ID   D4AJD4_ARTBC            Unreviewed;      1020 AA.
AC   D4AJD4;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   02-SEP-2026, entry version 79.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=ARB_04383 {ECO:0000313|EMBL:EFE36857.1};
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE36857.1, ECO:0000313|Proteomes:UP000008866};
RN   [1] {ECO:0000313|Proteomes:UP000008866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
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|PROSITE-ProRule:PRU10135, 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:EFE36857.1}.
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DR   EMBL; ABSU01000001; EFE36857.1; -; Genomic_DNA.
DR   RefSeq; XP_003017502.1; XM_003017456.1.
DR   AlphaFoldDB; D4AJD4; -.
DR   STRING; 663331.D4AJD4; -.
DR   GeneID; 9524612; -.
DR   KEGG; abe:ARB_04383; -.
DR   eggNOG; KOG0966; Eukaryota.
DR   HOGENOM; CLU_004844_1_1_1; -.
DR   OMA; EGIMIKH; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0032807; C:DNA ligase IV complex; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:TreeGrafter.
DR   GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IEA:TreeGrafter.
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   FunFam; 2.40.50.140:FF:000234; DNA ligase; 1.
DR   FunFam; 3.30.470.30:FF:000013; DNA ligase; 1.
DR   FunFam; 1.10.3260.10:FF:000008; DNA ligase 4; 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   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; 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|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU000617};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000617}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008866};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          413..538
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          723..807
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          897..1010
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          44..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          668..693
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        668..678
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        679..688
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        308
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10135"
SQ   SEQUENCE   1020 AA;  116241 MW;  E34AC539D072D3A8 CRC64;
     MEPNPGGAIR ETERELDEKP RNHGQTLPFH DLFISLFNPL NDLKKKPAGP PAARRKAGPT
     GRNNLSPHEL RRNVIERFIS RWRQQVGNDF FPAFRLIVPE KDRDRAMYGL KEKAIGKLLV
     KVMKIDKNSE DGYNLLNWKL PGQRAATAMT GDFAGRCFEV ISKRPLRTEV GDMSIADVNS
     RLDDLAVASK EDAQLPILAE FYRRMNPEEM MWLIRIILRQ MKVGATERTF FEIWHPDAES
     LFNISSSLRR VCWELYLPSI RLEADEARVT LMQCFQPQLA QFQMHSFQKI IERMRLAEDD
     PEFWIEEKLD GERMQLHMET NSSIPGGKRF EFWSRKAKEY TYLYGNGFYD DNGSLTRHLK
     NAFADGVESI ILDGEMITWD PEQDAPVPFG TLKTAALAEQ RNPFSASGHR PLFRIFDIVY
     LNGKPLTRYT LRDRRRALEA SVIPVHRRFE IHPYQVGKSA SDIEPLLRKV VAEASEGLVL
     KNPNSPYRLN ERNDDWMKVK PDYMTEFGES LDCIVVGGYY GSGKRGGNIS SYLCGLRVDD
     THAEDGTNPM KCYSFCKVGG GFTAADYANI RHHTDGKWHD WDPKKPPTEY IELAGGDAQH
     ERPDVWIKPD DSIVVCVKAA AVTPSDQFRL GLTVRFPRFK RLRMDKDWQS ALSVQEFMDL
     KAGAEQEKKE KDFQVDNSRR KKTKRSKKKE LTVAGSGEPN VAYVGSKTHI FDGLSFCGLK
     IQALEVNYAN IFIVVMTESV KPMKKSKADL EQLIKANGGK IYQTNNAAKD TYCIADRRTV
     KVASLQKSGL ENVIRPCWIS DCISQNEHDI GESSILLPLE PRHMFFTKED QKEEISNNVD
     KYDDSFARDT SIAELTEILH KMDAISDISG EERLDIMSDL TLDGDQGSVH SDVEGWLFKN
     LTIFFAPCSH LSSVPGEPYV DALSIRQQLA RNITIFTGAT VTDQQKNNRI THVIVDPSAD
     RDPETGKAKN YTTLRSEFAT RRAIPHFVTV QWVEECWKEK TLVDEERMYS MPAIALPGLC
//