NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1277787913|gb|PIU03794|]
View 

hypothetical protein COT44_01405 [Candidatus Shapirobacteria bacterium CG08_land_8_20_14_0_20_39_18]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10006981)

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
5-93 2.33e-14

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 64.34  E-value: 2.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277787913   5 LVFEIDGEVVSFVLLKWHGKETHPEYPDLEDLFTREDKRGKGYASALIKECENLVKEKGHKKIGLAANPdlneNARRLYE 84
Cdd:COG3153    42 LVAEDDGEIVGHVALSPVDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDP----SLLPFYE 117


                  ....*....
gi 1277787913  85 HLCYKHDGK 93
Cdd:COG3153   118 RFGFRPAGE 126
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
5-93 2.33e-14

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 64.34  E-value: 2.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277787913   5 LVFEIDGEVVSFVLLKWHGKETHPEYPDLEDLFTREDKRGKGYASALIKECENLVKEKGHKKIGLAANPdlneNARRLYE 84
Cdd:COG3153    42 LVAEDDGEIVGHVALSPVDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDP----SLLPFYE 117


                  ....*....
gi 1277787913  85 HLCYKHDGK 93
Cdd:COG3153   118 RFGFRPAGE 126
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 4-69 9.98e-12

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: 55.74  E-value: 9.98e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277787913   4 YLVFEIDGEVVSFVLLKWHGkeTHPEYPDLEDLFTREDKRGKGYASALIKECENLVKEKGHKKIGL 69
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDG--SGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 4-86 3.95e-11

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


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 55.60  E-value: 3.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277787913   4 YLVFEIDGEVVSFVLLKWHGKETHpeYPDLEDLFTREDKRGKGYASALIKECENLVKEKGHKKIGLAANPDlNENARRLY 83
Cdd:pfam00583  35 FFVAEEDGELVGFASLSIIDDEPP--VGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAAD-NLAAIALY 111


                  ...
gi 1277787913  84 EHL 86
Cdd:pfam00583 112 EKL 114
PRK03624 PRK03624
putative acetyltransferase; Provisional
 4-91 6.83e-05

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 39.53  E-value: 6.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277787913   4 YLVFEIDGEVVSFVLLKWHGKE-------THPEYpdledlftredkRGKGYASALIKECENLVKEKGHKKIGLAANPDlN 76
Cdd:PRK03624   47 FLVAEVGGEVVGTVMGGYDGHRgwayylaVHPDF------------RGRGIGRALVARLEKKLIARGCPKINLQVRED-N 113

                          90
                  ....*....|....*
gi 1277787913  77 ENARRLYEHLCYKHD 91
Cdd:PRK03624  114 DAVLGFYEALGYEEQ 128
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
5-93 2.33e-14

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 64.34  E-value: 2.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277787913   5 LVFEIDGEVVSFVLLKWHGKETHPEYPDLEDLFTREDKRGKGYASALIKECENLVKEKGHKKIGLAANPdlneNARRLYE 84
Cdd:COG3153    42 LVAEDDGEIVGHVALSPVDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDP----SLLPFYE 117


                  ....*....
gi 1277787913  85 HLCYKHDGK 93
Cdd:COG3153   118 RFGFRPAGE 126
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 4-69 9.98e-12

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: 55.74  E-value: 9.98e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277787913   4 YLVFEIDGEVVSFVLLKWHGkeTHPEYPDLEDLFTREDKRGKGYASALIKECENLVKEKGHKKIGL 69
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDG--SGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 16-86 1.00e-11

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 56.20  E-value: 1.00e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277787913  16 FVLLKWHGKETHPEypdLEDLFTREDKRGKGYASALIKECENLVKEKGHKKIGLAANPDlNENARRLYEHL 86
Cdd:COG0456     2 FALLGLVDGGDEAE---IEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVRED-NEAAIALYEKL 68
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 3-86 1.12e-11

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: 57.31  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277787913   3 EYLVFEIDGEVVSFVLLKWHGkethPEYPDLEDLFTREDKRGKGYASALIKECENLVKEKGHKKIGLAANPdlneNARRL 82
Cdd:COG1246    29 EFWVAEEDGEIVGCAALHPLD----EDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTS----AAIHF 100


