SGID Silkworm Genome Informatics Database
Gene
KWMTBOMO03495
Pre Gene Modal
BGIBMGA006347
Annotation
PREDICTED:_DNA_helicase_MCM9-like_isoform_X1_[Amyelois_transitella]
Full name
DNA helicase MCM9      
Alternative Name
Mini-chromosome maintenance deficient domain-containing protein 1
Minichromosome maintenance 9
Location in the cell
Nuclear   Reliability : 3.974
 

Sequence

CDS
ATGATTTTAGAATATATATTAAAGTTCCATTTGGATGATTGTTTTAATGTATTATCAGAAAAAGATAATCTAGGATATTTTAGCATTAAAATCGATTTTTTAAAATTATTTGAAAACCATCCTGATGTGGGAGACAGAGTTCTGTGTGCTCCCATTGAAACCCTGCCCATATGCAATAAAGATATAGTGATGGCCCAACAACACATTATAGAATCTGAGGAATTTAAAAATACAGTTTCGAAATTAGAATATGTTTTCGTAAAGAAGAATGTTCATGCCAGATTTTATGGTTTACCTGTTTGTCCGGAGTTACACAGAACAGTTTTCCCTAAAAATGTAGATCTGGGATGTTTTTTAAAAGTAACAGGTACAGTTGTCCGAGTGACCCAGTCCAAAATGTTGGAATATCAAAGAAAGTATGTCTGTATGAAATGCAAATATGAGAATTATGTTCAAGCAGATTTCGAAAGGAGATACATTCTTAAATCACCATCAAAATGTTGTAATATTGATCCAAAATGCAGAAGTACAATATTCTCACAAGTGAATCTTGTATCCAGAGAATATTGTAAAGATTATCAGGAAATAAAAATTCAGGAGCAAGTTAACAAGCTTAGCATTGGTACCATTCCAGGCTCATTCTGGGTGGTTTTAGAAGATGATTTAGTAGATTGTTGTAAACCTGGTGATGATGTTATAATTTGCGGTACTATTAGAAGACGTTGGCGACCATCATTTCAAACAAAAAAATCTGAAGTGGAACTAGTCCTCCAAGCAAATTACATAGAAGTGTGTAATGCGCTAAGATCTAAAGTGGTAGCCACAGCTCCTGACATAAAAGAATGCTTTGACAGTTTCTGGTCTTACTATGATTCGTGTCCTTTGAAAGGCAGAGATCATATACTTAGATCGATTTGTCCTCAAGTCTACGGTCTACATTTGGTAAAGTTGGCTGTGTTGCTCACGGTGATTACCGGATCGAATCACATAGTCGAGGAAACAGATGAAAAGAATACATCCTTTGACGATAATCATCATACAAAAGTGCGGGGTCAGTGTCATCTCCTGTTAGTTGGAGATCCAGGCACTGGGAAGTCGCAACTGCTTCGTTCAGGAGCAGATCTGACTTCGCGTTCGGTGTTCACTTCGGGAGCTGGCAGTACGCGAGCCGGCCTCACGTGTGCTGCGCTCAGGGAAGACGGCGAGTGGCAGCTAGAAGCTGGAGCACTGGTTCTGTCGGACGGCGGCGTGTGCTGTATAGATGAGATCTCCCAGCTGAAGGAGCACGACCGTACCGCCATACACGAGGCGATGGAGCAACAGACAATCTCCATAGCCAAGGCAGGTATAGTCTGCAAATTGAACACACGTTGTGCTGTGATAGCAGCCTGCAATCCTAAGGGGAACTACGATTCAAATCAACCGCTCAGTATGAATTTAGCACTTGGAACGCCACTTTTGAGCCGATTTGATCTAATTTTCATTCTATTGGATACAAAAAATAAAGCTTGGGATAAACTTGTATCTTCTTATATATTGTTCGGTGATTCAAATTTAGAACAAAATAAAAAATATTGGAATCTCGAAAAATTGCAGATGTACATTAGTCTAGTGGGACCAAGGACGACAAAGATGACAAAATCGGCAAACATTATCCTGCAATCGTATTATATGGCCCAGAGAAAAGCCGAAAGCAGAGATCCATCACGTACTACCGTGAGAATGCTCGACAGTCTGGTCAGACTATCACAAGCTCACTGCCGTTTGATGTATAGAACAACAATATATCCGATGGACGCCATTATAGCCGTATCTTTAGTAGATTTATCAATGCAAGACTGCACTTTATCAGACACTGCGGATGCGCTACATTCCAATTTCTATAAATACCCTGACTTTGAATACCTATGCACAGCAAAAAAACTATTAACAAAATTAAATTTGTACGAAATATGGCGAAATGAATTATTACACTACGGTAAATTACTTCAGGTCGATCACAAAACATTGGAACATGACATTGATAGCGGAATCATTAAGCTTTTCGCGAAATATGATGATGTCGCCGATGAAAATACACCTTTGTCAGCATCGGTAATAACAAGTTCTTATTTTAAGAAAGAAGAAAATGGATTGTTACATAATGACAAAAACAGTTTACCCGATGAAGAGAACAAAGATATCATAGAAGTAAATAAAATGTTGGCAGTGACATTGAAAAAACACGCAACTTTAAATAGAGACGAAAGAAAACTACCAGTAGCTCAGAAAAAACCTCAAAATAAAAGAAAACGGAAAGAAGTTACTGTGAATTCAAAAATTCTTAAAAGTTTAGTTCCTAAAAAGCGTAAGAAATCAAAGGAGGAAGTAAGGGATGCCAGTAGTCCTACAAACATTGACGTTGACCAGAATCATCTCTTAAATGCAGTGCCTAGTGTTAATGATGTGTTTGCAGAGTACGGTATCAATCTTAAGTTTGAAGGTGAAAGTCAACATAAATCAAGTGGTAAAAGAATCGAATTAAAAGAAAATAAGATTGATAATGAAATCATTGTTCCTAGAATTGAAAAAAAGGATCTTGTAGAAAACAAAACTAATTCTCATAAAGAACAAAATGCAAATATCTCAACAATAAATAAATTAAAACAGTTCGCATGTGAACAAAAATATAACATTGATAAATATGAAGAAAAGTTATCGATATCTGAATACAACAACAGTTTTAAATTTAATATTGAGAGTAAAAGTACAAATGCAGTTCAAGATAAGTCTGAACGAAGTTCCCAAATATCAATTTTTGAAAGTTCAGATTGTGATATTGATTTAGATTTATGA
Protein
MILEYILKFHLDDCFNVLSEKDNLGYFSIKIDFLKLFENHPDVGDRVLCAPIETLPICNKDIVMAQQHIIESEEFKNTVSKLEYVFVKKNVHARFYGLPVCPELHRTVFPKNVDLGCFLKVTGTVVRVTQSKMLEYQRKYVCMKCKYENYVQADFERRYILKSPSKCCNIDPKCRSTIFSQVNLVSREYCKDYQEIKIQEQVNKLSIGTIPGSFWVVLEDDLVDCCKPGDDVIICGTIRRRWRPSFQTKKSEVELVLQANYIEVCNALRSKVVATAPDIKECFDSFWSYYDSCPLKGRDHILRSICPQVYGLHLVKLAVLLTVITGSNHIVEETDEKNTSFDDNHHTKVRGQCHLLLVGDPGTGKSQLLRSGADLTSRSVFTSGAGSTRAGLTCAALREDGEWQLEAGALVLSDGGVCCIDEISQLKEHDRTAIHEAMEQQTISIAKAGIVCKLNTRCAVIAACNPKGNYDSNQPLSMNLALGTPLLSRFDLIFILLDTKNKAWDKLVSSYILFGDSNLEQNKKYWNLEKLQMYISLVGPRTTKMTKSANIILQSYYMAQRKAESRDPSRTTVRMLDSLVRLSQAHCRLMYRTTIYPMDAIIAVSLVDLSMQDCTLSDTADALHSNFYKYPDFEYLCTAKKLLTKLNLYEIWRNELLHYGKLLQVDHKTLEHDIDSGIIKLFAKYDDVADENTPLSASVITSSYFKKEENGLLHNDKNSLPDEENKDIIEVNKMLAVTLKKHATLNRDERKLPVAQKKPQNKRKRKEVTVNSKILKSLVPKKRKKSKEEVRDASSPTNIDVDQNHLLNAVPSVNDVFAEYGINLKFEGESQHKSSGKRIELKENKIDNEIIVPRIEKKDLVENKTNSHKEQNANISTINKLKQFACEQKYNIDKYEEKLSISEYNNSFKFNIESKSTNAVQDKSERSSQISIFESSDCDIDLDL

