ID A0A0D2CUN3_9EURO Unreviewed; 1082 AA.
AC A0A0D2CUN3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=PV07_00409 {ECO:0000313|EMBL:KIW33570.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW33570.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW33570.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW33570.1,
RC ECO:0000313|Proteomes:UP000054466};
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 Cladophialophora immunda CBS83496.";
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; KN847040; KIW33570.1; -; Genomic_DNA.
DR RefSeq; XP_016253786.1; XM_016386858.1.
DR AlphaFoldDB; A0A0D2CUN3; -.
DR STRING; 569365.A0A0D2CUN3; -.
DR GeneID; 27339603; -.
DR VEuPathDB; FungiDB:PV07_00409; -.
DR HOGENOM; CLU_004844_1_1_1; -.
DR OrthoDB; 8251at2759; -.
DR Proteomes; UP000054466; 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; 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 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:UP000054466};
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 780..879
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 1019..1081
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..749
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1082 AA; 123248 MW; BF5A92279D0167CB CRC64;
MSDDESMYDE SRHEDAPSRA DFEKQLDKEY PNRPRNHGKT LPFHTLFEDL FNPLIDNRQK
KPTAAIVNRR KVGPDGHSNL SPSERRRAII ERYIARWRKE VGPDFFPAFR LIIPDKDRER
GVYGLKEKII AKLLIKIMKI DKNSEDGYSL LNWKQPGQTA ASRMAGDFAG RCYEALSKRP
MRVEVGDMTI GEVNELLDKL SGAPREENQL PILAEFYKRM NAEELMWLIR VILKQMKVGA
TEKTFFHLWH PDAESLFNVS SNLRRVCWEL YSPEVRLQDE EAGVALMQCF QPMLAQFKQE
SLNKVVEALR PTPDDPEFWI EEKLDGERIQ MHMVTDDTQP GGRRFRFWSR KAKDYTYLYG
DGFHDPNGAL TPHIKDCFAD GVENIILDGE MITWDPNEKA LVPFGTLKTA ALAEQRNPFG
QGHRPVFRIF DILLLNDQPL SRYTLRDRRK ALAASVKSLP ERFEIHEYTV ATKVEDIEDL
LRKVVAEASE GLVLKNPRSM YRLDDRSGDW QKVKPEYMDG FGEELDCLII GGFYGSGRRG
GNLSSFLCGL RASGQAVQRV TQSQSQSQSH SQRRQQKSLS QSQSQDQAAQ RQQTQSQAQA
EGGELSETKG PTENFISFFK VGGGMTANDY ATIRHATDGK WHPWDSRRPA AKDYIDLGNL
SLLKERPDMW IKPSDSLVVQ VKAAQVTISE DYGFGKTLRF PRFMRLRRDK DWKTALSVNE
FEDLQIKAEH EEKEKAMKVD QQRKEKRKGR AGGYASRKKP LTVAGYNARD VNNVKLPEGP
RGTVFEGLTF YIMTESALPG DRKKSKLELE ALVKANGGKI VQTAAPTSED QETVVCIASR
RTVKVASLEK RGEKEIVKPM WIFDCIDQAK RDFARGYAEE MVVPLEPERH LYFIPDNMRE
LFEDNVDEYG DSFARDVSEE ELKEIMTKMG IVDIEEEEGE RIPDLFGDEF LNMKGFMLHG
LVLFFDQPIP AAQKATAPLS SSNSKTTSKT AAVTATYCTQ ALAQFAGAHL LSPTYTALSS
VPSNLRSTIT HIIADPASDL GGLRRQVSRW GTRKIPRIVT REWIDICWKE GTRVDEEAYI
AR
//
