ID A0A074XS94_AURPU Unreviewed; 393 AA.
AC A0A074XS94;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=M438DRAFT_395723 {ECO:0000313|EMBL:KEQ86509.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ86509.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ86509.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ86509.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584978; KEQ86509.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074XS94; -.
DR STRING; 1043002.A0A074XS94; -.
DR HOGENOM; CLU_037229_0_0_1; -.
DR OrthoDB; 169019at2759; -.
DR Proteomes; UP000030706; 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:0042138; P:meiotic DNA double-strand break formation; IEA:InterPro.
DR CDD; cd00223; TOPRIM_TopoIIB_SPO; 1.
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; IPR013048; Meiotic_Spo11.
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; PR01551; SPO11HOMOLOG.
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, ECO:0000313|EMBL:KEQ86509.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030706};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 99..160
FT /note="Spo11/DNA topoisomerase VI subunit A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04406"
FT DOMAIN 210..377
FT /note="Topoisomerase 6 subunit A/Spo11 TOPRIM"
FT /evidence="ECO:0000259|Pfam:PF21180"
SQ SEQUENCE 393 AA; 43975 MW; 741A670C7E331F28 CRC64;
MDDEFDHDML FEFESPVASP GSRDAFLLDA PQLSRQTKHN DVIAQIEAVF ETVADALLNE
RADITVSLAA HSTSSQDDPS TRGPKATFTF PGKNASDAWR FSVVIRILEL IHESLSDGVI
LTKRDLYYRD PALFGKQATV DRYVDQIAAA FAVPRSSLNV TAGVKGLMAG AAVIHRRDGS
KIGLTNVQNG VLVPSMEEVL SVDLSRVRWI LVVEKEATFQ SIISSEFWQE MMWHAVIVTG
KGYPDIATRA IARFMSIASP QNGFAEPPVF GLVDYDPDGM AILHTYKHGS KKMSEDNAAL
IVPTTQWMGL RSRDITDEDH THRNQGLMPL TRRDRHKARK MLEWEQFSDL EEAAQWRREL
QVMLMLNLKA EIQIIDSDPS GLAKMIKYAV KDT
//
