ID A0A161UCY6_9FLAO Unreviewed; 881 AA.
AC A0A161UCY6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=DNA topoisomerase IV {ECO:0000313|EMBL:KZE84848.1};
GN ORFNames=AV926_02420 {ECO:0000313|EMBL:KZE84848.1};
OS Myroides marinus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Myroides.
OX NCBI_TaxID=703342 {ECO:0000313|EMBL:KZE84848.1, ECO:0000313|Proteomes:UP000076630};
RN [1] {ECO:0000313|EMBL:KZE84848.1, ECO:0000313|Proteomes:UP000076630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L41 {ECO:0000313|EMBL:KZE84848.1,
RC ECO:0000313|Proteomes:UP000076630};
RA Hong K.W.;
RT "Whole genome sequencing of Myroides marinus L41.";
RL Submitted (JAN-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 -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000256|ARBA:ARBA00008263}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZE84848.1}.
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DR EMBL; LQNU01000002; KZE84848.1; -; Genomic_DNA.
DR RefSeq; WP_038985186.1; NZ_LQNU01000002.1.
DR AlphaFoldDB; A0A161UCY6; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000076630; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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-EC.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
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; IPR002205; Topo_IIA_dom_A.
DR PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:KZE84848.1};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 35..469
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 349..380
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 881 AA; 100499 MW; 082ED9B48E1DCA25 CRC64;
MSQEENLEQE LNNTNNEHQV EDFSDAQEEV TETITKVTGM YKDWFLDYAS YVILERAVPA
IEDGFKPVQR RIMHSMKELD DGRYNKVANI VGHTMQYHPH GDASIGDALV QLGQKDLLID
MQGNWGNILT GDGAAASRYI EARLSKFALD VLYSPKITNW QASYDGRRNE PINLPVKFPL
LLAQGGEGIA VGLSTKILPH NFNELIDASI KILKGKPFTI YPDFPTEGIA DVSNYNDGAR
GGRVRVRAKI APLDKNTLVI TQIPFSTTTT SLIDSILKAN EKGKIKIKKI EDNTAAQVEI
LIHLPPGTSP DKTIDALYAF TACETSIAPL GCVIQNNRPL FTGVSEMLKN STEQTVELLR
KELEIELNEL EEKWHFLSLE RIFIENRIYR AIEEEETWEG VLSAIDEGLK PFVKNLKRAI
TQDDIARLTE IRIKRISRFD IDKANQNIEA LEGEIETVKF NLEHLVDFAI KYFTTLKEKY
GKGRERLTEL RNFDTIEATK VVLRNTKLYV NREEGFFGTG LRKDEYVCDC SDIDDVIVFL
RDGSMMVSRV DEKKFVGKDI IHIAVWDKSD KRTIYNIIYR DGKSGSSFIK RFNVTGVTRD
KMYPLTQDKP GSQILYFSAN PNGEAEVVTI ILRQLTSVKK LKFDLDFAEL LIKGRAAKGN
VVTKYAIKKI ELKEKGISTL RPRKIWFDET VKRLNVDGRG ELLGEFKPED RLLIVSQSGK
VKTIIPELTT HFEEDMIVLE KWKANKPISA LYFDGEKMRY YLKRFLIENE NREELFITEH
ANSRLEIVST DFRPVFEIVY PKVKGVQKEN QTIDVEQFIT IKGIKALGNQ ISVDKIKQVN
ILESLAYTEE EEEEEEEEET IIIGEAPNTE IDDDGQQTLL F
//