ID A0A2W1FMW5_9PLEO Unreviewed; 988 AA.
AC A0A2W1FMW5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=Ptr86124_004722 {ECO:0000313|EMBL:KAI1516185.1}, PtrM4_05340
GN {ECO:0000313|EMBL:PWO14708.1}, PtrM4_084240
GN {ECO:0000313|EMBL:KAF7573519.1};
OS Pyrenophora tritici-repentis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=45151 {ECO:0000313|EMBL:KAF7573519.1, ECO:0000313|Proteomes:UP000245464};
RN [1] {ECO:0000313|EMBL:KAF7573519.1, ECO:0000313|Proteomes:UP000245464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M4 {ECO:0000313|EMBL:KAF7573519.1,
RC ECO:0000313|Proteomes:UP000245464};
RX PubMed=29685100; DOI=10.1186/s12864-018-4680-3;
RA Moolhuijzen P., See P.T., Hane J.K., Shi G., Liu Z., Oliver R.P.,
RA Moffat C.S.;
RT "Comparative genomics of the wheat fungal pathogen Pyrenophora tritici-
RT repentis reveals chromosomal variations and genome plasticity.";
RL BMC Genomics 19:279-279(2018).
RN [2] {ECO:0000313|EMBL:KAI1516185.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=86-124 {ECO:0000313|EMBL:KAI1516185.1};
RA Moolhuijzen P.M., Moffat C.S.;
RL Submitted (MAY-2021) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAI1516185.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=86-124 {ECO:0000313|EMBL:KAI1516185.1};
RA Moolhuijzen P., See P.T., Shi G., Powell H.R., Cockram J., Jorgensen L.N.,
RA Benslimane H., Strelkov S.E., Turner J., Liu Z., Moffat C.S.;
RT "A global pangenome for the wheat fungal pathogen Pyrenophora tritici-
RT repentis and prediction of effector protein structural homology.";
RL bioRxiv 0:0-0(2022).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF7573519.1}.
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DR EMBL; NQIK02000003; KAF7573519.1; -; Genomic_DNA.
DR EMBL; NRDI02000005; KAI1516185.1; -; Genomic_DNA.
DR EMBL; NQIK01000003; PWO14708.1; -; Genomic_DNA.
DR OMA; EGIMIKH; -.
DR Proteomes; UP000245464; Unassembled WGS sequence.
DR Proteomes; UP000249757; Unassembled WGS sequence.
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; 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; 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; PS50160; DNA_LIGASE_A3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000617};
KW Coiled coil {ECO:0000256|SAM:Coils};
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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 432..557
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 727..811
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 894..987
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT COILED 674..701
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 988 AA; 113313 MW; 5A4BA369A6F76F27 CRC64;
MAEDTPMPDA DAIKENTLMY GHDDDLDDKY PTRPINLHKT LPFHTLFTDL FNPLMETQKK
KQSVGARRRV GPHGHANMSP HEAKRNIIER FIANWRKQVG NDFYPAMRLI IPEKDRDRPM
YGLKEKAIAK VLIKLTRIGK DSDDAKHMLN WKLPGQLNKA SASTAGDFAG RCYEILSTRQ
LKTVYSDMTI AEVNNALDKL SQVGAEDEQV KIFQRFYRRM NAEEMTWLIR MILRQMKIGA
TEKTFLDIWH PDAETLFNIS SNLRRVCWEL FDTKLRLEGE DTGLSLMQCF QPQLAQFQDK
VGSFEKLVTR FKGDENDDTF WIEEKLDGER MQLHMMEDPD APGGKSFGFW SRKAKDYAYL
YGRHFDGDEA GALTRFITDA FGENVRNIIL DGEMITWDME TDHIVGFGTL KTAALSEKEN
KTNKNTGQRP LFRVFDCVYL NDKLLTQYTL RDRRRALESA VKGVPRRLEV HPYIEARSHT
EIEPALRKVI AESSEGLVLK NPRSMYCLSQ RNNDWMKVKP EYMSEFGESL DCVVVGGYFG
SGHRGGVHSS FLCALLTDKD AKPGDPKYEH CWSFFKVGGG FSREDYAAIR GRTEGKWHNW
DRRRPPLFIE LGGHEQNRQH ERPDQWIRPS ESVVLECKAA SVESSDKFRS TLTLRFPRFK
LLRVDKRWDQ ALSVQEFLDV KSRAEKEKSE KEKEFKIEQS RRKKARTAKK PLTVVSDDAI
KTPYAGPASK VFEGLAFYIM TEQVYPTKKS KADLEALVKA NGGRLVQRDS TAKDLVIVAD
KRLIKVASLE KRGTNNVVKP AWLQDCIMQN ERDAGAPPYL LPFEPNRHMY YLHDDDQMDY
EANLDDNGDS YARDIADMEE MRSLLDGMET PKTTFSRDGF LEQLEGHGED FSQFKTYMFR
NVKVKFSAEV GLELRAKLAK NYVRFGGGQI VGDGDEEDVT HVVVADGQTS AAKGKAKVSG
LARVVGLGWI EKCWEEGTRV DEERFQWG
//
