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Conserved domains on  [gi|821583407|dbj|GAO62766|]
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recombinase RecR [Bacillus anthracis]

Protein Classification

recombination mediator RecR( domain architecture ID 11417471)

recombination protein RecR is a recombination mediator protein in the RecFOR pathway of homologous recombinational repair

Gene Ontology:  GO:0006281|GO:0006310|GO:0003677|GO:0046872
PubMed:  15116069|9722641|17581636|23019218|9363943
SCOP:  4007649|4007650|3000737|4002927

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RecR COG0353
Recombinational DNA repair protein RecR [Replication, recombination and repair];
2-196 3.16e-129

Recombinational DNA repair protein RecR [Replication, recombination and repair];


:

Pssm-ID: 440122 [Multi-domain]  Cd Length: 195  Bit Score: 360.88  E-value: 3.16e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821583407   2 HYPEPISKLIDSFMKLPGIGPKTAVRLAFFVLDMKEDDVLGFAKALVNAKRDLAYCSVCGHITDRDPCYICNDSHRDQSV 81
Cdd:COG0353    1 MYPPPLERLIEALSKLPGIGPKSAQRLALHLLKRDEEEAERLAEALLEAKEKVRHCSVCGNLTEEDPCSICADPRRDRSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821583407  82 VCVVQEPKDVIAMEKMKEYQGVYHVLRGAISPMGGIGPEDINIPQLLKRLHDETVQEVILATNPNIEGEATAMYISRLLK 161
Cdd:COG0353   81 ICVVEEPADVLAIERTGEYRGLYHVLGGVLSPLDGIGPEDLNIDELLERLKEGGVKEVILATNPTVEGEATAHYIAELLK 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 821583407 162 PTGIKVTRIAHGLPVGGDLEYADEVTLSKALEGRR 196
Cdd:COG0353  161 PLGVKVTRLARGLPVGGELEYADEGTLARALEGRR 195
 
Name Accession Description Interval E-value
RecR COG0353
Recombinational DNA repair protein RecR [Replication, recombination and repair];
2-196 3.16e-129

Recombinational DNA repair protein RecR [Replication, recombination and repair];


Pssm-ID: 440122 [Multi-domain]  Cd Length: 195  Bit Score: 360.88  E-value: 3.16e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821583407   2 HYPEPISKLIDSFMKLPGIGPKTAVRLAFFVLDMKEDDVLGFAKALVNAKRDLAYCSVCGHITDRDPCYICNDSHRDQSV 81
Cdd:COG0353    1 MYPPPLERLIEALSKLPGIGPKSAQRLALHLLKRDEEEAERLAEALLEAKEKVRHCSVCGNLTEEDPCSICADPRRDRSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821583407  82 VCVVQEPKDVIAMEKMKEYQGVYHVLRGAISPMGGIGPEDINIPQLLKRLHDETVQEVILATNPNIEGEATAMYISRLLK 161
Cdd:COG0353   81 ICVVEEPADVLAIERTGEYRGLYHVLGGVLSPLDGIGPEDLNIDELLERLKEGGVKEVILATNPTVEGEATAHYIAELLK 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 821583407 162 PTGIKVTRIAHGLPVGGDLEYADEVTLSKALEGRR 196
Cdd:COG0353  161 PLGVKVTRLARGLPVGGELEYADEGTLARALEGRR 195
recR TIGR00615
recombination protein RecR; All proteins in this family for which functions are known are ...
 3-196 1.50e-118

recombination protein RecR; All proteins in this family for which functions are known are involved in the initiation of recombination and recombinational repair. RecF is also required. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273176 [Multi-domain]  Cd Length: 195  Bit Score: 334.31  E-value: 1.50e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821583407    3 YPEPISKLIDSFMKLPGIGPKTAVRLAFFVLDMKEDDVLGFAKALVNAKRDLAYCSVCGHITDRDPCYICNDSHRDQSVV 82
Cdd:TIGR00615   2 YPPPISKLIESLKKLPGIGPKSAQRLAFHLLKRDPSEVLRLAQALLEAKENLRTCSVCGAISDQEVCNICSDERRDNSVI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821583407   83 CVVQEPKDVIAMEKMKEYQGVYHVLRGAISPMGGIGPEDINIPQLLKRLHDETVQEVILATNPNIEGEATAMYISRLLKP 162
Cdd:TIGR00615  82 CVVEDPKDVFALEKTKEFRGRYHVLGGHISPLDGIGPEDLTIAALLKRLQEESVKEVILATNPTVEGEATALYIARLLQP 161

