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Database: UniProt
Entry: P52496
LinkDB: P52496
Original site: P52496 
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-SEP-2017, entry version 115.
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;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   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<893::AID-YEA973>3.0.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.,
RA   Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
RA   Davis R.W., 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
RT   aligned on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
RP   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
RT   allele-specific measurements and provides a simple model for repeat
RT   and indel 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
RT   Candida 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=10.1111/j.1567-1364.2002.tb00103.x;
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: Involved in ds DNA break (DSB) repair. Has a role in
CC       non-homologous integration (NHI) pathways where it is required in
CC       the final step of non-homologus end-joining (NHEJ). Not required
CC       for the repair of DSBs induced by ionizing radiation or UV light.
CC       Has a important role in morphogenesis, positively affecting the
CC       capacity to form hyphae. {ECO:0000269|PubMed:10487922,
CC       ECO:0000269|PubMed:11119499, ECO:0000269|PubMed:12702284}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000255|PROSITE-ProRule:PRU10135}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- INDUCTION: Cell cycle-regulated. Expression peaks in late G1 and
CC       during the morphological transition.
CC       {ECO:0000269|PubMed:10487922}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
DR   EMBL; X95001; CAA64457.2; -; Genomic_DNA.
DR   EMBL; CP017624; AOW27340.1; -; Genomic_DNA.
DR   RefSeq; XP_715339.2; XM_710246.2.
DR   ProteinModelPortal; P52496; -.
DR   SMR; P52496; -.
DR   PRIDE; P52496; -.
DR   GeneID; 3642986; -.
DR   KEGG; cal:CAALFM_C203030WA; -.
DR   CGD; CAL0000187710; LIG4.
DR   InParanoid; P52496; -.
DR   KO; K10777; -.
DR   OrthoDB; EOG092C18KW; -.
DR   PRO; PR:P52496; -.
DR   Proteomes; UP000000559; Chromosome 2.
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: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:0006260; P:DNA replication; IEA:UniProtKB-KW.
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:0009405; P:pathogenesis; IMP:CGD.
DR   CDD; cd00027; BRCT; 1.
DR   Gene3D; 3.40.50.10190; -; 2.
DR   InterPro; IPR001357; BRCT_dom.
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; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR10459:SF84; PTHR10459:SF84; 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; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52113; SSF52113; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 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; Complete proteome; DNA damage; DNA recombination;
KW   DNA repair; DNA replication; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Nucleus; Reference proteome; Repeat.
FT   CHAIN         1    928       DNA ligase 4.
FT                                /FTId=PRO_0000059584.
FT   DOMAIN      673    769       BRCT 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   DOMAIN      821    927       BRCT 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   ACT_SITE    304    304       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10135}.
FT   METAL       362    362       Magnesium 1. {ECO:0000255}.
FT   METAL       469    469       Magnesium 2. {ECO:0000255}.
FT   BINDING     302    302       ATP. {ECO:0000250}.
FT   BINDING     309    309       ATP. {ECO:0000250}.
FT   BINDING     324    324       ATP. {ECO:0000250}.
FT   BINDING     474    474       ATP. {ECO:0000250}.
FT   BINDING     486    486       ATP. {ECO:0000250}.
FT   BINDING     492    492       ATP. {ECO:0000250}.
FT   CONFLICT    531    534       VYYS -> FIIV (in Ref. 2; CAA64457).
FT                                {ECO:0000305}.
FT   CONFLICT    698    698       T -> R (in Ref. 2; CAA64457).
FT                                {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
//
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