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Database: UniProt/TrEMBL
Entry: A0JRM5_ARTS2
LinkDB: A0JRM5_ARTS2
Original site: A0JRM5_ARTS2 
ID   A0JRM5_ARTS2            Unreviewed;       845 AA.
AC   A0JRM5;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   24-JAN-2024, entry version 97.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
DE   AltName: Full=NHEJ DNA polymerase {ECO:0000256|ARBA:ARBA00029943};
GN   OrderedLocusNames=Arth_0294 {ECO:0000313|EMBL:ABK01695.1};
OS   Arthrobacter sp. (strain FB24).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=290399 {ECO:0000313|EMBL:ABK01695.1, ECO:0000313|Proteomes:UP000000754};
RN   [1] {ECO:0000313|Proteomes:UP000000754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB24 {ECO:0000313|Proteomes:UP000000754};
RX   PubMed=24501649; DOI=10.4056/sigs.4438185;
RA   Nakatsu C.H., Barabote R., Thompson S., Bruce D., Detter C., Brettin T.,
RA   Han C., Beasley F., Chen W., Konopka A., Xie G.;
RT   "Complete genome sequence of Arthrobacter sp. strain FB24.";
RL   Stand. Genomic Sci. 9:106-116(2013).
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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DR   EMBL; CP000454; ABK01695.1; -; Genomic_DNA.
DR   RefSeq; WP_011690165.1; NC_008541.1.
DR   AlphaFoldDB; A0JRM5; -.
DR   STRING; 290399.Arth_0294; -.
DR   KEGG; art:Arth_0294; -.
DR   eggNOG; COG1793; Bacteria.
DR   eggNOG; COG3285; Bacteria.
DR   HOGENOM; CLU_008325_2_1_11; -.
DR   OMA; QWLAHRM; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000000754; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
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   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; IPR014146; LigD_ligase_dom.
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; TIGR02777; LigD_PE_dom; 1.
DR   NCBIfam; TIGR02778; ligD_pol; 1.
DR   NCBIfam; TIGR02779; NHEJ_ligase_lig; 1.
DR   PANTHER; PTHR42705; BIFUNCTIONAL NON-HOMOLOGOUS END JOINING PROTEIN LIGD; 1.
DR   PANTHER; PTHR42705:SF2; BIFUNCTIONAL NON-HOMOLOGOUS END JOINING 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   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ABK01695.1};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000754};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          630..754
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          287..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          497..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..345
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   845 AA;  92365 MW;  5FE4487128634C0A CRC64;
     MAGSRERVRI QGRELVVTNL DKVMYPETGT TKADVLAYYT AVAPVLVPAA VNRPATRKRW
     VNGVGTAEAP GEMFFQKNLE DSTPGWIPRA SIRHKERTNQ YPLVNDAATL IWLAQMGSLE
     IHVPQWRVDP HGNPMNPDRL VLDLDPGEGA GLAECAEVAR LARAILRDVG LDPIPVTSGS
     KGVHLYAGLD GTQSSDQISE FAHELARALE SDHPDLAVSD MKKTLRTGKV LVDWSQNNAA
     KTTIVPYSLR GRLRPTVAAP RTWRELASPK LKQLDYREVM RRVKDGKDPF APVSAGGSHV
     RGHPGGGGSA AGPRDSTTAD GGSTDPRLEK YRSMRDPEGT PEPFSADRHG ADPNAGTIRE
     RFVIQEHHAS RLHYDFRLER DGVLVSWALP KGVPTSGTQN HLAVQTEDHP MDYLDFEGTI
     PKGQYGAGNV TIWDHGYYEC DKWIAGKEVI ATLTGADGGG LGGTRKFALI RTSRDSDTSK
     SPEQAQWLIH LMDRKGHAPA ATGTPPATGG PAEAAKQDEP PPDLSPAPDF LPMMASAGTP
     ADLRGLDWQF ELKWDGIRAL IIGDADRIRL ISRNGNDMTA SYPELTDRSC WPEQSFTADG
     EIVAVGPSGR PDFGLLQTRM KLTKAADVAK ARAATPVRLM VFDLLSDAGE DLRRMPLRRR
     RARLEQLDWP DGCPVHLSEV LDHEVEHILE SARELGLEGI MAKRLDGRYV SGERSRSWLK
     LKFERTQEVV VGGWRPGKGS RQGSVGSLLV GIPDGAKLRY VGRVGSGFSD RELKELRLQV
     DTLSRKTSPF TEVPAADASD AHWVAPGLVG EVTFGEWTGG GKLRHPVWRG WRLDKNADDV
     VAESG
//
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