ID A0A2V5HWF1_9EURO Unreviewed; 1863 AA.
AC A0A2V5HWF1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-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 ORFNames=BP00DRAFT_489750 {ECO:0000313|EMBL:PYI27032.1};
OS Aspergillus indologenus CBS 114.80.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI27032.1, ECO:0000313|Proteomes:UP000248817};
RN [1] {ECO:0000313|EMBL:PYI27032.1, ECO:0000313|Proteomes:UP000248817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI27032.1,
RC ECO:0000313|Proteomes:UP000248817};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-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}.
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DR EMBL; KZ825579; PYI27032.1; -; Genomic_DNA.
DR Proteomes; UP000248817; 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:0008270; F:zinc ion binding; IEA:InterPro.
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 GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd07903; Adenylation_DNA_ligase_IV; 1.
DR CDD; cd17722; BRCT_DNA_ligase_IV_rpt1; 1.
DR CDD; cd12148; fungal_TF_MHR; 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 InterPro; IPR007219; Transcription_factor_dom_fun.
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; PF04082; Fungal_trans; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00906; Fungal_trans; 1.
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; 1.
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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 449..574
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 747..832
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1101..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1616..1641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1744..1771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1796..1863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1616..1639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1744..1769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1797..1819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1837..1863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1863 AA; 209548 MW; B42681F49FC3420D CRC64;
MDSDENMEVE GSSTLHPPAG AEHTHEDMDL DENYPNRPHN HSPTPAFHTL FENLFNPLSA
IKRQPTSTTT AQRPPSARRK LGPHGQGASA SLNPAERRRD VIERFISQWR QTVGDDIYPA
FRLILPDKDR DRAMYGLKEK AIGKMLVKIL KIDKNSEDAV GLLNWKLPGY EARGFLAGDF
ARRCYDVVSK RPMRTEVGRM TIDEVNGRLD RLSAAGREGE QMAILGEFYR RMNPEELMWL
IRIILRQMKV GASERTLFDV WHPDAEGLYS ISSSLRRVCW ELHDPNVRLE DERRGIALMQ
CFQPQLAQFQ VQSLEKMVAK MRGVATVGDG DKEGEGKGEF WIEEKLDGER MQLHMGPDEE
VDGGRRFRFW SRKAKDYTYL YGNGLFDENG ALTRHLADAF ADGVESVILD GEMIAWNPEQ
DAPEPFGTLK SAAIAEQRNP FANGSRPLFR IFDILYLNGH DLTRYTLRDR RNALQKSVQD
VHRRFEVHPY EEATSTAEVE ASLRRVVAEA SEGLVLKNPR SPYRLNERHD DWMKVKPEYM
TEFGESLDLV VIGGYYGSGH RGGALSSFLC GLRVDDSATS SQHHAAEPSK CYSFCKVGGG
FTAADYANIR HHTDGKWKEW NPKKPPLAYI ELAGAGNAQH ERPDMWIKPE DSVVLCVKAA
SVSVSDQFRM GLTLRFPRFK RLRGDKDWTS ALSVQEFLDL KSNVEQEQKE KAFNVENFRK
KRQKKSTKKP LAIAGYDERA EVKSAGPSGH IFDGLNFFVM TDSTAPVKKT KAELEQLVKS
HGGKFYQTNT AAPDMICVAD RRTVKAASLQ KAGEVDIVRP SWILDCIRQS EIDAGLADLL
LPTEPRHMFY TTPEKEAEVA ASVDRFNDSY ARDTTLEELS EILKKMETDV PPGNSKALDK
LKGHLYDKIH SGWPLPCGWL FDGLVFYFPE LAHPTTPEDS PDDDFGELGT LQSHHDHHPL
QLTRNTARFA GARVVDTAQD PAITHVILPP TGLLVAEYRA LREPWAAADR IPHFVTTGWV
EESWRQQTLL DEESVYDPNS DHRRKGVYKK DTDTLRTKNA TLLTLIQALL NYEEEDAFDL
VRQIRSCDNL EDVAQSILGQ QNKPSLASDT PVASGDEADQ FESELSGKMS ELMLDGSRKL
IGGTSNLIYL PPGSELNEFN PNANHQDLGR GIDASVSHWT RVTDDEKLIS HLMQMYFTWH
YPFFTTLSRD LFYRDYVRGV SSQYCSSLLV NTMLALGCHF SSWEGAREDP GNSATAGDHF
FKEAKRLFFE NDEHANAKLC TVQALALMSV REAGCGRESK GWVYSGMSFR MASDLGLDFD
STSLGVRNLS EEEIDARRIT FWGCFLFDKC WSNYLGRQPQ WTVGDIGVSM PEIFPNEDAA
MWSSYTDAGG AEDQAQPSRT RAIAVQLSKL CQINGDLLVF FYDLKPKDKL SSKQTELKKL
SEIHTRLETW KKDLPKELGP QDGQLPQALL MHMFYQLLLI HLYRPFLKYT KSTSPLPQHV
SPRKLCTQAA SAISKLLRMY KRTYGFKQIC NVAVYMAHTA LTVHLLNLPE KNAQRDVVHG
VRHLEEMGES WLCARRTLRI LEISANKWHV ELPAEAVATF ENTHVRWGSW GSWDQALSPP
ASEDSPPTIS MSYPDSNSRG IGQPMPPRHA VMGGHGGNYM HKTPATTVGS MGSQVLPDLP
VPVSASAMRA VQRSLNAQLA QEPARLPEPT YLRPVAHAYA QYRNIPISQA DMWYNDENIR
AFSSAQDNSP ATTTSPANEY GGSENLVEES QDWWSRESHR FNFGMDNWVP DWNSNMPGRA
SAANPGSSFS MNVGQTSAPE SAPNPPPPMR FAVGAPSGTS NPDQSPTTPS YNNMPTSEAY
PRQ
//
