ID G7DXX7_MIXOS Unreviewed; 1026 AA.
AC G7DXX7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN Name=Mo02090 {ECO:0000313|EMBL:GAA95437.1};
GN ORFNames=E5Q_02090 {ECO:0000313|EMBL:GAA95437.1};
OS Mixia osmundae (strain CBS 9802 / IAM 14324 / JCM 22182 / KY 12970).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; Mixiomycetes;
OC Mixiales; Mixiaceae; Mixia.
OX NCBI_TaxID=764103 {ECO:0000313|EMBL:GAA95437.1, ECO:0000313|Proteomes:UP000009131};
RN [1] {ECO:0000313|Proteomes:UP000009131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 9802 / IAM 14324 / JCM 22182 / KY 12970
RC {ECO:0000313|Proteomes:UP000009131};
RX PubMed=21478649; DOI=10.2323/jgam.57.63;
RA Nishida H., Nagatsuka Y., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic basidiomycete Mixia osmundae.";
RL J. Gen. Appl. Microbiol. 57:63-67(2011).
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 -!- 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:GAA95437.1}.
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DR EMBL; BABT02000062; GAA95437.1; -; Genomic_DNA.
DR AlphaFoldDB; G7DXX7; -.
DR STRING; 764103.G7DXX7; -.
DR eggNOG; KOG0966; Eukaryota.
DR HOGENOM; CLU_004844_1_0_1; -.
DR InParanoid; G7DXX7; -.
DR Proteomes; UP000009131; 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 Gene3D; 3.40.50.10190; BRCT domain; 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; 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 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; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000009131};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1026
FT /note="DNA ligase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003492491"
FT DOMAIN 459..598
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 762..852
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 34..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..918
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1026 AA; 115298 MW; 17C2FD3505024A0D CRC64;
MSVASTVPLK ILSLSALDVA VAVFPASASQ MSSPIASSSK VKLEDSPKKY NKFSPAKDSS
PSKRPAGTQE RGNSSSPAKR SKDFAELKAK DPLDDRPHHD PRLIPHGPSP RFGVLSDILD
VIQEKQASKR RKPEITDKYI LAIFANWRKD VGLDLYPLIR LLLPDKDRER NNYGLKENNL
AKVYTKALNL DKDTSAAQRL RDWKNPTQGG KARAGDFASI AKEVIQERSG VTEHVLTIDE
VNENLDRLAA ASGEKDKGKV IAWFNERMTA NEQRWLIGII LKDMKLSLGE KRVMKVLHPD
AMGLFNVCSD LKRVCWTLFD AEITLTKDDT VIRCNRHFRP MFCKRNEKDL GDVIRLMHLN
NPDQKFVIEE KLDGERIQLH KFGNNFRYWS RQGTDYTNLY GGNKYKGSLT PHIQEAFDSA
ISQIILDGEM LVYDPMMDKL CAFGTLKSAA KQNQEPTFSD GSAQRPCLRI FDILLVKGAD
GVVYNLAQYP LQKRKEALRT LVKPIKGYIE FAHAVEGASL DDIKREMDVV LQASGEGLVI
KHPLTLYLPG QRNEAWIKLK PEYMDALWED LDLIIVGAFL GEGRRGGMYG SFAVACLDDQ
LSTEDHKVYA NVAKVGSGFK YTDYVNFYSG DEFKNLWTKF PARGQPDPSS LKFGAEKPDY
YIDPAKSIVV TVKASSLVRD AVNYGAEVTL RFPRCTAIRT DKDIEDIETL TSVWERLTKR
KQRLGATTTK LDGHLRRRVQ KRKAVSSEAS GDSQLPRSES QLKSRIFKGL TFLVMEDGPT
ATKKQLEILV ATHGGEYRQV PPIEDNRRII AHRLNFHRVR RLSEKGETII RPEWVMDCVD
ARRKLPLLEE YVLHAGNVPI ESEEDLDKTP EEDDSASPID FIPDVPMRTY VSDSETDDDV
PRAASHGSVK EENDESVGAT RDVASMWSSR SFFASEAPED TGQLTLAADE PETMHYDNEQ
IFKHLVFYID TREAALANGL DVSPGSVSEN EDDAREAATL LISRGAKLAS NLDNVQIFTS
ERDYPN
//
