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Database: UniProt
Entry: A0A0A2WCJ9_BEABA
LinkDB: A0A0A2WCJ9_BEABA
Original site: A0A0A2WCJ9_BEABA 
ID   A0A0A2WCJ9_BEABA        Unreviewed;       853 AA.
AC   A0A0A2WCJ9;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=DNA ligase 3 {ECO:0000313|EMBL:KGQ10689.1};
GN   ORFNames=BBAD15_g3982 {ECO:0000313|EMBL:KGQ10689.1};
OS   Beauveria bassiana D1-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ10689.1, ECO:0000313|Proteomes:UP000030106};
RN   [1] {ECO:0000313|EMBL:KGQ10689.1, ECO:0000313|Proteomes:UP000030106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-5 {ECO:0000313|EMBL:KGQ10689.1,
RC   ECO:0000313|Proteomes:UP000030106};
RA   Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA   Du Q., Sun Z.;
RT   "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT   bassiana D1-5.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|ARBA:ARBA00007572}.
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:KGQ10689.1}.
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DR   EMBL; ANFO01000291; KGQ10689.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2WCJ9; -.
DR   STRING; 1245745.A0A0A2WCJ9; -.
DR   eggNOG; KOG0967; Eukaryota.
DR   HOGENOM; CLU_005138_1_1_1; -.
DR   Proteomes; UP000030106; 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:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd07900; Adenylation_DNA_ligase_I_Euk; 1.
DR   CDD; cd07969; OBF_DNA_ligase_I; 1.
DR   Gene3D; 3.30.1490.70; -; 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; 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; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR45674:SF9; DNA LIGASE 3; 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; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 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.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KGQ10689.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030106}.
FT   DOMAIN          539..710
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          617..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          833..853
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   853 AA;  95059 MW;  C919B025B8DCFB67 CRC64;
     MSSPAKKRKL NNAVKSDKSQ SKGLEYFFTK QKQTKNGSTA APRSSHSETD DAALTDEELA
     RKLQAEWDKE SARADNQEPN AVEMATNESN VQDCDIVEVS KEQQTDAPKQ PSPVAVFGGK
     KTLALQSAGM DEDSITISIP LDEPPLTFEP SKYVSQLKEH WSRDGGNASY ALLTRCFVLV
     SGTASRIKIV DTLVNCLRIL IEGDPESLLP AVWLATNSIS PAYISMELGL GGSAISKALK
     QTCGLDGRSL KTLYDKYGDA GDVAFEAKKK QSFTLRKPKP LSIKGVFQSL VKIATTQGQG
     SNEIKQRIVD RLLQDARGGE ESRFIVRTLC QHLRIGAVKT TMLIALSRAF LLSKPTQADY
     ETRNIPALAK LKKEELAEIW VKAEEIVKAC FAKRPNYNDL IPNLLEIGVC EELLVRCGLA
     LHIPLRPMLG SITRDLSEML TKLQGRDFTC EYKYDGQRAQ VHCDEGGKVS IFSRHLELMT
     DKYPDLVELV PKIRGDGVSS FIMEGEVVAV DSASGELKNF QALTNRARKD VEIGSITVQS
     LLERPFRERR ELLRSLFIEV PNRFTWVKSL DATSSESESV LSFFKSATER KCEGIMVKIL
     DNLPDVAYLG DEDGEIKEQE PKLQIPKSKS KAKGKKKPED GESNEPAKKK SRRKALLATY
     EPDKRLDSWL KVKKDYNSSF DTLDLIPIAG WHGQGRKAKW WSPILLAVRN EESGMLEAVC
     KCISGFTDVF YKANKAFYDD GSETGEPKNT HLQMPSFIEY SGPMPDVWFE PQEVWEMAFA
     DITLSPTYTA AIGLVSDERG LSLRFPRFLK KRDDKGIEEA STNEFLAGLW RKQEVSASTT
     GPAKPMEEDE EAE
//
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