ID   B6HK40_PENRW            Unreviewed;       990 AA.
AC   B6HK40;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=Pc21g07170 {ECO:0000313|EMBL:CAP95614.1}, PCH_Pc21g07170
GN   {ECO:0000313|EMBL:CAP95614.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP95614.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP95614.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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; AM920436; CAP95614.1; -; Genomic_DNA.
DR   RefSeq; XP_002567758.1; XM_002567712.1.
DR   AlphaFoldDB; B6HK40; -.
DR   STRING; 500485.B6HK40; -.
DR   GeneID; 8314155; -.
DR   KEGG; pcs:Pc21g07170; -.
DR   VEuPathDB; FungiDB:PCH_Pc21g07170; -.
DR   eggNOG; KOG0966; Eukaryota.
DR   HOGENOM; CLU_004844_1_1_1; -.
DR   OMA; EGIMIKH; -.
DR   OrthoDB; 8251at2759; -.
DR   BioCyc; PCHR:PC21G07170-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c21.
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: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; 2.
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|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   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          423..548
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          713..798
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          875..988
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          53..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          674..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   990 AA;  113516 MW;  4ED51FADC197051E CRC64;
     MDSDEILGQD DVLKPEQEED LDEKYPNRPH NRAPTLPFHD LYLDLFNPLS ELKKKPSGPA
     PARRKAGPHG KGATSLNPFE RRRDVIERFI SRWRKDVGDD IYPALRLILP DKDRDRPMYG
     IKEKAIGRML VKIMKINKES EDGYNLLNWK LPGQGATTRM AGDFARRCFD VLSKRPMRTD
     PGDMTIEEVN EKLDKLSAAS KEDEQLPILT EFYRRMNPEE LLWLIRIILR QMKVGATERT
     FFDVWHPDAE NLYSISSSLR RVCWELHDPN IRLEGEERGI ALMQCFQPQL AQFQMHSFER
     IIARMKPTED DNVFWIEEKM DGERMQLHMA PDDSTKGGRK FGFWSRKAKE YTYLYGNGIY
     DENGALTRHL KDAFVDGVQS IILDGEMITW DPEQDAMVPF GTLKTAALAE QRNPFSNGPR
     PLFRVFDILH LNGRDLTKYT LRDRRNALEK TVRPVHRRFE IHSYEEATTT TEVEAALRKV
     VAEASEGLVL KNPRSPYRLN ERHDDWMKVK PDYMTEFGES LDVIVIGGYY GSGRRGGALS
     SFLCGLRVDD STQAAEKCWS FCKVGGGFTA ADYQEVRHHT DGKWKAWDAK KPPTTFVELA
     GGDAQHERPD MWIKPSDSIV LCVKAASVAI SDQFRMGLAL RFPRFKKLRK DKDWKTALSV
     QEFLDLKSNA EQEHREKEFS VDNSRKKRVK RATKKPLTVA GHEDNVDVQY LGPSGHVFDE
     LNFFIMTEST VPEKKTKLQL EQLVKANGGK IYQTKTAAVD TLCVAERRTV KVASLQKSGE
     QNIIRPSWLI DCVKQNEIDA GLPDLLLPFE PRHMFFMTEE KEEEVAANVD KFMDSYARDT
     TVNELKDADD VPDPETTQRI ETRIQERVNA GYTVPVGWLF RGLKFHFYSN GNQPDESASR
     EIRREDQRLQ FARNTARFAA AEIAKTLKSS GITHVIVDPE TVSSADKTSL RNTLAAKPGA
     KMPHLVSVGW VEECWKNGTL LDEERFPILR
//