ID   B0CPS5_LACBS            Unreviewed;       816 AA.
AC   B0CPS5;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=LACBIDRAFT_187450 {ECO:0000313|EMBL:EDR14981.1};
OS   Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS   (Laccaria laccata var. bicolor).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX   NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN   [1] {ECO:0000313|EMBL:EDR14981.1, ECO:0000313|Proteomes:UP000001194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX   PubMed=18322534; DOI=10.1038/nature06556;
RA   Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA   Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA   Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA   Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA   DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA   Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA   Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA   Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA   Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA   Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA   Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA   Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA   Tuskan G., Grigoriev I.V.;
RT   "The genome of Laccaria bicolor provides insights into mycorrhizal
RT   symbiosis.";
RL   Nature 452:88-92(2008).
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; DS547091; EDR14981.1; -; Genomic_DNA.
DR   RefSeq; XP_001873189.1; XM_001873154.1.
DR   AlphaFoldDB; B0CPS5; -.
DR   STRING; 486041.B0CPS5; -.
DR   GeneID; 6068938; -.
DR   KEGG; lbc:LACBIDRAFT_187450; -.
DR   HOGENOM; CLU_005138_0_1_1; -.
DR   InParanoid; B0CPS5; -.
DR   OrthoDB; 961at2759; -.
DR   Proteomes; UP000001194; 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; 1.
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:UP000001194}.
FT   DOMAIN          545..682
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          797..816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..155
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   816 AA;  90576 MW;  11389A672A9FBFF2 CRC64;
     MGRQQTLAKF FDMPKSVKTP PPQQASLKEM WGKRPIVTKT EEEDEKQDAM DIEPGNNSKA
     GSSKRTGALT RPGRSPKLKK RKIVQSNDEQ EEQPKRSTTA VVVESGKPTS DDPATFSSQS
     LKRKQKESVD AVEDMDAAAS AGEGEEEVEN DDSDMEVDDG VVSVSAQAAL RRKGEVDVKG
     GWKVGEPVLY AALTKAFSLI EATTKRLEKT AILTSFLLLV IQRSAKADHN SLLQAVYLCI
     NRLSPDYVGV ELGIGESLLI KAIAESTGRS LSLIKADLKR EGDLGLVAMN SKNSQKTLFK
     PKPLTLPFVF SNLRDIALTT GNSSQAKKVS VITKLLAACQ DFEAKYIVRS LEGKLRIGNA
     ERSVLVALAQ AVVLAEKEKV GKKWSQEKLT ARLEEGANII KAVYSELPSY DKVIPALLEV
     GIDGLRDKCK LTPGVPLKPM LAKPTKAIGE VLDRFENKRF TCEYKYDGER AQVHKLEDGT
     VDVFSRNSED MSKKYPDLVD QLPRCIKEST KSFVLDAEAV AIDRLTGKLM PFQELSRRKR
     KDVKVEDIQV QVCLFAFDLL YLNGEPLLQR PLYERRELLR QYFTPVPGEF DFAKSSDSET
     TEEIQTFLEE SVKDGCEGLM VKMLDSDASY YEPSRRSVNW LKLKKDYLAG VGDSLDLVVV
     GGYYGKGKRT NVYGAFLLAC YDSESEEYQT ICKIGTGFSE ENLQAHYDAL KPLETTKVRG
     DIKVGGAKPD IWFEPKIVWE VLTADLSLSP IYTAAQGLVE DRGISLRFPR FIRVRDDKGP
     DDATGPEQIA EMYERQALAQ SNGKKKKGGD ADDGFW
//