  73 GKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
PRK07757 PRK07757
N-acetyltransferase;
1-138 1.35e-09

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 53.66  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457   1 MIRKVCKEDAPAITAIYNHYITHTTITfelePVSEEEMWTRIQTissqypYFVYEVEGQIAGYCYVHGWKEKAAYNQSVe 80
Cdd:PRK07757    3 EIRKARLSDVKAIHALINVYAKKGLML----PRSLDELYENIRD------FYVAEEEGEIVGCCALHILWEDLAEIRSL- 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457  81 ttiYLAPSSTGKGLGTELMQHLIEECRRCGLHALIaCITegneasY--ALHEKLGFEKVS 138
Cdd:PRK07757   72 ---AVSEDYRGQGIGRMLVEACLEEARELGVKRVF-ALT------YqpEFFEKLGFREVD 121
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 51-115 1.15e-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: 46.50  E-value: 1.15e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1052974457  51 YFVYEVEGQIAGYCYVH--GWKEKAAYnqsVETtIYLAPSSTGKGLGTELMQHLIEECRRCGLHALI 115
Cdd:cd04301     1 FLVAEDDGEIVGFASLSpdGSGGDTAY---IGD-LAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 28-137 1.26e-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: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457  28 FELEPVSEEEMWTRIQTIS--SQYP--YFVYEVEGQIAGYCYVH-GWKEKAAYNqsvettIYLAPSSTGKGLGTELMQHL 102
Cdd:TIGR01575   6 LEIEAAAFAFPWTEAQFAEelANYHlcYLLARIGGKVVGYAGVQiVLDEAHILN------IAVKPEYQGQGIGRALLREL 79

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1052974457 103 IEECRRCGLHALIACITEGNEASYALHEKLGFEKV 137
Cdd:TIGR01575  80 IDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEI 114
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-160 1.89e-63

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 191.75  E-value: 1.89e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457   1 MIRKVCKEDAPAITAIYNHYITHTTITFELEPVSEEEMWTRIQTISSQ-YPYFVYEVEGQIAGYCYVHGWKEKAAYNQSV 79
Cdd:COG1247     3 TIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPgRPVLVAEEDGEVVGFASLGPFRPRPAYRGTA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457  80 ETTIYLAPSSTGKGLGTELMQHLIEECRRCGLHALIACITEGNEASYALHEKLGFEKVSSFREVGRKFGKWLGIVDYELI 159
Cdd:COG1247    83 EESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQKR 162


                  .
gi 1052974457 160 L 160
Cdd:COG1247   163 L 163
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 2-159 1.71e-24

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: 93.14  E-value: 1.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457   2 IRKVCKEDAPAITAIYNHyiTHTTITFELEPVSEEEMWTRIQTISSQY------PYFVYEVE-GQIAGYCYVHGWKEKaa 74
Cdd:COG1670    10 LRPLRPEDAEALAELLND--PEVARYLPGPPYSLEEARAWLERLLADWadggalPFAIEDKEdGELIGVVGLYDIDRA-- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457  75 yNQSVETTIYLAPSSTGKGLGTELMQHLIEEC-RRCGLHALIACITEGNEASYALHEKLGFEKVSSFREVGRKFGKWLGI 153
Cdd:COG1670    86 -NRSAEIGYWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDH 164


                  ....*.
gi 1052974457 154 VDYELI 159
Cdd:COG1670   165 VLYSLL 170
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 13-134 3.32e-18

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: 75.25  E-value: 3.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457  13 ITAIYNHYITHTTITFELEPVSEEEMWTRIQTissqYPYFVYEVEGQIAGY--CYVHGWKEKAAYnqsvETTIYLAPSST 90
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDAS----EGFFVAEEDGELVGFasLSIIDDEPPVGE----IEGLAVAPEYR 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1052974457  91 GKGLGTELMQHLIEECRRCGLHALIACITEGNEASYALHEKLGF 134
Cdd:pfam00583  73 GKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-138 1.41e-16

