ID J9I0F4_9SPIT Unreviewed; 661 AA.
AC J9I0F4;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=DNA ligase 1 {ECO:0000256|ARBA:ARBA00041131};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
DE AltName: Full=DNA ligase I {ECO:0000256|ARBA:ARBA00041666};
GN ORFNames=OXYTRI_06139 {ECO:0000313|EMBL:EJY72732.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY72732.1};
RN [1] {ECO:0000313|EMBL:EJY72732.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY72732.1};
RX PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT with 16,000 Tiny Chromosomes.";
RL PLoS Biol. 11:E1001473-E1001473(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 -!- 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:EJY72732.1}.
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DR EMBL; AMCR01014861; EJY72732.1; -; Genomic_DNA.
DR AlphaFoldDB; J9I0F4; -.
DR EnsemblProtists; EJY72732; EJY72732; OXYTRI_06139.
DR OrthoDB; 162082at2759; -.
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:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; 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; PS50160; DNA_LIGASE_A3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EJY72732.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 322..508
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 165..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 661 AA; 76587 MW; 7CEB411EC43E881A CRC64;
MSVAQNIIHQ SLIKTFSISQ AELRKMVVSQ GDYGNIAQKL FTEKNQQKLQ QKQQQEKNNI
SQNTLTLEDV VKVFVQLNDI KGEDSIIGKI SEISELLNKC QNEIEIKFIV RSLDKGLRIG
ISRPSVEACL LKLLNEGEIN NEFVDEYENT IFGYKIYNNS SFGDQGLNEN SEESQESEIK
PKQTGKLLPT NVPLKPMLGR PAKDFEEVLK LTSKFRKNQN DYLLAEYKYD GERTQIHFDG
EKVMMYSRNF DTQNQKFWRL NELLTTYFLE RKKQGKIDRC ILDGEVVYID NKTNKYMPFQ
NIERTLQMKS EDPLAQIEVD QLQEISTRPC VVLFDVLALN KKDCITENIL KRKEILKETF
SDEPNLLQLG QYHVLSLDDP LFDREEKKDI EPSKQKKKAS KKQDDEVVIK QTILEANPHL
LVVMLKVNEL MLQSLNDDCE GLIFKSANDN TYYDISGKRS QQWVKLKHKL NDNKGEMRDT
LDLIPIGAYY GLGRRTGTFG AYLIGAYNRE YKNFEAVCKL GTGFKDSDLK LLHERVTPLL
MEDKPTTFRV SSTIKPDYWI NPKYVWEIGA DQFSLSKTYT IGKGTLKDMN GVLLQDAGLS
LRFPKFIRER PDKEIKLEIK KDKTDHFYVQ DQEIGTEVGE ILRMYKMDIE SMQKIKDSDT
K
//
