ID A0A1E7F6K6_9STRA Unreviewed; 1167 AA.
AC A0A1E7F6K6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
DE Flags: Fragment;
GN Name=Top2a_1 {ECO:0000313|EMBL:OEU13493.1};
GN ORFNames=FRACYDRAFT_145893 {ECO:0000313|EMBL:OEU13493.1};
OS Fragilariopsis cylindrus CCMP1102.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Bacillariales; Bacillariaceae;
OC Fragilariopsis.
OX NCBI_TaxID=635003 {ECO:0000313|EMBL:OEU13493.1, ECO:0000313|Proteomes:UP000095751};
RN [1] {ECO:0000313|EMBL:OEU13493.1, ECO:0000313|Proteomes:UP000095751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1102 {ECO:0000313|EMBL:OEU13493.1,
RC ECO:0000313|Proteomes:UP000095751};
RG DOE Joint Genome Institute;
RA Mock T., Otillar R.P., Strauss J., Dupont C., Frickenhaus S., Maumus F.,
RA Mcmullan M., Sanges R., Schmutz J., Toseland A., Valas R., Veluchamy A.,
RA Ward B.J., Allen A., Barry K., Falciatore A., Ferrante M., Fortunato A.E.,
RA Gloeckner G., Gruber A., Hipkin R., Janech M., Kroth P., Leese F.,
RA Lindquist E., Lyon B.R., Martin J., Mayer C., Parker M., Quesneville H.,
RA Raymond J., Uhlig C., Valentin K.U., Worden A.Z., Armbrust E.V., Bowler C.,
RA Green B., Moulton V., Van Oosterhout C., Grigoriev I.;
RT "Extensive genetic diversity and differential bi-allelic expression allows
RT diatom success in the polar Southern Ocean.";
RL Submitted (SEP-2016) 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}.
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DR EMBL; KV784361; OEU13493.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E7F6K6; -.
DR EnsemblProtists; OEU13493; OEU13493; FRACYDRAFT_145893.
DR KEGG; fcy:FRACYDRAFT_145893; -.
DR InParanoid; A0A1E7F6K6; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000095751; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000095751};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 434..550
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1063..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1107..1165
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OEU13493.1"
FT NON_TER 1167
FT /evidence="ECO:0000313|EMBL:OEU13493.1"
SQ SEQUENCE 1167 AA; 131741 MW; 72D2B33520894715 CRC64;
KTVEETYQKK SQLEHILLRP DTYIGSVEPM TEQMFIYDEV EDAIINKTIT YTPGLYKIFD
EIIVNAADNK QRDENMDRLD VTIDEDNNSI SVKNNGKGIP VVRHGEHDCY VPTLLFGNLL
TGSNFDDNEK KTTGGRNGYG AKLANIFSTK FIVECVDVEN GKKFQQTFTK NMGHASEPII
KNITANERKK GDYTQITFSP ELSRFKMTSL DKDTVGLLSK RAYDIAGSMA NSKGKKLSVT
LNGKKLPIKS FQDYIKIFRG VNPPCAFERV DDKWEVGVSH SEDGSPMQIS FVNAICTSKG
GTHVSFVADK IAMSLAKAVE KKNKGGTKIS NNQIKNHLCI FVNALVENPT FDSQTKDHLT
NRKNCYKDEC ELSDKFLKAA CSAKGEILDS ILSFAMFKAK KELKKTGGSK KIKLTGIQKL
DDANRAGSKD SLKCTLILTE GDSAKSLAMS GLSVIGRDHY GVYPLKGKPL NVRDASHTQV
MKNEEIKNVI EILGLKHGVV YDETNLKTLR YGHLMIMADQ DHDGSHIKGL IINFLHTFWP
SLLDIPGFLQ QFITPIVKVT KGKKSETFFT IPQYEEWKEE TGNNGKGWKI KYYKGLGTST
AADAKEYFSN LDLHEVGFER ISLDSTSYGD GLIDMVFNKK RANDRKDWLQ QFEKDTYLNY
SDAQKGAGVK YSQFINEEYI LFSRADCERS IPHVMDGFKP SQRKVLFACF KRKLKDEIKV
AQLSGYIGEH SAYHHGEASL HTTIINMAQT YVGSNNINLL TPSGQFGTRR MGGKDHASPR
YIFTMLEKIT RAIFHPDDDE LLNYLHDDGV SIEPDYYMPV IPMVLVNGSD GIGTGWSSKV
PNYDPRQIIS NIRKMIKGEP VVKMDPFYSG FSGKIKPEGD GKYSVHGIIE REDDETLLIS
ELPVRGWTQD CKIALEKMIV SEKPGVTPEI KDFAENHTDT TVSFTITADK ASIDKWEKLP
KGGLYAKFKL ISSTSTTNMH LYDNERKIVK YEQPENILES FFGTRMEFYV KRKALLVKKL
HQEQKMLSNK ARFVDEVCNR TLVVSNRKKT ELLKELQSSG YDLFDKTNNG SNHDSDDDED
EEDSTSTSDL SKGYDYLLGM RIMALTYEKA ELLRKQLAER TAELEKLEAK TPSEIWCEDL
DAIEVALKER DEEILQAEVN EVNAQKK
//
