ID   DNLI4_CANAL             Reviewed;         928 AA.
AC   P52496; A0A1D8PGS3; Q5A0L3;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 4.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=DNA ligase 4;
DE            Short=CaLIG4;
DE            EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135};
DE   AltName: Full=DNA ligase IV;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] 4;
GN   Name=LIG4; Synonyms=CDC9; OrderedLocusNames=CAALFM_C203030WA;
GN   ORFNames=CaO19.13220, CaO19.5798;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 56884 / 366;
RX   PubMed=8840507;
RX   DOI=10.1002/(sici)1097-0061(199607)12:9%3c893::aid-yea973%3e3.0.co;2-i;
RA   Andaluz E., Larriba G., Calderone R.;
RT   "A Candida albicans gene encoding a DNA ligase.";
RL   Yeast 12:893-898(1996).
RN   [2]
RP   SEQUENCE REVISION TO C-TERMINUS.
RA   Larriba G.;
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN   [6]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=10487922;
RX   DOI=10.1002/(sici)1097-0061(19990915)15:12<1199::aid-yea447>3.0.co;2-s;
RA   Andaluz E., Ciudad A., Rubio Coque J., Calderone R., Larriba G.;
RT   "Cell cycle regulation of a DNA ligase-encoding gene (CaLIG4) from Candida
RT   albicans.";
RL   Yeast 15:1199-1210(1999).
RN   [7]
RP   FUNCTION.
RX   PubMed=11119499; DOI=10.1128/iai.69.01.137-147.2001;
RA   Andaluz E., Calderone R., Reyes G., Larriba G.;
RT   "Phenotypic analysis and virulence of Candida albicans LIG4 mutants.";
RL   Infect. Immun. 69:137-147(2001).
RN   [8]
RP   FUNCTION.
RX   PubMed=12702284; DOI=10.1016/s1567-1356(02)00094-6;
RA   Andaluz E., Ciudad T., Larriba G.;
RT   "An evaluation of the role of LIG4 in genomic instability and adaptive
RT   mutagenesis in Candida albicans.";
RL   FEMS Yeast Res. 2:341-348(2002).
CC   -!- FUNCTION: DNA ligase involved in DNA non-homologous end joining (NHEJ);
CC       required for double-strand break (DSB) repair. Not required for the
CC       repair of DSBs induced by ionizing radiation or UV light. Has an
CC       important role in morphogenesis, positively affecting the capacity to
CC       form hyphae. {ECO:0000269|PubMed:10487922, ECO:0000269|PubMed:11119499,
CC       ECO:0000269|PubMed:12702284}.
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:0000255|PROSITE-
CC         ProRule:PRU10135};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P49917};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q08387}.
CC   -!- INDUCTION: Cell cycle-regulated. Expression peaks in late G1 and during
CC       the morphological transition. {ECO:0000269|PubMed:10487922}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
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DR   EMBL; X95001; CAA64457.2; -; Genomic_DNA.
DR   EMBL; CP017624; AOW27340.1; -; Genomic_DNA.
DR   RefSeq; XP_715339.2; XM_710246.2.
DR   AlphaFoldDB; P52496; -.
DR   SMR; P52496; -.
DR   STRING; 237561.P52496; -.
DR   EnsemblFungi; C2_03030W_A-T; C2_03030W_A-T-p1; C2_03030W_A.
DR   GeneID; 3642986; -.
DR   KEGG; cal:CAALFM_C203030WA; -.
DR   CGD; CAL0000187710; LIG4.
DR   VEuPathDB; FungiDB:C2_03030W_A; -.
DR   eggNOG; KOG0966; Eukaryota.
DR   HOGENOM; CLU_004844_1_1_1; -.
DR   InParanoid; P52496; -.
DR   OrthoDB; 8251at2759; -.
DR   PHI-base; PHI:219; -.
DR   PRO; PR:P52496; -.
DR   Proteomes; UP000000559; Chromosome 2.
DR   GO; GO:0032807; C:DNA ligase IV complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; ISS:UniProtKB.
DR   GO; GO:0003909; F:DNA ligase activity; IGI:CGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0097680; P:double-strand break repair via classical nonhomologous end joining; ISS:UniProtKB.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR   GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR   GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR   GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IBA:GO_Central.
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; 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; 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; 1.
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; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; DNA damage; DNA recombination; DNA repair; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Nucleus; Reference proteome; Repeat.
FT   CHAIN           1..928
FT                   /note="DNA ligase 4"
FT                   /id="PRO_0000059584"
FT   DOMAIN          673..769
FT                   /note="BRCT 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   DOMAIN          821..927
FT                   /note="BRCT 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   ACT_SITE        304
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10135"
FT   BINDING         302
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P49917"
FT   BINDING         304
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P49917"
FT   BINDING         309
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P49917"
FT   BINDING         362
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P49917"
FT   BINDING         362
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         409
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P49917"
FT   BINDING         469
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P49917"
FT   BINDING         469
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         474
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P49917"
FT   BINDING         492
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P49917"
FT   BINDING         494
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P49917"
FT   CONFLICT        531..534
FT                   /note="VYYS -> FIIV (in Ref. 2; CAA64457)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        698
FT                   /note="T -> R (in Ref. 2; CAA64457)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   928 AA;  108012 MW;  D6C2AC6C2EDF3467 CRC64;
     MTYFLNDIRP PSPNDITPSF TLLTKELFDK LDGVRKESLG DFRTVTEKKA FIIKTFINTF
     RTHIGNDIYP SAKLIFPEKS GRIYFIKEVA LARLLIKMYK IPKESEDYIT LHDWNKSYQR
     SRRFSIDEKK IRDLPLQASR IISKRRPIVD KLEEYTVPQI NSSLDQLALE KVSQGQIDIL
     KPLFDNLSIP EVRWLIHILL NKSILTSMER FFFNTWHPDG YRVFSICNDL QKTLQFSTNP
     DLRLDPSQLA IHPCFKFKPQ LSERLTTSYK TLVKKLQRKH EMDPPYEKKF QELGLENKFY
     IEEKMDGDRM LLHKDGDSFK FFSRRLKDYS YLYGESFQFG ALTKFLAHAF AGNIQSVILD
     GEMVAYDYER NVILPFGTLK SSAIQESVRQ FTTIDQYEQQ TAYPFFLVFD ILFLNGKDLT
     NYPLFFRKNI LNRILRPIPN RFEVLDTRLG SSSEDIERAI REVVSSRCEG LVLKNVQSKY
     EIDGFRNPDW IKVKPEYLEK FGENLDLVVI GKSPAIKNSY MCGLKSVTDG VYYSFCTCAN
     GIEIEEFDKI ERLTHGKWIK TDVSMPPESL IKFGTKIPTF WIHPSDSLVL EIRARSIDTR
     AGTSYAVGST LHNNHCRKIR EDKSIDECVT LQEYTHIKAN YINDLNKAQT ALGKKREPVY
     SLDNESKLKK VKVESDLFSG IEFLIMSDKR EADGEVTTIE EMKAMVKQYG GKIVNSVDLA
     TNYQIMVITE RELPVSSQYL SKGIDLVKPI WIYECIKRGC VLQLEPYFIF ASKNWDNFNH
     MVDQYGDSYI IHHPLNIVVP KLSESELEDL RNGFDWGDLK PWIYLFKGLS FYVCGNNLSA
     RFLKERIERF SGDLSKHFIE CCYIVIPDNH SRPLMLREID KMSNQISREM VIDKNGGSSR
     IPHFVTEAFV QASIKMNYIP DPDDYKFR
//