ID   X0D0S7_FUSOX            Unreviewed;      1011 AA.
AC   X0D0S7;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=ATP-dependent DNA ligase family profile domain-containing protein {ECO:0000259|PROSITE:PS50160};
GN   ORFNames=FOQG_00587 {ECO:0000313|EMBL:EXL00391.1};
OS   Fusarium oxysporum f. sp. raphani 54005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXL00391.1, ECO:0000313|Proteomes:UP000030663};
RN   [1] {ECO:0000313|EMBL:EXL00391.1, ECO:0000313|Proteomes:UP000030663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54005 {ECO:0000313|EMBL:EXL00391.1,
RC   ECO:0000313|Proteomes:UP000030663};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum PHW815.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|ARBA:ARBA00007572}.
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DR   EMBL; JH658362; EXL00391.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0D0S7; -.
DR   eggNOG; KOG0967; Eukaryota.
DR   HOGENOM; CLU_004299_4_0_1; -.
DR   Proteomes; UP000030663; 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:InterPro.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd08039; Adenylation_DNA_ligase_Fungal; 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; IPR012310; DNA_ligase_ATP-dep_cent.
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   PANTHER; PTHR45997:SF2; ATP DEPENDENT DNA LIGASE DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_5G02430); 1.
DR   PANTHER; PTHR45997; DNA LIGASE 4; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030663}.
FT   DOMAIN          384..524
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          679..814
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        679..710
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        731..746
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        759..784
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1011 AA;  113597 MW;  30B0172CCE9D3245 CRC64;
     MPLPFSLVCE LLEQSFLLSL DKKSCSNTVT KWFTRHRNYV DAHDTNLPAL LSTLLPEKRT
     DRVYCIQSAS LERIIGRAYL LGLSRIKELA QYHQPGSGVD LADCVFRILT VTPSPSYDHK
     NLVTVEEIDQ LLHSLAAKIK WSSPSIRASQ ASLTPSNRTD LESLYRRLSA TEAKWFTRLV
     LKSYQPLVLD PYLIYRLCDP ILPCVVKIQD DFATAITSLQ AIRGRLLPNA GRKTPREQIM
     GTVKPQLGVK IGRQPWVKGR SIKHCLDMGH GRMSVEEKID GEYCQIHVDP SKVDKCIQIF
     SKSGKDSTED RVALHGIIQE SLKIGQPDTR VKKACILEGE LVVYDDSQEK ILPFHSIRKH
     VSRRGRFLNT ELDSLPGPQE HLMVIYYDVM LLEDQSLINL RHSERFKILS NLVCCRKGWA
     GLVPRQVIDF GQPLGASTLR KAFAMVILAW KEGLVLKPDE PYFDFTDQRR RFSSCCIKLK
     KEYIGNFGDV GDFSVVGARY DSTKALSYRI PGLKWTHFYI GCLDNREAVK SWGAKPEFTI
     VNVVELNETI LREVVTYSNP EPVSPDDNGA LALKLAPGVE QGSPPTFIFT KPLVFDLKCF
     SFDRVGNTGF WSLRFPSVTK VHFDREFTDT ISFEQLQALA KEATTAGKLE DSQENLQWIA
     KLEAADPRGI AVDAASQLTV TTMPTPSPRK STQNTTSTWS PKSPLATKSP VQVSPCRGRR
     ERVHRVPSLD LPSITATTSL RTEPSSPTKL CAKHKRGLPS TGPTSQHKRL KSSSKTSISQ
     KDYPHIDIAS QPRAPLAARD NNPRPQPAKS SCAPCCPSSP SESFFDESSN SDGVNAEVVK
     FIINPGTGEL QTETNPERLK PSTTKVTTAL KRKCVYAGED CMLANAVVLF LPGLLAMKEA
     KKLLAQHGVD APVTDIDTWL KAEKEARQKG KITIPSKAYV VCDSDNKLVF KHLAEKFKEL
     RKDNLFNKGT HIEIHDWRFL SYLTTQEDES IEEKYFHGFS DWRMRWKLHT I
//