                  ....
gi 1277787913  83 YEHL 86
Cdd:COG1246   101 YEKL 104
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 4-86 3.95e-11

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


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 55.60  E-value: 3.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277787913   4 YLVFEIDGEVVSFVLLKWHGKETHpeYPDLEDLFTREDKRGKGYASALIKECENLVKEKGHKKIGLAANPDlNENARRLY 83
Cdd:pfam00583  35 FFVAEEDGELVGFASLSIIDDEPP--VGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAAD-NLAAIALY 111


                  ...
gi 1277787913  84 EHL 86
Cdd:pfam00583 112 EKL 114
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
12-92 1.27e-10

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 53.37  E-value: 1.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277787913  12 EVVSFVLLKWHgketHPEYPDLEDLFTREDKRGKGYASALIKECENLVKEKGHKKIGLAANPDlNENARRLYEHLCYKHD 91
Cdd:COG3393     1 ELVAMAGVRAE----SPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDAD-NPAARRLYERLGFRPV 75


                  .
gi 1277787913  92 G 92
Cdd:COG3393    76 G 76
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
4-115 2.99e-10

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 54.23  E-value: 2.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277787913   4 YLVFEIDGEVVSFVLLKWHgkETHPEYPD--LEDLFTREDKRGKGYASALIKECENLVKEKGHKKIGLAANPDlNENARR 81
Cdd:COG1247    54 VLVAEEDGEVVGFASLGPF--RPRPAYRGtaEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLAD-NEASIA 130

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1277787913  82 LYEHLCYKHDGKKSYIdGIYNGVEDWVVDLEKEI 115
Cdd:COG1247   131 LYEKLGFEEVGTLPEV-GFKFGRWLDLVLMQKRL 163
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 3-86 3.61e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 49.76  E-value: 3.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277787913   3 EYLVFEIDGEVVSFVLLKWHGKETHPEYpdlEDLFTREDKRGKGYASALIKECENLVKEKGHKKIGLAAnpdlNENARRL 82
Cdd:pfam13508   4 RFFVAEDDGKIVGFAALLPLDDEGALAE---LRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET----TNRAAAF 76


                  ....
gi 1277787913  83 YEHL 86
Cdd:pfam13508  77 YEKL 80
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 4-115 2.95e-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: 45.72  E-value: 2.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277787913   4 YLVFEIDGEVVSFVLLKWHGKethpeypdLEDLFTREDKRGKGYASALIKECENLVKEKGHKKIGLAANPDLneNARRLY 83
Cdd:pfam13673  33 FFVAFEGGQIVGVIALRDRGH--------ISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASP--YAVPFY 102

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1277787913  84 EHLCYKHDGKKSYIDGIyngvedWVVDLEKEI 115
Cdd:pfam13673 103 EKLGFRATGPEQEFNGI------RFVPMEKEL 128
PRK03624 PRK03624
putative acetyltransferase; Provisional
 4-91 6.83e-05

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 39.53  E-value: 6.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277787913   4 YLVFEIDGEVVSFVLLKWHGKE-------THPEYpdledlftredkRGKGYASALIKECENLVKEKGHKKIGLAANPDlN 76
Cdd:PRK03624   47 FLVAEVGGEVVGTVMGGYDGHRgwayylaVHPDF------------RGRGIGRALVARLEKKLIARGCPKINLQVRED-N 113

                          90
                  ....*....|....*
gi 1277787913  77 ENARRLYEHLCYKHD 91
Cdd:PRK03624  114 DAVLGFYEALGYEEQ 128
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 27-88 1.90e-03

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


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 34.61  E-value: 1.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277787913  27 HPEYPDLEDLFTREDKRGKGYASALIKECENLVKEKGHkKIGLAANPDlNENARRLYEHLCY 88
Cdd:pfam08445  18 RLPGGELGALQTLPEHRRRGLGSRLVAALARGIAERGI-TPFAVVVAG-NTPSRRLYEKLGF 77
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH