ID DNLI1_METMA Reviewed; 579 AA.
AC Q8PVR7;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 01-MAY-2013, entry version 79.
DE RecName: Full=DNA ligase 1;
DE EC=6.5.1.1;
DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;
GN Name=lig1; OrderedLocusNames=MM_1895;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 /
OS JCM 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene
RT transfer between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
CC -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC during DNA replication, DNA recombination and DNA repair (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) +
CC (deoxyribonucleotide)(m) = AMP + diphosphate +
CC (deoxyribonucleotide)(n+m).
CC -!- COFACTOR: Divalent metal cations (By similarity).
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
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DR EMBL; AE008384; AAM31591.1; -; Genomic_DNA.
DR RefSeq; NP_633919.1; NC_003901.1.
DR HSSP; P18858; 1X9N.
DR ProteinModelPortal; Q8PVR7; -.
DR STRING; 192952.MM_1895; -.
DR EnsemblBacteria; AAM31591; AAM31591; MM_1895.
DR GeneID; 1480237; -.
DR KEGG; mma:MM_1895; -.
DR eggNOG; COG1793; -.
DR HOGENOM; HOG000036008; -.
DR KO; K10747; -.
DR OMA; PAFENTT; -.
DR ProtClustDB; CLSK281490; -.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:HAMAP.
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:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:HAMAP.
DR GO; GO:0006260; P:DNA replication; IEA:HAMAP.
DR Gene3D; 1.10.3260.10; -; 1.
DR Gene3D; 2.40.50.140; -; 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; SSF50249; Nucleic_acid_OB; 1.
DR SUPFAM; SSF117018; SSF117018; 1.
DR TIGRFAMs; TIGR00574; dnl1; 1.
DR PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR PROSITE; PS00333; DNA_LIGASE_A2; FALSE_NEG.
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; Metal-binding;
KW Nucleotide-binding.
FT CHAIN 1 579 DNA ligase 1.
FT /FTId=PRO_0000365259.
FT ACT_SITE 246 246 N6-AMP-lysine intermediate (By
FT similarity).
FT BINDING 244 244 ATP (By similarity).
FT BINDING 251 251 ATP (By similarity).
FT BINDING 266 266 ATP (By similarity).
FT BINDING 296 296 ATP (By similarity).
FT BINDING 342 342 ATP (By similarity).
FT BINDING 419 419 ATP (By similarity).
FT BINDING 425 425 ATP (By similarity).
SQ SEQUENCE 579 AA; 65867 MW; 9E11E66075B8DEEC CRC64;
MRFKELAELF EELEKTTSHR EIVRKISEFF KNLRGDEVKD SAYLFLGSTG PAFENTTLGI
KDMLAIRAIA GAYGVTREDV RKRYARTGDL GDVAFELSKK RESSLTIEDV FQRLLQIRET
SGKGSQEEKT ALFSDILQKA TPEEGKYIVR LVLGRLRLGF GDQFLLEAFA IAFTGDKKHA
AKIKESYSVC TDIGELAKIL AENGARATGF ISIKPGRPVK SMLSQRVESF EELEKRVKGK
KAAEEKYDGE RVQVHKTGEG IKAFSRRLED ITSQYPEIIE DVRKTVPANE IVLDGEIVAY
AELERNGNRI EEFYPFQNLM QRRRKYEIEN YRKKCPVAVF FFDILYLNGE PLLKRPYPER
RALLEMNVVE SGIIRLSKRI VTESVEEIED FFNETIEKGL EGIVVKSMSS NSYYEAGKRS
WFWFKWKQEY SEGMRETFDL VVVGSYYGRG RRKGSFGALL CAVLNKEGQR FETLTKVGTG
FTEADAEEIN RLLSDHIVSE IPKGVSIKKG MLPDIFIEPA VVIEVLGSEI TNSPGHTAGE
GEEETGLALR FPRFLRIRHD KTPYDAMTVK EVRDLKDGT
//
