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Conserved domains on  [gi|2793931334|ref|WP_372099041|]
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IS630 family transposase, partial [Vibrio sp. 10N.261.55.C5]

Protein Classification

transposase( domain architecture ID 1750089)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
transpos_IS630 super family cl41314
IS630 family transposase;
18-169 1.25e-44

IS630 family transposase;


The actual alignment was detected with superfamily member NF033545:

Pssm-ID: 468076 [Multi-domain]  Cd Length: 298  Bit Score: 149.71  E-value: 1.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793931334  18 ESVDVWFQDEARFGQQNTTTRLWATRGTR-PRVVKQQQFEYAYLFGSVCPSRGIGEAMVVPWVNKDIMINHLEQISKVTe 96
Cdd:NF033545  142 DPAEVVFIDESGIQLLDTRGRGWAPKGQRrPRVHVYGRRGTLNLFGALDPLTGKVFVLFTGRINSEDFIEFLEELLAAY- 220
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2793931334  97 KDRHSVVIMDGAGWH----TDDIANPFDNVSIIKLPPYSPELNPIEQVWSWLRQHYLANQNFIDYNDIVSKVCSAWN 169
Cdd:NF033545  221 PGKKIHLILDNASTHkskkVREWLEEHGRIELHYLPPYSPWLNPIERVWAVLKRRLLRNRAFRSVDELREAIDAFLN 297
 
Name Accession Description Interval E-value
transpos_IS630 NF033545
IS630 family transposase;
18-169 1.25e-44

IS630 family transposase;


Pssm-ID: 468076 [Multi-domain]  Cd Length: 298  Bit Score: 149.71  E-value: 1.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793931334  18 ESVDVWFQDEARFGQQNTTTRLWATRGTR-PRVVKQQQFEYAYLFGSVCPSRGIGEAMVVPWVNKDIMINHLEQISKVTe 96
Cdd:NF033545  142 DPAEVVFIDESGIQLLDTRGRGWAPKGQRrPRVHVYGRRGTLNLFGALDPLTGKVFVLFTGRINSEDFIEFLEELLAAY- 220
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2793931334  97 KDRHSVVIMDGAGWH----TDDIANPFDNVSIIKLPPYSPELNPIEQVWSWLRQHYLANQNFIDYNDIVSKVCSAWN 169
Cdd:NF033545  221 PGKKIHLILDNASTHkskkVREWLEEHGRIELHYLPPYSPWLNPIERVWAVLKRRLLRNRAFRSVDELREAIDAFLN 297
DDE_3 pfam13358
DDE superfamily endonuclease; This family of proteins are related to pfam00665 and are ...
21-160 5.56e-26

DDE superfamily endonuclease; This family of proteins are related to pfam00665 and are probably endonucleases of the DDE superfamily. 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.


Pssm-ID: 433142 [Multi-domain]  Cd Length: 146  Bit Score: 96.97  E-value: 5.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793931334  21 DVWFQDEARFGQQNTTTRLWATRGTRPRVVKQ-QQFEYAYLFGSVCPSRGIGEAMVVPWVNKDIMINHLEQISKVTEKDR 99
Cdd:pfam13358   1 PLVFLDESGFNLGTVRRYGWAPKGRRPRGLKPyGRGGRVNVIGALTYKGGLAFVTFEETVNAEDFIAFLEQLLKPYLQPK 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2793931334 100 HsVVIMDGAGWHT-----DDIANPFDNVSIIKLPPYSPELNPIEQVWSWLRQHYLANQNFIDYNDI 160
Cdd:pfam13358  81 I-VLVLDNASYHKskavrELVEAEADGLELHYLPPYSPELNPIEILWSVLKRELLNNRRFKDLEEL 145
COG3335 COG3335
Transposase [Mobilome: prophages, transposons];
59-185 4.90e-19

Transposase [Mobilome: prophages, transposons];