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: 71.56  E-value: 1.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457   1 MIRKVCKEDAPAITAIYNHYIthttitfelepvseeeMWTRIQTissqypYFVYEVEGQIAGYCYVHGWKEKAAYNQSVe 80
Cdd:COG1246     2 TIRPATPDDVPAILELIRPYA----------------LEEEIGE------FWVAEEDGEIVGCAALHPLDEDLAELRSL- 58

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1052974457  81 ttiYLAPSSTGKGLGTELMQHLIEECRRCGLHALIACITegnEASYALHEKLGFEKVS 138
Cdd:COG1246    59 ---AVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTT---SAAIHFYEKLGFEEID 110
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
2-150 7.11e-16

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 70.09  E-value: 7.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457   2 IRKVCKEDAPAITAIYNHYITHTTITFELEPVSEEEMWTRIQTISS--QYPYFVYEvEGQIAGYCYVHGWKekAAYNQSV 79
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVNPAFTQEYAHSSIEEFETFLAAYLSpgEIVFGVAE-SDRLIGYATLRQFD--YVKTHKA 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1052974457  80 ETTIYLAPSSTgKGLGTELMQHLIEECRRC-GLHALIACITEGNEASYALHEKLGFEKVSSFREVGRKFGKW 150
Cdd:pfam13420  78 ELSFYVVKNND-EGINRELINAIIQYARKNqNIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRW 148
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 2-135 8.84e-13

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 61.59  E-value: 8.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457   2 IRKVCKEDAPAITAIY-NHYITHTTITFelePVSEEEMWTRIQTISSQYPY---FVYEVE----GQI--AGYCYVHGWKE 71
Cdd:pfam13302   4 LRPLTEEDAEALFELLsDPEVMRYGVPW---PLTLEEAREWLARIWAADEAergYGWAIElkdtGFIgsIGLYDIDGEPE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052974457  72 KAaynqsvETTIYLAPSSTGKGLGTELMQHLIEEC-RRCGLHALIACITEGNEASYALHEKLGFE 135
Cdd:pfam13302  81 RA------ELGYWLGPDYWGKGYATEAVRALLEYAfEELGLPRLVARIDPENTASRRVLEKLGFK 139
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
2-141 2.75e-12

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 60.48  E-value: 2.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457   2 IRKVCKEDAPAITAIYNHyithttitfELEPVSEEEMWTRIQTISSQYPYFVYEVEGQIAGYcyVHGWKEKAAYNqsvET 81
Cdd:COG3153     1 IRPATPEDAEAIAALLRA---------AFGPGREAELVDRLREDPAAGLSLVAEDDGEIVGH--VALSPVDIDGE---GP 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052974457  82 TIYLA-----PSSTGKGLGTELMQHLIEECRRCGLHaliACITEGNEASYALHEKLGFEKVSSFR 141
Cdd:COG3153    67 ALLLGplavdPEYRGQGIGRALMRAALEAARERGAR---AVVLLGDPSLLPFYERFGFRPAGELG 128
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 82-142 1.23e-10

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 55.05  E-value: 1.23e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052974457  82 TIYLAPSSTGKGLGTELMQHLIEECRRCGLHALIACITEGNEASYALHEKLGFEKVSSFRE 142
Cdd:COG0456    18 DLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 33-144 1.26e-10

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: 55.74  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457  33 VSEEEMWTRIQtiSSQYPYFVYEVEGQIAGYCyvhgwkekAAYNQSVETTIYLAPSSTGKGLGTELMQHLIEECRRCGLH 112
Cdd:pfam13673  17 ISPEALRERID--QGEYFFFVAFEGGQIVGVI--------ALRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIK 86

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1052974457 113 ALiacITEGNEASYA--LHEKLGFEKVSSFREVG 144
Cdd:pfam13673  87 LS---ELTVNASPYAvpFYEKLGFRATGPEQEFN 117
PRK07757 PRK07757
N-acetyltransferase;
1-138 1.35e-09

