ID B8A7M7_ORYSI Unreviewed; 1226 AA.
AC B8A7M7;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=OsI_03304 {ECO:0000313|EMBL:EEC71290.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946 {ECO:0000313|EMBL:EEC71290.1, ECO:0000313|Proteomes:UP000007015};
RN [1] {ECO:0000313|EMBL:EEC71290.1, ECO:0000313|Proteomes:UP000007015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11 {ECO:0000313|Proteomes:UP000007015};
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C., Chen H., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA Zheng W., Hao B., Liu S., Wang W., Yuan L., Cao M., McDermott J.,
RA Samudrala R., Wang J., Wong G.K., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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; CM000126; EEC71290.1; -; Genomic_DNA.
DR AlphaFoldDB; B8A7M7; -.
DR STRING; 39946.B8A7M7; -.
DR EnsemblPlants; BGIOSGA001008-TA; BGIOSGA001008-PA; BGIOSGA001008.
DR Gramene; BGIOSGA001008-TA; BGIOSGA001008-PA; BGIOSGA001008.
DR HOGENOM; CLU_005138_3_0_1; -.
DR OMA; QEKPGHF; -.
DR Proteomes; UP000007015; Chromosome 1.
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: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 CDD; cd14273; UBA_TAP-C_like; 1.
DR Gene3D; 3.30.1490.70; -; 1.
DR Gene3D; 3.40.50.12650; -; 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; IPR000977; DNA_ligase_ATP-dep.
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; IPR011084; DRMBL.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR015940; UBA.
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; PF01068; DNA_ligase_A_M; 1.
DR Pfam; PF04675; DNA_ligase_A_N; 1.
DR Pfam; PF07522; DRMBL; 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; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 2.
DR PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
DR PROSITE; PS50030; UBA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000617};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, 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:UP000007015}.
FT DOMAIN 486..529
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 886..1031
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 359..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1226 AA; 137408 MW; C4F215362339B505 CRC64;
MGGASSLWML TIAPVPFNSS SAHLDQMRRD TTYCNPKFTF PPQKESLEYV VNSIKRVKEE
SRASGERVLC LIATYVVGKE RILLEVARRC GCKIHVDSRK MEILTLLGIG GEDGVFTEDA
AATDVHVTGW NILGETWPYF RPNFVKMKEI MVERGYNKAV GFVPTGWMYE TKKEGFAVRT
KDSLEIHLVP YSEHSSYNEL RDYVKFLHPK RVIPTVGLDG GKLDSKEAFA LQKHFAGLVD
ETANKQEFLM AFQRSSRNAT LGPEDAVTGL SQQEGEVQEL EEATLLPASL AFERSDSFQE
KITVEMKKEL SDFLPSWVSQ DLILDLLIKS AGDVVQAATD FFEKERDFFE EANVYNSETP
KSEIDLSSDH GSSADASSQQ EVPLFSQKPM DHSSKLLNLN AMRMKSNLSK RERKRGSNSA
DKPKKKGRST SFKPLTESSG RKQSTITNYF ARTMLAASKS DTSDKVTVDA NQNNVRNDDQ
FTEVVESEKQ SVSQLLQIVD GGMSRESAIS LLEKAKGDVN VAVDIFYSKT DNSNVLENDM
NIVTQNTENE MTDNLVVRAC FATLLRPLQR CRTYVYNLMW HKQIQSVYHC QLKSIYRSSM
EALGSSRSKI HEMYKTFGDL GDVAQECRQN QMLLAPPRPL SIRDVFSTLR KLSGIAGSGS
TGRRKILVLH LIRSCREMEM KFLVRTLVRN LRIGVMMKTI LPALAHAVVI DGKYSNSPVL
SLEGIKPQLQ ELSTEVAEAY NVIPNLDLLI PSLLREGTAF SASSLAMITG TPIPPMLARI
TNGLTQSLKL FNGRAFTCEY KYDGQRAQIH RSNDGSVQIF SRQMKESTSR FPDLVGMIKE
LCSIEVSSFI LDAEVVGIDR KKGNKLMSFQ ELSSRERGSK HSSIAIQNIK VDICVFVFDI
MFCNGQSLLN CSLRQRRKYI HDLFQEKPGH FELAQQLTVE ADEASVDNST TLERMNTFFK
MACQSSCEGI MLKILDVDAG YSASKRCDSW LKVKRDYVGL GDSLDLVPIG AWYGNGRKAG
WYSPFLMACY NPEYEEFQSV CRVMSGFSDE FYKEPQPAAT LADCRRCAQR PVAGGLPLLD
CSACRCATSR SPMLSPVVTH QLDAGSTPPI ARDGESMEMM KEFYSGDRIL PKKPVYYKTD
ELPELWFSAE QVWEIRGADL TLSPVHHAAI GLVHPSRGIS VRMPRYIRSR PDRSPEDCST
ATDVASLFKA QTRKMEVSSD GQDTSH
//
