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Database: UniProt/TrEMBL
Entry: D5EA92_METMS
LinkDB: D5EA92_METMS
Original site: D5EA92_METMS 
ID   D5EA92_METMS            Unreviewed;       561 AA.
AC   D5EA92;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   25-OCT-2017, entry version 45.
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=Mmah_0567 {ECO:0000313|EMBL:ADE36093.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE36093.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE36093.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Lykidis A., Saunders E., Brettin T., Detter J.C., Han C.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Spring S., Schneider S., Schroeder M., Klenk H.-P.,
RA   Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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; CP001994; ADE36093.1; -; Genomic_DNA.
DR   RefSeq; WP_013037036.1; NC_014002.1.
DR   ProteinModelPortal; D5EA92; -.
DR   STRING; 547558.Mmah_0567; -.
DR   EnsemblBacteria; ADE36093; ADE36093; Mmah_0567.
DR   GeneID; 8982715; -.
DR   KEGG; mmh:Mmah_0567; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; ETVCNIG; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000001059; 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; 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:UP000001059};
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:ADE36093.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059}.
FT   DOMAIN      334    462       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   ACT_SITE    256    256       N6-AMP-lysine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     254    254       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     261    261       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     276    276       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     306    306       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     346    346       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     421    421       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     427    427       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   561 AA;  62553 MW;  3F8B391E8D73AF83 CRC64;
     MTSFEYFANT CASIEHIPGS LEMTDVIAKL LKEVTIEELP IVTHFVMGSV FPAWSDRQMG
     VGNRLLYTAL SKSSGVSEEE IENIIRKTGD IGETAVQALS SNPAGQSTFS AFIEEKPGME
     IKEVYERFTH IADTAGKRSH GTKIKNLQYL FNSATPIEAR YLARLAIEQL RIGVGEGIVR
     DAISKAFETD VDVVERALML TNDLGLVAVA ACNGGNEEVQ KLDIQLNRPV KMMLAQVTSS
     IQSALNDLGE VAVEWKFDGA RVQIHKEGEN IHIFSRRLEN VTSSLPDVVK EVQENVNADT
     AILEGEAVAI GKDGKPRAFQ DILKRFRRKY DVEAIAKAIP LKLNLFDVLY LNGESLIDNP
     LRKRRELLFQ NVQSSDRILV DRQVITDNEE EIQEIYADAL RAGHEGIMIK KPDAPYSPGK
     RGKNWLKKKP LMETLDLVVI GAEWGYGRRA NLIGSYALGC YDPDTGKFPA IGKVATGITD
     EKLAELTTLF SDLVVYEAGR KIELKPEIVF EIAFEEIQKS PNYESGYALR FPRLVNVRDD
     KSPEEAESLE RIGEIYHSQR S
//
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