NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|251823779|ref|NP_001156574|]
View 

probable crossover junction endonuclease EME2 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
XPF_nuclease_EME2 cd20082
XPF-like nuclease domain of crossover junction endonuclease EME2; EME2 interacts with MUS81 to ...
64-254 1.37e-80

XPF-like nuclease domain of crossover junction endonuclease EME2; EME2 interacts with MUS81 to form a DNA structure-specific endonuclease which cleaves substrates such as 3'-flap structures. MUS81-EME2 is responsible for fork cleavage and restart in human cells. The MUS81-EME2 protein, whose actions are restricted to S phase, is also responsible for telomere maintenance in telomerase-negative ALT (Alternative Lengthening of Telomeres) cells. The nuclease domain of EME2 is a nuclease-like domain which is involved in targeting the MUS81-EME2 heterodimer complex to DNA.


:

Pssm-ID: 410858  Cd Length: 195  Bit Score: 244.93  E-value: 1.37e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823779  64 DQVLGRLVVCVDPAVLEDAGSDILMEALGTLGCECRIEPQHQARSLQWNVVRPDPAPSnvpLEAKAENEQEQLLLLEPQE 143
Cdd:cd20082    3 EQCLKSLTVCVDPALLQDAGSDVLLEALSSLEWRYSIEPQSLPHSITWRRELPQDEPC---CEAGTVEEDQVLMVLEPNE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823779 144 FLQGAAQLTQ-------------ITDPPCSIPWLSPKslTRSHLAVIGLDAYLWSHQLSSQKTwqlkksKEAHARGAISW 210
Cdd:cd20082   80 FLDMVASLKQvpngdgssgemesLLGPLFEYLNKDPT--KVVTLLVIGLDAYSWSNQLSGQKQ------KQLGSELGMTD 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 251823779 211 AEVEEILVLLQLHANLDVLLMASWQELSQYVCAFTRALSQLPSK 254
Cdd:cd20082  152 LDIEEALVFLQLHKNVSVLFLESWQELTDHVCAVTKALSKRPFK 195
 
Name Accession Description Interval E-value
XPF_nuclease_EME2 cd20082
XPF-like nuclease domain of crossover junction endonuclease EME2; EME2 interacts with MUS81 to ...
64-254 1.37e-80

XPF-like nuclease domain of crossover junction endonuclease EME2; EME2 interacts with MUS81 to form a DNA structure-specific endonuclease which cleaves substrates such as 3'-flap structures. MUS81-EME2 is responsible for fork cleavage and restart in human cells. The MUS81-EME2 protein, whose actions are restricted to S phase, is also responsible for telomere maintenance in telomerase-negative ALT (Alternative Lengthening of Telomeres) cells. The nuclease domain of EME2 is a nuclease-like domain which is involved in targeting the MUS81-EME2 heterodimer complex to DNA.


Pssm-ID: 410858  Cd Length: 195  Bit Score: 244.93  E-value: 1.37e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823779  64 DQVLGRLVVCVDPAVLEDAGSDILMEALGTLGCECRIEPQHQARSLQWNVVRPDPAPSnvpLEAKAENEQEQLLLLEPQE 143
Cdd:cd20082    3 EQCLKSLTVCVDPALLQDAGSDVLLEALSSLEWRYSIEPQSLPHSITWRRELPQDEPC---CEAGTVEEDQVLMVLEPNE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823779 144 FLQGAAQLTQ-------------ITDPPCSIPWLSPKslTRSHLAVIGLDAYLWSHQLSSQKTwqlkksKEAHARGAISW 210
Cdd:cd20082   80 FLDMVASLKQvpngdgssgemesLLGPLFEYLNKDPT--KVVTLLVIGLDAYSWSNQLSGQKQ------KQLGSELGMTD 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 251823779 211 AEVEEILVLLQLHANLDVLLMASWQELSQYVCAFTRALSQLPSK 254
Cdd:cd20082  152 LDIEEALVFLQLHKNVSVLFLESWQELTDHVCAVTKALSKRPFK 195
ERCC4 pfam02732
ERCC4 domain; This domain is a family of nucleases. The family includes EME1 which is an ...
74-244 2.47e-05

ERCC4 domain; This domain is a family of nucleases. The family includes EME1 which is an essential component of a Holliday junction resolvase. EME1 interacts with MUS81 to form a DNA structure-specific endonuclease.


