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Conserved domains on  [gi|1958742837|ref|XP_038952681|]
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DNA endonuclease RBBP8 isoform X4 [Rattus norvegicus]

Protein Classification

DNA endonuclease RBBP8( domain architecture ID 10564642)

DNA endonuclease RBBP8 similar to human RBBP8 that cooperates with the MRE11-RAD50-NBN complex in DNA-end resection, the first step of double-strand break (DSB) repair through the homologous recombination pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CtIP_N pfam10482
Tumour-suppressor protein CtIP N-terminal domain; CtIP is predominantly a nuclear protein that ...
 33-135 2.48e-52

Tumour-suppressor protein CtIP N-terminal domain; CtIP is predominantly a nuclear protein that complexes with both BRCA1 and the BRCA1-associated RING domain protein (BARD1). At the protein level, CtIP expression varies with cell cycle progression in a pattern identical to that of BRCA1. Thus, the steady-state levels of CtIP polypeptides, which remain low in resting cells and G1 cycling cells, increase dramatically as Dividing cells traverse the G1/S boundary. CtIP can potentially modulate the functions ascribed to BRCA1 in transcriptional regulation, DNA repair, and/or cell cycle checkpoint control. This N-terminal domain carries a coiled-coil region and is essential for homodimerization of the protein. The C-terminal domain is family pfam08573.


:

Pssm-ID: 463107 [Multi-domain]  Cd Length: 120  Bit Score: 178.32  E-value: 2.48e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742837  33 GLQIKVTKLKKERILDAQRLEEFFTKNQQLRDQQKVLQETIKILEDRLRAGLCDRCAVTEEHMHKKQQEFENIRQQNLRL 112
Cdd:pfam10482  18 GLQAKVSELKKERCLDAQRLEELFSKNQQLREQQKALQENIKVLENRLRAGLCDRCAVTQELAKKKQQEFENSQLQSLQH 97

                          90       100
                  ....*....|....*....|...
gi 1958742837 113 ITELMNEKSALQEENKKLSEQLQ 135
Cdd:pfam10482  98 ITILTNEMNTLKDENRKLKEELK 120
SAE2 pfam08573
DNA endonuclease activator SAE2/CtIP C-terminus; SAE2 is a protein involved in repairing ...
 789-852 5.71e-12

DNA endonuclease activator SAE2/CtIP C-terminus; SAE2 is a protein involved in repairing meiotic and mitotic double-strand breaks in DNA. It has been shown to negatively regulate DNA damage checkpoint signalling. SAE2 is homologous to the CtIP proteins in mammals and an homologous protein in plants. Crucial sequence motifs that are highly conserved are the CxxC and the RHR motifs in this C-terminal part of the protein. In budding yeast, genetic evidence suggests that the SAE2 protein is essential for the processing of hairpin DNA intermediates and meiotic double-strand breaks by Mre11/Rad50 complexes. SAE2 binds DNA and exhibits endonuclease activity on single-stranded DNA independently of Mre11/Rad50 complexes, but hairpin DNA structures are cleaved cooperatively in the presence of Mre11/Rad50 or Mre11/Rad50/Xrs2. Hairpin structures are not processed at the tip by SAE2 but rather at single-stranded DNA regions adjacent to the hairpin. The catalytic activities of SAE2 are important for its biological functions. Although proteins containing this domain were described as endonucleases, it is now known that they actually function as endonuclease activators. This domain contains highly conserved residues at its 15-residue extreme that are indispensable for MRN (Mre11-Rad50-Nbs1) complex activation, through the stimulation of Mre11 endonuclease activity.


:

Pssm-ID: 462525  Cd Length: 108  Bit Score: 63.15  E-value: 5.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742837 789 EVVRKKEERRKLLGHTCKEC--EIYYA------------------------------DLPAEERE--------KKLASC- 827
Cdd:pfam08573   4 EVVRGKDERKCLPGCTCPCCcgDYFRAmaplpgrlrqkeedqklledylgdeayklgTMSAEEREellveaktRKLANKy 83

                          90       100
                  ....*....|....*....|....*
gi 1958742837 828 SRHRFRYIPTNTPENFWEVGFPSTQ 852
Cdd:pfam08573  84 GRHRHHFERAPTPPGFWRTDFPSTQ 108
 
Name Accession Description Interval E-value
CtIP_N pfam10482
Tumour-suppressor protein CtIP N-terminal domain; CtIP is predominantly a nuclear protein that ...
 33-135 2.48e-52

Tumour-suppressor protein CtIP N-terminal domain; CtIP is predominantly a nuclear protein that complexes with both BRCA1 and the BRCA1-associated RING domain protein (BARD1). At the protein level, CtIP expression varies with cell cycle progression in a pattern identical to that of BRCA1. Thus, the steady-state levels of CtIP polypeptides, which remain low in resting cells and G1 cycling cells, increase dramatically as Dividing cells traverse the G1/S boundary. CtIP can potentially modulate the functions ascribed to BRCA1 in transcriptional regulation, DNA repair, and/or cell cycle checkpoint control. This N-terminal domain carries a coiled-coil region and is essential for homodimerization of the protein. The C-terminal domain is family pfam08573.


