ID DNLI_ASFWA Reviewed; 419 AA.
AC P0C991;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 08-NOV-2023, entry version 36.
DE RecName: Full=DNA ligase {ECO:0000250|UniProtKB:P35970};
DE EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135};
DE AltName: Full=Polydeoxyribonucleotide synthase [ATP];
GN OrderedLocusNames=War-110;
OS African swine fever virus (isolate Warthog/Namibia/Wart80/1980) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus; African swine fever virus.
OX NCBI_TaxID=561444;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kutish G.F., Rock D.L.;
RT "African swine fever virus genomes.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Very low-fidelity DNA ligase that seals nicks in double-
CC stranded DNA during DNA repair (By similarity). Together with the viral
CC repair DNA polymerase X, fills the single nucleotide gaps generated by
CC the AP endonuclease (By similarity). It is not essential for viral
CC replication and recombination (By similarity). Displays a very low
CC adenylation activity towards DNA with 3'-dideoxy- or 3'-amino-
CC terminated nicks compared to regular nick DNA (By similarity).
CC {ECO:0000250|UniProtKB:P35970}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC diphosphate.; EC=6.5.1.1; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10135};
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P35970}. Note=Found
CC in association with the viral nucleoid. {ECO:0000250|UniProtKB:P35970}.
CC -!- DOMAIN: The N-terminus domain (NTD) plays a critical role in DNA-
CC binding, catalytic complex assembly and catalysis.
CC {ECO:0000250|UniProtKB:P35970}.
CC -!- MISCELLANEOUS: Consistent with its intracellular location, ASFV encodes
CC its own replicative DNA polymerase and three base excision repair
CC enzymes: a class II AP endonuclease, the repair polymerase Pol X, and
CC an ATP-dependent DNA ligase.
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000305}.
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DR EMBL; AY261366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0C991; -.
DR Proteomes; UP000000858; Genome.
DR GO; GO:0044423; C:virion component; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR47810; DNA LIGASE; 1.
DR PANTHER; PTHR47810:SF5; LIGASE, PUTATIVE-RELATED; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 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; PS00333; DNA_LIGASE_A2; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; DNA damage; DNA recombination;
KW DNA repair; DNA replication; Ligase; Nucleotide-binding; Virion.
FT CHAIN 1..419
FT /note="DNA ligase"
FT /id="PRO_0000373090"
FT REGION 1..120
FT /note="NTD"
FT /evidence="ECO:0000250|UniProtKB:P35970"
FT REGION 121..317
FT /note="AD domain"
FT /evidence="ECO:0000250|UniProtKB:P35970"
FT REGION 318..419
FT /note="OB domain"
FT /evidence="ECO:0000250|UniProtKB:P35970"
FT ACT_SITE 151
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10135"
SQ SEQUENCE 419 AA; 48111 MW; ADEBF2669E0B59FF CRC64;
MLNHFPGHCS NNIFCFPPIE SETKSGKKAS WIICVQVVQH NTIIPITDEM FSTDVKDAVA
EIFTKFFVEE GTVRISKMTR VTEGKNLGKK NATTVVHQAF KDALSKYNRH ARQKRGAHTN
TGMIPPMLVK YFNIIPKTFF EEETDPIVQR KRNGVRAVAC QQGDGSILLY SRTEKEFLGL
DNIKKELKQL YLFIDVRVYL DGELYLHRKP LQWIAGQANA KTDSSELHFY VFDCFWSDQL
QMPSNKRQQL LTNIFKQKED LTFIHQVENF SVKNEDEALR LKAQFIKEGY EGAIVRNANG
PYEPGYNNYH SAHLAKLKPL LDAEFILVDY TQGKKGKDLG AILWVCELPN KKRFVVTPKH
LTYADRYALF QKLTPALFKK HLYGKELTVE YAELSPKTGI PLQARAVGFR EPINVLEII
//
