ID A0A398AMI3_BRACM Unreviewed; 1412 AA.
AC A0A398AMI3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN ORFNames=BRARA_A00830 {ECO:0000313|EMBL:RID77964.1};
OS Brassica campestris (Field mustard).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3711 {ECO:0000313|EMBL:RID77964.1, ECO:0000313|Proteomes:UP000264353};
RN [1] {ECO:0000313|EMBL:RID77964.1, ECO:0000313|Proteomes:UP000264353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B-3 {ECO:0000313|Proteomes:UP000264353};
RA Bowman J., Kohchi T., Yamato K., Jenkins J., Shu S., Ishizaki K.,
RA Yamaoka S., Nishihama R., Nakamura Y., Berger F., Adam C., Aki S.,
RA Althoff F., Araki T., Arteaga-Vazquez M., Balasubrmanian S., Bauer D.,
RA Boehm C., Briginshaw L., Caballero-Perez J., Catarino B., Chen F.,
RA Chiyoda S., Chovatia M., Davies K., Delmans M., Demura T., Dierschke T.,
RA Dolan L., Dorantes-Acosta A., Eklund D., Florent S., Flores-Sandoval E.,
RA Fujiyama A., Fukuzawa H., Galik B., Grimanelli D., Grimwood J.,
RA Grossniklaus U., Hamada T., Haseloff J., Hetherington A., Higo A.,
RA Hirakawa Y., Hundley H., Ikeda Y., Inoue K., Inoue S., Ishida S., Jia Q.,
RA Kakita M., Kanazawa T., Kawai Y., Kawashima T., Kennedy M., Kinose K.,
RA Kinoshita T., Kohara Y., Koide E., Komatsu K., Kopischke S., Kubo M.,
RA Kyozuka J., Lagercrantz U., Lin S., Lindquist E., Lipzen A., Lu C.,
RA Luna E., Martienssen R., Minamino N., Mizutani M., Mizutani M.,
RA Mochizuki N., Monte I., Mosher R., Nagasaki H., Nakagami H., Naramoto S.,
RA Nishitani K., Ohtani M., Okamoto T., Okumura M., Phillips J., Pollak B.,
RA Reinders A., Roevekamp M., Sano R., Sawa S., Schmid M., Shirakawa M.,
RA Solano R., Spunde A., Suetsugu N., Sugano S., Sugiyama A., Sun R.,
RA Suzuki Y., Takenaka M., Takezawa D., Tomogane H., Tsuzuki M., Ueda T.,
RA Umeda M., Ward J., Watanabe Y., Yazaki K., Yokoyama R., Yoshitake Y.,
RA Yotsui I., Zachgo S., Schmutz J.;
RT "WGS assembly of Brassica rapa FPsc.";
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}.
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DR EMBL; CM010628; RID77964.1; -; Genomic_DNA.
DR Proteomes; UP000264353; Chromosome a1.
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; 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 Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 452..566
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1171..1251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1292..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1016..1043
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1171..1186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1396..1412
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1412 AA; 157962 MW; 4317BD4DA3BC188B CRC64;
MATKLPLQTS NNVNVAKAAA AASRGGKTIE EMYQKKSQLE HILLRPDTYI GSIEKHTQTL
WVYENEEMVN RPVTYVPGLY KIFDEILVNA ADNKQRDPKM DSVKVVIDVA RNLISVCNSG
DGVPVEIHQE EGVYVPEMIF GHLLTSSNYN DNEKKTTGGR NGYGAKLTNI FSTEFTIETA
DGKRQKQYKQ VFENNMGKKS EPVITKCSKS DNWTKVSFKP DLGKFGMTHL EDDVVALMSK
RVFDIAGCLG KTVKVELNGK RIPIKSFTDY VDLYLTAANK SRTEPLPRMV EKVNDRWEVC
VSISEGQFQQ VSFVNSIATI KGGTHVDYVT SQITNYIVGI VNKKNKTANV KAHNVKNHLW
VFVNSLIDNP AFDSQTKETL TLRQSSFGSK CELSEDILKK VAKSGVVENL LSWATFKQSK
DLKKSDGTKT DRVQVEKLED ANKAGGKESQ RCTLILTEGD SAKALAMAGM AVVGRDYYGV
FPLRGKLLNV REATTTQITN NKEIENIKKI LGLKQNMVYE NVNSLRYGHM MIMTDQDHDG
SHIKGLLINF IHSFWPTLLK VPSFLVEFIT PIVKATRKNE VLSFYSMPEY ESWKESLSGN
ATGWTIKYYK GLGTSTSKEG KEYFGNLDIH KKDFVWEDEQ DGEAIELAFS KKKIEARKNW
LSHFEPGTHL DQKQQKISFS DFVNKELILF SMADLQRSIP SMVDGLKPGQ RKILFCSFKR
NFTKEAKVAQ FSGYVSEHSA YHHGEQSLAG TIIGMAQDYV GSNNINLLQP NGQFGTRNMG
GKDAASPRYI FTKLSSATRV LFPKDDDVLL NYLNEDGQKI EPTWYMPIIP TVLVNGSEGI
GTGWSTFIPN YNPRDIVANI RRLLNGESMV AMDPWYRNFK GTIEKTASKE GGSTYTITGV
YEEIDETIIR VTELPIRRWS EDYKQFLEAL KTNNNTPYFQ SVKAYNDDRS VDFELHLSEE
NMMMARQEGI LKMLKLTTTI ATTNMHLFDE NNLIKKYASP EQIVEEFFQL RLQYYEKRKR
VILENLELEL LKLENKVKFI LGVVSGEIIV NNRKKSELVQ ELGQKGFTPF PKKGKPVEAA
VAGATDSAEE ESEETSGVPG SRSTFISGSE YDYLLSLAIA TLTLEKVQEL CGERDKMEKA
VEDMKKATPR SLWFRDLESL DAELDKLDQE DAEAEKEIEK AQKKLRAKAG APKGGKAAAP
RKQAPKKTTK AASSSAMEIG DNVVEVAKPK GRQGAKKKAP AAAPADVKAD DDEMMDLAQR
LAQYNFGSTS ENPSKAAISL NDDEDDVVVE VAAPAKGGRK PAAASKTVKP PAAPRKRGPA
ASKKQPAAEV VTVSPEKKVR KMRSSPFNKK SSSVLGRLAN KEGEEESTET VAVETSSRPK
RANRKQMKYV LSDSESENDS EFDDIEDDEY DE
//
