Structure of PDB 8hf0 Chain A

Receptor sequence
>8hf0A (length=1561) Species: 7227 (Drosophila melanogaster) [Search protein sequence]
EDVEIKPRGYQLRLVDHLTKSNGIVYLPTGSGKTFVAILVLKRFSQDFDK
PIESGGKRALFMCNTVELARQQAMAVRRCTNFKVGFYVGEQGVDDWTRGM
WSDEIKKNQVLVGTAQVFLDMVTQTYVALSSLSVVIIDECHHGTGHHPFR
EFMRLFTIANQTKLPRVVGLTGVLIKGNEITNVATKLKELEITYRGNIIT
VSDTKEMENVMLYATKPTEVMVSFPHQEQVLTVTRLISAEIEKFYVSLDL
MNIGVQPIRRSKSLQCLRDPSKKSFVKQLFNDFLYQMKEYGIYAASIAII
SLIVEFDIKRRQAETLSVKLMHRTALTLCEKIRHLLVQKLQDMTYDDDDD
NVNTEEVIMNFSTPKVQRFLMSLKVSFADKDPKDICCLVFVERRYTCKCI
YGLLLNYIQSTPELRNVLTPQFMVGRNNISPDFESVLERKWQKSAIQQFR
DGNANLMICSSVLEEGIDVQACNHVFILDPVKTFNMYVQSKGRARTTEAK
FVLFTADKEREKTIQQIYQYRKAHNDIAEYLKDRVLEKTEPELYEIKGHF
QDDIDPFTNENGAVLLPNNALAILHRYCQTIPTDAFGFVIPWFHVLQEDE
RDRIFGVSAKGKHVISINMPVNCMLRDTIYSDPMDNVKTAKISAAFKACK
VLYSLGELNERFVPKTLKERVASIADVHFEHWNKYGDSVTATVNKADKSK
DRTYKTECPLEFYDALPRVGEICYAYEIFLEPQFESCEYTEHMYLNLQTP
RNYAILLRNKLPRLAEMPLFSNQGKLHVRVANAPLEVIIQNSEQLELLHQ
FHGMVFRDILKIWHPFFVLDRRSKENSYLVVPLILGAGEQKCFDWELMTN
FRRLPQSHGSNVQQREQQPAPRPEDFEGKIVTQWYANYDKPMLVTKVHRE
LTPLSYMEKNQQDKTYYEFTMSKYGNRIGDVVHKDKFMIEVRDLTEQLTF
YVHNRGKFNAKSKAKMKVILIPELCFNFNFPGDLWLKLIFLPSILNRMYF
LLHAEALRKRFNTYLNLHLLPFNGTDYMPRPLEIDYSLKRNGKVKPLLIL
QKTVSKEHITPAEQGEFLAAITASSAADVFDMERLEILGNSFLKLSATLY
LASKYSDWNEGTLTEVKSKLVSNRNLLFCLIDADIPKTLNTIQFTPRYTW
LPPGISLPHNVLALWRENPEFAKIIGPHNLRDLALGDEESLVKGNCSDIN
YNRFVEGCRANGQSFYAGADFSSEVNFCVGLVTIPNKVIADTLEALLGVI
VKNYGLQHAFKMLEYFKICRADIDKPLTQLLNLELGGKKMRANVNTTEID
GFLINHYYLEKNLGYTFKDRRYLLQALTHPSYPTNRITGSYQELEFIGNA
ILDFLISAYIFENNTKMNPGALTDLRSALVNNTTLACICVRHRLHFFILA
ENAKLSEIISKFVNFQESQGHRVTNYVRILLEVPPKGEFNMSTNVDVPKA
LGDVLEALIAAVYLDCRDLQRTWEVIFNLFEPELQEFTRKVPINHIRQLV
EHKHAKPVFSSPIVEGETVMVSCQFTCMEKTIKVYGFGSNKDQAKLSAAK
HALQQLSKCDA
3D structure
PDB8hf0 Structural mechanism of R2D2 and Loqs-PD synergistic modulation on DmDcr-2 oligomers.
ChainA
Resolution3.72 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.1.26.3: ribonuclease III.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003676 nucleic acid binding
GO:0003723 RNA binding
GO:0003730 mRNA 3'-UTR binding
GO:0004386 helicase activity
GO:0004518 nuclease activity
GO:0004521 RNA endonuclease activity
GO:0004525 ribonuclease III activity
GO:0004530 deoxyribonuclease I activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008186 ATP-dependent activity, acting on RNA
GO:0016887 ATP hydrolysis activity
GO:0016891 RNA endonuclease activity, producing 5'-phosphomonoesters
GO:0035197 siRNA binding
Biological Process
GO:0002230 positive regulation of defense response to virus by host
GO:0006309 apoptotic DNA fragmentation
GO:0006396 RNA processing
GO:0007626 locomotory behavior
GO:0009047 dosage compensation by hyperactivation of X chromosome
GO:0009597 detection of virus
GO:0009616 RNAi-mediated antiviral immune response
GO:0030422 siRNA processing
GO:0031047 regulatory ncRNA-mediated gene silencing
GO:0031054 pre-miRNA processing
GO:0031507 heterochromatin formation
GO:0033227 dsRNA transport
GO:0035194 regulatory ncRNA-mediated post-transcriptional gene silencing
GO:0045089 positive regulation of innate immune response
GO:0045752 positive regulation of Toll signaling pathway
GO:0051607 defense response to virus
GO:0070922 RISC complex assembly
GO:0098586 cellular response to virus
GO:0098795 global gene silencing by mRNA cleavage
GO:0110064 lncRNA catabolic process
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0016442 RISC complex
GO:0036464 cytoplasmic ribonucleoprotein granule
GO:0048471 perinuclear region of cytoplasm
GO:0070578 RISC-loading complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:8hf0, PDBe:8hf0, PDBj:8hf0
PDBsum8hf0
PubMed37633971
UniProtA1ZAW0|DCR2_DROME Endoribonuclease Dcr-2 (Gene Name=Dcr-2)

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