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Database: UniProt
Entry: L8WJ26_THACA
LinkDB: L8WJ26_THACA
Original site: L8WJ26_THACA 
ID   L8WJ26_THACA            Unreviewed;       526 AA.
AC   L8WJ26;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=ATP dependent DNA ligase domain-containing protein {ECO:0000313|EMBL:ELU36798.1};
GN   ORFNames=AG1IA_09177 {ECO:0000313|EMBL:ELU36798.1};
OS   Thanatephorus cucumeris (strain AG1-IA) (Rice sheath blight fungus)
OS   (Rhizoctonia solani).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX   NCBI_TaxID=983506 {ECO:0000313|EMBL:ELU36798.1, ECO:0000313|Proteomes:UP000011668};
RN   [1] {ECO:0000313|EMBL:ELU36798.1, ECO:0000313|Proteomes:UP000011668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG-1 IA {ECO:0000313|Proteomes:UP000011668};
RX   PubMed=23361014; DOI=10.1038/ncomms2427;
RA   Zheng A., Lin R., Xu L., Qin P., Tang C., Ai P., Zhang D., Liu Y., Sun Z.,
RA   Feng H., Wang Y., Chen Y., Liang X., Fu R., Li Q., Zhang J., Yu X., Xie Z.,
RA   Ding L., Guan P., Tang J., Liang Y., Wang S., Deng Q., Li S., Zhu J.,
RA   Wang L., Liu H., Li P.;
RT   "The evolution and pathogenic mechanisms of the rice sheath blight
RT   pathogen.";
RL   Nat. Commun. 4:1424-1424(2013).
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|ARBA:ARBA00001968};
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:ELU36798.1}.
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DR   EMBL; AFRT01003050; ELU36798.1; -; Genomic_DNA.
DR   AlphaFoldDB; L8WJ26; -.
DR   STRING; 983506.L8WJ26; -.
DR   HOGENOM; CLU_021047_1_0_1; -.
DR   OMA; VGWWISE; -.
DR   Proteomes; UP000011668; 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:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd07896; Adenylation_kDNA_ligase_like; 1.
DR   CDD; cd08041; OBF_kDNA_ligase_like; 1.
DR   Gene3D; 3.30.1490.70; -; 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; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR029319; DNA_ligase_OB.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR007527; Znf_SWIM.
DR   PANTHER; PTHR47810; DNA LIGASE; 1.
DR   PANTHER; PTHR47810:SF1; DNA LIGASE B; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF14743; DNA_ligase_OB_2; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
DR   PROSITE; PS50966; ZF_SWIM; 2.
PE   4: Predicted;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000313|EMBL:ELU36798.1};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00325};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011668};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00325};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}.
FT   DOMAIN          36..78
FT                   /note="SWIM-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50966"
FT   DOMAIN          197..237
FT                   /note="SWIM-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50966"
FT   DOMAIN          386..458
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          82..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          177..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..191
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   526 AA;  58189 MW;  79101C97F86B1C1E CRC64;
     MSDPLAVLSG GEIPKRLLAD GESVEVTGSS KSRSKYTIKR TDTHYYCSCK KFRNLCFCGV
     KVELRTCKHL KELLGDAYEV ARTSSNKPAP KPADRTQSTK KARLPPSSNS SAPSGSSTRS
     TRASKRKYSD DEPAEDQKND EDVPKASADN EDAANINPHT PATDVDDLAE INGIKPKVYM
     RDGEEREAKS QTSSSTYKIK RTWDHYYCTC PAWRNQGGVP VNARSCKHIK SILGEEYEAA
     RAKLKNPDGS NSPSCKDSRP SKRAKKDGAN SSGNGGGSTK TVPQLLLAVK WDLATGCDPT
     GWWMSEKLDG VRVYYDGKKM WSRLGNPFTP PQEFLDRLPK DVTLDGELFG GRGKFQDTVS
     IVKTVNSPHW KNITFQIFDI PSRGSEPFEE RVTYLKKHFQ NIPQVNVVEQ TMCKSRDHLL
     ETLKDVEHDG GEGVMLRQPG SEYEGKRSSS LLKVKTFYDG EAEVVGYEPG KGKHKGVTGA
     LKCVMASGKK FSVGSGLTDK QRRVPPKVGA IVTYRFQELT RDGVPR
//
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