ID   D5GCR9_TUBMM            Unreviewed;       976 AA.
AC   D5GCR9;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=GSTUM_00005992001 {ECO:0000313|EMBL:CAZ82312.1};
OS   Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ82312.1, ECO:0000313|Proteomes:UP000006911};
RN   [1] {ECO:0000313|EMBL:CAZ82312.1, ECO:0000313|Proteomes:UP000006911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mel28 {ECO:0000313|EMBL:CAZ82312.1,
RC   ECO:0000313|Proteomes:UP000006911};
RX   PubMed=20348908; DOI=10.1038/nature08867;
RA   Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA   Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA   Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA   Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA   Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA   Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA   Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA   Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA   Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA   Ottonello S., Wincker P.;
RT   "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT   of symbiosis.";
RL   Nature 464:1033-1038(2010).
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         ECO:0000256|RuleBase:RU000617};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; FN430120; CAZ82312.1; -; Genomic_DNA.
DR   RefSeq; XP_002838121.1; XM_002838075.1.
DR   AlphaFoldDB; D5GCR9; -.
DR   STRING; 656061.D5GCR9; -.
DR   EnsemblFungi; CAZ82312; CAZ82312; GSTUM_00005992001.
DR   GeneID; 9187931; -.
DR   KEGG; tml:GSTUM_00005992001; -.
DR   eggNOG; KOG0967; Eukaryota.
DR   HOGENOM; CLU_005138_0_1_1; -.
DR   InParanoid; D5GCR9; -.
DR   OMA; CYATHSE; -.
DR   OrthoDB; 961at2759; -.
DR   Proteomes; UP000006911; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd07900; Adenylation_DNA_ligase_I_Euk; 1.
DR   CDD; cd07969; OBF_DNA_ligase_I; 1.
DR   Gene3D; 3.30.1490.70; -; 1.
DR   Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 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; 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   NCBIfam; TIGR00574; dnl1; 1.
DR   PANTHER; PTHR45674:SF4; DNA LIGASE 1; 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 2.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 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; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000617};
KW   DNA damage {ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006911}.
FT   DOMAIN          702..839
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          22..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..151
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..180
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..255
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   976 AA;  107077 MW;  77612ADDCA79B985 CRC64;
     MSSSKKQTTL GYVKSQTTLG RFFSLPAGTN PATPIQSKLK TISKPGKAAD TDDVASPKVR
     KTSARGQARK KPTIPEDDGS DGGAGYTKAG VSFSETEMSD ASEPAIGSSK QKALGNSSTK
     RERPAARKCG IKPSNIKKET ETSEDEAPPS KRSKSAPTTK PLKKDCDESE LSDEDIAPRK
     RLPIINSPKA TAKKRKGKVV GKAVDVNTPV SPSGTTKGAR SSPISSPVVS PQESGESEPP
     LPESPSSTPK ISKSKSGSKA KVAKKSPSDK RSKKRGAASD TEAVDKPESS ATHKALDSDS
     GTEKPSLAPA AGREMIKKLS KSVPPAYPDW VAGEPTPYAA LVTTFNLLES TTKRLEKISH
     TSRFLRQVLQ LSPDELLLVI HLMINKLAAD FEGVEMGIGE SLLMKAIGES CGRSLERIRE
     DQRECGDLGL VAMKSRNNQK TLFAPRPLTI AVVHKGLLGI AKTKGEGGQG RKVSAIRKLL
     AAAKGDEAKF LIRGLEGKLR LGLAERTVLV SLSSAMITHE QELVGKTPTT AMLDQSELNL
     RSVYSELPSY EIIIPAMREH GIMDIKKYCK LQPGVPVKPM LAKPTKAISE VLDRFENKRF
     TCEYKYDGER AQIHYVSPKS SIEYPPATLS GEPIKNLAKV FSRNSEDLSG KYPDILAAMN
     EWVRPEVESF VLDCEAVGWD ETNNRLLPFQ MLQTRKKKDV ALEDVKIRVC VHAFDLLFLN
     GKPVVRESLD DRRKLMHKTF IEVPNQFVFA RYMDSSHLEE IRLFLDQSVK DSCEGLMVKM
     MDGPESFYEP SQRSRNWLKI KKDYIDELGD SLDLVVIGAY WGRGKRTSVY GSFLLACYNP
     GTQNYESLCN IGTGFTEAEL EEFYGTLHPL EIDRAKPFYD HPSGNAGKPD VWFEPKVLWE
     VKAADLTLSP RYKAAAGLAG HPDKGVSLRF PRFIGPRTDK TGEDATSSSQ IAEMYLRQDQ
     VAHKTGAKGV DDDFEY
//