ID M2X1Q8_GALSU Unreviewed; 741 AA.
AC M2X1Q8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=Gasu_24280 {ECO:0000313|EMBL:EME30280.1};
OS Galdieria sulphuraria (Red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC Galdieria.
OX NCBI_TaxID=130081 {ECO:0000313|EMBL:EME30280.1, ECO:0000313|Proteomes:UP000030680};
RN [1] {ECO:0000313|Proteomes:UP000030680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX PubMed=23471408; DOI=10.1126/science.1231707;
RA Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA Lercher M.J., Weber A.P.;
RT "Gene transfer from bacteria and archaea facilitated evolution of an
RT extremophilic eukaryote.";
RL Science 339:1207-1210(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}.
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DR EMBL; KB454501; EME30280.1; -; Genomic_DNA.
DR RefSeq; XP_005706800.1; XM_005706743.1.
DR AlphaFoldDB; M2X1Q8; -.
DR STRING; 130081.M2X1Q8; -.
DR EnsemblPlants; EME30280; EME30280; Gasu_24280.
DR GeneID; 17089018; -.
DR Gramene; EME30280; EME30280; Gasu_24280.
DR KEGG; gsl:Gasu_24280; -.
DR eggNOG; KOG0967; Eukaryota.
DR OMA; WIKYKRD; -.
DR OrthoDB; 961at2759; -.
DR Proteomes; UP000030680; 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; 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:UP000030680}.
FT DOMAIN 480..617
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 57..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 741 AA; 83177 MW; 9BA76CD115398D04 CRC64;
MRTRLCFLIP SVHKIFYVQR ASLTMKRKAS NISPRKQPST IPKSSIGSYL SILQKEEPSS
LDTERQAKEN VDQNTNDMRL ESQQGSETSS STSEHSSSLV ENAKVVCEEK LDECTFSSVS
WQPPSRTPFR FLAEAFEVME MTTSRLALIK ILTQVFRKIV NTTPDDLLPC VYLCTNMLGP
AHEGLELKAG EATVLNALSS ATGNSVKVLK ERLIKLGDIG DLAAECRTTQ QTMFKPPSLT
IQGVYQEFRT MANLAGKMST KEREKHLQKL LVSATSQEAK YIARIVLGKL RIHIAYKTVI
ASLATVFAPC SKTVGKTADE MDSIVKEATA TLNAVYSQLP MWDRIIPVLI QNKSTQGLED
HCRLTPGVPV GPMLAKPAKE ASDVLERFQE CSFVCEYKYD GMRAQIHYLP DGNVKIFSRN
AEDDTPKYPD IVENIKFALS KNKAVRSFII DSEVVAYDPE TNVMKSFQEL QGRARKEVKL
EDIKVSVCVF AFDILFFNGE SLLKWSLKER REKLIETFSP VQGKFQFTTS KVFTDWEGVD
EMMDEAIQAG CEGLMIKALT GEYSSYEPSN RSQNWLKMKK DYMNSIGDSL DLVPIGAYYG
RGKRSGVFGA FLLACYNSET EEFQTVCKLG TGFSDEFLSS ITKFYKDGHI LAEPKPYYGV
SDSPTIIPDV WFDPCQVWET RCADLTLSPS HTAAKGMLSE EDKGIALRFP RFIRIREDKS
VDDATTAEQI VELYSNQKSK M
//