Summary

Description
Component of the MCM8-MCM9 complex, a complex involved in the repair of double-stranded DNA breaks (DBSs) and DNA interstrand cross-links (ICLs) by homologous recombination (HR) (PubMed:23401855, PubMed:22771120). Required for DNA resection by the MRE11-RAD50-NBN/NBS1 (MRN) complex at double-stranded DNA breaks to generate ssDNA by recruiting the MRN complex to the repair site and by promoting the complex nuclease activity (By similarity). Probably by regulating the localization of the MNR complex, indirectly regulates the recruitment of downstream effector RAD51 to DNA damage sites including DBSs and ICLs (PubMed:22771120, PubMed:23401855). Acts as a helicase in DNA mismatch repair (MMR) following DNA replication errors to unwind the mismatch containing DNA strand (PubMed:22771120, PubMed:26300262). In addition, recruits MLH1, a component of the MMR complex, to chromatin (By similarity). The MCM8-MCM9 complex is dispensable for DNA replication and S phase progression (PubMed:21987787). Probably by regulating HR, plays a key role during gametogenesis (PubMed:21987787, PubMed:22771120).
Component of the MCM8-MCM9 complex, a complex involved in the repair of double-stranded DNA breaks (DBSs) and DNA interstrand cross-links (ICLs) by homologous recombination (HR) (PubMed:23401855). Required for DNA resection by the MRE11-RAD50-NBN/NBS1 (MRN) complex by recruiting the MRN complex to the repair site and by promoting the complex nuclease activity (PubMed:26215093). Probably by regulating the localization of the MRN complex, indirectly regulates the recruitment of downstream effector RAD51 to DNA damage sites including DBSs and ICLs (PubMed:23401855). Acts as a helicase in DNA mismatch repair (MMR) following DNA replication errors to unwind the mismatch containing DNA strand (PubMed:26300262). In addition, recruits MLH1, a component of the MMR complex, to chromatin (PubMed:26300262). The MCM8-MCM9 complex is dispensable for DNA replication and S phase progression (PubMed:23401855). Probably by regulating HR, plays a key role during gametogenesis (By similarity).
Component of the MCM8-MCM9 complex, a complex involved in homologous recombination repair following DNA interstrand cross-links and plays a key role during gametogenesis. The MCM8-MCM9 complex probably acts as a hexameric helicase required to process aberrant forks into homologous recombination substrates and to orchestrate homologous recombination with resection, fork stabilization and fork restart. In eggs, required for MCM2-7 loading onto chromatin during DNA replication. Probably not required for DNA replication in other cells (By similarity).
Catalytic Activity
ATP + H2O = ADP + H(+) + phosphate
Subunit
Component of the MCM8-MCM9 complex, which forms a hexamer composed of MCM8 and MCM9 (PubMed:22771120). Interacts with the DNA mismatch repair (MMR) complex composed at least of MSH2, MSH3, MSH6, PMS1 and MLH1 (By similarity). Interacts with MLH1; the interaction recruits MLH1 to chromatin (By similarity). Interacts with MSH2; the interaction recruits MCM9 to chromatin (By similarity). Interacts with MSH6 (By similarity). Interacts with the MRN complex composed of MRE11, RAD50 and NBN/NBS1; the interaction recruits the MRN complex to DNA damage sites (By similarity). Interacts with RAD51; the interaction recruits RAD51 to DNA damage sites (By similarity).
Component of the MCM8-MCM9 complex, which forms a hexamer composed of MCM8 and MCM9 (PubMed:23401855, PubMed:26300262, PubMed:26215093). Interacts with the DNA mismatch repair (MMR) complex composed at least of MSH2, MSH3, MSH6, PMS1 and MLH1 (PubMed:26300262). Interacts with MLH1; the interaction recruits MLH1 to chromatin (PubMed:26300262). Interacts with MSH2; the interaction recruits MCM9 to chromatin (PubMed:26300262). Interacts with MSH6 (PubMed:26300262). Interacts with the MRN complex composed of MRE11, RAD50 and NBN/NBS1; the interaction recruits the MRN complex to DNA damage sites (PubMed:26215093). Interacts with RAD51; the interaction recruits RAD51 to DNA damage sites (PubMed:23401855).
Component of the MCM8-MCM9 complex, which forms a hexamer composed of mcm8 and mcm9. Interacts with cdt1 (By similarity).
Similarity
Belongs to the MCM family.
Keywords
Alternative splicing   ATP-binding   Chromosome   Complete proteome   DNA damage   DNA repair   DNA-binding   Helicase   Hydrolase   Nucleotide-binding   Nucleus   Phosphoprotein   Reference proteome   DNA replication  
Feature
chain  DNA helicase MCM9
splice variant  In isoform 2.
EC Number
3.6.4.12
Pfam
PF17855   MCM_lid        + More
PF00493   MCM
PF17207   MCM_OB
PF08799   PRP4
PF02840   Prp18
Interpro
IPR001208   MCM_dom        + More
IPR031327   MCM       
IPR003593   AAA+_ATPase       
IPR012340   NA-bd_OB-fold       
IPR027417   P-loop_NTPase       
IPR033762   MCM_OB       
IPR041562   MCM_lid       
IPR004098   Prp18       
IPR036285   PRP4-like_sf       
IPR014906   PRP4-like       
IPR018525   MCM_CS       
SUPFAM
SSF50249   SSF50249        + More
SSF52540   SSF52540       
SSF158230   SSF158230       
Gene 3D
PDB
3F9V     E-value=2.13819e-77,     Score=739

Ontologies

Topology

Subcellular location
Nucleus   Colocalizes to nuclear foci with RPA1 following DNA damage (PubMed:23401855). Localizes to double-stranded DNA breaks (By similarity). Recruited to chromatin by MSH2 (By similarity).   With evidence from 1 publications.
Chromosome   Colocalizes to nuclear foci with RPA1 following DNA damage (PubMed:23401855). Localizes to double-stranded DNA breaks (By similarity). Recruited to chromatin by MSH2 (By similarity).   With evidence from 1 publications.
Length:
944
Number of predicted TMHs:
0
Exp number of AAs in TMHs:
0.0087
Exp number, first 60 AAs:
0
Total prob of N-in:
0.00028
outside
1  -  944
 
 

Population Genetic Test Statistics

Pi
203.925675
Theta
195.770812
Tajima's D
-1.796531
CLR
128.875481
CSRT
0.0284985750712464
Interpretation
Uncertain
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