ID A1CBF1_ASPCL Unreviewed; 1029 AA.
AC A1CBF1;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 99.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=ACLA_015070 {ECO:0000313|EMBL:EAW13069.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW13069.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW13069.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027049; EAW13069.1; -; Genomic_DNA.
DR RefSeq; XP_001274495.1; XM_001274494.1.
DR AlphaFoldDB; A1CBF1; -.
DR STRING; 344612.A1CBF1; -.
DR EnsemblFungi; EAW13069; EAW13069; ACLA_015070.
DR GeneID; 4706930; -.
DR KEGG; act:ACLA_015070; -.
DR VEuPathDB; FungiDB:ACLA_015070; -.
DR eggNOG; KOG0966; Eukaryota.
DR HOGENOM; CLU_004844_1_1_1; -.
DR OMA; EGIMIKH; -.
DR OrthoDB; 8251at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0032807; C:DNA ligase IV complex; IEA:EnsemblFungi.
DR GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
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; 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:UP000006701};
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 915..1024
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 1..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1029 AA; 117611 MW; 12350CBF4A8E68BA CRC64;
MNSDDIGPDE GHPRAPVENE ESDLDEKYPN RPRNHSSTLP FHELFQTLFN PLSEIKKKPA
GAVAARRKVG PHGQSAANLN PLERRRDVIE RFISRWRKEV GDDIYPAFRL ILPDKDRDRA
MYGIKEKAIG KMLVKIMKID KNSEDGFNLL NWKLPGQAAA TRMAGDFAGR CYDVLSKRPM
RTDVGDMSIE EVNEKLDNLS AASKEEQQLP ILAEFYRRMN PEELMWLIRI ILRQMKVGAT
ERTFFDVWHP DAENLYSISS SLRRVCWELH DPNIRLDAED RGISLMQCFQ PQLAQFQMQS
LDKMVSRMRP TEDDPVFWIE EKLDGERMQL HMESDDSVPG GRRFRFWSRK AKEYTYLYGN
GIYDENGSLT RHLKDAFADG VDSLILDGEM ITWDPEQDAP APFGTLKTAA LAEQRNPFST
TGARPLFRVF DILYLNGRDL TGYTLRDRRN ALQKSVRPVH RRFEIHPYEE ATTKDEVEVA
LRKVVAEASE GLVLKNPRSP YRLNERHDDW MKVKPEYMTE FGESLDLIVI GGYFGSGRRG
GNLSSFLCGL RADDTHASQG SNASKCYSFC KVGGGFNAAD YANIRHHTDG KWVEWNPKKP
PTAYIELAGK DAQYERPDMW IKPEDSVVVC VKAASVSVSD QFRIGLTLRF PRFKRLRMDK
DWRSALSVQG FLDLKSNVEQ EHREKEFSVD NFRRKRIKRT TKKPLAVAGY DADEEAKYAG
PSGHIFEGLN FYILTDANAP VKKSKQELEQ LVKANGGKFY QTNNAAPHTV CIADRRTVKA
ASLQKSGNVD IIRPSWLLDC VKQNEIDAGL PDLLLPMEPK HMFFARPEKQ EEVAANVDQF
NDSYARNTTS EELKNVLFLP NWWLRKTSAD CFKTLHQMMK EHRFKGSQCP EGIAKLTERI
QERVHSGYEI PCGWLFKGLT ILFQHRSMDD TGSSGNTVPS DHSYRLRLAI NTARFAGANI
ASSPNQASIT HVVVDPESPS SEISSLRGTW SKKQGQKVPH IVAVDWIEES WKERTLLDEE
RFQPKRSKA
//