NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|519053068|ref|WP_020208943|]
View 

recombination mediator RecR [Gilvimarinus chinensis]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RecR COG0353
Recombinational DNA repair protein RecR [Replication, recombination and repair];
1-195 3.30e-120

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


:

Pssm-ID: 440122 [Multi-domain]  Cd Length: 195  Bit Score: 338.16  E-value: 3.30e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519053068   1 MFSPLIDELMQALRCLPGVGPKSAQRMAMQLLEHDRAGATRLADCLNRAVEGVARCRRCRTLTEQELCGVCSNERRDNTL 80
Cdd:COG0353    1 MYPPPLERLIEALSKLPGIGPKSAQRLALHLLKRDEEEAERLAEALLEAKEKVRHCSVCGNLTEEDPCSICADPRRDRSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519053068  81 LCVVETPADVLAIEQAGSYQGKYFVLLGHLSPIDGVGPEDIGIDQLITLLDAEPISEIILATNPTVEGEATAYYISERAR 160
Cdd:COG0353   81 ICVVEEPADVLAIERTGEYRGLYHVLGGVLSPLDGIGPEDLNIDELLERLKEGGVKEVILATNPTVEGEATAHYIAELLK 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 519053068 161 RAGVTVSRIAHGVPLGGELEYIDGGTLAHAFSSRR 195
Cdd:COG0353  161 PLGVKVTRLARGLPVGGELEYADEGTLARALEGRR 195
 
Name Accession Description Interval E-value
RecR COG0353
Recombinational DNA repair protein RecR [Replication, recombination and repair];
1-195 3.30e-120

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


Pssm-ID: 440122 [Multi-domain]  Cd Length: 195  Bit Score: 338.16  E-value: 3.30e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519053068   1 MFSPLIDELMQALRCLPGVGPKSAQRMAMQLLEHDRAGATRLADCLNRAVEGVARCRRCRTLTEQELCGVCSNERRDNTL 80
Cdd:COG0353    1 MYPPPLERLIEALSKLPGIGPKSAQRLALHLLKRDEEEAERLAEALLEAKEKVRHCSVCGNLTEEDPCSICADPRRDRSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519053068  81 LCVVETPADVLAIEQAGSYQGKYFVLLGHLSPIDGVGPEDIGIDQLITLLDAEPISEIILATNPTVEGEATAYYISERAR 160
Cdd:COG0353   81 ICVVEEPADVLAIERTGEYRGLYHVLGGVLSPLDGIGPEDLNIDELLERLKEGGVKEVILATNPTVEGEATAHYIAELLK 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 519053068 161 RAGVTVSRIAHGVPLGGELEYIDGGTLAHAFSSRR 195
Cdd:COG0353  161 PLGVKVTRLARGLPVGGELEYADEGTLARALEGRR 195
recR TIGR00615
recombination protein RecR; All proteins in this family for which functions are known are ...
 1-195 1.72e-92

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: 268.05  E-value: 1.72e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519053068    1 MFSPLIDELMQALRCLPGVGPKSAQRMAMQLLEHDRAGATRLADCLNRAVEGVARCRRCRTLTEQELCGVCSNERRDNTL 80
Cdd:TIGR00615   1 QYPPPISKLIESLKKLPGIGPKSAQRLAFHLLKRDPSEVLRLAQALLEAKENLRTCSVCGAISDQEVCNICSDERRDNSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519053068   81 LCVVETPADVLAIEQAGSYQGKYFVLLGHLSPIDGVGPEDIGIDQLITLLDAEPISEIILATNPTVEGEATAYYISERAR 160
Cdd:TIGR00615  81 ICVVEDPKDVFALEKTKEFRGRYHVLGGHISPLDGIGPEDLTIAALLKRLQEESVKEVILATNPTVEGEATALYIARLLQ 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 519053068  161 RAGVTVSRIAHGVPLGGELEYIDGGTLAHAFSSRR 195
Cdd:TIGR00615 161 PFGVKVTRIASGLPVGGDLEYADEVTLARALEGRR 195
TOPRIM_recR cd01025
TOPRIM_recR: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the ...
 79-190 3.88e-60

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: 183.10  E-value: 3.88e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519053068  79 TLLCVVETPADVLAIEQAGSYQGKYFVLLGHLSPIDGVGPEDIGIDQLITLLDAEPISEIILATNPTVEGEATAYYISER 158
Cdd:cd01025    1 NKLCVVEEPRDVLAIEESGEYRGLYHVLGGLISPLDGIGPDDLNIDKLLERIAKGQVKEVILATNPTVEGEATALYIAKL 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 519053068 159 ARRAGVTVSRIAHGVPLGGELEYIDGGTLAHA 190
Cdd:cd01025   81 LKDFGVKVTRLAQGIPVGGELEYADEITLSRA 112
Toprim_4 pfam13662
Toprim domain; The toprim domain is found in a wide variety of enzymes involved in nucleic ...
 81-170 3.72e-29

