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Database: UniProt
Entry: P0C991
LinkDB: P0C991
Original site: P0C991 
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   15-MAR-2017, entry version 18.
DE   RecName: Full=DNA ligase;
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)
OS   (ASFV).
OC   Viruses; dsDNA viruses, no RNA stage; Asfarviridae; Asfivirus.
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, during DNA
CC       repair, nicks in double-stranded DNA. Together with the viral
CC       repair DNA polymerase X, fills the single nucleotide gaps
CC       generated by the AP endonuclease. It is not essential for viral
CC       replication and recombination. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000255|PROSITE-ProRule:PRU10135}.
CC   -!- MISCELLANEOUS: Consistent with its intracellular location, ASFV
CC       encodes its own replicative DNA polymerase and three base excision
CC       repair enzymes: a class II AP endonuclease, the repair polymerase
CC       Pol X, and an ATP-dependent DNA ligase.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
DR   EMBL; AY261366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PRIDE; P0C991; -.
DR   OrthoDB; VOG09000097; -.
DR   Proteomes; UP000000858; 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:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; 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; Complete proteome; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Ligase;
KW   Nucleotide-binding.
FT   CHAIN         1    419       DNA ligase.
FT                                /FTId=PRO_0000373090.
FT   ACT_SITE    151    151       N6-AMP-lysine intermediate.
FT                                {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
//
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