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Database: UniProt
Entry: D2PKZ8_KRIFD
LinkDB: D2PKZ8_KRIFD
Original site: D2PKZ8_KRIFD 
ID   D2PKZ8_KRIFD            Unreviewed;       517 AA.
AC   D2PKZ8;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   05-DEC-2018, entry version 56.
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=Kfla_3406 {ECO:0000313|EMBL:ADB32465.1};
OS   Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Kribbella.
OX   NCBI_TaxID=479435 {ECO:0000313|EMBL:ADB32465.1, ECO:0000313|Proteomes:UP000007967};
RN   [1] {ECO:0000313|Proteomes:UP000007967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC   {ECO:0000313|Proteomes:UP000007967};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Saunders E., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Pukall R., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Kribbella flavida DSM 17836.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADB32465.1, ECO:0000313|Proteomes:UP000007967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC   {ECO:0000313|Proteomes:UP000007967};
RX   PubMed=21304701;
RA   Pukall R., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA   Cheng J.-F., Lucas S., Chen F., Nolan M., LaButti K., Pati A.,
RA   Ivanova N., Mavrommatis K., Mikhailova N., Pitluck S., Bruce D.,
RA   Goodwin L., Land M., Hauser L., Chang Y.-J., Jeffries C.D., Chen A.,
RA   Palaniappan K., Chain P., Rohde M., Goeker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P., Brettin T.;
RT   "Complete genome sequence of Kribbella flavida type strain (IFO
RT   14399).";
RL   Stand. Genomic Sci. 2:186-193(2010).
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:
CC       Reaction=ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP +
CC         diphosphate.; EC=6.5.1.1; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00407, 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; CP001736; ADB32465.1; -; Genomic_DNA.
DR   STRING; 479435.Kfla_3406; -.
DR   EnsemblBacteria; ADB32465; ADB32465; Kfla_3406.
DR   KEGG; kfl:Kfla_3406; -.
DR   eggNOG; ENOG4107RYT; Bacteria.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG091H0BGA; -.
DR   BioCyc; KFLA479435:G1GG1-3406-MONOMER; -.
DR   Proteomes; UP000007967; 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; -; 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 {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:UP000007967};
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:ADB32465.1};
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:UP000007967}.
FT   DOMAIN      293    417       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   ACT_SITE    218    218       N6-AMP-lysine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     216    216       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     223    223       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     238    238       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     267    267       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     305    305       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   517 AA;  56216 MW;  0B14317245D9FA00 CRC64;
     MGQTGVMLLA DVVATSSSLS GTRSRLAKAK FIAELLTAAT DPVETEVVVT YLSGELRQRR
     TGVGWRTLAD VPEPAATPSL TVEQVDRTFA ELAEIAGAGS QARRREAVNA LFGRATEPEQ
     RFLRQLVAGE LRQGALDGVM ADAVAKATGI ALEKIRAATM LRGAAAPVAV AALTEGEAGL
     AQFGLEVGRG VQPMLAQSAT TVAEAMTKTG TPAAIEWKLD GIRIQVHRDG DRVVVYTRTL
     DDITDRAPEV VTATLELEAE QVVLDGELIA LRPDGRPEAF QVTGSRTATR AATGPETVPL
     TPYFFDILHL DGQDLLGLGG AERHEWLSRL VPEHRRIPRL VTDDAEAGQA FFADAVKRGH
     EGVMVKSLSV PYEAGRRGSG WVKVKQTHTL DLVVLAAEWG HGRRTGWLSN LHLGARDEQT
     GEFVMLGKTF KGLTDELLRW QTERFQQLEV SRDAYTVYLR PEIVVEIAFD GVQTSPRYPA
     GMALRFARVL RYREDKTADQ VDTVQTVRAI HQPGEDT
//
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