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Entry: A0A1Q3M3F1_9BACT
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ID   A0A1Q3M3F1_9BACT        Unreviewed;       796 AA.
AC   A0A1Q3M3F1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   13-SEP-2023, entry version 21.
DE   RecName: Full=DNA topoisomerase 1 {ECO:0000256|HAMAP-Rule:MF_00952};
DE            EC=5.6.2.1 {ECO:0000256|HAMAP-Rule:MF_00952};
DE   AltName: Full=DNA topoisomerase I {ECO:0000256|HAMAP-Rule:MF_00952};
GN   Name=topA {ECO:0000256|HAMAP-Rule:MF_00952};
GN   ORFNames=BGN96_09760 {ECO:0000313|EMBL:OJU53240.1};
OS   Bacteroidales bacterium 45-6.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX   NCBI_TaxID=1895719 {ECO:0000313|EMBL:OJU53240.1, ECO:0000313|Proteomes:UP000185892};
RN   [1] {ECO:0000313|EMBL:OJU53240.1, ECO:0000313|Proteomes:UP000185892}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=45-6 {ECO:0000313|EMBL:OJU53240.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Releases the supercoiling and torsional tension of DNA, which
CC       is introduced during the DNA replication and transcription, by
CC       transiently cleaving and rejoining one strand of the DNA duplex.
CC       Introduces a single-strand break via transesterification at a target
CC       site in duplex DNA. The scissile phosphodiester is attacked by the
CC       catalytic tyrosine of the enzyme, resulting in the formation of a DNA-
CC       (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH
CC       DNA strand. The free DNA strand then undergoes passage around the
CC       unbroken strand, thus removing DNA supercoils. Finally, in the
CC       religation step, the DNA 3'-OH attacks the covalent intermediate to
CC       expel the active-site tyrosine and restore the DNA phosphodiester
CC       backbone. {ECO:0000256|HAMAP-Rule:MF_00952}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC         passage and rejoining.; EC=5.6.2.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000213, ECO:0000256|HAMAP-
CC         Rule:MF_00952};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00952}.
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000256|ARBA:ARBA00009446, ECO:0000256|HAMAP-Rule:MF_00952}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00952}.
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:OJU53240.1}.
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DR   EMBL; MKRS01000305; OJU53240.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3M3F1; -.
DR   Proteomes; UP000185892; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   CDD; cd00186; TOP1Ac; 1.
DR   CDD; cd03363; TOPRIM_TopoIA_TopoI; 1.
DR   Gene3D; 3.40.50.140; -; 1.
DR   Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 2.
DR   Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR   Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 1.
DR   HAMAP; MF_00952; Topoisom_1_prok; 1.
DR   InterPro; IPR000380; Topo_IA.
DR   InterPro; IPR003601; Topo_IA_2.
DR   InterPro; IPR023406; Topo_IA_AS.
DR   InterPro; IPR013497; Topo_IA_cen.
DR   InterPro; IPR013824; Topo_IA_cen_sub1.
DR   InterPro; IPR013825; Topo_IA_cen_sub2.
DR   InterPro; IPR013826; Topo_IA_cen_sub3.
DR   InterPro; IPR023405; Topo_IA_core_domain.
DR   InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR   InterPro; IPR005733; TopoI_bac-type.
DR   InterPro; IPR028612; Topoisom_1_IA.
DR   InterPro; IPR025589; Toprim_C_rpt.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034149; TOPRIM_TopoI.
DR   NCBIfam; TIGR01051; topA_bact; 1.
DR   PANTHER; PTHR42785; DNA TOPOISOMERASE, TYPE IA, CORE; 1.
DR   PANTHER; PTHR42785:SF1; OMEGA-PROTEIN; 1.
DR   Pfam; PF01131; Topoisom_bac; 2.
DR   Pfam; PF01751; Toprim; 1.
DR   Pfam; PF13368; Toprim_C_rpt; 3.
DR   PRINTS; PR00417; PRTPISMRASEI.
DR   SMART; SM00437; TOP1Ac; 1.
DR   SMART; SM00436; TOP1Bc; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR   PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00952};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00952};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW   Rule:MF_00952}.
FT   DOMAIN          3..113
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          163..168
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   REGION          761..796
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        761..785
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        287
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            33
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            139
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            140
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            143
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            155
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            289
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            477
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
SQ   SEQUENCE   796 AA;  90088 MW;  46EE6651014D286B CRC64;
     MQKNLVIVES PAKAKTIEKF LGKDYHVLSS YGHIRDLKKK DFGIDLNNSY KPQYEVPADK
     KKLVAELKKA AKEAEVVWLA SDEDREGEAI SWHLYETLGL TDDRAKRIAF HEITKDAILN
     AINNPRKINF NLVDAQQARR VLDRIVGFEL SPVLWKKVKP ALSAGRVQSV AVRLIVERER
     EIREFQTEAA YRVVAIFVKQ ENGNTYELKA ELPQRLKTKE EALALLEKLK TADFTIDSVV
     TKPTKRSPAA PFTTSTLQQE AARKLGFTVA QTMRVAQGLY ESGKITYMRT DSVNLSSLAL
     NTSKAEIIAS YGEKYTHPRN YTTKSKGAQE AHEAIRPTYM SEHTVSGSAQ EKKLYDLIWK
     RTIASQMADA ELEKTTVTIS VSNSDYSFVA AGEVIKFDGF LHVYMEDSDD EQPESDSHLL
     PPLHKGEVLE MAETSATERF SQRPARYTEA SLVKKMEELG IGRPSTYAPT ISTIQNREYV
     EKKTIEGTPR EYNVMTLKNG FIRDEKNTEI TGADKNKLFP TDTGEVVNDF LTEFFPEIMK
     YNFTARLEER FDEVAEGKEN WTELIDGFYK LFHPVVNEVM NAQTEHKIGE RVLGVDPKSG
     RQISVKIGRF GPMVQIGVQE EEEKPQFASL QKDQSISTIT LEEALRLFDL PRTLGEFEEK
     VMTVAIGRFG PYVRHNSQFV SLPKGCDPYS ITSEEAIELI LEKRKKDSER LIKEFTEDAE
     LQILNGRYGP YITHQKNNYK IPKGKEPASL TYEEVMEIIK ATPESDKKGK RTPAKKAEAK
     TSKAKSTAKK KPAAGK
//
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