ID   G4N7T1_PYRO7            Unreviewed;       896 AA.
AC   G4N7T1;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=MGG_06370 {ECO:0000313|EMBL:EHA50885.1};
OS   Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Magnaporthe oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507 {ECO:0000313|EMBL:EHA50885.1, ECO:0000313|Proteomes:UP000009058};
RN   [1] {ECO:0000313|EMBL:EHA50885.1, ECO:0000313|Proteomes:UP000009058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958
RC   {ECO:0000313|Proteomes:UP000009058};
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M., Kulkarni R., Xu J.R., Pan H., Read N.D., Lee Y.H.,
RA   Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S., Soanes D.M.,
RA   Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M., Kim S.,
RA   Lebrun M.H., Bohnert H., Coughlan S., Butler J., Calvo S., Ma L.J.,
RA   Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=70-15;
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Dead R., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Magnaporthe oryzae 70-15.";
RL   Submitted (MAY-2011) 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         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; CM001234; EHA50885.1; -; Genomic_DNA.
DR   RefSeq; XP_003717204.1; XM_003717156.1.
DR   AlphaFoldDB; G4N7T1; -.
DR   STRING; 242507.G4N7T1; -.
DR   EnsemblFungi; MGG_06370T0; MGG_06370T0; MGG_06370.
DR   GeneID; 2684525; -.
DR   KEGG; mgr:MGG_06370; -.
DR   VEuPathDB; FungiDB:MGG_06370; -.
DR   eggNOG; KOG0967; Eukaryota.
DR   HOGENOM; CLU_005138_0_1_1; -.
DR   InParanoid; G4N7T1; -.
DR   OMA; WIKYKRD; -.
DR   OrthoDB; 961at2759; -.
DR   Proteomes; UP000009058; Chromosome 4.
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; 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:UP000009058}.
FT   DOMAIN          621..758
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          860..896
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..184
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        877..896
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   896 AA;  99144 MW;  1550C541A0D111A0 CRC64;
     MAPKQATLGK FFGKGSQPAP TQQTKLSFAT KPTPSKEKEK EEKDKDEVVS SPGTNDELAS
     DQDTKKRPRV LSATVTNKSS PKGKSDAVKN KEPDDQEPPV KKARRSRKVV EEDEDDEVMD
     DVKAEATASD QDSKPAKRQR SPWVKKEAKE DKSKLVKDEP TRTTKASKSG KAAVKEEDGD
     GSAKEVSASE SASELEDEID EEDEKPTVAA KLRKTVQKTL LQPTTKDPYP DWKPGEPVPY
     AALCTTFSLV ELTTKRLIII EHCSRFLRQV LKLTPEDLLP TVLLMINKLA ADYAGIELGI
     GESLIMKAIG ESTGRSLAII KQDQREIGDL GLVAVKSRST QPTMFKPKPL TVRGVFAGLT
     NIATITGNGA QGRKVDIIKK LLSAADVNNA GKVDISKDKG GPSEAKFIVR FLEGKLRLGL
     AERTVLPSLA QAVIAHESSK KGTIPSTSDV EKAEQMLKTV YSELPSYEVI IPALLEHGIM
     NLKDNCKLRP GIPLKPMLAK PTKAITEVLD RFENQTFTCE YKYDGERAQI HYVAKEANEE
     LSTALPGATK AVGSGLAAIF SRNSEDLSQK YPDILAKLDS WVKPETKSFV LDCETVAWDV
     QEKKVLPFQQ LMTRKKKDVK IEDVKVKVCV FAFDLLYLNG EAVVEKSLRE RRTLLESSFK
     PIEGEFAYAT HMNGQELDEI QTFLDESVKA SCEGLMVKML DGTESGYEPS KRSRNWLKIK
     KDYLSGIGDS LDLVVLGAYY GKGKRTSVYG AFLLACYNPS SDKYETVCNI GTGFSEAVLE
     ELHTQLKDTV IDRPKPFYSH SSGGQHQPDV WFEPRFVWEV KTADLTLSPR YKAGCGEGVD
     PSGTKGISLR FPRFIKLRDD KKPDEATSSR QVAEMYRKQE SVSKNKGPAV DDDFEY
//