ID A0A0D1Z7P2_9EURO Unreviewed; 940 AA.
AC A0A0D1Z7P2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=PV11_04911 {ECO:0000313|EMBL:KIV82838.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV82838.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV82838.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV82838.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) 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 -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|RuleBase:RU004196}.
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DR EMBL; KN846952; KIV82838.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1Z7P2; -.
DR STRING; 1016849.A0A0D1Z7P2; -.
DR HOGENOM; CLU_005138_0_1_1; -.
DR OrthoDB; 961at2759; -.
DR Proteomes; UP000053599; Unassembled WGS sequence.
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:0006310; P:DNA recombination; 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; cd07900; Adenylation_DNA_ligase_I_Euk; 1.
DR CDD; cd07969; OBF_DNA_ligase_I; 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; IPR000977; DNA_ligase_ATP-dep.
DR InterPro; IPR012309; DNA_ligase_ATP-dep_C.
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; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR00574; dnl1; 1.
DR PANTHER; PTHR45674:SF4; DNA LIGASE 1; 1.
DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR Pfam; PF04679; DNA_ligase_A_C; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 2.
DR Pfam; PF04675; DNA_ligase_A_N; 1.
DR SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR PROSITE; PS00333; DNA_LIGASE_A2; 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|RuleBase:RU000617};
KW DNA repair {ECO:0000256|RuleBase:RU000617};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000617};
KW Reference proteome {ECO:0000313|Proteomes:UP000053599}.
FT DOMAIN 666..803
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 92..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 940 AA; 103765 MW; 4909ACAC073B8626 CRC64;
MQLMTKAASK TSQAVTSLLF ILHGTCRLSG VGNTVARAQS LPRPSYPYRP RYRSGRPLCT
IVGLAKPAAM PQPRQSTLGK FLGNKQDGIK AKSQSTLSFG QKPTAKKDDA SSEIGDADVQ
NGKNATPDTD MKDANEGSIE ADEVCDDTTS KKHKRRTSPV QEEEDDSDDQ PVVKKRRRMS
NPRPSSKDGL KNSTPKANGI KAGIKADAMP EEESLKSSKP THGDSALSDD DKSPSEPEEV
SSSSESEKPR VNKKQVAKLQ ATIKSSGKDP YPDWKAGEPA PYAALCTTFS LIELTTKRLQ
ITAYCSAFLQ QVLRLTPQDL LPTIQLMLNK LAADYAGIEL GIGESLIMKA IGESSGRSLS
VIKADHQKIG DLGLVAAKSK SKQGQMFKPK ALTVRGVHQG LLDIAKMEGH GSQDQKVRAI
NKLMASADVS SASKQVDITK DKGGPSEAKF LVRFLEGKLR LGLAEKTVII ALAQAVVTHE
AAKKGKVPST DQLAKGEAQL KTVYSELPSY EVIVPAMLEH GISNLHESCK LQPGVPLKPM
LAKPTKSITE VLDRFEGKNF TCEYKYDGER AQIHYVAPEA MADFPAAKNT LTKDAKSFKG
LAAIFSRNSE DLSKKYPDIL EKLNTWIKPS TKSFVLDCET VAWDPQNKKV LPFQQLMTRK
RKDVKTSEVT VKVCVFAFDM LFYNGEPLVK KTLRERRELL HEAFEPTEGE FAFAQHGDAM
DIEEIQHLLD DSVKASCEGL MVKMLDTEES GYEPSKRSRN WLKVKKDYLS GIGDSLDLVV
LGAYHGKGKR TSWFGAFLLA AYNPETQMFE TVCNIGTGFS EAVLEEFHKD LSDIIIERAK
PFYSHSTTKN DQPDVWFEPR YVWEVKTADL TLSPRYRAAI DEMGGKNGIS LRFPRFIQKR
EDKKPEDATT TKAIAEMYRK QEVVAKDGHG KGGVDDDFEY
//
