ID G7PY14_MACFA Unreviewed; 1014 AA.
AC G7PY14;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=EGM_09925 {ECO:0000313|EMBL:EHH59738.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1] {ECO:0000313|EMBL:EHH59738.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH59738.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
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; CM001294; EHH59738.1; -; Genomic_DNA.
DR AlphaFoldDB; G7PY14; -.
DR eggNOG; KOG0967; Eukaryota.
DR Proteomes; UP000009130; Chromosome 19.
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; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 2.
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 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|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 722..858
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 42..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1014 AA; 111606 MW; 9D9C64F710193AC1 CRC64;
MTLWLATCSC GWGFPETLSS PDVLPTCSYR HFAYRSFFHP KKEGKAKKPE KEASNGSRET
EPPPKVALKE WNGVVSESDS PVKRPGRKAA RVLGSEGEEE DEALSPAKGQ NCSFVFQKPA
PDCSQVSPPR PATSPENNAS LSDTSPTDSS PSGIPKRRTA RKQLPKRTIQ EVLEEQSADE
DREAKRKKVE EEVETPEESL TEAEVATEKE GEDRDQPTTP PKPLKTSEAE TLTESVSEPE
VATRQELQEE EEQTKPPRSA PKTLSSFFTP RKPAVKKEVK EEEPGAPGKE GAAEGPLDPS
GYNPAKNNYH PVEDACWKPG QKVPYLAVAR TFEKIEEVSA RLRMVETLSN LLRSVVALSP
PDLLPVLYLS LNHLGPPQQG LELGVGDGVL LKAVAQATGR QLESVRAEAA EKGDVGLVAE
NSRSTQRLML PPPPLTASGV FSKFRDIARL TGSASTAKKI DIIKGLFVAC RHSEARFIAR
SLSGRLRLGL AGQSVLAALS QAVSLTPPGQ EFPPAVVDAG KGKTAEARKT WLEEQGMILK
QTFCEVPDLD RIIPVLLEHG LERLPEHCKL SPGIPLKPML AHPTRGVSEV LKRFEEAAFT
CEYKYDGQRA QIHALEGGEV KIFSRNQEDN TGKYPDIISR IPKIKLPSVT SFILDTEAVA
WDREKKQIQP FQVLTTRKRK VASPAPLPAK APYFLIFRPV LAVGPAQCPE GQSVSLDAEV
DASEIQVQVC LYAFDLIYLN GESLVREPLS RRRQLLRENF VETEGEFVFA TSLDTKDVEQ
IAEFLEQSVK DSCEGLMVKT LDVDATYEIA KRSHNWLKLK KDYLDGVGDT LDLVVIGAYL
GRGKRAGRYG GFLLASYDED SEELQAICKL PTSLVFCGYC IDQKAVGAMS LGTGFSDEEL
EEHHQSLKAL VLPSPRPYVR IDGAVTPDHW LDPSAVWEVK CADLSLSPIY PAARGLVDSD
KGISLRFPRF IRVREDKQPE QATTSAQVAC LYRKQSQIQN QQGEDSGSDP EDTY
//
