Transcript | Ll_transcript_145161 |
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CDS coordinates | 181-1767 (+) |
Peptide sequence | MGIHGLLPQLKSIMVPIHIKDLNGSSVAIDTYSWLHKGALSCSTNLCKGIPTTRHIEYCMHRVNLLRHFGVKPVLVFDGGLLPMKGDQENKRARARKENFERAVQHESDGNSTAAFECYQKAVDISPVIALDLIQVLKRENVQYIVAPYEADAQMTFLAITKQVDAVITEDSDLIPFGCPRIIFKMDKFGQGVQFQYSMLEKNKELSFEGFNRQMLLEMCILSGCDYLQSLPGMGLKRAHAIIKKFKSYDKVLKHLRYSGVSVPPFYEESFKKAILTFQYQRVYDPINEDIVHLSTIPDDSGDELDFVGPPMPKNIAQGIAKGDLDPFTKMPFEKFQGQNLTAKLANAGTFQFKTPESVKKKIDLPVQKNLLTNYFCFASLEAKRNFRAPRISPTTANESTFDFSSGGPLEHETSEATASGTKNSATSVVSFEKWGSSPLTSNHIENSLSSTVSEFTESPSRVYMVDEKKISTEHTILRQPRQPIHKPCLGSHKEDERTNAEYTVEVKTREETKVIVRSAYFQHKQVEN |
ORF Type | 3prime_partial |
Blastp | Exonuclease 1 from Arabidopsis with 62.19% of identity |
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Blastx | Exonuclease 1 from Arabidopsis with 62.19% of identity |
Eggnog | 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 (By similarity)(COG0258) |
Kegg | Link to kegg annotations (AT1G29630) |
CantataDB | - |
Mirbase | - |
Ncbi protein | Link to NCBI protein (XP_019444639.1) |
Pfam | XPG N-terminal domain (PF00752.16) |
Rfam | - |
GO | Links to GO: General; Genes and gene products; Annotations; Ontology; Links to GO: General; Genes and gene products; Annotations; Ontology; |
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Alignmet by MSA Viewer