Pssm-ID: 426945 [Multi-domain]  Cd Length: 139  Bit Score: 43.57  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823779   74 VDPAVLEdagSDILMEALGTLGCECRIEPQHQARSLqWnvvrpdpapsnVPLEAKAENEQEQLLLLEPQEFLQGAAQLT- 152
Cdd:pfam02732   1 VDTRELR---SSIPELLLEELGVEVVVETLPVGDYL-W-----------VPREYDLELEVVLDVIVERKSLDDLVSSIId 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823779  153 -----QITDppcsipwLSpKSLTRSHLAVIGLDAylWSHQLSSQKTWqlkkskeahargaISWAEVEEILVLLQLHANLD 227
Cdd:pfam02732  66 grlfeQKSR-------LK-RGYKKPILLVEGLDL--FSRKLKNKRRD-------------INPNAIEGALASLQVDYGVR 122
                         170
                  ....*....|....*..
gi 251823779  228 VLLMASWQELSQYVCAF 244
Cdd:pfam02732 123 IIRTRSAEETAEWLASL 139
 
Name Accession Description Interval E-value
XPF_nuclease_EME2 cd20082
XPF-like nuclease domain of crossover junction endonuclease EME2; EME2 interacts with MUS81 to ...
64-254 1.37e-80

XPF-like nuclease domain of crossover junction endonuclease EME2; EME2 interacts with MUS81 to form a DNA structure-specific endonuclease which cleaves substrates such as 3'-flap structures. MUS81-EME2 is responsible for fork cleavage and restart in human cells. The MUS81-EME2 protein, whose actions are restricted to S phase, is also responsible for telomere maintenance in telomerase-negative ALT (Alternative Lengthening of Telomeres) cells. The nuclease domain of EME2 is a nuclease-like domain which is involved in targeting the MUS81-EME2 heterodimer complex to DNA.


Pssm-ID: 410858  Cd Length: 195  Bit Score: 244.93  E-value: 1.37e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823779  64 DQVLGRLVVCVDPAVLEDAGSDILMEALGTLGCECRIEPQHQARSLQWNVVRPDPAPSnvpLEAKAENEQEQLLLLEPQE 143
Cdd:cd20082    3 EQCLKSLTVCVDPALLQDAGSDVLLEALSSLEWRYSIEPQSLPHSITWRRELPQDEPC---CEAGTVEEDQVLMVLEPNE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823779 144 FLQGAAQLTQ-------------ITDPPCSIPWLSPKslTRSHLAVIGLDAYLWSHQLSSQKTwqlkksKEAHARGAISW 210
Cdd:cd20082   80 FLDMVASLKQvpngdgssgemesLLGPLFEYLNKDPT--KVVTLLVIGLDAYSWSNQLSGQKQ------KQLGSELGMTD 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 251823779 211 AEVEEILVLLQLHANLDVLLMASWQELSQYVCAFTRALSQLPSK 254
Cdd:cd20082  152 LDIEEALVFLQLHKNVSVLFLESWQELTDHVCAVTKALSKRPFK 195
XPF_nuclease_EME cd20083
XPF-like nuclease domain of crossover junction endonucleases, EME1, EME2 and similar proteins; ...
70-254 2.28e-34

XPF-like nuclease domain of crossover junction endonucleases, EME1, EME2 and similar proteins; The Mus81-EME1 complex is a structure-selective endonuclease with a critical role in the resolution of recombination intermediates during DNA repair after interstrand cross-links, replication fork collapse, or double-strand breaks. ERCC4 domain of Eme1 is a nuclease-like domain which is involved in targeting the MUS81-EME1 heterodimer complex to DNA.


Pssm-ID: 410859  Cd Length: 179  Bit Score: 125.09  E-value: 2.28e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823779  70 LVVCVDPAVLEDAGSDILMEALGTLGCECRIEPQHQARSLQW--NVVRPDPAPSNVPLEAKAENEQEQLLLLEPQEFLQG 147
Cdd:cd20083    2 IRVVIDPKILEESYGGELLSALQEKGLKYEIESQPIPNSITWtrNVPEDTVADNEVALEESEEDEPYVLLILSAEEFVKM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823779 148 AAQLTqITDPPCSIPWLSPksLTRSHLAVIGLDAYLWSHQLSSQKTWQLKKSKEahargaISWAEVEEILVLLQLHANLD 227
Cdd:cd20083   82 VKNGT-LLDHISSVKSLFP--NYPITLVIYGLNKYKRYHKKKEQSKKKKKNLKN------VSRPPVEEALIELQLHAKCS 152
                        170       180
                 ....*....|....*....|....*..
gi 251823779 228 VLLMASWQELSQYVCAFTRALSQLPSK 254
Cdd:cd20083  153 SRLCETEAELALHVAQLTKAIAEAPYK 179
XPF_nuclease_EME1 cd20081
XPF-like nuclease domain of crossover junction endonuclease EME1; EME1, also called MMS4 ...
64-257 5.17e-18

XPF-like nuclease domain of crossover junction endonuclease EME1; EME1, also called MMS4 homolog (hMMS4), interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Its typical substrates include 3'-flap structures, replication forks and nicked Holliday junctions. EME1 may be required in mitosis for the processing of stalled or collapsed replication forks. The nuclease domain of EME1 is a nuclease-like domain which is involved in targeting the MUS81-EME1 heterodimer complex to DNA.


