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Database: UniProt
Entry: A0A0G4J096_PLABS
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ID   A0A0G4J096_PLABS        Unreviewed;       859 AA.
AC   A0A0G4J096;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=PBRA_001808 {ECO:0000313|EMBL:CEP00754.1};
OS   Plasmodiophora brassicae (Clubroot disease agent).
OC   Eukaryota; Sar; Rhizaria; Endomyxa; Phytomyxea; Plasmodiophorida;
OC   Plasmodiophoridae; Plasmodiophora.
OX   NCBI_TaxID=37360 {ECO:0000313|EMBL:CEP00754.1, ECO:0000313|Proteomes:UP000039324};
RN   [1] {ECO:0000313|EMBL:CEP00754.1, ECO:0000313|Proteomes:UP000039324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E3 {ECO:0000313|EMBL:CEP00754.1};
RA   Chooi Y.-H.;
RL   Submitted (FEB-2015) 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; CDSF01000101; CEP00754.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4J096; -.
DR   STRING; 37360.A0A0G4J096; -.
DR   EnsemblProtists; CEP00754; CEP00754; PBRA_001808.
DR   OMA; WIKYKRD; -.
DR   OrthoDB; 961at2759; -.
DR   Proteomes; UP000039324; 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; 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; 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:SF4; DNA LIGASE 1; 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 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, 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:UP000039324}.
FT   DOMAIN          600..739
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          40..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..168
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..187
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   859 AA;  95268 MW;  75B3CAE2B5ECC722 CRC64;
     MTARWGIAFV GREQPYSRRY GCASEGGCRS ACSQKRSILR QRDLRAGSPM TTTATKKKKQ
     ASLASFFSAK GNASEQCAEG DTATDDSAKA VSINAGDRSE PDATVEEPAP KRAKLQGAPA
     DHPEQTSSAK GQKLRRRVIE SDDDDGGDAR AEADNLQTAE RTDSEIDDEG SAGVASDGDE
     VVESEDDSPV EPSTTKRKST VSSKKELSAS SVPVRVSKYD PIADADWPAG KDLPYIHLAR
     LFNKLENESS RLAKIDLVTN FLRSVIVKTP DALTAVIYLC VNKLGPDYEG LEIGVGDGLL
     VKVLASSTGR SAKVIQQDLR ESGDLGLIAE RCRSTQRTIF PPPPLTVMKL LATFRRIASE
     KPDKKMGSIK QLLVSSRECE ARYITRSFQG NLRIGCSLRT VLPSLARACT VTPPLTPEER
     SEPLNSLEET RLDRSLHWSD TKLSTAIQTA TSIVNRVWVE VPNLDKIVSA ILAYGVEHLR
     EHCYLTPGIP IKSMLAAPAK SISEVLSNFE GHEFVLEYKY DGERAQIHYL DDGSVQIFSR
     NAECTTNKYP DLVSMLPRAF KTDVVKSCIL DSEVVAFDRL TRKIRPFQIL STRKRKDVTE
     ESIKVDVCVF VFDIIYLNGE SLLDYPLVER RSKMRECLAE IDDQLRFVIE KRTSDEADIQ
     TFLDEAVADN CEGLMVKCLD GDAALSHYEP DKRSHAWRKL KKDYLEGLTD SFDLVPIGAY
     HGKGKRTGSY GGYLLAVYDA DSEEFQSVCK IGTGFSDEVL QKLTADMEPH ILEVPRSYYR
     YSDKDVPDVW LDGHQVWEVR AADISISPAH KAAVGIVHDS KGVALRFPRF VQVRPDKRPE
     DATTSEQIAE LYNNQVNRQ
//
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