ID F4YA40_9CAUD Unreviewed; 616 AA.
AC F4YA40;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
OS Fletchervirus NCTC12673.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Eucampyvirinae; Fletchervirus.
OX NCBI_TaxID=934027 {ECO:0000313|EMBL:AEA86362.1, ECO:0000313|Proteomes:UP000008310};
RN [1] {ECO:0000313|EMBL:AEA86362.1, ECO:0000313|Proteomes:UP000008310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21965409; DOI=10.1128/AEM.05562-11;
RA Kropinski A.M., Arutyunov D., Foss M., Cunningham A., Ding W., Singh A.,
RA Pavlov A.R., Henry M., Evoy S., Kelly J., Szymanski C.M.;
RT "Genome and Proteome of Campylobacter jejuni Bacteriophage NCTC 12673.";
RL Appl. Environ. Microbiol. 77:8265-8271(2011).
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=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; GU296433; AEA86362.1; -; Genomic_DNA.
DR RefSeq; YP_004421570.1; NC_015464.1.
DR GeneID; 10896825; -.
DR KEGG; vg:10896825; -.
DR Proteomes; UP000008310; 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; IPR006171; TOPRIM_domain.
DR PANTHER; PTHR10169:SF38; DNA TOPOISOMERASE 2; 1.
DR PANTHER; PTHR10169; DNA TOPOISOMERASE/GYRASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
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; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AEA86362.1}.
FT DOMAIN 409..517
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 616 AA; 70142 MW; 85F04C5BC375201C CRC64;
MIENKIVHAE NEVEYYLNLP HLITGALTSF NNTVKVLENN KIINKEIVYN QTLTKQIDEA
IQNSIDEFTR TGGKYANKIS LKIDKDSGII TISDNGRGLP IDTYVMATTK FRTSSNYTFL
EKEKKDRITI GAHGIGSKLI PLFSSEYQLT TITLEGDRGI VKCLNNMSII EHKEDKAPAS
STHGVTIKFK PDFERLELKE INDDLINHIH ALLINIAYSN PGIEFTFQGK LIKVKEFKEF
IKYYSDSFSI LQSDENLELA IFPTDEYKFV HIVNSLDLNK GGVALDYISN NIVNAFGNRL
RKGYSKITNT AVKSRIGVIL ILKNKKNLRF GGGQTKEEIK NTITELGIPT LKYTDFAELL
FKNTHIKDPI IELYKVQQEL ENRKQNTFER KEAKERFNPK FTKHTKDPKF MYIAEGDSAL
SSLIQAVGRD CSSFLPLTGK LQNALKCSTA QLLKNQRVMD IVEAMGLGLP ETKYENMVIA
TDADLDGNHI ACLITALVYK LQPNLLTEGR VYRLKTPIIS VLQNDKLIKW YYTLGEYQKD
QDNLPKNAEV IYMKGLGSWS AANYRIVFAK DGIDNCLEKI EWKDNDEKVL EQWMSDNGID
FRKQILSTKS FNIENL
//
