ID G9MN43_HYPVG Unreviewed; 878 AA.
AC G9MN43;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=TRIVIDRAFT_64213 {ECO:0000313|EMBL:EHK23335.1};
OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK23335.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK23335.1, ECO:0000313|Proteomes:UP000007115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
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:EHK23335.1}.
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DR EMBL; ABDF02000005; EHK23335.1; -; Genomic_DNA.
DR RefSeq; XP_013957567.1; XM_014102092.1.
DR AlphaFoldDB; G9MN43; -.
DR STRING; 413071.G9MN43; -.
DR EnsemblFungi; EHK23335; EHK23335; TRIVIDRAFT_64213.
DR GeneID; 25796574; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_64213; -.
DR eggNOG; KOG0967; Eukaryota.
DR HOGENOM; CLU_005138_1_1_1; -.
DR InParanoid; G9MN43; -.
DR OMA; RDFSCEY; -.
DR OrthoDB; 961at2759; -.
DR Proteomes; UP000007115; 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:UP000007115}.
FT DOMAIN 538..729
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 878 AA; 97672 MW; 7A1669BD874AD0BB CRC64;
MSSPAKKRKL NSGKKQPAAQ SKGLEYFFSR QKQSDALNSS AGEDGAQSSS SAILSDEELA
RKLQAEWNQE AANEAHTPSD GQNATPKDKD IGSIAETVED DSMPTSASQP DQLPLATTPK
KQDAKKTLSL QSTGMADDIV TTSIPLDESP LTFEPSKYVK ELQEYWAPEN GDASYALLTR
CFVLVSATTS RIKIVDTLVN CLRILVEGDP SSLLPAVWLA TNSISPPYIS MELGLGGSAI
SKALRQVCGL DNRSLKAIYD KYGDPGDVAF EAKKKQSFTL RKPKPLTIKG VYQSLVKIAT
THGQGSGEVK QRIVDRLLQD ARGGEESRFI VRTVSQYLRI GAVKTTMLIA LSRAFLLSKA
PGSEYGTKDI TELSKLKKEE LAEVWSRAEE IVKASFARHP NYNDLVPALL DIGVCEELLL
RCGLTLHVPL RPMLGSITRD LSEMLTKLQG RDFACEYKYD GQRAQVHCDE KGKVSIFSRH
LELMTEKYPD LVELVPKIRG EGIGSFIMEG EVVAVDRETG ELKNFQTLTN RARKDVAIGD
IKIDVCLFAF DLMYLNGQSL LDRPFRERRE LLRSLFIEVP HHFTWVQSLD ATSGDSEAVL
EFFKSALENK CEGIMVKILD NIPDLPLVED EPEQPLEDTE KLSLPKTKTK GKGKTKSTAK
GDGDEKSTKS RRKPLLATYE PDKRLDSWLK VKKDYNSSFD TLDMIPVAGW HGQGRKAKWW
SPILLAVRNE ESGTLEVVCK CISGFTDAFY KANKEFYDNG EESGEPKNTK LQKPSFIEYY
GPSPDVWFEP QEVWEMAFAD ITLSPVYTAA IGLVSDERGL SLRFPRFLKK RDDKSIDEAS
TNEFLANLWR KQEAKAASST PKNGDAEMED VLDGDQDE
//
