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Database: UniProt
Entry: A0A1G2HVE9_9BACT
LinkDB: A0A1G2HVE9_9BACT
Original site: A0A1G2HVE9_9BACT 
ID   A0A1G2HVE9_9BACT        Unreviewed;      1319 AA.
AC   A0A1G2HVE9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=A2822_01635 {ECO:0000313|EMBL:OGZ66435.1};
OS   Candidatus Staskawiczbacteria bacterium RIFCSPHIGHO2_01_FULL_41_41.
OC   Bacteria; Candidatus Staskawiczbacteria.
OX   NCBI_TaxID=1802203 {ECO:0000313|EMBL:OGZ66435.1, ECO:0000313|Proteomes:UP000178774};
RN   [1] {ECO:0000313|EMBL:OGZ66435.1, ECO:0000313|Proteomes:UP000178774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGZ66435.1}.
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DR   EMBL; MHOP01000005; OGZ66435.1; -; Genomic_DNA.
DR   Proteomes; UP000178774; 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:0004519; F:endonuclease activity; IEA:InterPro.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   CDD; cd00187; TOP4c; 1.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1.
DR   Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR   Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 2.
DR   Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR   InterPro; IPR006691; GyrA/parC_rep.
DR   InterPro; IPR035516; Gyrase/topoIV_suA_C.
DR   InterPro; IPR003586; Hint_dom_C.
DR   InterPro; IPR036844; Hint_dom_sf.
DR   InterPro; IPR027434; Homing_endonucl.
DR   InterPro; IPR006142; INTEIN.
DR   InterPro; IPR030934; Intein_C.
DR   InterPro; IPR004042; Intein_endonuc.
DR   InterPro; IPR004860; LAGLIDADG_2.
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   NCBIfam; TIGR01063; gyrA; 1.
DR   NCBIfam; TIGR01443; intein_Cterm; 1.
DR   PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 2.
DR   Pfam; PF14890; Intein_splicing; 1.
DR   Pfam; PF14528; LAGLIDADG_3; 2.
DR   PRINTS; PR00379; INTEIN.
DR   SMART; SM00305; HintC; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR   SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR   SUPFAM; SSF55608; Homing endonucleases; 2.
DR   SUPFAM; SSF56719; Type II DNA topoisomerase; 2.
DR   PROSITE; PS50818; INTEIN_C_TER; 1.
DR   PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          218..365
FT                   /note="DOD-type homing endonuclease"
FT                   /evidence="ECO:0000259|PROSITE:PS50819"
FT   DOMAIN          542..564
FT                   /note="Intein C-terminal splicing"
FT                   /evidence="ECO:0000259|PROSITE:PS50818"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1319 AA;  146655 MW;  062AC929D339977B CRC64;
     MAKDKEKDPA KSPKGDRGAA KKEEQATNAI GNVSKREIVD ELKESYIDYA MSVIVARALP
     DVRDGLKPVH RKILYTMNEM GLNASAKFRK SATVVGECFV KDTLILSKKG LVSIQDIQVG
     DEVYTQKGMQ KVVQTYEMPE KPLLKVVLDN GLSNVVTLSQ KFKVLTPDWK FIWKEAKDLT
     DQDYLIIKSD YPEIGHQVKL QTTGEDQPSH LNENVAYILG LFVSDGWISE DYSAKKTTRI
     GFTAGNDKEI AERIVSIFKK EFNHHPSIEE RLFDGRRKKI YNVRVNSAAI NEFFVANFDI
     KGAWALTKKI PNEIFQSPSD IISSFISGLI EGDGYISHKQ NRVNYVSISE KLTDQLMALL
     LSQGIFSSKY KTDVVSGDSA VLNRKINGKH PSFSLEIKGE NAVALSSKLN LVSKSKGQRA
     ARLGSKKLTS HDRKGPNRHD VIPYASNILF QELSNNHLGG GWYQDVDGEK FRMGVKYPDG
     TKIRYSSNLH EMPLRKTQVI DWGIKDKLEK IGSPNLEFLE EIIKNKIHFL KVSLIKKVAP
     QKTFDFEVEN DHEFIANGVV SHNCMGKYHP HGDMAIYDSL VRMAQDFNMR YPLAHPQGNF
     GSQDGDSAAA PRYTEIKLSK IGELLLADIE KDTVRFMDNY DGTRQEPTVL PSPVPQLLLN
     GSLGIAVGMA TNIPPHNLTE LTDAISHILD NPKAETPDLF QFIQGPDFPT GGIIYDQKEI
     ITAYSQGKGS IVMRGKAEIT EKKDGSEQIL ITEIPYQVLK STLVEEMANL VSEKKIEGIR
     DIKDLSDREG MGIIIDIKKG FDANRVLNRL YKFTNLQKTF HLNLLALVDG IQPEILSIAD
     VLKYFISHRT EVVTRRTKFD LEKAKDRAHI LEGLMIALNN IDAVIKVIKQ SKDREDAKLN
     LIKKFKLSEK QAVAILEMKL QTLAGLERQK IQDELKAILE LIKELTAILA SPAKLKAIIK
     KELAEVKEKF GDARRTKVVK GKLGEITEID LVPLEETIVT LTTGGYIKRI NPATYKIQKR
     GGKGIIGMKT MQEDIVEHFL SASTHDNLMF FTDSGKVFQT QVYEIPEGTR VARGRGISNF
     LEGISNEEKV LSLVTKAKAK PDAPSADKYL VMVTKNGRIK KTSLEEFENV RKSGIIAIKL
     EKGDALKKVV KTSGEDDIVL ATKSGIAIRF KEKDIRPMGR SAAGVKGIRI KGNDEVIGMD
     VVTNEAASAK GSGAPKQYLM VVMENGYGKR TEISEYKVQG RGGSGIKTAN ITAKTGGIVI
     SSILHDSVDE EDLIVISQHG QVIRTATKSI SVLGRATQGV RIMRLEPGDK VASGTCVKE
//
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