ID U5KBN2_9BBAC Unreviewed; 553 AA.
AC U5KBN2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=DNA ligase {ECO:0000256|ARBA:ARBA00013308};
GN ORFNames=CaLGV105 {ECO:0000313|EMBL:AGQ20363.1};
OS Clostera anastomosis granulovirus Henan.
OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Betabaculovirus;
OC Betabaculovirus clanastomosis.
OX NCBI_TaxID=1986291 {ECO:0000313|EMBL:AGQ20363.1, ECO:0000313|Proteomes:UP000204024};
RN [1] {ECO:0000313|EMBL:AGQ20363.1, ECO:0000313|Proteomes:UP000204024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CaLGV-Henan {ECO:0000313|EMBL:AGQ20363.1};
RX PubMed=23649176; DOI=10.1007/s00705-013-1710-y;
RA Liang Z., Zhang X., Yin X., Song X., Shao X., Wang L.;
RT "Comparative analysis of the genomes of Clostera anastomosis (L.)
RT granulovirus and Clostera anachoreta granulovirus.";
RL Arch. Virol. 158:2109-2114(2013).
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DR EMBL; KC179784; AGQ20363.1; -; Genomic_DNA.
DR OrthoDB; 3365at10239; -.
DR Proteomes; UP000204024; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1490.70; -; 1.
DR Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 2.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR InterPro; IPR036599; DNA_ligase_N_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR PANTHER; PTHR45674:SF9; DNA LIGASE 3; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 2.
DR Pfam; PF04675; DNA_ligase_A_N; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AGQ20363.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 287..397
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 553 AA; 64285 MW; 9E765DA0275678A2 CRC64;
MLFSTFADIH EAFVNLNSTT DFASFVENYC KTIKERSDAY TWLHDTRKLG GRFKINDKHL
LTIFCKITEP HIDRQNLRTA FKKHGVAETC GDVLKLNDLP SSLTMVDVYD FLHKLQTAPC
KSVSLMHLFK CIVFKCSRKE LLCLIRLIRT THKTKRSNVK KKHAFLLKRY LEFSRREVTD
NTDSQVVDRK SAQVVTKPGQ PIECMLAQPC KTIDNACFAE TCLEVKYDGE RVQLHKCNGV
VTCYKRNLNP SLKCNCILNA IQRVLRTVDN VILDCELVGN SIDNYYIVVF DVLYAHDRCL
VNEPLKTRKE ILNKLMVNQE ARMCVIDYES HLDGDNVNTR IIEMLRSGLP DVEGVMVKDY
NGTYEPKRKK WLKIRREYFE NVCSADLVVV GGWRGDKNMT IYLVATPIYD HVSNMCLFLP
VAKVKYSKND YRHLMVPYST DECKWLIVND RIKSLKKVPD MVAVDPYSMP VWEMEGDFIR
SGEAWVFGDL THNYVSIRLP RFVRVRDDKD YRQANTIFDL ALLSTISNKT FTYDALYEFF
VQDNVRNYLP RVQ
//
