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Flap endonuclease 1-A (FEN-1-A) (EC 3.1.-.-) (Flap structure-specific endonuclease 1-A) (xFEN-1a)

 FEN1A_XENLA             Reviewed;         382 AA.
P70040; B7ZQC8; O57351; Q08AW7;
27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
16-JAN-2019, entry version 91.
RecName: Full=Flap endonuclease 1-A {ECO:0000255|HAMAP-Rule:MF_03140};
Short=FEN-1-A {ECO:0000255|HAMAP-Rule:MF_03140};
EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140};
AltName: Full=Flap structure-specific endonuclease 1-A {ECO:0000255|HAMAP-Rule:MF_03140};
Short=xFEN-1a;
Name=fen1-a;
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355;
[1] {ECO:0000305, ECO:0000312|EMBL:AAB88707.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION IN A COMPLEX WITH
PCNA, AND VARIANT ILE-33.
TISSUE=Oocyte {ECO:0000269|PubMed:9535864};
PubMed=9535864; DOI=10.1074/jbc.273.15.8842;
Kim K., Biade S., Matsumoto Y.;
"Involvement of flap endonuclease 1 in base excision DNA repair.";
J. Biol. Chem. 273:8842-8848(1998).
[2] {ECO:0000305, ECO:0000312|EMBL:AAB06176.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, IDENTIFICATION IN A
COMPLEX WITH PCNA, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
VARIANT ILE-33.
TISSUE=Tadpole head {ECO:0000269|PubMed:9852084};
PubMed=9852084; DOI=10.1074/jbc.273.51.34222;
Bibikova M., Wu B., Chi E., Kim K.-H., Trautman J.K., Carroll D.;
"Characterization of FEN-1 from Xenopus laevis. cDNA cloning and role
in DNA metabolism.";
J. Biol. Chem. 273:34222-34229(1998).
[3] {ECO:0000312|EMBL:AAD02814.1}
NUCLEOTIDE SEQUENCE [MRNA].
Li J.-L., Cox L.S.;
"Cloning and investigation of Xenopus Fen1: developmental expression
and function in DNA replication.";
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000312|EMBL:AAD02814.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-33.
TISSUE=Oocyte, and Ovary;
NIH - Xenopus Gene Collection (XGC) project;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: 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.
{ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:9535864,
ECO:0000269|PubMed:9852084}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_03140};
Note=Binds 2 magnesium ions per subunit. They probably participate
in the reaction catalyzed by the enzyme. May bind an additional
third magnesium ion after substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03140};
-!- SUBUNIT: 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. {ECO:0000255|HAMAP-Rule:MF_03140}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
Rule:MF_03140}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-
Rule:MF_03140}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03140}.
Note=Resides mostly in the nucleoli and relocalizes to the
nucleoplasm upon DNA damage. {ECO:0000255|HAMAP-Rule:MF_03140}.
-!- DEVELOPMENTAL STAGE: First expressed at a low level in stage II
oocytes. Expression increases dramatically from oocyte stages III
to V (at protein level). Also expressed in embryos.
{ECO:0000269|PubMed:9852084}.
-!- PTM: Phosphorylated. Phosphorylation upon DNA damage induces
relocalization to the nuclear plasma. {ECO:0000255|HAMAP-
Rule:MF_03140}.
-!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1
subfamily. {ECO:0000250|UniProtKB:P39748, ECO:0000255|HAMAP-
Rule:MF_03140}.
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EMBL; AF036327; AAB88707.1; -; mRNA.
EMBL; U64563; AAB06176.1; -; mRNA.
EMBL; AF065397; AAD02814.1; -; mRNA.
EMBL; BC169761; AAI69761.1; -; mRNA.
EMBL; BC169765; AAI69765.1; -; mRNA.
EMBL; BC124977; AAI24978.1; -; mRNA.
RefSeq; NP_001080960.1; NM_001087491.1.
UniGene; Xl.440; -.
ProteinModelPortal; P70040; -.
BioGrid; 98905; 1.
IntAct; P70040; 2.
PRIDE; P70040; -.
GeneID; 394303; -.
KEGG; xla:394303; -.
CTD; 394303; -.
Xenbase; XB-GENE-955523; fen1.
