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Database: UniProt
Entry: Q4QCK3_LEIMA
LinkDB: Q4QCK3_LEIMA
Original site: Q4QCK3_LEIMA 
ID   Q4QCK3_LEIMA            Unreviewed;       812 AA.
AC   Q4QCK3;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891};
DE            EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891};
GN   ORFNames=LMJF_21_0125 {ECO:0000313|EMBL:CAJ03761.1};
OS   Leishmania major.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5664 {ECO:0000313|EMBL:CAJ03761.1, ECO:0000313|Proteomes:UP000000542};
RN   [1] {ECO:0000313|EMBL:CAJ03761.1, ECO:0000313|Proteomes:UP000000542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX   PubMed=16020728; DOI=10.1126/science.1112680;
RA   Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA   Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA   Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA   Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA   Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M.,
RA   De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA   Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA   Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA   Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA   Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S.,
RA   Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA   Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA   Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA   Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K.,
RA   Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA   Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA   Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA   Barrell B., Myler P.J.;
RT   "The genome of the kinetoplastid parasite, Leishmania major.";
RL   Science 309:436-442(2005).
RN   [2] {ECO:0000313|EMBL:CAJ03761.1, ECO:0000313|Proteomes:UP000000542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC         passage and rejoining.; EC=5.6.2.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000213};
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000256|ARBA:ARBA00009446}.
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DR   EMBL; FR796417; CAJ03761.1; -; Genomic_DNA.
DR   RefSeq; XP_001682945.1; XM_001682893.1.
DR   AlphaFoldDB; Q4QCK3; -.
DR   STRING; 5664.Q4QCK3; -.
DR   EnsemblProtists; CAJ03761; CAJ03761; LMJF_21_0125.
DR   GeneID; 5651546; -.
DR   KEGG; lma:LMJF_21_0125; -.
DR   VEuPathDB; TriTrypDB:LmjF.21.0125; -.
DR   VEuPathDB; TriTrypDB:LMJFC_210007100; -.
DR   VEuPathDB; TriTrypDB:LMJLV39_210006400; -.
DR   VEuPathDB; TriTrypDB:LMJSD75_210006400; -.
DR   eggNOG; KOG1956; Eukaryota.
DR   HOGENOM; CLU_349701_0_0_1; -.
DR   InParanoid; Q4QCK3; -.
DR   OMA; ARHAMDR; -.
DR   Proteomes; UP000000542; Chromosome 21.
DR   GO; GO:0005737; C:cytoplasm; ISO:GeneDB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   CDD; cd01028; TOPRIM_TopoIA; 1.
DR   Gene3D; 3.40.50.140; -; 1.
DR   Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR   Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR   Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 1.
DR   InterPro; IPR000380; Topo_IA.
DR   InterPro; IPR003601; Topo_IA_2.
DR   InterPro; IPR013497; Topo_IA_cen.
DR   InterPro; IPR013824; Topo_IA_cen_sub1.
DR   InterPro; IPR013825; Topo_IA_cen_sub2.
DR   InterPro; IPR013826; Topo_IA_cen_sub3.
DR   InterPro; IPR023405; Topo_IA_core_domain.
DR   InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   PANTHER; PTHR42785:SF1; DNA TOPOISOMERASE; 1.
DR   PANTHER; PTHR42785; DNA TOPOISOMERASE, TYPE IA, CORE; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   PRINTS; PR00417; PRTPISMRASEI.
DR   SMART; SM00437; TOP1Ac; 1.
DR   SMART; SM00436; TOP1Bc; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:CAJ03761.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000542};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          10..166
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          385..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          758..812
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        760..788
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   812 AA;  89497 MW;  5289D2E62A0E1A72 CRC64;
     MLRRSVRALE KLVIVESPNK VIKVEGLLSD PKVIPDWSFN NSKLRAISTG AEKAIAMATT
     GHFMSLKELT WSPQSSSPAS GVTAADFPAN GLLVSFSLEW ELIPGRRIQD TVSHYIEEKA
     DNLTEIIVAT DPDREGELIA VHAQNLIRRM FPQLNAPFTR AYMHSITADG IRRAMEERHE
     AFDYNLANAA EARHAMDRIF GFLGSSVVRY ANPQMRSIGR VQTPALILIN DREDKIKSYL
     ESHASTFEIQ VVCYFTSKHH QRFSQVVKVT PARKGGAAPV DWSDKATVKQ RCEQWALSSA
     THFSVSPGAK PQETVTPPPK PFTMATLIAR ANRQLHYSSD MVSSCLQDLF QMGYITYPRT
     DSTRIDESIL PSIYAAVRRE HGKRLLQEQD GPSKAGVRRS TAQKEAADAN VEDAHEAIRP
     TNIDTTVEEL GAVSAPMKHI YDLVRRNTMA VHMIPMKTER IVVLVACKAA NGEEVEFELQ
     GKHVVEPGWS AAFHGSKGTA TPVTETDQDV EAVEDGGVVV PSISDDEFKA IMDIAAQRGG
     GTGVQKGSMQ LESAQVAENR PSPPLPFSEG GLIEQLKNNG VGRPSTYPMI VKTLLARNYI
     TVNKGRCETT PVGRMLVDTS RATFPSIVDI GFTSAFEKKL DRIAKPRSTK ELALPPNVSD
     ADYVLSSFIS NFLNYVTEAT KAQRVAITTR SLALQQEKRA ASNTPMSPTD FQANLEKETK
     RVLTQVPDLV DNMKSYRTFT ALQNSLNDYL RRNFPPSAAA MAPASSSGTA RSYGSSSSSS
     SSTKKKESYG ATYRVDKKTP RHFRAKLKKA KK
//
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