ID A0A0C3ACH6_9AGAM Unreviewed; 1010 AA.
AC A0A0C3ACH6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=SCLCIDRAFT_1214942 {ECO:0000313|EMBL:KIM62592.1};
OS Scleroderma citrinum Foug A.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Sclerodermataceae;
OC Scleroderma.
OX NCBI_TaxID=1036808 {ECO:0000313|EMBL:KIM62592.1, ECO:0000313|Proteomes:UP000053989};
RN [1] {ECO:0000313|EMBL:KIM62592.1, ECO:0000313|Proteomes:UP000053989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Foug A {ECO:0000313|EMBL:KIM62592.1,
RC ECO:0000313|Proteomes:UP000053989};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Foug A {ECO:0000313|Proteomes:UP000053989};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA ligase involved in DNA non-homologous end joining (NHEJ);
CC required for double-strand break (DSB) repair.
CC {ECO:0000256|ARBA:ARBA00043870}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN822041; KIM62592.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3ACH6; -.
DR STRING; 1036808.A0A0C3ACH6; -.
DR HOGENOM; CLU_004844_1_0_1; -.
DR InParanoid; A0A0C3ACH6; -.
DR OrthoDB; 8251at2759; -.
DR Proteomes; UP000053989; Unassembled WGS sequence.
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; cd18435; BRCT_BRC1_like_rpt1; 1.
DR CDD; cd17722; BRCT_DNA_ligase_IV_rpt1; 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; 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; 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; PF16589; BRCT_2; 1.
DR Pfam; PF04679; DNA_ligase_A_C; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 1.
DR Pfam; PF04675; DNA_ligase_A_N; 1.
DR SMART; SM00292; BRCT; 2.
DR SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
DR SUPFAM; SSF52113; BRCT domain; 2.
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; 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|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 Reference proteome {ECO:0000313|Proteomes:UP000053989};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 370..504
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 664..760
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 900..1010
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1010 AA; 114649 MW; B5C917A846820048 CRC64;
MQPTPAPSSR PGSPRPRPAE STGYPAPPQN RGSAPFSVLA GLFEKLATER KPDRRKRMLS
VWFSRWREQV GNDLYPALRL ILPQKDRERA VYGLKEKNIG KMYIKLIPLG MRDPDAIRLL
NWKKPIGTNQ AAGDFPTVLY DVVNTRSSVV EGSLSVNDLN GLLDELSENM GKQDAQAKIM
QRIYNRTTAE EQRWIVRIIL KDMIISVKET TVFAVFHPDA EDLFNTCSDL KKVAWELSDP
SHRLNPEDKA IQLFRAFAPM LCKRPTHKIE DSVKEMQGRT FIIEEKLDGE RMQLHRRGNE
YFYCSRKGKD YTYLYGKHVG QGSLTPYIDA AFDTRIDDII LDGEMLVWDP ISERLLPFGT
LKTAARDTSK QALSPRPCFK VFDLLYLNGM SLHKKSLKFR KHNLRACIKE IPGRMEFVTE
FEGKTAKDIR NKMDEIMATR GEGLILKHPG SEYILNGRNK DWIKVKPEYM DNMGETVDVL
VVGGNYGTGK RSGGVSTLLC AVLDDRRVSD DDEPKYSTFV RIGTGLSFAD YVWVRQKPWK
TWDPKNPPEF LQTTKRGHED KCDVYIEPAD SFILKVKAAE ITTSDEYHLG VTMRFPRALS
VREDLSIADC MTASAVLESI RAERKRKMES EASMDDRKKR KKVTTKKPTV MPQFQGPDLS
SVEMESHIFK DMKFMVSADP KSRTGDHDRK ELMKLVHAHG GTCVQVITSQ QPALAVYGGT
TTPYDIKLLV TNGKVDIIRP QWVLDCIARE ELIPLRKKYF FHASDDRQLS AEYNQPDTDE
DYEMVDGTQE RGASVKISTL SESSVKALAE EVDPTLAEWL TVDAKPSGQD GSETESETDA
DSVNDDAKAE SEEWFPVELR GTDDLNETLE EAKEHHETGA VEKPDVQDVT MGEEGAHEYD
PALIFRHLCF YLDTPQGAGE NGMTVNTKYE KEITEHFNKV LREIEANGGK VVGLDDPKLT
HIVLDKRDTS RRLSLMQWTA KPKRRRLVVS DYISACLDEE TLLDEEDFAP
//