Pssm-ID: 463107 [Multi-domain]  Cd Length: 120  Bit Score: 178.32  E-value: 2.48e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742837  33 GLQIKVTKLKKERILDAQRLEEFFTKNQQLRDQQKVLQETIKILEDRLRAGLCDRCAVTEEHMHKKQQEFENIRQQNLRL 112
Cdd:pfam10482  18 GLQAKVSELKKERCLDAQRLEELFSKNQQLREQQKALQENIKVLENRLRAGLCDRCAVTQELAKKKQQEFENSQLQSLQH 97

                          90       100
                  ....*....|....*....|...
gi 1958742837 113 ITELMNEKSALQEENKKLSEQLQ 135
Cdd:pfam10482  98 ITILTNEMNTLKDENRKLKEELK 120
SAE2 pfam08573
DNA endonuclease activator SAE2/CtIP C-terminus; SAE2 is a protein involved in repairing ...
 789-852 5.71e-12

DNA endonuclease activator SAE2/CtIP C-terminus; SAE2 is a protein involved in repairing meiotic and mitotic double-strand breaks in DNA. It has been shown to negatively regulate DNA damage checkpoint signalling. SAE2 is homologous to the CtIP proteins in mammals and an homologous protein in plants. Crucial sequence motifs that are highly conserved are the CxxC and the RHR motifs in this C-terminal part of the protein. In budding yeast, genetic evidence suggests that the SAE2 protein is essential for the processing of hairpin DNA intermediates and meiotic double-strand breaks by Mre11/Rad50 complexes. SAE2 binds DNA and exhibits endonuclease activity on single-stranded DNA independently of Mre11/Rad50 complexes, but hairpin DNA structures are cleaved cooperatively in the presence of Mre11/Rad50 or Mre11/Rad50/Xrs2. Hairpin structures are not processed at the tip by SAE2 but rather at single-stranded DNA regions adjacent to the hairpin. The catalytic activities of SAE2 are important for its biological functions. Although proteins containing this domain were described as endonucleases, it is now known that they actually function as endonuclease activators. This domain contains highly conserved residues at its 15-residue extreme that are indispensable for MRN (Mre11-Rad50-Nbs1) complex activation, through the stimulation of Mre11 endonuclease activity.


Pssm-ID: 462525  Cd Length: 108  Bit Score: 63.15  E-value: 5.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742837 789 EVVRKKEERRKLLGHTCKEC--EIYYA------------------------------DLPAEERE--------KKLASC- 827
Cdd:pfam08573   4 EVVRGKDERKCLPGCTCPCCcgDYFRAmaplpgrlrqkeedqklledylgdeayklgTMSAEEREellveaktRKLANKy 83

                          90       100
                  ....*....|....*....|....*
gi 1958742837 828 SRHRFRYIPTNTPENFWEVGFPSTQ 852
Cdd:pfam08573  84 GRHRHHFERAPTPPGFWRTDFPSTQ 108
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
34-150 1.75e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742837  34 LQIKVTKLKKERILDAQRLEEFFTKNQQLRDQQKVLQETIKILEDRLRAGLcDRCAVTEEHMHKKQQEFENIRQQnlrlI 113
Cdd:COG4372    43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ-AELAQAQEELESLQEEAEELQEE----L 117

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958742837 114 TELMNEKSALQEENKKLSEQlQQKMESGQQDQVAELE 150
Cdd:COG4372   118 EELQKERQDLEQQRKQLEAQ-IAELQSEIAEREEELK 153
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 34-158 3.44e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 3.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742837   34 LQIKVTKLKKERILDAQRLEEFFTKNQQLRDQQKVLQETIKILEDRLRAGLCDRCAVTEEhMHKKQQEFENIRQQNLRL- 112
Cdd:TIGR02169  355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE-LQRLSEELADLNAAIAGIe 433

