DNLI4_ASPOR
ID DNLI4_ASPOR Reviewed; 1006 AA.
AC Q2U6A1;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=DNA ligase 4;
DE EC=6.5.1.1;
DE AltName: Full=DNA ligase IV;
DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] 4;
GN Name=lig4; ORFNames=AO090120000322;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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:0000250}.
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:0000255|PROSITE-
CC ProRule:PRU10135};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP007166; BAE62914.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2U6A1; -.
DR SMR; Q2U6A1; -.
DR STRING; 510516.Q2U6A1; -.
DR EnsemblFungi; BAE62914; BAE62914; AO090120000322.
DR VEuPathDB; FungiDB:AO090120000322; -.
DR HOGENOM; CLU_004844_1_1_1; -.
DR OMA; EGIMIKH; -.
DR Proteomes; UP000006564; Chromosome 5.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IMP:AspGD.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd07903; Adenylation_DNA_ligase_IV; 1.
DR Gene3D; 1.10.3260.10; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.10190; -; 2.
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 PANTHER; PTHR45997; PTHR45997; 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; SSF117018; SSF117018; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52113; SSF52113; 2.
DR TIGRFAMs; TIGR00574; dnl1; 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; DNA damage; DNA recombination; DNA repair; DNA replication;
KW Ligase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..1006
FT /note="DNA ligase 4"
FT /id="PRO_0000278376"
FT DOMAIN 718..811
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 890..1002
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 320
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10135"
FT BINDING 318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 387
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 487
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 503
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 509
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1006 AA; 114882 MW; 75D212090D2D03E4 CRC64;
MDSDDDYNGP ADTNPRLEDE ESDLDEKYPN RPRNHSTTLP FHVLFQTLFY PLSEIKKKPA
GPARKKVGPH GLSSVNLTPL EKRRDIIDRF ISRWRKEVGD DIYPAFRLIL PDKDRDRAMY
GMKEKAIGKL LIRIMKIDKN SEDALNLLNW KLPGQTTTSS MAGDFAGRCF GVLSKRPMRT
EVGDMTIEEV NEKLDHLSAA SKENQQLPIL TEFYRRMNPE ELMWLIRIIL RQMKVGATER
TFFDVFHPDA ENLYSISSSL RRVCWELHDP NIRLEAEDRG ITLMQCFQPQ LAQFQMHSLD
RMISRMRLTE DDPVFWIEEK LDGERMQLHM DSNDSVPGGR TFRFWSRKAK DYTYLYGNGI
QDENGALTRY LSDAFADGVE SLILDGEMIT WDTEQDAIAP FGTLKTAALS EQRNPYSSTT
RPLFRIFDIL YLNGRDLTRY TLRDRRNALQ KSIKPVYRRF EIHPYEEATG KTEIEEALRR
VVEEASEGLV LKNPRSPYRL NERHDDWMKV KPEYMTEFGE SLDVVVIGGY YGSGHRGGGL
SSFLCGLRVD DAHSSQGMVA SKCYSFCKVG GGFTAADYAN IRHHTDGKWH EWKSRKPPTT
YIELAGGDAQ YERPDMWIKP EDSVVLCVKA ASVAVSDQFR IGLTLRFPRF KKLRMDKDWK
SALSVQEFLD LKANAERERK EKEFNVDNSR KKRAKRDNKK PLAIVGYSAE AEAQYTGPSG
NIFEGLNFYI TTDSNTPVKK SKAELEQLVK ANGGKFFQTS NAAPSTICIA DRRTVKAASL
QKSGNVNIIR PSWILDCIRQ SEIDAGLPDS LLPLEPRHVF FATQDKKEEI AASVDRFNDS
YARNTTNDEL KEILKQMSKD HHFHASQNPK IVRKLNERIQ EKVNAGWEMP SGWLFKGLTI
LFPQNDKVDD AEVDETSQTH QQYRLNLARN TVRFAGANVV DSKSSSVTHI VVAPGSSSSD
VSSIRKSHSA KPGKKVPHLV TAEWIEECWK QRTLLGEEGF QPSRGT
