ID   A7TGW3_VANPO            Unreviewed;       965 AA.
AC   A7TGW3;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=Kpol_1032p7 {ECO:0000313|EMBL:EDO18415.1};
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN   [1] {ECO:0000313|EMBL:EDO18415.1, ECO:0000313|Proteomes:UP000000267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC   NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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|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; DS480389; EDO18415.1; -; Genomic_DNA.
DR   RefSeq; XP_001646273.1; XM_001646223.1.
DR   AlphaFoldDB; A7TGW3; -.
DR   STRING; 436907.A7TGW3; -.
DR   GeneID; 5546698; -.
DR   KEGG; vpo:Kpol_1032p7; -.
DR   eggNOG; KOG0966; Eukaryota.
DR   HOGENOM; CLU_004844_1_1_1; -.
DR   InParanoid; A7TGW3; -.
DR   OMA; EGIMIKH; -.
DR   OrthoDB; 8251at2759; -.
DR   PhylomeDB; A7TGW3; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
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; cd17744; BRCT_MDC1_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; 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; 2.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SMART; SM00292; BRCT; 2.
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:UP000000267};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          392..524
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          702..794
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          863..964
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
SQ   SEQUENCE   965 AA;  112453 MW;  18173392179317B9 CRC64;
     MRNPTPILVS TNTNTNATFT SKADTNDIEE PHNFSPSPDF KWLCDELFVK LDQIQFRPKE
     LNGSKPKYIE YYDIINNFID IWRRTVGNDI YPALILTIPY RDRRMYNIKE SKLIRIVCDY
     LKLPKNSETE RRLMRWKHRA DRNVRLSTFC VEEIKKRKGE PREKIKITID KLNECLDNLV
     LERGYKGSKS QKISESETFK FCFENMTYVE LKYFFDILLK DKIVGGLEHK FLNCWHPDAQ
     DYLSVVSDLK IVSSKLWNPE FRLKYDDLTI NIDHAFTPET AKRLTYSYDT IARRLKNDFF
     IEEKMDGERI QLHYMNYGAK LKFLSRRGLD YSYLYGDNRN NGAIGRYLNF HKDVKECILD
     GEMVTYDSVK NCILPFGLVK SSAMQSLSVS DIEPDGYHPL YMAFDLVYLN GSSLSTLPLH
     QRKNYLDKLL IPCPDFVEIL PALHCNDSSL IKSSLEKAIE LGSEGIILKR FDSQYLVAKR
     SDDWIKIKPE YLEQFGENMD LIVIGRDPGK KDSLMCGLIL TGDNEPEEIT SLDSNPTDTA
     ESFLKPDKRK IISFCNIANG ISQKEFRDID RYTFGHWIKF DDELPPQDLF EFGTKHPIEW
     IYPEHSVVLE IKARSLETNE SARIKYGTGS TLFGGYCRQI RYDKDWVSCF TYNEFMESRN
     LKNALVNYPD NKNLIGRKKR PKKRMFNSLT EIFENTKDAP DESNVIFRGL HFYVISDYID
     ETDGSRLSKS DLCNLVLEHN GKLVHNPISR IDILNRLRII SMKYTRETTS LIERGYDIIH
     PQWILDCISN RKLVRLLPSH CFNVSSSLME VTKTRVDRYG DSYETSLTEK DFEILINRQV
     LKSESADKRI TEGENHLKIP ILLFCNRRFF IPETLPSTPI YELKSKVELY GGKLVNKISD
     CNVIVFTNTH TENRKEVMKK IRRALVCLDP NSMQVPVLPR IVDANWIDAC ISECVQVPEE
     DYPAV
//