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Conserved domains on  [gi|485651566|ref|WP_001297068|]
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MULTISPECIES: fatty acid biosynthesis protein FabY [Enterobacteriaceae]

Protein Classification

bifunctional GNAT family N-acetyltransferase/hotdog fold thioesterase( domain architecture ID 10456982)

bifunctional GNAT family N-acetyltransferase/hotdog fold thioesterase containing an N-terminal domain that may catalyze the transfer of an acetyl group from acetyl-CoA to a substrate and a C-terminal thioesterase domain, similar to Escherichia coli putative acetyltransferase YiiD

CATH:  3.10.129.10
EC:  2.3.1.-|3.1.2.-
Gene Ontology:  GO:0008080
PubMed:  10940244|9175471|15307895
SCOP:  3000149|3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YiiD_C pfam09500
Putative thioesterase (yiiD_Cterm); This entry consists of a broadly distributed ...
 158-298 5.47e-68

Putative thioesterase (yiiD_Cterm); This entry consists of a broadly distributed uncharacterized domain often found as a standalone protein. The member from Shewanella oneidensis is described from crystallography work as a putative thioesterase because it belongs to the HotDog clan of enzymes. About half of the members of this family are fused to an Acetyltransf_1 domain pfam00583.


:

Pssm-ID: 430649  Cd Length: 144  Bit Score: 208.65  E-value: 5.47e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485651566  158 CAQLQQAWYEHIPLSEKMGVRIQQYTGQKFITTMPETGNQNPHHTLFAGSLFSLATLTGWGLIWLMLRERHLGGTIILAD 237
Cdd:pfam09500   1 CQELQETWHDHIPLSRAMGIKVTQYDGQEFILSAPLAPNINHHGTMFAGSIYTLATLTGWGLLWLLLKEAGLEGDIVLAD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 485651566  238 AHIRYSKPISGKPHAVADL---GALSGDLDRLARGRKARVQMQVEIFGDETPGAVFEGTYIVLP 298
Cdd:pfam09500  81 GNIRYLKPVTGDPTARVSLptpEAWSGFLSRLARGGKARITLEVEIYSGGELAAEFTGRYVVLK 144
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
10-146 1.78e-32

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


:

Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 117.21  E-value: 1.78e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485651566  10 EEELERYYQFRWEMLRKPLHQPKGSERDAWDAMAHHQMVVDEqGNLVAVGRLYINADNEASIRFMAVHPDVQDKGLGTLM 89
Cdd:COG2153    1 AEELYDALALRREVFVVEQGVPPYLELDGKDEDARHLLAYDD-GELVATARLLPPGDGEAKIGRVAVLPEYRGQGLGRAL 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 485651566  90 AMTLESVARQEGVKRVTCSAREDAVEFFAKLGFVNQGEitTPTTTPIRHFLMIKPVA 146
Cdd:COG2153   80 MEAAIEEARERGARRIVLSAQAHAVGFYEKLGFVPVGE--EFLEAGIPHIDMRKPLS 134
 
Name Accession Description Interval E-value
YiiD_C pfam09500
Putative thioesterase (yiiD_Cterm); This entry consists of a broadly distributed ...
 158-298 5.47e-68

Putative thioesterase (yiiD_Cterm); This entry consists of a broadly distributed uncharacterized domain often found as a standalone protein. The member from Shewanella oneidensis is described from crystallography work as a putative thioesterase because it belongs to the HotDog clan of enzymes. About half of the members of this family are fused to an Acetyltransf_1 domain pfam00583.


Pssm-ID: 430649  Cd Length: 144  Bit Score: 208.65  E-value: 5.47e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485651566  158 CAQLQQAWYEHIPLSEKMGVRIQQYTGQKFITTMPETGNQNPHHTLFAGSLFSLATLTGWGLIWLMLRERHLGGTIILAD 237
Cdd:pfam09500   1 CQELQETWHDHIPLSRAMGIKVTQYDGQEFILSAPLAPNINHHGTMFAGSIYTLATLTGWGLLWLLLKEAGLEGDIVLAD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 485651566  238 AHIRYSKPISGKPHAVADL---GALSGDLDRLARGRKARVQMQVEIFGDETPGAVFEGTYIVLP 298
Cdd:pfam09500  81 GNIRYLKPVTGDPTARVSLptpEAWSGFLSRLARGGKARITLEVEIYSGGELAAEFTGRYVVLK 144
yiiD_Cterm TIGR02447
thioesterase domain, putative; This family consists of a broadly distributed uncharacterized ...
 164-298 8.91e-61

