SGID Silkworm Genome Informatics Database
Gene
KWMTBOMO12176  Validated by peptides from experiments
Pre Gene Modal
BGIBMGA004227
Annotation
flap_endonuclease-1_[Bombyx_mori]
Full name
Flap endonuclease 1      
Alternative Name
Flap structure-specific endonuclease 1
Location in the cell
Cytoplasmic   Reliability : 3.031
 

Sequence

CDS
ATGGGTATTCTAGGTTTATCTAAGTTAATTGCTGACATAGCACCTCATGCTGTCAAAGAAATGGAAATCAAAAATTACTTTGGAAGAAAAATAGCTATTGATGCTTCTATGAGCTTATATCAGTTCCTTATCGCCGTAAGAAGTGAAGGAGCCCAACTAGTCTCTGTAGACGGAGAGACTACATCACATCTGATGGGTACATTTTACCGTACTATAAGACTGGTAGAAAATGGGATTAAACCAGTGTATGTCTTTGACGGGAAACCTCCAGACATGAAGGCTCATCAGTTGAATAAGAGAGCAGAAAGGAGAGAGGAAGCAGAGAAAGAATTGCAAAAAGCTACTGAAGCCGGTGACACAGCTTCAGTGGACAAGTTCAACAGACGTTTGGTTAAAGTAACAAAACAACACAGTGAAGAGGCTAAACAACTCCTCAAATTGATGGGTGTCCCGGTTGTTGATGCACCCTGTGAGGCTGAAGCCCAGTGTGCAGCTCTTGTAAAATCCGGTAAAGTTTTTGCAGCAGCCACAGAAGATATGGATGCCCTAACCTTTGGTGCACCAGTGCTATTGAGACACTTAACGTTTTCTGAAGCAAGGAAAATGCCCGTGCAAGAATTCCATTTAAATAATGTACTACAGGGATTGGAATTGAAACAGAATGAGTTTATTGACCTCTGCATACTCCTTGGCTGTGATTACTGTGGTTCCATTAGAGGGGTTGGCCCAAAACGAGCCATCGACCTCATAAGACAACATCGGACACTGGATGAAGTACTCAAGAATATAGACACTGAGAAGTACCAACCTCCCACTGACTGGGATTACGAGCGAGCTAGGAGTCTGTTCATGGAACCTGAAGTCGCTGACCCTAAAGACATTGAGCTGAAATGGACTGATCCCGATGAAGAGGGCCTCGTGAAGTTTCTGTGTGGGGACAGACAGTTCAATGAAGAACGAGTGAGGAATGGAGCTAAGAAGTTAATTAAAGCCAGGACGGGCACCACACAGGCCAGATTAGATGGGTTCTTCACGTTAACGACAACGCCTAATTCGAAACGTAAAGCTGAAGAGGACAAGAAGAATTCAGCAAAGAAGAAAACTAAGACCGGAGGTGGAGGACGCGGTCGGAAACCGAAATGA
Protein
MGILGLSKLIADIAPHAVKEMEIKNYFGRKIAIDASMSLYQFLIAVRSEGAQLVSVDGETTSHLMGTFYRTIRLVENGIKPVYVFDGKPPDMKAHQLNKRAERREEAEKELQKATEAGDTASVDKFNRRLVKVTKQHSEEAKQLLKLMGVPVVDAPCEAEAQCAALVKSGKVFAAATEDMDALTFGAPVLLRHLTFSEARKMPVQEFHLNNVLQGLELKQNEFIDLCILLGCDYCGSIRGVGPKRAIDLIRQHRTLDEVLKNIDTEKYQPPTDWDYERARSLFMEPEVADPKDIELKWTDPDEEGLVKFLCGDRQFNEERVRNGAKKLIKARTGTTQARLDGFFTLTTTPNSKRKAEEDKKNSAKKKTKTGGGGRGRKPK