                         170       180       190
                  ....*....|....*....|....*....|....
gi 821583407  163 TGIKVTRIAHGLPVGGDLEYADEVTLSKALEGRR 196
Cdd:TIGR00615 162 FGVKVTRIASGLPVGGDLEYADEVTLARALEGRR 195
TOPRIM_recR cd01025
TOPRIM_recR: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the ...
 80-191 1.27e-63

TOPRIM_recR: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in Escherichia coli RecR. RecR participates in the RecFOR pathway of homologous recombinational repair in prokaryotes. This pathway provides a single-stranded DNA molecule coated with RecA to allow invasion of a homologous molecule. The RecFOR system directs the loading of RecA onto gapped DNA coated with SSB protein. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). In RecR sequences this glutamate in the first turn of the TOPRIM domain is semiconserved, the DXD motif is not conserved.


Pssm-ID: 173775  Cd Length: 112  Bit Score: 191.96  E-value: 1.27e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821583407  80 SVVCVVQEPKDVIAMEKMKEYQGVYHVLRGAISPMGGIGPEDINIPQLLKRLHDETVQEVILATNPNIEGEATAMYISRL 159
Cdd:cd01025    1 NKLCVVEEPRDVLAIEESGEYRGLYHVLGGLISPLDGIGPDDLNIDKLLERIAKGQVKEVILATNPTVEGEATALYIAKL 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 821583407 160 LKPTGIKVTRIAHGLPVGGDLEYADEVTLSKA 191
Cdd:cd01025   81 LKDFGVKVTRLAQGIPVGGELEYADEITLSRA 112
Toprim_4 pfam13662
Toprim domain; The toprim domain is found in a wide variety of enzymes involved in nucleic ...
 80-171 1.47e-28

Toprim domain; The toprim domain is found in a wide variety of enzymes involved in nucleic acid manipulation.


Pssm-ID: 433387 [Multi-domain]  Cd Length: 85  Bit Score: 101.98  E-value: 1.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821583407   80 SVVCVVQEPKDVIAMEKMkEYQGVYHVLRGAISPMGGIGPEDINIPQLlkrlhdETVQEVILATNPNIEGEATAMYISRL 159
Cdd:pfam13662   1 SEIIVVEGYADVIALEKA-GYKGAVAVLGGALSPLDGIGPEDLNIDSL------GGIKEVILALDGDVAGEKTALYLAEA 73

                          90
                  ....*....|..
gi 821583407  160 LKPTGIKVTRIA 171
Cdd:pfam13662  74 LLEEGVKVSRLA 85
TOPRIM smart00493
topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins;
80-164 1.67e-15

topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins;


Pssm-ID: 214695 [Multi-domain]  Cd Length: 75  Bit Score: 68.06  E-value: 1.67e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821583407    80 SVVCVVQEPKDVIAMEKMKEYQGVYHVLRGAISPmggigpedINIPQLLKRLHDEtvQEVILATNPNIEGEATAMYISRL 159
Cdd:smart00493   1 KVLIIVEGPADAIALEKAGGKRGNVVALGGHLLS--------KEQIKLLKKLAKK--AEVILATDPDREGEAIAWELAEL 70


                   ....*
gi 821583407   160 LKPTG 164
Cdd:smart00493  71 LKPAG 75
 
Name Accession Description Interval E-value
RecR COG0353
Recombinational DNA repair protein RecR [Replication, recombination and repair];
2-196 3.16e-129

Recombinational DNA repair protein RecR [Replication, recombination and repair];


Pssm-ID: 440122 [Multi-domain]  Cd Length: 195  Bit Score: 360.88  E-value: 3.16e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821583407   2 HYPEPISKLIDSFMKLPGIGPKTAVRLAFFVLDMKEDDVLGFAKALVNAKRDLAYCSVCGHITDRDPCYICNDSHRDQSV 81
Cdd:COG0353    1 MYPPPLERLIEALSKLPGIGPKSAQRLALHLLKRDEEEAERLAEALLEAKEKVRHCSVCGNLTEEDPCSICADPRRDRSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821583407  82 VCVVQEPKDVIAMEKMKEYQGVYHVLRGAISPMGGIGPEDINIPQLLKRLHDETVQEVILATNPNIEGEATAMYISRLLK 161
Cdd:COG0353   81 ICVVEEPADVLAIERTGEYRGLYHVLGGVLSPLDGIGPEDLNIDELLERLKEGGVKEVILATNPTVEGEATAHYIAELLK 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 821583407 162 PTGIKVTRIAHGLPVGGDLEYADEVTLSKALEGRR 196
Cdd:COG0353  161 PLGVKVTRLARGLPVGGELEYADEGTLARALEGRR 195
recR TIGR00615
recombination protein RecR; All proteins in this family for which functions are known are ...
 3-196 1.50e-118

