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Database: UniProt
Entry: A0A177QH59_9PLAN
LinkDB: A0A177QH59_9PLAN
Original site: A0A177QH59_9PLAN 
ID   A0A177QH59_9PLAN        Unreviewed;       892 AA.
AC   A0A177QH59;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
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   ORFNames=AYO44_10160 {ECO:0000313|EMBL:OAI47131.1};
OS   Planctomycetaceae bacterium SCGC AG-212-F19.
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae.
OX   NCBI_TaxID=1799658 {ECO:0000313|EMBL:OAI47131.1, ECO:0000313|Proteomes:UP000186541};
RN   [1] {ECO:0000313|Proteomes:UP000186541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCGC AG-212-F19 {ECO:0000313|Proteomes:UP000186541};
RA   Choi J., Stepanauskas R., Howe A.;
RL   Submitted (FEB-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};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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:OAI47131.1}.
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DR   EMBL; LSTD01000270; OAI47131.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A177QH59; -.
DR   Proteomes; UP000186541; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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: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; cd07971; OBF_DNA_ligase_LigD; 1.
DR   CDD; cd04862; PaeLigD_Pol_like; 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; IPR014146; LigD_ligase_dom.
DR   InterPro; IPR014144; LigD_PE_domain.
DR   InterPro; IPR014145; LigD_pol_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014143; NHEJ_ligase_prk.
DR   InterPro; IPR033651; PaeLigD_Pol-like.
DR   NCBIfam; TIGR02777; LigD_PE_dom; 1.
DR   NCBIfam; TIGR02778; ligD_pol; 1.
DR   NCBIfam; TIGR02779; NHEJ_ligase_lig; 1.
DR   NCBIfam; TIGR02776; NHEJ_ligase_prk; 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; 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};
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:UP000186541};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          330..423
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          194..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..565
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   892 AA;  99200 MW;  B95932ED5B362241 CRC64;
     MSLTEYQCKR HFKRTPEPAG KRAAKPGHLF VVQKHQARQL HYDFRLELDG VLKSWAVPKG
     PSLDPSVKRL AVQVEDHPVE YGSFEGIIPP GEYGGGTVML WDQGEWEPVG DPEDGYRAGR
     LKFKLHGAKL RGGWMLVHTG GGASGRDKRQ WLLIKERDEE ATPSKDGDIL EHMPLSVATG
     RSLEEIAADR HRVWTSKAKS PMQSARQTPR KKSATERSQR TSVAAAIPGR KTRSLPSRVA
     VQLATLAAEA PEGDEWLHEI KLDGYRMICR IANGRVAFMS RNHQDWTARF PALVAAAQRL
     PIRQAIFDGE VVAVRPDGST NFQDLQNAFR DVRTDQLYYF VFDILHLDGH DLAGLPLAER
     KRLLAKLLGE TGVPPTIRLS EHIEGNGPAF FKKVCAMGLE GIISKRRDQP YRPGRGYDWL
     KVKCMQTGEF VIGGFTEPTG GRAKFGALLL GYYNAKGELV YAGKVGTGFD NRTLHSLFAR
     LKPLEQDESP FSNLPRGGPK THWVEPRLVA QVTFGGWTRD GLLRHPSFQG LREDKPAAEV
     TRDLAIPVSS AMRRQRSSKS PPQGVNGRNG RDRRMKKSGP NGAANGETGY DANEQRLAGV
     RLTSPDKILY PEQRITKLEL AQYYQAIAEW MLPHIADRPL VLVRCPEGRG KACFYQKHPS
     PGTPDTLRRI PVREKAKTED YVIVDDVAGL ISLAQIGALE IHAWGARADN LEQPDRLIFD
     LDPDPSVSWS RVVDSAGAVR DFLQELGLTS FVKTTGGKGL HLVVPILRRQ DWEEVKAFCK
     RVADAIVAAD AARYTANMSK AARPGKIFID YLRNARGATA VVPYSPRARP GAPVSVPLTW
     KELSPRIGPA QFTIRNIMDR LRSLKRDPWE EIASVRQGLA GPIKKLQTVF TS
//
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