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Conserved domains on  [gi|2335495012|ref|WP_265895039|]
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transposase, partial [Klebsiella variicola]

Protein Classification

transposase( domain architecture ID 1750097)

IS5 family transposase binds to the end of a transposon and catalyzes the movement of the transposon to another part of the genome by a cut and paste mechanism or a replicative transposition mechanism

Gene Ontology:  GO:0003677|GO:0032196
PubMed:  20215432|30454069

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
transpos_IS5_2 super family cl41331
IS5 family transposase;
1-77 1.04e-32

IS5 family transposase;


The actual alignment was detected with superfamily member NF033579:

Pssm-ID: 468096 [Multi-domain]  Cd Length: 287  Bit Score: 113.53  E-value: 1.04e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2335495012   1 WRKLHLAVDSNTHEIICADLSLNNVTDSEAFPGLIRQTHRKIRAASADGAYDTRLCHDELRRKKISALIPPRKGAGY 77
Cdd:NF033579  139 WRKVHLAVDVKTGEILAVEVTTNKVHDAKVLPDLLRQIPEDIDSVLADGAYDTKKCHEAIRERGARPLIPPRKNARL 215
 
Name Accession Description Interval E-value
transpos_IS5_2 NF033579
IS5 family transposase;
1-77 1.04e-32

IS5 family transposase;


Pssm-ID: 468096 [Multi-domain]  Cd Length: 287  Bit Score: 113.53  E-value: 1.04e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2335495012   1 WRKLHLAVDSNTHEIICADLSLNNVTDSEAFPGLIRQTHRKIRAASADGAYDTRLCHDELRRKKISALIPPRKGAGY 77
Cdd:NF033579  139 WRKVHLAVDVKTGEILAVEVTTNKVHDAKVLPDLLRQIPEDIDSVLADGAYDTKKCHEAIRERGARPLIPPRKNARL 215
DDE_Tnp_1 pfam01609
Transposase DDE domain; Transposase proteins are necessary for efficient DNA transposition. ...
1-76 2.21e-12

Transposase DDE domain; Transposase proteins are necessary for efficient DNA transposition. This domain is a member of the DDE superfamily, which contain three carboxylate residues that are believed to be responsible for coordinating metal ions needed for catalysis. The catalytic activity of this enzyme involves DNA cleavage at a specific site followed by a strand transfer reaction. This family contains transposases for IS4, IS421, IS5377, IS427, IS402, IS1355, IS5, which was original isolated in bacteriophage lambda.


Pssm-ID: 376573 [Multi-domain]  Cd Length: 196  Bit Score: 58.79  E-value: 2.21e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2335495012   1 WRKLHLAVDSNTHEIICADLSLNNVTDSEAFPGLIRQT-HRKIRAASADGAYDTRLCHDELRRKKISALIPPRKGAG 76
Cdd:pfam01609  35 GYKLHIAVDTRTGLILAVVLTPGNVHDSKGLLQLLDELrRRKGRLVLADAGYGGKELLDKLEEKGVDYLIRLKKNAK 111
transpos_IS5_3 NF033580
IS5 family transposase;
2-73 1.70e-05

IS5 family transposase;


Pssm-ID: 468097 [Multi-domain]  Cd Length: 257  Bit Score: 40.64  E-value: 1.70e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2335495012   2 RKLHLAVDSNTHeIICADLSLNNVTDSEAFPGLI----RQTHRKIRAASADGAYDTRLCHDELRRKKISALIPPRK 73
Cdd:NF033580  128 TKIHIAVDALGL-PLAFVLTGANVHDSKGALPLLdglpVLRPPRPKHLLADKGYDSDALRAALRERGAVPVIPRRR 202
 
Name Accession Description Interval E-value
transpos_IS5_2 NF033579
IS5 family transposase;
1-77 1.04e-32

IS5 family transposase;


Pssm-ID: 468096 [Multi-domain]  Cd Length: 287  Bit Score: 113.53  E-value: 1.04e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2335495012   1 WRKLHLAVDSNTHEIICADLSLNNVTDSEAFPGLIRQTHRKIRAASADGAYDTRLCHDELRRKKISALIPPRKGAGY 77
Cdd:NF033579  139 WRKVHLAVDVKTGEILAVEVTTNKVHDAKVLPDLLRQIPEDIDSVLADGAYDTKKCHEAIRERGARPLIPPRKNARL 215
DDE_Tnp_1 pfam01609
Transposase DDE domain; Transposase proteins are necessary for efficient DNA transposition. ...
1-76 2.21e-12

Transposase DDE domain; Transposase proteins are necessary for efficient DNA transposition. This domain is a member of the DDE superfamily, which contain three carboxylate residues that are believed to be responsible for coordinating metal ions needed for catalysis. The catalytic activity of this enzyme involves DNA cleavage at a specific site followed by a strand transfer reaction. This family contains transposases for IS4, IS421, IS5377, IS427, IS402, IS1355, IS5, which was original isolated in bacteriophage lambda.


Pssm-ID: 376573 [Multi-domain]  Cd Length: 196  Bit Score: 58.79  E-value: 2.21e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2335495012   1 WRKLHLAVDSNTHEIICADLSLNNVTDSEAFPGLIRQT-HRKIRAASADGAYDTRLCHDELRRKKISALIPPRKGAG 76
Cdd:pfam01609  35 GYKLHIAVDTRTGLILAVVLTPGNVHDSKGLLQLLDELrRRKGRLVLADAGYGGKELLDKLEEKGVDYLIRLKKNAK 111
transpos_IS5_3 NF033580
IS5 family transposase;
2-73 1.70e-05

IS5 family transposase;


Pssm-ID: 468097 [Multi-domain]  Cd Length: 257  Bit Score: 40.64  E-value: 1.70e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2335495012   2 RKLHLAVDSNTHeIICADLSLNNVTDSEAFPGLI----RQTHRKIRAASADGAYDTRLCHDELRRKKISALIPPRK 73
Cdd:NF033580  128 TKIHIAVDALGL-PLAFVLTGANVHDSKGALPLLdglpVLRPPRPKHLLADKGYDSDALRAALRERGAVPVIPRRR 202
 
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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