recombination protein RecR; All proteins in this family for which functions are known are involved in the initiation of recombination and recombinational repair. RecF is also required. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273176 [Multi-domain]  Cd Length: 195  Bit Score: 334.31  E-value: 1.50e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821583407    3 YPEPISKLIDSFMKLPGIGPKTAVRLAFFVLDMKEDDVLGFAKALVNAKRDLAYCSVCGHITDRDPCYICNDSHRDQSVV 82
Cdd:TIGR00615   2 YPPPISKLIESLKKLPGIGPKSAQRLAFHLLKRDPSEVLRLAQALLEAKENLRTCSVCGAISDQEVCNICSDERRDNSVI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821583407   83 CVVQEPKDVIAMEKMKEYQGVYHVLRGAISPMGGIGPEDINIPQLLKRLHDETVQEVILATNPNIEGEATAMYISRLLKP 162
Cdd:TIGR00615  82 CVVEDPKDVFALEKTKEFRGRYHVLGGHISPLDGIGPEDLTIAALLKRLQEESVKEVILATNPTVEGEATALYIARLLQP 161

                         170       180       190
                  ....*....|....*....|....*....|....
gi 821583407  163 TGIKVTRIAHGLPVGGDLEYADEVTLSKALEGRR 196
Cdd:TIGR00615 162 FGVKVTRIASGLPVGGDLEYADEVTLARALEGRR 195
TOPRIM_recR cd01025
TOPRIM_recR: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the ...
 80-191 1.27e-63

TOPRIM_recR: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in Escherichia coli RecR. RecR participates in the RecFOR pathway of homologous recombinational repair in prokaryotes. This pathway provides a single-stranded DNA molecule coated with RecA to allow invasion of a homologous molecule. The RecFOR system directs the loading of RecA onto gapped DNA coated with SSB protein. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). In RecR sequences this glutamate in the first turn of the TOPRIM domain is semiconserved, the DXD motif is not conserved.


Pssm-ID: 173775  Cd Length: 112  Bit Score: 191.96  E-value: 1.27e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821583407  80 SVVCVVQEPKDVIAMEKMKEYQGVYHVLRGAISPMGGIGPEDINIPQLLKRLHDETVQEVILATNPNIEGEATAMYISRL 159
Cdd:cd01025    1 NKLCVVEEPRDVLAIEESGEYRGLYHVLGGLISPLDGIGPDDLNIDKLLERIAKGQVKEVILATNPTVEGEATALYIAKL 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 821583407 160 LKPTGIKVTRIAHGLPVGGDLEYADEVTLSKA 191
Cdd:cd01025   81 LKDFGVKVTRLAQGIPVGGELEYADEITLSRA 112
Toprim_4 pfam13662
Toprim domain; The toprim domain is found in a wide variety of enzymes involved in nucleic ...
 80-171 1.47e-28

Toprim domain; The toprim domain is found in a wide variety of enzymes involved in nucleic acid manipulation.


Pssm-ID: 433387 [Multi-domain]  Cd Length: 85  Bit Score: 101.98  E-value: 1.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821583407   80 SVVCVVQEPKDVIAMEKMkEYQGVYHVLRGAISPMGGIGPEDINIPQLlkrlhdETVQEVILATNPNIEGEATAMYISRL 159
Cdd:pfam13662   1 SEIIVVEGYADVIALEKA-GYKGAVAVLGGALSPLDGIGPEDLNIDSL------GGIKEVILALDGDVAGEKTALYLAEA 73

                          90
                  ....*....|..
gi 821583407  160 LKPTGIKVTRIA 171
Cdd:pfam13662  74 LLEEGVKVSRLA 85
TOPRIM smart00493
topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins;
80-164 1.67e-15

topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins;


Pssm-ID: 214695 [Multi-domain]  Cd Length: 75  Bit Score: 68.06  E-value: 1.67e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821583407    80 SVVCVVQEPKDVIAMEKMKEYQGVYHVLRGAISPmggigpedINIPQLLKRLHDEtvQEVILATNPNIEGEATAMYISRL 159
Cdd:smart00493   1 KVLIIVEGPADAIALEKAGGKRGNVVALGGHLLS--------KEQIKLLKKLAKK--AEVILATDPDREGEAIAWELAEL 70


