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Database: UniProt
Entry: C0QSL7
LinkDB: C0QSL7
Original site: C0QSL7 
ID   DNLI_PERMH              Reviewed;         582 AA.
AC   C0QSL7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 58.
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=PERMA_1901;
OS   Persephonella marina (strain DSM 14350 / EX-H1).
OC   Bacteria; Aquificae; Aquificales; Hydrogenothermaceae; Persephonella.
OX   NCBI_TaxID=123214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14350 / EX-H1;
RX   PubMed=19136599; DOI=10.1128/JB.01645-08;
RA   Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA   Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA   Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT   "Complete and draft genome sequences of six members of the
RT   Aquificales.";
RL   J. Bacteriol. 191:1992-1993(2009).
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; CP001230; ACO03229.1; -; Genomic_DNA.
DR   RefSeq; WP_012675468.1; NC_012440.1.
DR   ProteinModelPortal; C0QSL7; -.
DR   SMR; C0QSL7; -.
DR   STRING; 123214.PERMA_1901; -.
DR   PRIDE; C0QSL7; -.
DR   EnsemblBacteria; ACO03229; ACO03229; PERMA_1901.
DR   KEGG; pmx:PERMA_1901; -.
DR   eggNOG; ENOG4107TRG; Bacteria.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; ETVCNIG; -.
DR   OrthoDB; POG091H09SJ; -.
DR   Proteomes; UP000001366; 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; 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; 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    582       Probable DNA ligase.
FT                                /FTId=PRO_1000134730.
FT   ACT_SITE    250    250       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     248    248       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     255    255       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     270    270       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     299    299       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     339    339       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     416    416       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     422    422       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   582 AA;  66893 MW;  86B7BDB3B593C637 CRC64;
     MEYTKLAQLY QILEETTSRI KMTQALVDLF KETPPELIDK VVYLSIGRIA PEYTGLDYNF
     SEKSAIKALS TVLNISEHDI QHQVLQTGDL GDAGKKLYEE KGVKPEGILT VEEVYRTLRE
     IAQTTGYGST KKKLQLFTEL LKKASPLEVK YLLRTITERL RLGIGDNTIM DALSIAFTGK
     KENREIIERA YNISSDLGYV ARILAEKGLD AVKNIKIEIG RPIRPMLAER MAIPSYILKK
     LGGKAGAEYK YDGERIQVHR KGDTFYLFSR RLENITDQFP DLIEFLKESI PEECIIELEA
     VVIDPSSGAI RPFQDLMNRR VKYVTRFHIM MYPIAGFIFD IMYLNGEDLT LKPYPERRKI
     LEENIKITER INLSERKIVD NVEDLESFFH QAIEDGCEGL VCKSLQKDSI YQAGKRGFLW
     IKYKRDYKSH LADTLDLVVV GAFYGKGART GYFGSLLMAC YDPETDQFKT VCKVGTGFKE
     DDFKKLDDLL KEHTLDHKHP RVNSILSADI WYEPFLVLEI TGAELTLSPV HTCGWDRIKI
     NRGLGLRFPR FTGRYRFDKR PEDATTEEEI INMYKNQIQI KS
//
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