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Database: UniProt
Entry: A0A0D1ZLN9_9EURO
LinkDB: A0A0D1ZLN9_9EURO
Original site: A0A0D1ZLN9_9EURO 
ID   A0A0D1ZLN9_9EURO        Unreviewed;      1029 AA.
AC   A0A0D1ZLN9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=PV11_03254 {ECO:0000313|EMBL:KIV87728.1};
OS   Exophiala sideris.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV87728.1, ECO:0000313|Proteomes:UP000053599};
RN   [1] {ECO:0000313|EMBL:KIV87728.1, ECO:0000313|Proteomes:UP000053599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV87728.1,
RC   ECO:0000313|Proteomes:UP000053599};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala sideris CBS121828.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN846951; KIV87728.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D1ZLN9; -.
DR   STRING; 1016849.A0A0D1ZLN9; -.
DR   HOGENOM; CLU_004844_1_1_1; -.
DR   OrthoDB; 8251at2759; -.
DR   Proteomes; UP000053599; 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; IPR021536; DNA_ligase_IV_dom.
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   Pfam; PF11411; DNA_ligase_IV; 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; 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:UP000053599};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          427..552
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          737..820
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          956..1028
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1029 AA;  117405 MW;  D4C407DCD3345F5C CRC64;
     MSDDERMDVD SGDGGQPSRA DIERQLNEEY PNRPHNKHRA LPFHTLIRDL FNPLLDNRTK
     KAGGAVINRR KVGPNGGSSA SPSELRRAII ERYIARWRRD VGQDFFPAFR LIIPDKDRER
     GVYGLKEKIL GKLLVRVMKI DKNSEDGFNL LNWKIPGGGN NASRSAGDFA LRCHEIISKR
     PMRTEYGDMD IDQVNELLDQ LSAAPREEHQ LPILAEFYKR MNADELQWVI RIILRTMKVG
     ATEKTFFHIW HPDAESLFNI SSNLRRVCWE LWDPAKRLDS DETGVALMQC FQPQLAQFSQ
     EPLKRVVQKV QSPEDNEFWI EEKLDGERMQ LHMVSDNNTV GGRRFQFWSR KGKDYTYLYG
     NGLYADNAAL TPFIKDCFPD KVENIILDGE MITWDPKERA TVAFGTLKSA ALAEQRNPYA
     EGQRPLFRVF DILLVNDRPL TRHTLDDRRR ALVASVNSEP ERLEIHGYQI ATTVEEVEES
     LREVIAQASE GLVLKNPRSA YKLDDRNGDW QKVKPEYMMD GGESLDCLII GGFYGSGKRG
     GNISSFMCGL RLAPTGQSQS QRQSQSQSQA TEPFRKFVSF FKVGGGFNAN DYATIRHETE
     GKWHDWNAKR PPTQYIELGG GPQGQREKPD VWIKPEDSLV IEVKAAQVTA SEDYGCGMTL
     RFPRFRKLRR DRDWQTALSL EEFLDLRNVI EDRQKEKAMN VDEQKKKRRQ PNTRKKVITV
     AGYNAKEINN AALPTGPKGN VFEGLTFYIM TESIPPTEKK SKLELEALVK ANGGKIVQTH
     TTDEHTMCIA ARRTVKVASL EKTGKKEIVK PAWIFDCIQQ AHQDFAHGLP EMVLPLEPAR
     HLFFVPHDME DRWTEDVDEY GDSFARDTNV EELRETMDKM ANIDAQDDEE SSIPELFPDY
     MDMQGYMFHG LVFLFDLSAA SKQDDPSGAN GDLEGAADDL NDSTDLMTRN IALFAGAELL
     PDSDLSAITA KEKHRVTHIV AQPHSDLQSL RRDISRWKAR RIPRIMSANW IQECWKAGTK
     VDEEAYVAR
//
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