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Conserved domains on  [gi|1755806350|gb|QEZ85331|]
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ImmA/IrrE family metallo-endopeptidase [Listeria monocytogenes]

Protein Classification

M78 family metallopeptidase domain-containing protein( domain architecture ID 1522)

M78 family metallopeptidase domain-containing protein which includes the catalytic domain of ImmA/IrrE family metallo-endopeptidase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_M78 super family cl01076
IrrE N-terminal-like domain; This entry includes the catalytic domain of the protein ImmA, ...
 13-121 4.55e-09

IrrE N-terminal-like domain; This entry includes the catalytic domain of the protein ImmA, which is a metallopeptidase containing an HEXXH zinc-binding motif from peptidase family M78. ImmA is encoded on a conjugative transposon. Conjugating bacteria are able to transfer conjugative transposons that can, for example, confer resistance to antibiotics. The transposon is integrated into the chromosome, but during conjugation excises itself and then moves to the recipient bacterium and re-integrate into its chromosome. Typically a conjugative tranposon encodes only the proteins required for this activity and the proteins that regulate it. During exponential growth, the ICEBs1 transposon of Bacillus subtilis is inactivated by the immunity repressor protein ImmR, which is encoded by the transposon and represses the genes for excision and transfer. Cleavage of ImmR relaxes repression and allows transfer of the transposon. ImmA has been shown to be essential for the cleavage of ImmR. This domain is also found in in metalloprotease IrrE, a central regulator of DNA damage repair in Deinococcaceae, HTH-type transcriptional regulators RamB and PrpC.


The actual alignment was detected with superfamily member pfam06114:

Pssm-ID: 470062  Cd Length: 122  Bit Score: 51.27  E-value: 4.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755806350  13 VTIREEKMP----YKLPGLYLNGTIFISKDQSSIEKGCVLVEELMHYKYTVGNITKQETIMDK---KQEIFARRKGYEEL 85
Cdd:pfam06114   6 IRVFFLPLGaedgDGRRFDRHTPVIFLNENLSPTRQRFTLAHELGHLLLHEGGDTLSDQFDFKtaeAREREANIFAAALL 85

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1755806350  86 IPLDDIIACFYLGLREYF-EVAEFLEVTEDFLRHTVS 121
Cdd:pfam06114  86 MPYEAFLAAAETLRYDLElLLAERFGVSYEAVAHRLS 122
 
Name Accession Description Interval E-value
Peptidase_M78 pfam06114
IrrE N-terminal-like domain; This entry includes the catalytic domain of the protein ImmA, ...
 13-121 4.55e-09

IrrE N-terminal-like domain; This entry includes the catalytic domain of the protein ImmA, which is a metallopeptidase containing an HEXXH zinc-binding motif from peptidase family M78. ImmA is encoded on a conjugative transposon. Conjugating bacteria are able to transfer conjugative transposons that can, for example, confer resistance to antibiotics. The transposon is integrated into the chromosome, but during conjugation excises itself and then moves to the recipient bacterium and re-integrate into its chromosome. Typically a conjugative tranposon encodes only the proteins required for this activity and the proteins that regulate it. During exponential growth, the ICEBs1 transposon of Bacillus subtilis is inactivated by the immunity repressor protein ImmR, which is encoded by the transposon and represses the genes for excision and transfer. Cleavage of ImmR relaxes repression and allows transfer of the transposon. ImmA has been shown to be essential for the cleavage of ImmR. This domain is also found in in metalloprotease IrrE, a central regulator of DNA damage repair in Deinococcaceae, HTH-type transcriptional regulators RamB and PrpC.


Pssm-ID: 399250  Cd Length: 122  Bit Score: 51.27  E-value: 4.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755806350  13 VTIREEKMP----YKLPGLYLNGTIFISKDQSSIEKGCVLVEELMHYKYTVGNITKQETIMDK---KQEIFARRKGYEEL 85
Cdd:pfam06114   6 IRVFFLPLGaedgDGRRFDRHTPVIFLNENLSPTRQRFTLAHELGHLLLHEGGDTLSDQFDFKtaeAREREANIFAAALL 85

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1755806350  86 IPLDDIIACFYLGLREYF-EVAEFLEVTEDFLRHTVS 121
Cdd:pfam06114  86 MPYEAFLAAAETLRYDLElLLAERFGVSYEAVAHRLS 122
 
Name Accession Description Interval E-value
Peptidase_M78 pfam06114
IrrE N-terminal-like domain; This entry includes the catalytic domain of the protein ImmA, ...
 13-121 4.55e-09

IrrE N-terminal-like domain; This entry includes the catalytic domain of the protein ImmA, which is a metallopeptidase containing an HEXXH zinc-binding motif from peptidase family M78. ImmA is encoded on a conjugative transposon. Conjugating bacteria are able to transfer conjugative transposons that can, for example, confer resistance to antibiotics. The transposon is integrated into the chromosome, but during conjugation excises itself and then moves to the recipient bacterium and re-integrate into its chromosome. Typically a conjugative tranposon encodes only the proteins required for this activity and the proteins that regulate it. During exponential growth, the ICEBs1 transposon of Bacillus subtilis is inactivated by the immunity repressor protein ImmR, which is encoded by the transposon and represses the genes for excision and transfer. Cleavage of ImmR relaxes repression and allows transfer of the transposon. ImmA has been shown to be essential for the cleavage of ImmR. This domain is also found in in metalloprotease IrrE, a central regulator of DNA damage repair in Deinococcaceae, HTH-type transcriptional regulators RamB and PrpC.


Pssm-ID: 399250  Cd Length: 122  Bit Score: 51.27  E-value: 4.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755806350  13 VTIREEKMP----YKLPGLYLNGTIFISKDQSSIEKGCVLVEELMHYKYTVGNITKQETIMDK---KQEIFARRKGYEEL 85
Cdd:pfam06114   6 IRVFFLPLGaedgDGRRFDRHTPVIFLNENLSPTRQRFTLAHELGHLLLHEGGDTLSDQFDFKtaeAREREANIFAAALL 85

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1755806350  86 IPLDDIIACFYLGLREYF-EVAEFLEVTEDFLRHTVS 121
Cdd:pfam06114  86 MPYEAFLAAAETLRYDLElLLAERFGVSYEAVAHRLS 122
 
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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