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Database: UniProt
Entry: Q73V97
LinkDB: Q73V97
Original site: Q73V97 
ID   DNLI_MYCPA              Reviewed;         519 AA.
AC   Q73V97;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-OCT-2017, entry version 92.
DE   RecName: Full=Probable DNA ligase {ECO:0000255|HAMAP-Rule:MF_00407};
DE            EC=6.5.1.1 {ECO:0000255|HAMAP-Rule:MF_00407};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] {ECO:0000255|HAMAP-Rule:MF_00407};
GN   Name=lig {ECO:0000255|HAMAP-Rule:MF_00407};
GN   OrderedLocusNames=MAP_3117;
OS   Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D.,
RA   Banerji N., Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair.
CC       {ECO:0000255|HAMAP-Rule:MF_00407}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000255|HAMAP-Rule:MF_00407}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00407};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00407}.
DR   EMBL; AE016958; AAS05665.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q73V97; -.
DR   SMR; Q73V97; -.
DR   STRING; 262316.MAP3117; -.
DR   EnsemblBacteria; AAS05665; AAS05665; MAP_3117.
DR   KEGG; mpa:MAP_3117; -.
DR   eggNOG; ENOG4107QIM; Bacteria.
DR   eggNOG; COG1793; LUCA.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG091H0BGA; -.
DR   Proteomes; UP000000580; Chromosome.
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   HAMAP; MF_00407; DNA_ligase; 1.
DR   InterPro; IPR022865; DNA_ligae_ATP-dep_bac/arc.
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; Magnesium;
KW   Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    519       Probable DNA ligase.
FT                                /FTId=PRO_0000365226.
FT   ACT_SITE    223    223       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     221    221       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     228    228       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     243    243       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     272    272       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     312    312       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     384    384       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     390    390       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   519 AA;  54125 MW;  68D302030E941C0B CRC64;
     MSPSHAKLAT VLLFDVATAS ADVGGTPSRL TKVARIADLL RRAAPNAALV AIVVSWLSGE
     LRQRQIGVGW AALRSRPPAA AHPTLTVVAV DAAFAEIGAV AGKGAQARRA ALLNALFAAA
     TETEQTFLLR LLGGELRQGA LAGIMADAVA RAAGIPAAAV QRAAMLGGDL PAVAAAALSG
     EASALDAFTL RVGRPVAPML AQTAAGVAQA IERHGGQAIF EAKLDGARVQ IHRAGDQVTV
     YTRSLDDVTA RLPEVVTATL ALPVEALIAD GEAIALRPDN SPQRFQVTAS RFGRSLDVAA
     AVAAQPLSVF IFDILHCDGI DLLDAPTTDR LAALDALVPP AQRVDRLLTA DPDAAGRFLE
     ATLAAGHEGV MAKAPGAPYQ AGRRGAGWLK VKPVHTLDLV VLAVEWGSGR RRGKLSNIHL
     GARDPATGEF VMVGKTFKGM TDAMLDWQTA RFTELAVGGT DGYVVRVRPE QVVEVAVDGV
     QKSSRYPGGL ALRFARVLRY RDDKGPAEAD TIDAVRALY
//
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