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Conserved domains on  [gi|1140785689|ref|WP_076646126|]
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bifunctional GNAT family N-acetyltransferase/hotdog fold thioesterase [Vibrio sp. 10N.222.47.A9]

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 ...
 157-297 3.30e-78

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: 234.84  E-value: 3.30e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140785689 157 CNELQQRWENQIPISDKMGIKINQYTGYQFECSAQLNPNLNPHNTMFAGSAFTLATLTGWGMTWLLMKERGLTGDIVLAD 236
Cdd:pfam09500   1 CQELQETWHDHIPLSRAMGIKVTQYDGQEFILSAPLAPNINHHGTMFAGSIYTLATLTGWGLLWLLLKEAGLEGDIVLAD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1140785689 237 SNIRYRHPVEQNPVASTSL---DGISGDLDRLASGRKARIIIHVTINSGDVEAVEFTGTYMLIP 297
Cdd:pfam09500  81 GNIRYLKPVTGDPTARVSLptpEAWSGFLSRLARGGKARITLEVEIYSGGELAAEFTGRYVVLK 144
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
10-145 3.60e-36

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


:

Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 126.45  E-value: 3.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140785689  10 ENQLNKYYHFRWQMLREPWRMPVGSERDEYDAMSHHRMIVDGrGRPMAIGRLYITPDLEGQIRYMAVKKSRQSKGMGSLI 89
Cdd:COG2153     1 AEELYDALALRREVFVVEQGVPPYLELDGKDEDARHLLAYDD-GELVATARLLPPGDGEAKIGRVAVLPEYRGQGLGRAL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1140785689  90 LVALESLARQEGAKRLVCNAREDAISFYEKNEFERRGEINDQRGpVRHQQMVKPLD 145
Cdd:COG2153    80 MEAAIEEARERGARRIVLSAQAHAVGFYEKLGFVPVGEEFLEAG-IPHIDMRKPLS 134
 
Name Accession Description Interval E-value
YiiD_C pfam09500
Putative thioesterase (yiiD_Cterm); This entry consists of a broadly distributed ...
 157-297 3.30e-78

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: 234.84  E-value: 3.30e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140785689 157 CNELQQRWENQIPISDKMGIKINQYTGYQFECSAQLNPNLNPHNTMFAGSAFTLATLTGWGMTWLLMKERGLTGDIVLAD 236
Cdd:pfam09500   1 CQELQETWHDHIPLSRAMGIKVTQYDGQEFILSAPLAPNINHHGTMFAGSIYTLATLTGWGLLWLLLKEAGLEGDIVLAD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1140785689 237 SNIRYRHPVEQNPVASTSL---DGISGDLDRLASGRKARIIIHVTINSGDVEAVEFTGTYMLIP 297
Cdd:pfam09500  81 GNIRYLKPVTGDPTARVSLptpEAWSGFLSRLARGGKARITLEVEIYSGGELAAEFTGRYVVLK 144
yiiD_Cterm TIGR02447
thioesterase domain, putative; This family consists of a broadly distributed uncharacterized ...
 164-297 2.12e-53

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: 171.00  E-value: 2.12e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140785689 164 WENQIPISDKMGIKINQYTGYQFECSAQLNPNLNPHNTMFAGSAFTLATLTGWGMTWLLMKERGLTGDIVLADSNIRYRH 243
Cdd:TIGR02447   2 LHSAIPLSEAMGIAVSSYTGGELRLSAPLAANINHHGTMFGGSLYTLATLSGWGLLWLRLQELGIDGDIVIADSHIRYLA 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1140785689 244 PVEQNPVAST---SLDGISGDLDRLASGRKARIIIHVTINSGDVEAVEFTGTYMLIP 297
Cdd:TIGR02447  82 PVTGDPVANCeapDLESWEAFLATLQRGGKARVKLEAQISSDGKLAATFSGEYVALP 138
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
10-145 3.60e-36

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 126.45  E-value: 3.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140785689  10 ENQLNKYYHFRWQMLREPWRMPVGSERDEYDAMSHHRMIVDGrGRPMAIGRLYITPDLEGQIRYMAVKKSRQSKGMGSLI 89
Cdd:COG2153     1 AEELYDALALRREVFVVEQGVPPYLELDGKDEDARHLLAYDD-GELVATARLLPPGDGEAKIGRVAVLPEYRGQGLGRAL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1140785689  90 LVALESLARQEGAKRLVCNAREDAISFYEKNEFERRGEINDQRGpVRHQQMVKPLD 145
Cdd:COG2153    80 MEAAIEEARERGARRIVLSAQAHAVGFYEKLGFVPVGEEFLEAG-IPHIDMRKPLS 134
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 13-122 4.41e-09

