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Database: UniProt
Entry: M7WLJ2_RHOT1
LinkDB: M7WLJ2_RHOT1
Original site: M7WLJ2_RHOT1 
ID   M7WLJ2_RHOT1            Unreviewed;       874 AA.
AC   M7WLJ2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   05-DEC-2018, entry version 25.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=RHTO_05499 {ECO:0000313|EMBL:EMS18931.1};
OS   Rhodosporidium toruloides (strain NP11) (Yeast) (Rhodotorula
OS   gracilis).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS18931.1, ECO:0000313|Proteomes:UP000016926};
RN   [1] {ECO:0000313|EMBL:EMS18931.1, ECO:0000313|Proteomes:UP000016926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NP11 {ECO:0000313|EMBL:EMS18931.1,
RC   ECO:0000313|Proteomes:UP000016926};
RX   PubMed=23047670; DOI=10.1038/ncomms2112;
RA   Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA   Ye M., Zou H., Zou H., Zhao Z.K.;
RT   "A multi-omic map of the lipid-producing yeast Rhodosporidium
RT   toruloides.";
RL   Nat. Commun. 3:1112-1112(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;
CC         Evidence={ECO:0000256|RuleBase:RU000617};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; KB722674; EMS18931.1; -; Genomic_DNA.
DR   RefSeq; XP_016270050.1; XM_016419160.1.
DR   EnsemblFungi; EMS18931; EMS18931; RHTO_05499.
DR   GeneID; 27369512; -.
DR   OrthoDB; EOG092C0FHN; -.
DR   Proteomes; UP000016926; Unassembled WGS sequence.
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   Gene3D; 1.10.3260.10; -; 1.
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; IPR012340; NA-bd_OB-fold.
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; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 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|RuleBase:RU000617};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000016926};
KW   DNA damage {ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|RuleBase:RU000617};
KW   Ligase {ECO:0000256|RuleBase:RU000617, ECO:0000313|EMBL:EMS18931.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000617}.
FT   DOMAIN      601    738       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   COILED       71     91       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   874 AA;  95969 MW;  92A1E00CBF477E82 CRC64;
     MVKGKQPSGE RAPDQGGLNA FLGKPDSRPH QKTLNFFSKE QRDRQTAPSP AVEPKAEQKD
     VEMAPGIVAD AAGEKREKKR AASETDEAEG EADKDDKASP SKKAKTSNGD AAAEKGVSPS
     KDKDAASPVA SSSSAAKAST SASPSTSKAK AADSDKPPVS SFFAPRSTTA PKKTSADDKG
     KAKAKVQDDD EEREARDASE APSGEGEVSE EEEEDEEDEK AAVKFADIFT KSSKPDKAQT
     SWKSGEPVPY AALTATFSKI EATTKRLEIS AYLTRFLIDV IEKTPEDLLK TVYLCINRLA
     PEYESIELGI GESLLMKAIG ESCGRTLAQV KAEYKKIGDL GEVAFNSRTR QKTLFKSKPL
     TVKGVFDELK KVAKTSGKDS QGRKVGLIKS LLAKCEGEET KFLIRSLEGK LRIGLAEKTV
     LVSLAHAAVT AEHNKSGKKW SRERLSAQLE EGAEILKSVF SEIPSYDLVV PALLDKGMSH
     LQEACSLTPG IPLKPMLAKP TKAITEVLDR FEGKQFTCEY KYDGERAQIH YLEDGSVKVF
     SRNSEDMTVK FPEFVTQLPK CIKPNTKSFV IDAEAVAWDT EEKRLLEFQK LSTRKRKDVK
     AEDIKVKVHL FAFDLLYLNG ESLLEKNLRE RRQLLRDHLQ PVEGEFAFAQ SDDASTVEEI
     QTFLDQSIKD GCEGLMVKML EGEGASYEPS RRSIHWLKLK KDYLQGVGDS FDLVVIGGDY
     GKGKRTNVYG AFHLACFDAE SGTYQMICKI GTGFSDEALK QHHETLKPLE LAQKKAYYDI
     GTAKGPDVYF EPKVVWEVLA ADLSLSPIYS AAKGLCGDRG ISLRFPRFIR VRDDKDPESS
     TEPEQIAEAY RRQGIHTAGG GKKGKGAADD GDFW
//
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