ID A0A397VL76_9GLOM Unreviewed; 1368 AA.
AC A0A397VL76;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|ARBA:ARBA00019635, ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895, ECO:0000256|RuleBase:RU362094};
GN ORFNames=C2G38_1999612 {ECO:0000313|EMBL:RIB20633.1};
OS Gigaspora rosea.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Diversisporales; Gigasporaceae; Gigaspora.
OX NCBI_TaxID=44941 {ECO:0000313|EMBL:RIB20633.1, ECO:0000313|Proteomes:UP000266673};
RN [1] {ECO:0000313|EMBL:RIB20633.1, ECO:0000313|Proteomes:UP000266673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 194757 {ECO:0000313|EMBL:RIB20633.1,
RC ECO:0000313|Proteomes:UP000266673};
RA Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT "Comparative genomics reveals the genomic features of Rhizophagus
RT irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT symbiotic lifestyle signature.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Control of topological states of DNA by transient breakage
CC and subsequent rejoining of DNA strands. Topoisomerase II makes double-
CC strand breaks. {ECO:0000256|RuleBase:RU362094}.
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 ECO:0000256|RuleBase:RU362094};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU362094}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00011080, ECO:0000256|RuleBase:RU362094}.
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:RIB20633.1}.
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DR EMBL; QKWP01000407; RIB20633.1; -; Genomic_DNA.
DR STRING; 44941.A0A397VL76; -.
DR Proteomes; UP000266673; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR CDD; cd16930; HATPase_TopII-like; 1.
DR CDD; cd00187; TOP4c; 1.
DR CDD; cd03481; TopoIIA_Trans_ScTopoIIA; 1.
DR CDD; cd03365; TOPRIM_TopoIIA; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.1490.30; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR001241; Topo_IIA.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a_sf.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR InterPro; IPR001154; TopoII_euk.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR031660; TOPRIM_C.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034157; TOPRIM_TopoII.
DR PANTHER; PTHR10169:SF38; DNA TOPOISOMERASE 2; 1.
DR PANTHER; PTHR10169; DNA TOPOISOMERASE/GYRASE; 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF16898; TOPRIM_C; 1.
DR PRINTS; PR01158; TOPISMRASEII.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00433; TOP2c; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362094};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362094};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362094};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362094};
KW Reference proteome {ECO:0000313|Proteomes:UP000266673};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 641..758
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1368 AA; 156073 MW; B6C0C0B721B85261 CRC64;
MSDSENSDYY QSTSTTKKLL PTRRAKTAKK TIIDIDSDIS EDFSGSDYAP SAPKETTKNS
KTKKKTQVIE EVSSSKTAKK SIFDVDCDNS EELSGNDCAP SVSKEKKQTT KNAKTKKKTQ
VIEEEASSKT AKKSIFDVDC DNSEEFSGND CAPSVSKEKK QTTKNAKTKK KTQVIEEEIS
DIDDFSPSLK ENKQPEASSS KTNTSNKKKT VEEIYQKKTQ IEHILLRPDT YIGSVECVTE
KLWVYDSEKD SMVYRDVTIV PGLYKIVDEI LVNAADNKIR DPSMNTIKVK IDKEQNLISI
YNNGKGIPIE MHKDENIYVP ELIFGHLLTS SNYDDNEKKV TGGRNGYGAK LTNIFSTEFI
VETTDTTAKK KYRQVFKDNM SVKQNAKLTS YSKKEEYTEI TFKPDLAKFG LTELTDDIIA
LLKKRVFDMA GCSKNVKVFL NDERLKIRNF KEYIQKYLPP PPNPSEDSTT RPPDVIHEQV
NERWEVGFTP SQEGQFQQVS FVNSIATTKG GTHVNHVVDQ LVTRIKETVK KKQKDAKLKP
FQIKNHISIY INCLIENPSF TSQTKEFMSL KEKSFGSSCT LSENFINKVL KSVIITDIIE
EVKQKQDKEL KKTDGAKKSS VLSIEKLEDA GNAGGKFAQN CTLILTEGDS AKSLAVAGIS
VVGRKNFGVF PLRGKLLNVR DASHTSIMSN EEIQNIKKIL GLQHNKQYTS TKDLRYGHLM
IMTDQDYDGS HIKGLIINLL DHFYPSLLKI PDFLREFITP IVKCTHNRTK EIISFYTIPE
YEQWKSSNDD GKGWTIKYYK GLGTSEAKDA KEYFSDLPTH MKPFRELQQD ERSLIDMAFN
KKKADDRKEW LRTYQPGTFM DHSVDEITIS DFINKELILY SMADNARSIP SVIDGFKPGQ
RKVMYGCFKR NLNKEVKVAQ LAGYISEHSA YHHGEQSLTS TIIGLAYDFV GSNNINLLQP
RGTFGTRAQG GKDAASARYI NTALQPITRL IFHKSDDNLL KYLNDDGQMI EPEWYCPIIP
MVLVNGSEGI GTGWSSYIPN YNPMDLVKNI LRLMEGKEQE PMHPWYRGFK GTIKPLDKDK
YTNNGVIERI SPTEIKITEL PVRTWTQNYK KDLIDKFMGF INKFDEEHKS HTVEFDISLK
EEVADLSDED LAKKFKIIST LATSNMVCFD PEGRLKKYQT PEDILQEFYH IRLDLYSKRK
DYLIAEVKHE CLKLANKVRF INMKIKHQLE FEGLRKKAII ELLEANGFDK VHKRPIIKYG
SEETSESDEE NANDSGYNYL MSTPAWAFSK EESERINSLK NEKEKELKIL EAKPPKEFWK
DDLKAFEDQW NNDLAEFEEN MNAGGVTKKG KKRVGLGISE VKRKKTKL
//
