ID A0A1X9I962_9CAUD Unreviewed; 637 AA.
AC A0A1X9I962;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=vB_SenM-2_146 {ECO:0000313|EMBL:ANT44604.1};
OS Salmonella phage vB_SenM-2.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Ackermannviridae; Cvivirinae; Kuttervirus; Kuttervirus Det7.
OX NCBI_TaxID=1868843 {ECO:0000313|EMBL:ANT44604.1, ECO:0000313|Proteomes:UP000224711};
RN [1] {ECO:0000313|Proteomes:UP000224711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Gasior T.;
RL Submitted (APR-2016) 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=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; KX171211; ANT44604.1; -; Genomic_DNA.
DR Proteomes; UP000224711; 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; 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; IPR031660; TOPRIM_C.
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; PF01751; Toprim; 1.
DR Pfam; PF16898; TOPRIM_C; 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.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ANT44604.1}.
FT DOMAIN 270..369
FT /note="DNA topoisomerase type IIA subunit B"
FT /evidence="ECO:0000259|Pfam:PF00204"
FT DOMAIN 427..533
FT /note="Toprim"
FT /evidence="ECO:0000259|Pfam:PF01751"
FT DOMAIN 536..628
FT /note="C-terminal associated"
FT /evidence="ECO:0000259|Pfam:PF16898"
SQ SEQUENCE 637 AA; 71890 MW; 0CA3D2CAFF891FAD CRC64;
MSNKIDIERK YKKLTHIEHI LLRPERHLGS IRSSVGTVWI YDPTKEKVIF RDNFEYSPAL
IKQFDEIITN CVDHSKTPEG KGLTEITVTV SPMNGQIIVS DNGGIPVVKH GVTNEWLPEM
LFGSLYAGSN FNDEDEEYNN QKSGGQNGEG ASLVNVFSKW FRVATSDGKK SYTQLFEDNM
SKKSNPVIGN TPKEFGTTIA WIPDYARLGV KGLDQNNLLM IYRRAFEVAA CNPRLKVVLN
GKQIRIDRFG HFVDYFYAGS AVDETDDWSV AITPSSGAFM HASYVNSIAT HIGGPHVDYV
ADQIVAAIRP QLVKKFKTEL KPAMIKNHMS LFIAADINNP RFDSQTKERM TTPVSQFGTS
YKPSDKLIRK ALEFVTAGLS KELASLRNEQ EDAEFEKAKK DISKRDYREI EKYYPATARG
DRSGCSLLLT EGDSASNPIL NARDTKKIGL FPLRGKFINC LNAPRSKVMA NEEFKNLCTI
HGGAVPGQPL DISRYPQTVV ATDADDDGIH IRGLLITLYC TFWPEYVRQG RLKLLRTPYM
RVWCGNIMHE FMNNAEYEEF LKTPDAKKIT KKKYLKGLGG NSTEDFKRIL NNLDAYTTTV
TLDDGYKQSL KNGFGDEAAD YRKTWFSDVC LFETEDE
//
