ID A0A2J6TW88_9HELO Unreviewed; 868 AA.
AC A0A2J6TW88;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-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=K444DRAFT_550592 {ECO:0000313|EMBL:PMD67292.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD67292.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD67292.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD67292.1,
RC ECO:0000313|Proteomes:UP000235371};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (APR-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; KZ613740; PMD67292.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6TW88; -.
DR STRING; 1095630.A0A2J6TW88; -.
DR InParanoid; A0A2J6TW88; -.
DR OrthoDB; 961at2759; -.
DR Proteomes; UP000235371; 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:UP000235371}.
FT DOMAIN 543..725
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 868 AA; 96862 MW; 5F6B8033A300513E CRC64;
METGTPAKKR KLNDSKSPAA GRSLEYFFGK QRQSNTTQPL VGIEDTPRRG SEGEELTDEE
LARKLQAEWN QEDVQEPQKV SMSYITDQQS PPINGEASRS TSPEKFVPTF EDEATSEAIP
RPFLIQPKSK NTLSLQSAGS AEDIISSNIP LDESPLTFEP SKYAAELQGH WATEGGDASY
AILARCFVLV NSTQSRIKIV DTLVNLLRVI IEADPTSLLP TVWLATNAIS PPYISLELGL
GGSAISKALK NVCGLDNRSL KALYDRVGDA GDVAFEAKKK QSFTLRKPKP LSIKGVYSSL
VKIANTQGAG SGEIKQRVVD RLLQDARGAE ESRYIVRTLC QHLRIGAVKT TMLIALSRAF
LLSRPPGAEF PLKSRKKLAA LKKEELAEIW SKSEEIVKKC FAQRPNYNDL IPILLEVGVC
DELLIRCGLA LHIPLRPMLG SITRDLSEML TKLQGRDFSC EYKYDGQRAQ VHCDDQGKVS
IFSRHLELMT DKYPDLVALI PKIRGEGVGS FIMEGEVVAV DQVSGELKTF QTLANRPRKD
VAIGSVKVEV CLFAFDLMYL NGAPLLDRSF RERRELLRGL FTEVPNQFTW VKSTDATSQD
SEIVLEFFKS ATDVKCEGIM VKILDNLKDV KVPDETEDLS VMEPPAPSRI KEGMKKAGKK
ETEKKTRRKA LLATYEPDKR LDSWLKVKKD YSTSFDTLDL IPIAGWHGQG RKSKWWSPIL
LAVRNEETGS LEAVCKCISG FTDTFYKANK EYYEQGGDHV LSGKPSYIDY EGGYPDCWFE
PQEVWEMAFA DITLSPTYTA AIGLVSGERG LSLRFPRFLR KRDDKGIDEA STSEFLAGLW
RKQEKAPTVG KETQDERGED EDEDEEAL
//
