ID   A3LP53_PICST            Unreviewed;       719 AA.
AC   A3LP53;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 2.
DT   04-NOV-2026, entry version 114.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=PICST_56005 {ECO:0000313|EMBL:ABN64436.2};
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC   Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN64436.2, ECO:0000313|Proteomes:UP000002258};
RN   [1] {ECO:0000313|EMBL:ABN64436.2, ECO:0000313|Proteomes:UP000002258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC   {ECO:0000313|Proteomes:UP000002258};
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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   -!- 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; CP000496; ABN64436.2; -; Genomic_DNA.
DR   RefSeq; XP_001382465.2; XM_001382428.1.
DR   AlphaFoldDB; A3LP53; -.
DR   FunCoup; A3LP53; 709.
DR   STRING; 322104.A3LP53; -.
DR   GeneID; 4837358; -.
DR   KEGG; pic:PICST_56005; -.
DR   eggNOG; KOG0967; Eukaryota.
DR   HOGENOM; CLU_005138_4_1_1; -.
DR   InParanoid; A3LP53; -.
DR   OMA; AACECPN; -.
DR   OrthoDB; 206088at2759; -.
DR   Proteomes; UP000002258; Chromosome 2.
DR   GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0006284; P:base-excision repair; IEA:EnsemblFungi.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:EnsemblFungi.
DR   GO; GO:0035753; P:maintenance of DNA trinucleotide repeats; IEA:EnsemblFungi.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:EnsemblFungi.
DR   GO; GO:1903461; P:Okazaki fragment processing involved in mitotic DNA replication; IEA:EnsemblFungi.
DR   CDD; cd07900; Adenylation_DNA_ligase_I_Euk; 1.
DR   CDD; cd07969; OBF_DNA_ligase_I; 1.
DR   FunFam; 1.10.3260.10:FF:000001; DNA ligase; 1.
DR   FunFam; 2.40.50.140:FF:000062; DNA ligase; 1.
DR   FunFam; 3.30.470.30:FF:000016; 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:SF4; DNA LIGASE 1; 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 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; PS00333; DNA_LIGASE_A2; 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   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
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   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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002258}.
FT   DOMAIN          461..598
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          23..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        378
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10135"
SQ   SEQUENCE   719 AA;  81417 MW;  7A08F415B801CBEE CRC64;
     MAPRQQSIGR FFGSAMSVDS LLSQTVNKSP KNQKSESLTD EQNKREAFQV SQQESEKDQE
     QKPDTDPSES EPEKDKTEEI KEASELIKLS EKEHEKHVGE KLSAKIPYSK LTDVLDKIEA
     ESSRLKITAI VSEFFLEILK QSTVDKLVKI VYLFINRLGP DYEPDLELGL GETILIKAIS
     ECYGRPSTKI KKDYQEVGDL GLVAQKSRSG QPTMFKPAPL DVDQVFENLT KIAKSTGKDS
     QAKKISLINK MLTACNAKSS EAKFLIRSLE GKLRIGLAEK TVLIGLAQAF VNYEAKDSKR
     INPEKLTQSE DVVREAFSQI PNYEILIRNA YEYGIFNLLD HCQLTPGIPL KPMLAKPTKS
     ISEVLDRFQG EEFTCEYKYD GERAQVHLLH DGTVRIYSRN SEDMSERYPD LISIMKDFIK
     TQEGQAPSMI LDCEAVAWDR VANKILPFQV LSTRKRKDVD EKDITVHICL FAFDILYFDN
     EPLITKSLKE RRQVMEENLT PMDGKFQFAT AKNSSNLDEL QQFLDQSVKD SCEGLMVKML
     NGKESYYEPS KRSRNWLKLK KDYLAGVGDS LDLVVIGAYI GRGKRTGNYG GFLLASYNQD
     TGEYETTCKI GTGFSDEDLA SLHTKLKPTE ISVPKPYYVY DTTNSNAKPD VWFEPTTIFE
     VLTADLSLSP IYKAAHQEYG KGISLRFPRF LRIRDDKGIE DATSSTQVSE FYERQASVN
//