ID A0A0S3RHL6_PHAAN Unreviewed; 671 AA.
AC A0A0S3RHL6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN Name=Vigan.02G309100 {ECO:0000313|EMBL:BAT80120.1};
GN ORFNames=VIGAN_02309100 {ECO:0000313|EMBL:BAT80120.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT80120.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT80120.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
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; AP015035; BAT80120.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3RHL6; -.
DR Proteomes; UP000291084; Chromosome 2.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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 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; 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; 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 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:UP000291084}.
FT DOMAIN 330..479
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 606..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 671 AA; 76338 MW; 2E1E342E1F3AD183 CRC64;
MATEQTKFSV LCSLFTWTQR SKSAAKKRSK FRKFLDAFCI DRNFFPAIRL ILPNLDRERG
SYGLKESVLA TSLIDALGIS RDSPDALRLI NWRKGGAATG ATAGNFALVA TEVLHRRQGT
ASGGLTIREL NELLDRLASG ENRAEKILVL STLIQKTNAQ EMKWIIMIIL KDLKLGISEK
SIFHEFHPDA EDLFNVTCDL KLVCEKLRDR NQRHKRQDIE VGKAVRPQLA KRVANATEAW
KKLHGKEVVV ECKFDGDRIQ IHKNGTEIHF FSRNFIDHSE YAHAMSDIII QNILVDRCIL
DGEMLVWDKS SKRFAEFGSN QEIAKAARDG LDSDRQLCYV AFDILYFGDT SVIHQSLKER
HEILCKVVRP MKGRLEVLVP NAGINSHLTS GEPCWSFIAH KVDEVERFFK ETIENRDEGI
VLKDHSSKWE PSDRSGKWLK LKPEYIQAGS DLDVLIIGGY YGSGRRGGQV AQFLVGLAER
QSPNAQPMRF ISFCRVGTGL SDEELDVVIT KLKPYFRKYE YPKKRPPSFY QVTNHSKERP
DVWVDSPEKS IILSITSDIR TIESEVFAAP YSLRFPRIDR VRYDKAWNEC LDVQSFIELV
HSSNGTTQRD TEYGSKQDSK PKRMKSSTRG EKKNMSIVPS HLIQTDISSI KGGSLILSNM
MFCILVNFAS Y
//
