ID C1DYX0_MICCC Unreviewed; 861 AA.
AC C1DYX0;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 60.
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=MICPUN_79081 {ECO:0000313|EMBL:ACO61502.1};
OS Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Mamiellaceae; Micromonas.
OX NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO61502.1, ECO:0000313|Proteomes:UP000002009};
RN [1] {ECO:0000313|EMBL:ACO61502.1, ECO:0000313|Proteomes:UP000002009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX PubMed=19359590; DOI=10.1126/science.1167222;
RA Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA Grigoriev I.V.;
RT "Green evolution and dynamic adaptations revealed by genomes of the marine
RT picoeukaryotes Micromonas.";
RL Science 324:268-272(2009).
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; CP001323; ACO61502.1; -; Genomic_DNA.
DR RefSeq; XP_002500244.1; XM_002500198.1.
DR AlphaFoldDB; C1DYX0; -.
DR STRING; 296587.C1DYX0; -.
DR GeneID; 8240954; -.
DR KEGG; mis:MICPUN_79081; -.
DR eggNOG; KOG1957; Eukaryota.
DR InParanoid; C1DYX0; -.
DR OMA; GKWSFAN; -.
DR OrthoDB; 166270at2759; -.
DR Proteomes; UP000002009; Chromosome 2.
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 CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03362; TOPRIM_TopoIA_TopoIII; 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 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; 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; IPR006171; TOPRIM_domain.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR PANTHER; PTHR11390:SF20; DNA TOPOISOMERASE 3-BETA-1; 1.
DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
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; PS50880; TOPRIM; 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:UP000002009};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU362092}.
FT DOMAIN 6..150
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 374..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..861
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 861 AA; 94861 MW; 38BB0B10C7BE0A01 CRC64;
MSGLPVVLCV AEKPSLAASI AGFLSEGKHR SRRGGQEVHE FERDFNGARC HFKVTAVIGH
VLSIDFPAKF QSWDLDPAIL FDAPVQKKEA TPKARVVEHL EREAKGASHL ILWLDCDREG
ENICFEVIDA CAPVMRPNRG DTFVHRAKFS AVSKESIERA MRTLGAPNRA EALAVDARQE
LDLKVGVAFT RFQTRFFQGR YSHLDASVIS YGPCQTPTLN FAVQRHLEIV SHTPEDFWSL
HVEVRSTSLG KTLVTRWERE RVFDGDVGEM FRSMVAGDRH ALVESVEETE EFKRRPPGLN
TVDLLKAASA GMGMGAHRAM QVAERLYIQG FISYPRTEST AYPPGFDLKG TLKAQRGHPD
WGEWVEELLA GSMTKPRGGK DEGDHPPITP VRSATESAVG GGEAWRLYDF VARHFIASVS
PDCAYVSRRA TLVAGGERFR VSGQTVIAPG WTTVMPHRAV EDDPLGEIER GESLPIATVE
LRQGATSPPP YLSEAELIGL MERNGIGTDA SIPTHINNIE SRKYVTIQSQ GGRRVVPTDL
GVTLVQGYHR IDPELALPAV RSHVEKQLDM IATGKADHES IVRHTLAQFA AKFRNFVDQI
ERMDTLFEAS FDPTCSSGKP FSKCGRCLRY MRLVSTRPQR LYCPTQEEVL ELPAGTVKLY
NNRECQLCGF ELLLYQNGDR TYPMCPWCFN HPPFVGGSRP TKGLVSGAPH PRAHPIVDAL
VVCPCPECGE DDKLKGREGG WLMLEPVGGP RWKFVCTGCA LVVKLNDSVH RVTVDKLDVC
GACGARCPTV IYHKDRTPLA GGETAHVACL ACDDLLNSSI ELARGRGAAR GGGRGGRGGR
GRGRGRKPPS DHDQKMSFKD F
//
