ID   G2RBC7_THETT            Unreviewed;      1040 AA.
AC   G2RBC7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=THITE_2080045 {ECO:0000313|EMBL:AEO69098.1};
OS   Thermothielavioides terrestris (strain ATCC 38088 / NRRL 8126) (Thielavia
OS   terrestris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides;
OC   Thermothielavioides terrestris.
OX   NCBI_TaxID=578455 {ECO:0000313|EMBL:AEO69098.1, ECO:0000313|Proteomes:UP000008181};
RN   [1] {ECO:0000313|EMBL:AEO69098.1, ECO:0000313|Proteomes:UP000008181}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38088 / NRRL 8126 {ECO:0000313|Proteomes:UP000008181};
RX   PubMed=21964414; DOI=10.1038/nbt.1976;
RA   Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I.,
RA   Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M.,
RA   Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P.,
RA   Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P.,
RA   Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J.,
RA   Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S.,
RA   Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W.,
RA   Tsang A.;
RT   "Comparative genomic analysis of the thermophilic biomass-degrading fungi
RT   Myceliophthora thermophila and Thielavia terrestris.";
RL   Nat. Biotechnol. 29:922-927(2011).
CC   -!- FUNCTION: DNA ligase involved in DNA non-homologous end joining (NHEJ);
CC       required for double-strand break (DSB) repair.
CC       {ECO:0000256|ARBA:ARBA00043870}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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; CP003012; AEO69098.1; -; Genomic_DNA.
DR   RefSeq; XP_003655434.1; XM_003655386.1.
DR   AlphaFoldDB; G2RBC7; -.
DR   STRING; 578455.G2RBC7; -.
DR   GeneID; 11520347; -.
DR   KEGG; ttt:THITE_2080045; -.
DR   eggNOG; KOG0966; Eukaryota.
DR   HOGENOM; CLU_004844_1_1_1; -.
DR   OrthoDB; 8251at2759; -.
DR   Proteomes; UP000008181; Chromosome 4.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd07903; Adenylation_DNA_ligase_IV; 1.
DR   CDD; cd17722; BRCT_DNA_ligase_IV_rpt1; 1.
DR   CDD; cd07968; OBF_DNA_ligase_IV; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 2.
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; IPR044125; Adenylation_DNA_ligase_IV.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
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; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   NCBIfam; TIGR00574; dnl1; 1.
DR   PANTHER; PTHR45997; DNA LIGASE 4; 1.
DR   PANTHER; PTHR45997:SF1; DNA LIGASE 4; 1.
DR   Pfam; PF00533; BRCT; 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   SMART; SM00292; BRCT; 2.
DR   SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
DR   SUPFAM; SSF52113; BRCT domain; 2.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50172; BRCT; 2.
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|ARBA:ARBA00023172,
KW   ECO:0000256|RuleBase:RU000617}; DNA repair {ECO:0000256|RuleBase:RU000617};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000617}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008181};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          464..587
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          770..853
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          934..1039
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          73..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          720..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1040 AA;  116374 MW;  F35809FF60A6B6F0 CRC64;
     MSSRTKRAKS PDVDAIEEDE KQYGSGPLTL EELDEQFPNR PRNHSKTPPF SDLFQSLFNP
     LIDCKPSTAG AASAPARARA RARAGPSFSS SSSSTKLSYH EQRRHIIERF MARWRADVGP
     DFYPAMRLIL PDKDRDRGVY GLKENTIGKL LVKVMKIDRN SEDGYALMHW KLPGHAGGGG
     GRFGGGAGGG GGGGSRGSAG DFAGRCFEIV SKRQMRTEPG NFTIGEVNVM LDRLAGASGE
     AEQLPIFEEF YQGMNAEELM WLVRIILKDM KVGATERTFL GLWHPDAEAL FSVSSSLRRV
     CWELYDPEFR LEQQETGVTL MSCFQPQLAQ FQMTTTFAKL VANLGVTEEN PEFWIEEKLD
     GERMQMHMQE DDSVPGGYRF AFWSRKAKDY TYLYGSGLED DNSALTRHLK NAFHSGVRNL
     ILDGEMITWD PEVDKIVPFG TLKTAALEQQ KNPFQNGPRP LYRVFDILLL NDKSLTEYTL
     ADRHRALERA VKGEPRRLEI HPYETATSAD AIEPLLRKVV AEASEGLVLK NPRSRYQLNS
     RNNDWIKVKP EYMSEFGESL DCVVIGGYYG SGRRGGTLSS FLCGVRVSEN FVKSGAAASR
     EKCLSFCKVG GGFKAEDYGE IRHHTEGKWR DWDAANPPSE FIELGGGERL QYERPDVWIR
     PSESVVLSVK AASFAPSDQF ATGWTLRFPR FRKLRLDKAW DAAMDVDECE ALRTKVKQEE
     KERKAMEMES RKRRPTKRQK RELVIAGAAD PAATAATATA TAEFLDVKTP RSELFRGLDF
     CVLSEMLRPR KMTKPELEKL LKENGGRIHQ TVDKGSGMIL LADKNVVKVA SLKKAGDADI
     VRPKWVLDCL EQGGGEGYLL PFEEGHLLFA TEEMRRVAEE NTDQYGDSYA RDVGIDELRA
     ILDAMDMPDG GGAEFDVSQF LDQLEEHGNG LEDLKSFMFR RCRMYFALGD GVPETTALRL
     GNYVKFGSGE VADGVEDEKI THVVVVGGEQ DTAASEKVLA ADVRYRVSSR RAVPRIVSSR
     WVEDCWKEGT LVDEEAYAPN
//