thioesterase domain, putative; This family consists of a broadly distributed uncharacterized domain found often as a standalone protein. The member from Shewanella oneidensis, PDB|1T82_A (Forouhar, et al., unpublished) is described from crystallography work as a putative thioesterase. About half of the members of this family are fused to an Acetyltransf_1 domain (pfam00583). The function of this protein is unknown.


Pssm-ID: 131500  Cd Length: 138  Bit Score: 190.26  E-value: 8.91e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485651566  164 AWYEHIPLSEKMGVRIQQYTGQKFITTMPETGNQNPHHTLFAGSLFSLATLTGWGLIWLMLRERHLGGTIILADAHIRYS 243
Cdd:TIGR02447   1 YLHSAIPLSEAMGIAVSSYTGGELRLSAPLAANINHHGTMFGGSLYTLATLSGWGLLWLRLQELGIDGDIVIADSHIRYL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 485651566  244 KPISGKPHA---VADLGALSGDLDRLARGRKARVQMQVEIFGDETPGAVFEGTYIVLP 298
Cdd:TIGR02447  81 APVTGDPVAnceAPDLESWEAFLATLQRGGKARVKLEAQISSDGKLAATFSGEYVALP 138
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
10-146 1.78e-32

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 117.21  E-value: 1.78e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485651566  10 EEELERYYQFRWEMLRKPLHQPKGSERDAWDAMAHHQMVVDEqGNLVAVGRLYINADNEASIRFMAVHPDVQDKGLGTLM 89
Cdd:COG2153    1 AEELYDALALRREVFVVEQGVPPYLELDGKDEDARHLLAYDD-GELVATARLLPPGDGEAKIGRVAVLPEYRGQGLGRAL 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 485651566  90 AMTLESVARQEGVKRVTCSAREDAVEFFAKLGFVNQGEitTPTTTPIRHFLMIKPVA 146
Cdd:COG2153   80 MEAAIEEARERGARRIVLSAQAHAVGFYEKLGFVPVGE--EFLEAGIPHIDMRKPLS 134
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 13-122 2.69e-13

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: 65.23  E-value: 2.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485651566   13 LERYYQFRWEMLRKPLHQPKGSERDAWDAM-AHHQMVVDEQGNLVAVGRLYINAD--NEASIRFMAVHPDVQDKGLGTLM 89
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDaSEGFFVAEEDGELVGFASLSIIDDepPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 485651566   90 AMTLESVARQEGVKRVTCSARED---AVEFFAKLGF 122
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADnlaAIALYEKLGF 116
PRK07757 PRK07757
N-acetyltransferase;
48-122 3.30e-12

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 63.29  E-value: 3.30e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 485651566  48 VVDEQGNLVAVGRLYINADNEASIRFMAVHPDVQDKGLGTLMAMTLESVARQEGVKRVTCSAREdaVEFFAKLGF 122
Cdd:PRK07757  45 VAEEEGEIVGCCALHILWEDLAEIRSLAVSEDYRGQGIGRMLVEACLEEARELGVKRVFALTYQ--PEFFEKLGF 117
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 163-301 1.34e-10

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 58.42  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485651566 163 QAWYEHIPLSEKMGVRIQQYTGQKFITTMP-ETGNQNPHHTLFAGSLFSLATLTGWGLIWLMLRERHLGGTIilaDAHIR 241
Cdd:COG2050    9 EGFLAANPFAELLGIELVEVEPGRAVLRLPvRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTI---ELNIN 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 485651566 242 YSKPI-SGKP-HAVADLgalsgdldrLARGRKARVqMQVEIF-GDETPGAVFEGTYIVLPAKP 301
Cdd:COG2050   86 FLRPArLGDRlTAEARV---------VRRGRRLAV-VEVEVTdEDGKLVATATGTFAVLPKRP 138
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 48-108 1.30e-06

