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Database: UniProt
Entry: A0A094L090_ANTCR
LinkDB: A0A094L090_ANTCR
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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
//
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