Pssm-ID: 442564 [Multi-domain]  Cd Length: 292  Bit Score: 82.22  E-value: 4.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793931334  59 YLFGSVCPSRGIGEAMVVPWVNKDIMINHLEQIsKVTEKDRHSVVIMDGAGWHTDDIANPF---DNVSIIKLPPYSPELN 135
Cdd:COG3335   160 NLIGALNLDGGLAVMVFDGSINGEVFIAFLEQL-LLPYLKPGIVVILDNASFHKSKAVREWleeAGIELLFLPPYSPDLN 238
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2793931334 136 PIEQVWSWLRQHYLANQNFIDYNDIVSKVCSAWNGFLECKDRVTKMCTRD 185
Cdd:COG3335   239 PIERLWSKLKALLRKNRAFRSKDELKAAVRSFLDRISPDPERVRNWFRHA 288
 
Name Accession Description Interval E-value
transpos_IS630 NF033545
IS630 family transposase;
18-169 1.25e-44

IS630 family transposase;


Pssm-ID: 468076 [Multi-domain]  Cd Length: 298  Bit Score: 149.71  E-value: 1.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793931334  18 ESVDVWFQDEARFGQQNTTTRLWATRGTR-PRVVKQQQFEYAYLFGSVCPSRGIGEAMVVPWVNKDIMINHLEQISKVTe 96
Cdd:NF033545  142 DPAEVVFIDESGIQLLDTRGRGWAPKGQRrPRVHVYGRRGTLNLFGALDPLTGKVFVLFTGRINSEDFIEFLEELLAAY- 220
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2793931334  97 KDRHSVVIMDGAGWH----TDDIANPFDNVSIIKLPPYSPELNPIEQVWSWLRQHYLANQNFIDYNDIVSKVCSAWN 169
Cdd:NF033545  221 PGKKIHLILDNASTHkskkVREWLEEHGRIELHYLPPYSPWLNPIERVWAVLKRRLLRNRAFRSVDELREAIDAFLN 297
DDE_3 pfam13358
DDE superfamily endonuclease; This family of proteins are related to pfam00665 and are ...
21-160 5.56e-26

DDE superfamily endonuclease; This family of proteins are related to pfam00665 and are probably endonucleases of the DDE superfamily. 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.


Pssm-ID: 433142 [Multi-domain]  Cd Length: 146  Bit Score: 96.97  E-value: 5.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793931334  21 DVWFQDEARFGQQNTTTRLWATRGTRPRVVKQ-QQFEYAYLFGSVCPSRGIGEAMVVPWVNKDIMINHLEQISKVTEKDR 99
Cdd:pfam13358   1 PLVFLDESGFNLGTVRRYGWAPKGRRPRGLKPyGRGGRVNVIGALTYKGGLAFVTFEETVNAEDFIAFLEQLLKPYLQPK 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2793931334 100 HsVVIMDGAGWHT-----DDIANPFDNVSIIKLPPYSPELNPIEQVWSWLRQHYLANQNFIDYNDI 160
Cdd:pfam13358  81 I-VLVLDNASYHKskavrELVEAEADGLELHYLPPYSPELNPIEILWSVLKRELLNNRRFKDLEEL 145
COG3335 COG3335
Transposase [Mobilome: prophages, transposons];
59-185 4.90e-19

Transposase [Mobilome: prophages, transposons];


Pssm-ID: 442564 [Multi-domain]  Cd Length: 292  Bit Score: 82.22  E-value: 4.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793931334  59 YLFGSVCPSRGIGEAMVVPWVNKDIMINHLEQIsKVTEKDRHSVVIMDGAGWHTDDIANPF---DNVSIIKLPPYSPELN 135
Cdd:COG3335   160 NLIGALNLDGGLAVMVFDGSINGEVFIAFLEQL-LLPYLKPGIVVILDNASFHKSKAVREWleeAGIELLFLPPYSPDLN 238
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2793931334 136 PIEQVWSWLRQHYLANQNFIDYNDIVSKVCSAWNGFLECKDRVTKMCTRD 185
Cdd:COG3335   239 PIERLWSKLKALLRKNRAFRSKDELKAAVRSFLDRISPDPERVRNWFRHA 288
 
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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