ID A0A397HT27_9EURO Unreviewed; 1006 AA.
AC A0A397HT27;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN Name=LIG4 {ECO:0000313|EMBL:RHZ64726.1};
GN ORFNames=CDV56_109109 {ECO:0000313|EMBL:RHZ64726.1};
OS Aspergillus thermomutatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ64726.1, ECO:0000313|Proteomes:UP000215305};
RN [1] {ECO:0000313|EMBL:RHZ64726.1, ECO:0000313|Proteomes:UP000215305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ64726.1,
RC ECO:0000313|Proteomes:UP000215305};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT aspirate.";
RL Submitted (AUG-2018) 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}.
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:RHZ64726.1}.
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DR EMBL; NKHU02000021; RHZ64726.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397HT27; -.
DR STRING; 41047.A0A397HT27; -.
DR VEuPathDB; FungiDB:CDV56_109109; -.
DR OrthoDB; 8251at2759; -.
DR Proteomes; UP000215305; 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; 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:UP000215305};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 418..552
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 721..806
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 937..1004
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1006 AA; 114874 MW; E1AC11CACEC2230E CRC64;
MDSDEINPDE EHPNVPAGDE ESDIDEKYPN RPRNHSPTLP FHELFQTLFN PLSEIKKKPA
GAVAARRKVG PHGQSAANLN PLERRRDVIE RFISRWRKEV GDDIYPAFRL ILPDKDRDRA
MYGIKEKVIG KMLVKIMKID KNSEDGFNLL NWKLPGQAAA SRMAGDFAGR CYDVISKRPM
RTDVGDMLIE EVNEKLDKLS AASKEEQQLP ILAEFYRRMN PEELMWLIRI ILRQMKVGAT
ERTFFDVWHP DAENLYSISS SLRRVCWELY DPNIRLDAED RGISLMQCFQ PQLAQFQMHS
LDRMVGRMRP TEEDPVFWIE EKLDGERMQL HMESDDSVPG GRRFRFWSRK AKEYTYLYGN
GIYDENGSLT RHLKDAFADG VQSLILDGEM ITWDPEQDAP APFGTLKTAA LSEQRNPFST
TGARPLLRVF DILYLNGRDL TGYTLRDRRN ALQKAVRPVH RRFEIHPYEE ATTKDEVEAA
LRKVVAEASE GLVLKNPRSP YRLNERHDDW MKVKPEYMTE FGESLDLIVI GGYYGSGRRG
GNLSSFLCGL RVDDAHASQG ASASKCYSFC KVGGGFNAAD YANIRHHTDG KWMEWNPKKP
PTAYIELAGR EAQYERPDMW IKPEDSVVIC VKAASVSASD QFRIGLTLRF PRFKRLRMDK
DWKSALSVQE FLDLKSNVEQ EHREKELSVD NSRRKRVKRT TKKPLTVAGY DIDEYVKYAG
PSGHIFDGLN FYILTDSNAP VKKTKPELEQ LVKANGGMFF QTNNAAPHTI CVADRRTVKA
ASLQKSGDVD IIRPSWILDC VKQNEIDAGL PDLLLPFEPR HMFFATPGKQ EEVTANVDQF
GDSYARNTTS EELSAVLKQM TKHHFKISQC PEAATKLIER IQERVNSGHE MPCGWLFKSL
TILFPHKNGD ASESESVTPS DAHCRLRFAI NTARFAGANI AKSSSHPSIT HVVVDPDSSA
AEISSLRGWW SRKSGKKVPH IVTVDWVEES WKHRTLLDEE RFQPKR
//
