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Conserved domains on  [gi|1778752171|ref|WP_154915079|]
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Mu transposase C-terminal domain-containing protein [Klebsiella grimontii]

Protein Classification

transposase( domain architecture ID 19300204)

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
Mu-transpos_C pfam09299
Mu transposase, C-terminal; Members of this family are found in various prokaryotic integrases ...
531-591 1.03e-20

Mu transposase, C-terminal; Members of this family are found in various prokaryotic integrases and transposases. They adopt a beta-barrel structure with Greek-key topology.


:

Pssm-ID: 430512  Cd Length: 61  Bit Score: 86.05  E-value: 1.03e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1778752171 531 RHMFMPETECSVRRCEIQLFNNLYYSEALREEHGRKVRVSYDIHDATKIIVRRMDGSLICE 591
Cdd:pfam09299   1 DLLLLPRETRTVQRDGIRLFGNRYWSPELAGYVGEKVVVRYDPRDLSRIYVYDLDGRFICE 61
HTH_MerR-SF super family cl02600
Helix-Turn-Helix DNA binding domain of transcription regulators from the MerR superfamily; ...
7-137 2.35e-09

Helix-Turn-Helix DNA binding domain of transcription regulators from the MerR superfamily; Helix-turn-helix (HTH) transcription regulator MerR superfamily, N-terminal domain. The MerR family transcription regulators have been shown to mediate responses to stress including exposure to heavy metals, drugs, or oxygen radicals in eubacterial and some archaeal species. They regulate transcription of multidrug/metal ion transporter genes and oxidative stress regulons by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates.


The actual alignment was detected with superfamily member pfam02316:

Pssm-ID: 470628  Cd Length: 134  Bit Score: 56.14  E-value: 2.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778752171   7 ELAGLPGLPGTPQGIRAMMGKLVKQNQTLvRKRQGSKAFEYHIDSLPLVAQKALRDRQvkelmNNQDAAL-PAPECSAVT 85
Cdd:pfam02316   2 ELAGLPGLPKTSAGVIYVAKKQGWQKQKR-AGVKGGKAYEYHVNSLPVETRAALLLRQ-----GEIGASLgEKEIARPTV 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1778752171  86 EKSDTRLslyrdhpvlmEQKLTGLTSD-QQKIADARIALVSEVMKLGEIPGFS 137
Cdd:pfam02316  76 ETHDYRL----------EALWSKLEPDeQRRAAEALMPAVQAADKMLNQGGSS 118
Tra5 super family cl34487
Transposase InsO and inactivated derivatives [Mobilome: prophages, transposons];
328-512 3.61e-07

Transposase InsO and inactivated derivatives [Mobilome: prophages, transposons];


The actual alignment was detected with superfamily member COG2801:

Pssm-ID: 442053 [Multi-domain]  Cd Length: 309  Bit Score: 52.46  E-value: 3.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778752171 328 VTFILDGSCRYIVGWSLALSESVIAVADALRHGIKNNGVPY--IYYSDNGGGETNSTLdaniTGILPRLGVDHRLGIPEN 405
Cdd:COG2801   168 LAAVIDLFSREIVGWSVSDSMDAELVVDALEMAIERRGPPKplILHSDNGSQYTSKAY----QELLKKLGITQSMSRPGN 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778752171 406 PQGRGIIEILNKTLgmrisrqfatyygtgadksttrkvsksliaalnavdkgreltaKQE-QTLRDFPSWNELIGEIEAG 484
Cdd:COG2801   244 PQDNAFIESFFGTL-------------------------------------------KYElLYRRRFESLEEAREAIEEY 280
                         170       180
                  ....*....|....*....|....*....
gi 1778752171 485 VHWYNN-RAHESLplkangEHFTPAQFRK 512
Cdd:COG2801   281 IEFYNHeRPHSSL------GYLTPAEYEK 303
 
Name Accession Description Interval E-value
Mu-transpos_C pfam09299
Mu transposase, C-terminal; Members of this family are found in various prokaryotic integrases ...
531-591 1.03e-20

Mu transposase, C-terminal; Members of this family are found in various prokaryotic integrases and transposases. They adopt a beta-barrel structure with Greek-key topology.


