ID A0A0E0KUV8_ORYPU Unreviewed; 1277 AA.
AC A0A0E0KUV8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=DNA ligase IV {ECO:0000256|ARBA:ARBA00031942};
DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] 4 {ECO:0000256|ARBA:ARBA00030676};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC04G21990.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC04G21990.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC04G21990.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A0E0KUV8; -.
DR EnsemblPlants; OPUNC04G21990.1; OPUNC04G21990.1; OPUNC04G21990.
DR Gramene; OPUNC04G21990.1; OPUNC04G21990.1; OPUNC04G21990.
DR Proteomes; UP000026962; Chromosome 4.
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: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; 2.
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; 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 PANTHER; PTHR45997; DNA LIGASE 4; 1.
DR PANTHER; PTHR45997:SF1; DNA LIGASE 4; 1.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF04679; DNA_ligase_A_C; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 2.
DR Pfam; PF04675; DNA_ligase_A_N; 1.
DR Pfam; PF11411; DNA_ligase_IV; 1.
DR SMART; SM00292; BRCT; 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; 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};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 318..430
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 628..716
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 775..885
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 879..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..1002
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1054
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1277 AA; 143808 MW; 6EC0687C4BB232EF CRC64;
MAATVRFGLL VAMFQAMSRD RTAAKKRGRL RALLDRAYGP GGRDDYFSAL RLVLPGLDRE
RGSYGLKEAA LASVLVDALG IAKDSPDAVR LTNWRRGGGF RNAGNFALVA AEVLQRRQGM
ISGGLTIKEV NDALDRLAAT ENRSEKASIL SSLIKKTNAL EMKWLLMIIL KDLKLGISEK
SVFHEFHPDA EDLFNVTCDL RLVCEKLNDR SQRHKRQDIE VGKAVRPQLA MRVSNASSAW
KKLHGKQVVA ECKFDGDRIQ IHKNGEEIHF FSRVCTWNVQ TKAAKEGLET DRQLCCILEW
IASYVPALCL DILSCQDYVA FDILYAGDTS VIHQSLTERH EILRKVVRPL KGHLEILVPT
GGLNIHRPPD EPCWSIFAQS LDDVEKFFKD TVDNRDEGII LKDLESKWEP GDRSGKWLKL
KPDYIHAGAD LDVGIMAQDV EEERCVAQFL IGLAVPSDDN SYPKRFLSFC RVGTGLSDEE
LDALVTKLKP HFRKNEYPKK PPRFYEVTNH SKERPDVWIE SPDKSVIISI TSDIRTIKSE
VFAAPYSLRF PRIQRLRYDK PWHECLDVQA FVDIVHSSNG TTHRAADDDN GLKNVKVKQP
RTNKKGEKKN VSIIPSHLMK TDISGLKGET LIFANTMFYF VNIPPSYNLD YFHKLVVENG
GSFSMNLNDS VTHCIAAEKK GIKYQAATRQ GRIIHYSWII DCCKEKHLLH LQPKYILFLA
DFARHKFPEE IDSYADYFYW DIDISDLKQI FSNMDRAVVD SNMVHRYKKK YCTDERFCFF
QGCCVYFYHA PLVNADYNVI SDLALKRVKQ DLTMHGGQVC SILAPATHLI IVSVLQAYNF
DMLYKSLPPA ERRYLHDKRL QVVSNKWLED SVEKQTRLPE TTYSLKPDTL EEIEIERSEE
TVQPSNDKLE ENEEVDTSRV KHVPRKRGRP SSSASKTAKP APRPVRRTRA RRGNQHAKID
DVEPEESDHG ETGLDDQIPD TDNISKMEVD SFDKDQVSAR PVRRTWARRG KQHAKIDYGQ
SGESDPGETG QDDQKLDADY ISKMEEDYSD RDQGAHPAAP RAVQKSRAQR GKRLAKIDHG
ESEESGPGET GQDDKKLDAD SISKMEEHAH DNDQEPPPGA QFITLDEQEP EGIKSSTTET
PSNSTKHERY ETVLRTDTAE ATSSATCEKM EQMVDPLHAM LLDMIPSLGR KKTDVGNRVA
EAKADKNPPW VGSSTSSYVA PVPQASASSA SNSGVPAQHA GSSTQSTGVP APDPTAGAPK
KKKVSYKDVA GELLKDW
//
