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Database: UniProt
Entry: A0A061J5A9_TRYRA
LinkDB: A0A061J5A9_TRYRA
Original site: A0A061J5A9_TRYRA 
ID   A0A061J5A9_TRYRA        Unreviewed;       393 AA.
AC   A0A061J5A9;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   28-MAR-2018, entry version 26.
DE   RecName: Full=Flap endonuclease 1 {ECO:0000256|HAMAP-Rule:MF_03140};
DE            Short=FEN-1 {ECO:0000256|HAMAP-Rule:MF_03140};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_03140};
DE   AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000256|HAMAP-Rule:MF_03140};
GN   Name=FEN1 {ECO:0000256|HAMAP-Rule:MF_03140};
GN   ORFNames=TRSC58_02223 {ECO:0000313|EMBL:ESL10049.1};
OS   Trypanosoma rangeli SC58.
OC   Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma;
OC   Herpetosoma.
OX   NCBI_TaxID=429131 {ECO:0000313|EMBL:ESL10049.1, ECO:0000313|Proteomes:UP000031737};
RN   [1] {ECO:0000313|EMBL:ESL10049.1, ECO:0000313|Proteomes:UP000031737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC58 {ECO:0000313|EMBL:ESL10049.1,
RC   ECO:0000313|Proteomes:UP000031737};
RA   Stoco P.H., Wagner G., Gerber A., Zaha A., Thompson C.,
RA   Bartholomeu D.C., Luckemeyer D.D., Bahia D., Loreto E., Prestes E.B.,
RA   Lima F.M., Rodrigues-Luiz G., Vallejo G.A., Filho J.F., Monteiro K.M.,
RA   Tyler K.M., de Almeida L.G., Ortiz M.F., Siervo M.A., de Moraes M.H.,
RA   Cunha O.L., Mendonca-Neto R., Silva R., Teixeira S.M., Murta S.M.,
RA   Sincero T.C., Mendes T.A., Urmenyi T.P., Silva V.G., da Rocha W.D.,
RA   Andersson B., Romanha A.J., Steindel M., de Vasconcelos A.T.,
RA   Grisard E.C.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Structure-specific nuclease with 5'-flap endonuclease
CC       and 5'-3' exonuclease activities involved in DNA replication and
CC       repair. During DNA replication, cleaves the 5'-overhanging flap
CC       structure that is generated by displacement synthesis when DNA
CC       polymerase encounters the 5'-end of a downstream Okazaki fragment.
CC       It enters the flap from the 5'-end and then tracks to cleave the
CC       flap base, leaving a nick for ligation. Also involved in the long
CC       patch base excision repair (LP-BER) pathway, by cleaving within
CC       the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a
CC       genome stabilization factor that prevents flaps from equilibrating
CC       into structurs that lead to duplications and deletions. Also
CC       possesses 5'-3' exonuclease activity on nicked or gapped double-
CC       stranded DNA, and exhibits RNase H activity. Also involved in
CC       replication and repair of rDNA and in repairing mitochondrial DNA.
CC       {ECO:0000256|HAMAP-Rule:MF_03140, ECO:0000256|SAAS:SAAS00725765}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03140};
CC       Note=Binds 2 magnesium ions per subunit. They probably participate
CC       in the reaction catalyzed by the enzyme. May bind an additional
CC       third magnesium ion after substrate binding. {ECO:0000256|HAMAP-
CC       Rule:MF_03140};
CC   -!- SUBUNIT: Interacts with PCNA. Three molecules of FEN1 bind to one
CC       PCNA trimer with each molecule binding to one PCNA monomer. PCNA
CC       stimulates the nuclease activity without altering cleavage
CC       specificity. {ECO:0000256|HAMAP-Rule:MF_03140}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-
CC       Rule:MF_03140, ECO:0000256|SAAS:SAAS00725720}. Nucleus, nucleolus
CC       {ECO:0000256|HAMAP-Rule:MF_03140}. Nucleus, nucleoplasm
CC       {ECO:0000256|HAMAP-Rule:MF_03140}. Note=Resides mostly in the
CC       nucleoli and relocalizes to the nucleoplasm upon DNA damage.