Summary

Description
Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structurs that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.
Cofactor
Mg(2+)
Subunit
Interacts with PCNA. Three molecules of 101741812 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of Fen1 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of Fen1_1 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of FEN1 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of 100160968 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of 109401579 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of LOC108744458 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of CSON014361 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of CSON009372 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of 109542723 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of HaOG214678 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of LOC412308 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of 100114897 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of putative Flap endonuclease 1 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of 101891979 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of 8232021 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of Fen1_0 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of DsimGD25512 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of LOC108090516 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Similarity
Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily.
Keywords
Complete proteome   DNA damage   DNA repair   DNA replication   Endonuclease   Exonuclease   Hydrolase   Magnesium   Metal-binding   Mitochondrion   Nuclease   Nucleus   Phosphoprotein   Reference proteome  
Feature
chain  Flap endonuclease 1
EC Number
3.1.-.-
EMBL
BABH01040234    FJ844436    ACY92094.1    NWSH01004790    PCG64683.1    ODYU01001261    + More
SOQ37231.1    GAIX01004327    JAA88233.1    KQ459053    KPJ04199.1    AGBW02009194    OWR51426.1    GBHO01045055    GBRD01011951    GDHC01020956    JAF98548.1    JAG53873.1    JAP97672.1    NEVH01024527    PNF17057.1    GEZM01007136    JAV95354.1    PNF17059.1    GFXV01008178    MBW19983.1    GGMS01008407    MBY77610.1    CH477362    KQ971352    EFA06383.1    ABLF02010587    JXUM01069301    KQ562544    KXJ75657.1    ACPB03005124    GBBI01002398    JAC16314.1    KK852513    KDR22281.1    GL888398    EGI61676.1    KQ981720    KYN37295.1    GFDL01003374    JAV31671.1    GL445323    EFN89831.1    ADTU01013894    GANO01000755    JAB59116.1    KQ976417    KYM89616.1    UFQS01000794    UFQT01000794    SSX06945.1    SSX27289.1    KQ977019    KYN06276.1    CH940648    LBMM01000187    KMR04549.1    KQ982080    KYQ60174.1    AXCM01000772    UFQS01003718    UFQT01003718    SSX15877.1    SSX35220.1    CH916367    KQ765071    OAD54145.1    APGK01052259    BT128613    KB741211    KB632263    AEE63570.1    ENN72811.1    ERL90946.1    KK107109    QOIP01000008    EZA59309.1    RLU19537.1    AXCN02002114    KZ150433    PZC70885.1    GGFK01009125    MBW42446.1    ADMH02000540    ETN66057.1    KQ414666    KOC65019.1    GL441701    EFN64391.1    ATLV01022351    KE525331    KFB47549.1    APCN01001943    KZ288186    PBC34739.1    GGFK01009126    MBW42447.1    AAAB01008966    KQ434839    KZC08018.1    GGFJ01006334    MBW55475.1    CVRI01000063    CRL04575.1    CH933808    KQ981145    KYN09135.1    GAMC01010575    JAB95980.1    AAZO01004118    DS235357    EEB15188.1    GDRN01086084    JAI61239.1    NNAY01000337    OXU29107.1    OUUW01000001    SPP74629.1    GAKP01016084    JAC42868.1    GBYB01001137    JAG70904.1    CH674335    CH479183    CM000158    KB201262    ESO98353.1    CH902619    GDHF01032604    GDHF01026005    JAI19710.1    JAI26309.1    AE013599    AL031863    BT100031    KQ435876    KOX70179.1    CH954179    CM002911    KMY94377.1    DS469531    CM000362    CH480816    GGFJ01006456    MBW55597.1    EZ423697    GDIQ01253391    JAJ98333.1    GEBQ01013403    JAT26574.1    GDIP01102844    JAM00871.1   
Pfam
PF00752   XPG_N        + More
PF00867   XPG_I
Interpro
IPR006085   XPG_DNA_repair_N        + More
IPR023426   Flap_endonuc       
IPR036279   5-3_exonuclease_C_sf       
IPR029060   PIN-like_dom_sf       
IPR006086   XPG-I_dom       
IPR019974   XPG_CS       
IPR006084   XPG/Rad2       
IPR008918   HhH2       
IPR002421   5-3_exonuclease_N       
SUPFAM
SSF88723   SSF88723        + More
SSF47807   SSF47807       
PDB
1UL1     E-value=8.13901e-128,     Score=1170

Ontologies

Topology

Subcellular location
Mitochondrion   Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage.   With evidence from 1 publications.
Nucleus   Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage.   With evidence from 1 publications.
Nucleolus   Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage.   With evidence from 1 publications.
Nucleoplasm   Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage.   With evidence from 1 publications.
Length:
380
Number of predicted TMHs:
0
Exp number of AAs in TMHs:
0.00591
Exp number, first 60 AAs:
0.00383
Total prob of N-in:
0.00183
outside
1  -  380
 
 

Population Genetic Test Statistics

Pi
194.472224
Theta
161.164295
Tajima's D
0.85523
CLR
0.152995
CSRT
0.626218689065547
Interpretation
Uncertain
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