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Database: UniProt
Entry: Q4JAM1
LinkDB: Q4JAM1
Original site: Q4JAM1 
ID   DNLI_SULAC              Reviewed;         598 AA.
AC   Q4JAM1;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   07-JUN-2017, entry version 79.
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=Saci_0788;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 /
OS   NBRC 15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/JB.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
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; CP000077; AAY80158.1; -; Genomic_DNA.
DR   RefSeq; WP_011277660.1; NC_007181.1.
DR   ProteinModelPortal; Q4JAM1; -.
DR   SMR; Q4JAM1; -.
DR   STRING; 330779.Saci_0788; -.
DR   EnsemblBacteria; AAY80158; AAY80158; Saci_0788.
DR   GeneID; 3473850; -.
DR   KEGG; sai:Saci_0788; -.
DR   PATRIC; fig|330779.12.peg.755; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000001018; 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; 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; Reference proteome.
FT   CHAIN         1    598       DNA ligase.
FT                                /FTId=PRO_0000059616.
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   598 AA;  67576 MW;  D8C6D946CF2D76A4 CRC64;
     MEFKLIAEYF DRLEKISSRI QLTALLTDLL KKSDKDVIDK VIYITQGKLW PDFFEKPEIG
     LGEKLMIKAL SVSTNIKEDE IEKQLRILGD LGEVAYKLKR TNSSQNVLSY LGSTKVTKLT
     VEEVYESLSK IALSEGEGSR DMKIRSLAGL LKKADPLEAK YIIRFIDGRL RVGIGDATIM
     DALANVFGGG TAARPLIERA YNLRADLGNI AKLLAENGIE TIKSIKPEVG IPIRPMLAER
     LTDPSEILAK VGGKGIVDYK YDGERAQIHK KGEKVYIFSR RLENITRQYP DVVEYIKNSI
     KSNEVILEGE IVAIDKESGE ILPFQNLMHR KRKNDIGEAI KEYPVNVYLF DLMYNDGEDY
     TQKPLPDRRE KLEEIVTQND IVKVADHKYI DKVNELVEYF HQAISDGTEG VIVKSIGKDS
     IYQAGARGFL WIKLKKDYQS EMADSVDLVI VGAFYGRGKR GGKLSSLLMA AYDPDKDTFY
     TVCKVASGFS DAELEEVQKM LSEAKLDKKD PRVESEIQPD IWVKPKYVAE IIGAEITLSP
     LHTCCKGVVS EEAGLSIRFP RFIRWRDDKS VEEATTPNEI LEMYQSRLKK KVEDITET
//
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