ID A0A067TPS2_GALM3 Unreviewed; 2702 AA.
AC A0A067TPS2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|ARBA:ARBA00019635};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
DE AltName: Full=DNA topoisomerase II {ECO:0000256|ARBA:ARBA00031138};
GN ORFNames=GALMADRAFT_149704 {ECO:0000313|EMBL:KDR85220.1};
OS Galerina marginata (strain CBS 339.88).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Galerina.
OX NCBI_TaxID=685588 {ECO:0000313|EMBL:KDR85220.1, ECO:0000313|Proteomes:UP000027222};
RN [1] {ECO:0000313|Proteomes:UP000027222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 339.88 {ECO:0000313|Proteomes:UP000027222};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(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=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 -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00011080}.
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DR EMBL; KL142367; KDR85220.1; -; Genomic_DNA.
DR STRING; 685588.A0A067TPS2; -.
DR HOGENOM; CLU_227317_0_0_1; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000027222; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR GO; GO:0061982; P:meiosis I cell cycle process; IEA:UniProt.
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; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR Gene3D; 3.40.250.10; Rhodanese-like 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; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_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 InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
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; PF00581; Rhodanese; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF16898; TOPRIM_C; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR01158; TOPISMRASEII.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00433; TOP2c; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000027222}.
FT DOMAIN 534..648
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT DOMAIN 1585..1701
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 1915..2208
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 2164..2185
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1265..1487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1744..1772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1825..1853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2282..2323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2337..2357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2375..2436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2458..2511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2584..2611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2628..2702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1190..1217
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1176
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1443..1462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2375..2423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2466..2488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2593..2607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2641..2677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2702 AA; 299970 MW; AFF6AF511EF0D6E1 CRC64;
