ID A0A2C5X7D8_9PEZI Unreviewed; 855 AA.
AC A0A2C5X7D8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN Name=Lig1 {ECO:0000313|EMBL:PHH53897.1};
GN ORFNames=CFIMG_002761RA {ECO:0000313|EMBL:PHH53897.1};
OS Ceratocystis fimbriata CBS 114723.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX NCBI_TaxID=1035309 {ECO:0000313|EMBL:PHH53897.1, ECO:0000313|Proteomes:UP000222788};
RN [1] {ECO:0000313|EMBL:PHH53897.1, ECO:0000313|Proteomes:UP000222788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH53897.1,
RC ECO:0000313|Proteomes:UP000222788};
RX PubMed=23931120; DOI=10.1016/j.funbio.2013.06.004;
RA Simpson M.C., Wilken P.M., Coetzee M.P., Wingfield M.J., Wingfield B.D.;
RT "Analysis of microsatellite markers in the genome of the plant pathogen
RT Ceratocystis fimbriata.";
RL Fungal Biol. 117:545-555(2013).
RN [2] {ECO:0000313|EMBL:PHH53897.1, ECO:0000313|Proteomes:UP000222788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH53897.1,
RC ECO:0000313|Proteomes:UP000222788};
RX PubMed=24563841; DOI=10.5598/imafungus.2013.04.02.14;
RA Wilken P.M., Steenkamp E.T., Wingfield M.J., de Beer Z.W., Wingfield B.D.;
RT "IMA Genome-F 1: Ceratocystis fimbriata: Draft nuclear genome sequence for
RT the plant pathogen, Ceratocystis fimbriata.";
RL IMA Fungus 4:357-358(2013).
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:PHH53897.1}.
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DR EMBL; APWK03000035; PHH53897.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5X7D8; -.
DR STRING; 1035309.A0A2C5X7D8; -.
DR OrthoDB; 961at2759; -.
DR Proteomes; UP000222788; 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; 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; 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:UP000222788}.
FT DOMAIN 529..713
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 24..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 855 AA; 94927 MW; A29D61EDDDE74D4B CRC64;
MVSPSKKRKL NSGLSAHGLE YFFAKQQRTK DDGTTPKADV DGTSHHYESS SVLATDEELA
RRLQAEFDLE AQAQPNQTDP RNTAKIDVTE TSSLANPESV VDESIPITVA RDSTSTKTLA
LQSTSTADDK LSESLPLDQS PFVFEPCQYL PALKDQWKSQ GGNASYAVLI RCFVLINSTA
SRIKIVDTLV NCLRLLIEGD PTSLLPAVWL ATNAISSPYE SLELGLGSSA ISRALKKVCG
LDNRALKALF NKHGDAGDVA FEAKKKQTFT LRKREPLTIQ DVYSSLVKIA QAKGQGSGEI
KQSIVNRLLQ NARGGEESRY LVRTLCQHLR IGAVKATMLI ALSRAFVISK PLDKEFPIRS
TENLSKLKKE ELAEIWMRGE QLVKGCFARR PNYADIIPVL LEMGVSDELA LRCGLSLHTP
LRPMLASITR DLSEMLNNLH GRDFTCEFKY DGQRAQIHCD EQGKISLFSR HLELMTDKYP
DLVALIHKIR GEGVNSFIME GEVVAVDPES GDLMNFQTLS GRARKDVDIG SVKIQICLFA
FDLMYLNGRS LLDSQLRDRR DLLRSSFVEI PGQFTWAKSI DATSQDSEAV LDFYQSAIRS
KCEGIMVKIL DNAIDSKSLD GPHVSSSTER STAKDLSKRR GKSGQGEVIT KPGGYRKTLL
ATYEPDKRLE SWLKVKKDYN ASFDTLDLIP VAAWHGSGRK AKWWSPILMA VRNEETGSLE
AVCKCMSGFT DVFYKANRAF YSDGTGEGEA QNTRESQPAF VEYTGPSPDI WFEPQEVWEM
GFADITLSPT YSAGIELVND GRGLSLRFPR FIKKREDKSI EEASTNEFLA ELYRKQEAAG
PKPAQEAIGE GVEEE
//
