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Conserved domains on  [gi|1958657411|ref|XP_038941509|]
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crossover junction endonuclease EME1 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
XPF_nuclease-like super family cl41760
nuclease domain of XPF/MUS81 family proteins; The XPF/MUS81 family belongs to 3'-flap ...
1-190 3.56e-82

nuclease domain of XPF/MUS81 family proteins; The XPF/MUS81 family belongs to 3'-flap endonuclease that act upon 3'-flap structures and involved in DNA repair pathways that are necessary for the removal of UV-light-induced DNA lesions and cross-links between DNA strands. Family members exist either as heterodimers or as homodimers in their functionally competent states which consist of a catalytic and a noncatalytic subunit. The catalytic subunits have a DX(n)RKX(3)D motif. This motif is required for metal-dependent endonuclease activity but not for DNA junction binding. The equivalent regions of the noncatalytic subunits (ERCC1, EME1, and FAAP24) have diverged. The noncatalytic subunits have roles such as binding ssDNA or an ability to target the endonuclease to defined DNA structures or sites of DNA damage.


The actual alignment was detected with superfamily member cd20081:

Pssm-ID: 425391  Cd Length: 179  Bit Score: 245.82  E-value: 3.56e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657411   1 MEGGGQLLGALQAMECSCVIEAQVVPQSITWRRKT-ELEEDGDDWVEEPTILVLVLKEVFMSMVYNSKQGNPGSTEKGKE 79
Cdd:cd20081    20 MEGGGQLLSALQAMECSCVIEAQAIPRSVTWRRRAaPSQVDEEDWVEEPTVLVLLPAEEFVSMVHNYKQESLGSTTEGKE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657411  80 TLRGFVTDVTART-GKALSLVIVDQEKCLRaqnppkrrksgmankkakekhqqrresstrlmVSRVDMEEALVDLQLYTE 158
Cdd:cd20081   100 TLQSFVTDITAKTaGKALSLVVVDMEKYFR--------------------------------VSRVDVEEALVDLQLHTG 147
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958657411 159 AQARIVQSWRELADFACAFTKAVAEAPFKKLR 190
Cdd:cd20081   148 VQVQFLETWKEFADFICMFTKAVAEAPFKKLR 179
 
Name Accession Description Interval E-value
XPF_nuclease_EME1 cd20081
XPF-like nuclease domain of crossover junction endonuclease EME1; EME1, also called MMS4 ...
1-190 3.56e-82

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: 245.82  E-value: 3.56e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657411   1 MEGGGQLLGALQAMECSCVIEAQVVPQSITWRRKT-ELEEDGDDWVEEPTILVLVLKEVFMSMVYNSKQGNPGSTEKGKE 79
Cdd:cd20081    20 MEGGGQLLSALQAMECSCVIEAQAIPRSVTWRRRAaPSQVDEEDWVEEPTVLVLLPAEEFVSMVHNYKQESLGSTTEGKE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657411  80 TLRGFVTDVTART-GKALSLVIVDQEKCLRaqnppkrrksgmankkakekhqqrresstrlmVSRVDMEEALVDLQLYTE 158
Cdd:cd20081   100 TLQSFVTDITAKTaGKALSLVVVDMEKYFR--------------------------------VSRVDVEEALVDLQLHTG 147
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958657411 159 AQARIVQSWRELADFACAFTKAVAEAPFKKLR 190
Cdd:cd20081   148 VQVQFLETWKEFADFICMFTKAVAEAPFKKLR 179
 
Name Accession Description Interval E-value
XPF_nuclease_EME1 cd20081
XPF-like nuclease domain of crossover junction endonuclease EME1; EME1, also called MMS4 ...
1-190 3.56e-82

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: 245.82  E-value: 3.56e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657411   1 MEGGGQLLGALQAMECSCVIEAQVVPQSITWRRKT-ELEEDGDDWVEEPTILVLVLKEVFMSMVYNSKQGNPGSTEKGKE 79
Cdd:cd20081    20 MEGGGQLLSALQAMECSCVIEAQAIPRSVTWRRRAaPSQVDEEDWVEEPTVLVLLPAEEFVSMVHNYKQESLGSTTEGKE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657411  80 TLRGFVTDVTART-GKALSLVIVDQEKCLRaqnppkrrksgmankkakekhqqrresstrlmVSRVDMEEALVDLQLYTE 158
Cdd:cd20081   100 TLQSFVTDITAKTaGKALSLVVVDMEKYFR--------------------------------VSRVDVEEALVDLQLHTG 147
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958657411 159 AQARIVQSWRELADFACAFTKAVAEAPFKKLR 190
Cdd:cd20081   148 VQVQFLETWKEFADFICMFTKAVAEAPFKKLR 179
XPF_nuclease_EME-like cd20080
XPF-like nuclease domain of the family of Essential Meiotic Endonucleases (EMEs) and similar ...
1-187 4.92e-55

