ID A0A3F3Q8N1_9EURO Unreviewed; 884 AA.
AC A0A3F3Q8N1;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, 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 ORFNames=BDQ94DRAFT_158287 {ECO:0000313|EMBL:RDH35479.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH35479.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH35479.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH35479.1,
RC ECO:0000313|Proteomes:UP000253729};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (JUL-2018) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KZ852040; RDH35479.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3F3Q8N1; -.
DR STRING; 1341132.A0A3F3Q8N1; -.
DR OrthoDB; 961at2759; -.
DR Proteomes; UP000253729; 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: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:UP000253729}.
FT DOMAIN 606..743
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 884 AA; 97089 MW; CC0811102628A5F9 CRC64;
MADSKSRKQA TLGRFFGSNS DPKEAPKKQT TLSFSNKKSK SAKKDSESET AQDPEPVNGH
GTSGDANGGA DTVDSAIKSK QEAVKADEPV DQNKLKRENS SEDEDSDVQP VSKRRRKTSR
GDEAASSPKR KSPSPKSPKK RSQSRERSPP AVIEKASGEK TPQKELSVSD DEVAEEEAQS
ASEDEEKPEV KKKKIEKAQA TLKAAGNEPY PDWKAGDPVP YAALCTTFSL IEMTTKRLVI
LAHCSLFLRQ VLRLTPQDLL PTVQLMINKL AADYAGIELG IGESLIMKAI GESTGRSLAV
IKTDQHEIGD LGLVAAKSRS NQPTMFKPKP LTVRGVHEGL LGIAKVQGHG SQDKKISGIK
KLLSAADAAT AGKGSKGIDI TKDKGGPSEA KYIVRFLEGK LRLGLAEKTV LVALAQAVVA
HEAAMEGHKT PSAEKLAEGE AILKTVYSEL PAYEVIIPAI LEHGLSNLPK VCKLQPGIPL
KPMLAKPTKS ITEVLDRFEG KEFTCEYKYD GERAQIHYVA PDSIHQYPGA TATLKKDAKG
LSAIFSRNSE DLSKKYPDVL AKLDGWIKEG VQSFVLDCET VAWDTENKKV LPFQQLMTRK
RKDVKAEDVK VKVCIFAFDL LFLNGEPTVK KSLRERRELL HESFQVTEGE FQFAQYGNTN
VLDEIQTLLD DSVKASCEGL MVKMLDTEES GYEPSKRSRN WLKVKKDYLS GVGDSLDLVV
LGAYHGRGKR TSVYGAFLLA AYNSSTQTYE TICNIGTGFS EAVLEEFYNA LSPLTIDRPK
PFYSHSNVPK DQPDVWFEPR LVWEVKTADL TLSPRYKAAA DEFMGTTGGG KGVSLRFPRF
IKSRDDKKPE QATTTRAVAE MYRKQEAVQK ENAGKGGVDD DFEY
//