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: 44.96  E-value: 1.30e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 485651566  48 VVDEQGNLVAVGRLYIN--ADNEASIRFMAVHPDVQDKGLGTLMAMTLESVARQEGVKRVTCS 108
Cdd:cd04301    3 VAEDDGEIVGFASLSPDgsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
N-Ac-Glu-synth TIGR01890
amino-acid N-acetyltransferase; This model represents a clade of amino-acid ...
 48-127 3.00e-04

amino-acid N-acetyltransferase; This model represents a clade of amino-acid N-acetyltransferases acting mainly on glutamate in the first step of the "acetylated" ornithine biosynthesis pathway. For this reason it is also called N-acetylglutamate synthase. The enzyme may also act on aspartate. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273856 [Multi-domain]  Cd Length: 429  Bit Score: 42.09  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485651566   48 VVDEQGNLVAVGRLYINADNE-ASIRFMAVHPDVQDKGLGTLMAMTLESVARQEGVKRVTCSAREDAvEFFAKLGFVNQG 126
Cdd:TIGR01890 326 IIEHDGNIIGCAALYPYAEEDcGEMACLAVSPEYQDGGRGERLLAHIEDRARQMGISRLFVLTTRTG-HWFRERGFQTAS 404


                  .
gi 485651566  127 E 127
Cdd:TIGR01890 405 V 405
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 175-296 6.25e-03

PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ).


Pssm-ID: 239527 [Multi-domain]  Cd Length: 113  Bit Score: 36.00  E-value: 6.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485651566 175 MGVRIQQYTGQKFITTMP-ETGNQNPHHTLFAGSLFSLATLTGWGLIWLMLRERHLGGTIilaDAHIRYSKPISGKP-HA 252
Cdd:cd03443    2 LGIRVVEVGPGRVVLRLPvRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTV---DLNVNYLRPARGGDlTA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 485651566 253 VADLgalsgdldrLARGRkaRVQ-MQVEIF-GDETPGAVFEGTYIV 296
Cdd:cd03443   79 RARV---------VKLGR--RLAvVEVEVTdEDGKLVATARGTFAV 113
 
Name Accession Description Interval E-value
YiiD_C pfam09500
Putative thioesterase (yiiD_Cterm); This entry consists of a broadly distributed ...
 158-298 5.47e-68

Putative thioesterase (yiiD_Cterm); This entry consists of a broadly distributed uncharacterized domain often found as a standalone protein. The member from Shewanella oneidensis is described from crystallography work as a putative thioesterase because it belongs to the HotDog clan of enzymes. About half of the members of this family are fused to an Acetyltransf_1 domain pfam00583.


Pssm-ID: 430649  Cd Length: 144  Bit Score: 208.65  E-value: 5.47e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485651566  158 CAQLQQAWYEHIPLSEKMGVRIQQYTGQKFITTMPETGNQNPHHTLFAGSLFSLATLTGWGLIWLMLRERHLGGTIILAD 237
Cdd:pfam09500   1 CQELQETWHDHIPLSRAMGIKVTQYDGQEFILSAPLAPNINHHGTMFAGSIYTLATLTGWGLLWLLLKEAGLEGDIVLAD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 485651566  238 AHIRYSKPISGKPHAVADL---GALSGDLDRLARGRKARVQMQVEIFGDETPGAVFEGTYIVLP 298
Cdd:pfam09500  81 GNIRYLKPVTGDPTARVSLptpEAWSGFLSRLARGGKARITLEVEIYSGGELAAEFTGRYVVLK 144
yiiD_Cterm TIGR02447
thioesterase domain, putative; This family consists of a broadly distributed uncharacterized ...
 164-298 8.91e-61

thioesterase domain, putative; This family consists of a broadly distributed uncharacterized domain found often as a standalone protein. The member from Shewanella oneidensis, PDB|1T82_A (Forouhar, et al., unpublished) is described from crystallography work as a putative thioesterase. About half of the members of this family are fused to an Acetyltransf_1 domain (pfam00583). The function of this protein is unknown.


