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Database: UniProt/TrEMBL
Entry: A0A0E3SRM4_METMT
LinkDB: A0A0E3SRM4_METMT
Original site: A0A0E3SRM4_METMT 
ID   A0A0E3SRM4_METMT        Unreviewed;       561 AA.
AC   A0A0E3SRM4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   28-MAR-2018, entry version 16.
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   ORFNames=MCMEM_1588 {ECO:0000313|EMBL:AKB85641.1};
OS   Methanococcoides methylutens MM1.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=1434104 {ECO:0000313|EMBL:AKB85641.1, ECO:0000313|Proteomes:UP000033048};
RN   [1] {ECO:0000313|EMBL:AKB85641.1, ECO:0000313|Proteomes:UP000033048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MM1 {ECO:0000313|EMBL:AKB85641.1,
RC   ECO:0000313|Proteomes:UP000033048};
RA   Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA   Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT   "Methanogenic archaea and the global carbon cycle.";
RL   Submitted (JUL-2014) 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; CP009518; AKB85641.1; -; Genomic_DNA.
DR   RefSeq; WP_048205708.1; NZ_CP009518.1.
DR   EnsemblBacteria; AKB85641; AKB85641; MCMEM_1588.
DR   GeneID; 24894149; -.
DR   KEGG; mmet:MCMEM_1588; -.
DR   PATRIC; fig|1434104.5.peg.1727; -.
DR   KO; K10747; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000033048; 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:UP000033048};
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:AKB85641.1};
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      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;  61941 MW;  3812FD5EC8AB2158 CRC64;
     MTDFKDFADV CKRIEHTSGS LDMTDIVSEM FHSVSAEELP VVAHFVMGDV FPAWSTEQLG
     VGPSLLYTAL SRSSGLPLKE IETLVRNTGD IGETAIAALK KETRNQATFS AFMDETPSLS
     IMEVFERFNN ISGTTGKGSQ TTKIKNLQYL FNSATPEEAR YLARLAIEDL RIGVGEGIVR
     DAIAKAFGVP AGDVERGFML TNDLGLVAVA AKEGGVEAVS QLGMELNRPI KMMLAQVTPT
     IETAINDLGV VAVEWKFDGA RVQIHKDGDN INIFSRRLEN VTGSLPDIVQ AVKDHVKADT
     AILEGEAVAV DEHGNPRAFQ DILKRFRRKY DVETTVREIP LTLNLFDLLY LNDEVLIDMP
     LTDRRDALVD CVENTNGIRV DEQVLTKDPE KVNEIYSAAL AAGHEGVMIK NPEAPYSPGK
     RGKNWLKKKP IMETLDLVVV GAEWGYGRRA NLIGSYALAC FDPDTGDFLP IGKVATGFSD
     EQLAELTDLL SDLIVVESGR DIELKPEVVF EVAFEEIQKS TNYESGYALR FPRLVNIRDD
     KSPEEAETLE RIESIYLSQR S
//
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