ID A0A195C4U4_9HYME Unreviewed; 1502 AA.
AC A0A195C4U4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN ORFNames=ALC62_13740 {ECO:0000313|EMBL:KYM95625.1};
OS Cyphomyrmex costatus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Cyphomyrmex.
OX NCBI_TaxID=456900 {ECO:0000313|EMBL:KYM95625.1, ECO:0000313|Proteomes:UP000078542};
RN [1] {ECO:0000313|EMBL:KYM95625.1, ECO:0000313|Proteomes:UP000078542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS0001 {ECO:0000313|EMBL:KYM95625.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYM95625.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Cyphomyrmex costatus WGS genome.";
RL Submitted (MAR-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; KQ978287; KYM95625.1; -; Genomic_DNA.
DR RefSeq; XP_018403240.1; XM_018547738.1.
DR STRING; 456900.A0A195C4U4; -.
DR GeneID; 108780140; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000078542; 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; 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:UP000078542};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 447..564
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1225..1502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1130..1180
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1225..1251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1303..1322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1346..1369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1383..1411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1502 AA; 171697 MW; 75CFDD4B70560D33 CRC64;
MSSAVANGAG NSKPTSKQKT IEGIYQKKSQ LEHILLRPDT YIGSVEPVTE MMWVFDKEKE
MMVQKDIKYV PGLYKIFDEI LVNAADNKQR DPKMDAIKID IDSENNTISV WNNGKGIPVV
IHKEENMYVP TMIFGHLLTS SNYDDEEEKV TGGRNGYGAK LCNIFSHRFT VETATKEYKK
CLKQTWGDNM GKASEPRIKE YSGEDFTKVT FSPDLSKFKM QSLDDDIVSL MSRRAYDVAA
STKGVKVFLN GSRIPVKNFK DYVDFYIKGK EDDIGNPLKI VYEACSPRWE VALTLSDKGY
QQMSFVNSIA TTKGGRHVDH VTELIVKQLI ETLKKKNKAG VAIKPFQIKN HLWIFVNCLI
NNPTFDSQTK ENMTLQPKGF GSKCTLSDKF ITSITKIGVV EAVLTWAKFK ADSQLEKLGP
KSKQRKLHGI PKLEDANDAG TAKSLECTLI LTEGDSAKTM AVSGIASIGR DKYGIFPLRG
KMLNVREATH KQILENAEIN NLIKILGLQY KKKYESREDM KTLRYGKMMI MTDQDQDGSH
IKGLLINFIH HNWPSLLKLN FIEEFITPIV KATKGSQVLS FFSLPEFEMW KKETENFHTY
KIKYYKGLGT STAKEAKEYF ENMARHRIRF RYDGEQDDQN IMMAFSKKCV DQRKDWLMNH
MNETKRRKEI GLSERYLYEK DTRTVSFSDF INVELVLYSN YDNVRSIPNM MDGFKPGQRK
VMFTCLKRND KREVKVAQLA GSVAEHSAYH HGETSLMATI VNLAQNFVGS NNINLLQPIG
QFGTRLAGGK DSASPRYIFT MLSPLARYIF HKHDDPLLKH EYDDNQRIEP VHYIPVIPMV
LINGADGIGT GWMTKIPNYN PREIIENLQR MMDGADPKPM IPYYKNFKGV VESCGDFRYV
ISGEISVIGP DKVEITELPI GTWTQTYKET VLEPMLHGTD KTPAIITDYK EYNTDTAVHF
IVIMNRDKLV ELERDGLHKI FKLQTTMTIT SMCAFDENLC LNKYDSVIQI LKGFYKVRLE
TYYKRKDYLE GVLQAEATKL SNQARFILEK CDGTLVIENK KKKDMIAELV RRNYESDPVV
AWKLSQNREQ VLEEVAENDE ESTPTTSTIE KENFDYLLGM TMWSLTKEKK DDLLRQRDEK
IAELKRLQAR TPISLWKEDL DNLLTELNKV EEKEQKEQIK TKQNVKKPPS KFYSKMEDTR
RIVPVIDVEL KKKIEKADIV SKDKKEGVKK SRVKKEQISM EDKDEFDVLV DSNTKSLEQR
LGSSPEKLEK KPAKKGLKQT TLQFKPIKKG AKKKDNDSDE SNDIDFGSIS PLPQPRTSRR
NTAKKNYNFD SDDSDASQEL FNRSSDSEQA FKKKETLIEL SDSDDNIKPN KKPQPAPTSE
ELFDSLVGSS PEKQSSLEKK PLVSSSGEDS PTKFMPPKKA RTKKKTENGG NKGVKRQKKK
LKSSEDSDTD DLLFTTKQKK KKKKTSESDE EIVSDNSPPR TFGRARKPVS YALKSDDSDD
SD
//
