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Database: UniProt/TrEMBL
Entry: A0A1B2H1E0_STRNR
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ID   A0A1B2H1E0_STRNR        Unreviewed;       511 AA.
AC   A0A1B2H1E0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   25-OCT-2017, entry version 8.
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   ECO:0000313|EMBL:ANZ20004.1};
GN   ORFNames=SNOUR_33865 {ECO:0000313|EMBL:ANZ20004.1};
OS   Streptomyces noursei ATCC 11455.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=316284 {ECO:0000313|EMBL:ANZ20004.1, ECO:0000313|Proteomes:UP000093521};
RN   [1] {ECO:0000313|EMBL:ANZ20004.1, ECO:0000313|Proteomes:UP000093521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11455 {ECO:0000313|EMBL:ANZ20004.1,
RC   ECO:0000313|Proteomes:UP000093521};
RA   Ruckert C., Albersmeier A., Winkler A., Zotchev S., Kalinowski J.;
RT   "Complete genome sequence of Streptomyces noursei ATCC 11455, a
RT   producer of the medically important antifungal antibiotic nystatin.";
RL   Submitted (APR-2015) 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; CP011533; ANZ20004.1; -; Genomic_DNA.
DR   RefSeq; WP_067354195.1; NZ_CP011533.1.
DR   EnsemblBacteria; ANZ20004; ANZ20004; SNOUR_33865.
DR   KEGG; snr:SNOUR_33865; -.
DR   PATRIC; fig|316284.13.peg.7208; -.
DR   KO; K10747; -.
DR   Proteomes; UP000093521; 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; 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:UP000093521};
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:ANZ20004.1};
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}.
FT   DOMAIN      299    417       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   ACT_SITE    210    210       N6-AMP-lysine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     208    208       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     215    215       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     230    230       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     259    259       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     299    299       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     377    377       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     383    383       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   511 AA;  54069 MW;  C5345323378AE301 CRC64;
     MLLAALARVS AEVAATSARS RKTALLAELF SAADPVDAPL VIPYLAGRLP QGRIGVGWSA
     LRDPPPPADR PTLTVRDVDA ALTALAGVAG PGAQAERRRL VGGLLAAATD QEQRFLHGLL
     TGEVRQGALD ALAVEGLAAA TGAPPDAVRR AVMLAGSLPD VARALLSDGP PALAGFRLTV
     GRPVGPMLAR TAASVAEAID RLGRCAVEEK LDGIRVQVHR DGSRVRIHTR TLDEVTDRLP
     EVTALVRELP AERLVLDGEV IALGADGRPV PFQRVAGRFG SRTDVAAARA ALPLTPVFFD
     LLALGDRALL DLPGDRRHAE LAALVPESTR VRRCVVEDPD DPGARAAAED FFDRTLRRGH
     EGVVVKALDA PYSAGRRGAA WLKVKPVHTL DLVVLAAEWG HGRRTGRLSN LHLGARAADG
     GFVMLGKTFK GLTDATLGWQ TERLGRLAVA DDGHVVTVRP ELVVEIAYDG LQTSPRYPAG
     VTLRFARVVR YREDKTAAEA DTLDTVLAAH G
//
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