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958742837  113 --ITELMNEKSALQEENKKLSEQLQQ--KMESGQQDQVAELECEENIIPD 158
Cdd:TIGR02169  434 akINELEEEKEDKALEIKKQEWKLEQlaADLSKYEQELYDLKEEYDRVEK 483
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 26-145 9.40e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 39.78  E-value: 9.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742837   26 TKRSVEpgLQIKVTKLKKERILDAQRLEE----FFTKNQQLRDQQKV--LQETIKILE---DRLRAGL-CDRCAVTEEHM 95
Cdd:PRK10246   439 QKRLAQ--LQVAIQNVTQEQTQRNAALNEmrqrYKEKTQQLADVKTIceQEARIKDLEaqrAQLQAGQpCPLCGSTSHPA 516

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958742837   96 HKKQQEFENIRQQNLRLitELMNEKSALQEENKKLSEQLQQKMESGQQDQ 145
Cdd:PRK10246   517 VEAYQALEPGVNQSRLD--ALEKEVKKLGEEGAALRGQLDALTKQLQRDE 564
 
Name Accession Description Interval E-value
CtIP_N pfam10482
Tumour-suppressor protein CtIP N-terminal domain; CtIP is predominantly a nuclear protein that ...
 33-135 2.48e-52

Tumour-suppressor protein CtIP N-terminal domain; CtIP is predominantly a nuclear protein that complexes with both BRCA1 and the BRCA1-associated RING domain protein (BARD1). At the protein level, CtIP expression varies with cell cycle progression in a pattern identical to that of BRCA1. Thus, the steady-state levels of CtIP polypeptides, which remain low in resting cells and G1 cycling cells, increase dramatically as Dividing cells traverse the G1/S boundary. CtIP can potentially modulate the functions ascribed to BRCA1 in transcriptional regulation, DNA repair, and/or cell cycle checkpoint control. This N-terminal domain carries a coiled-coil region and is essential for homodimerization of the protein. The C-terminal domain is family pfam08573.


Pssm-ID: 463107 [Multi-domain]  Cd Length: 120  Bit Score: 178.32  E-value: 2.48e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742837  33 GLQIKVTKLKKERILDAQRLEEFFTKNQQLRDQQKVLQETIKILEDRLRAGLCDRCAVTEEHMHKKQQEFENIRQQNLRL 112
Cdd:pfam10482  18 GLQAKVSELKKERCLDAQRLEELFSKNQQLREQQKALQENIKVLENRLRAGLCDRCAVTQELAKKKQQEFENSQLQSLQH 97

                          90       100
                  ....*....|....*....|...
gi 1958742837 113 ITELMNEKSALQEENKKLSEQLQ 135
Cdd:pfam10482  98 ITILTNEMNTLKDENRKLKEELK 120
SAE2 pfam08573
DNA endonuclease activator SAE2/CtIP C-terminus; SAE2 is a protein involved in repairing ...
 789-852 5.71e-12

DNA endonuclease activator SAE2/CtIP C-terminus; SAE2 is a protein involved in repairing meiotic and mitotic double-strand breaks in DNA. It has been shown to negatively regulate DNA damage checkpoint signalling. SAE2 is homologous to the CtIP proteins in mammals and an homologous protein in plants. Crucial sequence motifs that are highly conserved are the CxxC and the RHR motifs in this C-terminal part of the protein. In budding yeast, genetic evidence suggests that the SAE2 protein is essential for the processing of hairpin DNA intermediates and meiotic double-strand breaks by Mre11/Rad50 complexes. SAE2 binds DNA and exhibits endonuclease activity on single-stranded DNA independently of Mre11/Rad50 complexes, but hairpin DNA structures are cleaved cooperatively in the presence of Mre11/Rad50 or Mre11/Rad50/Xrs2. Hairpin structures are not processed at the tip by SAE2 but rather at single-stranded DNA regions adjacent to the hairpin. The catalytic activities of SAE2 are important for its biological functions. Although proteins containing this domain were described as endonucleases, it is now known that they actually function as endonuclease activators. This domain contains highly conserved residues at its 15-residue extreme that are indispensable for MRN (Mre11-Rad50-Nbs1) complex activation, through the stimulation of Mre11 endonuclease activity.


Pssm-ID: 462525  Cd Length: 108  Bit Score: 63.15  E-value: 5.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742837 789 EVVRKKEERRKLLGHTCKEC--EIYYA------------------------------DLPAEERE--------KKLASC- 827
Cdd:pfam08573   4 EVVRGKDERKCLPGCTCPCCcgDYFRAmaplpgrlrqkeedqklledylgdeayklgTMSAEEREellveaktRKLANKy 83

                          90       100
                  ....*....|....*....|....*
gi 1958742837 828 SRHRFRYIPTNTPENFWEVGFPSTQ 852
Cdd:pfam08573  84 GRHRHHFERAPTPPGFWRTDFPSTQ 108
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
34-150 1.75e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742837  34 LQIKVTKLKKERILDAQRLEEFFTKNQQLRDQQKVLQETIKILEDRLRAGLcDRCAVTEEHMHKKQQEFENIRQQnlrlI 113
Cdd:COG4372    43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ-AELAQAQEELESLQEEAEELQEE----L 117