                   ....*
gi 821583407   160 LKPTG 164
Cdd:smart00493  71 LKPAG 75
RecR pfam02132
RecR protein;
39-78 8.16e-15

RecR protein;


Pssm-ID: 460456  Cd Length: 40  Bit Score: 65.13  E-value: 8.16e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 821583407   39 DVLGFAKALVNAKRDLAYCSVCGHITDRDPCYICNDSHRD 78
Cdd:pfam02132   1 EAERLAEALLEAKENIRYCSVCGNLTDEDPCPICSDPRRD 40
TOPRIM cd00188
Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type ...
 80-171 7.40e-12

Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type IA, type IIA and type IIB topoisomerases, bacterial DnaG-type primases, small primase-like proteins from bacteria and archaea, OLD family nucleases from bacterial and archaea, and bacterial DNA repair proteins of the RecR/M family. This domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). This glutamate and two aspartates, cluster together to form a highly acid surface patch. The conserved glutamate may act as a general base in nucleotide polymerization by primases and in strand joining in topoisomerases and, as a general acid in strand cleavage by topisomerases and nucleases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function.


Pssm-ID: 173773 [Multi-domain]  Cd Length: 83  Bit Score: 58.59  E-value: 7.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821583407  80 SVVCVVQEPKDVIAMEKMKEYQGVYHVLRGAISPmggigpediNIPQLLKRLHDEtVQEVILATNPNIEGEATAMYISRL 159
Cdd:cd00188    1 KKLIIVEGPSDALALAQAGGYGGAVVALGGHALN---------KTRELLKRLLGE-AKEVIIATDADREGEAIALRLLEL 70

                         90
                 ....*....|..
gi 821583407 160 LKPTGIKVTRIA 171
Cdd:cd00188   71 LKSLGKKVRRLL 82
Toprim pfam01751
Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim ...
 81-170 6.30e-09

Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim domain common to DnaG primases, topoisomerases, OLD family nucleases and RecR proteins. Both DnaG motifs IV and V are present in the alignment, the DxD (V) motif may be involved in Mg2+ binding and mutations to the conserved glutamate (IV) completely abolish DnaG type primase activity. DNA primase EC:2.7.7.6 is a nucleotidyltransferase it synthesizes the oligoribonucleotide primers required for DNA replication on the lagging strand of the replication fork; it can also prime the leading stand and has been implicated in cell division. This family also includes the atypical archaeal A subunit from type II DNA topoisomerases. Type II DNA topoisomerases catalyze the relaxation of DNA supercoiling by causing transient double strand breaks.


Pssm-ID: 396354 [Multi-domain]  Cd Length: 93  Bit Score: 51.20  E-value: 6.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821583407   81 VVCVVQEPKDVIAMEKM--KEYQGVYHVLRGAISPMGGigPEDINIPQLLKRLHDetVQEVILATNPNIEGEATAMYIS- 157
Cdd:pfam01751   1 ELIIVEGPSDAIALEKAlgGGFQAVVAVLGHLLSLEKG--PKKKALKALKELALK--AKEVILATDPDREGEAIALKLLe 76

                          90
                  ....*....|....*..
gi 821583407  158 --RLLKPTG--IKVTRI 170
Cdd:pfam01751  77 lkELLENAGgrVEFSEL 93
TOPRIM_TopoIA_TopoI cd03363
TOPRIM_TopoIA_TopoI: The topoisomerase-primase (TOPRIM) domain found in members of the type IA ...
 135-171 6.42e-03

TOPRIM_TopoIA_TopoI: The topoisomerase-primase (TOPRIM) domain found in members of the type IA family of DNA topoisomerases (Topo IA) similar to Escherichia coli DNA topoisomerase I. Type IA DNA topoisomerases remove (relax) negative supercoils in the DNA by: cleaving one strand of the DNA duplex, covalently linking to the 5' phosphoryl end of the DNA break and, allowing the other strand of the duplex to pass through the gap. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). For topoisomerases the conserved glutamate is believed to act as a general base in strand joining and, as a general acid in strand cleavage. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function.


Pssm-ID: 173783 [Multi-domain]  Cd Length: 123  Bit Score: 35.23  E-value: 6.42e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 821583407 135 TVQEVILATNPNIEGEATAMYISRLLKPtGIKVTRIA 171
Cdd:cd03363   72 KADEIYLATDPDREGEAIAWHLAEVLKL-KKNVKRVV 107
 
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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