CC       {ECO:0000256|HAMAP-Rule:MF_03140}.
CC   -!- PTM: Phosphorylated. Phosphorylation upon DNA damage induces
CC       relocalization to the nuclear plasma. {ECO:0000256|HAMAP-
CC       Rule:MF_03140}.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_03140}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03140}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ESL10049.1}.
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DR   EMBL; AUPL01002223; ESL10049.1; -; Genomic_DNA.
DR   EnsemblProtists; ESL10049; ESL10049; TRSC58_02223.
DR   Proteomes; UP000031737; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008409; F:5'-3' exonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0017108; F:5'-flap endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0043137; P:DNA replication, removal of RNA primer; IEA:UniProtKB-UniRule.
DR   CDD; cd09867; PIN_FEN1; 1.
DR   HAMAP; MF_00614; Fen; 1.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR   InterPro; IPR023426; Flap_endonuc.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR006086; XPG-I_dom.
DR   InterPro; IPR006084; XPG/Rad2.
DR   InterPro; IPR019974; XPG_CS.
DR   InterPro; IPR006085; XPG_DNA_repair_N.
DR   PANTHER; PTHR11081; PTHR11081; 1.
DR   Pfam; PF00867; XPG_I; 1.
DR   Pfam; PF00752; XPG_N; 1.
DR   PRINTS; PR00853; XPGRADSUPER.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00484; XPGI; 1.
DR   SMART; SM00485; XPGN; 1.
DR   SUPFAM; SSF47807; SSF47807; 1.
DR   SUPFAM; SSF88723; SSF88723; 1.
DR   PROSITE; PS00841; XPG_1; 1.
DR   PROSITE; PS00842; XPG_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031737};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_03140};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_03140};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_03140};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_03140,
KW   ECO:0000313|EMBL:ESL10049.1};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_03140};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_03140};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_03140};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03140};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03140,
KW   ECO:0000256|SAAS:SAAS00725731};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_03140};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03140,
KW   ECO:0000256|SAAS:SAAS00636222};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_03140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031737}.
FT   DOMAIN        1    111       XPGN. {ECO:0000259|SMART:SM00485}.
FT   DOMAIN      150    222       XPGI. {ECO:0000259|SMART:SM00484}.
FT   REGION      126    257       I-domain. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   REGION      340    348       Interaction with PCNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_03140}.
FT   COILED       98    121       {ECO:0000256|SAM:Coils}.
FT   METAL        34     34       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL        90     90       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       162    162       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       164    164       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       183    183       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       185    185       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       237    237       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   BINDING      74     74       DNA substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   BINDING     162    162       DNA substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   BINDING     235    235       DNA substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   BINDING     237    237       DNA substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
SQ   SEQUENCE   393 AA;  43971 MW;  AD0A1C820C6006AD CRC64;
     MGILGLSKLL YDRSPTAIRE HELKNYFGRR IAIDASMTIY QFLIAMKGFQ DGQGVELTNE
     AGEVTSHLNG LFARTLRMVD EGLRPIYVFD GKPPTLKASE LQERQRRAEE AQQLFEAAKE
     EGNDELMEKM SKRTVRVSKE QMGEAKKLLR LMGIPVVQAP SEAEAQCAEL VKKKKAWAVA
     TEDMDALTFG APVMLRHLTY SEAKKRPIAE FHLDEVLIMT GLTMPQFIDL CILLGCDYVP
     KIPGIGPQKA WEGIKKHGNI ETLLKSLDTA RHTVPDGFHY EEARQFFLAP EVTPGEEIDI
     QFREPDEEGL IKFLVEEKLF NRDRVVKGIQ RLRSALTRKT QGRLDQFFTI KKPAPKPGTG
     GTTAGVKRGH GAIALSGTLQ QKGSGGHKKM VKK
//
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