Pssm-ID: 410857  Cd Length: 179  Bit Score: 80.95  E-value: 5.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823779  64 DQVLGRLVVCVDPAVLEDAGSDILMEALGTLGCECRIEPQHQARSLQWNVVRPDPAPSN------------VPLE---AK 128
Cdd:cd20081    3 EECLKHIVVVLDPGLLQMEGGGQLLSALQAMECSCVIEAQAIPRSVTWRRRAAPSQVDEedwveeptvlvlLPAEefvSM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823779 129 AEN-EQEQL-LLLEPQEFLQGAAQltQITDppcSIPWLSPKsltrshLAVIGLDAYLwshqlssqktwqlkkskeaharg 206
Cdd:cd20081   83 VHNyKQESLgSTTEGKETLQSFVT--DITA---KTAGKALS------LVVVDMEKYF----------------------- 128
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 251823779 207 AISWAEVEEILVLLQLHANLDVLLMASWQELSQYVCAFTRALSQLPSKQHR 257
Cdd:cd20081  129 RVSRVDVEEALVDLQLHTGVQVQFLETWKEFADFICMFTKAVAEAPFKKLR 179
ERCC4 pfam02732
ERCC4 domain; This domain is a family of nucleases. The family includes EME1 which is an ...
74-244 2.47e-05

ERCC4 domain; This domain is a family of nucleases. The family includes EME1 which is an essential component of a Holliday junction resolvase. EME1 interacts with MUS81 to form a DNA structure-specific endonuclease.


Pssm-ID: 426945 [Multi-domain]  Cd Length: 139  Bit Score: 43.57  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823779   74 VDPAVLEdagSDILMEALGTLGCECRIEPQHQARSLqWnvvrpdpapsnVPLEAKAENEQEQLLLLEPQEFLQGAAQLT- 152
Cdd:pfam02732   1 VDTRELR---SSIPELLLEELGVEVVVETLPVGDYL-W-----------VPREYDLELEVVLDVIVERKSLDDLVSSIId 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823779  153 -----QITDppcsipwLSpKSLTRSHLAVIGLDAylWSHQLSSQKTWqlkkskeahargaISWAEVEEILVLLQLHANLD 227
Cdd:pfam02732  66 grlfeQKSR-------LK-RGYKKPILLVEGLDL--FSRKLKNKRRD-------------INPNAIEGALASLQVDYGVR 122
                         170
                  ....*....|....*..
gi 251823779  228 VLLMASWQELSQYVCAF 244
Cdd:pfam02732 123 IIRTRSAEETAEWLASL 139
XPF_nuclease_EME-like cd20080
XPF-like nuclease domain of the family of Essential Meiotic Endonucleases (EMEs) and similar ...
69-254 7.19e-04

XPF-like nuclease domain of the family of Essential Meiotic Endonucleases (EMEs) and similar proteins; The family of EMEs includes EME1 and EME2. EME1, also called MMS4 homolog (hMMS4), interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Its typical substrates include 3'-flap structures, replication forks and nicked Holliday junctions. EME1 may be required in mitosis for the processing of stalled or collapsed replication forks. EME2 interacts with MUS81 to form a DNA structure-specific endonuclease which cleaves substrates such as 3'-flap structures. MUS81-EME2 is responsible for fork cleavage and restart in human cells. The MUS81-EME2 protein, whose actions are restricted to S phase, is also responsible for telomere maintenance in telomerase-negative ALT (Alternative Lengthening of Telomeres) cells. The nuclease domain of EMEs is a nuclease-like domain which is involved in targeting the MUS81-EME heterodimer complex to DNA. The family also includes budding yeast Mms4 (also known as Eme1 in other organisms), a putative transcriptional (co)activator that protects Saccharomyces cerevisiae cells from endogenous and environmental DNA damage. It interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. The nuclease domain of Mms4 lacks the catalytic motif.


Pssm-ID: 410856  Cd Length: 164  Bit Score: 40.06  E-value: 7.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823779  69 RLVVCVDPAVLEDAGSDILMEALGTLGCECRIEPQHQARSLQWnVVRPDPAPS-----NVPLEAKAENEQEQLLLLEPQE 143
Cdd:cd20080    1 HIIVVLDPVLLQLEGGGQLLGALQTAECRCVIEAQAVPCSVTW-RRRAGPSEDredwvEEPTVLVLLRAEAFVSYIDNGK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823779 144 F------LQGAAQLTQ-ITDppcsipwLSPKSLTR--SHLAVIgldaylwshqlssqktwqLKKSKeahargaiswAEVE 214
Cdd:cd20080   80 QgsldstMKGKETLQGfVTD-------ITAKTAGKalSLVIVD------------------QEKIR----------VDAE 124
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 251823779 215 EILVLLQLHANLDVLLMASWQELSQYVCAFTRALSQLPSK 254
Cdd:cd20080  125 EALVDLQLHTEAQAQIVQSWKELADFTCAFTKAVAEAPFK 164
 
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