Pssm-ID: 131500  Cd Length: 138  Bit Score: 190.26  E-value: 8.91e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485651566  164 AWYEHIPLSEKMGVRIQQYTGQKFITTMPETGNQNPHHTLFAGSLFSLATLTGWGLIWLMLRERHLGGTIILADAHIRYS 243
Cdd:TIGR02447   1 YLHSAIPLSEAMGIAVSSYTGGELRLSAPLAANINHHGTMFGGSLYTLATLSGWGLLWLRLQELGIDGDIVIADSHIRYL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 485651566  244 KPISGKPHA---VADLGALSGDLDRLARGRKARVQMQVEIFGDETPGAVFEGTYIVLP 298
Cdd:TIGR02447  81 APVTGDPVAnceAPDLESWEAFLATLQRGGKARVKLEAQISSDGKLAATFSGEYVALP 138
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
10-146 1.78e-32

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 117.21  E-value: 1.78e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485651566  10 EEELERYYQFRWEMLRKPLHQPKGSERDAWDAMAHHQMVVDEqGNLVAVGRLYINADNEASIRFMAVHPDVQDKGLGTLM 89
Cdd:COG2153    1 AEELYDALALRREVFVVEQGVPPYLELDGKDEDARHLLAYDD-GELVATARLLPPGDGEAKIGRVAVLPEYRGQGLGRAL 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 485651566  90 AMTLESVARQEGVKRVTCSAREDAVEFFAKLGFVNQGEitTPTTTPIRHFLMIKPVA 146
Cdd:COG2153   80 MEAAIEEARERGARRIVLSAQAHAVGFYEKLGFVPVGE--EFLEAGIPHIDMRKPLS 134
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 48-123 1.79e-18

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: 80.04  E-value: 1.79e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 485651566  48 VVDEQGNLVAVGRLYINADNEASIRFMAVHPDVQDKGLGTLMAMTLESVARQEGVKRVTCSAREDAVEFFAKLGFV 123
Cdd:COG1246   32 VAEEDGEIVGCAALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAIHFYEKLGFE 107
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 13-122 2.69e-13

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: 65.23  E-value: 2.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485651566   13 LERYYQFRWEMLRKPLHQPKGSERDAWDAM-AHHQMVVDEQGNLVAVGRLYINAD--NEASIRFMAVHPDVQDKGLGTLM 89
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDaSEGFFVAEEDGELVGFASLSIIDDepPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 485651566   90 AMTLESVARQEGVKRVTCSARED---AVEFFAKLGF 122
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADnlaAIALYEKLGF 116
PRK07757 PRK07757
N-acetyltransferase;
48-122 3.30e-12

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 63.29  E-value: 3.30e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 485651566  48 VVDEQGNLVAVGRLYINADNEASIRFMAVHPDVQDKGLGTLMAMTLESVARQEGVKRVTCSAREdaVEFFAKLGF 122
Cdd:PRK07757  45 VAEEEGEIVGCCALHILWEDLAEIRSLAVSEDYRGQGIGRMLVEACLEEARELGVKRVFALTYQ--PEFFEKLGF 117
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 163-301 1.34e-10

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 58.42  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485651566 163 QAWYEHIPLSEKMGVRIQQYTGQKFITTMP-ETGNQNPHHTLFAGSLFSLATLTGWGLIWLMLRERHLGGTIilaDAHIR 241
Cdd:COG2050    9 EGFLAANPFAELLGIELVEVEPGRAVLRLPvRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTI---ELNIN 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 485651566 242 YSKPI-SGKP-HAVADLgalsgdldrLARGRKARVqMQVEIF-GDETPGAVFEGTYIVLPAKP 301
Cdd:COG2050   86 FLRPArLGDRlTAEARV---------VRRGRRLAV-VEVEVTdEDGKLVATATGTFAVLPKRP 138
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 48-123 2.02e-10

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 56.31  E-value: 2.02e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 485651566   48 VVDEQGNLVAVGRLYINADNEASIR-FMAVHPDVQDKGLGTLMAMTLESVARQEGVKRVTCSAREDAVEFFAKLGFV 123
Cdd:pfam13508   7 VAEDDGKIVGFAALLPLDDEGALAElRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFE 83
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 48-127 1.36e-09

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 55.44  E-value: 1.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485651566  48 VVDEQGNLVAVGRLYINADNEASIRFMAVHPDVQDKGLGTLMAMTLESVARQEGVK--RVTCSAR-EDAVEFFAKLGFVN 124
Cdd:COG0454   38 AVDDKGEPIGFAGLRRLDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTalELDTLDGnPAAIRFYERLGFKE 117


