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Database: UniProt
Entry: VF205_IIV6
LinkDB: VF205_IIV6
Original site: VF205_IIV6 
ID   VF205_IIV6              Reviewed;         615 AA.
AC   Q91FW5;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 90.
DE   RecName: Full=Putative DNA ligase 205R;
DE            EC=6.5.1.2;
GN   ORFNames=IIV6-205R;
OS   Invertebrate iridescent virus 6 (IIV-6) (Chilo iridescent virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Iridoviridae; Betairidovirinae; Iridovirus.
OX   NCBI_TaxID=176652;
OH   NCBI_TaxID=6997; Acheta domesticus (House cricket).
OH   NCBI_TaxID=168631; Chilo suppressalis (Asiatic rice borer moth).
OH   NCBI_TaxID=6999; Gryllus bimaculatus (Two-spotted cricket).
OH   NCBI_TaxID=58607; Gryllus campestris.
OH   NCBI_TaxID=7108; Spodoptera frugiperda (Fall armyworm).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11448171; DOI=10.1006/viro.2001.0963;
RA   Jakob N.J., Mueller K., Bahr U., Darai G.;
RT   "Analysis of the first complete DNA sequence of an invertebrate iridovirus:
RT   coding strategy of the genome of Chilo iridescent virus.";
RL   Virology 286:182-196(2001).
RN   [2]
RP   GENOME REANNOTATION.
RX   PubMed=17239238; DOI=10.1186/1743-422x-4-11;
RA   Eaton H.E., Metcalf J., Penny E., Tcherepanov V., Upton C., Brunetti C.R.;
RT   "Comparative genomic analysis of the family Iridoviridae: re-annotating and
RT   defining the core set of iridovirus genes.";
RL   Virol. J. 4:11-11(2007).
CC   -!- FUNCTION: Catalyzes the formation of phosphodiester linkages between
CC       5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD
CC       as a coenzyme and as the energy source for the reaction. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-
CC         nicotinamide D-nucleotide.; EC=6.5.1.2;
CC   -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family.
CC       {ECO:0000305}.
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DR   EMBL; AF303741; AAK82067.1; -; Genomic_DNA.
DR   RefSeq; NP_149668.1; NC_003038.1.
DR   SMR; Q91FW5; -.
DR   GeneID; 1733308; -.
DR   KEGG; vg:1733308; -.
DR   OrthoDB; 2744at10239; -.
DR   Proteomes; UP000001359; Genome.
DR   GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR001679; DNA_ligase.
DR   InterPro; IPR013839; DNAligase_adenylation.
DR   InterPro; IPR013840; DNAligase_N.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004150; NAD_DNA_ligase_OB.
DR   InterPro; IPR010994; RuvA_2-like.
DR   Pfam; PF01653; DNA_ligase_aden; 1.
DR   Pfam; PF03120; DNA_ligase_OB; 1.
DR   Pfam; PF14520; HHH_5; 1.
DR   PIRSF; PIRSF001604; LigA; 1.
DR   SMART; SM00532; LIGANc; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF47781; RuvA domain 2-like; 1.
PE   3: Inferred from homology;
KW   DNA replication; Ligase; NAD; Reference proteome.
FT   CHAIN           1..615
FT                   /note="Putative DNA ligase 205R"
FT                   /id="PRO_0000376962"
FT   ACT_SITE        101
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   615 AA;  70152 MW;  A3B98D1C37B317A8 CRC64;
     MDETQQLLYK FKNLTISENE KLKLKEKADH FYFNTEKEIL TDNEYDILAE QLQSTNVGCS
     PLISKTDLPL WMGSLDKVYN DKELNLWIKK VASDKYIIQC KLDGVSCLII NKDNKLKAYT
     RGNGKVGTDI SHLIKYFIKD KCLPNNIALR CEIIIKKETF NQKYKHAFSN PRSFVSGVVN
     RKQENIVISE LNDLCLIAYE LINFPVNEYQ KNILTQIEII EQLNFIQFVN FKTISNEFLT
     QKALSNLFKE MKNNSLFEMD GLVILANTPY IRVTEGNPKH SIAFKVRGDN VKEAKVTFIE
     WNVGKTGVFT PKVHIVPTEI NGTTVSCFTG FNANYLIEKG IGEGAIILVT RAGDAIPQII
     GVKQTGVLTF PKDYEWKGDC RIVEKIESKE RIIKQILHFV ESVDIPYIKE ATINKLYNNG
     CTSIELFLKL TQKDLLLFGP KLSSTIYNSI QKSFEAPIEK FLSGYNAFGD YIGEKKILLL
     LQKYPNLFEL ENLDAIDLVS IEGIGSKTAT QIKQHFINAK LIYNNIIQNK LFKGVLHTPS
     KQNTVELFKV CVSGTRDPLF IQELKNRGFV LSDNITKKVK VLIVKNSNEE TTKVKKANSV
     GITILTLEDF KQKYF
//
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