ID R1G787_EMIHU Unreviewed; 791 AA.
AC R1G787;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891, ECO:0000256|RuleBase:RU362092};
DE EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891, ECO:0000256|RuleBase:RU362092};
GN ORFNames=EMIHUDRAFT_194121 {ECO:0000313|EMBL:EOD41689.1};
OS Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC Noelaerhabdaceae; Emiliania.
OX NCBI_TaxID=2903 {ECO:0000313|EMBL:EOD41689.1};
RN [1] {ECO:0000313|EMBL:EOD41689.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP1516 {ECO:0000313|EMBL:EOD41689.1};
RG DOE Joint Genome Institute;
RA Read B., Kegel J., Klute M., Kuo A., Lefebvre S.C., Maumus F., Mayer C.,
RA Miller J., Allen A., Bidle K., Borodovsky M., Bowler C., Brownlee C.,
RA Claverie J.-M., Cock M., De Vargas C., Elias M., Frickenhaus S.,
RA Gladyshev V.N., Gonzalez K., Guda C., Hadaegh A., Herman E.,
RA Iglesias-Rodriguez D., Jones B., Lawson T., Leese F., Lin Y.-C.,
RA Lindquist E., Lobanov A., Lucas S., Malik S.-H.B., Marsh M.E., Mock T.,
RA Monier A., Moreau H., Mueller-Roeber B., Napier J., Ogata H., Parker M.,
RA Probert I., Quesneville H., Raines C., Rensing S., Riano-Pachon D.M.,
RA Richier S., Rokitta S., Salamov A., Sarno A.F., Schmutz J., Schroeder D.,
RA Shiraiwa Y., Soanes D.M., Valentin K., Van Der Giezen M., Van Der Peer Y.,
RA Vardi A., Verret F., Von Dassow P., Wheeler G., Williams B., Wilson W.,
RA Wolfe G., Wurch L.L., Young J., Dacks J.B., Delwiche C.F., Dyhrman S.,
RA Glockner G., John U., Richards T., Worden A.Z., Zhang X., Grigoriev I.V.;
RT "Genome variability drives Emilianias global distribution.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000013827}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP1516 {ECO:0000313|Proteomes:UP000013827};
RX PubMed=23760476; DOI=10.1038/nature12221;
RA Read B.A., Kegel J., Klute M.J., Kuo A., Lefebvre S.C., Maumus F.,
RA Mayer C., Miller J., Monier A., Salamov A., Young J., Aguilar M.,
RA Claverie J.M., Frickenhaus S., Gonzalez K., Herman E.K., Lin Y.C.,
RA Napier J., Ogata H., Sarno A.F., Shmutz J., Schroeder D., de Vargas C.,
RA Verret F., von Dassow P., Valentin K., Van de Peer Y., Wheeler G.,
RA Dacks J.B., Delwiche C.F., Dyhrman S.T., Glockner G., John U., Richards T.,
RA Worden A.Z., Zhang X., Grigoriev I.V., Allen A.E., Bidle K., Borodovsky M.,
RA Bowler C., Brownlee C., Cock J.M., Elias M., Gladyshev V.N., Groth M.,
RA Guda C., Hadaegh A., Iglesias-Rodriguez M.D., Jenkins J., Jones B.M.,
RA Lawson T., Leese F., Lindquist E., Lobanov A., Lomsadze A., Malik S.B.,
RA Marsh M.E., Mackinder L., Mock T., Mueller-Roeber B., Pagarete A.,
RA Parker M., Probert I., Quesneville H., Raines C., Rensing S.A.,
RA Riano-Pachon D.M., Richier S., Rokitta S., Shiraiwa Y., Soanes D.M.,
RA van der Giezen M., Wahlund T.M., Williams B., Wilson W., Wolfe G.,
RA Wurch L.L.;
RT "Pan genome of the phytoplankton Emiliania underpins its global
RT distribution.";
RL Nature 499:209-213(2013).
RN [3] {ECO:0000313|EnsemblProtists:EOD41689}
RP IDENTIFICATION.