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: 103.52  E-value: 3.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519053068   81 LCVVETPADVLAIEQAGsYQGKYFVLLGHLSPIDGVGPEDIGIDQLitlldaEPISEIILATNPTVEGEATAYYISERAR 160
Cdd:pfam13662   3 IIVVEGYADVIALEKAG-YKGAVAVLGGALSPLDGIGPEDLNIDSL------GGIKEVILALDGDVAGEKTALYLAEALL 75

                          90
                  ....*....|
gi 519053068  161 RAGVTVSRIA 170
Cdd:pfam13662  76 EEGVKVSRLA 85
TOPRIM smart00493
topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins;
81-163 8.42e-17

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


Pssm-ID: 214695 [Multi-domain]  Cd Length: 75  Bit Score: 71.52  E-value: 8.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519053068    81 LCVVETPADVLAIEQAGSYQGKYFVLLGHLSPidgvgpedigIDQLITLLDAEPISEIILATNPTVEGEATAYYISERAR 160
Cdd:smart00493   3 LIIVEGPADAIALEKAGGKRGNVVALGGHLLS----------KEQIKLLKKLAKKAEVILATDPDREGEAIAWELAELLK 72


                   ...
gi 519053068   161 RAG 163
Cdd:smart00493  73 PAG 75
PRK08780 PRK08780
DNA topoisomerase I; Provisional
 81-173 1.12e-03

DNA topoisomerase I; Provisional


Pssm-ID: 181555 [Multi-domain]  Cd Length: 780  Bit Score: 38.97  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519053068  81 LCVVETPADVLAIEQagsYQGKYFVLL---GH---LSPIDG-VGPEDiGIDQLITLLD------------AEPISEIILA 141
Cdd:PRK08780   5 LVIVESPAKAKTINK---YLGKDFTVLasyGHvrdLVPKEGaVDPEN-GFAMRYDLIDknekhveaiakaAKSADDLYLA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 519053068 142 TNPTVEGEATAYYISERARRAGVTVSRIAHGV 173
Cdd:PRK08780  81 TDPDREGEAISWHLAEILKERGLLKDKPMQRV 112
 
Name Accession Description Interval E-value
RecR COG0353
Recombinational DNA repair protein RecR [Replication, recombination and repair];
1-195 3.30e-120

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


Pssm-ID: 440122 [Multi-domain]  Cd Length: 195  Bit Score: 338.16  E-value: 3.30e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519053068   1 MFSPLIDELMQALRCLPGVGPKSAQRMAMQLLEHDRAGATRLADCLNRAVEGVARCRRCRTLTEQELCGVCSNERRDNTL 80
Cdd:COG0353    1 MYPPPLERLIEALSKLPGIGPKSAQRLALHLLKRDEEEAERLAEALLEAKEKVRHCSVCGNLTEEDPCSICADPRRDRSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519053068  81 LCVVETPADVLAIEQAGSYQGKYFVLLGHLSPIDGVGPEDIGIDQLITLLDAEPISEIILATNPTVEGEATAYYISERAR 160
Cdd:COG0353   81 ICVVEEPADVLAIERTGEYRGLYHVLGGVLSPLDGIGPEDLNIDELLERLKEGGVKEVILATNPTVEGEATAHYIAELLK 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 519053068 161 RAGVTVSRIAHGVPLGGELEYIDGGTLAHAFSSRR 195
Cdd:COG0353  161 PLGVKVTRLARGLPVGGELEYADEGTLARALEGRR 195
recR TIGR00615
recombination protein RecR; All proteins in this family for which functions are known are ...
 1-195 1.72e-92

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: 268.05  E-value: 1.72e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519053068    1 MFSPLIDELMQALRCLPGVGPKSAQRMAMQLLEHDRAGATRLADCLNRAVEGVARCRRCRTLTEQELCGVCSNERRDNTL 80
Cdd:TIGR00615   1 QYPPPISKLIESLKKLPGIGPKSAQRLAFHLLKRDPSEVLRLAQALLEAKENLRTCSVCGAISDQEVCNICSDERRDNSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519053068   81 LCVVETPADVLAIEQAGSYQGKYFVLLGHLSPIDGVGPEDIGIDQLITLLDAEPISEIILATNPTVEGEATAYYISERAR 160
Cdd:TIGR00615  81 ICVVEDPKDVFALEKTKEFRGRYHVLGGHISPLDGIGPEDLTIAALLKRLQEESVKEVILATNPTVEGEATALYIARLLQ 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 519053068  161 RAGVTVSRIAHGVPLGGELEYIDGGTLAHAFSSRR 195
Cdd:TIGR00615 161 PFGVKVTRIASGLPVGGDLEYADEVTLARALEGRR 195
TOPRIM_recR cd01025
TOPRIM_recR: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the ...
 79-190 3.88e-60

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: 183.10  E-value: 3.88e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519053068  79 TLLCVVETPADVLAIEQAGSYQGKYFVLLGHLSPIDGVGPEDIGIDQLITLLDAEPISEIILATNPTVEGEATAYYISER 158
Cdd:cd01025    1 NKLCVVEEPRDVLAIEESGEYRGLYHVLGGLISPLDGIGPDDLNIDKLLERIAKGQVKEVILATNPTVEGEATALYIAKL 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 519053068 159 ARRAGVTVSRIAHGVPLGGELEYIDGGTLAHA 190
Cdd:cd01025   81 LKDFGVKVTRLAQGIPVGGELEYADEITLSRA 112
Toprim_4 pfam13662
Toprim domain; The toprim domain is found in a wide variety of enzymes involved in nucleic ...
 81-170 3.72e-29

