ID A0A094L090_ANTCR Unreviewed; 1183 AA.
AC A0A094L090;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
DE Flags: Fragment;
GN ORFNames=N321_08950 {ECO:0000313|EMBL:KFZ64793.1};
OS Antrostomus carolinensis (Chuck-will's-widow) (Caprimulgus carolinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Caprimulgiformes;
OC Caprimulgidae; Antrostomus.
OX NCBI_TaxID=279965 {ECO:0000313|EMBL:KFZ64793.1, ECO:0000313|Proteomes:UP000053620};
RN [1] {ECO:0000313|EMBL:KFZ64793.1, ECO:0000313|Proteomes:UP000053620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N321 {ECO:0000313|EMBL:KFZ64793.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Key decatenating enzyme that alters DNA topology by binding
CC to two double-stranded DNA molecules, generating a double-stranded
CC break in one of the strands, passing the intact strand through the
CC broken strand, and religating the broken strand.
CC {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|RuleBase:RU362094};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU362094};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU362094};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU362094}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00011080, ECO:0000256|RuleBase:RU362094}.
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DR EMBL; KL359973; KFZ64793.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094L090; -.
DR Proteomes; UP000053620; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:SF61; DNA TOPOISOMERASE 2-ALPHA; 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|RuleBase:RU362094};
KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
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|RuleBase:RU362094};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053620};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 400..517
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1033..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFZ64793.1"
FT NON_TER 1183
FT /evidence="ECO:0000313|EMBL:KFZ64793.1"
SQ SEQUENCE 1183 AA; 134984 MW; BBA70C3BBD6AB8BF CRC64;
PSFQQMWVFD EGVGLNCRDV TFVPGLYKIF DEILVNAADN KQRDKSMSCI KVTIDVENNT
ISVWNNGKGI PVVEHKVEKV YVPALIFGQL LTSSNYDDNE KKVTGGRNGY GAKLCNIFST
KFTVETACRE YKKLFKQTWT NNMGKAGEVH LKYFDGEDYT CVTFQPDLSK FKMTILDKDI
VALMSRRAYD IAGSTKDVKV FLNGQRLPVK GFRSYVDLYL KDKEDETGNA LKVIHEEVNS
RWEVCLTLSE KGFQQVSFVN SIATTKGGRH VDYVADQIVT KLIDIVKKKN KNGVGVKPFQ
VKNHMWIFVN ALIENPTFDS QTKENMTLQA KSFGSTCKLS EKFIKGVIGC GIVESILNWV
KFKAQNQLNK KCSAVKHTKI KGVPKLDDAN DAGSKNSLDC TLILTEGDSA KTLAVSGLGV
VGRDKYGVFP LRGKILNVRE ASHKQIMENA EINNIIKIVG LQYKKNYEDQ ESLKSLRYGK
IMIMTDQDQD GSHIKGLLIN FIHHNWPSLL RHNFLEEFIT PIIKASKNKE EIAFYSIPEF
EEWKSSTQNY NSWKIKYYKG LGTSTSKEAK EYFADMAKHR IGFKYSGPED DAAITLAFSK
KKVEERKEWL TNFMEDRRQR KLHGLPEEYL YGKNTNYLTY NDFINKELVL FSNSDNERSI
PSLVDGLKPG QRKVLFTCFK RNDKREVKVA QLAGSVAEMS SYHHGEASLM MTIINLAQNF
VGSNNLNLLQ PIGQFGTRLH GGKDSASPRY IFTMLSPLAR LLFPPTDDNI LRFLYDDNQR
VEPEWYMPII PMVLINGAEG IGTGWSCKIP NFDIREVVNN IRRLMDGEEP LPMLPSYKNF
KGTIDELGPN QYVISGEVSI LDSTTIEITE LPVRTWTQTY KEQVLEPMLN GTEKTPPLIT
DYKEYHTDTT VKFIVKMTEE KLAEAKAAGL HKVFKLQTNL TCNSMVLFDH VGFLKKYDSA
QDILKEFFEL RLRYYNLRKE WLIGMLGAES AKLSNQARFI LEKIDGKIVI ENKPKKELIQ
VLIQRGYESD PVKAWKESQN KEEEEGEEDE SDKESAGATG PDFNYLLNMP LWYLTKEKKD
ELCKQSDKKQ KELEDLKCKT PSDLWKEDLA VFVEELDVLE NQQIQDEMAG FAGKPLKVKG
GKMKVKKMQV SEVMPSPHGE RVVPRITAEM RAEAEKRTKR KVK
//