ID A0A1H8PDC0_9FLAO Unreviewed; 897 AA.
AC A0A1H8PDC0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Topoisomerase-4 subunit A {ECO:0000313|EMBL:SEO39638.1};
GN ORFNames=SAMN04487942_2636 {ECO:0000313|EMBL:SEO39638.1};
OS Flavobacterium sinopsychrotolerans.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=604089 {ECO:0000313|EMBL:SEO39638.1, ECO:0000313|Proteomes:UP000198657};
RN [1] {ECO:0000313|EMBL:SEO39638.1, ECO:0000313|Proteomes:UP000198657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8704 {ECO:0000313|EMBL:SEO39638.1,
RC ECO:0000313|Proteomes:UP000198657};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FODN01000006; SEO39638.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8PDC0; -.
DR STRING; 604089.SAMN04487942_2636; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000198657; 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:SEO39638.1};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 48..482
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 366..393
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 897 AA; 101366 MW; 4E16E9CC02FB677D CRC64;
MKDEEDENIL PQGQEEENTA GEDAFEDIIS TGGQHFYDNQ EDGKDTITKV TGMYKDWFLD
YASYVILERA VPAIEDGFKP VQRRIMHSLK ELDDGRYNKV ANVVGHTMQY HPHGDQSIGD
AMVQIGQKEL LIDCQGNWGN ILTGDGAAAS RYIEARLSKF ALEVIYSPKI TDWGVSYDGR
RAEPNNLPVK FPLLLASGAE GIAVGLSTKV LPHNFNELID SSIKILKGKP FTLYPDFLTQ
GIADVSNYND GLRGGRVRVR AKIAQLDKNT LVITQIPFST NTTTLIDSIL KANDKGKIKI
KKIEDNTAAE VEILIHLFPG VSPDKTIDAL FAFTACETSV APLGCVIEDN KPLFIGVSAM
LKISTNRTVQ LLKSELEIQL SELEEQWHFL SLERIFIENK IYRDIEEMTT RETVIKAVDD
GLKPHTKHLK RAVTEEDILR LLDIRIMRIS KFDSNKAQDK IESLEGDIEQ VKHNLEHLID
FAIAYFTKLK EKYGKGRERQ TELRVFDDIE ATKVVLRNTK LYVNKEEGFV GTSLKKDEYV
TDCSDIDDVI VFLRDGKMMI TKVDAKTFVG KDIIHIAIFD KSDKRTIYNM IYRDGKSGPS
YIKRFNVSGV TRDKAYDLTN ETAGSQVLYF SCNPNGEAEV ITILLRQIGT VKKLKFDIDF
ASLAIKGRSS KGNLVTKYPI KKIELKEKGI STLLPRKVWF DDTVQRLNVD ARGELLGEFR
PNDKILVISQ SGKIKVITPE LSTHFDEDMI VLEKWIPKKP ISAIYYDGEK ERYYIKRFLV
ETENKEESFI TEHPNSHLEI VSTDYRPVAE LVFTKVKGVQ KENMTVDIES FIALKGFKAL
GNQLTTDKLK QVNLLASLPY EVPVEVIPEE LEVKGETDAD DASIQLDDDG QITLSLE
//
