ID D8SZD6_SELML Unreviewed; 1020 AA.
AC D8SZD6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891};
DE EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891};
DE AltName: Full=Omega-protein {ECO:0000256|ARBA:ARBA00032877};
DE AltName: Full=Relaxing enzyme {ECO:0000256|ARBA:ARBA00032235};
DE AltName: Full=Swivelase {ECO:0000256|ARBA:ARBA00030003};
DE AltName: Full=Untwisting enzyme {ECO:0000256|ARBA:ARBA00031985};
GN ORFNames=SELMODRAFT_427375 {ECO:0000313|EMBL:EFJ10264.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ10264.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
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 -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00009446}.
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DR EMBL; GL377655; EFJ10264.1; -; Genomic_DNA.
DR RefSeq; XP_002988753.1; XM_002988707.1.
DR AlphaFoldDB; D8SZD6; -.
DR STRING; 88036.D8SZD6; -.
DR EnsemblPlants; EFJ10264; EFJ10264; SELMODRAFT_427375.
DR GeneID; 9639009; -.
DR Gramene; EFJ10264; EFJ10264; SELMODRAFT_427375.
DR KEGG; smo:SELMODRAFT_427375; -.
DR eggNOG; KOG1956; Eukaryota.
DR HOGENOM; CLU_002929_0_0_1; -.
DR InParanoid; D8SZD6; -.
DR OMA; YAQPKQR; -.
DR OrthoDB; 167550at2759; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03363; TOPRIM_TopoIA_TopoI; 1.
DR Gene3D; 3.40.50.140; -; 1.
DR Gene3D; 3.30.65.10; Bacterial Topoisomerase I, domain 1; 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; IPR013498; Topo_IA_Znf.
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; 2.
DR Pfam; PF01396; zf-C4_Topoisom; 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; PS00396; TOPOISOMERASE_I_PROK; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW Signal {ECO:0000256|SAM:SignalP};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1020
FT /note="DNA topoisomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003123182"
FT DOMAIN 228..343
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 76..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1020 AA; 112724 MW; 33A42B9A7F7B5F36 CRC64;
MGALKASSSL FSRLLCSSSA AFLPSIAPGR ISCGIFESGS QGRWGIAQSG QKFVLYQFSR
DFSSASSRRW FRRKGKKGAA LNASTAESQQ TAGAENVAKK SPGRKSKGTA KPEEETQDPQ
AVDKKKARSK VAVEQKPSDA TNATKKKKKN ESNATKEDDG GKVKSAAKTT KPKDAAKLKP
AKEVKDGGDL KEAPSKRSKK KAEVVAATTI DSTIETGEQE NGAALSGKVV VVVESPAKAK
TIEKYLGENY VVVASYGHVR DLAARSGSVR PQDDFDLVWE VPDTAKSRFN QIKTALKGAQ
AMVLASDPDR EGEAIAWHIL EMIRLEGIMK KGLKIQRVTF NEITKTAVQQ GMKSPRNISQ
ELVDAYLARR ALDYLIGFDI SPLLWRKLPG SKSAGRVQSA ALCLLADREK EIESFTPREY
WTVEAEICPA DSKGQVSFPA RLVSYNGVKL DQFSLTGSEA EAAASYIGQS SLRVDGMKNS
VIRRNAPGPY ITSSLQQDAS SKLGFGASKT MLLAQKLYEG VKLPDGELVG LITYMRTDSM
QLSAQAIESI RKFGEERYGK NYVLSSPRKF SSKVKNAQEA HEAIRPTGIE RIPSELAKVL
EQDALRLYAL IWRRTMACQL EQAVFNHVSL DVEDPKGVVR LRSTASTMEF PGFQIVYRDK
DALAGDNEEE ESATEKKLPS LKAGSCVSAI DVKHKQHFTE PPPRYTEGSL VKKMEELGIG
RPSTYAHVLK TLQLRQYMQI EKQRIIPRVR GRMVAAFLSR YFTEFVDYGF TAKMEEQLDA
VSSGSMKWKE VLQQFWPNFH DKVTSTAKVP TQQVADMLAS LFSDKLAGKD KTCPNCHTGE
LQLKLTKFGT GYFLGCNRYP SCHYSNSLDK DEEEEEEECG SPVAKSRSKV LGVDSSTGLP
VLYKEGPYGD YVQIGEDAKG KLKPKRVRVP ESINYNAFTL EMAMELMKYP KELGVDPEGK
PVMIGIGRFG CYIRREGYSV YVPKDQKVEE LTLEMALDIF VKGKEDRRKV RKSPVKIAFA
//
