GenomeNet

Database: UniProt/TrEMBL
Entry: F6SA46_MONDO
LinkDB: F6SA46_MONDO
Original site: F6SA46_MONDO 
ID   F6SA46_MONDO            Unreviewed;       911 AA.
AC   F6SA46;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   25-OCT-2017, entry version 48.
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:ENSMODP00000036738};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000036738, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000036738, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L.,
RA   Duke S., Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J.,
RA   Kamal M., Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A.,
RA   Benos P.V., Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L.,
RA   Deakin J.E., Fazzari M.J., Glass J.L., Grabherr M., Greally J.M.,
RA   Gu W., Hore T.A., Huttley G.A., Kleber M., Jirtle R.L., Koina E.,
RA   Lee J.T., Mahony S., Marra M.A., Miller R.D., Nicholls R.D., Oda M.,
RA   Papenfuss A.T., Parra Z.E., Pollock D.D., Ray D.A., Schein J.E.,
RA   Speed T.P., Thompson K., VandeBerg J.L., Wade C.M., Walker J.A.,
RA   Waters P.D., Webber C., Weidman J.R., Xie X., Zody M.C., Baldwin J.,
RA   Abdouelleil A., Abdulkadir J., Abebe A., Abera B., Abreu J.,
RA   Acer S.C., Aftuck L., Alexander A., An P., Anderson E., Anderson S.,
RA   Arachi H., Azer M., Bachantsang P., Barry A., Bayul T., Berlin A.,
RA   Bessette D., Bloom T., Bloom T., Boguslavskiy L., Bonnet C.,
RA   Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P.,
RA   Costello M., D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C.,
RA   Dhargay N., Dooley K., Dooley E., Doricent M., Dorje P., Dorjee K.,
RA   Dupes A., Elong R., Falk J., Farina A., Faro S., Ferguson D.,
RA   Fisher S., Foley C.D., Franke A., Friedrich D., Gadbois L., Gearin G.,
RA   Gearin C.R., Giannoukos G., Goode T., Graham J., Grandbois E.,
RA   Grewal S., Gyaltsen K., Hafez N., Hagos B., Hall J., Henson C.,
RA   Hollinger A., Honan T., Huard M.D., Hughes L., Hurhula B., Husby M.E.,
RA   Kamat A., Kanga B., Kashin S., Khazanovich D., Kisner P., Lance K.,
RA   Lara M., Lee W., Lennon N., Letendre F., LeVine R., Lipovsky A.,
RA   Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., Lubonja R.,
RA   Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A.,
RA   Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N.,
RA   Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., Osman S.,
RA   Markiewicz E., Oyono O.L., Patti C., Phunkhang P., Pierre F.,
RA   Priest M., Raghuraman S., Rege F., Reyes R., Rise C., Rogov P.,
RA   Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., Shih D.,
RA   Sparrow T., Spaulding J., Stalker J., Stange-Thomann N.,
RA   Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T.,
RA   Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T.,
RA   Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A.,
RA   Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C.,
RA   Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in
RT   non-coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000036738}
RP   IDENTIFICATION.
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:ENSMODP00000036738}.
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DR   RefSeq; XP_007501369.1; XM_007501307.2.
DR   RefSeq; XP_007501371.1; XM_007501309.2.
DR   RefSeq; XP_007501372.1; XM_007501310.1.
DR   RefSeq; XP_007501373.1; XM_007501311.1.
DR   RefSeq; XP_007501374.1; XM_007501312.2.
DR   RefSeq; XP_007501375.1; XM_007501313.1.
DR   RefSeq; XP_016280412.1; XM_016424926.1.
DR   RefSeq; XP_016280413.1; XM_016424927.1.
DR   ProteinModelPortal; F6SA46; -.
DR   STRING; 13616.ENSMODP00000036738; -.
DR   Ensembl; ENSMODT00000038333; ENSMODP00000036738; ENSMODG00000025064.
DR   GeneID; 100018117; -.
DR   KEGG; mdo:100018117; -.
DR   CTD; 3981; -.
DR   eggNOG; KOG0966; Eukaryota.
DR   eggNOG; COG1793; LUCA.
DR   GeneTree; ENSGT00860000133881; -.
DR   InParanoid; F6SA46; -.
DR   KO; K10777; -.
DR   OMA; HMCPSTK; -.
DR   OrthoDB; EOG091G03K0; -.
DR   TreeFam; TF312980; -.
DR   Proteomes; UP000002280; Chromosome 7.
DR   Bgee; ENSMODG00000025064; -.
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; IPR036420; BRCT_dom_sf.
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; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR10459:SF7; PTHR10459:SF7; 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:UP000002280};
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:UP000002280}.
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;  104526 MW;  E15C3098EB18E360 CRC64;
     MATSQPSRTV ASQVPFADLC STLERIQKSK ARPEKIKYFK EFLDSWRRFH DALHKKEKEV
     TDSFYPAMRL ILPQLERERM AYGIKETMLA KLYIELLNLP KEGKDAQKLL NYRTPTGTRG
     DAGDFAMIAY FVLKPRCPKQ GSLTIQQVND ILDLIASNNS ANRKDLVKKN LLQLITQSSA
     LEQKWLIRMI IKDLKLGFSQ QTIFSLFHRD AAELHNVTTD LEKVCRQLHN PLVGLSDISI
     TLFSAFKPML AAVADIQRIE KDMKHQGFYI ETKLDGERMQ MHKDGDVYKF FSRNGYDYTE
     QFGDSSLNGS LIPFIHKAFK TNIQNCILDG EMMAYNPNTQ TFMQKGSKFD IKRMVEDSDL
     QTCYCVFDVL MVNNKKLGHE ALRKRYEIIS TVFTPIKGRL EVVQKTEANT KKEVIDALNE
     AIDKREEGIM IKNPLSIYKP DKRGEGWLKI KPEYINELMD ELDILIVGGY WGKGLRGGMM
     SHFLCAVAET PPPGEKPSVF YTLCRVGSGY TMKELYDLGL KLSKHWKPFH KRAPPNSILC
     GTEKPEVYIE PCNSVIVQVK AAEIVSSDMY KTNCTLRFPR IEKIREDKEW YKCMTLDELE
     NLRGKASGKL ASKHLFIGGD DEEPQGKKRK AIKVKKTIGI IEHLKAPDLS NINRISNVFE
     DVEFCVMTGT DSHSKPDLES HIAELGGYIV QNPGPDTYCV IAGTENVRVR NIISSNKHDV
     VKPEWLLECF KAKECVPWQP QFMIHMCPST KEHFACEYDC YGDSYFADTD VVQLKEVFSR
     IKNVKEESPN EMASVIADLE DRYSWDNCPL SMFRHCTMYV DIYAIINDLT TQIEGTRLAI
     KALELRFHGA KVVSCLEEGV SHVIIGEDHS RVEEFKAFRR TLKRKYKILQ ELWVTDSLKK
     GELQEENQYL I
//
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