ID   RNL1_NPVAC              Reviewed;         694 AA.
AC   P41476;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Putative bifunctional polynucleotide kinase/RNA ligase;
DE   Includes:
DE     RecName: Full=Polynucleotide kinase;
DE              Short=PNK;
DE              EC=2.7.1.78;
DE     AltName: Full=Polynucleotide 5'-hydroxy-kinase;
DE   Includes:
DE     RecName: Full=RNA ligase;
DE              EC=6.5.1.3 {ECO:0000305};
GN   Name=PNK/PNL; ORFNames=ORF86;
OS   Autographa californica nuclear polyhedrosis virus (AcMNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=46015;
OH   NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6;
RX   PubMed=8030224; DOI=10.1006/viro.1994.1380;
RA   Ayres M.D., Howard S.C., Kuzio J., Lopez-Ferber M., Possee R.D.;
RT   "The complete DNA sequence of Autographa californica nuclear polyhedrosis
RT   virus.";
RL   Virology 202:586-605(1994).
RN   [2]
RP   FUNCTION, AND DOMAIN.
RX   PubMed=14747466; DOI=10.1074/jbc.m313386200;
RA   Martins A., Shuman S.;
RT   "Characterization of a baculovirus enzyme with RNA ligase, polynucleotide
RT   5'-kinase, and polynucleotide 3'-phosphatase activities.";
RL   J. Biol. Chem. 279:18220-18231(2004).
CC   -!- FUNCTION: Trifunctional enzyme that possesses a bifunctional
CC       polynucleotide kinase/phosphatase activity and an ATP-dependent RNA
CC       ligase activity. May therefore play a role to evade an RNA damage-based
CC       host response. {ECO:0000269|PubMed:14747466}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end dephospho-2'-deoxyribonucleoside-DNA + ATP = a 5'-end
CC         5'-monophospho-2'-deoxyribonucleoside-DNA + ADP + H(+);
CC         Xref=Rhea:RHEA:15669, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:13184,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:136412,
CC         ChEBI:CHEBI:136416, ChEBI:CHEBI:456216; EC=2.7.1.78;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (ribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (ribonucleotide)m = (ribonucleotide)n+m + AMP + diphosphate.;
CC         EC=6.5.1.3; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L22858; AAA66716.1; -; Genomic_DNA.
DR   PIR; G72860; G72860.
DR   RefSeq; NP_054116.1; NC_001623.1.
DR   SMR; P41476; -.
DR   PRIDE; P41476; -.
DR   GeneID; 1403919; -.
DR   KEGG; vg:1403919; -.
DR   Proteomes; UP000008292; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046404; F:polydeoxyribonucleotide 5'-hydroxyl-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003972; F:RNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0042245; P:RNA repair; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR019039; RNA_ligase_T4-Rnl1_N.
DR   Pfam; PF09511; RNA_lig_T4_1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
PE   4: Predicted;
KW   ATP-binding; Kinase; Ligase; Multifunctional enzyme; Nucleotide-binding;
KW   Reference proteome; RNA repair; Transferase.
FT   CHAIN           1..694
FT                   /note="Putative bifunctional polynucleotide kinase/RNA
FT                   ligase"
FT                   /id="PRO_0000132846"
FT   REGION          1..385
FT                   /note="Ligase domain"
FT                   /evidence="ECO:0000269|PubMed:14747466"
FT   REGION          394..694
FT                   /note="Bifunctional 5'-OH polynucleotide
FT                   kinase/polynucleotide 3'-phosphatase"
FT                   /evidence="ECO:0000269|PubMed:14747466"
FT   BINDING         401..408
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   694 AA;  80760 MW;  3B81C296C54FCAEA CRC64;
     MLHVSRLLAN GGVKNLCDKF KVKIKNYTEH DLMVLNYESF ERDRDHPVVV ECRGLILNSR
     TYAVVSRSFD RFFNFQELLQ NIGGEDAHHK LFQSKENFKF YEKIDGSLIK IYKYNGEWHA
     STRGSAFAEN LCVSDVTFKR LVLQALQLDE AHNQFQALCN EYLDCASTHM FELTSKHNRI
     VTVYDEQPTL WYLASRNNET GDYFYCSNLP FCKYPKCYEF TSVQECVEHA AQLKNLEEGF
     VVYDKNNAPL CKIKSDVYLN MHKNQSRAEN PTKLAQLVIN GEHDDFLALF PHLKSVIKPY
     VDARNTFTNE STINIMVSGL TLNQQRFNEL VQTLPWKCLA YRCRKAQTID VESEFLKLTE
     PEKIKMIKNI IKFVSTKQAL NNKLAPTIKL PSSKQLLVLI GISGSGKSTY AKSLKGYTEI
     NRDDVRVKLF LNGDYTKLNA FYNQSRKCRQ TKEEQITKMC IEQFLKAAKC GANVVVSDTN
     LNTQSVDMWQ KMAATHNYHF LTRLMDVSLE TALERNYKRS DKFPLNPETI KKQYKKFLKV
     NNFEYYVPVG DKFPRAVLCD LDGTVALPTN RSFYDFDNRV AQDEARLDVI TCVKYLANCH
     DAIIVFMSGR SVICEQPTRN WIEKYFDIKS YKLFMRPSDD TCKDYLLKLK LFNNYIRGKY
     NVIAVFDDRP CVVRMWQDLK IPTVFNVCRD YLEF