ID A0A1I7VGW4_LOALO Unreviewed; 1147 AA.
AC A0A1I7VGW4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 39.
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};
OS Loa loa (Eye worm) (Filaria loa).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Loa.
OX NCBI_TaxID=7209 {ECO:0000313|Proteomes:UP000095285, ECO:0000313|WBParaSite:EN70_2422};
RN [1] {ECO:0000313|Proteomes:UP000095285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease;
RA Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Henn M.R.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Loa loa.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:EN70_2422}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- FUNCTION: Plays an important role in regulating the size of
CC autophagosomes during the formation process.
CC {ECO:0000256|ARBA:ARBA00035002}.
CC -!- FUNCTION: Structure-specific nuclease with 5'-flap endonuclease and 5'-
CC 3' exonuclease activities involved in DNA replication and repair.
CC During DNA replication, cleaves the 5'-overhanging flap structure that
CC is generated by displacement synthesis when DNA polymerase encounters
CC the 5'-end of a downstream Okazaki fragment. It enters the flap from
CC the 5'-end and then tracks to cleave the flap base, leaving a nick for
CC ligation. Also involved in the long patch base excision repair (LP-BER)
CC pathway, by cleaving within the apurinic/apyrimidinic (AP) site-
CC terminated flap. Acts as a genome stabilization factor that prevents
CC flaps from equilibrating into structures that lead to duplications and
CC deletions. Also possesses 5'-3' exonuclease activity on nicked or
CC gapped double-stranded DNA, and exhibits RNase H activity. Also
CC involved in replication and repair of rDNA and in repairing
CC mitochondrial DNA. {ECO:0000256|HAMAP-Rule:MF_03140}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03140};
CC Note=Binds 2 magnesium ions per subunit. They probably participate in
CC the reaction catalyzed by the enzyme. May bind an additional third
CC magnesium ion after substrate binding. {ECO:0000256|HAMAP-
CC Rule:MF_03140};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004163}; Single-pass type IV membrane protein
CC {ECO:0000256|ARBA:ARBA00004163}. Membrane
CC {ECO:0000256|ARBA:ARBA00004211}; Single-pass type IV membrane protein
CC {ECO:0000256|ARBA:ARBA00004211}. Nucleus, nucleolus {ECO:0000256|HAMAP-
CC Rule:MF_03140}. Nucleus, nucleoplasm {ECO:0000256|HAMAP-Rule:MF_03140}.
CC Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03140}. Note=Resides mostly in
CC the nucleoli and relocalizes to the nucleoplasm upon DNA damage.
CC {ECO:0000256|HAMAP-Rule:MF_03140}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03140}.
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DR AlphaFoldDB; A0A1I7VGW4; -.
DR STRING; 7209.A0A1I7VGW4; -.
DR WBParaSite; EN70_2422; EN70_2422; EN70_2422.
DR eggNOG; KOG0191; Eukaryota.
DR eggNOG; KOG0713; Eukaryota.
DR InParanoid; A0A1I7VGW4; -.
DR Proteomes; UP000095285; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0006914; P:autophagy; IEA:UniProtKB-KW.
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; cd06257; DnaJ; 1.
DR CDD; cd09907; H3TH_FEN1-Euk; 1.
DR CDD; cd09867; PIN_FEN1; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 6.
DR HAMAP; MF_00614; Fen; 1.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR023426; Flap_endonuc.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
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; PTHR44340; DNAJ HOMOLOG SUBFAMILY C MEMBER 10; 1.
DR PANTHER; PTHR44340:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 10; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF00085; Thioredoxin; 4.
DR Pfam; PF00867; XPG_I; 1.
DR Pfam; PF00752; XPG_N; 1.
DR PRINTS; PR00625; JDOMAIN.
DR PRINTS; PR00853; XPGRADSUPER.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00484; XPGI; 1.
DR SMART; SM00485; XPGN; 1.
DR SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 5.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 3.
DR PROSITE; PS00841; XPG_1; 1.
DR PROSITE; PS00842; XPG_2; 1.
PE 3: Inferred from homology;
KW Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_03140};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_03140};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_03140};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW Rule:MF_03140};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_03140}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03140};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03140};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03140}; Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03140};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_03140};
KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03140};
KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_03140};
KW Reference proteome {ECO:0000313|Proteomes:UP000095285};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 370..388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 392..457
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 472..591
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 803..912
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 913..1045
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 1147 AA; 132334 MW; 9A558A1B4BA6DCA7 CRC64;
MGVKDLSKVI GDHSPGSIRL KEFKGYFGRK VAVDASMCLY QFLIAVRQDG SQLQTESGET
TSHLLGMFYR TIRMIDNGIK PVYVFDGKPP QMKTSELEKR IERRAEAEKQ RSDAVELGDE
ASVNKFARRL VKVTKEQNEE AKRLVTLMGI PVLDAPCEAE AQCAALARAG KVFATVSEDM
DALTFGSPIL LRQMIASEAK KLPVKEMNLN QVLKDFGMNM EQFIDLCILL GCDYVSTIRG
IGPKKAFELI KKHECIENVL KIIDQTKYAI PKNWQYKEAR RLFLEPDVMD CENVELVWKE
PDVEGIVQFL CGEKSFNEDR VRGSLTRMQK GRQAAQQIRI DSFFLWLSFS FWLISVSLQR
FFVETEPRMV MHFIFILQFL LFLSISFVSC EDFYHLLGIS READNRAIRR AFKKLALVRH
PDKNPNDGNA HKEFMKLYRA YEVLMDEELR KKYDRYGEEG LSDNFKENHQ YQSWQFYKDN
FGIYDEDKEI VTLSRSDFER TVSEMGEIWF INFYSTFCSH CHQLAPTWRK FAQEMENVLR
VGAVNCAEDP MLCHSQGVMS YPSLMIYPHR HFFHGQRQLN QIVAFAMKYV TGVVLQLMDS
DIEQFKIKKS EKDTRGWLLD FCEHQSSDCL SELNRKKLAA NLRGLVNVAK VNCDESVKLC
TLFDRKSGVV YFRPTDGRKP NEAQEINSFD FKEIATTVLT YVPDIPYIDK LLEKIVEAQI
RDRSFLVRFG TGEADNNAEL KKLSAILTTG EIEVYFADCS KAKDICKNLE LTSLPKWILF
KKQGSYEIYH GKMEIVHDIA LFAIESHSSP LVTLTPETYT SAVNSGDEWL IDYYAPWCPP
CLRLLKELRR LHNYVESIKI GTIDCDQYGD ICRKANTNAY PNIVWHSGGR SSARAGYVDV
NTIVEFIEDA RDPIVVDLSP SNFDPLVLNG RKGTVWLVDF YAPWCGPCNQ LAPEYKKLAR
NMHMKKFVHF GMVDCDYHRQ LCINLGVQSY PTIRFYSSGS YTVDYPTNWW RDHRSMEVWL
RNYLPSRVIS IENDFFAKVL DDNEPWLVDF FVTWCSHCIE FAPVFERIAE VLEGRVKLAK
VDCGLWPNVC RNVGVTAYPT VRFYGGSRGS HIQIATGVRI ESQHADTIVR QVEKELIKID
RLFKIEL
//
