ID A0A250X4Q0_9CHLO Unreviewed; 824 AA.
AC A0A250X4Q0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=DNA ligase (NAD(+)) {ECO:0000256|ARBA:ARBA00012722};
DE EC=6.5.1.2 {ECO:0000256|ARBA:ARBA00012722};
GN ORFNames=CEUSTIGMA_g5509.t1 {ECO:0000313|EMBL:GAX78067.1};
OS Chlamydomonas eustigma.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=1157962 {ECO:0000313|EMBL:GAX78067.1, ECO:0000313|Proteomes:UP000232323};
RN [1] {ECO:0000313|EMBL:GAX78067.1, ECO:0000313|Proteomes:UP000232323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2499 {ECO:0000313|EMBL:GAX78067.1,
RC ECO:0000313|Proteomes:UP000232323};
RA Hirooka S., Hirose Y., Kanesaki Y., Higuchi S., Fujiwara T., Onuma R.,
RA Era A., Ohbayashi R., Uzuka A., Nozaki H., Yoshikawa H., Miyagishima S.Y.;
RT "Acidophilic green algal genome provides insights into adaptation to an
RT acidic environment.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA ligase that catalyzes the formation of phosphodiester
CC linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-
CC stranded DNA using NAD as a coenzyme and as the energy source for the
CC reaction. It is essential for DNA replication and repair of damaged
CC DNA. {ECO:0000256|ARBA:ARBA00004067}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-
CC nicotinamide D-nucleotide.; EC=6.5.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00034005};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAX78067.1}.
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DR EMBL; BEGY01000029; GAX78067.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A250X4Q0; -.
DR STRING; 1157962.A0A250X4Q0; -.
DR OrthoDB; 11121at2759; -.
DR Proteomes; UP000232323; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd17748; BRCT_DNA_ligase_like; 1.
DR CDD; cd00114; LIGANc; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR Gene3D; 1.10.287.610; Helix hairpin bin; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_01588; DNA_ligase_A; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR041663; DisA/LigA_HHH.
DR InterPro; IPR001679; DNA_ligase.
DR InterPro; IPR018239; DNA_ligase_AS.
DR InterPro; IPR013839; DNAligase_adenylation.
DR InterPro; IPR013840; DNAligase_N.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004150; NAD_DNA_ligase_OB.
DR InterPro; IPR010994; RuvA_2-like.
DR NCBIfam; TIGR00575; dnlj; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF01653; DNA_ligase_aden; 1.
DR Pfam; PF03120; DNA_ligase_OB; 1.
DR Pfam; PF12826; HHH_2; 1.
DR PIRSF; PIRSF001604; LigA; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00278; HhH1; 2.
DR SMART; SM00532; LIGANc; 1.
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 SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS01055; DNA_LIGASE_N1; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000232323};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 746..817
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 695..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 824 AA; 88539 MW; 78373EF540CDCF33 CRC64;
MQASVIRISP GGWFPPQNRF INMTLNHRII NVPFFLGWTA RQHEGGNVSN VTCPSQLSRG
SASHIQNSVD INYDELNRLR AQVVHHDQLY HSQGAPEISD DAYDALKARL KLMESVTPAS
SSSHPAPVGS YPTPSALTKI KHMVPMLSLL SVKSVQEVNE WHRKLLTKLP ADWSLGGTSG
QILSWMVEPK VDGLALSLLY RDGRLVQAAT RGDGATGENV THNASVIKGI PLAMEAAGSK
EVQGILEVRG EVYMLREDLE KVNQEQVSSG LSTFANTRNA AAGSLRLLDP ATCAARRLSF
FAYQLLTQPL PNIEIEGLEA SSHEGSLAAF PVGIQTQSGC LDWLSSQGFA TSSDNLLCTD
GLENALKAAQ EWMEGRNALG YEVDGVVLKL NELRLQSLLG HSGADPEWAI ALKFPAQEAF
TKLTGLSVNV GRSGQVIPVA ELEPVSINGV SISRATLHNI GVVQSLDVRV GDTVLVKRAG
DVIPQVVMPM VEMRTGTEVP WQAPACCPCC GQGLVIEGGK GDNALSLWCK NPVCGGQSAQ
LILHFAKTCL VGSNLGIGIV TQLMEAGLLT SIVDFFTLTE EKLLTLPNFG QKRAAQVVTG
IASAAEHMTC ATLLAGLGVP TVGHKTSKDL ERAFDGNFQR VQSASLEQLT TIPGIGPKTA
ASLISWFQNP ANMEMLRHLE LCGLSCMSPL KARSSKGTRE SISSKRTSLD SSSTSVTGLI
GERNAQYREE MRSEELPDEI CSLSGLEGKT FVMTGSLSVR TLSRKQFSDL LSAHGAALID
TVTTKVDAVL FGEKPGKSKI EKAKKCGVAL MSEKEFWDTY GRDG
//