MSSSEGEDFQ NFDNVMSGSE SEDYEPVAKK AAPKPKSAPK VAGKPKPSTV KAKPKATLKK
VLVDHDDNAD ENAMDIDKDA SDDEQPNAST SKSEPKKKKT ATETYTKLTQ LEHILKRPDS
YIGSVETITQ TMWTYDAETK RMVYRDVKYV PGFFKIVDEI LVNAADNKIN DSNMDTLKVT
IDVEESTISV FNNGRGIPIE IHEREKIYVP ELIFGHLLSS SNYDDDEKKL TGGRNGYGAK
LANIYSHEFT VETADKNTQQ KYRQTWTDNM GKCGKPKITK NPKSEEYTRI TFKPDLKRFG
MDKIDEDTAS LLRKRVYDMA GVVKDIKVFL NDERLKIKNF KQYVEMYINS AQAEAAETSG
GAAQPKPTVI HDQAGSRWEI AFAVSDGTFQ HVSFANSIST SKGGTHVAYI ADQIAKNLVT
AISKKNKAAT VKPAQIKNHM WIFINALIVN PTFDSQTKET LTLPASKFGS KPVLSEDFMK
KVLKSSIVDN VLNWAKYKAD QQIKKTDGTK RERLLGLTKL SDANNAGTKH AKDCTLILTE
GDSAKALAVG GLGVVGRDNF GVFPLRGKLL NVREAKHDQI MKNEEIQNIK KIMGLQHNKD
YSSTTSLRYG RIMIMTDQDH DGSHIKGLLI NFLDHFYPSL LKLPEFLVEF VTPIVRVTKG
KQRRDFFTIP EYEQWLEDTP DAKRWVSKYF KGLGTSEDAD AREYFNHMEK HMIPFAPMEE
GERDLIDLAF SKKKADDRKE WLRQFKPGTY LDHRMDEIPY TDFINKELIL FSMADNIRSI
PSVADGLKPG QRKVIWGLFK RKLKTEAKVF QLCGYIAEKS AYHHGEVSLG ATIINLAQEF
VGSNNLNLLR PKGQFGTRDT GGKDHAAARY IFTEPMPLAR VIFNPSDDPL LNQQKDDNSL
IEPEFYMPII PLVLINGAEG IGTGWSTNIP CYNPTDIVAN IRRLMNGEEL VPMVPWWRGF
KGEIKPVAKH KYDVFGVVKK LNDTTVEITE LPIHRWTQPY KAELEAMILG DKEKDREGVI
KDFKEHHDNM NVHFIVTMSA KDLEKAEEQG LLEFFKLTSK LNTSNMICFD FEGKIKKYDS
PEEILEDFYP IRLAYYQKRK DFAANEIQTQ FEKLMNQARF VQMIVNKELV VSNRKKVDIV
ADLRKHKFRP FPKNAKNKGD EEEEEEEVDG NEAGNEADSD FDYLLGMAIW SLTKEKIERL
KEQAAEKEAE LLALLEKSPK DLWNTDLDMF VKEWERSCIE FEEKKIMGAN GKKVKRKQAV
LRTRKSIGTR DGSDNDDDFK PIKATAAAKR KPAETKRVAS GSKEKEDVKP KKEDAPPKRK
AAVQQKKVIE LDDSDDEAAP PPKPKSKTTA KKPAVAIKSD EEDEPPLPKS KPKAPAKKPV
GSESDSDVEV VEKAPTKPIA GSDSDQAPPK RKAASKPMVI DSDSESDAAP SKGKGKAPVR
PKRKSMGSTD SESEDELAPS KPAKKIKAGP AGKLARKMKP ASPKKGSSDY ETIAVARAPG
RAAKAGAKKY VEIVSDDSES GGSMFVDDFA ANPVAVPCHP HAHFAKAIAD RFASSPMLSA
QTTPVPAPSS PFPAIDLPDL PACLDDPATL LLDIRPHAAY SNARIPRAVS LSVPSTLLKR
PLFSLERLSA MLPSASARNR FSAWHAASRI LVYDADSVAV ADSSNIAGLL RKFKSDGFQG
DLVWLKGGFQ AVWRDRRDLI DTLPPTPDAE ADDEDDDHHK SSILRTRHLP MAAFSLSSTT
VHNSPHFNSS VAPPARRPPS LHPLPAATSA SANSHPAFNP FFDTIRQNTE LSHGITERIP
LRLPRRVRRR IPDLPFPWLQ EIARRAANAP PHDKSLSDSS SSESEDDEGA NPTDIEEGKE
ALAMQFFKIE LSEQRRLMGV MEHHSKESGQ HSEQSSQSAV PFPYSITAGV EKGAKNRYRH
IWPFEHARVR LHQKREADDD YVNASYIQPL GTNRRYIATQ GPLPATFTDF WTLCWEQNVH
VIVMLTREVE GAMVKCGAYW TDTVFGPLRL RLVSTEGLAP PDERPATAGF FAGHSTMSVH
SSRPQSRRFP HSAGSQRRYR HHHYHNKRSE TVKRTFELTH IGYPAVKPRK IIHLQYLEWP
DLNVPEDPRG VLSLIKQVDE AVEETRMDAQ LSDVKKRKKG DQIPIHEIDE NSGIGKHALA
SNHPVLLHCS AGVGRTGGFI AVDAILDAIR REVRSKNMGA TDDDAMDVDH GDTKGTISTA
PLAVSSGVEC GKTAEQGSGL LVHVPVATPM QVDQPDSAGS DVGCPATFPS GTMRWAENVR
DETGVSGTSA QRQPTIQDEV VSANSTASLS TPGSSRGGSS SETRQFHGSY YYNSSSSIGT
SVSGTSSSSK ANIPSSSYTR DISLTSDLRQ TALNNQQSAI ERTRTMSTPS MNTRTLPPSL
SKGSLPQLGQ AARSTPSLSK QSERTNGQKD ESPTNRVAQT SALSFDFSNT SPFKLKSLVG
GMSSDGEPPS RSQSPSADEA TTYRLSLPPQ PSIPVIPSYP MDGSSPEEQQ TKTFDYKEPR
PLHEDHTPPV LTTLGDPIWE VIQDMREQRM SLCQSLRQYV FVHAAIIEGA LMVIDEEREI
AEGLKPRTRS SKADQESSPT SPVFTDAQPP LRVQPTHPYS HEIASIASSS SMSIGKRGAS
PTELTKEDKE GDVMLSKRPS IKRKQRSGDD LLVDDARYHP VPARATPRAL HAGVSSARAM
PP
//
