ID A0A1D1VTD4_RAMVA Unreviewed; 1675 AA.
AC A0A1D1VTD4;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN Name=RvY_14533-1 {ECO:0000313|EMBL:GAV04221.1};
GN Synonyms=RvY_14533.1 {ECO:0000313|EMBL:GAV04221.1};
GN ORFNames=RvY_14533 {ECO:0000313|EMBL:GAV04221.1};
OS Ramazzottius varieornatus (Water bear) (Tardigrade).
OC Eukaryota; Metazoa; Ecdysozoa; Tardigrada; Eutardigrada; Parachela;
OC Hypsibioidea; Ramazzottiidae; Ramazzottius.
OX NCBI_TaxID=947166 {ECO:0000313|EMBL:GAV04221.1, ECO:0000313|Proteomes:UP000186922};
RN [1] {ECO:0000313|EMBL:GAV04221.1, ECO:0000313|Proteomes:UP000186922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YOKOZUNA-1 {ECO:0000313|EMBL:GAV04221.1,
RC ECO:0000313|Proteomes:UP000186922};
RX PubMed=27649274; DOI=10.1038/ncomms12808;
RA Hashimoto T., Horikawa D.D., Saito Y., Kuwahara H., Kozuka-Hata H.,
RA Shin-I T., Minakuchi Y., Ohishi K., Motoyama A., Aizu T., Enomoto A.,
RA Kondo K., Tanaka S., Hara Y., Koshikawa S., Sagara H., Miura T.,
RA Yokobori S., Miyagawa K., Suzuki Y., Kubo T., Oyama M., Kohara Y.,
RA Fujiyama A., Arakawa K., Katayama T., Toyoda A., Kunieda T.;
RT "Extremotolerant tardigrade genome and improved radiotolerance of human
RT cultured cells by tardigrade-unique protein.";
RL Nat. Commun. 7:12808-12808(2016).
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:GAV04221.1}.
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DR EMBL; BDGG01000010; GAV04221.1; -; Genomic_DNA.
DR STRING; 947166.A0A1D1VTD4; -.
DR Proteomes; UP000186922; 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; 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; 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:UP000186922};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 521..638
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 46..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1275..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1342..1643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1655..1675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1200
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1342..1417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1418..1442
FT /note="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 1491..1505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1619..1642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1675 AA; 189165 MW; F5123CB7AC956C2B CRC64;
MWRRLFSVTL LPDRKFAATT VGQRTTGCGA LSRSFVPSSV LTRRLKMSSS DEMEPTPVKT
TPKKKTGKQA QTVEEQYVKL KLDEQILLRP DTYIGSIATA EKVKMRIVDL KELKIIEAKI
DYVPGLYKIF DEIVVNAADN KQRDPKMDRL EITIEQENNV ISVFNNGRGI PITKHAKEKV
WIPTMIFGHL LTSSNYQDDD KKVVGGRNGY GAKLCNLFST KFTVETACKK GANYPAKIFK
QTWEQNMKVG EENFQILANE DRKEYTKVTF QPDLRRFNME KLDDHIAGLM ARRAFDLAGT
CKGVKVKLNT KEIKVNGFED YVKFLVKDAK DEYDNPIEKI AFARSDPIKV TNEDGKEISQ
VRWEVACVPS TNGEFQQVSF VNSIATTKGG QHVNYIADQI ADHLITVAKK KNKSGTELTR
NHIKQHMWVF VNCLIENPTF DSQTKEYMTL AKKSFGSTFK LPEKFCKTVA SLSIAESAVA
MMNLKAEAKL QRAGGTKTSR LKGIVKLMDA NQAGSKHSKE CTLILTEGDS AKCLVEAGFA
VVGRDRYGVF PLRGKLLNVR DATSKQLTEN KEIEHLVKIL GLDYRRQYTT EEDFKRLRYG
RLMIMTDQDQ DGSHIKGLLI NFLHAKFPHL LRRTPNNAFL EEFITPIVKV TRKIGGREEE
QSFYSLPEFE QWKSKLDEKE RKGWKEKYYK GLGTSTAKEA KEYFNNLTRH RIKFGYSGAN
DDDNIDMAFS KKRADDRKNW LTEGMRQRTE LKNTNQPPIY LYQKDTKAVT YTDFVNKELY
YFSNMDNERS IPSMVDGLKP GQRKVMFTCF KRNDKKEVKV AQLAGSVGEA SAYHHGEQSL
MSTIVGLAQD FVGSNNINLL QPRGQFGTRN LGGKDSASPR YIFTLLSPTA RAIFHKDDMP
LLNYLYDDNQ KIEPEWYCPI IPMVLVNGAE GIGTGWSTKI PNYNPEDIIN NIRRMLNGEE
PRPMLPWFRG FRGQIQPIDA GRRVVASGVV SVLDEEDSIE ITELPVRTWT QSYKESVIEP
MLTGTEKDGG KGKPQQITDY REYHTDATVR FVVRMQPAKF KEFEREGFHK VFKLQSPMAL
TQMVLFDANG QIKKYDSAEH ILKEFYELRL KRYQMRKDYL VGMLSAAAKK LMNQARFIVE
KIEKKITIEN KKRTIMIDDL IKAKYDPDPE LAWKKSLKQQ QELEEEDEEA EDMVENEGEV
ADDANADKTK DKDKKSDYDY LLGMRMWALT LERKEALLKE RDDKIRELEV MKSRTPKDLW
NADLDALLIA LEKAKDEEHE MHDQPVDGSP DGKKPAKGKG GVKGRGKKNV IPNAADTLPA
KNAKLVEPVI DAALILRLEK ANEAKERKEK GEPAKKGGQK KKEVGEDGEP LETSANDSAE
KPKKKAAAKD TKKTKQTTLD GVVKKTQKKK KGSDNEEESD YDSDNLTDGE DDEEDNETEV
VDKTTTEDEY DFGEKIPEKK NRKVVSNGPS TSKKVESDDD DIQEITEVEN AVKPSKSKGE
AVYEPKKPSS KTLADSSKPA KVSKAAAVPK AAEKPKAADR KKAMTNGTPS KTIKLVSSDE
EDSEDEMPAV KKAAASKAST AASKPAIVKK PVLKRKALDS GTDDEDFEPS TSTPPKKQSK
NDGKAKAKAV VSDSDEEIPP PRARVARAAA VRKVLYSDSS MENLDDDDDY LNSVN
//
