ID A0A0E0NQ39_ORYRU Unreviewed; 915 AA.
AC A0A0E0NQ39;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 28-JUN-2023, entry version 36.
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};
OS Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI03G04550.3, ECO:0000313|Proteomes:UP000008022};
RN [1] {ECO:0000313|Proteomes:UP000008022}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA Zhao Q.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORUFI03G04550.3}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) 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 AlphaFoldDB; A0A0E0NQ39; -.
DR EnsemblPlants; ORUFI03G04550.3; ORUFI03G04550.3; ORUFI03G04550.
DR Gramene; ORUFI03G04550.3; ORUFI03G04550.3; ORUFI03G04550.
DR HOGENOM; CLU_002929_1_1_1; -.
DR Proteomes; UP000008022; 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: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; IPR006171; TOPRIM_domain.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR InterPro; IPR001878; Znf_CCHC.
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; 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; 1.
DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR PROSITE; PS50880; TOPRIM; 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 Reference proteome {ECO:0000313|Proteomes:UP000008022};
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:PRU01343}.
FT DOMAIN 11..157
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT DOMAIN 795..834
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT REGION 389..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 915 AA; 102343 MW; 1999B6144B2D8EAD CRC64;
MHHGGGGGAI RVLNVAEKPS VAKSVAEILS RPSGGMRSRE GRSRYNRVFE FDYSIGGRAC
HMLVTSVTGH LMELEFDDRF RRWHSCDPAD LFHAPVRKSV PQDKQDIKRT LEEEARKCQW
LVLWLDCDRE GENIAYEVID ICAGANSRLN IWRARFSALI DREIHEAVQH LDRPNKLFAD
AVDARQEIDL RIGASFTRFQ TMLLKDAFVL DDTGDDRNII LSYGPCQFPT LGFIVERFWE
IQAHEPEEFW TINCSHTSDE GTASFGWIRG HLFDYSSAVV IYEMCVEEPM ATVQNVRNQE
KLKYPPYPLS TIELQKRASR YFRMSSEHTM KVAEELYQAG FISYPRTETD NFSPNTDLHS
IVHEQVAHPN WGTYAQRLLD PEARLWRNPS NGGHDDKAHP PIHPTKFSAG ETNWTDNHKK
LYELVVRHFL ACCSQPAVGA ETTVEIDIAG EQFNASGRVV LAKNYLDVYR FDSWGGTLLP
TYIIGQQFVP TTLTLDSGMT RPPPLLAEAD LLGCMDKAGI GTDATMHDHI KKLLDRCYAT
KDANTRFSPT NLGEALVMGY DEMGYELWKP YLRSMMEADM KSVSIGTKSK SEVLENCLQQ
MKACFLDARA NKVKLFDAMG TFFARSSRPV NETQNSIETV RPCAACNESE MFLKQRPCRN
VVWLPRSLSG AAVTDQVCPT CAPGPVYKIQ FKFRRRDIPP NFDVDHLGCI GGCDDILKEL
MELSRFGSHS QTATPARNQS QTASGVRQGS SRQDLHTSFH PAVQFTNGQT PVVNPQGFRS
THTQSSGNAS GQVQCTSCRE PCVLRTANTE ANRGRKFYKC QNLACGFFAW EDDVENSAPR
GRGGRGRGGR SSSRQSSASA SAGRRGGTQG RGRRGRGRNA DGMMFVAATG EPVYGSCFIC
GDPTHFANVC PNLGR
//
