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Database: UniProt/TrEMBL
Entry: A0A1V0V1H3_9ACTN
LinkDB: A0A1V0V1H3_9ACTN
Original site: A0A1V0V1H3_9ACTN 
ID   A0A1V0V1H3_9ACTN        Unreviewed;       511 AA.
AC   A0A1V0V1H3;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   25-OCT-2017, entry version 5.
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   ORFNames=B7C62_02725 {ECO:0000313|EMBL:ARF71289.1};
OS   Kitasatospora albolonga.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Kitasatospora.
OX   NCBI_TaxID=68173 {ECO:0000313|EMBL:ARF71289.1, ECO:0000313|Proteomes:UP000192251};
RN   [1] {ECO:0000313|EMBL:ARF71289.1, ECO:0000313|Proteomes:UP000192251}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 101047 {ECO:0000313|EMBL:ARF71289.1,
RC   ECO:0000313|Proteomes:UP000192251};
RA   Yin M., Jiang Y.;
RT   "The complete genome sequence of Streptomyces albolongus YIM 101047,
RT   the producer of novel bafilomycins and novel odoriferous
RT   sesquiterpenoids.";
RL   Submitted (APR-2017) 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; CP020563; ARF71289.1; -; Genomic_DNA.
DR   Proteomes; UP000192251; 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:UP000192251};
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:ARF71289.1};
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:UP000192251}.
FT   DOMAIN      287    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;  54471 MW;  1A2955A5E43E2167 CRC64;
     MLLAELAQVS LEVAATSARS RKVALLAALF RDAGPDDVPV AIPYLAGRLP QGRIGVGWRS
     LGDPVEPAAE PTLTVTGVDA GLTALAAISG TGSQALRRER LRALFAAATA DEQHFLKALL
     TGELRQGALD AVAADALARA AEAPPADVRR AVMLAGSLPE VARPLLAEGP GALASFRLTV
     GRPVQPMLAH TAASVTEAVE KLGACAVEEK LDGIRVQVHR DGDRVRAYTR TLDDITDRLP
     ELVAAVAGLE TGRFILDGEV IALGEDGRPR PFQETASRVG SRRDVAAAAA DVPIVPVFFD
     ALSADGDDLL DLPFADRHAA LARLVPEPLR VRRTLVPDPG DADARRAAEA FLAETLERGH
     EGVVVKDLAA AYSAGRRGAS WLKVKPVHTL DLVVLAAEWG SGRRTGKLSN LHLGARRPDG
     TFAMLGKTFK GLTDALLEWQ TEKLRELATG EDGHIVTVRP ELVVEIAYDG LQRSTRYPAG
     VTLRFARVLR YREDKTAQEA DTVETVLSQQ R
//
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