Pssm-ID: 430512  Cd Length: 61  Bit Score: 86.05  E-value: 1.03e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1778752171 531 RHMFMPETECSVRRCEIQLFNNLYYSEALREEHGRKVRVSYDIHDATKIIVRRMDGSLICE 591
Cdd:pfam09299   1 DLLLLPRETRTVQRDGIRLFGNRYWSPELAGYVGEKVVVRYDPRDLSRIYVYDLDGRFICE 61
HTH_Tnp_Mu_1 pfam02316
Mu DNA-binding domain; This family consists of MuA-transposase and repressor protein CI. These ...
7-137 2.35e-09

Mu DNA-binding domain; This family consists of MuA-transposase and repressor protein CI. These proteins contain homologous DNA-binding domains at their N-termini which compete for the same DNA site within the Mu bacteriophage genome.


Pssm-ID: 367032  Cd Length: 134  Bit Score: 56.14  E-value: 2.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778752171   7 ELAGLPGLPGTPQGIRAMMGKLVKQNQTLvRKRQGSKAFEYHIDSLPLVAQKALRDRQvkelmNNQDAAL-PAPECSAVT 85
Cdd:pfam02316   2 ELAGLPGLPKTSAGVIYVAKKQGWQKQKR-AGVKGGKAYEYHVNSLPVETRAALLLRQ-----GEIGASLgEKEIARPTV 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1778752171  86 EKSDTRLslyrdhpvlmEQKLTGLTSD-QQKIADARIALVSEVMKLGEIPGFS 137
Cdd:pfam02316  76 ETHDYRL----------EALWSKLEPDeQRRAAEALMPAVQAADKMLNQGGSS 118
Tra5 COG2801
Transposase InsO and inactivated derivatives [Mobilome: prophages, transposons];
328-512 3.61e-07

Transposase InsO and inactivated derivatives [Mobilome: prophages, transposons];


Pssm-ID: 442053 [Multi-domain]  Cd Length: 309  Bit Score: 52.46  E-value: 3.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778752171 328 VTFILDGSCRYIVGWSLALSESVIAVADALRHGIKNNGVPY--IYYSDNGGGETNSTLdaniTGILPRLGVDHRLGIPEN 405
Cdd:COG2801   168 LAAVIDLFSREIVGWSVSDSMDAELVVDALEMAIERRGPPKplILHSDNGSQYTSKAY----QELLKKLGITQSMSRPGN 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778752171 406 PQGRGIIEILNKTLgmrisrqfatyygtgadksttrkvsksliaalnavdkgreltaKQE-QTLRDFPSWNELIGEIEAG 484
Cdd:COG2801   244 PQDNAFIESFFGTL-------------------------------------------KYElLYRRRFESLEEAREAIEEY 280
                         170       180
                  ....*....|....*....|....*....
gi 1778752171 485 VHWYNN-RAHESLplkangEHFTPAQFRK 512
Cdd:COG2801   281 IEFYNHeRPHSSL------GYLTPAEYEK 303
transpos_IS3 NF033516
IS3 family transposase;
328-511 2.24e-04

IS3 family transposase;


Pssm-ID: 468052 [Multi-domain]  Cd Length: 369  Bit Score: 44.09  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778752171 328 VTFILDGSCRYIVGWSLALSESVIAVADALRHGIKNNGVPY--IYYSDNGGGETNSTLDAnitgILPRLGVDHRLGIPEN 405
Cdd:NF033516  235 LAVVLDLFSREIVGWSVSTSMSAELVLDALEMAIEWRGKPEglILHSDNGSQYTSKAYRE----WLKEHGITQSMSRPGN 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778752171 406 PQGRGIIEILNKTLgmrisrqfatyygtgadksttrkvsksliaalnavdkgreltaKQE-QTLRDFPSWNELIGEIEAG 484
Cdd:NF033516  311 CWDNAVAESFFGTL-------------------------------------------KREcLYRRRFRTLEEARQAIEEY 347
                         170       180
                  ....*....|....*....|....*...
gi 1778752171 485 VHWYNN-RAHESLplkaNGEhfTPAQFR 511
Cdd:NF033516  348 IEFYNHeRPHSSL----GYL--TPAEFE 369
PHA02517 PHA02517
putative transposase OrfB; Reviewed
272-419 6.49e-04

putative transposase OrfB; Reviewed


Pssm-ID: 222853 [Multi-domain]  Cd Length: 277  Bit Score: 42.16  E-value: 6.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778752171 272 VVKQHRRITGS-EARQIEGFVRRDWLCLPVNYVWIGDghgmkMKVASPEHGnpiTPEVTFILDGSCRYIVGWSLALSESV 350
Cdd:PHA02517   80 LRGKKVRTTISrKAVAAPDRVNRQFVATRPNQLWVAD-----FTYVSTWQG---WVYVAFIIDVFARRIVGWRVSSSMDT 151
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1778752171 351 IAVADALRHGIKNNGVP--YIYYSDNGGGETNStldaNITGILPRLGVDHRLGIPENPQGRGIIEILNKTL 419
Cdd:PHA02517  152 DFVLDALEQALWARGRPggLIHHSDKGSQYVSL----AYTQRLKEAGIRASTGSRGDSYDNAPAESINGLY 218
rve pfam00665
Integrase core domain; Integrase mediates integration of a DNA copy of the viral genome into ...
300-406 1.40e-03

