ID M2Z8X8_PSEFD Unreviewed; 967 AA.
AC M2Z8X8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=MYCFIDRAFT_132548 {ECO:0000313|EMBL:EME86230.1};
OS Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS fungus) (Mycosphaerella fijiensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=383855 {ECO:0000313|EMBL:EME86230.1, ECO:0000313|Proteomes:UP000016932};
RN [1] {ECO:0000313|EMBL:EME86230.1, ECO:0000313|Proteomes:UP000016932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIRAD86 {ECO:0000313|EMBL:EME86230.1,
RC ECO:0000313|Proteomes:UP000016932};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
CC -!- FUNCTION: Involved in ds DNA break repair. Has a role in non-homologous
CC integration (NHI) pathways where it is required in the final step of
CC non-homologous end-joining. {ECO:0000256|ARBA:ARBA00002476}.
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; KB446556; EME86230.1; -; Genomic_DNA.
DR RefSeq; XP_007923579.1; XM_007925388.1.
DR AlphaFoldDB; M2Z8X8; -.
DR STRING; 383855.M2Z8X8; -.
DR GeneID; 19330817; -.
DR KEGG; pfj:MYCFIDRAFT_132548; -.
DR eggNOG; KOG0966; Eukaryota.
DR HOGENOM; CLU_004844_1_1_1; -.
DR OrthoDB; 8251at2759; -.
DR Proteomes; UP000016932; 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; 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 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 DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW 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:UP000016932};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 414..537
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 710..802
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 875..966
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 967 AA; 110840 MW; 97A2ED11E153AB37 CRC64;
MYGRGTMTEQ ELDEKYPNRP HNHSRTLPFR DLFFTLFNPL NDNRKKPSGP AIARKKLGSY
GGPSQAPNEV RRQIIDRFIS RWRKEVGDDI YPAMRLIVPE KDRDRGMYGL KEMTIAKLLV
KILKIDKNSD DGRNLTHWKQ PGLNSTSAMA GDFAGRCFEV ISKRPMRTTP GDMTIAEVNE
RLDRLAVAQK EENQLPILEQ FYSRMNAEEM MWLVRMILRQ MKVGATEKTF FEIWHPDAET
LFNISSSLRR VCWELYDPAV RLEGESRGIC LMQCFQPQLA AFQMRSTEHM VAKMGTTDED
PVFWIEEKLD GERMQMHVME DDDHPGGVRF GFWSRKAKDY TYLYGSGFED DHSALTRHIK
DAFASGVRNI ILDGEMITWD IQLDAIVTFG TLKTAAIEQQ QNPFADGNRP LYRVFDCLYL
NDKDLTRYTL RDRRNALQCS IKNVRRRIEI HEYQEEKTAS KVDETLRRVV AEASEGLVLK
NPRSLYHLNA RNDDWIKVKP EYMTEFGESL DCIVVGGYYG SGKRGGGLSS FLCGLYVPSQ
KKEIQPDINP QKTLSFFKVG GGFSASDYAQ IKHMTEGKWN DWDRKKPPFD WVELGGGMVK
QYERPDVWIK PEDSFVVSVK AASVGASDQF ACGFTLRFPR FKKLRTDKSW QQALSHDDFI
ELKTKAQNEK EEKKMKMDES RRGRKTKKRK KEIVIQGQEE GDLKTPYAGP VTKVFEGLSF
FIMTEAPKPI KKSKAELEQL VKANGGQIVA SHKDPKTILV ADRNVVKVAS VKKSDNRNIV
KPSWLLDCIK QSELDVGRPT LLLPLEPHHL EYTQSADQGK FDDNVDEYGD SYARDVTPSS
LLALCNKMPA KVEDGYEPLE ILEQLNEQNN ELDALAGFMF RGTKAYIEPS IPRESIRLYE
FAGGDLAKTL KDEDITQVVV QQGSQSLADI RKAVSSRSKL PRIVTEDWVK ESWIEETRLD
EERFAPV
//