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Conserved domains on  [gi|910098713|ref|WP_050002534|]
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nucleotidyltransferase domain-containing protein [Thermococcus eurythermalis]

Protein Classification

nucleotidyltransferase domain-containing protein( domain architecture ID 16068202)

nucleotidyltransferase domain-containing protein similar to Methanocaldococcus jannaschii MJ1547, a HEPN (higher eukaryotes and prokaryotes nucleotide-binding) domain and a cognate MNT (minimal nucleotidyltransferase) domain-containing toxin-antitoxin system

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Polbeta pfam18765
Polymerase beta, Nucleotidyltransferase; A member of the nucleotidyltransferase fold found in ...
12-104 3.64e-18

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: 73.71  E-value: 3.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 910098713   12 EKIIELLREHllkmKEVVFAYLHGSFTED--RPFRDVDIAVYVKGNAPPFYEEELEEELSRLM-GLPVDVRLLNNAPVTF 88
Cdd:pfam18765   1 EKIKEILKKN----PEIEAAYLFGSRAKGdaREDSDIDLAVLYDEKLDFEELLELASELEDILlLRKVDLVDLNKAPPVL 76
                          90
                  ....*....|....*..
gi 910098713   89 RFRAIG-GLLLFSRDER 104
Cdd:pfam18765  77 AHQILKeGKLLYSRDEE 93
 
Name Accession Description Interval E-value
Polbeta pfam18765
Polymerase beta, Nucleotidyltransferase; A member of the nucleotidyltransferase fold found in ...
12-104 3.64e-18

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: 73.71  E-value: 3.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 910098713   12 EKIIELLREHllkmKEVVFAYLHGSFTED--RPFRDVDIAVYVKGNAPPFYEEELEEELSRLM-GLPVDVRLLNNAPVTF 88
Cdd:pfam18765   1 EKIKEILKKN----PEIEAAYLFGSRAKGdaREDSDIDLAVLYDEKLDFEELLELASELEDILlLRKVDLVDLNKAPPVL 76
                          90
                  ....*....|....*..
gi 910098713   89 RFRAIG-GLLLFSRDER 104
Cdd:pfam18765  77 AHQILKeGKLLYSRDEE 93
NT_KNTase_like cd05403
Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, ...
8-93 1.07e-11

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: 57.04  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 910098713   8 KEEKEKIIELLREHLlkmKEVVFAYLHGSFT--EDRPFRDVDIAVYVKGNAPPFYEEELEEELSRLMGLPVDVRLLNNAP 85
Cdd:cd05403    1 EEILEEILEILRELL---GGVEKVYLFGSYArgDARPDSDIDLLVIFDDPLDPLELARLLEELELLLGRPVDLVVLNALE 77

                 ....*...
gi 910098713  86 VTFRFRAI 93
Cdd:cd05403   78 LELLLRIL 85
MJ0604 COG1708
Predicted nucleotidyltransferase, MJ0604 family [General function prediction only];
8-89 1.18e-07

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


Pssm-ID: 441314  Cd Length: 95  Bit Score: 46.56  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 910098713   8 KEEKEKIIELLREHLLKMKEVVFAYLHGSFT--EDRPFRDVDIAVYVKGNAPPFYEEELEEELSRLMGLPVDVRLLNNAP 85
Cdd:COG1708    2 STLLRELLEEIVEALRRGPEVAAVYLFGSYArgDARPDSDIDLLVVVDDPPLPDERLELLADLLRELGLPVDLVVLTPAE 81

                 ....
gi 910098713  86 VTFR 89
Cdd:COG1708   82 LELR 85
 
Name Accession Description Interval E-value
Polbeta pfam18765
Polymerase beta, Nucleotidyltransferase; A member of the nucleotidyltransferase fold found in ...
12-104 3.64e-18

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: 73.71  E-value: 3.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 910098713   12 EKIIELLREHllkmKEVVFAYLHGSFTED--RPFRDVDIAVYVKGNAPPFYEEELEEELSRLM-GLPVDVRLLNNAPVTF 88
Cdd:pfam18765   1 EKIKEILKKN----PEIEAAYLFGSRAKGdaREDSDIDLAVLYDEKLDFEELLELASELEDILlLRKVDLVDLNKAPPVL 76
                          90
                  ....*....|....*..
gi 910098713   89 RFRAIG-GLLLFSRDER 104
Cdd:pfam18765  77 AHQILKeGKLLYSRDEE 93
NT_KNTase_like cd05403
Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, ...
8-93 1.07e-11

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: 57.04  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 910098713   8 KEEKEKIIELLREHLlkmKEVVFAYLHGSFT--EDRPFRDVDIAVYVKGNAPPFYEEELEEELSRLMGLPVDVRLLNNAP 85
Cdd:cd05403    1 EEILEEILEILRELL---GGVEKVYLFGSYArgDARPDSDIDLLVIFDDPLDPLELARLLEELELLLGRPVDLVVLNALE 77

                 ....*...
gi 910098713  86 VTFRFRAI 93
Cdd:cd05403   78 LELLLRIL 85
MJ0604 COG1708
Predicted nucleotidyltransferase, MJ0604 family [General function prediction only];
8-89 1.18e-07

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


Pssm-ID: 441314  Cd Length: 95  Bit Score: 46.56  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 910098713   8 KEEKEKIIELLREHLLKMKEVVFAYLHGSFT--EDRPFRDVDIAVYVKGNAPPFYEEELEEELSRLMGLPVDVRLLNNAP 85
Cdd:COG1708    2 STLLRELLEEIVEALRRGPEVAAVYLFGSYArgDARPDSDIDLLVVVDDPPLPDERLELLADLLRELGLPVDLVVLTPAE 81

                 ....
gi 910098713  86 VTFR 89
Cdd:COG1708   82 LELR 85
MJ0435 COG1669
Predicted nucleotidyltransferase MJ0435 [General function prediction only];
11-93 5.08e-07

Predicted nucleotidyltransferase MJ0435 [General function prediction only];


Pssm-ID: 441275  Cd Length: 96  Bit Score: 44.91  E-value: 5.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 910098713  11 KEKIIELLREHLLKMKE---VVFAYLHGSFT--EDRPFRDVDIAVYVKGNAPPFYEEELEEELSRLMGLPVDVRLLNNAP 85
Cdd:COG1669    3 REEILEILREVIEELAErygVSRLGLFGSVArgEAREDSDIDLLVEFDEPTSLFDLFELEEELEELLGRKVDLVTLDGLS 82

                 ....*...
gi 910098713  86 VTFRFRAI 93
Cdd:COG1669   83 PRLRERIL 90
 
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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