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DNA topoisomerase 1 (EC 5.99.1.2) (DNA topoisomerase I)

 A0A193PP55_9VIBR        Unreviewed;       875 AA.
A0A193PP55;
05-OCT-2016, integrated into UniProtKB/TrEMBL.
05-OCT-2016, sequence version 1.
27-SEP-2017, entry version 8.
RecName: Full=DNA topoisomerase 1 {ECO:0000256|HAMAP-Rule:MF_00952, ECO:0000256|SAAS:SAAS00744975};
EC=5.99.1.2 {ECO:0000256|HAMAP-Rule:MF_00952, ECO:0000256|SAAS:SAAS00721057};
AltName: Full=DNA topoisomerase I {ECO:0000256|HAMAP-Rule:MF_00952};
Name=topA {ECO:0000256|HAMAP-Rule:MF_00952,
ECO:0000313|EMBL:BAV18315.1};
Vibrio algivorus.
Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
Vibrionaceae; Vibrio.
NCBI_TaxID=1667024 {ECO:0000313|EMBL:BAV18315.1};
[1] {ECO:0000313|EMBL:BAV18315.1}
NUCLEOTIDE SEQUENCE.
STRAIN=SA2 {ECO:0000313|EMBL:BAV18315.1};
Doi H., Chinen A., Fukuda H., Usuda Y.;
"Vibrio algivorus sp. nov., an alginate and agarose assimilating
bacterium isolated from the gut flora of a turban shell marine
snail.";
Int. J. Syst. Evol. Microbiol. 0:0-0(2016).
-!- FUNCTION: Releases the supercoiling and torsional tension of DNA,
which is introduced during the DNA replication and transcription,
by transiently cleaving and rejoining one strand of the DNA
duplex. Introduces a single-strand break via transesterification
at a target site in duplex DNA. The scissile phosphodiester is
attacked by the catalytic tyrosine of the enzyme, resulting in the
formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the
expulsion of a 3'-OH DNA strand. The free DNA strand then
undergoes passage around the unbroken strand, thus removing DNA
supercoils. Finally, in the religation step, the DNA 3'-OH attacks
the covalent intermediate to expel the active-site tyrosine and
restore the DNA phosphodiester backbone. {ECO:0000256|HAMAP-
Rule:MF_00952}.
-!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded
DNA, followed by passage and rejoining. {ECO:0000256|HAMAP-
Rule:MF_00952, ECO:0000256|SAAS:SAAS00721095}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|SAAS:SAAS00721088};
-!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00952,
ECO:0000256|SAAS:SAAS00709415}.
-!- SIMILARITY: Belongs to the type IA topoisomerase family.
{ECO:0000256|HAMAP-Rule:MF_00952, ECO:0000256|SAAS:SAAS00721110}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00952}.
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EMBL; LC164154; BAV18315.1; -; Genomic_DNA.
GO; GO:0005694; C:chromosome; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003917; F:DNA topoisomerase type I activity; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
CDD; cd00186; TOP1Ac; 1.
CDD; cd03363; TOPRIM_TopoIA_TopoI; 1.
Gene3D; 2.70.20.10; -; 1.
HAMAP; MF_00952; Topoisom_1_prok; 1.
InterPro; IPR000380; Topo_IA.
InterPro; IPR003601; Topo_IA_2.
InterPro; IPR023406; Topo_IA_AS.
InterPro; IPR013497; Topo_IA_cen.
InterPro; IPR013825; Topo_IA_cen_sub2.
InterPro; IPR023405; Topo_IA_core_domain.
InterPro; IPR003602; Topo_IA_DNA-bd_dom.
InterPro; IPR013498; Topo_IA_Znf.
InterPro; IPR005733; TopoI_bac-type.
InterPro; IPR013263; TopoI_Znr_bac.
InterPro; IPR028612; Topoisom_1_IA.
InterPro; IPR006171; TOPRIM_domain.
InterPro; IPR034149; TOPRIM_TopoI.
PANTHER; PTHR42785; PTHR42785; 1.
Pfam; PF08272; Topo_Zn_Ribbon; 2.
Pfam; PF01131; Topoisom_bac; 1.
Pfam; PF01751; Toprim; 1.
Pfam; PF01396; zf-C4_Topoisom; 2.