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 53.66  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457   1 MIRKVCKEDAPAITAIYNHYITHTTITfelePVSEEEMWTRIQTissqypYFVYEVEGQIAGYCYVHGWKEKAAYNQSVe 80
Cdd:PRK07757    3 EIRKARLSDVKAIHALINVYAKKGLML----PRSLDELYENIRD------FYVAEEEGEIVGCCALHILWEDLAEIRSL- 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457  81 ttiYLAPSSTGKGLGTELMQHLIEECRRCGLHALIaCITegneasY--ALHEKLGFEKVS 138
Cdd:PRK07757   72 ---AVSEDYRGQGIGRMLVEACLEEARELGVKRVF-ALT------YqpEFFEKLGFREVD 121
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 28-138 1.02e-08

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 51.08  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457  28 FELEPVSEEEMWTRIQTISSQ---YPYFVYEVEGQIAGYcyvhgwkekaAYNQSV--ETT---IYLAPSSTGKGLGTELM 99
Cdd:PRK09491   16 YHIEQRAHAFPWSEKTFASNQgerYLNLKLTVNGQMAAF----------AITQVVldEATlfnIAVDPDYQRQGLGRALL 85

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1052974457 100 QHLIEECRRCGLHALIACITEGNEASYALHEKLGFEKVS 138
Cdd:PRK09491   86 EHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVT 124
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 51-136 1.27e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 49.38  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457  51 YFVYEVEGQIAGYCYVHGWKEKAAYnqsVETTIYLAPSSTGKGLGTELMQHLIEECRRCGLHALiacITEGNEASYALHE 130
Cdd:pfam13508   5 FFVAEDDGKIVGFAALLPLDDEGAL---AELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLL---ELETTNRAAAFYE 78


                  ....*.
gi 1052974457 131 KLGFEK 136
Cdd:pfam13508  79 KLGFEE 84
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
59-143 2.06e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 48.75  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457  59 QIAGYCYVHGWKEKAAYNQSVettiYLAPSSTGKGLGTELMQHLIEECRRCGLHALIACITEGNEASYALHEKLGFEKVS 138
Cdd:COG3393     1 ELVAMAGVRAESPGVAEISGV----YTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVG 76


                  ....*
gi 1052974457 139 SFREV 143
Cdd:COG3393    77 EYATV 81
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 51-115 1.15e-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: 46.50  E-value: 1.15e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1052974457  51 YFVYEVEGQIAGYCYVH--GWKEKAAYnqsVETtIYLAPSSTGKGLGTELMQHLIEECRRCGLHALI 115
Cdd:cd04301     1 FLVAEDDGEIVGFASLSpdGSGGDTAY---IGD-LAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 28-137 1.26e-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: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457  28 FELEPVSEEEMWTRIQTIS--SQYP--YFVYEVEGQIAGYCYVH-GWKEKAAYNqsvettIYLAPSSTGKGLGTELMQHL 102
Cdd:TIGR01575   6 LEIEAAAFAFPWTEAQFAEelANYHlcYLLARIGGKVVGYAGVQiVLDEAHILN------IAVKPEYQGQGIGRALLREL 79

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1052974457 103 IEECRRCGLHALIACITEGNEASYALHEKLGFEKV 137
Cdd:TIGR01575  80 IDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEI 114
PRK03624 PRK03624
putative acetyltransferase; Provisional
 51-153 2.70e-05

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 41.84  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457  51 YFVYEVEGQIAGYCYV----H-GWkekaAYnqsvettiYLA--PSSTGKGLGTELMQHLIEECRRCGLHALIACITEGNE 123
Cdd:PRK03624   47 FLVAEVGGEVVGTVMGgydgHrGW----AY--------YLAvhPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDND 114

                          90       100       110
                  ....*....|....*....|....*....|
gi 1052974457 124 ASYALHEKLGFEKVSSFrevgrKFGKWLGI 153
Cdd:PRK03624  115 AVLGFYEALGYEEQDRI-----SLGKRLIE 139
Eis COG4552
Predicted acetyltransferase [General function prediction only];
2-143 3.80e-05

