GenomeNet

Database: UniProt
Entry: A4HEY9_LEIBR
LinkDB: A4HEY9_LEIBR
Original site: A4HEY9_LEIBR 
ID   A4HEY9_LEIBR            Unreviewed;       633 AA.
AC   A4HEY9;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Putative DNA ligase k alpha {ECO:0000313|EMBL:CAM39398.1};
DE            EC=6.5.1.1 {ECO:0000313|EMBL:CAM39398.1};
GN   ORFNames=LBRM_26_1360 {ECO:0000313|EMBL:CAM39398.1};
OS   Leishmania braziliensis.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC   Leishmania braziliensis species complex.
OX   NCBI_TaxID=5660 {ECO:0000313|EMBL:CAM39398.1, ECO:0000313|Proteomes:UP000007258};
RN   [1] {ECO:0000313|EMBL:CAM39398.1, ECO:0000313|Proteomes:UP000007258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM39398.1,
RC   ECO:0000313|Proteomes:UP000007258};
RX   PubMed=17572675; DOI=10.1038/ng2053;
RA   Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA   Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA   Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA   Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA   Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA   Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA   Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA   Mottram J.C., Smith D.F., Berriman M.;
RT   "Comparative genomic analysis of three Leishmania species that cause
RT   diverse human disease.";
RL   Nat. Genet. 39:839-847(2007).
RN   [2] {ECO:0000313|EMBL:CAM39398.1, ECO:0000313|Proteomes:UP000007258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM39398.1,
RC   ECO:0000313|Proteomes:UP000007258};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|ARBA:ARBA00001968};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FR799001; CAM39398.1; -; Genomic_DNA.
DR   RefSeq; XP_001562367.1; XM_001562317.1.
DR   AlphaFoldDB; A4HEY9; -.
DR   STRING; 5660.A4HEY9; -.
DR   GeneID; 5416488; -.
DR   KEGG; lbz:LBRM_26_1360; -.
DR   VEuPathDB; TriTrypDB:LbrM.26.1360; -.
DR   VEuPathDB; TriTrypDB:LBRM2903_260018700; -.
DR   InParanoid; A4HEY9; -.
DR   OMA; FECCDDA; -.
DR   Proteomes; UP000007258; Chromosome 26.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd08041; OBF_kDNA_ligase_like; 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; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR029319; DNA_ligase_OB.
DR   InterPro; IPR025487; DUF4379.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR47810; DNA LIGASE; 1.
DR   PANTHER; PTHR47810:SF1; DNA LIGASE B; 1.
DR   Pfam; PF14743; DNA_ligase_OB_2; 1.
DR   Pfam; PF14311; DUF4379; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   4: Predicted;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000313|EMBL:CAM39398.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007258}.
FT   DOMAIN          386..570
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          27..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          500..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..168
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   633 AA;  69024 MW;  6BB2FD4CE79897C7 CRC64;
     MMKATVLLRL GGGGSGLIGR PTLLRRQTAK RVATTKAKDT TTGGRNKKAT APTADGGWCS
     HKLSLADFHP AIARTWIAAA SNKMLQPQHV TPDSRKLAWW ICPSCHHQHN KRIDRHLAAG
     GACPQCGAKP TLDVGRSARK DASSPRSASN AASLSTKTKR TTAASAQKSV PAVAVLRHRC
     RPSSTLDTIA APNANLLSKS VADDQYLRVQ ETRNLLPMLA KSYDKERWKI ASDEVLQVSP
     KLDGIRCVAA YRVDTKQVLF FSRSGTLFEC CDDAIEPALR HLFEKDPTLV LDGELYNDSV
     NLVQLSTVRT AAGKSPRLSP TAALSGEDPV SAFYNSLLAA AYGNKKHKHN SVAAAGVAQT
     DLPAVIRFDQ LTSAIRTTRQ WLTPEVSALQ RQLQYHVFDI LYSREFPGGR GSAVPFSVRY
     GVLERLLASV TVHNLAHISR YDPLVLRRVP SYLCTIDAVD TVLHAAMRVG YEGIMIRREC
     RGATTVADRD SNKVESAVKK IKRGSASNEG KARAGAATEN SDGGYGYGQR SSTLLKYKVM
     QDAEYVIVGA VEGSGKWKGF LGSFICVTPD KKHRFTVTPA STDAEKRRMW QSWKTAYKGK
     VLTVQYQEIT PDGVPRFPVG KCVRGAADGH DWL
//
DBGET integrated database retrieval system