ID   B2AF11_PODAN            Unreviewed;       857 AA.
AC   B2AF11;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   02-SEP-2026, entry version 97.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC   Podospora anserina.
OX   NCBI_TaxID=515849 {ECO:0000313|EMBL:CDP29104.1, ECO:0000313|Proteomes:UP000001197};
RN   [1] {ECO:0000313|EMBL:CDP29104.1, ECO:0000313|Proteomes:UP000001197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197};
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA   Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA   Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA   Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA   de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA   El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2] {ECO:0000313|Proteomes:UP000001197}
RP   GENOME REANNOTATION.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197};
RX   PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA   Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA   Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
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   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; FO904940; CDP29104.1; -; Genomic_DNA.
DR   RefSeq; XP_001904250.1; XM_001904215.1.
DR   AlphaFoldDB; B2AF11; -.
DR   STRING; 515849.B2AF11; -.
DR   GeneID; 6188259; -.
DR   KEGG; pan:PODANSg1268; -.
DR   VEuPathDB; FungiDB:PODANS_5_880; -.
DR   eggNOG; KOG0967; Eukaryota.
DR   HOGENOM; CLU_005138_1_1_1; -.
DR   OrthoDB; 206088at2759; -.
DR   Proteomes; UP000001197; Chromosome 5.
DR   GO; GO:0005634; C:nucleus; 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:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006273; P:lagging strand elongation; IEA:TreeGrafter.
DR   CDD; cd07900; Adenylation_DNA_ligase_I_Euk; 1.
DR   CDD; cd07969; OBF_DNA_ligase_I; 1.
DR   FunFam; 1.10.3260.10:FF:000004; DNA ligase; 1.
DR   FunFam; 2.40.50.140:FF:000062; DNA ligase; 1.
DR   FunFam; 3.30.470.30:FF:000018; DNA ligase; 1.
DR   Gene3D; 3.30.1490.70; -; 1.
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; IPR050191; ATP-dep_DNA_ligase.
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; IPR012340; NA-bd_OB-fold.
DR   NCBIfam; TIGR00574; dnl1; 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR45674:SF9; DNA LIGASE 3; 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; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 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|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001197}.
FT   DOMAIN          523..711
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          618..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          829..857
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..70
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..638
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        842..857
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        443
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10135"
SQ   SEQUENCE   857 AA;  95351 MW;  95684E0CA3EAE3B6 CRC64;
     MASPAKKRKL NSDTKKAAVP ATKGIQYFFA KQQQNGSSSR TTSEIQQNGS QSEKSDEQLT
     DEELARKLQA EWDAEVQASN QRQQQLQPEP NTSPALPAPP SPLKLSVSPK VDTAKSKNTL
     SLSSVTAVED QVTATIPLDE SPLTFDPSKY VPQLQESWAA ERGKSSYALL TRCFVLVSST
     QSRIKIVDTL VNCLRLLIEG DPNSLLPAVW LATNAISPPY ISMELGLGGS AISKALKQVC
     GLDNRALKAM HDRLGDPGDV AFEAKKKQSF TLKKPKPLTI KGVFESLVKI AKTQGQGSGD
     IKQRIVDRLL QDARGGEESR YIVRTLCQHT TMLIALSRAF LLSKPPGADF PTREPAELAK
     LSKEELAEIW SRGEELVKAS FARHPDYNDL IPVLLDIGIS DELPIRCGLN LHIPLRPMLG
     SITRDLSEML TKLQGRDFAC EYKYDGQRAQ VHCDADGKVS IFSRHLELMT DKYPDLVSLV
     PKIRGEDVQS FIMEGEVVAV DQTTGELKNF QTLSNRARKD VAVGSITINV CLFAFDLMYL
     NGQPLLDRPF RERRDMLRSL FIEIPHHFTW VKSLDATSQD SEPVLTFFKS ALETKCEGIM
     VKILDNLPDI PYEDQSAAAG LLDNTKPTTT TTTTNKTPLN PPPPQKRSRR KPLLSTYEPD
     KRLDSWLKVK KDYSTSLSSS SEPLDLIPIA AWHGTGRKSQ FWSPFLLAVR NEDVGSLEAV
     CKCMSGFTDN FYKANKAYYD PAIEGRTLGK KPGFVEYYGP EPDVWFNPTE VWEVAFADVT
     VSPTYTAAVG MVHPDKGLSL RFPRFVRKRE DKGIEEASTS EVLAGLYRKQ EAGPAKRPME
     EVEKEQEEGE DIMDEDE
//