ID A0A261KT02_9CYAN Unreviewed; 943 AA.
AC A0A261KT02;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=AFK68_09300 {ECO:0000313|EMBL:OZH54698.1};
OS Hydrocoleum sp. CS-953.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Hydrocoleum.
OX NCBI_TaxID=1671698 {ECO:0000313|EMBL:OZH54698.1, ECO:0000313|Proteomes:UP000215798};
RN [1] {ECO:0000313|EMBL:OZH54698.1, ECO:0000313|Proteomes:UP000215798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS-953 {ECO:0000313|EMBL:OZH54698.1,
RC ECO:0000313|Proteomes:UP000215798};
RA Willis A., Parks M., Jameson I., Burford M.A.;
RT "Comparative genomics of marine benthic cyanobacteria including Hydrocoleum
RT sp. CS-953 from Moreton Bay, Australia.";
RL Submitted (JUL-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:OZH54698.1}.
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DR EMBL; LGSU01000792; OZH54698.1; -; Genomic_DNA.
DR OrthoDB; 9804262at2; -.
DR Proteomes; UP000215798; 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:UP000215798};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00952}.
FT DOMAIN 2..126
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 175..180
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT REGION 920..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 320
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 32
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 151
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 152
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 160
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 167
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 322
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 515
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
SQ SEQUENCE 943 AA; 105433 MW; 7D8F234D56E342DE CRC64;
MSTLVIVESP TKARTIRNYL PSDYRVEASM GHVRDLPPSA EEIPEKYKGE KWAHLGVNVE
SDFEPVYVVP KDKKKTVKEL KDALKEADEL VLATDEDREG ESISWHLLQL LKPKVPTKRM
VFHEITPEAI RKAIENCRNI DEQLVRAQET RRILDRLYGY TLSPVLWKKI AWGLSAGRVQ
SVAVRLLVNR ERQRQAFKQG GYWDLKASLE QEKSPFESKL VTLGGTKVAT GSDFDENTGK
IAEGRNVVLL DETQAEALKE RLEDKPWTVS SVEERAVKRK PSPPFTTSTL QQEANRKLRM
GAKQTMRTAQ NLYEQGFITY MRTDSVHLSD EAIAAARSCV EKMYGAEYLS PQPRQYTTKS
KGAQEAHEAI RPAGQTFRTP QETGLKDQEF ALYDLIWKRT VACQMADSRQ THITVNLQVE
DAGFRSNGKR IDFPGFLRAY VEGSDDPEAA LENQEVPLPP LKQGDRPNCR EIEVVGHETQ
PPARFTEASL VKTLESEGIG RPSTYATVIS TIVDRRYAKL QGNALVPTFT AFGVTSLLER
HFPEFVDVKF TARMEQTLDD ISTGEAQWLP YLREFYSGES GLDTQIKEQE EYIDPKLART
IELENLDTDP EMTYRICIGK FGAYIEAEND EGIVKASIPE DLTPSDLDPE QIEKILKQKT
EGPEELGIHP EEDKPIYIMT GRYGPYVQLG DEVEGSKKKP KRSSLPKGVN MEDVTLDMAV
GLLSLPRTLG THPETGCKIQ TNLGRFGPYV VHDQGKEGGK DYRSLKAGDD VLTITLERAL
ELLAQPKRAR RGSAKAAPPL KDLGKHPEDG EVVGIYDGRY GPYVKHGKVN AXLKAGDDVL
TITLERALEL LAQPKRARRG SAKAAPPLKD LGKHPEDGEV VGIYDGRYGP YVKHGKVNAS
LPKDTAVEDV TLEQALELLQ AKASTKKSTR GRKSTKTKAA ENN
//
