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Database: UniProt
Entry: Q566D8_RAT
LinkDB: Q566D8_RAT
Original site: Q566D8_RAT 
ID   Q566D8_RAT              Unreviewed;       913 AA.
AC   Q566D8; F1M624;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   Name=Lig1 {ECO:0000313|EMBL:AAH93604.1, ECO:0000313|RGD:621424};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|EMBL:AAH93604.1};
RN   [1] {ECO:0000313|EMBL:AAH93604.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000313|EMBL:AAH93604.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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; BC093604; AAH93604.1; -; mRNA.
DR   RefSeq; NP_001019439.1; NM_001024268.2.
DR   AlphaFoldDB; Q566D8; -.
DR   SMR; Q566D8; -.
DR   GeneID; 81513; -.
DR   KEGG; rno:81513; -.
DR   CTD; 3978; -.
DR   RGD; 621424; Lig1.
DR   VEuPathDB; HostDB:ENSRNOG00000014193; -.
DR   HOGENOM; CLU_005138_0_2_1; -.
DR   OrthoDB; 961at2759; -.
DR   Bgee; ENSRNOG00000014193; Expressed in thymus and 19 other cell types or tissues.
DR   Genevisible; Q566D8; RN.
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: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; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   1: Evidence at protein level;
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}.
FT   DOMAIN          643..779
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   913 AA;  101875 MW;  CA3DF9A306F1FED5 CRC64;
     MQRSIMSFFQ PTTTEGKAKK PEKEIPSSIR EKEPPPKVAL KERNRAVPES DSPVKRPGRK
     VAQVLSSEGE DEDEAPGTPQ VQKPVSDSKQ SSPPSPDSCP ENSSPSMDIS PSGFPKRRTA
     RKQLPKRTIQ DTLEEHNEDK DKAAKKRKKE DTQTPTESLT EAEEVKQKEE QVEDQPTVPP
     EPTESPESVT LTKTENIPMC KAGVKQKPQE EEQSKPPARG AKPLSSFFTP RKPAVKTEVK
     QEESDTPRKE ETKGAPDPTN YNPSKSNYHP IEDACWKHGQ KVPFLAVART FEKIEEVSAR
     LKMVETLSNL LRSVVALSPT DLLPVLYLSL NRLGPPQQGL ELGVGDGVLL KAVAQATGRQ
     LESIRAEVAE KGDVGLVAEN SRSTQRLMLP PPPLTVSGVF TKFCDIARLT GSASMAKKMD
     IIKGLFVACR YSEARFIARS LSGRLRLGLA EQSVLAALAQ AVSLTPPGQE FPTAVVDAGK
     GKTAEARKMW LEEQGMILKQ TFCEVPDLDR IIPVLLEHGL ESLPEHCKLS PGVPLKPMLA
     HPTRGVREVL KRFEEVDFTC EYKYDGQRAQ IHVLEGGEVK IFSRNQEDNS GKYPDIISRI
     PKIKHPSVTS FILDTEAVAW DREKKQIQPF QVLTTRKRKE VDASEIQVQV CLYAFDLIYL
     NGESLARQPL SRRRQLLREN FVETEGEFVF ATSLDTKDIE QIAEFLEQSV KDSCEGLMVK
     TLDVDATYEI AKRSHNWLKL KKDYLEGVGD TLDLVVIGAY LGRGKRAGRY GGFLLAAYDE
     ESEELQAICK LGTGFSDEEL EEHHQSMQAL LLPTPRPYVR IDGAVAPDHW LDPSVVWEVK
     CADLSLSPIY PAARGLVDKE KGISLRFPRF IRVREDKQPE QATTSDQVAS LYRKQSQIQN
     QQSSDLDSDV EDY
//
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