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 42.58  E-value: 3.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457   2 IRKVCKEDAPAITAIYNHyithttiTFeLEPVSEEEMWTRIQTISSQYPYFVYEvEGQIAGYC-------YVHGWKEKAA 74
Cdd:COG4552     3 IRPLTEDDLDAFARLLAY-------AF-GPEPDDEELEAYRPLLEPGRVLGVFD-DGELVGTLalypftlNVGGARVPMA 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052974457  75 YNQSVETtiylAPSSTGKGLGTELMQHLIEECRRCG--LHALIAcitegneASYALHEKLGFEKVSSFREV 143
Cdd:COG4552    74 GITGVAV----APEHRRRGVARALLREALAELRERGqpLSALYP-------FEPGFYRRFGYELAGDRRRY 133
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 83-136 7.84e-05

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: 39.24  E-value: 7.84e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1052974457  83 IYLAPSSTGKGLGTELMQHLIEECRRCGLHALiACITEGNEASYALHEKLGFEK 136
Cdd:pfam08445  27 LQTLPEHRRRGLGSRLVAALARGIAERGITPF-AVVVAGNTPSRRLYEKLGFRK 79
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
91-138 8.39e-05

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 40.17  E-value: 8.39e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1052974457  91 GKGLGTELMQHLIEECRRCGLHALIACITEGNEASYalhEKLGFEKVS 138
Cdd:COG2153    72 GQGLGRALMEAAIEEARERGARRIVLSAQAHAVGFY---EKLGFVPVG 116
mycothiol_MshD TIGR03448
mycothiol synthase; Members of this family are MshD, the acetyltransferase that catalyzes the ...
 85-139 8.01e-04

mycothiol synthase; Members of this family are MshD, the acetyltransferase that catalyzes the final step of mycothiol biosynthesis in various members of the Actinomyctes, Mycothiol replaces glutathione in these species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 132489 [Multi-domain]  Cd Length: 292  Bit Score: 38.54  E-value: 8.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1052974457  85 LAPSSTGKGLGTELMQHLIEECRRCGLHALIACITEGNEASYALHEKLGFEKVSS 139
Cdd:TIGR03448 234 VDPAAQGRGLGDALTLIGLHHLAARGLPAVMLYVEADNEAAVRTYEKLGFTVAEV 288
PRK10562 PRK10562
putative acetyltransferase; Provisional
 1-101 6.18e-03

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 35.04  E-value: 6.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052974457   1 MIRKVCKEDAPAITA------IYNHYITHTTITFELEPVSEEEMWTRIQTissqypyFVYEVEGQIAGYCYVHGWKEKAA 74
Cdd:PRK10562    1 MIREYQPSDLPAILQlwlestIWAHPFIKEQYWRESAPLVRDVYLPAAQT-------WVWEEDGKLLGFVSVLEGRFVGA 73

                          90       100
                  ....*....|....*....|....*..
gi 1052974457  75 ynqsvettIYLAPSSTGKGLGTELMQH 101
Cdd:PRK10562   74 --------LFVAPKAVRRGIGKALMQH 92
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
86-125 6.60e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 35.27  E-value: 6.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1052974457  86 APSSTGKGLGTELMQHLIEECRRCGL-HALIACiTEGNEAS 125
Cdd:COG3981   100 RPSERGKGYATEMLRLALEEARELGLdRVLITC-DKDNIAS 139
GNAT_acetyltran pfam12746
GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance ...
 73-135 7.13e-03

GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance proteins, whereas others are listed as being GNAT acetyltransferases. The family has similarities to the GNAT acetyltransferase family.


Pssm-ID: 403833  Cd Length: 239  Bit Score: 35.71  E-value: 7.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052974457  73 AAYNQSVETTIYLAPSSTGKGLGTELMQHLIEECRRCGLHALIACItegNEASYALHEKLGFE 135
Cdd:pfam12746 172 SVYEGGIEIEIDTHPDYRGKGLATICAAALILECLKRGLYPSWDAH---NEASVALAEKLGYE 231
 
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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