ID A0A099YYV0_TINGU Unreviewed; 746 AA.
AC A0A099YYV0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 08-NOV-2023, entry version 33.
DE RecName: Full=DNA topoisomerase I {ECO:0000256|RuleBase:RU365101};
DE EC=5.6.2.1 {ECO:0000256|RuleBase:RU365101};
DE AltName: Full=DNA topoisomerase 1 {ECO:0000256|RuleBase:RU365101};
DE Flags: Fragment;
GN ORFNames=N309_12131 {ECO:0000313|EMBL:KGL74063.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL74063.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL74063.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL74063.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Releases the supercoiling and torsional tension of DNA
CC introduced during the DNA replication and transcription by transiently
CC cleaving and rejoining one strand of the DNA duplex. Introduces a
CC single-strand break via transesterification at the specific target site
CC 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is
CC attacked by the catalytic tyrosine of the enzyme, resulting in the
CC formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the
CC expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes
CC passage around the unbroken strand thus removing DNA supercoils.
CC Finally, in the religation step, the DNA 5'-OH attacks the covalent
CC intermediate to expel the active-site tyrosine and restore the DNA
CC phosphodiester backbone. {ECO:0000256|RuleBase:RU365101}.
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:RU365101};
CC -!- SIMILARITY: Belongs to the type IB topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00006645, ECO:0000256|RuleBase:RU365101}.
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DR EMBL; KL886610; KGL74063.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099YYV0; -.
DR STRING; 94827.A0A099YYV0; -.
DR Proteomes; UP000053641; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR CDD; cd00659; Topo_IB_C; 1.
DR CDD; cd03488; Topoisomer_IB_N_htopoI_like; 1.
DR Gene3D; 1.10.132.10; -; 1.
DR Gene3D; 2.170.11.10; DNA Topoisomerase I, domain 2; 1.
DR Gene3D; 1.10.10.41; Yeast DNA topoisomerase - domain 1; 1.
DR InterPro; IPR011010; DNA_brk_join_enz.
DR InterPro; IPR013034; DNA_topo_DNA_db_N_dom1.
DR InterPro; IPR013030; DNA_topo_DNA_db_N_dom2.
DR InterPro; IPR001631; TopoI.
DR InterPro; IPR018521; TopoI_AS.
DR InterPro; IPR025834; TopoI_C_dom.
DR InterPro; IPR014711; TopoI_cat_a-hlx-sub_euk.
DR InterPro; IPR014727; TopoI_cat_a/b-sub_euk.
DR InterPro; IPR013500; TopoI_cat_euk.
DR InterPro; IPR008336; TopoI_DNA-bd_euk.
DR InterPro; IPR036202; TopoI_DNA-bd_euk_N_sf.
DR InterPro; IPR013499; TopoI_euk.
DR InterPro; IPR048045; Topoisomer_I_DNA-bd.
DR PANTHER; PTHR10290; DNA TOPOISOMERASE I; 1.
DR PANTHER; PTHR10290:SF1; DNA TOPOISOMERASE I, MITOCHONDRIAL; 1.
DR Pfam; PF14370; Topo_C_assoc; 1.
DR Pfam; PF01028; Topoisom_I; 1.
DR Pfam; PF02919; Topoisom_I_N; 1.
DR PRINTS; PR00416; EUTPISMRASEI.
DR SMART; SM00435; TOPEUc; 1.
DR SUPFAM; SSF56349; DNA breaking-rejoining enzymes; 1.
DR SUPFAM; SSF46596; Eukaryotic DNA topoisomerase I, dispensable insert domain; 1.
DR SUPFAM; SSF56741; Eukaryotic DNA topoisomerase I, N-terminal DNA-binding fragment; 1.
DR PROSITE; PS00176; TOPOISOMERASE_I_EUK; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU365101};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU365101};
KW Reference proteome {ECO:0000313|Proteomes:UP000053641};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU365101}.
FT DOMAIN 341..718
FT /note="DNA topoisomerase I eukaryotic-type"
FT /evidence="ECO:0000259|SMART:SM00435"
FT REGION 1..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 291..318
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 625..692
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL74063.1"
FT NON_TER 746
FT /evidence="ECO:0000313|EMBL:KGL74063.1"
SQ SEQUENCE 746 AA; 87125 MW; 04BF887A24EF3536 CRC64;
QDKKKQVKLK AEKSKKVKSE QEKSRDKKEK GERKKIKNEK VSEVEKTDEE QEKQEGPGGS
EGQVGEEKES KDGKGIKQEG EEEDEQGGEG LGTAWNMEFG QEAKDEVDAG TEVPRKGKKQ
QAKAKKPKEE EKEKGRKSKE KSKETETLEK TQKRKYKEEE KNSKKAKKEK KVKEVKKENI
ENKWKWWEEE KMGDGIKWKQ LEHKGPYFAP LYEPLPENVQ FYYDGKPLKL SLATEEIATF
YAKMLDHEYT TKEIFQNNFF NDWRKEMTPA EQKIIKNLEK CDFKEIHKYF VDKSEARKAL
SKEEKQKLKE EADKIQEEYG YCILDGHREK IGNFKTEPPG LFRGRGDHPK MGMLKKRIMP
EDVVINCSKD SKIPEPPAGH KWKEVRFDNT VTWLASWTEN IQNTLKYIML NPSSKLKGEK
DWQKYEVARR LKDVVHKIRA QYQADWKSKE MKKRQRAVAL YFIDKLALRA GNEKEEGETA
DTVGCCSLRV EHIKLYHKLD GQEHVVEFDF LGKDSIRYYN KVPVEKLVFK NLQLFMKNKD
PGDDLFDRLN TSILNRHLQH LMKGLSAKVF RTYNASITLQ EQLKALTNAG DSVAGKLLSY
NRANRAVAIL CNHQRSAPKT FEKSMQILQT KIDAKKQQLE EAQLELKKAE DELKDKNDDK
TEVNVQKKKK LLERLTEQLA KLEVQATDKE ENKQIALGTS KLNYLDPRIT IAWCKKFGVP
IEKVYNKTQR EKFAWAIDMT DEDFEF
//
