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Conserved domains on  [gi|1376784323|gb|PTP78493|]
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hypothetical protein CWO23_00795 [Vibrio splendidus]

Protein Classification

Tn7 transposase TnsA N-terminal domain-containing protein( domain architecture ID 10555234)

Tn7 transposase TnsA N-terminal catalytic domain-containing protein is part of Tn7 transposase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tn7_TnsA-like_N pfam08722
TnsA-like endonuclease N terminal; The Tn7 transposase is composed of proteins TnsA and TnsB. ...
46-120 8.41e-10

TnsA-like endonuclease N terminal; The Tn7 transposase is composed of proteins TnsA and TnsB. DNA breakage at the 5' end of the transposon is carried out by TnsA, and breakage and joining at the 3' end is carried out by TnsB. The N terminal domain of TnsA is catalytic. This domain is also found in Bacteriophage T4 gp4-like head completion protein whose nuclease activity is required for packaging. This domain contains the catalytic triad of one basic and two acidic residues that form a restriction endonuclease-like active site and conserved between TnsA with gp4 proteins.


:

Pssm-ID: 462579 [Multi-domain]  Cd Length: 83  Bit Score: 53.38  E-value: 8.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376784323  46 DVVSFESQPKGFLY--DFDGKQLPYTPDFFVIYTDGC---YSFVETKPYSKTLS--KEFKLKFRARKQAAKKLGFDLILV 118
Cdd:pfam08722   2 DVIDIREQPLTIPYasELGIKTRVYTPDFLVTYKDGDgkpYEAIEVKPSKDLEDwlLRTLEKLEAAREYWEERGIPFRII 81

                  ..
gi 1376784323 119 TD 120
Cdd:pfam08722  82 TE 83
 
Name Accession Description Interval E-value
Tn7_TnsA-like_N pfam08722
TnsA-like endonuclease N terminal; The Tn7 transposase is composed of proteins TnsA and TnsB. ...
46-120 8.41e-10

TnsA-like endonuclease N terminal; The Tn7 transposase is composed of proteins TnsA and TnsB. DNA breakage at the 5' end of the transposon is carried out by TnsA, and breakage and joining at the 3' end is carried out by TnsB. The N terminal domain of TnsA is catalytic. This domain is also found in Bacteriophage T4 gp4-like head completion protein whose nuclease activity is required for packaging. This domain contains the catalytic triad of one basic and two acidic residues that form a restriction endonuclease-like active site and conserved between TnsA with gp4 proteins.


Pssm-ID: 462579 [Multi-domain]  Cd Length: 83  Bit Score: 53.38  E-value: 8.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376784323  46 DVVSFESQPKGFLY--DFDGKQLPYTPDFFVIYTDGC---YSFVETKPYSKTLS--KEFKLKFRARKQAAKKLGFDLILV 118
Cdd:pfam08722   2 DVIDIREQPLTIPYasELGIKTRVYTPDFLVTYKDGDgkpYEAIEVKPSKDLEDwlLRTLEKLEAAREYWEERGIPFRII 81

                  ..
gi 1376784323 119 TD 120
Cdd:pfam08722  82 TE 83
 
Name Accession Description Interval E-value
Tn7_TnsA-like_N pfam08722
TnsA-like endonuclease N terminal; The Tn7 transposase is composed of proteins TnsA and TnsB. ...
46-120 8.41e-10

TnsA-like endonuclease N terminal; The Tn7 transposase is composed of proteins TnsA and TnsB. DNA breakage at the 5' end of the transposon is carried out by TnsA, and breakage and joining at the 3' end is carried out by TnsB. The N terminal domain of TnsA is catalytic. This domain is also found in Bacteriophage T4 gp4-like head completion protein whose nuclease activity is required for packaging. This domain contains the catalytic triad of one basic and two acidic residues that form a restriction endonuclease-like active site and conserved between TnsA with gp4 proteins.


Pssm-ID: 462579 [Multi-domain]  Cd Length: 83  Bit Score: 53.38  E-value: 8.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376784323  46 DVVSFESQPKGFLY--DFDGKQLPYTPDFFVIYTDGC---YSFVETKPYSKTLS--KEFKLKFRARKQAAKKLGFDLILV 118
Cdd:pfam08722   2 DVIDIREQPLTIPYasELGIKTRVYTPDFLVTYKDGDgkpYEAIEVKPSKDLEDwlLRTLEKLEAAREYWEERGIPFRII 81

                  ..
gi 1376784323 119 TD 120
Cdd:pfam08722  82 TE 83
 
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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