ID G1Q2N1_MYOLU Unreviewed; 911 AA.
AC G1Q2N1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
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:ENSMLUP00000017964.1};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000017964.1, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000017964.1, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000017964.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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; AAPE02014015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006086975.1; XM_006086913.2.
DR AlphaFoldDB; G1Q2N1; -.
DR STRING; 59463.ENSMLUP00000017964; -.
DR Ensembl; ENSMLUT00000001268.2; ENSMLUP00000017964.1; ENSMLUG00000001267.2.
DR GeneID; 102430494; -.
DR KEGG; mlf:102430494; -.
DR CTD; 3981; -.
DR eggNOG; KOG0966; Eukaryota.
DR GeneTree; ENSGT00860000133881; -.
DR HOGENOM; CLU_004844_2_0_1; -.
DR InParanoid; G1Q2N1; -.
DR OMA; EGIMIKH; -.
DR OrthoDB; 8251at2759; -.
DR TreeFam; TF312980; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0000793; C:condensed chromosome; IEA:Ensembl.
DR GO; GO:0032807; C:DNA ligase IV complex; IEA:Ensembl.
DR GO; GO:0005958; C:DNA-dependent protein kinase-DNA ligase 4 complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; 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; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0071479; P:cellular response to ionizing radiation; 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:1904155; P:DN2 thymocyte differentiation; 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; IEA:Ensembl.
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:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0033152; P:immunoglobulin V(D)J recombination; IEA:Ensembl.
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:0022008; P:neurogenesis; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IEA:Ensembl.
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:0072089; P:stem cell proliferation; IEA:Ensembl.
DR GO; GO:0033153; P:T cell receptor V(D)J recombination; IEA:Ensembl.
DR CDD; cd07903; Adenylation_DNA_ligase_IV; 1.
DR CDD; cd17722; BRCT_DNA_ligase_IV_rpt1; 1.
DR CDD; cd17717; BRCT_DNA_ligase_IV_rpt2; 1.
DR CDD; cd07968; OBF_DNA_ligase_IV; 1.
DR Gene3D; 6.10.250.520; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 2.
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; IPR044125; Adenylation_DNA_ligase_IV.
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 NCBIfam; TIGR00574; dnl1; 1.
DR PANTHER; PTHR45997; DNA LIGASE 4; 1.
DR PANTHER; PTHR45997:SF1; DNA LIGASE 4; 1.
DR Pfam; PF00533; BRCT; 2.
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; ATP-dependent DNA ligase DNA-binding domain; 1.
DR SUPFAM; SSF52113; BRCT domain; 2.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 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|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000617};
KW DNA damage {ECO:0000256|RuleBase:RU000617};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172,
KW ECO:0000256|RuleBase:RU000617}; DNA repair {ECO:0000256|RuleBase:RU000617};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000617}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 355..489
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 654..743
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 808..911
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
SQ SEQUENCE 911 AA; 103983 MW; FD5D7619AFDAB4EC CRC64;
MAASQTSQTV ASHVPFADLC STLERIQRSK GRADKIRHFR EFLDSWRKFH DALHKNQKDV
TDSFYPAMRL ILPQLERERM AYGIKETMLA KLYIELLNLP KDGKDALKLL NYRTPTGTRG
DAGDFAMIAY FVLKPRCLQK GSLTIQQVND ILDSIATNNS AKRKDLVKKS LLQLITQSSA
LEQKWLIRMI VKDLKLGFSQ QTVFSLFHND AAELHNVTTD LEKVCRQLHD PSVGLSDISI
TLFSPFKPML AAIADIGRIE KDMKNQSFYI ETKLDGERMQ MHKDGDVYAY FSRNGYKYTE
QFGASPQEGS LTPFIHNAFR TDIQICILDG EMMAYNPNTQ TFMQKGNKFD IKRMVEDSDL
QTCYCVFDVL MVNNKKLGHE TLRKRYEILS SIFTPVPGRI EIVEKTQAHT NKEVIDALNE
AIDKREEGIM IKHPLSIYKP DKRGEGWLKI KPEYVNGLMD ELDIIIVGGY WGKGSRGGLM
SHFLCAVAEK HASGEKPSVF HTLCRIGSGY TMKELYDLGL KLAKHWKPFH KKAPPSSILF
GTEKPEVYIE PCNSVIVQIK ASEIVPSDMY KTGCTLRFPR IEKIREDKEW HECMTLDDLE
QLRGKASGKL ASKHLYVGGD DEPQVKKRKA PPKIKKVIGI IEHLKAPNLS NVNKVSNIFE
DVEFCVMSGI SGHPKPDLEN RIAEFGGYIV QNPGPDTYCV IAGSENIRVK NIISSNKHDV
VKPEWLLECF KTKSCVPWQP HFMIHMCPST KQHFAREYDC YGDSYFVDTD LNQLKEVFSG
IKDSSEQTPK EMASVIADLE YRYSWDCSPL NMFRNHTIYL DLYTVINDLN TKIEGTRLAI
TALELRFHGA EVVSCLAKGV SHVIIGEDHS RVADFKTFRR TLKRKFKILQ EGWIIDSIDK
CELQDENQYL V
//
