GenomeNet

Database: UniProt
Entry: C3N834
LinkDB: C3N834
Original site: C3N834 
ID   DNLI_SULIY              Reviewed;         601 AA.
AC   C3N834;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-OCT-2017, entry version 55.
DE   RecName: Full=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=YG5714_2067;
OS   Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=439386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y.G.57.14 / Yellowstone #1;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(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; CP001403; ACP46321.1; -; Genomic_DNA.
DR   RefSeq; WP_012716463.1; NC_012622.1.
DR   SMR; C3N834; -.
DR   PRIDE; C3N834; -.
DR   EnsemblBacteria; ACP46321; ACP46321; YG5714_2067.
DR   GeneID; 7805625; -.
DR   KEGG; siy:YG5714_2067; -.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000002308; 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; 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; Cell cycle; Cell division; Complete proteome; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding.
FT   CHAIN         1    601       DNA ligase.
FT                                /FTId=PRO_1000205960.
FT   ACT_SITE    260    260       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     258    258       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     265    265       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     280    280       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     310    310       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     350    350       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     427    427       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     433    433       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   601 AA;  67730 MW;  5441249BBE9E413A CRC64;
     MEFKVIAEYF DKLEKISSRL QLTALLADLL SKSDKAIIDK VVYIIQGKLW PDFLGYPELG
     IGEKFLIKAI SIATNTDENS VENLYKSIGD LGEVARRLKS KQQSTGILGF LGTSSKESLK
     VDEVYSTLSK VALTTGEGSR DLKIRLLAGL LKKADPLEAK FLVRFVEGRL RVGIGDATVL
     DAMAIAFGGG QSASEIVERA YNLRADLGNI AKIIVEKGIE ALKTLKPEVG IPIRPMLAER
     LSNPEEILKK VGGSALVDYK YDGERAQIHK KDDKIFIFSR RLENITSQYP DVVEYISKYT
     EGKEFIIEGE IVAVDPESGE MRSFQELMHR KRKSDIYEAI KEYPVNVFLF DLMYYEDVDY
     TTKPLEVRRK LLESIVKPND YVKIAHHIQV NNIEDLKSFF YRAISEGGEG VMVKAIGKDA
     IYQAGARGWL WIKLKRDYQS EMADTVDLVV VGGFYGKGKR GGKISSLLMA AYNPKTDTFE
     SVCKVASGFS DEQLDELQKK LMEIKRDIKH PRVNSKMEPD IWVEPVYVAE IIGAEITISP
     LHTCCQDVVE KDAGLSIRFP RFIRWRDDKS PEDATTTDEI LEMYNKQPKK KIESPPIDES
     V
//
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