ID   DNLI_ASFK5              Reviewed;         419 AA.
AC   P0C992;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 25.
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=Ken-112;
OS   African swine fever virus (isolate Pig/Kenya/KEN-50/1950) (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=561445;
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; AY261360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; P0C992; -.
DR   Proteomes; UP000000861; Genome.
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   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   SUPFAM; SSF50249; SSF50249; 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_0000373091"
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;  48147 MW;  EF69CD1F30D21BF8 CRC64;
     MLNQFPGQLS NNVFCFPPIE SETKSGKKAS WIICVQVMHH NTILPITDEM FSTDVKDAVA
     EIFTKFFVEE GAVRISKTTR VTEGKNLGKK NATTVVHQAF KDALSKYNRH ARQKRGAHTN
     RGMIPPMLVK HFNIIPKTFF EDETDPIVQR KRNGVRAVAC QQGDGSILLY SRTEKEFLGL
     DNIKKELKQL YLFIDVRVYL DGELYLHHKP LQWIAGQANA KVDSSELHFY VFDCFWSDQL
     QMPSNKRQQL LTNIFKQKED LIFIHQVENF SIKDEDEALR LKTQFIKEGY EGAIVRNANG
     PYEPGYNNYH SPHLAKLKPL LDAEFILVDY TQGKKGKDLG AILWVCELPN KKRFVVTPKH
     LTYADRYALF QKLTPALFKK HLYGKELTVE YAELSPKTGI PLQARAVGFR EPINVLEII