ID A0A2X0KVD5_9BASI Unreviewed; 912 AA.
AC A0A2X0KVD5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=BZ3500_MVSOF-1268-A1-R1_CHR3-3G06493
GN {ECO:0000313|EMBL:SCZ97972.1};
OS Microbotryum saponariae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=289078 {ECO:0000313|EMBL:SCZ97972.1, ECO:0000313|Proteomes:UP000249723};
RN [1] {ECO:0000313|Proteomes:UP000249723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jeantristanb JTB J.-T., Ricardo R.;
RL Submitted (OCT-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; FMWP01000094; SCZ97972.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X0KVD5; -.
DR STRING; 289078.A0A2X0KVD5; -.
DR Proteomes; UP000249723; 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:UP000249723}.
FT DOMAIN 624..761
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..240
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 912 AA; 99846 MW; BC040D24A06549FF CRC64;
MSKNKPRAKS TYKEPAPNQK GLEKFLGISA PARQQRLSFG SSALTATSTS DAMSEEGGLI
TSQGASKEDE HVKMQVDEEE DAVVKGPAKK RRAVIADSSD VEEEAEESKV VGKEQKVGKS
PSIKESSPKK IKIEPNAAST SQAASAASSS GPAPAASAST SRISSKAAKS VTKTADTKPP
VFSFFAPRKP APPKAAPVAS TSQKKVESEK EPASSAPPKV DAERNEADDD DGEDESEEDT
EAAVKFAEIF ARNDDVTSTK KGWEAGKDFP YSALAETFEL IAETTKRLEI TAMLTKFLIS
VIEKTPSDLL RTVYLCINRL APDYESIELG IGESLLMKAI CQSTGRKMDQ IKSEFKAQGD
LGLVAMTSRA KQLMLHKPPP LTIKKVFDLL KNVATASGKD SQSRKIGFIQ KLLLACEGTE
TKYIIRSLEG KLRIGLAERT IITSLAQAVV TTEARKEGRK LSPEKMAQRL EEGTSILKDV
FSQLPSYDLV IPALIEHGIS NLKTNCHLTP GVPLKPMLAK PTKAISEVLD RFEDKLFTCE
YKYDGERAQV HYLEDGSIKI FSRNSEDMSQ KYPDIIEQLP ACINREAGTT SFVIDCEAVA
WDPDEKKLLP FQELSRRRRK DVKAEEITVK VHLFAFDLLY LNGKALLGEN LIDRRRLLRA
HLSPVPEQFD FATSKDATTV EQIQEFLDLS IKGGCEGLMV KMLEGEGATY EPSRRSINWL
KLKKDYLDGH GDTFDLVVVG ADFGSGKRTG VYGALHLACF DDETQTFQAI CKTGTGFEEK
DLVSLHARLT RKTEHGDEGD EGEGELSSKP HDVDFGRVVP KSLPDVYFTP SKSIVIEVIA
ADLSLSPVYP AAVGKCDSRG ISLRFPRFER VRDDKGPEQA TDSDQIAEAY RRQAIITKPG
KYGGGGDDGG FY
//