                 ...
gi 485651566 125 QGE 127
Cdd:COG0454  118 IER 120
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 65-146 3.57e-09

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 53.12  E-value: 3.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485651566  65 ADNEASIRFMAVHPDVQDKGLGTLMAMTLESVARQEGVKRVTCSARED---AVEFFAKLGFVNQGEitTPTTTPIRHFLM 141
Cdd:COG0456   10 GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDneaAIALYEKLGFEEVGE--RPNYYGDDALVM 87


                 ....*
gi 485651566 142 IKPVA 146
Cdd:COG0456   88 EKELA 92
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
31-144 7.13e-09

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 53.55  E-value: 7.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485651566  31 PKGSERDAWDAMAHHQ-----MVVDEQGNLVAVGRLY----INADNEASIRFMAVHPDVQDKGLGTLMAMTLESVARQEG 101
Cdd:COG3153   21 GPGREAELVDRLREDPaaglsLVAEDDGEIVGHVALSpvdiDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERG 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 485651566 102 VKRVTCSAREDAVEFFAKLGFVNQGEitTPTTTPIRHFLMIKP 144
Cdd:COG3153  101 ARAVVLLGDPSLLPFYERFGFRPAGE--LGLTLGPDEVFLAKE 141
PRK07922 PRK07922
amino-acid N-acetyltransferase;
49-123 9.78e-09

amino-acid N-acetyltransferase;


Pssm-ID: 236132 [Multi-domain]  Cd Length: 169  Bit Score: 53.77  E-value: 9.78e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 485651566  49 VDEQGNLVAVGRLYINADNEASIRFMAVHPDVQDKGLGTLMAMTLESVARQEGVKRVTCSAREdaVEFFAKLGFV 123
Cdd:PRK07922  51 EHLDGEVVGCGALHVMWEDLAEIRTVAVDPAARGRGVGHAIVERLLDVARELGLSRVFVLTFE--VEFFARHGFV 123
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 9-127 1.27e-07

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: 49.58  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485651566    9 TEEELERYYQF-RWEMLRKPLHQPkgserdawdamAHHQMVVDEQGNLVAVGRLYinadNEASIRFMAVHPDVQDKGLGT 87
Cdd:pfam13673   6 SEEGIETFYEFiSPEALRERIDQG-----------EYFFFVAFEGGQIVGVIALR----DRGHISLLFVDPDYQGQGIGK 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 485651566   88 LMAMTLESVARQEGVK--RVTCSAREDAVEFFAKLGFVNQGE 127
Cdd:pfam13673  71 ALLEAVEDYAEKDGIKlsELTVNASPYAVPFYEKLGFRATGP 112
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 48-108 1.30e-06

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: 44.96  E-value: 1.30e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 485651566  48 VVDEQGNLVAVGRLYIN--ADNEASIRFMAVHPDVQDKGLGTLMAMTLESVARQEGVKRVTCS 108
Cdd:cd04301    3 VAEDDGEIVGFASLSPDgsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
55-127 2.13e-06

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 44.90  E-value: 2.13e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 485651566  55 LVAVGRLYINADNEASIRFMAVHPDVQDKGLGTLMAMTLESVARQEGVKRVTCSARED---AVEFFAKLGFVNQGE 127
Cdd:COG3393    2 LVAMAGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADnpaARRLYERLGFRPVGE 77
PTZ00330 PTZ00330
acetyltransferase; Provisional
 76-122 1.50e-05

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 44.06  E-value: 1.50e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 485651566  76 VHPDVQDKGLGTLMAMTLESVARQEGVKRVTCSAREDAVEFFAKLGF 122
Cdd:PTZ00330  90 VDPSYRGQGLGRALISDLCEIARSSGCYKVILDCTEDMVAFYKKLGF 136
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
35-127 6.90e-05

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 42.67  E-value: 6.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485651566  35 ERDAWDAMAHHQ----MVVDEQGNLVAVGRLYINADNEASIR----FMAVHPDVQDKGLGTLMAMTLESVARQEGVKRV- 105
Cdd:COG1247   39 EREAWFAAILAPgrpvLVAEEDGEVVGFASLGPFRPRPAYRGtaeeSIYVDPDARGRGIGRALLEALIERARARGYRRLv 118