Integrase core domain; Integrase mediates integration of a DNA copy of the viral genome into the host chromosome. Integrase is composed of three domains. The amino-terminal domain is a zinc binding domain pfam02022. This domain is the central catalytic domain. The carboxyl terminal domain that is a non-specific DNA binding domain pfam00552. The catalytic domain acts as an endonuclease when two nucleotides are removed from the 3' ends of the blunt-ended viral DNA made by reverse transcription. This domain also catalyzes the DNA strand transfer reaction of the 3' ends of the viral DNA to the 5' ends of the integration site.


Pssm-ID: 459897 [Multi-domain]  Cd Length: 98  Bit Score: 38.45  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778752171 300 VNYVWIGDGhgmkMKVASPEHGNPITpeVTFILDGSCRYIVGWSLALSESVIAVADALRHGIKN-NGVPYIYYSDNGGGE 378
Cdd:pfam00665   1 PNQLWQGDF----TYIRIPGGGGKLY--LLVIVDDFSREILAWALSSEMDAELVLDALERAIAFrGGVPLIIHSDNGSEY 74
                          90       100
                  ....*....|....*....|....*...
gi 1778752171 379 TNSTLDAnitgILPRLGVDHRLGIPENP 406
Cdd:pfam00665  75 TSKAFRE----FLKDLGIKPSFSRPGNP 98
 
Name Accession Description Interval E-value
Mu-transpos_C pfam09299
Mu transposase, C-terminal; Members of this family are found in various prokaryotic integrases ...
531-591 1.03e-20

Mu transposase, C-terminal; Members of this family are found in various prokaryotic integrases and transposases. They adopt a beta-barrel structure with Greek-key topology.


Pssm-ID: 430512  Cd Length: 61  Bit Score: 86.05  E-value: 1.03e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1778752171 531 RHMFMPETECSVRRCEIQLFNNLYYSEALREEHGRKVRVSYDIHDATKIIVRRMDGSLICE 591
Cdd:pfam09299   1 DLLLLPRETRTVQRDGIRLFGNRYWSPELAGYVGEKVVVRYDPRDLSRIYVYDLDGRFICE 61
HTH_Tnp_Mu_1 pfam02316
Mu DNA-binding domain; This family consists of MuA-transposase and repressor protein CI. These ...
7-137 2.35e-09

Mu DNA-binding domain; This family consists of MuA-transposase and repressor protein CI. These proteins contain homologous DNA-binding domains at their N-termini which compete for the same DNA site within the Mu bacteriophage genome.


Pssm-ID: 367032  Cd Length: 134  Bit Score: 56.14  E-value: 2.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778752171   7 ELAGLPGLPGTPQGIRAMMGKLVKQNQTLvRKRQGSKAFEYHIDSLPLVAQKALRDRQvkelmNNQDAAL-PAPECSAVT 85
Cdd:pfam02316   2 ELAGLPGLPKTSAGVIYVAKKQGWQKQKR-AGVKGGKAYEYHVNSLPVETRAALLLRQ-----GEIGASLgEKEIARPTV 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1778752171  86 EKSDTRLslyrdhpvlmEQKLTGLTSD-QQKIADARIALVSEVMKLGEIPGFS 137
Cdd:pfam02316  76 ETHDYRL----------EALWSKLEPDeQRRAAEALMPAVQAADKMLNQGGSS 118
Tra5 COG2801
Transposase InsO and inactivated derivatives [Mobilome: prophages, transposons];
328-512 3.61e-07

Transposase InsO and inactivated derivatives [Mobilome: prophages, transposons];


