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Database: UniProt
Entry: A0A163LDL0_DIDRA
LinkDB: A0A163LDL0_DIDRA
Original site: A0A163LDL0_DIDRA 
ID   A0A163LDL0_DIDRA        Unreviewed;       649 AA.
AC   A0A163LDL0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=DNA ligase (ATP) {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ST47_g1125 {ECO:0000313|EMBL:KZM27699.1};
OS   Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS   rabiei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX   NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM27699.1, ECO:0000313|Proteomes:UP000076837};
RN   [1] {ECO:0000313|EMBL:KZM27699.1, ECO:0000313|Proteomes:UP000076837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ArDII {ECO:0000313|EMBL:KZM27699.1,
RC   ECO:0000313|Proteomes:UP000076837};
RX   PubMed=27091329; DOI=10.1038/srep24638;
RA   Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT   "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT   Ascochyta rabiei provides insight into the necrotrophic effector
RT   repertoire.";
RL   Sci. Rep. 6:24638-24638(2016).
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:KZM27699.1}.
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DR   EMBL; JYNV01000060; KZM27699.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A163LDL0; -.
DR   STRING; 5454.A0A163LDL0; -.
DR   Proteomes; UP000076837; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   CDD; cd07905; Adenylation_DNA_ligase_LigC; 1.
DR   CDD; cd04865; LigD_Pol_like_2; 1.
DR   CDD; cd07970; OBF_DNA_ligase_LigC; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 3.90.920.10; DNA primase, PRIM domain; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR044119; Adenylation_LigC-like.
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; IPR014145; LigD_pol_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR044117; OBF_LigC-like.
DR   PANTHER; PTHR42705:SF3; -; 1.
DR   PANTHER; PTHR42705; BIFUNCTIONAL NON-HOMOLOGOUS END JOINING PROTEIN LIGD; 1.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF21686; LigD_Prim-Pol; 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.
PE   4: Predicted;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076837}.
FT   DOMAIN          6..202
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|Pfam:PF01068"
FT   DOMAIN          221..317
FT                   /note="DNA ligase ATP-dependent C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04679"
FT   DOMAIN          337..592
FT                   /note="DNA ligase D polymerase"
FT                   /evidence="ECO:0000259|Pfam:PF21686"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          620..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        634..649
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   649 AA;  71879 MW;  AA785D2FC1D47EC0 CRC64;
     MPPLAPMLAK AAATVPPQPE SGDPTWSYEP KWDGFRAIIF RDGDEVVLGS RGGKDLARYF
     PEAVEAVKSE LPEKCVVDGE LVVPREIDGV TRLSWEALSE RIHPAASRVA LLSEQTPAQF
     VGFDLLALGD RDVSIEDFGV RRALLLDCVG GGPSCHVTAA TADSAEAMAW FETFEGAGLD
     GVVAKKLAGP YLPNKREMIK VKHARTADVV LLGYRPHKSQ PGIGSMLLGL YDGSELKMVG
     GASAFTAARR IELLAELEPL RLGDDVVAEG EASRWRSAAD RSWIPLRPER VLEVAYDQME
     GERFRHAARF LRWRPDRVPD ECTFDQLEVP LGEDGGTKRH LVEYYRTVAL QGAALRALQD
     RPTHLQRFPD GIEGEEVYQK RLPAKRPEHV ESCEVTFPSG RKADVLRVRS AANIVWAANL
     GTVTFHPWAV RCPDTDHPDE LRIDLDPQPG TGFDEAVAIA DEVLRPLLAE LGLEGFPKTS
     GGRGLHVYIP LEARWDFVEV RHAGIALARE VERRSADRAT TAWWKEERGE RIFIDFNQNA
     RDRTIAAAYS ARKTPIATVS TPVTWDELRD VHPDDCTIAT VPGLLADRGD PMEAMHDKAF
     ALDVLLEMWE KDLAAGLGDL PYPPNYPKMP GEPKRVQPSK DRDRKNKDG
//
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