Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna22956.1-v1.0-hybrid |
Family | GH5 |
Protein Properties | Length: 733 Molecular Weight: 81957 Isoelectric Point: 6.7192 |
Chromosome | Chromosome/Scaffold: 6 Start: 3804070 End: 3811281 |
Description | 5'-3' exonuclease family protein |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH5 | 391 | 695 | 4.4e-25 |
NGKPFYMNGFNAYWMMYMASDPSTQLMVTSAFQQASKYKMNVARTWGFSDGGDRPLQISPGSYNENMFKLSEQLRSFWGRKQYVQWAREQGQSLSSDDDF YSNVVVKGFYKNHVKAILTRMNTITNVAYKDDPTIFAWELINEPRCQSDVSGALLQQWVNEMAAYLKSIDGNHLLEVGLEGFYGATTPEKKQYNPGNQDW GSDFIATNLLPQIDFATIHIYAEQWLSGQSEEAQAAFVDKWVQVHIDDCNTIVKKPLIMGEFGKSSKYPGYSIENRNSYFGKLYDDVYNSAKSGGSCVGG LFWQL |
Full Sequence |
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Protein Sequence Length: 733 Download |
MGIKGLTKLL ADNAPKCMKE QKFESYFGRK IAIDASMSIY QFLIVVGRTG TEMLTNEAGE 60 VTSHLQGMFS RTIRLLEAGI KPVYVFDGKP PELKSQELAK RYSKRVDATQ DLATAVESGN 120 KEDIEKFSKR TVKVTKQHNE DCRKLLRLMG VPVIEAPSEA EAQCAVLCKA GKAKDMDSLT 180 FGAPKFLRHL MDPSSRKIPV MEFDVAKVLE ELNLTMDQFI DLCILSGCDY CDSIRGIGGQ 240 TALKLIRQHG SIESILENIN KERYQIPDNW PYEEARRLFK EPVALTDDEQ LEIKWTAPDE 300 EGLISFLVNE NGFNNDRVIK AIEKIKAAKN KGSQGRLESF FKPTATTSVP LKRKETPSTA 360 KETSNKKTKG GGAAQAGSSF GGTTGTRFVM NGKPFYMNGF NAYWMMYMAS DPSTQLMVTS 420 AFQQASKYKM NVARTWGFSD GGDRPLQISP GSYNENMFKL SEQLRSFWGR KQYVQWAREQ 480 GQSLSSDDDF YSNVVVKGFY KNHVKAILTR MNTITNVAYK DDPTIFAWEL INEPRCQSDV 540 SGALLQQWVN EMAAYLKSID GNHLLEVGLE GFYGATTPEK KQYNPGNQDW GSDFIATNLL 600 PQIDFATIHI YAEQWLSGQS EEAQAAFVDK WVQVHIDDCN TIVKKPLIMG EFGKSSKYPG 660 YSIENRNSYF GKLYDDVYNS AKSGGSCVGG LFWQLLAQGM ATYGDGYEVV LEESQSTGDV 720 IAQQSQRLQL LN* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd09867 | PIN_FEN1 | 3.0e-14 | 289 | 341 | 53 | + PIN domain of Flap Endonuclease-1, a structure-specific, divalent-metal-ion dependent, 5' nuclease and homologs. Flap endonuclease-1 (FEN1) is involved in multiple DNA metabolic pathways, including DNA replication processes (5' flap DNA endonuclease activity and double stranded DNA 5'-exonuclease activity) and DNA repair processes (long-patch base excision repair) in eukaryotes and archaea. Interaction between FEN1 and PCNA (Proliferating cell nuclear antigen) is an essential prerequisite to FEN1's DNA replication functionality and stimulates FEN1 nuclease activity by 10-50 fold. FEN1 belongs to the FEN1-EXO1-like family of structure-specific, 5' nucleases. These nucleases contain a PIN (PilT N terminus) domain with a helical arch/clamp region (I domain) of variable length (approximately 45 residues in FEN1 PIN domains) and a H3TH (helix-3-turn-helix) domain, an atypical helix-hairpin-helix-2-like region. Both the H3TH domain (not included here) and the helical arch/clamp region are involved in DNA binding. Nucleases within this group also have a carboxylate-rich active site that is involved in binding essential divalent metal ion cofactors (Mg2+/Mn2+). FEN1 has a C-terminal extension containing residues forming the consensus PIP-box - Qxx(M/L/I)xxF(Y/F) which serves to anchor FEN1 to PCNA. | ||
PRK03980 | PRK03980 | 1.0e-98 | 55 | 341 | 303 | + flap endonuclease-1; Provisional | ||
TIGR03674 | fen_arch | 7.0e-104 | 1 | 341 | 357 | + flap structure-specific endonuclease. Endonuclease that cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Has 5'-endo-/exonuclease and 5'-pseudo-Y-endonuclease activities. Cleaves the junction between single and double-stranded regions of flap DNA | ||
cd09867 | PIN_FEN1 | 1.0e-119 | 4 | 217 | 219 | + PIN domain of Flap Endonuclease-1, a structure-specific, divalent-metal-ion dependent, 5' nuclease and homologs. Flap endonuclease-1 (FEN1) is involved in multiple DNA metabolic pathways, including DNA replication processes (5' flap DNA endonuclease activity and double stranded DNA 5'-exonuclease activity) and DNA repair processes (long-patch base excision repair) in eukaryotes and archaea. Interaction between FEN1 and PCNA (Proliferating cell nuclear antigen) is an essential prerequisite to FEN1's DNA replication functionality and stimulates FEN1 nuclease activity by 10-50 fold. FEN1 belongs to the FEN1-EXO1-like family of structure-specific, 5' nucleases. These nucleases contain a PIN (PilT N terminus) domain with a helical arch/clamp region (I domain) of variable length (approximately 45 residues in FEN1 PIN domains) and a H3TH (helix-3-turn-helix) domain, an atypical helix-hairpin-helix-2-like region. Both the H3TH domain (not included here) and the helical arch/clamp region are involved in DNA binding. Nucleases within this group also have a carboxylate-rich active site that is involved in binding essential divalent metal ion cofactors (Mg2+/Mn2+). FEN1 has a C-terminal extension containing residues forming the consensus PIP-box - Qxx(M/L/I)xxF(Y/F) which serves to anchor FEN1 to PCNA. | ||
PTZ00217 | PTZ00217 | 0 | 1 | 365 | 372 | + flap endonuclease-1; Provisional |
Gene Ontology | |
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GO Term | Description |
GO:0004518 | nuclease activity |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
GO:0006281 | DNA repair |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1rh9_A | 0 | 376 | 731 | 2 | 372 | A Chain A, Family Gh5 Endo-Beta-Mannanase From Lycopersicon Esculentum (Tomato) |
PDB | 1ul1_Z | 0 | 2 | 375 | 1 | 374 | X Chain X, Crystal Structure Of The Human Fen1-Pcna Complex |
PDB | 1ul1_Y | 0 | 2 | 375 | 1 | 374 | X Chain X, Crystal Structure Of The Human Fen1-Pcna Complex |
PDB | 1ul1_X | 0 | 2 | 375 | 1 | 374 | X Chain X, Crystal Structure Of The Human Fen1-Pcna Complex |
PDB | 3q8l_A | 0 | 2 | 342 | 1 | 341 | X Chain X, Crystal Structure Of The Human Fen1-Pcna Complex |
Sequence Alignments (This image is cropped. Click for full image.) |
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