ID   F9X2V5_ZYMTI            Unreviewed;       964 AA.
AC   F9X2V5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=MYCGRDRAFT_68344 {ECO:0000313|EMBL:EGP90536.1};
OS   Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS   fungus) (Septoria tritici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP90536.1, ECO:0000313|Proteomes:UP000008062};
RN   [1] {ECO:0000313|EMBL:EGP90536.1, ECO:0000313|Proteomes:UP000008062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX   PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA   Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA   Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA   Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA   Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA   Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA   van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA   Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA   Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA   Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA   Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA   de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA   Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT   "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT   reveals dispensome structure, chromosome plasticity, and stealth
RT   pathogenesis.";
RL   PLoS Genet. 7:E1002070-E1002070(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; CM001197; EGP90536.1; -; Genomic_DNA.
DR   RefSeq; XP_003855560.1; XM_003855512.1.
DR   AlphaFoldDB; F9X2V5; -.
DR   STRING; 336722.F9X2V5; -.
DR   EnsemblFungi; Mycgr3T68344; Mycgr3P68344; Mycgr3G68344.
DR   GeneID; 13399568; -.
DR   KEGG; ztr:MYCGRDRAFT_68344; -.
DR   eggNOG; KOG0966; Eukaryota.
DR   HOGENOM; CLU_004844_1_1_1; -.
DR   InParanoid; F9X2V5; -.
DR   OMA; EGIMIKH; -.
DR   OrthoDB; 8251at2759; -.
DR   Proteomes; UP000008062; Chromosome 2.
DR   GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR   GO; GO:0032807; C:DNA ligase IV complex; IEA:EnsemblFungi.
DR   GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
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; PF16589; BRCT_2; 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; 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; 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:UP000008062};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          411..536
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          709..801
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          874..963
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          38..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   964 AA;  110023 MW;  C1CE5B7451D732CF CRC64;
     MYGHGSMTQD EMDEKYPGRP KNHAKTLPFH ELYTTLFNPL NENKKKPTGP SIARKKEGPH
     GQGQAPHEAR RSIIDRFISR WRKQVGNDIF PAIRLIVPEK DRERGMYGIK EMTLGKLLVR
     VMKINKDSED GYNLLHWKLP GVKASSAMAG DFAGRCFEVI SKRPMRQTPG DMTIAQVNEM
     LDRLSVAQKE ENQRPIIEEF YNRMCAEEMM WLIRMILRQM KVGASERTFF DVWHQDAENL
     FNISSNLRRV CWELWDPDVR LEGDSAGIAL MQCFQPQLAA FQMRSMEQMV ARMKPTEEDA
     EFWIEEKLDG ERMQLHMVED DQIPGGKRFG FWSRKAKDYT YLYGKHFEDD NSALTRHIKN
     AFNEGVRNII LDGEMITWDP KEQALVPFGT LKTAALSEQQ NPFSTGNRPV FRIFDCLFLN
     DKDLTHYTLR VRHEALLKSV TSIDQRMEIH EHQKATQASE IEPVLRKVVA EASEGLVLKN
     PRSEYRLNER NDDWIKVKPE YMTEFGESLD CIVVGGYYGS GKRGGGLSSF LCGLKPQQAI
     FSSQNRNINP QMVLSFFKVG GGFAASDYAE IRHRTEGKWT DWNAKKPPTD WVVLGGGDRQ
     FEKPDVWIKP EDSIVLSVKA ASVTGTTQFA TGCTLRFPRF KKLRTDKDWT QALTQDEFNA
     LRKRVEAEVE EKKMKIDDTR KQKVGPKRKK RELVIQGQED AVRAPYAGPA TKVFEGLSFF
     VMTEAPKPLK KTKAELEQLI KANGGNVVAS EKDPDTIIIA DRNMVKVASI SKHDKRSIIR
     PSWLLDCVRQ SEIDIGRPAL LLPLEKFHLF HTASAEQGRF DDNVDEYGDS YARDITTEEL
     LALCNAMPSK MEDGLNPDEV LEQFHDHGHE LDAMKGFMFR GTTAYFDDVP AEAIRLFKFA
     GGQIADSIED DQLTHVVLHT GCSPAATRKA VSSKQQLPRI VTESWVADSW SEATRLDEEQ
     FVPS
//