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Database: UniProt
Entry: C4XX38_CLAL4
LinkDB: C4XX38_CLAL4
Original site: C4XX38_CLAL4 
ID   C4XX38_CLAL4            Unreviewed;       339 AA.
AC   C4XX38;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=CLUG_00511 {ECO:0000313|EMBL:EEQ36388.1};
OS   Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Clavispora.
OX   NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ36388.1, ECO:0000313|Proteomes:UP000007703};
RN   [1] {ECO:0000313|EMBL:EEQ36388.1, ECO:0000313|Proteomes:UP000007703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ36388.1,
RC   ECO:0000313|Proteomes:UP000007703};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the TOP6A family.
CC       {ECO:0000256|ARBA:ARBA00006559}.
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DR   EMBL; CH408076; EEQ36388.1; -; Genomic_DNA.
DR   RefSeq; XP_002619352.1; XM_002619306.1.
DR   AlphaFoldDB; C4XX38; -.
DR   STRING; 306902.C4XX38; -.
DR   GeneID; 8500041; -.
DR   KEGG; clu:CLUG_00511; -.
DR   VEuPathDB; FungiDB:CLUG_00511; -.
DR   HOGENOM; CLU_037229_2_0_1; -.
DR   InParanoid; C4XX38; -.
DR   OMA; YICTMAN; -.
DR   OrthoDB; 169019at2759; -.
DR   Proteomes; UP000007703; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006259; P:DNA metabolic process; IEA:InterPro.
DR   GO; GO:0022414; P:reproductive process; IEA:UniProt.
DR   GO; GO:0019953; P:sexual reproduction; IEA:UniProt.
DR   Gene3D; 3.40.1360.10; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR002815; Spo11/TopoVI_A.
DR   InterPro; IPR013049; Spo11/TopoVI_A_N.
DR   InterPro; IPR036078; Spo11/TopoVI_A_sf.
DR   InterPro; IPR034136; TOPRIM_Topo6A/Spo11.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR10848; MEIOTIC RECOMBINATION PROTEIN SPO11; 1.
DR   PANTHER; PTHR10848:SF0; MEIOTIC RECOMBINATION PROTEIN SPO11; 1.
DR   Pfam; PF21180; TOP6A-Spo11_Toprim; 1.
DR   Pfam; PF04406; TP6A_N; 1.
DR   PRINTS; PR01550; TOP6AFAMILY.
DR   SUPFAM; SSF56726; DNA topoisomerase IV, alpha subunit; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007703};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          42..104
FT                   /note="Spo11/DNA topoisomerase VI subunit A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04406"
FT   DOMAIN          156..328
FT                   /note="Topoisomerase 6 subunit A/Spo11 TOPRIM"
FT                   /evidence="ECO:0000259|Pfam:PF21180"
SQ   SEQUENCE   339 AA;  38367 MW;  68F108F00612F66B CRC64;
     MANVADSQEI LLLMKSPKRH RGKTSSYVCH REMAETEHQS MKFAATVRVM NILIDQLQNR
     QVSTMRDIYY KDVTLFKGRQ AHSNNVLDAI ANSLNVSLQS DLGVYPTPKG VIWSNNPIEI
     TVGEQKKMSF DPCNEPLLIC HRETSENLSV VGDVDMVVVF EKEAILKSFM CFVKKIATGV
     KLILATGKGF PDRATLSFLG GLQACLPSTP MVYFVDSDVY GLQIFWSYMQ MSELLAQNAK
     LGGAFICDDR TEWLTMDKRE WIRSVNFLQR NARTECCPSV SVPVEQHLQL MGRELRRSLL
     LFKKAEINVI KDDEASFQSV NQYLWSKITL YVPGTGDLT
//
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