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Conserved domains on  [gi|2048208783|ref|WP_214805043|]
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nucleotidyltransferase domain-containing protein [Exiguobacterium sp. s46]

Protein Classification

COG1708 family protein( domain architecture ID 10004355)

COG1708 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MJ0604 COG1708
Predicted nucleotidyltransferase, MJ0604 family [General function prediction only];
26-122 1.29e-08

Predicted nucleotidyltransferase, MJ0604 family [General function prediction only];


:

Pssm-ID: 441314  Cd Length: 95  Bit Score: 51.18  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048208783  26 RYRAVIQDVVAYVQTLSAFHGVYLYGSVAKGTARPfESDLDFTLILTEPLTEEEHMQLderTEDWLKDypfvtkIDYDIG 105
Cdd:COG1708     4 LLRELLEEIVEALRRGPEVAAVYLFGSYARGDARP-DSDIDLLVVVDDPPLPDERLEL---LADLLRE------LGLPVD 73

                          90
                  ....*....|....*..
gi 2048208783 106 LLrdVMRDDEVLRWGVW 122
Cdd:COG1708    74 LV--VLTPAELELRLFL 88
 
Name Accession Description Interval E-value
MJ0604 COG1708
Predicted nucleotidyltransferase, MJ0604 family [General function prediction only];
26-122 1.29e-08

Predicted nucleotidyltransferase, MJ0604 family [General function prediction only];


Pssm-ID: 441314  Cd Length: 95  Bit Score: 51.18  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048208783  26 RYRAVIQDVVAYVQTLSAFHGVYLYGSVAKGTARPfESDLDFTLILTEPLTEEEHMQLderTEDWLKDypfvtkIDYDIG 105
Cdd:COG1708     4 LLRELLEEIVEALRRGPEVAAVYLFGSYARGDARP-DSDIDLLVVVDDPPLPDERLEL---LADLLRE------LGLPVD 73

                          90
                  ....*....|....*..
gi 2048208783 106 LLrdVMRDDEVLRWGVW 122
Cdd:COG1708    74 LV--VLTPAELELRLFL 88
NT_KNTase_like cd05403
Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, ...
 45-91 5.84e-06

Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins; S. aureus KNTase is a plasmid encoded enzyme which confers resistance to a wide range of aminoglycoside antibiotics which have a 4'- or 4''-hydroxyl group in the equatorial position, such as kanamycin A. This enzyme transfers a nucleoside monophosphate group from a nucleotide (ATP,GTP, or UTP) to the 4'-hydroxyl group of kanamycin A. This enzyme is a homodimer, having two NT active sites. The nucleotide and antibiotic binding sites of each active site include residues from each monomer. Included in this subgroup is Escherichia coli AadA5 which confers resistance to the antibiotic spectinomycin and is a putative aminoglycoside-3'-adenylyltransferase. It is part of the aadA5 cassette of a class 1 integron. This subgroup also includes Haemophilus influenzae HI0073 which forms a 2:2 heterotetramer with an unrelated protein HI0074. Structurally HI0074 is related to the substrate-binding domain of S. aureus KNTase. The genes encoding HI0073 and HI0074 form an operon. Little is known about the substrate specificity or function of two-component NTs. The characterized members of this subgroup may not be representive of the function of this subgroup. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, co-ordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are conserved in this subgroup.


Pssm-ID: 143393  Cd Length: 93  Bit Score: 43.56  E-value: 5.84e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2048208783  45 HGVYLYGSVAKGTARPfESDLDFTLILTEPLTEEEHMQLDERTEDWL 91
Cdd:cd05403    19 EKVYLFGSYARGDARP-DSDIDLLVIFDDPLDPLELARLLEELELLL 64
Polbeta pfam18765
Polymerase beta, Nucleotidyltransferase; A member of the nucleotidyltransferase fold found in ...
 47-117 3.32e-05

Polymerase beta, Nucleotidyltransferase; A member of the nucleotidyltransferase fold found in polymorphic toxins (NTox45) and polyvalent proteins.


Pssm-ID: 465859  Cd Length: 93  Bit Score: 41.74  E-value: 3.32e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2048208783  47 VYLYGSVAKGTARPfESDLDFTLILTEPLTEEEHMQLdertEDWLKDYPFVTKIDY------DIGLLRDVMRDDEVL 117
Cdd:pfam18765  16 AYLFGSRAKGDARE-DSDIDLAVLYDEKLDFEELLEL----ASELEDILLLRKVDLvdlnkaPPVLAHQILKEGKLL 87
 
Name Accession Description Interval E-value
MJ0604 COG1708
Predicted nucleotidyltransferase, MJ0604 family [General function prediction only];
26-122 1.29e-08

Predicted nucleotidyltransferase, MJ0604 family [General function prediction only];