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: 53.68  E-value: 4.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140785689  13 LNKYYHFRWQMLREPWRMPVGSERDEYDAMSHHRMIVDGR-GRPMAIGRLYITPD--LEGQIRYMAVKKSRQSKGMGSLI 89
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEdGELVGFASLSIIDDepPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1140785689  90 LVALESLARQEGAKRLVCNARED---AISFYEKNEF 122
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADnlaAIALYEKLGF 116
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 162-297 4.17e-05

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 42.62  E-value: 4.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140785689 162 QRWENQIPISDKMGIKINQYTGYQFECSAQLNP-NLNPHNTMFAGSAFTLA-TLTGW-GMTWLLMKERGLTGDIvladsN 238
Cdd:COG2050     9 EGFLAANPFAELLGIELVEVEPGRAVLRLPVRPeHLNPPGTVHGGALAALAdSAAGLaANSALPPGRRAVTIEL-----N 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140785689 239 IRYRHPVeqnpVASTSLDGIsGDLDRLasGRKaRIIIHVTINSGDVEAV-EFTGTYMLIP 297
Cdd:COG2050    84 INFLRPA----RLGDRLTAE-ARVVRR--GRR-LAVVEVEVTDEDGKLVaTATGTFAVLP 135
PRK07757 PRK07757
N-acetyltransferase;
48-107 5.38e-04

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 39.79  E-value: 5.38e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1140785689  48 IVDGRGRPMAIGRLYI-TPDLeGQIRYMAVKKSRQSKGMGSLILVALESLARQEGAKRLVC 107
Cdd:PRK07757   45 VAEEEGEIVGCCALHIlWEDL-AEIRSLAVSEDYRGQGIGRMLVEACLEEARELGVKRVFA 104
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 48-108 6.96e-04

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


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 37.26  E-value: 6.96e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1140785689  48 IVDGRGRPMAIGRLYITPDLE--GQIRYMAVKKSRQSKGMGSLILVALESLARQEGAKRLVCN 108
Cdd:cd04301     3 VAEDDGEIVGFASLSPDGSGGdtAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
YiiD_C pfam09500
Putative thioesterase (yiiD_Cterm); This entry consists of a broadly distributed ...
 157-297 3.30e-78

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: 234.84  E-value: 3.30e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140785689 157 CNELQQRWENQIPISDKMGIKINQYTGYQFECSAQLNPNLNPHNTMFAGSAFTLATLTGWGMTWLLMKERGLTGDIVLAD 236
Cdd:pfam09500   1 CQELQETWHDHIPLSRAMGIKVTQYDGQEFILSAPLAPNINHHGTMFAGSIYTLATLTGWGLLWLLLKEAGLEGDIVLAD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1140785689 237 SNIRYRHPVEQNPVASTSL---DGISGDLDRLASGRKARIIIHVTINSGDVEAVEFTGTYMLIP 297
Cdd:pfam09500  81 GNIRYLKPVTGDPTARVSLptpEAWSGFLSRLARGGKARITLEVEIYSGGELAAEFTGRYVVLK 144
yiiD_Cterm TIGR02447
thioesterase domain, putative; This family consists of a broadly distributed uncharacterized ...
 164-297 2.12e-53

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: 171.00  E-value: 2.12e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140785689 164 WENQIPISDKMGIKINQYTGYQFECSAQLNPNLNPHNTMFAGSAFTLATLTGWGMTWLLMKERGLTGDIVLADSNIRYRH 243
Cdd:TIGR02447   2 LHSAIPLSEAMGIAVSSYTGGELRLSAPLAANINHHGTMFGGSLYTLATLSGWGLLWLRLQELGIDGDIVIADSHIRYLA 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1140785689 244 PVEQNPVAST---SLDGISGDLDRLASGRKARIIIHVTINSGDVEAVEFTGTYMLIP 297
Cdd:TIGR02447  82 PVTGDPVANCeapDLESWEAFLATLQRGGKARVKLEAQISSDGKLAATFSGEYVALP 138
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
10-145 3.60e-36

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 126.45  E-value: 3.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140785689  10 ENQLNKYYHFRWQMLREPWRMPVGSERDEYDAMSHHRMIVDGrGRPMAIGRLYITPDLEGQIRYMAVKKSRQSKGMGSLI 89
Cdd:COG2153     1 AEELYDALALRREVFVVEQGVPPYLELDGKDEDARHLLAYDD-GELVATARLLPPGDGEAKIGRVAVLPEYRGQGLGRAL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1140785689  90 LVALESLARQEGAKRLVCNAREDAISFYEKNEFERRGEINDQRGpVRHQQMVKPLD 145
Cdd:COG2153    80 MEAAIEEARERGARRIVLSAQAHAVGFYEKLGFVPVGEEFLEAG-IPHIDMRKPLS 134
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 53-145 6.92e-14

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: 67.32  E-value: 6.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140785689  53 GRPMAIGRLYITPDLEGQIRYMAVKKSRQSKGMGSLILVALESLARQEGAKRLVCNAREDAISFYEKNEFErrgEINDQR 132
Cdd:COG1246    37 GEIVGCAALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAIHFYEKLGFE---EIDKED 113