Pssm-ID: 442053 [Multi-domain]  Cd Length: 309  Bit Score: 52.46  E-value: 3.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778752171 328 VTFILDGSCRYIVGWSLALSESVIAVADALRHGIKNNGVPY--IYYSDNGGGETNSTLdaniTGILPRLGVDHRLGIPEN 405
Cdd:COG2801   168 LAAVIDLFSREIVGWSVSDSMDAELVVDALEMAIERRGPPKplILHSDNGSQYTSKAY----QELLKKLGITQSMSRPGN 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778752171 406 PQGRGIIEILNKTLgmrisrqfatyygtgadksttrkvsksliaalnavdkgreltaKQE-QTLRDFPSWNELIGEIEAG 484
Cdd:COG2801   244 PQDNAFIESFFGTL-------------------------------------------KYElLYRRRFESLEEAREAIEEY 280
                         170       180
                  ....*....|....*....|....*....
gi 1778752171 485 VHWYNN-RAHESLplkangEHFTPAQFRK 512
Cdd:COG2801   281 IEFYNHeRPHSSL------GYLTPAEYEK 303
transpos_IS3 NF033516
IS3 family transposase;
328-511 2.24e-04

IS3 family transposase;


Pssm-ID: 468052 [Multi-domain]  Cd Length: 369  Bit Score: 44.09  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778752171 328 VTFILDGSCRYIVGWSLALSESVIAVADALRHGIKNNGVPY--IYYSDNGGGETNSTLDAnitgILPRLGVDHRLGIPEN 405
Cdd:NF033516  235 LAVVLDLFSREIVGWSVSTSMSAELVLDALEMAIEWRGKPEglILHSDNGSQYTSKAYRE----WLKEHGITQSMSRPGN 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778752171 406 PQGRGIIEILNKTLgmrisrqfatyygtgadksttrkvsksliaalnavdkgreltaKQE-QTLRDFPSWNELIGEIEAG 484
Cdd:NF033516  311 CWDNAVAESFFGTL-------------------------------------------KREcLYRRRFRTLEEARQAIEEY 347
                         170       180
                  ....*....|....*....|....*...
gi 1778752171 485 VHWYNN-RAHESLplkaNGEhfTPAQFR 511
Cdd:NF033516  348 IEFYNHeRPHSSL----GYL--TPAEFE 369
PHA02517 PHA02517
putative transposase OrfB; Reviewed
272-419 6.49e-04

putative transposase OrfB; Reviewed


Pssm-ID: 222853 [Multi-domain]  Cd Length: 277  Bit Score: 42.16  E-value: 6.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778752171 272 VVKQHRRITGS-EARQIEGFVRRDWLCLPVNYVWIGDghgmkMKVASPEHGnpiTPEVTFILDGSCRYIVGWSLALSESV 350
Cdd:PHA02517   80 LRGKKVRTTISrKAVAAPDRVNRQFVATRPNQLWVAD-----FTYVSTWQG---WVYVAFIIDVFARRIVGWRVSSSMDT 151
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1778752171 351 IAVADALRHGIKNNGVP--YIYYSDNGGGETNStldaNITGILPRLGVDHRLGIPENPQGRGIIEILNKTL 419
Cdd:PHA02517  152 DFVLDALEQALWARGRPggLIHHSDKGSQYVSL----AYTQRLKEAGIRASTGSRGDSYDNAPAESINGLY 218
rve pfam00665
Integrase core domain; Integrase mediates integration of a DNA copy of the viral genome into ...
300-406 1.40e-03

Integrase core domain; Integrase mediates integration of a DNA copy of the viral genome into the host chromosome. Integrase is composed of three domains. The amino-terminal domain is a zinc binding domain pfam02022. This domain is the central catalytic domain. The carboxyl terminal domain that is a non-specific DNA binding domain pfam00552. The catalytic domain acts as an endonuclease when two nucleotides are removed from the 3' ends of the blunt-ended viral DNA made by reverse transcription. This domain also catalyzes the DNA strand transfer reaction of the 3' ends of the viral DNA to the 5' ends of the integration site.


Pssm-ID: 459897 [Multi-domain]  Cd Length: 98  Bit Score: 38.45  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778752171 300 VNYVWIGDGhgmkMKVASPEHGNPITpeVTFILDGSCRYIVGWSLALSESVIAVADALRHGIKN-NGVPYIYYSDNGGGE 378
Cdd:pfam00665   1 PNQLWQGDF----TYIRIPGGGGKLY--LLVIVDDFSREILAWALSSEMDAELVLDALERAIAFrGGVPLIIHSDNGSEY 74
                          90       100
                  ....*....|....*....|....*...
gi 1778752171 379 TNSTLDAnitgILPRLGVDHRLGIPENP 406
Cdd:pfam00665  75 TSKAFRE----FLKDLGIKPSFSRPGNP 98
 
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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