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Database: UniProt
Entry: A0A1G6RVG4_9MICO
LinkDB: A0A1G6RVG4_9MICO
Original site: A0A1G6RVG4_9MICO 
ID   A0A1G6RVG4_9MICO        Unreviewed;       900 AA.
AC   A0A1G6RVG4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=SAMN05216410_2789 {ECO:0000313|EMBL:SDD08632.1};
OS   Sanguibacter gelidistatuariae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Sanguibacteraceae;
OC   Sanguibacter.
OX   NCBI_TaxID=1814289 {ECO:0000313|EMBL:SDD08632.1, ECO:0000313|Proteomes:UP000199039};
RN   [1] {ECO:0000313|EMBL:SDD08632.1, ECO:0000313|Proteomes:UP000199039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISLP-3 {ECO:0000313|EMBL:SDD08632.1,
RC   ECO:0000313|Proteomes:UP000199039};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; FMYH01000005; SDD08632.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6RVG4; -.
DR   STRING; 1814289.SAMN05216410_2789; -.
DR   Proteomes; UP000199039; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1.
DR   CDD; cd04863; MtLigD_Pol_like; 1.
DR   CDD; cd07971; OBF_DNA_ligase_LigD; 1.
DR   Gene3D; 3.30.1490.70; -; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 3.90.920.10; DNA primase, PRIM domain; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
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; IPR014144; LigD_PE_domain.
DR   InterPro; IPR014145; LigD_pol_dom.
DR   InterPro; IPR033649; MtLigD_Pol-like.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   NCBIfam; TIGR02778; ligD_pol; 1.
DR   PANTHER; PTHR42705; BIFUNCTIONAL NON-HOMOLOGOUS END JOINING PROTEIN LIGD; 1.
DR   PANTHER; PTHR42705:SF2; MULTIFUNCTIONAL NON-HOMOLOGOUS END JOINING DNA REPAIR PROTEIN LIGD; 1.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF13298; LigD_N; 1.
DR   Pfam; PF21686; LigD_Prim-Pol; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:SDD08632.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199039}.
FT   DOMAIN          619..742
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          319..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          742..805
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        748..765
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   900 AA;  97465 MW;  26D61A7F808BCACB CRC64;
     MPTDSAREIV TIDGHSVTLT NLARVVYPQT GTTKAEVLAY FAAVAGPLVV HAAHRPATRK
     RWVHGTGGPV FFQKNLEDSA PAWVHRREIQ HSDHVNTYPL VDDLATLTWL GQIGALEIHV
     PQWRFGRTGA QHFPDRLVLD LDPGPGTGLA ECAEVARWAR TILTEMGMDL FPVTSGSKGI
     HLYATLDGTQ SWEAASAVAH ELARALEADH GDLVVSEMKK SLRVGKVLVD WSQNNRNKTT
     ITPYSLRGRE RPTVAAPRTW AELDDPGLAH LEADEVVSRF MHDGDLLAGL LAGGRAGLEP
     TPGRLATFEQ GADRLAVYRS RRDPGRTPEP VPSADEPAIA GGSEAPIFVI QDHHARGHHF
     DFRLERDGVL VSWALPKGEP VDPSTNHLAV QTEDHPLEYA NFSGTIPRGE YGAGTVSIWD
     AGTYEVEKWR EGEEIIVVVH SSGVGGVDRG SRRLALIHTG HGGRGRSENS WLIHRMGGRG
     VSRGGVQGLG LGGAGTRDTP AALADEPTAL PARPPEPMLA TPGTFADLER LEDSEAWAFE
     MKWDGIRALA SVTGGIVRLT SRNGIDLTAT YPELAELSGC VGEDVLLDGE IVALNRSGRP
     DFGLLQNRMN LTREAEVAAA RAEQPVDFMA FDLLHRGSRR MTTLGYDARR RALEEVLDEH
     GRVHLPPAFT SGARAAIEAS LALGLEGVVA KRRSSTYRPG RRSPAWIKVK HVQTREVVVV
     GWRTGKGSRA STLGSLLVAV PGDAVPNNLP PDNSTSHNSR PRDSQPGTII PIDIDRKAPG
     ISPPDNSPPD DPTPHISVPD DAAPSQSARL RYAGRVGTGF TDKTLTRLRC ELDLIPHDTA
     PLDDVPDADR IDAHWVVPDH VGEVSFAGWT GAGRLRHPVW LGWRPDKSPT EVTIEADESH
//
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