                          90
                  ....*....|....*....
gi 1140785689 133 GPVRHQQ------MVKPLD 145
Cdd:COG1246   114 LPYAKVWqrdsvvMEKDLE 132
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 56-145 1.88e-10

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 56.59  E-value: 1.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140785689  56 MAIGRLYITPDlEGQIRYMAVKKSRQSKGMGSLILVALESLARQEGAKRLVCNARED---AISFYEKNEFERRGEINDQR 132
Cdd:COG0456     2 FALLGLVDGGD-EAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDneaAIALYEKLGFEEVGERPNYY 80

                          90
                  ....*....|...
gi 1140785689 133 GPVRHqQMVKPLD 145
Cdd:COG0456    81 GDDAL-VMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 13-122 4.41e-09

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: 53.68  E-value: 4.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140785689  13 LNKYYHFRWQMLREPWRMPVGSERDEYDAMSHHRMIVDGR-GRPMAIGRLYITPD--LEGQIRYMAVKKSRQSKGMGSLI 89
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEdGELVGFASLSIIDDepPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1140785689  90 LVALESLARQEGAKRLVCNARED---AISFYEKNEF 122
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADnlaAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
69-144 7.40e-09

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 53.55  E-value: 7.40e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1140785689  69 GQIRYMAVKKSRQSKGMGSLILVALESLARQEGAKRLVCNAREDAISFYEKNEFERRGEINDQRGPVRHqQMVKPL 144
Cdd:COG3153    68 LLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAGELGLTLGPDEV-FLAKEL 142
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 48-124 1.76e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 50.92  E-value: 1.76e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1140785689  48 IVDGRGRPMAIGRLYITPDLEGQIR-YMAVKKSRQSKGMGSLILVALESLARQEGAKRLVCNAREDAISFYEKNEFER 124
Cdd:pfam13508   7 VAEDDGKIVGFAALLPLDDEGALAElRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFEE 84
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 162-297 4.17e-05

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 42.62  E-value: 4.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140785689 162 QRWENQIPISDKMGIKINQYTGYQFECSAQLNP-NLNPHNTMFAGSAFTLA-TLTGW-GMTWLLMKERGLTGDIvladsN 238
Cdd:COG2050     9 EGFLAANPFAELLGIELVEVEPGRAVLRLPVRPeHLNPPGTVHGGALAALAdSAAGLaANSALPPGRRAVTIEL-----N 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140785689 239 IRYRHPVeqnpVASTSLDGIsGDLDRLasGRKaRIIIHVTINSGDVEAV-EFTGTYMLIP 297
Cdd:COG2050    84 INFLRPA----RLGDRLTAE-ARVVRR--GRR-LAVVEVEVTDEDGKLVaTATGTFAVLP 135
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
76-130 1.29e-04

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 41.90  E-value: 1.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1140785689  76 VKKSRQSKGMGSLILVALESLARQEGAKRL---VCNAREDAISFYEKNEFERRGEIND 130
Cdd:COG1247    88 VDPDARGRGIGRALLEALIERARARGYRRLvavVLADNEASIALYEKLGFEEVGTLPE 145
PRK07757 PRK07757
N-acetyltransferase;
48-107 5.38e-04

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 39.79  E-value: 5.38e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1140785689  48 IVDGRGRPMAIGRLYI-TPDLeGQIRYMAVKKSRQSKGMGSLILVALESLARQEGAKRLVC 107
Cdd:PRK07757   45 VAEEEGEIVGCCALHIlWEDL-AEIRSLAVSEDYRGQGIGRMLVEACLEEARELGVKRVFA 104
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 48-108 6.96e-04

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


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 37.26  E-value: 6.96e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1140785689  48 IVDGRGRPMAIGRLYITPDLE--GQIRYMAVKKSRQSKGMGSLILVALESLARQEGAKRLVCN 108
Cdd:cd04301     3 VAEDDGEIVGFASLSPDGSGGdtAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PTZ00330 PTZ00330
acetyltransferase; Provisional
 69-125 2.15e-03

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 37.90  E-value: 2.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1140785689  69 GQIRYMAVKKSRQSKGMGSLILVALESLARQEGAKRLVCNAREDAISFYEKNEFERR 125
Cdd:PTZ00330   83 GHIEDVVVDPSYRGQGLGRALISDLCEIARSSGCYKVILDCTEDMVAFYKKLGFRAC 139
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 74-142 6.51e-03

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: 36.09  E-value: 6.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1140785689  74 MAVKKSRQSKGMGSLILVALESLARQEGAK--RLVCNAREDAISFYEK-------NEFERRGeindqrgpVRHQQMVK 142
Cdd:pfam13673  57 LFVDPDYQGQGIGKALLEAVEDYAEKDGIKlsELTVNASPYAVPFYEKlgfratgPEQEFNG--------IRFVPMEK 126
 
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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