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: 176.42  E-value: 4.92e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657411   1 MEGGGQLLGALQAMECSCVIEAQVVPQSITWRRKTELEEDGDDWVEEPTILVLVLKEVFMSMVYNSKQGNPGSTEKGKET 80
Cdd:cd20080    13 LEGGGQLLGALQTAECRCVIEAQAVPCSVTWRRRAGPSEDREDWVEEPTVLVLLRAEAFVSYIDNGKQGSLDSTMKGKET 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657411  81 LRGFVTDVTART-GKALSLVIVDQEKClraqnppkrrksgmankkakekhqqrresstrlmvsRVDMEEALVDLQLYTEA 159
Cdd:cd20080    93 LQGFVTDITAKTaGKALSLVIVDQEKI------------------------------------RVDAEEALVDLQLHTEA 136
                         170       180
                  ....*....|....*....|....*...
gi 1958657411 160 QARIVQSWRELADFACAFTKAVAEAPFK 187
Cdd:cd20080   137 QAQIVQSWKELADFTCAFTKAVAEAPFK 164
XPF_nuclease_EME cd20083
XPF-like nuclease domain of crossover junction endonucleases, EME1, EME2 and similar proteins; ...
1-187 2.04e-37

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: 131.25  E-value: 2.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657411   1 MEGGGQLLGALQAMECSCVIEAQVVPQSITWRRKTELE-------EDGDDWVEEPTILVLVLKEVFMSMVYNskqgnpgs 73
Cdd:cd20083    13 ESYGGELLSALQEKGLKYEIESQPIPNSITWTRNVPEDtvadnevALEESEEDEPYVLLILSAEEFVKMVKN-------- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657411  74 tekgkETLRGFVTDVTART-GKALSLVIVDQEKCLRAQNPPKRRKSGMANKKakekhqqrresstrlMVSRVDMEEALVD 152
Cdd:cd20083    85 -----GTLLDHISSVKSLFpNYPITLVIYGLNKYKRYHKKKEQSKKKKKNLK---------------NVSRPPVEEALIE 144
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958657411 153 LQLYTEAQARIVQSWRELADFACAFTKAVAEAPFK 187
Cdd:cd20083   145 LQLHAKCSSRLCETEAELALHVAQLTKAIAEAPYK 179
XPF_nuclease_EME2 cd20082
XPF-like nuclease domain of crossover junction endonuclease EME2; EME2 interacts with MUS81 to ...
7-187 7.61e-31

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: 114.73  E-value: 7.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657411   7 LLGALQAMECSCVIEAQVVPQSITWRRKT-ELEEDGDDW-VEEPTILVLVLKEVFMSMVYNSKQG-NPGSTEKGKETLRG 83
Cdd:cd20082    26 LLEALSSLEWRYSIEPQSLPHSITWRRELpQDEPCCEAGtVEEDQVLMVLEPNEFLDMVASLKQVpNGDGSSGEMESLLG 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657411  84 FVTDVTART-GKALSLVIVDQEKclraqnppkRRKSGmankkaKEKHQQRRESSTRLMVSRVDMEEALVDLQLYTEAQAR 162
Cdd:cd20082   106 PLFEYLNKDpTKVVTLLVIGLDA---------YSWSN------QLSGQKQKQLGSELGMTDLDIEEALVFLQLHKNVSVL 170
                         170       180
                  ....*....|....*....|....*
gi 1958657411 163 IVQSWRELADFACAFTKAVAEAPFK 187
Cdd:cd20082   171 FLESWQELTDHVCAVTKALSKRPFK 195
XPF_nuclease-like cd19940
nuclease domain of XPF/MUS81 family proteins; The XPF/MUS81 family belongs to 3'-flap ...
2-179 3.51e-15

nuclease domain of XPF/MUS81 family proteins; The XPF/MUS81 family belongs to 3'-flap endonuclease that act upon 3'-flap structures and involved in DNA repair pathways that are necessary for the removal of UV-light-induced DNA lesions and cross-links between DNA strands. Family members exist either as heterodimers or as homodimers in their functionally competent states which consist of a catalytic and a noncatalytic subunit. The catalytic subunits have a DX(n)RKX(3)D motif. This motif is required for metal-dependent endonuclease activity but not for DNA junction binding. The equivalent regions of the noncatalytic subunits (ERCC1, EME1, and FAAP24) have diverged. The noncatalytic subunits have roles such as binding ssDNA or an ability to target the endonuclease to defined DNA structures or sites of DNA damage.


Pssm-ID: 410849 [Multi-domain]  Cd Length: 126  Bit Score: 70.87  E-value: 3.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657411   2 EGGGQLLGALQAMECSCVIEAQVVPqSITWRRkteleedgddwveePTILVLVLKEVFMSMVYnskqgnpgstekgKETL 81
Cdd:cd19940     8 ERRSELLSELQRLGVQVEFEDLAVG-DYVLSN--------------RTCVERKSLSDLVSSIN-------------KGRL 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657411  82 RGFVTDVTaRTGKALSLVIVDQEKClraqnppkrrksgmankkakekhqqrressTRLMVSRVDMEEALVDLQLYTEAQA 161
Cdd:cd19940    60 REQLQRLT-RKFERRVLLVEKDRSK------------------------------FRSMVSSVQALSALTKLQLLTGIRL 108
                         170
                  ....*....|....*...
gi 1958657411 162 RIVQSWRELADFACAFTK 179
Cdd:cd19940   109 LIVASPKETADLLEELTQ 126
 
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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