ID A0A0X8HRL6_9SACH Unreviewed; 951 AA.
AC A0A0X8HRL6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=AW171_hschr32034 {ECO:0000313|EMBL:AMD20157.1};
OS Eremothecium sinecaudum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=45286 {ECO:0000313|EMBL:AMD20157.1, ECO:0000313|Proteomes:UP000243052};
RN [1] {ECO:0000313|EMBL:AMD20157.1, ECO:0000313|Proteomes:UP000243052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58844 {ECO:0000313|EMBL:AMD20157.1,
RC ECO:0000313|Proteomes:UP000243052};
RA Dietrich F.S.;
RT "Genome sequence of the yeast Holleya sinecauda.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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; CP014243; AMD20157.1; -; Genomic_DNA.
DR RefSeq; XP_017987153.1; XM_018131664.1.
DR AlphaFoldDB; A0A0X8HRL6; -.
DR STRING; 45286.A0A0X8HRL6; -.
DR GeneID; 28723393; -.
DR OrthoDB; 8251at2759; -.
DR Proteomes; UP000243052; Chromosome iii.
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; 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; PF01068; DNA_ligase_A_M; 1.
DR Pfam; PF04675; DNA_ligase_A_N; 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 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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 381..500
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 688..786
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 849..950
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
SQ SEQUENCE 951 AA; 109726 MW; 667F1A6D0F159C93 CRC64;
MEKEEEESSP ELILEAESKP VNFSPSPDFV WLCNELFVKL EDASIKKNEL GKPRRLRLLE
IISHFYRLWR TTVGNDIYPA LILALPYLDK RTFRLKEATL VQAICRYLKL PRNSETEKRL
IYWKKNAPRG SKLSKSCVEE IQKRKKEYLG PSRLSIDKVN ECLDQLHHDS NVGKWGYIGL
SKSKTFRYCM EHMSFTEMRY FFDIILKVSV VGGLEGLLLR CWHPDAETYF KVVSDLRVVT
ETLWNQSKRL EKNDLTVRIG YPFSPQLALR LKKSDEDLAR GYKNDFMIEE KMDGERIQLH
YKDYGHTISY WSRNGINYTY LYGENQNLGS ISNCLQFVDG VKNCILDGEM VTYNRETNMI
LPFGLTKTSA GNQLTYEATG EYESSYRPLY MVFDLIYLNG KPLTALELWK RKEYLQKILV
PTENVVEILP FSRCSEASSI SASLGAAISR GSEGIILKDS HSKYLLGRRS DCWIKIKPEY
LENFGENLDL VIIGRIRGKK DSFICALAIV EDINANDDSL KIADMETTPE PHIVEPNIRK
FISFCSIANG ISNEEFKQIE RLTRGNWISY SENPPSTDWV EFGTKTPNEW IDPKHSIVLE
VKARSIDNEE VGKERYKTGS TLHGAYCRCI RYDKDWKTAC TLEEFKQARE AKEYYNHHYG
NSVVKSKKSP SKKREFHVVG TVEDSKVTGK RFLHGCHFYV LSGYFDKRFG IRVDNTMVAE
NIVAHGGTYV HNLNIRAGLG KLYILGGKLT RECKILIDRG YDIIHPSWLM DSVMYGTMLR
IEPRYIYNVG IEFMANVSAR VDEYNDSYQI PIECSEYEHI IGESKELLLS EESPALNTNT
VNEELPFLLF QRMNIFILAD DVHYQDRVDL IKWKIRAYQG ALTDDIANAN LIVAIEYNYS
KAGIEQVRHT VASLIGENIP GRPIPKITVD RWIEACIEEQ CLVDEEDYLA V
//