RG EnsemblProtists;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Introduces a single-strand break via transesterification at a
CC target site in duplex DNA. Releases the supercoiling and torsional
CC tension of DNA introduced during the DNA replication and transcription
CC by transiently cleaving and rejoining one strand of the DNA duplex. The
CC scissile phosphodiester is attacked by the catalytic tyrosine of the
CC enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme
CC intermediate and the expulsion of a 3'-OH DNA strand.
CC {ECO:0000256|RuleBase:RU362092}.
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,
CC ECO:0000256|RuleBase:RU362092};
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00009446, ECO:0000256|RuleBase:RU362092}.
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DR EMBL; KB863010; EOD41689.1; -; Genomic_DNA.
DR RefSeq; XP_005794118.1; XM_005794061.1.
DR STRING; 2903.R1G787; -.
DR PaxDb; 2903-EOD41689; -.
DR EnsemblProtists; EOD41689; EOD41689; EMIHUDRAFT_194121.
DR GeneID; 17286959; -.
DR KEGG; ehx:EMIHUDRAFT_194121; -.
DR eggNOG; KOG1956; Eukaryota.
DR HOGENOM; CLU_355066_0_0_1; -.
DR OMA; RMWIQSM; -.
DR Proteomes; UP000013827; 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-EC.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR Gene3D; 3.40.50.140; -; 1.
DR Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 2.
DR Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 1.
DR InterPro; IPR000380; Topo_IA.
DR InterPro; IPR003601; Topo_IA_2.
DR InterPro; IPR013497; Topo_IA_cen.
DR InterPro; IPR013824; Topo_IA_cen_sub1.
DR InterPro; IPR013826; Topo_IA_cen_sub3.
DR InterPro; IPR023405; Topo_IA_core_domain.
DR InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362092};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362092};
KW Reference proteome {ECO:0000313|Proteomes:UP000013827};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU362092}.
FT DOMAIN 86..194
FT /note="DNA topoisomerase type IA"
FT /evidence="ECO:0000259|SMART:SM00436"
FT DOMAIN 215..457
FT /note="DNA topoisomerase type IA DNA-binding"
FT /evidence="ECO:0000259|SMART:SM00437"
FT REGION 136..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 791 AA; 87687 MW; EACA8C6D8842CA7E CRC64;
MKVLAVAEKP SSYRTQQGPS QYNRLFEFST PYRGSQCQMI VTSVTGHLME LEFCDERHAK
WKRCDLIELF DAPIRQRAIG FEVVDVCKRA NPRLQALANL VPPDQRLADA VSARSEIDLR
LGAAFTRFQT LTLQERSTAS NRTPPRAPPF TPHHVRGQDQ YEGLDGLLSY GPCQFPTMWF
VARIDAFVRE AFYAIEVMLY EICVERRLAT VTKVDGHEKR KWRPTPLHTG FLSYPRTETD
KFKARGTTDG FDLAALINEQ AGHPEWGGFA RELQAGGFQA LTPSLYPFLP PAQAHPPIHP
LKSGAPLQGD EARVYELVTR RFLACCACDA LGFETTVDIE MAGEQFSSRG LMVWKWERWS
ARKIPSYYLG EQFEPTALHL HEGHTSPPSP LSEARAPSKA ERSFGRLAEL IGMMDEQGIG
TDATIAQHIK KTLDRGYVEK RVPNNTFHPL PLSRILLDSY TRMPQAFDLG VPHLRAEMER
DMAPAASAEL ARRGRDACGG KVCSGQMTRQ ECVDKTARKS EALHQPWVDM MRGLYRHASV
NSRCLHAAAA AILARPDASS WAPQRLSDGS RPSCGKCQGL MDLRHYDVPG GDLASHGHRC
PLDQFQVLSV TNTATGKTHQ ICPKCFKDPP AEATGGKAVD GLRCFACLAD CPLASGSKVL
RPCPSCQRGE LLFKAPKAMN GTLLECSNSG EGCDMKLYLP GGTTLQRLSA QPCAGCSHSL
LSFTFNRASL EPRLRMHPYD ACCFCSEPNL AEILRDCNDT ADGRRRVALL CSRCCGHGRC
GGDVSVDAWR R
//