HOVERGEN; HBG000844; -.
KO; K04799; -.
OrthoDB; 1094524at2759; -.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0008409; F:5'-3' exonuclease activity; IEA:UniProtKB-UniRule.
GO; GO:0017108; F:5'-flap endonuclease activity; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0006284; P:base-excision repair; IDA:UniProtKB.
GO; GO:0006260; P:DNA replication; IPI:UniProtKB.
GO; GO:0043137; P:DNA replication, removal of RNA primer; IEA:UniProtKB-UniRule.
CDD; cd09867; PIN_FEN1; 1.
HAMAP; MF_00614; Fen; 1.
InterPro; IPR036279; 5-3_exonuclease_C_sf.
InterPro; IPR023426; Flap_endonuc.
InterPro; IPR008918; HhH2.
InterPro; IPR029060; PIN-like_dom_sf.
InterPro; IPR006086; XPG-I_dom.
InterPro; IPR006084; XPG/Rad2.
InterPro; IPR019974; XPG_CS.
InterPro; IPR006085; XPG_DNA_repair_N.
PANTHER; PTHR11081; PTHR11081; 1.
Pfam; PF00867; XPG_I; 1.
Pfam; PF00752; XPG_N; 1.
PRINTS; PR00853; XPGRADSUPER.
SMART; SM00279; HhH2; 1.
SMART; SM00484; XPGI; 1.
SMART; SM00485; XPGN; 1.
SUPFAM; SSF47807; SSF47807; 1.
SUPFAM; SSF88723; SSF88723; 1.
PROSITE; PS00841; XPG_1; 1.
1: Evidence at protein level;
DNA damage; DNA repair; DNA replication; Endonuclease; Exonuclease;
Hydrolase; Magnesium; Metal-binding; Mitochondrion; Nuclease; Nucleus;
Phosphoprotein; Polymorphism.
CHAIN 1 382 Flap endonuclease 1-A.
/FTId=PRO_0000244491.
REGION 1 104 N-domain. {ECO:0000255}.
REGION 122 253 I-domain. {ECO:0000255}.
REGION 336 344 Interaction with PCNA.
{ECO:0000255|HAMAP-Rule:MF_03140}.
METAL 34 34 Magnesium 1. {ECO:0000255|HAMAP-
Rule:MF_03140}.
METAL 86 86 Magnesium 1. {ECO:0000255|HAMAP-
Rule:MF_03140}.
METAL 158 158 Magnesium 1. {ECO:0000255|HAMAP-
Rule:MF_03140}.
METAL 160 160 Magnesium 1. {ECO:0000255|HAMAP-
Rule:MF_03140}.
METAL 179 179 Magnesium 2. {ECO:0000255|HAMAP-
Rule:MF_03140}.
METAL 181 181 Magnesium 2. {ECO:0000255|HAMAP-
Rule:MF_03140}.
METAL 233 233 Magnesium 2. {ECO:0000255|HAMAP-
Rule:MF_03140}.
BINDING 47 47 DNA substrate.
{ECO:0000250|UniProtKB:P39748,
ECO:0000255|HAMAP-Rule:MF_03140}.
BINDING 70 70 DNA substrate.
{ECO:0000250|UniProtKB:P39748,
ECO:0000255|HAMAP-Rule:MF_03140}.
BINDING 158 158 DNA substrate.
{ECO:0000250|UniProtKB:P39748,
ECO:0000255|HAMAP-Rule:MF_03140}.
BINDING 231 231 DNA substrate.
{ECO:0000250|UniProtKB:P39748,
ECO:0000255|HAMAP-Rule:MF_03140}.
BINDING 233 233 DNA substrate.
{ECO:0000250|UniProtKB:P39748,
ECO:0000255|HAMAP-Rule:MF_03140}.
VARIANT 33 33 V -> I (in allele fen-1a').
{ECO:0000269|PubMed:9535864,
ECO:0000269|PubMed:9852084,
ECO:0000269|Ref.4}.