                         90       100
                 ....*....|....*....|....
gi 485651566 106 --TCSAREDAVEFFAKLGFVNQGE 127
Cdd:COG1247  119 avVLADNEASIALYEKLGFEEVGT 142
PRK12308 PRK12308
argininosuccinate lyase;
48-123 1.15e-04

argininosuccinate lyase;


Pssm-ID: 183425 [Multi-domain]  Cd Length: 614  Bit Score: 43.62  E-value: 1.15e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 485651566  48 VVDEQGNLVAVGRLYINADNEASIRFMAVHPDVQDKGLGTLMAMTLESVARQEGVKRVTCSARedAVEFFAKLGFV 123
Cdd:PRK12308 507 VAEHHGEVTGCASLYIYDSGLAEIRSLGVEAGWQVQGQGSALVQYLVEKARQMAIKKVFVLTR--VPEFFMKQGFS 580
N-Ac-Glu-synth TIGR01890
amino-acid N-acetyltransferase; This model represents a clade of amino-acid ...
 48-127 3.00e-04

amino-acid N-acetyltransferase; This model represents a clade of amino-acid N-acetyltransferases acting mainly on glutamate in the first step of the "acetylated" ornithine biosynthesis pathway. For this reason it is also called N-acetylglutamate synthase. The enzyme may also act on aspartate. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273856 [Multi-domain]  Cd Length: 429  Bit Score: 42.09  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485651566   48 VVDEQGNLVAVGRLYINADNE-ASIRFMAVHPDVQDKGLGTLMAMTLESVARQEGVKRVTCSAREDAvEFFAKLGFVNQG 126
Cdd:TIGR01890 326 IIEHDGNIIGCAALYPYAEEDcGEMACLAVSPEYQDGGRGERLLAHIEDRARQMGISRLFVLTTRTG-HWFRERGFQTAS 404


                  .
gi 485651566  127 E 127
Cdd:TIGR01890 405 V 405
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 68-122 1.76e-03

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: 37.69  E-value: 1.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 485651566   68 EASIRFMAVHPDVQDKGLGTLMAMTLESVARQEGVKRVTCSARED---AVEFFAKLGF 122
Cdd:TIGR01575  54 EAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSniaAQALYKKLGF 111
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-127 3.81e-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: 37.67  E-value: 3.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485651566   1 MYHLRvPQTEEELERYYQFR--WEMLRkPLHQPKGSERDAWDAMAHHQ------------MVVDEQGNLVAVGRLY-INA 65
Cdd:COG1670    7 RLRLR-PLRPEDAEALAELLndPEVAR-YLPGPPYSLEEARAWLERLLadwadggalpfaIEDKEDGELIGVVGLYdIDR 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 485651566  66 DN-EASIRFMaVHPDVQDKGLGTLMAMTLESVARQE-GVKRVTCSARED---AVEFFAKLGFVNQGE 127
Cdd:COG1670   85 ANrSAEIGYW-LAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDntaSIRVLEKLGFRLEGT 150
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 175-296 6.25e-03

PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ).


Pssm-ID: 239527 [Multi-domain]  Cd Length: 113  Bit Score: 36.00  E-value: 6.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485651566 175 MGVRIQQYTGQKFITTMP-ETGNQNPHHTLFAGSLFSLATLTGWGLIWLMLRERHLGGTIilaDAHIRYSKPISGKP-HA 252
Cdd:cd03443    2 LGIRVVEVGPGRVVLRLPvRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTV---DLNVNYLRPARGGDlTA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 485651566 253 VADLgalsgdldrLARGRkaRVQ-MQVEIF-GDETPGAVFEGTYIV 296
Cdd:cd03443   79 RARV---------VKLGR--RLAvVEVEVTdEDGKLVATARGTFAV 113
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
 75-123 6.41e-03

tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA(Met) C34 N-acetyltransferase TmcA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441053 [Multi-domain]  Cd Length: 703  Bit Score: 38.27  E-value: 6.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 485651566  75 AVHPDVQDKGLGTLMAMTLESVARQEGVKRVTCS--AREDAVEFFAKLGFV 123
Cdd:COG1444  492 AVHPALQRRGLGSRLLAEIREEAKEEGLDWLGVSfgATPELLRFWQRNGFV 542
 
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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