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: 103.52  E-value: 3.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519053068   81 LCVVETPADVLAIEQAGsYQGKYFVLLGHLSPIDGVGPEDIGIDQLitlldaEPISEIILATNPTVEGEATAYYISERAR 160
Cdd:pfam13662   3 IIVVEGYADVIALEKAG-YKGAVAVLGGALSPLDGIGPEDLNIDSL------GGIKEVILALDGDVAGEKTALYLAEALL 75

                          90
                  ....*....|
gi 519053068  161 RAGVTVSRIA 170
Cdd:pfam13662  76 EEGVKVSRLA 85
TOPRIM smart00493
topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins;
81-163 8.42e-17

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


Pssm-ID: 214695 [Multi-domain]  Cd Length: 75  Bit Score: 71.52  E-value: 8.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519053068    81 LCVVETPADVLAIEQAGSYQGKYFVLLGHLSPidgvgpedigIDQLITLLDAEPISEIILATNPTVEGEATAYYISERAR 160
Cdd:smart00493   3 LIIVEGPADAIALEKAGGKRGNVVALGGHLLS----------KEQIKLLKKLAKKAEVILATDPDREGEAIAWELAELLK 72


                   ...
gi 519053068   161 RAG 163
Cdd:smart00493  73 PAG 75
TOPRIM cd00188
Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type ...
 81-170 5.26e-14

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: 64.37  E-value: 5.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519053068  81 LCVVETPADVLAIEQAGSYQGKYFVLLGHLSPIDgvgpedigIDQLITLLDAepISEIILATNPTVEGEATAYYISERAR 160
Cdd:cd00188    3 LIIVEGPSDALALAQAGGYGGAVVALGGHALNKT--------RELLKRLLGE--AKEVIIATDADREGEAIALRLLELLK 72

                         90
                 ....*....|
gi 519053068 161 RAGVTVSRIA 170
Cdd:cd00188   73 SLGKKVRRLL 82
Toprim pfam01751
Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim ...
 81-169 1.03e-12

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: 61.22  E-value: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519053068   81 LCVVETPADVLAIEQA-GSYQGKYFVLLGHLSPIDGvGPEDIGIDQLITLldAEPISEIILATNPTVEGEATAYYISE-- 157
Cdd:pfam01751   2 LIIVEGPSDAIALEKAlGGGFQAVVAVLGHLLSLEK-GPKKKALKALKEL--ALKAKEVILATDPDREGEAIALKLLElk 78

                          90
                  ....*....|....*
gi 519053068  158 ---RARRAGVTVSRI 169
Cdd:pfam01751  79 ellENAGGRVEFSEL 93
RecR pfam02132
RecR protein;
38-77 1.47e-11

RecR protein;


Pssm-ID: 460456  Cd Length: 40  Bit Score: 56.66  E-value: 1.47e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 519053068   38 GATRLADCLNRAVEGVARCRRCRTLTEQELCGVCSNERRD 77
Cdd:pfam02132   1 EAERLAEALLEAKENIRYCSVCGNLTDEDPCPICSDPRRD 40
TOPRIM_TopoIA_TopoI cd03363
TOPRIM_TopoIA_TopoI: The topoisomerase-primase (TOPRIM) domain found in members of the type IA ...
 81-170 7.11e-06

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: 43.70  E-value: 7.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519053068  81 LCVVETPADVLAIEQagsYQGKYFVLL---GH---LSPID-GVGPEDIG--------------IDQLITLldAEPISEII 139
Cdd:cd03363    3 LVIVESPAKAKTIKK---YLGKEYEVLasvGHirdLPKKGlGVDGEDDGfepkyvvipgkkkvVKELKKL--AKKADEIY 77

                         90       100       110
                 ....*....|....*....|....*....|.
gi 519053068 140 LATNPTVEGEATAYYISERArRAGVTVSRIA 170
Cdd:cd03363   78 LATDPDREGEAIAWHLAEVL-KLKKNVKRVV 107
PRK08780 PRK08780
DNA topoisomerase I; Provisional
 81-173 1.12e-03

DNA topoisomerase I; Provisional


Pssm-ID: 181555 [Multi-domain]  Cd Length: 780  Bit Score: 38.97  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519053068  81 LCVVETPADVLAIEQagsYQGKYFVLL---GH---LSPIDG-VGPEDiGIDQLITLLD------------AEPISEIILA 141
Cdd:PRK08780   5 LVIVESPAKAKTINK---YLGKDFTVLasyGHvrdLVPKEGaVDPEN-GFAMRYDLIDknekhveaiakaAKSADDLYLA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 519053068 142 TNPTVEGEATAYYISERARRAGVTVSRIAHGV 173
Cdd:PRK08780  81 TDPDREGEAISWHLAEILKERGLLKDKPMQRV 112
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH