ID A0A151N713_ALLMI Unreviewed; 906 AA.
AC A0A151N713;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN Name=LIG3 {ECO:0000313|EMBL:KYO32541.1};
GN ORFNames=Y1Q_0013052 {ECO:0000313|EMBL:KYO32541.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO32541.1};
RN [1] {ECO:0000313|EMBL:KYO32541.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO32541.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(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 -!- 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO32541.1}.
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DR EMBL; AKHW03003911; KYO32541.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151N713; -.
DR STRING; 8496.A0A151N713; -.
DR eggNOG; KOG4437; Eukaryota.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0008270; F:zinc ion binding; IEA:InterPro.
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; cd07902; Adenylation_DNA_ligase_III; 1.
DR CDD; cd18431; BRCT_DNA_ligase_III; 1.
DR CDD; cd07967; OBF_DNA_ligase_III; 1.
DR Gene3D; 3.30.1490.70; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 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 Gene3D; 3.30.1740.10; Zinc finger, PARP-type; 1.
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; IPR036599; DNA_ligase_N_sf.
DR InterPro; IPR031916; LIG3_BRCT.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR001510; Znf_PARP.
DR InterPro; IPR036957; Znf_PARP_sf.
DR NCBIfam; TIGR00574; dnl1; 1.
DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR PANTHER; PTHR45674:SF9; DNA LIGASE 3; 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; PF16759; LIG3_BRCT; 1.
DR Pfam; PF00645; zf-PARP; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM01336; zf-PARP; 1.
DR SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
DR PROSITE; PS00347; ZF_PARP_1; 1.
DR PROSITE; PS50064; ZF_PARP_2; 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 DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000617}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 6..98
FT /note="PARP-type"
FT /evidence="ECO:0000259|PROSITE:PS50064"
FT DOMAIN 496..630
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 830..906
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 98..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..820
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 906 AA; 101560 MW; 8DD921630C2A6336 CRC64;
MAEQRYCVDY AKRGTAGCKK CKEKILKGMV RIGKVVPNPF TESGGDMKEW YHVKCIFEKL
ERARATTKKI EDITDLEGWE ELQDAEKDLI NQLISEATSK SASTPKKKAT VQAKLSPSGQ
ITSPKKDPGA VPNPSPKKFS GFTAKPGSSG DTPANSSHKS TLSSKKCDPK HKDCLLREFR
KLCAMVADKP SYNVKTQIIQ DFLQKGTGGD GFHGDLYLTI KLLLPGVIKI IYNLNDKQIV
KLFSRIFNCS QDEMVRDLEQ GDVSETVRIF FEESRSCPPA AKSLLTIQEV DEFLIGLSKL
TKEDDQQTLL QGITRRCTGN DLKCIIRLIK HDLKMNAGAK HVLDALDPNA YEAFKASRNL
QDVVERVLRN QQEAEKQPGL KRTLSVQASL MTPVQPMLAE ACKSIEYAMK KCPNGMYAEI
KYDGERVQVH KNGDHFSYFS RSLKPVLPHK VAHFKDFIPR AFPGGHSMIL DSEVLLIDNK
TGKPLPFGTL GVHKKAAFQD ANVCLFVFDC VYFNDVSLMD RPLCERRKFL HDNMVEIPSR
ILFSEMKHVT RASDLADMIS RVIREGLEGL VLKDIKSTYE PGKRHWLKVK KDYLNEGAMA
DTADLVVLGA FYGQGSKGGM MSIFLMGCYD PKTEKWCTVT KCSGGHDDAT LARLQNELDM
VKISKDPNKI PSWLKINKLY YPDFIVPDPK KAPVWEITGA EFSKAEAHTA DGISIRFPRC
TRIRDDKDWK TATNLPQLKE LYQLSKEKSD FSVVAGEEEV STAGSSGENN GNSGSSTPHN
TPKTPPRKSP AKTKKSEGNN LVYMTPKKKV EDKRGEKRKA AELDDNGKKI LLDIFTGVRL
YLPPSVENFS KIRRYFVAYD GDLVQEFDTA SATHVIGDLE ENPGAKRVSP SWIWECIRKR
RLVAPC
//