SEQUENCE 382 AA; 42668 MW; 9B1DB0EDAD158D57 CRC64;
MGIHGLAKLI ADVAPAAIKE HDIKSYFGRK VAVDASMCIY QFLIAVRQDG NTLQNEEGET
TSHLMGMFYR TIRMVEHGIK PVYVFDGKPP QMKSGELAKR SERRAEAEKL LEAAEEAGEV
ENIEKFTKRL VKVTKQHNEE CKKLLTLMGI PYVDAPCEAE ATCAALVKAG KVYAAATEDM
DALTFGTPVL LRHLTASEAK KLPIQEFHLN RVIQDIGITH EQFVDLCILL GSDYCETIRG
IGPKRAIDLI RQHKTIDEII DNIDLKKYPV PENWLHKEAK HLFLEPEVVD TDITELKWIE
PDEEGLVAFM CGEKQFSEDR IRNGAKKLAK NRQGSTQGRL DDFFKVTGSV SSTKRKEAES
KGSAKKKAKT GGTPAGKFKR GK


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Related Genes :
[FEN1A Os05g0540100 LOC_Os05g46270 OsJ_19381 OSJNBa0052K01.23] Flap endonuclease 1-A (FEN-1-A) (EC 3.1.-.-) (Flap structure-specific endonuclease 1-A) (OsFEN-1) (OsFEN-1a)
[fen1-a] Flap endonuclease 1-A (FEN-1-A) (EC 3.1.-.-) (Flap structure-specific endonuclease 1-A) (xFEN-1a)
[dnr-8 fen1 NCU10776] Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (DNA repair protein 8) (Flap structure-specific endonuclease 1)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[FEN1 RAD2] Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (DNase IV) (Flap structure-specific endonuclease 1) (Maturation factor 1) (MF1) (hFEN-1)
[VMA1 CLS8 TFP1 YDL185W D1286] V-type proton ATPase catalytic subunit A (V-ATPase subunit A) (EC 7.1.2.2) (Vacuolar proton pump subunit A) [Cleaved into: Endonuclease PI-SceI (EC 3.1.-.-) (Sce VMA intein) (VMA1-derived endonuclease) (VDE)]
[crn-1 Y47G6A.8] Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (Cell death-related nuclease 1) (Flap structure-specific endonuclease 1)
[RAD27 FEN1 RTH1 YKL113C YKL510] Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (Flap structure-specific endonuclease 1) (RAD2 homolog nuclease 1) (RTH1 nuclease) (Structure-specific endonuclease RAD27)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1 (EC 3.4.22.-); Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.19.12) (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); Serine protease nsp4 (3CLSP) (EC 3.4.21.-) (3C-like serine proteinase) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase nsp10 (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[dim-5 29E8.110 NCU04402] Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5 (EC 2.1.1.43) (Histone H3-K9 methyltransferase dim-5) (H3-K9-HMTase dim-5) (HKMT)
[Fen1 Fen-1] Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (Flap structure-specific endonuclease 1)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO) (SARS coronavirus main proteinase); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[RAD27 FEN1 SCRG_03908] Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (Flap structure-specific endonuclease 1)
[rad2 fen1 SPAC3G6.06c] Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (DNA repair protein rad2) (Flap structure-specific endonuclease 1)
[FEN1 MVLG_02451] Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (Flap structure-specific endonuclease 1)
[al-3 B8P8.010 NCU01427] Geranylgeranyl pyrophosphate synthase (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Albino-3 protein) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10)
[aro-1 aro-2 aro-4 aro-5 aro-9 B14H13.20 NCU016321] Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
[al-2 B22I21.230 NCU00585] Bifunctional lycopene cyclase/phytoene synthase (Protein albino-2) [Includes: Lycopene beta-cyclase (EC 5.5.1.19) (Carotene cyclase) (Lycopene cyclase); Phytoene synthase (EC 2.5.1.32)]
[Fen1] Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (Flap structure-specific endonuclease 1)
[FEN1-A PHYPADRAFT_207454] Flap endonuclease 1-A (FEN-1-A) (EC 3.1.-.-) (Flap structure-specific endonuclease 1-A)
[FEN1 RTH-1] Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (Flap structure-specific endonuclease 1)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[FEN1] Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (Flap structure-specific endonuclease 1)
[FEN1-A Sb09g026950] Flap endonuclease 1-A (FEN-1-A) (EC 3.1.-.-) (Flap structure-specific endonuclease 1-A)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]

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