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Entry: A0A2L0UZ51_9CAUD
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ID   A0A2L0UZ51_9CAUD        Unreviewed;       604 AA.
AC   A0A2L0UZ51;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
OS   Agrobacterium phage Atu_ph07.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Polybotosvirus; Polybotosvirus Atuph07.
OX   NCBI_TaxID=2024264 {ECO:0000313|EMBL:AUZ94816.1, ECO:0000313|Proteomes:UP000223025};
RN   [1] {ECO:0000313|EMBL:AUZ94816.1, ECO:0000313|Proteomes:UP000223025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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   -!- 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   -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC       {ECO:0000256|ARBA:ARBA00011080}.
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DR   EMBL; MF403008; AUZ94816.1; -; Genomic_DNA.
DR   OrthoDB; 931at10239; -.
DR   Proteomes; UP000223025; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
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   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; IPR013759; Topo_IIA_B_C.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR   InterPro; IPR001154; TopoII_euk.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   PANTHER; PTHR10169:SF38; DNA TOPOISOMERASE 2; 1.
DR   PANTHER; PTHR10169; DNA TOPOISOMERASE/GYRASE; 1.
DR   Pfam; PF00204; DNA_gyraseB; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   PRINTS; PR01158; TOPISMRASEII.
DR   PRINTS; PR00418; TPI2FAMILY.
DR   SMART; SM00433; TOP2c; 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   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AUZ94816.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000223025}.
FT   DOMAIN          402..519
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   604 AA;  69195 MW;  1264C0FBA077F5DD CRC64;
     MYLGSPDPHT QQIISYDNGQ PILAEMTWVP ALYTGFREII DNALDEVVGH GFGNRIDITY
     NEKDLIFSVK DNGRGIPITY DEEHQMYAAT MALTEPKAGR NFEERGAVAG TNGIGASATN
     ITAEYFNFEI VRDGKKFKQR CTEGNVVLGD YLQIFDPEIT KSASSSYTYI EYKPSREVYK
     HRILPEQFVK DRLYEIAVAN PDIKISYNGE VIKVKLRPEQ NLFPNKKPII IEHHNENMRV
     KFWLLPEWSK ENEFMTTIVN NINAFNGGVH METFRRSFLT NFLNSLTKES KRRKLQPNRS
     DVTEGLLIYN ITVMNAPNFD SQSKTRLINE EVEKELKKAF DDEALYKNII KKNPEWIEAI
     FERCARRTMK KDASEIEKIA KKNSRLKIAK LMDATGKDRS KCILLLGEGD SAIAGAAAVR
     DPEIHGGLPL RGKVLNVTGE DLKKVVNNAE LINITTSLGL VIGQKADREN MRYGQVYIAT
     DSDEDGKNIA ALLVNFFNTF WPELLEDTEK PFLNIFQTPF IIMEKGKQRQ YVYAHNYSEF
     DPKDYSGWQI IRAKGLGTLE EVDWKYALDN PLLFPIIKDE NLNDTLDLIF NEKRADDRKE
     WIGM
//
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