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958742837 114 TELMNEKSALQEENKKLSEQlQQKMESGQQDQVAELE 150
Cdd:COG4372   118 EELQKERQDLEQQRKQLEAQ-IAELQSEIAEREEELK 153
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
18-148 4.09e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 4.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742837  18 DTKVRRASTKRSVEPGLQiKVTKLKKERILDAQRLEEFFTKNQQLRD---QQKVLQETIKILEDRLRAGLCDRCAVTEEH 94
Cdd:COG4717   115 REELEKLEKLLQLLPLYQ-ELEALEAELAELPERLEELEERLEELREleeELEELEAELAELQEELEELLEQLSLATEEE 193

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958742837  95 MHKKQQEFENIRQQnlrlITELMNEKSALQEENKKLSEQLQQKMESGQQDQVAE 148
Cdd:COG4717   194 LQDLAEELEELQQR----LAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 33-227 1.39e-03

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 42.43  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742837  33 GLQIKVTKL-KKERILDAQRLEEFFTKNQQLRDQqkVLQETIKILEDRLRAGLCDRCAVTEEHMHKKQQEFENIRQQNLR 111
Cdd:pfam07111 544 GQQLEVARQgQQESTEEAASLRQELTQQQEIYGQ--ALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHR 621

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742837 112 LITElmneksalQEENKKLSE-QLQQKMESGQQ--DQVAELECEENIIPDSpitsfsfsginrlRRKENLHVRYVEQTHT 188
Cdd:pfam07111 622 ATQE--------KERNQELRRlQDEARKEEGQRlaRRVQELERDKNLMLAT-------------LQQEGLLSRYKQQRLL 680

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958742837 189 klehSACTSELRKFSKGSTPAPVNSEEHEILVADTCDQS 227
Cdd:pfam07111 681 ----AVLPSGLDKKSVVSSPRPECSASAPIPAAVPTRES 715
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 34-154 3.28e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742837  34 LQIKVTKLKKERILDAQRLEEFFTKNQQLRDQQKVLQETIKILEDRLRAgLCDRCAVTEEHMHKKQQEFENIRQQNLRLI 113
Cdd:COG1196   293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE-LEEELEEAEEELEEAEAELAEAEEALLEAE 371

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958742837 114 TELMNEKSALQEENKKLSEQLQQKMESGQQDQVAELECEEN 154
Cdd:COG1196   372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 34-158 3.44e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 3.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742837   34 LQIKVTKLKKERILDAQRLEEFFTKNQQLRDQQKVLQETIKILEDRLRAGLCDRCAVTEEhMHKKQQEFENIRQQNLRL- 112
Cdd:TIGR02169  355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE-LQRLSEELADLNAAIAGIe 433

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958742837  113 --ITELMNEKSALQEENKKLSEQLQQ--KMESGQQDQVAELECEENIIPD 158
Cdd:TIGR02169  434 akINELEEEKEDKALEIKKQEWKLEQlaADLSKYEQELYDLKEEYDRVEK 483
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
35-150 4.14e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 4.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742837  35 QIKVTKLKKERILDAQ-RLEEFFTKNQQLRDQQKVLQETIKILEDRLRA-GLCDRCAVTEEHMHKKQQEFENIRQQnLRL 112
Cdd:COG4717    79 ELKEAEEKEEEYAELQeELEELEEELEELEAELEELREELEKLEKLLQLlPLYQELEALEAELAELPERLEELEER-LEE 157

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958742837 113 ITELMNEKSALQEENKKLSEQLQQKMESGQQDQVAELE 150
Cdd:COG4717   158 LRELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 26-145 9.40e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 39.78  E-value: 9.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742837   26 TKRSVEpgLQIKVTKLKKERILDAQRLEE----FFTKNQQLRDQQKV--LQETIKILE---DRLRAGL-CDRCAVTEEHM 95
Cdd:PRK10246   439 QKRLAQ--LQVAIQNVTQEQTQRNAALNEmrqrYKEKTQQLADVKTIceQEARIKDLEaqrAQLQAGQpCPLCGSTSHPA 516

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958742837   96 HKKQQEFENIRQQNLRLitELMNEKSALQEENKKLSEQLQQKMESGQQDQ 145
Cdd:PRK10246   517 VEAYQALEPGVNQSRLD--ALEKEVKKLGEEGAALRGQLDALTKQLQRDE 564
 
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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