GenomeNet

Database: UniProt
Entry: O57250
LinkDB: O57250
Original site: O57250 
ID   DNLI_VACCA              Reviewed;         552 AA.
AC   O57250;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-OCT-2017, entry version 75.
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=MVA163R, ACAM3000_MVA_163;
OS   Vaccinia virus (strain Ankara) (VACV).
OC   Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae;
OC   Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=126794;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9601507; DOI=10.1006/viro.1998.9123;
RA   Antoine G., Scheiflinger F., Dorner F., Falkner F.G.;
RT   "The complete genomic sequence of the modified vaccinia Ankara strain:
RT   comparison with other orthopoxviruses.";
RL   Virology 244:365-396(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Acambis 3000;
RA   Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S.,
RA   Osborne J., Khristova M., Wohlhueter R.M.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair. It is
CC       not essential for viral replication and recombination.
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   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
DR   EMBL; U94848; AAB96541.1; -; Genomic_DNA.
DR   EMBL; AY603355; AAT10561.1; -; Genomic_DNA.
DR   PIR; T37436; T37436.
DR   ProteinModelPortal; O57250; -.
DR   SMR; O57250; -.
DR   PRIDE; O57250; -.
DR   Proteomes; UP000159908; Genome.
DR   Proteomes; UP000172909; 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: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:0071897; P:DNA biosynthetic process; IEA:InterPro.
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   Gene3D; 1.10.3260.10; -; 1.
DR   InterPro; IPR000977; DNA_ligase_ATP-dep.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
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   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 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    552       DNA ligase.
FT                                /FTId=PRO_0000059587.
FT   ACT_SITE    231    231       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10135}.
FT   METAL       283    283       Divalent metal cation 1. {ECO:0000250}.
FT   METAL       377    377       Divalent metal cation 2. {ECO:0000250}.
FT   BINDING     229    229       ATP. {ECO:0000250}.
FT   BINDING     236    236       ATP. {ECO:0000250}.
FT   BINDING     251    251       ATP. {ECO:0000250}.
FT   BINDING     283    283       ATP. {ECO:0000250}.
FT   BINDING     317    317       ATP. {ECO:0000250}.
FT   BINDING     393    393       ATP. {ECO:0000250}.
FT   BINDING     397    397       ATP. {ECO:0000250}.
SQ   SEQUENCE   552 AA;  63468 MW;  AC7E18C59F4C00C1 CRC64;
     MTSLREFRKL CCDIYHASGY KEKSKLIRDF ITDRDDKYLI IKLLLPGLDD RIYNMNDKQI
     IKLYSIIFKQ SQEDMLQDLG YGYIGDTIRT FFKENTEIRP RDKSILTLEE VDSFLTTLSS
     VTKESHQIKL LTDIASVCTC NDLKCVVMLI DKDLKIKAGP RYVLNAISPH AYDVFRKSNN
     LKEIIENASK QNLDSISISV MTPINPMLAE SCDSVNKAFK KFPSGMFAEV KYDGERVQVH
     KNNNEFAFFS RNMKPVLSHK VDYLKEYIPK AFKKATSIVL DSEIVLVDEH NVPLPFGSLG
     IHKKKEYKNS NMCLFVFDCL YFDGFDMTDI PLYERRSFLK DVMVEIPNRI VFSELTNISN
     ESQLTDVLDD ALTRKLEGLV LKDINGVYEP GKRRWLKIKR DYLNEGSMAD SADLVVLGAY
     YGKGAKGGIM AVFLMGCYDD ESGKWKTVTK CSGHDDNTLR ELQDQLKMIK INKDPKKIPE
     WLVVNKIYIP DFVVEDPKQS QIWEISGAEF TSSKSHTANG ISIRFPRFTR IREDKTWKES
     THLNDLVNLT KS
//
DBGET integrated database retrieval system