ID A0A1S7UNI0_ROSNE Unreviewed; 980 AA.
AC A0A1S7UNI0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=SAMD00023353_3900280 {ECO:0000313|EMBL:GAP84994.1};
OS Rosellinia necatrix (White root-rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX NCBI_TaxID=77044 {ECO:0000313|EMBL:GAP84994.1};
RN [1] {ECO:0000313|EMBL:GAP84994.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W97 {ECO:0000313|EMBL:GAP84994.1};
RA Kanematsu S.;
RT "Draft genome sequence of Rosellinia necatrix.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|RuleBase:RU004196}.
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DR EMBL; DF977484; GAP84994.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S7UNI0; -.
DR STRING; 77044.A0A1S7UNI0; -.
DR OMA; RDFSCEY; -.
DR OrthoDB; 961at2759; -.
DR Proteomes; UP000054516; 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:UniProtKB-EC.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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; 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; 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; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR00574; dnl1; 1.
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; 2.
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|RuleBase:RU000617};
KW DNA repair {ECO:0000256|RuleBase:RU000617};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000617};
KW Reference proteome {ECO:0000313|Proteomes:UP000054516}.
FT DOMAIN 580..787
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..980
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 980 AA; 106628 MW; 892EA6BB969E5656 CRC64;
MASPAKKRKL NSDSKNSLPS RGLEYFFAKQ RDQNGTGSAV PKGNGQAQER DAVHPAQDDE
MTDEELARKL QAEWDREERM ARGATASNTG QPGNSRVPSH NPQPDEGDVG PHAHGIPFEP
PKMNIVVASN KGGEKESGKG KGTLSLQSVA TSVDTISETI PFDESPLTFD PNEYLPQLQE
HWARDNGNAS YALLTRCFVL VSGTSSRIKI VDTLVNCLRV LIEGDPESLL PAVWLSTNAI
SPPYKSLELG LGGSAISKAL RQVCGLDNRS LKAIYDRHGD AGDVAFEAKK KQSLTLRAPR
PLTIRGVYDS LVRIAAAQGP GSAEAKQRLV DRLLRDARGG EESRYVVRTL CQHLRIGAVK
TTLLIALSRA FLLSRRPSPP TSTTTTATTT TSSAGVGDGG GNTDEYPLRS AADLRRLRKE
ELAEVWGRGE EIVKACFARR PDYDELVPAL LDVGVGPALL ARCALGPHVP LRPMLGSITR
DLAEMLTRLQ GGRGFACEFK YDGQRAQVHC DDAGKVSIFS RHLELMTDKY PDLVALVPRI
RGEGVGSFIM EGEVVAVDQA TGDLKNFQTL TNRARKDVAI GSITIDVCLF AFDLMYLNGQ
PLLDRPFRER RSLLRSLFTE IPNRFTWVRS LDATPEDSEA VLDFFKQATD HKCEGIMVKI
LDNLPHPPAP LPSAAAAGDD RGAASQQPGN GTGRAKSGKG KSKASVAAAK DGDGEKQPPP
PPPATKPTRR KPLLATYEPD KRLDSWLKVK KDYSASFDTL DLVPVAGWHG QGRKARWWSP
ILLAVRDEET GSLEAVCKCM SGFTDAFYKA NRRFYDDGSG DPDTGASASS VRGVRAGGEH
AEDADGEGGD RSDAGNDDDE DGSQGREYKN IRKSKPGFVE YAGHPDVWFE PQEVWEVAFA
DITLSPTYTA AIGLASQDRG LSLRFPRFLR KREDKGIEEA STNEFLAGLF RKQEAKAPPP
TTNGEGDDDD EEEEEEENDA
//