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Database: UniProt
Entry: P26813
LinkDB: P26813
Original site: P26813 
ID   DNLI_ASFM2              Reviewed;         419 AA.
AC   P26813;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   15-MAR-2017, entry version 72.
DE   RecName: Full=DNA ligase;
DE            EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP];
GN   Name=LIG; OrderedLocusNames=Mal-108; ORFNames=g3L;
OS   African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV).
OC   Viruses; dsDNA viruses, no RNA stage; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=10500;
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 [GENOMIC DNA].
RX   PubMed=1614852; DOI=10.1093/nar/20.11.2667;
RA   Hammond J.M., Kerr S.M., Smith G.L., Dixon L.K.;
RT   "An African swine fever virus gene with homology to DNA ligases.";
RL   Nucleic Acids Res. 20:2667-2671(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8021596; DOI=10.1099/0022-1317-75-7-1655;
RA   Dixon L.K., Twigg S.R.F., Baylis S.A., Vydelingum S., Bristow C.,
RA   Hammond J.M., Smith G.L.;
RT   "Nucleotide sequence of a 55 kbp region from the right end of the
RT   genome of a pathogenic African swine fever virus isolate (Malawi
RT   LIL20/1).";
RL   J. Gen. Virol. 75:1655-1684(1994).
RN   [3]
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   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
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; X65192; CAA46310.1; -; Genomic_DNA.
DR   EMBL; X71982; CAA50805.1; -; Genomic_DNA.
DR   EMBL; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; S23018; S23018.
DR   ProteinModelPortal; P26813; -.
DR   SMR; P26813; -.
DR   PRIDE; P26813; -.
DR   OrthoDB; VOG09000097; -.
DR   Proteomes; UP000000860; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Metal-binding;
KW   Nucleotide-binding.
FT   CHAIN         1    419       DNA ligase.
FT                                /FTId=PRO_0000059594.
FT   ACT_SITE    151    151       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10135}.
FT   METAL       203    203       Divalent metal cation 1. {ECO:0000250}.
FT   METAL       291    291       Divalent metal cation 2. {ECO:0000250}.
FT   BINDING     156    156       ATP. {ECO:0000250}.
FT   BINDING     172    172       ATP. {ECO:0000250}.
FT   BINDING     203    203       ATP. {ECO:0000250}.
FT   BINDING     232    232       ATP. {ECO:0000250}.
FT   BINDING     316    316       ATP. {ECO:0000250}.
FT   CONFLICT    149    150       HG -> QR (in Ref. 3). {ECO:0000305}.
SQ   SEQUENCE   419 AA;  48041 MW;  DA781C64CA1B10F0 CRC64;
     MLSQFPGQCS NNVFCFPPIE SETKNGKKAS WIICVQVMQH NTILPITDEM FSTDVKDAVA
     EIFTKFFVEE GAVRISKTTR VTEGKNLGKK NATTVVHQAF KDALSKYNRH ARQKRGAHTN
     RGMIPPMLVK YFNIIPKTFF EEETDPIVHG KRNGVRAVAC QQGDGSILLY SRTEKEFLGL
     DNIKKELKQL YLFIDVRVYL DGELYLHRKP LQWIAGQANA KADSSELHFY VFDCFWSDQL
     QMPSNKRQQL LTNIFKQKED LTFIHQVENF SVKNEDEALR LKTQFIKEGY EGAIVRNANG
     PYEPGYNNYH SPHLAKLKPL LDAEFILVDY TQGKKGKDLG AILWVCELPN KKRFVVTPKH
     LTYADRYALF QKLTPALFKK HLYGKELTVE YAELSPKTGI PLQARAVGFR EPINVLEII
//
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