ID A0A434AY02_9BACT Unreviewed; 866 AA.
AC A0A434AY02;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=DNA gyrase/topoisomerase IV subunit A {ECO:0000313|EMBL:RUT79338.1};
GN ORFNames=DLK05_03705 {ECO:0000313|EMBL:RUT79338.1};
OS Ancylomarina longa.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae;
OC Ancylomarina.
OX NCBI_TaxID=2487017 {ECO:0000313|EMBL:RUT79338.1, ECO:0000313|Proteomes:UP000282985};
RN [1] {ECO:0000313|EMBL:RUT79338.1, ECO:0000313|Proteomes:UP000282985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T3-2 S1-C {ECO:0000313|EMBL:RUT79338.1,
RC ECO:0000313|Proteomes:UP000282985};
RA Fu T.;
RT "Parancylomarina longa gen. nov., sp. nov., isolated from sediments of
RT southern Okinawa.";
RL Submitted (NOV-2018) 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:RUT79338.1}.
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DR EMBL; RJJX01000003; RUT79338.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A434AY02; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000282985; 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:RUT79338.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000282985};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 30..465
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 866 AA; 98860 MW; 75E8F729840AD1ED CRC64;
MSSEETNDME NPEEEEKELN GAQPEAMRNV TYLSGMYQNW FLDYASYVIL ERAVPYVNDG
LKPVQRRILH AMKRLDDGRY NKVANIIGNT MQYHPHGDAS IGDALVQLGQ KDLLIDMQGN
WGNILTGDSA AAPRYIEARL SKFALEVVFN AKTTNWKLSY DGRNKEPITL PVKFPLLLAQ
GVEGIAVGLA SKILPHNFNE LIKACIAYLR EEEFVLYPDF PTAGMIEVSR YNDGLRGGAV
KVRAKIEKED NKTLKITQIP YGRNTTSLID SIIKANDKGK IKIKKIDDNT AADVEIMIHL
ASGISSDKTI DALYAFTDCE ISISPNACII ENDKPKFIGV SEILKRSADN TVALLKLELE
IRKKELEEAW HYASLERIFI ENKIYRDIEE CETWESVLET IDKGLKPFTQ NLMRAVTPDD
IVRLTEIKIK RISKFDMDKA MDLIKAIESE IEEINVHIAN IIPYTIRYFQ AIKKKFGKGR
ERKTEIRSFE NIVATKVVVA NQKLYVNYEE GFLGTALKKD KYVCDCSDID DVIIFRKDGT
YFVTKVADKL FIGKNILHIA IFRKNDKRTI FNVAYRDGRG GNSYVKRFPV TSITRDKEYN
LTKETTGSRV IYFSANPNGE AEVIRIVLKP KPRLKKLNFE FDFAELAVKG RASMGNILTR
NDVHKITLKH EGVSTLGGRK IWFDPDVLRL NTDHRGDFIG EFSGEDKILI ISKPASFHFT
SFDLSNHYAD NISIIEKYDP EKIWSAVFYD ADQEYYYLKR FTMEGNGKTV DFIGENPNNK
LICLTDESYP RFEITYGGKN EDRPKDIVEG IDFIGVKSHK ARGKRLSIYE IKKIVELDPL
PREENSEELV LEKPDVDKQN DINSEK
//