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Database: UniProt
Entry: A0A1R3IM24_COCAP
LinkDB: A0A1R3IM24_COCAP
Original site: A0A1R3IM24_COCAP 
ID   A0A1R3IM24_COCAP        Unreviewed;       878 AA.
AC   A0A1R3IM24;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   03-MAY-2023, 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   ORFNames=CCACVL1_11312 {ECO:0000313|EMBL:OMO83625.1};
OS   Corchorus capsularis (Jute).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX   NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO83625.1, ECO:0000313|Proteomes:UP000188268};
RN   [1] {ECO:0000313|EMBL:OMO83625.1, ECO:0000313|Proteomes:UP000188268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC   TISSUE=Whole seedling {ECO:0000313|EMBL:OMO83625.1};
RA   Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA   Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA   Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT   "Corchorus capsularis genome sequencing.";
RL   Submitted (SEP-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OMO83625.1}.
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DR   EMBL; AWWV01009851; OMO83625.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R3IM24; -.
DR   STRING; 210143.A0A1R3IM24; -.
DR   EnsemblPlants; OMO83625; OMO83625; CCACVL1_11312.
DR   Gramene; OMO83625; OMO83625; CCACVL1_11312.
DR   OMA; AFWNDLI; -.
DR   OrthoDB; 10940at2759; -.
DR   Proteomes; UP000188268; 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   Gene3D; 1.10.132.10; -; 1.
DR   Gene3D; 2.170.11.10; DNA Topoisomerase I, domain 2; 2.
DR   InterPro; IPR011010; DNA_brk_join_enz.
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 BETA; 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; 2.
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   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:UP000188268};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW   ECO:0000256|RuleBase:RU365101}.
FT   DOMAIN          475..851
FT                   /note="DNA topoisomerase I eukaryotic-type"
FT                   /evidence="ECO:0000259|SMART:SM00435"
FT   REGION          1..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          754..781
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        26..127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..208
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        258..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..306
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..330
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   878 AA;  98279 MW;  88335E283EB3B2F7 CRC64;
     MAVEASPAKN VYDFDDDDDD GPVRFKRSNT SSSKQNQLNS ELKKASSQRS EGLSVRQVSD
     VRSPNGQTSN VLKNKTNPSS KSPPVRSPIM SPKASTSSSK ASAVKLPVTN SKASASLSEQ
     SKQELKQNMD TSVKDERSPT KDAAEPKIDD EDDDDDDDKP LSSRLKVTSN QGNKGTSTSA
     SAQSKQLVPK TEVKVSAEDS DDEVPVAMRL KNKMSNPGTS NNKPYESDEK KPIASKIQQN
     GSMSKDKMQK SSLLSGKRPL DKGNSSDQSL AKKPKVCGTP TTVKTKQVTV KAEKADEDDD
     HIPIAQRMKK STLSNSKPSS KPTKVVSSSL KKINKKSKKE MKSSKYSKST KELPSSGDGQ
     KKWSTLVHNG VIFPPPYKPH GVKVLYNGRP VDLTPEQEEV ATMYAIMKDT DYMNKEQFKK
     NFWEDWSKIL GKNHIIKDLK NCDFDKIYEW HLLEKEKKKQ MSAEVGNFRV EPPGLFRGRG
     EHPKMGKLKK RIRPSDITIN IGKDAPIPEC PIPGERWKEI KHDNTVTWLA FWNDPINPKE
     FKYVFLAASS SLKGQSDKEK YEKARMLKGY IKNIRAAYTK DFTTKDVMKR QIAVATYLID
     KLALRAGNEK DDDEADTVGC CTLKVGNVEC IPPNKLKFDF LGKDSIQYVN TVEVELPVYK
     AIGQFQTGKS KIDDLFDKLD TSKLNAHLKE LMPGLTAKVF RTYNASITLD EMLNKETKEG
     DVTEKVAVYQ RANKEVAIIC NHQRSVSKSH GAQISKLTDK IKELKDVIKE LKIDLDRAKK
     GKSPLKGADG KQKRNLAPAA LEKKIAQTNA KIEKFERDMQ IKEDLKTVAL GTSKINYLDP
     RISVAWCKRH EVPIEKIFNK SLLAKFAWAM DVDPDFRF
//
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