ID A0A059B9F5_EUCGR Unreviewed; 914 AA.
AC A0A059B9F5;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=EUGRSUZ_H05141 {ECO:0000313|EMBL:KCW62501.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW62501.1};
RN [1] {ECO:0000313|EMBL:KCW62501.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW62501.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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; KK198760; KCW62501.1; -; Genomic_DNA.
DR RefSeq; XP_010025764.1; XM_010027462.2.
DR AlphaFoldDB; A0A059B9F5; -.
DR EnsemblPlants; KCW62501; KCW62501; EUGRSUZ_H05141.
DR GeneID; 104416017; -.
DR Gramene; KCW62501; KCW62501; EUGRSUZ_H05141.
DR OrthoDB; 166270at2759; -.
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:0008270; F:zinc ion binding; IEA:InterPro.
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; 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; IPR006171; TOPRIM_domain.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR InterPro; IPR010666; Znf_GRF.
DR PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF01396; zf-C4_Topoisom; 1.
DR Pfam; PF06839; zf-GRF; 1.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR PROSITE; PS50880; TOPRIM; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
DR PROSITE; PS51999; ZF_GRF; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU362092}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00047}.
FT DOMAIN 9..154
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT DOMAIN 804..843
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT DOMAIN 895..911
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 384..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 101869 MW; D9432161B3D2E0D4 CRC64;
MSGGGRAINV LNVAEKPSVA KSVATLLSRG QGMRVREGRS RYNKIFEFDY GIRGQRCRML
VTSVTGHLME LEFEDRFRKW HSCDPADLYA APVRKSVPQD KLDIKRTLEE EARRCQWLVL
WLDCDREGEN IAFEVIDTCT AANCNLTIKR ARFSALIERE IHDSVQNLVE PNRWFADAVD
ARQEIDLRIG ASFTRFQTML LRDAFVIDSA ADDRNLVLSY GPCQFPTLGF VVERFWEIQS
HEPEEFWIIN CSHKSEEGIA TFNWTRGHLF DYTCAVIIYE MCVEEPPATV AGVRQQEKYK
YPPHPLSTIE LEKRASRYFR MSSEHTMKVA EELYQAGFIS YPRTETDNFS ARTDLHAIVQ
EQRGHPVWGS YAQRLLDPSS GLWRNPSNGG HDDKAHPPIH PTKFSGGERN WSQDHHRLYE
LVVRHFLACV SQPAVGAETT VEIDIAGEQF AASGRVIIAK NYLDVYRFES WGGSVIPTYV
PGQQFIPTTL TLDSGVTRPP PLLSEADLLN CMDKAGIGTD ATMHDHIKKL LDRFYATKDQ
NMRFSPTNLG EALVMGYDDM GYKLWKPNLR SMMEFDMRAV SEGAKTKAEV LETCLQQMKA
CFLDARSNKQ KLMEAMAVFF ERAARTARDE QHVVGEFVRL CGLCHQSNMV LKRNRDGNFM
VGCLGFPQCR NVVWLPGSVS EAVVTANICN SCSPGPIYMI QFKFRRLEIP PIFSVDHLGC
IGGCDDTLQQ LTEICGTGSR MSARGGGPTP LSSSAQRSNS RQQACSSCRQ LGHSSTDCPS
VISGTRNSRS RRADQQDGGL SVSCDTCGAS CPMRTANTAN NKGRKFYSCQ SEGCNFFVWE
DSLQNGGGRH GANGGASNSR ARSNSLGGRG RGGRGGNNAT NGTFVSATGD PVTGRCYVCG
DPSHFANACP NRFT
//
