ID A0A0Q8PSI1_9ACTN Unreviewed; 902 AA.
AC A0A0Q8PSI1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=ASE01_14185 {ECO:0000313|EMBL:KRB76541.1};
OS Nocardioides sp. Root190.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736488 {ECO:0000313|EMBL:KRB76541.1, ECO:0000313|Proteomes:UP000050886};
RN [1] {ECO:0000313|EMBL:KRB76541.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB76541.1,
RC ECO:0000313|Proteomes:UP000050886};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB76541.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB76541.1,
RC ECO:0000313|Proteomes:UP000050886};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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: 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:KRB76541.1}.
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DR EMBL; LMIA01000010; KRB76541.1; -; Genomic_DNA.
DR RefSeq; WP_056754785.1; NZ_LMIA01000010.1.
DR AlphaFoldDB; A0A0Q8PSI1; -.
DR STRING; 1736488.ASE01_14185; -.
DR OrthoDB; 9804262at2; -.
DR Proteomes; UP000050886; 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; 1.
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:SF1; DNA TOPOISOMERASE; 1.
DR PANTHER; PTHR42785; DNA TOPOISOMERASE, TYPE IA, CORE; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF13368; Toprim_C_rpt; 4.
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 Reference proteome {ECO:0000313|Proteomes:UP000050886};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00952}.
FT DOMAIN 3..127
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 177..182
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT REGION 854..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..902
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 325
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 153
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 154
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 157
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 162
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 169
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 327
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 525
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
SQ SEQUENCE 902 AA; 98389 MW; 7AA9E5C516F6684D CRC64;
MAHKLVIVES PAKARTIGGY LGDGFVVESS IGHIRDLPNN AADTPAKIKD KPWGRLAIDV
ENGFEPYYVV PRDKKSHISK LKSLLKDADE LFLATDEDRE GEAIAWHLLD ELKPKNIPVK
RMVFHEITKA AIQEAAANPR ELDMDLVEAQ ETRRILDRLY GYEVSPVLWR KVMSGLSAGR
VQSVATRLVV DKEKERMAFK VASYWDLEGT FDAGSKHDQR IFPAKVHSID GTRVASGSNF
GQDGQLKGKA EVVHLDRQRA EALVSALSDS TYDVRSVESK PYRRSPYAPF RTTTLQQEAS
RKLGMSASVT MSVAQRLYEN GFITYMRTDS TTLSGSAVGA ARTQVAELYG SEYLPDEPRT
YASKVKNAQE AHEAIRPAGE SFRTPAQTGL TGEQFRLYEL IWMRTVASQM KDAVGQSVSI
RIGGRASSGE DVVFSASGRV ITFHGFLKAY VEGTDDSAST KDDQETRLPN LQEGDAVSAA
SLSANGHETK PPARYTEATL IKELEEREIG RPSTYASIIG TILNRGYVYK KGTALVPAWI
AFSVVRLLTE HFTRLIDYDF TASMETVLDD IARGEKSRVN ELTEFYYGSE RLAGLQRLVT
ELGDIDAKEL ATFPVGTAED GIDLRVGKYG PYLEGPDDGA GTRVRANVPD DLPPDELTVE
KALELLANPA GEEIDLGVHP ETGLQVVAKN GRFGPYVTEV LPEDAPKNAK ARTGSLFKSM
SLDTVTLDDA MKLISLPRVV GAGEDGEEIT AQNGRYGPYL KKGTDSRSLV SEDQIFGISL
DEALKIYAQP KQRGRAAAAP PLKELGNDPV SGQPIVVKAG RFGEYVTDGE YNATLRKDDS
VEAVTLERAA ELLAERRAKG PAKKAAKKGA KKAPAKKAAA KKTAAKKTAA KKAPAKKAAK
KS
//
