DNLI4_CANAL
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 03-AUG-2022, entry version 138.
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=10.1111/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 non-
CC homologous integration (NHI) pathways where it is required in the final
CC step of non-homologous end-joining (NHEJ). Not required for the repair
CC of DSBs induced by ionizing radiation or UV light. Has an important
CC role in morphogenesis, positively affecting the capacity to form
CC 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; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus.
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 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; 274264at2759; -.
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; IBA:GO_Central.
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:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IBA:GO_Central.
DR CDD; cd07903; Adenylation_DNA_ligase_IV; 1.
DR Gene3D; 1.10.3260.10; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.10190; -; 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 PANTHER; PTHR45997; PTHR45997; 1.
DR Pfam; PF00533; BRCT; 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; DNA damage; DNA recombination; DNA repair; DNA replication;
KW Ligase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus;
KW 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"
FT BINDING 309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 324
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
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"
FT BINDING 486
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
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
