ID L8YCR4_TUPCH Unreviewed; 967 AA.
AC L8YCR4;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=TREES_T100005658 {ECO:0000313|EMBL:ELV14017.1};
OS Tupaia chinensis (Chinese tree shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELV14017.1, ECO:0000313|Proteomes:UP000011518};
RN [1] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhang G., Fan Y., Yao Y., Huang Z.;
RT "Genome of the Chinese tree shrew, a rising model animal genetically
RT related to primates.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23385571; DOI=10.1038/ncomms2416;
RA Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT "Genome of the Chinese tree shrew.";
RL Nat. Commun. 4:1426-1426(2013).
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; KB359564; ELV14017.1; -; Genomic_DNA.
DR AlphaFoldDB; L8YCR4; -.
DR STRING; 246437.L8YCR4; -.
DR eggNOG; KOG1956; Eukaryota.
DR InParanoid; L8YCR4; -.
DR Proteomes; UP000011518; 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: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; 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 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; 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; 2.
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 SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR PROSITE; PS50880; TOPRIM; 1.
DR PROSITE; PS51999; ZF_GRF; 2.
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:UP000011518};
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 35..159
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT DOMAIN 795..834
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT DOMAIN 880..922
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT REGION 734..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 967 AA; 108281 MW; 0E48243B922F00DB CRC64;
MIFPVSRFAL RWLRRPGGRA LSRATMEVAF RGVRKVLCVA EKNDAAKGIA DLLSNGRMRR
NVAMVMTSVS GHLLVHDFQM QFRKWQSCNP LVLFEAEIEK YCPENFVDIK KTLERETRQC
QALVIWTDCD REGENIGFEI IHVCTAVKPS LRVLRARFSE ITPHAVRTAC ENLTEPDQRV
SDAVDVRQEL DLRIGAAFTR FQTLRLQRVF PEVLTEQLIS YGSCQFPTLG FVVERFKAIQ
AFVPETFHRI KVNHDHEDGI VEFNWKRHRL FNHTACLVLY HLCMEDPMAT VVEVKSKPKS
KWRPQALDTV ELEKLASRKL RINAKETMRI AEKLYTQGFI SYPRTETNIF PKDLNLTALV
DQQTQDPRWG AFARSILERG GPNPRNGNKS DQAHPPIHPT KYASNLQGDE QRLYEFIVRH
FLACCSQDAQ GQETTVEIDI AQERFVAHGL VILARNYLDV YPYDHWSDKL LPVYERGSRF
QPSAVEMVDG ETSPPQLLTE ADLIALMEKH GIGTDATHAE HIETIKARMY VGLTPDKRFL
PGHLGMGLVE GYDSMGYEMS KPDLRAELEA DLKLICEGKK DKHVVLRQQV QKYKQVFTEA
VAKAKKLDEA LSQYFGERAE VVQQEEMYPA MPEPIRKCPQ CNKDMVLRTK KTGGFYLSCT
GFPECRSAVW FPDSVLEASR DGSVCPVCQP HPVYRLKLKF KRGSLPPTMP LEFVGCIGGC
DETLREILDL RFSRGPPRVS QPSGHLQASQ SLNRMDSSQR AHAQPPDHRQ TGPSKALARA
LPPPPTAGEG NSVTCNCGQE AVLLTVRKEG PNQGRQFYKC NSGGCSFFLW ADSSPPGAGA
KLPALASRPP GSSLGPLPAS GSHPTGFSHP RDGGGGGTSC LCSQPAVTRT VQKDGPNKGR
QFHTCAKPRE QQCGFFQWAD ENMAPGYSRC HGIRISLLWT CSAGGHPPAV VWYCCPAHRG
SLAGCIQ
//
