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Database: UniProt
Entry: A0A1S4D8F4_TOBAC
LinkDB: A0A1S4D8F4_TOBAC
Original site: A0A1S4D8F4_TOBAC 
ID   A0A1S4D8F4_TOBAC        Unreviewed;      1116 AA.
AC   A0A1S4D8F4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   Name=LOC107827172 {ECO:0000313|RefSeq:XP_016509745.1};
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016509745.1};
RN   [1] {ECO:0000313|Proteomes:UP000084051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX   PubMed=24807620; DOI=10.1038/ncomms4833;
RA   Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA   Goepfert S., Peitsch M.C., Ivanov N.V.;
RT   "The tobacco genome sequence and its comparison with those of tomato and
RT   potato.";
RL   Nat. Commun. 5:3833-3833(2014).
RN   [2] {ECO:0000313|RefSeq:XP_016509745.1}
RP   IDENTIFICATION.
RG   RefSeq;
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   RefSeq; XP_016509745.1; XM_016654259.1.
DR   AlphaFoldDB; A0A1S4D8F4; -.
DR   GeneID; 107827172; -.
DR   OrthoDB; 8251at2759; -.
DR   Proteomes; UP000084051; Unplaced.
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:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd07903; Adenylation_DNA_ligase_IV; 1.
DR   CDD; cd07968; OBF_DNA_ligase_IV; 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; 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; 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; 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; 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|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:UP000084051};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          343..492
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          802..872
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          923..1005
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1019..1055
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1070..1105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        961..978
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1080..1105
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1116 AA;  126127 MW;  DD1066D08DFE47A6 CRC64;
     MATSAVDGGG SSIGGEDIKF SVMVSLFQWI QKSKSSAQKR SKFRKFLDAF CRKPQDNFAA
     MRLILPGLDR ERGSYGLKEH VLATCLIDAL AMSRDSDDAR RLLNWRKGGP KTGSNAGNFS
     LVAAEVLQRR QGMASAGLTI KELNEFLDHL ASSENRAEKT SILSDLIRKT NAQEMKWIIM
     IILKDLKLGI SEKSIFHEFH PDAEDLFNVT CDLKLVCEKL RDRSQRHKRQ DIEVGKAVRP
     QLALRVSNAS AAWKKLHGKE VVVECKFDGD RIQIHKNNSD LNFFSRNFLD HQEYAHGMLD
     VITQNILVDK CILDGEMLVW DASMNRFAEF GSNQEIAKAA REGLDSDRQL CYIAFDILYV
     GDTSVIHRSL KERQEILQEV VKPIKGRLEI LVPNGGLNAH RPSGEPCWSI IAHSVDDVDK
     FFKETVENRD EGIVLKDLTS KWEPSDRSGK WLKLKPEYVR AGSDLDVLII GGYYGSGRHG
     GEVAQFLVGL AERPAPNTYP RRFISFCRVG TGVSDEERNT IVTRLKPYFR KYEYPKQAPP
     AFYQVTNNAK ERPDVWVESP EKSIIVSITS DIRTIRTEVF AAPYSLRFPR IDRVRYDKPW
     HECLDVQSFV DLVHSSNGTT QREADYGIGQ DHEPKATIRS SRKRGKKNVS AVPSHFVQTD
     VSHIKGIKFQ AAKLHGDVIH CSWLFDCCLQ KRLLPLQPKY FLFLSDSTKR KLEAEVDEYS
     DSFYSDLSVK DIRKLLSDIE HSEYSKTVEY YKKKYCPKDK WARFHGCCIY FFIPEQCLKY
     SDCKALVELA TRRMKVEISV GGGKVGGNLC HATHVVVMSL PDFDVNFNEV LNSFSEAEKH
     VLYNTKLHVV RARWLEDSFK EDQKLHEDSY SLKPSNFQMS ISEKRHDKLR GKTVKCKRAS
     SPDNHGVQIK AEGISDQCQA ITLPKGDRKR NRLRPTGTAT AKAKPAINMP RRVRRKATNR
     RAKIHENESD ESATSGEHLH NGESDGAAGT RGSHENVAEH GSGIQNKDVA DDLELSPHGE
     TFLQGTSECS RSRERLDEAH ETSYGSGNIA SGKLEDPVDP VQAMLLHMIP HLDSKPSQSV
     DSLVKDDKPE ADANPSPKKK KKVSYKDVAG ELLKDW
//
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