DNLI4_COPCI
ID DNLI4_COPCI Reviewed; 1025 AA.
AC Q7Z7W5;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=DNA ligase 4;
DE EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135};
DE AltName: Full=DNA ligase IV;
DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] 4;
GN Name=LIG4;
OS Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=5346;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=ATCC 56838;
RX PubMed=12904551; DOI=10.1099/mic.0.26311-0;
RA Namekawa S., Ichijima Y., Hamada F., Kasai N., Iwabata K., Nara T.,
RA Teraoka H., Sugawara F., Sakaguchi K.;
RT "DNA ligase IV from a basidiomycete, Coprinus cinereus, and its expression
RT during meiosis.";
RL Microbiology 149:2119-2128(2003).
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:0000269|PubMed:12904551}.
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}.
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DR EMBL; AB098474; BAC76766.1; -; mRNA.
DR EMBL; AB072455; BAD93669.1; -; mRNA.
DR AlphaFoldDB; Q7Z7W5; -.
DR SMR; Q7Z7W5; -.
DR VEuPathDB; FungiDB:CC1G_14831; -.
DR VEuPathDB; FungiDB:CC2G_011852; -.
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: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; IEA:UniProtKB-KW.
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; 2.
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; PS00333; DNA_LIGASE_A2; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; DNA damage; DNA recombination; DNA repair; DNA replication;
KW Ligase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Repeat.
FT CHAIN 1..1025
FT /note="DNA ligase 4"
FT /id="PRO_0000278380"
FT DOMAIN 667..763
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 915..1025
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 REGION 773..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..820
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..846
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..870
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 291
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10135"
FT BINDING 289
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 447
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 452
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1025 AA; 116825 MW; ACAE9D076932868C CRC64;
MMQPTPAPSS APGSPQRTQA EPEMETPSYP QPPQNVGTAP FSVLVKLFEK LATERKQERR
RKLLDAWFRH WRREKGFDLY PVLRLLLPQK DRDRAVYGLK EKNLAKTYIK LIPLGMRDPD
AIRLLNWKKP TERDKSSGDF PQVLCEVVSK RSSVIEGTLT IDELNEILDD IAKNMGKSDV
QSKILRRIYN NSTADEQRWI IRIILKDMNI SVKETTVFAV FHPDAQDLYN TCSDLKKVAW
ELWDPSRRLN AKDKEIQIFH AFAPMLCKRP TRKIEETVKA MGGSKFIIEE KLDGERMQLH
KRGNEYFYCS RKGKDYTYLY GKHIGAGSLT PFIDSAFDSR IDDIILDGEM LVWDPVSERN
LPFGTLKTAA LDRSKKENNP RPCFKVFDLL YLNGMSLLDK TVKFRKNNLR HCIKPIPGRI
EFVEEYQGET ANDIRKRMEQ VMENRGEGLV IKHPKAKYIL NGRNTDWIKV KPEYMDNMGE
TVDVLVVAGN YGSGKRGGGV STLICAVMDD RRPDSDDEPK YSSFVRIGTG LSFADYVWVR
SKPWKVWDPK NPPEFLQTAK KGQEDKGDVY LEPEDSFILK VKAAEITPSD QYHMGFTMRF
PRALAIRDDL SIADCMTATE VFESLKSERK RKMEDDAGIT TKKRKTTVKK VALLPEYSGP
NLKKVAVKTD IFNGMKFVVF SDPKSRTGEA DKKELMKTIH ANGGTCSQIV NKNSEAIVIY
GGSITPYDLK LVIDKGIHDV IKPSWITDSV TLGEPAPFKK KYFFHATEER KYADEYNEDD
GEEEGAVPSA DEQERDVKSG TVEPGSETED EDEEQAPEIK EEQDGELHEW LKVDDRKSPA
LPAHDEEDSV TEDDSDNADV ADEEEPDLDD WFQVKGETED EGAGALATAS RHRETTPDVD
GDVKMGESEE AMDYDPDVIF KHLCFYLDSP ANAQRHGMAT RPKYEAAITK SFEEVEKLIK
DNGGKIVDLD EPKLTHVVLD KRDDSRRVEL MKRTSKPRRR HLVLSDYIEA CIDEGTLLDE
EEFAP
