ID A0A369GFE6_9HYPO Unreviewed; 996 AA.
AC A0A369GFE6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=CP532_0776 {ECO:0000313|EMBL:RDA84048.1};
OS Ophiocordyceps camponoti-leonardi (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2039875 {ECO:0000313|EMBL:RDA84048.1, ECO:0000313|Proteomes:UP000252748};
RN [1] {ECO:0000313|EMBL:RDA84048.1, ECO:0000313|Proteomes:UP000252748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 80369 {ECO:0000313|EMBL:RDA84048.1,
RC ECO:0000313|Proteomes:UP000252748};
RA Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA Luangsa-Ard J.-J., Giraud T.;
RT "A genome scan of diversifying selection in the zombie-ant fungus
RT Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT coevolution and host-specificity.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA ligase involved in DNA non-homologous end joining (NHEJ);
CC required for double-strand break (DSB) repair.
CC {ECO:0000256|ARBA:ARBA00043870}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:RDA84048.1}.
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DR EMBL; PDHP01000140; RDA84048.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369GFE6; -.
DR STRING; 2039875.A0A369GFE6; -.
DR Proteomes; UP000252748; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd07903; Adenylation_DNA_ligase_IV; 1.
DR CDD; cd17722; BRCT_DNA_ligase_IV_rpt1; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 2.
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; IPR044125; Adenylation_DNA_ligase_IV.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
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; IPR029710; LIG4.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR00574; dnl1; 1.
DR PANTHER; PTHR45997; DNA LIGASE 4; 1.
DR PANTHER; PTHR45997:SF1; DNA LIGASE 4; 1.
DR Pfam; PF00533; BRCT; 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 SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
DR SUPFAM; SSF52113; BRCT domain; 2.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50172; BRCT; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|RuleBase:RU000617};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172,
KW ECO:0000256|RuleBase:RU000617}; DNA repair {ECO:0000256|RuleBase:RU000617};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000617}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000252748};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 428..553
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 724..806
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 889..996
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 666..693
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 996 AA; 112941 MW; 850C2E180E8CE429 CRC64;
MASPRDPAAV REDEIQYGAV GLTHQELDEK YPNRPRNHSK TLPFHDLFDR LFNPLNENKK
QPPRGKAPRG AFHHGPSPQE QRRRIIESFI TRWRKNVGDD FYPALRLILP DKDRDRGVYG
LKENAIGKLL VKLTKIDKNS DDGYALLHWK IPGQTAAARL AGDFAGRCFE VLSKRPMRTT
VGDMTIAEVN VQLDKLAAAS GEVESLAVFE TLYERMNAEE MMWLIRIVLK QLKVGVSEKT
MLYLWHPDGE SLFNVSSSLQ RVCWELHDPK LRLEREEAGI GLMQCFQPQL AQFQMPASFQ
KMVELLRPTD EDAEFWIEEK LDGERMQMHV VEDASHPGGW RFRFWSRKAK DYTYLYGDGL
LDESSSLTRH LKHALAPGVR NLILDGEMIT WDMDLDKIVA FGTLKSAALS EQKKRMGDDD
DNGHRPLFRV FDMLYLNDKQ LTQYTLRDRR RALEKAVRPV HRRLELHKFT RATTADAIEP
LLREVVANAS EGLVLKNPRS MYRLNSRNDD WLKVKPEYMS EFGESLDCVV IGGYYGSGRR
GGILSSFLCG LRVTANHVQA GANPEKCFSF FRVGGGFSAE DYAEIRHRTE GKWQVWDASK
PPSEFIELAG GERRQIERPD MWIRPSDSVV VSVKAASIGP SDSFARGITL RFPRFRRLRL
DRSWDSALTL EELEDLKRRV DEESHEKAMT VEDNKRRKPK RVKRELVIAG DEDAPPPLPQ
AAVHRTGIFQ GFEFSVLSES SRPFKKTKVQ LEAMIKENGG SVSQRASPGT QAVLVADKKT
VKVASLIKAG GDVDIIRPIW IKDCLEPGDG GSAAALLPYE ERHLLHTTEA TREAAARNTD
RFGDSFARAV SVEELRRTTD AMAASHESDM DVAAFLAELE ERGKGLSHMR AFMFARCIVR
LRAADERCAT RRAVDRSARY VRYAGGRCAG EEEEEEEEVT HVVVFGEDAD EVRRVAEGVS
RGQVNGGRGI ARVVKGQWVE DCWREGTLLD EELYAV
//
