ID B8P0P1_POSPM Unreviewed; 980 AA.
AC B8P0P1;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=POSPLDRAFT_96457 {ECO:0000313|EMBL:EED85575.1};
OS Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS (Poria monticola).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Postiaceae; Postia.
OX NCBI_TaxID=561896 {ECO:0000313|Proteomes:UP000001743};
RN [1] {ECO:0000313|EMBL:EED85575.1, ECO:0000313|Proteomes:UP000001743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44394 / Madison 698-R {ECO:0000313|Proteomes:UP000001743};
RX PubMed=19193860; DOI=10.1073/pnas.0809575106;
RA Martinez D., Challacombe J., Morgenstern I., Hibbett D., Schmoll M.,
RA Kubicek C.P., Ferreira P., Ruiz-Duenas F.J., Martinez A.T., Kersten P.,
RA Hammel K.E., Vanden Wymelenberg A., Gaskell J., Lindquist E., Sabat G.,
RA Splinter BonDurant S., Larrondo L.F., Canessa P., Vicuna R., Yadav J.,
RA Doddapaneni H., Subramanian V., Pisabarro A.G., Lavin J.L., Oguiza J.A.,
RA Master E., Henrissat B., Coutinho P.M., Harris P., Magnuson J.K.,
RA Baker S.E., Bruno K., Kenealy W., Hoegger P.J., Kuees U., Ramaiya P.,
RA Lucas S., Salamov A., Shapiro H., Tu H., Chee C.L., Misra M., Xie G.,
RA Teter S., Yaver D., James T., Mokrejs M., Pospisek M., Grigoriev I.V.,
RA Brettin T., Rokhsar D., Berka R., Cullen D.;
RT "Genome, transcriptome, and secretome analysis of wood decay fungus Postia
RT placenta supports unique mechanisms of lignocellulose conversion.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(2009).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EQ966237; EED85575.1; -; Genomic_DNA.
DR RefSeq; XP_002469273.1; XM_002469228.1.
DR AlphaFoldDB; B8P0P1; -.
DR STRING; 561896.B8P0P1; -.
DR KEGG; ppl:POSPLDRAFT_96457; -.
DR HOGENOM; CLU_004844_1_0_1; -.
DR InParanoid; B8P0P1; -.
DR OMA; DYLWIRD; -.
DR OrthoDB; 8251at2759; -.
DR Proteomes; UP000001743; 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 CDD; cd07968; OBF_DNA_ligase_IV; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 2.
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 SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
DR SUPFAM; SSF52113; BRCT domain; 2.
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:UP000001743};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 335..478
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 642..738
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..836
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 980 AA; 112218 MW; 7CD313ECF3FF83B8 CRC64;
MLPTPAPTSP PSSPRPEVTA AAEDHPIVYP PPPPTRGSAP FQVLAALFDK LQGERRPEKR
RRLLDSWFNK DRERAVYGLK EKNLAKIYIK LIPLNPRDPD AIRMLNWKRP TERNQSSGDF
PSVLYEVISK RSSVVEGTLT IHELNDHLDE ISKNMGHSTT SEEQRWIARI ILKDMQISVK
ETTVFAVFHP DAHALFNTCS DIKKIAWELW DPKRKLNDEV HLSPLRRIED TVKEMQGSNF
IIEEKLDGER VQLHKRGNEY FYCSSSWATN RKGKDYTYLY GKHVGEGSLT PWIHKAFDAR
VDEIILDGEM LVWDPVSERN LPFGTLKTAA LDRSKKERAP RPCFKIFDLL YLNGTPLLNK
SLKFRKRNLR ACLKEVPGRM EFAVEYEGRT ADDVRTRMED IMASRGEGLV IKHPNSQYVL
SGRNSDWIKA SCWTRGFNVK PEYMDSMGET VDVIVVAGNY GTGRRSGGVS TLVCAVVDDR
RPADEVEPKY STFVRIGTGL SYADYIWVRQ KPWKTWDPKN PPSFIQVAKK GSEDKGDVYL
EPQDSFLLKI KAAEITNSDL YHMGVTMRFP RAIQIREDLD TSDCTTATAV FESLRSDRKR
KMSDTDELSD CVNPKKKQRR TTKKPVILLP QYQSLKLEDV EVESDLFEGM TFMVSSDPKS
RTGEQDKKEL LRMIRANGGK YVQMAKNNPD VLVVYGGTIT PYDIKLIMNR DVCDIIKPQW
IRESVTKSER MPLTKRYFFH ATSRRMEEDE YVQDDGSLEE LALTDQHEEP LETNDKGDAT
QEDPSIADWF KVEKSSNRSE IQHDDTDSET EPDSDNDDVN RDEDIADEDD ISDWVNVDNE
DSLKTEEDPV QDASESEPQV RMGETEEARE YDQELIFRHL CFYLDSPANA KKNSMSVKSK
NQDELNKGFE KLTTLITEHG GRVVDLDEPK LTHVVVDKRD LSLSSSRLAW TKKHCLMKMA
SAWQLALFLV LTPAPTEFAP
//
