ID A0A0S3SEJ1_PHAAN Unreviewed; 893 AA.
AC A0A0S3SEJ1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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};
GN Name=Vigan.06G255300 {ECO:0000313|EMBL:BAT91240.1};
GN ORFNames=VIGAN_06255300 {ECO:0000313|EMBL:BAT91240.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT91240.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT91240.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP015039; BAT91240.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3SEJ1; -.
DR Proteomes; UP000291084; Chromosome 6.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
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; cd00660; Topoisomer_IB_N; 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 PANTHER; PTHR10290:SF23; DNA TOPOISOMERASE 1; 1.
DR PANTHER; PTHR10290; DNA TOPOISOMERASE I; 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; SSF56741; Eukaryotic DNA topoisomerase I, N-terminal DNA-binding fragment; 1.
DR PROSITE; PS00176; TOPOISOMERASE_I_EUK; 1.
PE 3: Inferred from homology;
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:UP000291084};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU365101}.
FT DOMAIN 490..866
FT /note="DNA topoisomerase I eukaryotic-type"
FT /evidence="ECO:0000259|SMART:SM00435"
FT REGION 1..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 893 AA; 101199 MW; 4BD35C94F84FFA34 CRC64;
MAVETSDKPN LPHDFDDDDD APIIYKRISS KKNQTHSEAR KSNSHIHDGQ SYRQAPNAPS
SNGQTSSLQK GNTAPSLKPS AMKPSVGISR TPNSVGNTSS VKLPVANSKS PSLGDKQKMS
VDVKVEPKST EHSGKNFCED SEDDEDDKPL SFRLKNSNHD NKVTSVVKKS YEDSDDDDDV
PLAKKLPRNL NLGTTSNNHE DSDKKPISKI QKDRQNGSGM SNKQDRPSPL PAKRPLDNSN
SLQPSVKKPK VSASDASIKT ELVSEKRELK TEDDDDDDHI PISQRIKKQG MTGDKSSSTK
KVLQKVTKVN KSISKPFKKQ TKKIVKKSGS GSEYSKSSKL LPSSGDGQKK WTTLVHNGVI
FPPPYQQHGV KMLYKGRPVD LTPEQEEVAT MYAVMRDTEY MQKDKFKDNF WNDWRKLLGR
NHVIQNLKDC DFTPIYDWYQ GVKDKKKQMT TEEKKILKEE KMKQEEKYMW AMVDGVKEKV
GNFRVEPPGL FRGRGEHPKM GKLKKRIHPG DITINIGKDA PIPECPIPGE RWKEIRHDNT
VTWLAYWSDP INPKLFKYVF LAASSSLKGQ SDKEKYEKAR MLKDYIENIR SAYTKDFTNK
DITKLQIAVA TYLIDKLALR AGNEKDDDEA DTVGCCTLKV ENVTREPPNK LKFNFLGKDS
IKYENTVEVE LPVYNAILKL QKDKRPGDDL FDKLDTSKLN AHLKELMPGL TAKVFRTFNA
SITLDNMLNQ ETKDGDVGEK IVVYQHANKQ VAIICNHQRS VSKSHDAQMS KLTEKIDELQ
AVLKELKTDL DRARKGKPPL KSSDGKTKKN LTPEVLEKKM SQTNAKIEKM QRDMKTKEDL
KTVALGTSKI NYLDPRITVA WCKRHEVPIE KIFNKSLLAK FCWAMDVDPD FRF
//
