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Database: UniProt
Entry: A0A0G0AAY8_9BACT
LinkDB: A0A0G0AAY8_9BACT
Original site: A0A0G0AAY8_9BACT 
ID   A0A0G0AAY8_9BACT        Unreviewed;       603 AA.
AC   A0A0G0AAY8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   28-MAR-2018, entry version 12.
DE   RecName: Full=Probable 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=UR43_C0003G0089 {ECO:0000313|EMBL:KKP53768.1};
OS   candidate division TM6 bacterium GW2011_GWF2_33_332.
OC   Bacteria; Candidatus Dependentiae.
OX   NCBI_TaxID=1619080 {ECO:0000313|EMBL:KKP53768.1, ECO:0000313|Proteomes:UP000034634};
RN   [1] {ECO:0000313|EMBL:KKP53768.1, ECO:0000313|Proteomes:UP000034634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a
RT   large radiation of phyla.";
RL   Nature 0:0-0(2015).
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00407}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KKP53768.1}.
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DR   EMBL; LBPE01000003; KKP53768.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKP53768; KKP53768; UR43_C0003G0089.
DR   Proteomes; UP000034634; Unassembled WGS sequence.
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; 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:UP000034634};
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:KKP53768.1};
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:UP000034634}.
FT   DOMAIN      337    476       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     261    261       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     280    280       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     309    309       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     349    349       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     429    429       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     435    435       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   603 AA;  68409 MW;  08CFA3709F121C44 CRC64;
     MKFKFVTESF EQIEKESSRT SITKMIAELL KKSSPQEAAI ISYLALGELR PSYQGTQFHV
     AEKSLINVIA AALNKSVATV KTYLKKIGDL GLVFVEFGFS GQHQENLFED SHKKDLSVLE
     VYEKLNSVLD ISGTGSQDKK ENEILHLLKI LDPISAKYIL RIIVGKLRLG FSDMTLLDAF
     SWMESGDKSL RVKLEDAYNV SADIGLIIKT LKEDGIKGIE KMKIIPGVPI RPAAAERLAN
     AKAIFAKLGP CVAQPKFDGF RLQVHKFKHK GKVEVRFFSR NLQDMSHMFP ELTEAVKNMQ
     IDSFVAEGEA ISFDVETGTF LPFQETVKRR RKYEVEKFSQ DFPLKLFLFD LLYFEGESIL
     NKEYKYRRAE LKNLISKVSK DAHAIIELTE EKKMDSAQEM EQFFHENISD GLEGIVVKKL
     DAIYQPGKRN FNWVKLKREE AGHLEDTIDC VILGYNAGHG KRAHFGLGAF LVGVFNPKKD
     IFQTVAKIGT GLSDQEWKDL KKKCDEFEVA NKPKNVDCKK ELYPDIWVSP EIVCAIRADE
     ITISPIHTAG SVEAIKTHEG FALRFPRIMG YRPDKSATDA TTVEELKHLF DIQFKSEKKN
     KKK
//
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