PRINTS; PR00417; PRTPISMRASEI.
SMART; SM00437; TOP1Ac; 1.
SMART; SM00436; TOP1Bc; 1.
SMART; SM00493; TOPRIM; 1.
SUPFAM; SSF56712; SSF56712; 1.
TIGRFAMs; TIGR01051; topA_bact; 1.
PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
PROSITE; PS50880; TOPRIM; 1.
3: Inferred from homology;
DNA-binding {ECO:0000256|HAMAP-Rule:MF_00952,
ECO:0000256|SAAS:SAAS00721076};
Isomerase {ECO:0000256|HAMAP-Rule:MF_00952,
ECO:0000256|SAAS:SAAS00721067};
Magnesium {ECO:0000256|SAAS:SAAS00721141};
Metal-binding {ECO:0000256|SAAS:SAAS00721137};
Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00952,
ECO:0000256|SAAS:SAAS00721067}.
DOMAIN 3 148 Toprim. {ECO:0000259|PROSITE:PS50880}.
REGION 198 203 Interaction with DNA. {ECO:0000256|HAMAP-
Rule:MF_00952}.
ACT_SITE 325 325 O-(5'-phospho-DNA)-tyrosine intermediate.
{ECO:0000256|HAMAP-Rule:MF_00952}.
SITE 33 33 Interaction with DNA. {ECO:0000256|HAMAP-
Rule:MF_00952}.
SITE 174 174 Interaction with DNA. {ECO:0000256|HAMAP-
Rule:MF_00952}.
SITE 175 175 Interaction with DNA. {ECO:0000256|HAMAP-
Rule:MF_00952}.
SITE 178 178 Interaction with DNA. {ECO:0000256|HAMAP-
Rule:MF_00952}.
SITE 190 190 Interaction with DNA. {ECO:0000256|HAMAP-
Rule:MF_00952}.
SITE 327 327 Interaction with DNA. {ECO:0000256|HAMAP-
Rule:MF_00952}.
SITE 512 512 Interaction with DNA. {ECO:0000256|HAMAP-
Rule:MF_00952}.
SEQUENCE 875 AA; 97480 MW; E23F411A59F98B15 CRC64;
MGKSLVIVES PAKAKTINKY LGKDFVVKSS VGHVRDLPTA GQSSGKKAAA ISTKGMSPEE
KARIKKEKDK AALIKKMGIN PYQGWEANYQ ILPGKEKVVA ELQKLAKDAD CVYLATDLDR
EGEAIAWHLR EIIGGDDARY KRVVFNEITK NAIQQAFETP GELNLDGVNA QQTRRFLDRV
VGFMASPLLW KKVARGLSAG RVQSVAVKLL VEREREINAF IPEEFWDIHA DTTTLNNTDF
RLLVAQQGGS AFKPVNEAET KAALSVLEKA TYEVCKREDR PTSSKPSAPY ITSTLQQAAS
TRLGYGVKKT MMLAQRLYEA GYITYMRTDS TNLSKEAVEA CREFIQSEFG DAYLPASPLA
YGSKQGAQEA HEAIRPSNVE VKAEDLNGME ADAHKLYALI WNQFVACQMT PAKYDSTTVS
VKADDFTLKA KGRILKFDGW TRVQRPMGKN EDQILPEVKV GDTLSLKQLD PKQHFTKPPA
RYTEAALVKE LEKRGIGRPS TYASIISTIQ DRGYVKVDQR RFYAEKMGEI VTDRLDGSFN
DLMDYDFTAR MEEKLDKIAE GNLTWTQVLD EFFDAFTADL DKAELDESEG GMMPNKIVET
SIECPTCSRP MGIRTASTGV FLGCSGYALP PKERCKTTIN LGDEEGVVNV LEEDVETAAL
RAKKRCPICE TAMDAYLIDD KRKMHVCGNN PNCDGYVVEF GEFKPKGYDG PLVECDKCGS
DMVLKNGRFG KYMGCTNEEC KNTRKILRNG EVAPPKEDPV HFPELPCSNS DAYFVLRDGA
SGLFMAASNF PKSRETRAPL VAEMAEYKDR ISEKFHYLAS APVADPDGIP TVVRFSRKSK
EHYVRSEVDG KPSGWTALYI DGKWEITDKR KKAKK


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