ID A0A0M8MME9_9BASI Unreviewed; 861 AA.
AC A0A0M8MME9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891};
DE EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891};
GN ORFNames=Malapachy_2449 {ECO:0000313|EMBL:KOS15426.1};
OS Malassezia pachydermatis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS15426.1, ECO:0000313|Proteomes:UP000037751};
RN [1] {ECO:0000313|EMBL:KOS15426.1, ECO:0000313|Proteomes:UP000037751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS15426.1,
RC ECO:0000313|Proteomes:UP000037751};
RA Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT pachydermatis CBS1879.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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 IB topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00006645}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOS15426.1}.
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DR EMBL; LGAV01000002; KOS15426.1; -; Genomic_DNA.
DR RefSeq; XP_017993058.1; XM_018136938.1.
DR AlphaFoldDB; A0A0M8MME9; -.
DR STRING; 77020.A0A0M8MME9; -.
DR GeneID; 28728813; -.
DR VEuPathDB; FungiDB:Malapachy_2449; -.
DR OrthoDB; 10940at2759; -.
DR Proteomes; UP000037751; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
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:InterPro.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR Gene3D; 1.10.132.10; -; 1.
DR Gene3D; 2.170.11.10; DNA Topoisomerase I, domain 2; 1.
DR Gene3D; 1.10.10.41; Yeast DNA topoisomerase - domain 1; 1.
DR InterPro; IPR011010; DNA_brk_join_enz.
DR InterPro; IPR013034; DNA_topo_DNA_db_N_dom1.
DR InterPro; IPR013030; DNA_topo_DNA_db_N_dom2.
DR InterPro; IPR001631; TopoI.
DR InterPro; IPR018521; TopoI_AS.
DR InterPro; IPR025834; TopoI_C_dom.
DR InterPro; IPR014711; TopoI_cat_a-hlx-sub_euk.
DR InterPro; IPR014727; TopoI_cat_a/b-sub_euk.
DR InterPro; IPR013500; TopoI_cat_euk.
DR InterPro; IPR008336; TopoI_DNA-bd_euk.
DR InterPro; IPR036202; TopoI_DNA-bd_euk_N_sf.
DR InterPro; IPR013499; TopoI_euk.
DR PANTHER; PTHR10290:SF23; DNA TOPOISOMERASE 1; 1.
DR PANTHER; PTHR10290; DNA TOPOISOMERASE I; 1.
DR Pfam; PF14370; Topo_C_assoc; 1.
DR Pfam; PF01028; Topoisom_I; 1.
DR Pfam; PF02919; Topoisom_I_N; 1.
DR PRINTS; PR00416; EUTPISMRASEI.
DR SMART; SM00435; TOPEUc; 1.
DR SUPFAM; SSF56349; DNA breaking-rejoining enzymes; 1.
DR SUPFAM; SSF56741; Eukaryotic DNA topoisomerase I, N-terminal DNA-binding fragment; 1.
DR PROSITE; PS00176; TOPOISOMERASE_I_EUK; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:KOS15426.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037751};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 256..768
FT /note="DNA topoisomerase I eukaryotic-type"
FT /evidence="ECO:0000259|SMART:SM00435"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 682..709
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 24..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..73
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 861 AA; 98040 MW; 9AE3DD11E4CEC5B1 CRC64;
MEKRAQRFKE EEESDDDMPL SVQVKASDSD SDSDVPMSQQ AASSRRTRPV NYNESEDEED
EEEDEDDEDE DDDKPLAGTK RKRTSKAKSS EQQTKADIEG GGEPRWVTLI HKGPKFPEPY
SPLPKEIKLK YDGHPVPLPP ESEEVAMFYA VKLETQHATN PIFNKNFFED FQMYLKKYPP
LDGTRINKFE KLDFRDMYNY WKSLKDAEAE RKKSMAPSAR KAEIAARKAI ENEYKSCLVD
GVEQKAGNVT VEPPGLFLGR GAHPKAGRVK TRILPEQITI NHSADHPPPA PPAGHKWGEV
VERKDVTWLA LWRENINGSF KYVFLDASST FKTESDREKF EKARRLDACV KQVRADVLKN
LKSKDRVEQM VATIVWLIDN FSLRAGNEKG EDEAETFGVC SLRCGHATLV PPNKLNLSFL
GKDSMKFDET LTISNHDVYK NIGTFLTTDG TKVNGRLMKK GPDDPIFAAP KVRGDKLTPL
APDVVNQFLG TYMKGLSAKV FRTYNASATF QGLLDQTEEW LVSRPTPQER EINPANLRIA
YNEANRQVAI LCNHQKTVNH ITLNKSLERT REKIFALKYD IMKEQQKLLT FHKASDLKKE
YLPKDHDFAK HWALILTEPD LDKSRIQEHE EALITAKKAR LQAAFDRQES ERLYQEEQRK
AAQGKVKKEE VADIKPSKIA TKADLHAELK KLDAQLQVLE RERKKNKSEA ASCNVASCAR
RILGKYEAIK KQEAELLNKN NTSDVSLGTS KMNYIDPRIT VAWLKKWDMR LQSQQPAKPP
KGKGAEKNGK VKKEGPVDPA TSEKMELNLQ VMNIGQFFPM TLQKKFKWAS FDDDGKPLPA
KWSFVKDAQK KMRKLGSAER N
//
