ID A0A182F1D1_ANOAL Unreviewed; 1536 AA.
AC A0A182F1D1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
OS Anopheles albimanus (New world malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7167 {ECO:0000313|EnsemblMetazoa:AALB000255-PA, ECO:0000313|Proteomes:UP000069272};
RN [1] {ECO:0000313|EnsemblMetazoa:AALB000255-PA}
RP IDENTIFICATION.
RC STRAIN=STECLA/ALBI9_A {ECO:0000313|EnsemblMetazoa:AALB000255-PA};
RG EnsemblMetazoa;
RL Submitted (AUG-2022) to UniProtKB.
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 STRING; 7167.A0A182F1D1; -.
DR EnsemblMetazoa; AALB000255-RA; AALB000255-PA; AALB000255.
DR VEuPathDB; VectorBase:AALB000255; -.
DR VEuPathDB; VectorBase:AALB20_027746; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000069272; Chromosome 2L.
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 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}.
SQ SEQUENCE 1536 AA; 172538 MW; D5B8C1171FE3C30C CRC64;
MTDIRAAFAA QQNGAALAAA ATSSPKIGGK SIEKIYQKKS QLEHILLRPD TYIGSIEMLK
EQMWIYDKEA AKMVQKEITY VPGLYKIFDE ILVNAADNKQ RDPKMSMIKV EINQETNTIS
VWNNGQGIPV VMHKEEKMYV PTMIFGHLLT SSNYNDEEAK VTGGRNGYGA KLCNIFSTKF
TVETATKQYK KCFKQTWGDN MAKASEPKIK EDFHGEDYTK ITFSPDLTKF KMEKLDDDIV
GLLSRRAFDV AASTRGVAVY LNGTRVPVKS FKDYVDLFLK DAKDDMGGQV KMCYESVNER
WEVAVAISER GFQQVSFVNS IATTKGGRHV DYVTDMVVKQ LTEVLKKKNK GGVAIKPFQI
KNHMWVFVNC LIVNPTFDSQ TKENMTLQSK SFGSKCNLSE KFINAVAKSG IVESVLQWAK
FKAQTDLAKT SGSKKSKIKG IPKLEDANDA GSRNSLNCTL ILTEGDSAKT LAVSGLGVVG
RDTYGVFPLR GKLLNVREAT HKQILENAEI NNLIKILGLQ YKKKYLTTED LKTLRYGKVM
IMTDQDQDGS HIKGLLINFI HTNWPELLRL PFLEEFITPI VKATKKNGTE LSFFSLPEFE
EWKAETPNAH TFNIKYYKGL GTSTSKEAKE YFQNMERHRI LFRYEDNGDD DAIMMAFSRK
AVDQRKDWLT AHMEECRHRK QVGLQERYLY TKTTKAISYK DFVNLELVLF SNSDNVRSIP
CMLDGLKPGQ RKVLFTCFKR NDKREVKVAQ LAGSVAEMSA YHHGEQSLCS TIINLAQNFV
GSNNINLLYP GGQFGTRLTG GKDSASPRYI FTMLSSLTRL IFHPLDDPLL EYQYEDNQRI
EPIWYLPIIP MLLVNGAEGI GTGWSTKIPN HNPRDVIANI RRMLNGEEPK VLNPWYKNFR
GLVESVGPQK YLTVGNVALL DGQKIEISEL PIGTWTQTYK ENVLEPLLHG SDKQKAVIAD
YKEYNTDTTV RFVVSFLPGE YAKLYAEEGG FHRVFKLTSS ISTTTMNAFD DKNYLKRYDH
ANSIFQDFYT IRLEYYGKRR EYLLGMLQAE ADSMSDKARF IMEKCNGQLT VENKKRKALI
EEMIKRGYRP DPIKEWKRRV QSAEDQEAEE AAEEEGAEEE DEELQDVKPG KASTSKKGGA
AADPEKAFQR LTDVKKFDYL LGMSMWMLTE ERKNEILKQR DQKLMELKSL QAKTLQMLWM
EDLDALSRKL DEVEEKERLD AISTEKKLKS AAMKGSATAG GRKVVASKKT AIDDTKPSVD
AESVRFRVTE ELLKKYEKAA ATAAAGKVKK EKKEPGENGG GAADGPDEFD ALVEGGTAGE
KPKAKPRVKK EPKEPKVKKE KGSPGEKTAG KRGRKKKTTS SDEDDGAFNS DMSGDEFVPP
VNVPTREKTG RRAAATKKVN YSLLDGGEDD EDANFDRSDD ELFDNNPEGR SAGQAATADS
DSDVEVQESR PAAVVNLDDD EEEDSSPVKK RKPGPNKRAL GPKVADAAAK PAAKRGRKVA
DSSSEAEKPK KKPKKVIVES ESEEDPPSDD DFDSDY
//
