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Database: UniProt/TrEMBL
Entry: G8RRH7_MYCRN
LinkDB: G8RRH7_MYCRN
Original site: G8RRH7_MYCRN 
ID   G8RRH7_MYCRN            Unreviewed;       515 AA.
AC   G8RRH7;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   25-OCT-2017, entry version 40.
DE   RecName: Full=Probable DNA ligase {ECO:0000256|HAMAP-Rule:MF_00407};
DE            EC=6.5.1.1 {ECO:0000256|HAMAP-Rule:MF_00407};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] {ECO:0000256|HAMAP-Rule:MF_00407};
GN   Name=lig {ECO:0000256|HAMAP-Rule:MF_00407};
GN   OrderedLocusNames=MycrhN_6018 {ECO:0000313|EMBL:AEV76480.1};
OS   Mycobacterium rhodesiae (strain NBB3).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=710685 {ECO:0000313|EMBL:AEV76480.1, ECO:0000313|Proteomes:UP000005442};
RN   [1] {ECO:0000313|EMBL:AEV76480.1, ECO:0000313|Proteomes:UP000005442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBB3 {ECO:0000313|EMBL:AEV76480.1,
RC   ECO:0000313|Proteomes:UP000005442};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T.,
RA   Holmes A., Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT   "Complete sequence of Mycobacterium rhodesiae NBB3.";
RL   Submitted (DEC-2011) 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.
CC       {ECO:0000256|HAMAP-Rule:MF_00407}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000256|HAMAP-Rule:MF_00407,
CC       ECO:0000256|RuleBase:RU000617}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00407};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00407, ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; CP003169; AEV76480.1; -; Genomic_DNA.
DR   RefSeq; WP_014214217.1; NC_016604.1.
DR   STRING; 710685.MycrhN_6018; -.
DR   EnsemblBacteria; AEV76480; AEV76480; MycrhN_6018.
DR   KEGG; mrh:MycrhN_6018; -.
DR   PATRIC; fig|710685.3.peg.6043; -.
DR   eggNOG; ENOG4107RYT; Bacteria.
DR   eggNOG; COG1793; LUCA.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG091H0BGA; -.
DR   Proteomes; UP000005442; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-UniRule.
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-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.3260.10; -; 2.
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 {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005442};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617, ECO:0000313|EMBL:AEV76480.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005442}.
FT   DOMAIN      292    416       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   ACT_SITE    215    215       N6-AMP-lysine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     213    213       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     220    220       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     235    235       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     264    264       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     304    304       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     376    376       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     382    382       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   515 AA;  54464 MW;  5646D39EF2AB4048 CRC64;
     MQLLDVAAAS AEVGASSARL KKIARIADLL RRAGEEDDAK LVAVVVSWLS GELPQRQIGV
     GWATLRSLPA AAAQASMTVL DVDARLSEIG AVAGKGSQAR RADLVTELFG AATAVEQMFL
     RRLLSGELRQ GALIGVMADA VAKAADVPAA AVRRAAMLGG ALPSVAAAAL TAGEAALEQF
     TLTVGRPVGP MLAQTATGVA DALERLGGTG AFEAKLDGAR VQIHRSGDAV SIYTRSLDDV
     TARLPEIVEA TLALPVTDLI ADAEAIALRP DNRPHRFQVT ASRFGRSVDI AAARSAQPLS
     MFVFDLLHLD GTDLLDLPTS ERVAALDEVV PKVHRVDRLI TDDVDAATGF LDATLAAGHE
     GVMAKSLTAP YEAGRRGAGW LKVKPVHTLD LVVLAVEWGS GRRTGKLSNI HLGARDPESG
     EFIMLGKTFK GMTDAMLDWQ TARFTELADG PTDGYVVKVR PEQVVEIALD GVQTSSRYPG
     GMALRFARVL RYRDDKSPAE VDTIDTVRAL HQRGD
//
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