GenomeNet

Database: UniProt/TrEMBL
Entry: E2R0G7_CANLF
LinkDB: E2R0G7_CANLF
Original site: E2R0G7_CANLF 
ID   E2R0G7_CANLF            Unreviewed;       911 AA.
AC   E2R0G7;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   30-AUG-2017, entry version 58.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   Name=LIG4 {ECO:0000313|Ensembl:ENSCAFP00000009027};
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000009027, ECO:0000313|Proteomes:UP000002254};
RN   [1] {ECO:0000313|Ensembl:ENSCAFP00000009027, ECO:0000313|Proteomes:UP000002254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000009027,
RC   ECO:0000313|Proteomes:UP000002254};
RX   PubMed=16341006; DOI=10.1038/nature04338;
RG   Broad Sequencing Platform;
RA   Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA   Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C.,
RA   Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A.,
RA   Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F.,
RA   Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A.,
RA   Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M.,
RA   Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L.,
RA   Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J.,
RA   Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA   Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA   Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L.,
RA   Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A.,
RA   Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N.,
RA   Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A.,
RA   Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N.,
RA   Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N.,
RA   Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K.,
RA   Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G.,
RA   Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E.,
RA   Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C.,
RA   Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L.,
RA   Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C.,
RA   Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T.,
RA   Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J.,
RA   Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J.,
RA   Marabella R., Maru K., Matthews C., McDonough S., Mehta T.,
RA   Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K.,
RA   Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J.,
RA   Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA   Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K.,
RA   Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F.,
RA   Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C.,
RA   Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S.,
RA   Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J.,
RA   Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S.,
RA   Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S.,
RA   Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T.,
RA   Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T.,
RA   Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X.,
RA   Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.;
RT   "Genome sequence, comparative analysis and haplotype structure of the
RT   domestic dog.";
RL   Nature 438:803-819(2005).
RN   [2] {ECO:0000313|Ensembl:ENSCAFP00000009027}
RP   IDENTIFICATION.
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000009027};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000256|RuleBase:RU000617}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|RuleBase:RU004196}.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSCAFP00000009027}.
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DR   EMBL; AAEX03013370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005634152.1; XM_005634095.2.
DR   RefSeq; XP_542663.2; XM_542663.4.
DR   ProteinModelPortal; E2R0G7; -.
DR   STRING; 9615.ENSCAFP00000009027; -.
DR   PaxDb; E2R0G7; -.
DR   Ensembl; ENSCAFT00000009725; ENSCAFP00000009027; ENSCAFG00000006031.
DR   GeneID; 485544; -.
DR   KEGG; cfa:485544; -.
DR   CTD; 3981; -.
DR   eggNOG; KOG0966; Eukaryota.
DR   eggNOG; COG1793; LUCA.
DR   GeneTree; ENSGT00860000133881; -.
DR   InParanoid; E2R0G7; -.
DR   KO; K10777; -.
DR   OMA; HMCPSTK; -.
DR   OrthoDB; EOG091G03K0; -.
DR   TreeFam; TF312980; -.
DR   Reactome; R-CFA-5693571; Nonhomologous End-Joining (NHEJ).
DR   Proteomes; UP000002254; Chromosome 22.
DR   Bgee; ENSCAFG00000006031; -.
DR   GO; GO:0000793; C:condensed chromosome; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0032807; C:DNA ligase IV complex; IBA:GO_Central.
DR   GO; GO:0005958; C:DNA-dependent protein kinase-DNA ligase 4 complex; IBA:GO_Central.
DR   GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IBA:GO_Central.
DR   GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR   GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
DR   GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
DR   GO; GO:0051276; P:chromosome organization; IEA:Ensembl.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0051102; P:DNA ligation involved in DNA recombination; IEA:Ensembl.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IBA:GO_Central.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0097680; P:double-strand break repair via classical nonhomologous end joining; IEA:Ensembl.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR   GO; GO:0033152; P:immunoglobulin V(D)J recombination; IBA:GO_Central.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0045190; P:isotype switching; IEA:Ensembl.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IBA:GO_Central.
