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Database: UniProt/TrEMBL
Entry: F4HIS4_PYRSN
LinkDB: F4HIS4_PYRSN
Original site: F4HIS4_PYRSN 
ID   F4HIS4_PYRSN            Unreviewed;       559 AA.
AC   F4HIS4;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   25-OCT-2017, entry version 38.
DE   RecName: Full=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=PNA2_0205 {ECO:0000313|EMBL:AEC51123.1};
OS   Pyrococcus sp. (strain NA2).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=342949 {ECO:0000313|EMBL:AEC51123.1, ECO:0000313|Proteomes:UP000008293};
RN   [1] {ECO:0000313|EMBL:AEC51123.1, ECO:0000313|Proteomes:UP000008293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA2 {ECO:0000313|EMBL:AEC51123.1,
RC   ECO:0000313|Proteomes:UP000008293};
RX   PubMed=21602357; DOI=10.1128/JB.05150-11;
RA   Lee H.S., Bae S.S., Kim M.S., Kwon K.K., Kang S.G., Lee J.H.;
RT   "Complete genome sequence of hyperthermophilic Pyrococcus sp. strain
RT   NA2, isolated from a deep-sea hydrothermal vent area.";
RL   J. Bacteriol. 193:3666-3667(2011).
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   -!- 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; CP002670; AEC51123.1; -; Genomic_DNA.
DR   RefSeq; WP_013747681.1; NC_015474.1.
DR   ProteinModelPortal; F4HIS4; -.
DR   STRING; 342949.PNA2_0205; -.
DR   EnsemblBacteria; AEC51123; AEC51123; PNA2_0205.
DR   GeneID; 10553665; -.
DR   KEGG; pyn:PNA2_0205; -.
DR   PATRIC; fig|342949.8.peg.204; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   KO; K10747; -.
DR   OMA; ETVCNIG; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000008293; 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   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008293};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00407};
KW   DNA recombination {ECO:0000256|HAMAP-Rule:MF_00407};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00407};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00407, ECO:0000313|EMBL:AEC51123.1};
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}.
FT   DOMAIN      327    455       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   ACT_SITE    249    249       N6-AMP-lysine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     247    247       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     254    254       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     269    269       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     299    299       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     339    339       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     414    414       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     420    420       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   559 AA;  63673 MW;  B7F132A0AD0B9DC2 CRC64;
     MRYLELAQLY QKLEKTTMKL IKTRLVADFL KKVPEDHLDF IPYLILGDVF PEWDERELGV
     GEKLLIRAVS MATGVDPQEI ENSVKDTGDL GESIALAVKK RKQRSFFSQP LTIKRVYQTL
     VKVAETTGEG SQEKKMKYLA NLFMDAEPIE AKYIARTVLG TMRTGVAEGL LRDAIALAFH
     VKVELVERAY MLTSDFGFVA KIAKAEGNEG LSKVTIQLGK PIKPMLAQQA ANIKEALLEM
     GGEAEFEIKY DGARVQVHKD GNKVIVYSRR LENVTRAIPE IVEAIRSAIK AERAIVEGEL
     VAIGENGRPL PFQYVLRRFR RKHNIEEMMK KIPLELNLFD VLYVDGTSYI DTEFIKRRET
     LERIVEPNGK IKIAENLITR KVEEAEEFYK RALEMGHEGL MAKRLDAVYE PGNRGKKWLK
     IKPTMENLDL VIIGAEWGEG RRAHLLGSFI LGAYDPETGE FVEVGKVGSG FTDDDLLEFT
     KMLKPLIIKE EGKRVWVQPK IVIEVTYQEI QKSPKYKSGF ALRFPRYVAL RDDKSPEDAD
     TIERIAQLYE LQERMKGKI
//
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