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Database: UniProt
Entry: A0A1Q7HX61_9CHLR
LinkDB: A0A1Q7HX61_9CHLR
Original site: A0A1Q7HX61_9CHLR 
ID   A0A1Q7HX61_9CHLR        Unreviewed;       341 AA.
AC   A0A1Q7HX61;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=ATP-dependent DNA ligase family profile domain-containing protein {ECO:0000259|PROSITE:PS50160};
GN   ORFNames=AUH85_07635 {ECO:0000313|EMBL:OLC56026.1};
OS   Chloroflexi bacterium 13_1_40CM_4_68_4.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1805077 {ECO:0000313|EMBL:OLC56026.1, ECO:0000313|Proteomes:UP000185706};
RN   [1] {ECO:0000313|EMBL:OLC56026.1, ECO:0000313|Proteomes:UP000185706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC         diphosphate.; EC=6.5.1.1; Evidence={ECO:0000256|ARBA:ARBA00034003};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OLC56026.1}.
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DR   EMBL; MNFM01000075; OLC56026.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7HX61; -.
DR   Proteomes; UP000185706; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   CDD; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1.
DR   Gene3D; 3.30.1490.70; -; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR45674:SF15; DNA LIGASE (ATP); 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   4: Predicted;
FT   DOMAIN          116..198
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   341 AA;  38143 MW;  C0EF3DF9CFE0998B CRC64;
     METTKDAPPL PRHLAPMQPR LAIAAFNSDD FIFEVKWDGV RALVAKDATG LRVTDRHGMD
     LLARVPELAR AARQLPEGVL LDAELVICDA QGRPRYEQLA ARLGRAQRKA GRGPLLLAFD
     LLYESYRSLM DHPLLERRER LVRLVVPGAP ILVPEHLESD GEPFLEAVRE FGLEGVVAKR
     HDSTYVPGAR AADWFKVHAV GRMDVAVCGV IDRDGAPYRL VCGAYRDQSL TYVGRAYIPP
     FLREYVRREL EGLERDDSPL DAPVELQPGL NWVAPERCAI VEHAGGDGAP LGDDARLRSF
     RVDLRPEDCH VEEAVRMPSG APRLERDRPR LVVLRSLFPH D
//
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