DR   GO; GO:2001252; P:positive regulation of chromosome organization; IEA:Ensembl.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR   GO; GO:0050769; P:positive regulation of neurogenesis; IEA:Ensembl.
DR   GO; GO:0002328; P:pro-B cell differentiation; IEA:Ensembl.
DR   GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR   GO; GO:0010165; P:response to X-ray; IEA:Ensembl.
DR   GO; GO:0000012; P:single strand break repair; IEA:Ensembl.
DR   GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR   GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
DR   GO; GO:0033153; P:T cell receptor V(D)J recombination; IEA:Ensembl.
DR   CDD; cd00027; BRCT; 2.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   Gene3D; 3.40.50.10190; -; 2.
DR   InterPro; IPR001357; BRCT_dom.
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; IPR021536; DNA_ligase_IV_dom.
DR   InterPro; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR10459:SF84; PTHR10459:SF84; 1.
DR   Pfam; PF16589; BRCT_2; 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   Pfam; PF11411; DNA_ligase_IV; 1.
DR   SMART; SM00292; BRCT; 2.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52113; SSF52113; 2.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS50172; BRCT; 2.
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|RuleBase:RU000617};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002254};
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|RuleBase:RU000617};
KW   Ligase {ECO:0000256|RuleBase:RU000617};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002254}.
FT   DOMAIN      355    489       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   DOMAIN      654    743       BRCT. {ECO:0000259|PROSITE:PS50172}.
FT   DOMAIN      845    911       BRCT. {ECO:0000259|PROSITE:PS50172}.
SQ   SEQUENCE   911 AA;  104181 MW;  648D82719A4A8879 CRC64;
     MAATQTSQTV ASHVPFADLC STLERIQRSK GREEKIRHFR EFLDSWRRFH DALHKNQKDV
     RDSFYPAMRL ILPQLERERM AYGIKETMLA KLYIELLNLP KEGKDALKLL NYRTPTGTRG
     DAGDFATIAY FVLKPRCLQK GSLTIQQVND ILDSIASNNS ARKKDLIKKS LLQLITQSSA
     LEQKWLIRMI VKDLKLGFSE QSVFSAFHND AAELHNVTTD LEKVCRQLHD PSIGLSDISI
     TLFSAFKPML AAIADIERIE KDMKHQSFYI ETKLDGERMQ MHKDGDVYQY FSRNGYNYTD
     QFGDSPREGS LTPFIHSAFK TDVQICILDG EMMAFNPNTQ TFMQKGNKFD IKRMVEDSDL
     QTCYCVFDVL MVNNKKLGRE TLKKRYEILT SVFTPIPGRI EIVQKTQAHT KKEVIDALNE
     AIDKREEGIM IKHPLSIYKP DKRGEGWLKI KPEYVDGLMD ELDILIVGGY WGKGSRGGMM
     SHFLCAVAEK PPPGEKPSVF HTLCRVGSGY TMKELYDLGL KLAKHWKPFH KKALPSSILC
     GTEKPEVYIE PCNSVIVQVK ATEIVSSDMY KTGCTLRFPR IEKIREDKEW HECTTVDDLE
     QLRGKASGKL ASKHLDIGGD DEPQEKKRKA APKIKKIIGI IEHLKAPNLS NINKVSNIFE
     DVEFCVMSGT DSHPKPDLEN RIAEFGGYIV QNPGPDTYCV IAGSENIRVK NIISSNKHDV
     VKPEWLLECF KTKSCVPWQP RFMIHMCPST KEHFAREYDC YGDSYFVDLD LNQLKEVFSG
     IKNSSKQTPR EMASLIADLE YRYSWDRSPL CLFRHCIVYL DLYAVINDLS TKIEGTRLAI
     TALELRFHGA KVVSCLAQGV SHVIIGEDHS RVAVLKSFRR TLKRKFKILQ QDWVTESIDK
     CELQEENQYL V
//
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