ID A0A0W8CQ00_PHYNI Unreviewed; 931 AA.
AC A0A0W8CQ00;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, 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=AM587_10011306 {ECO:0000313|EMBL:KUF86301.1}, AM588_10009363
GN {ECO:0000313|EMBL:KUF97529.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF86301.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|Proteomes:UP000052943, ECO:0000313|Proteomes:UP000054636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Race 0 {ECO:0000313|EMBL:KUF86301.1}, race 0
RC {ECO:0000313|Proteomes:UP000052943}, race 1
RC {ECO:0000313|Proteomes:UP000054636}, and Race 1
RC {ECO:0000313|EMBL:KUF97529.1};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-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}.
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:KUF86301.1}.
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DR EMBL; LNFO01002312; KUF86301.1; -; Genomic_DNA.
DR EMBL; LNFP01000110; KUF97529.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W8CQ00; -.
DR STRING; 4790.A0A0W8CQ00; -.
DR EnsemblProtists; KUF86301; KUF86301; AM587_10011306.
DR EnsemblProtists; KUF97529; KUF97529; AM588_10009363.
DR OMA; WIKYKRD; -.
DR OrthoDB; 961at2759; -.
DR Proteomes; UP000052943; Unassembled WGS sequence.
DR Proteomes; UP000054636; 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; PS00333; DNA_LIGASE_A2; 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:UP000052943}.
FT DOMAIN 647..797
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..96
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 931 AA; 104111 MW; EB678ADEF1A4A975 CRC64;
MAKRAAPKQS SIMSFFGAGA SPPAKKRKPA ENDAVKPAES PVTPAKKPKV EKEEKIEVVD
VVEEEQQQDE EDKQVEEEPE NVEMQEEEDV EMQEDDDDEV KSKPKPGRRR LRQRVVDEED
EDSDLDLPMS SEKKEKKQEV IDITSPTSTP EKSKKKEGKK AMTPVKTVKS PKKEVKNPKS
TKKEEEDVEV VGESKKVEET KPKETKKNEI TKETASASKT SFFTPVANKK NKLTSTPSDD
KKVCKIKSES VTTDSKETQA DGDEPRETPY FELAHLFAKI EEITGRLVIQ DLLTAFFRDV
IRRSPDDLLA CIYLCVCVDL APPFENLKIG IGDAILMKAI GEATGANLKF IKEMYHKEGD
LGKVAQNARS KQKTLSFTSL KPATSNGSGL TVQHVYNQFV KIAKMTGNNS QQQKCSIIKG
LLVKCEKEKK DKGAQTAAEG AKYIIRGLQG KLRIGLAEKS ILMGLTYAFM ADKEYKDKDK
QQEALTFVKK AFAECPSYNA LVAAFYEVQK EISSAPFLRV KDFAKVAEKC VLTPGTPVSP
MLARPTKAYA MVFDRFEGKP FTCEYKYDGE RAQIHILPNG EIAIFSRNFE NSTERFPDVK
LAITNAAKKG VVDSCIVDAE VVAVDRVTNK RLPFQILSTR SRKNVKVEDI KVPVCIYAFD
LLFLSGESFL GTPLAKRREK LREMFDVKPG IFEFATSLDV EDGVDVKDNP EAMEEAVDKV
RNFLEEAVRE NCEGLMVKTL EKEATYEPAN RSHKWLKLKK DYLDGIGDSA DLVPIGAFYG
RGKRTGVYGA YLLACYDPDT EMYQPITKLG TGLSDEVLKQ FYEQLKEKVV DKPPSDYAIG
DGIKPDVWFE ASCVWEILGA DLSISPKYTA AIGLVAKDKG ISLRFPRFIR IRDDKETTQA
TNSSQIADLY RAQGLTTVTN GEEEEDDDML I
//