Pssm-ID: 441314  Cd Length: 95  Bit Score: 51.18  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048208783  26 RYRAVIQDVVAYVQTLSAFHGVYLYGSVAKGTARPfESDLDFTLILTEPLTEEEHMQLderTEDWLKDypfvtkIDYDIG 105
Cdd:COG1708     4 LLRELLEEIVEALRRGPEVAAVYLFGSYARGDARP-DSDIDLLVVVDDPPLPDERLEL---LADLLRE------LGLPVD 73

                          90
                  ....*....|....*..
gi 2048208783 106 LLrdVMRDDEVLRWGVW 122
Cdd:COG1708    74 LV--VLTPAELELRLFL 88
MJ0435 COG1669
Predicted nucleotidyltransferase MJ0435 [General function prediction only];
26-123 8.87e-07

Predicted nucleotidyltransferase MJ0435 [General function prediction only];


Pssm-ID: 441275  Cd Length: 96  Bit Score: 46.06  E-value: 8.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048208783  26 RYRAVIQDVVAYVQTLSAFHGV---YLYGSVAKGTARPfESDLDFTLILTEPLTEEEHMQLDERTEDWLKdypfvTKID- 101
Cdd:COG1669     2 NREEILEILREVIEELAERYGVsrlGLFGSVARGEARE-DSDIDLLVEFDEPTSLFDLFELEEELEELLG-----RKVDl 75

                          90       100
                  ....*....|....*....|..
gi 2048208783 102 YDIGLLRDVMRdDEVLRWGVWL 123
Cdd:COG1669    76 VTLDGLSPRLR-ERILKEGVLL 96
NT_KNTase_like cd05403
Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, ...
 45-91 5.84e-06

Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins; S. aureus KNTase is a plasmid encoded enzyme which confers resistance to a wide range of aminoglycoside antibiotics which have a 4'- or 4''-hydroxyl group in the equatorial position, such as kanamycin A. This enzyme transfers a nucleoside monophosphate group from a nucleotide (ATP,GTP, or UTP) to the 4'-hydroxyl group of kanamycin A. This enzyme is a homodimer, having two NT active sites. The nucleotide and antibiotic binding sites of each active site include residues from each monomer. Included in this subgroup is Escherichia coli AadA5 which confers resistance to the antibiotic spectinomycin and is a putative aminoglycoside-3'-adenylyltransferase. It is part of the aadA5 cassette of a class 1 integron. This subgroup also includes Haemophilus influenzae HI0073 which forms a 2:2 heterotetramer with an unrelated protein HI0074. Structurally HI0074 is related to the substrate-binding domain of S. aureus KNTase. The genes encoding HI0073 and HI0074 form an operon. Little is known about the substrate specificity or function of two-component NTs. The characterized members of this subgroup may not be representive of the function of this subgroup. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, co-ordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are conserved in this subgroup.


Pssm-ID: 143393  Cd Length: 93  Bit Score: 43.56  E-value: 5.84e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2048208783  45 HGVYLYGSVAKGTARPfESDLDFTLILTEPLTEEEHMQLDERTEDWL 91
Cdd:cd05403    19 EKVYLFGSYARGDARP-DSDIDLLVIFDDPLDPLELARLLEELELLL 64
Polbeta pfam18765
Polymerase beta, Nucleotidyltransferase; A member of the nucleotidyltransferase fold found in ...
 47-117 3.32e-05

Polymerase beta, Nucleotidyltransferase; A member of the nucleotidyltransferase fold found in polymorphic toxins (NTox45) and polyvalent proteins.


Pssm-ID: 465859  Cd Length: 93  Bit Score: 41.74  E-value: 3.32e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2048208783  47 VYLYGSVAKGTARPfESDLDFTLILTEPLTEEEHMQLdertEDWLKDYPFVTKIDY------DIGLLRDVMRDDEVL 117
Cdd:pfam18765  16 AYLFGSRAKGDARE-DSDIDLAVLYDEKLDFEELLEL----ASELEDILLLRKVDLvdlnkaPPVLAHQILKEGKLL 87
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
 47-93 2.81e-03

Nucleotidyltransferase domain; Members of this family belong to a large family of nucleotidyltransferases. This family includes kanamycin nucleotidyltransferase (KNTase) which is a plasmid-coded enzyme responsible for some types of bacterial resistance to aminoglycosides. KNTase in-activates antibiotics by catalysing the addition of a nucleotidyl group onto the drug.


Pssm-ID: 396474  Cd Length: 91  Bit Score: 36.24  E-value: 2.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2048208783  47 VYLYGSVAKGTARPfESDLDFtLILTEPLTEEEHMQLDERTEDWLKD 93
Cdd:pfam01909  17 VVLFGSYARGTALP-GSDIDL-LVVFPEPVEEERLLKLAKIIKELEE 61
 
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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