ID A0A2A3EH92_APICC Unreviewed; 1025 AA.
AC A0A2A3EH92;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=APICC_06219 {ECO:0000313|EMBL:PBC31078.1};
OS Apis cerana cerana (Oriental honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Apis.
OX NCBI_TaxID=94128 {ECO:0000313|EMBL:PBC31078.1, ECO:0000313|Proteomes:UP000242457};
RN [1] {ECO:0000313|EMBL:PBC31078.1, ECO:0000313|Proteomes:UP000242457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Pupae without intestine {ECO:0000313|EMBL:PBC31078.1};
RA Diao Q., Sun L., Zheng H., Zheng H., Xu S., Wang S., Zeng Z., Hu F., Su S.,
RA Wu J.;
RT "Genomic and transcriptomic analysis on Apis cerana provide comprehensive
RT insights into honey bee biology.";
RL Submitted (JUL-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; KZ288250; PBC31078.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3EH92; -.
DR STRING; 94128.A0A2A3EH92; -.
DR Proteomes; UP000242457; 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: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; 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:UP000242457};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU365101}.
FT DOMAIN 622..997
FT /note="DNA topoisomerase I eukaryotic-type"
FT /evidence="ECO:0000259|SMART:SM00435"
FT REGION 1..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 572..599
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 902..971
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 37..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..352
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1025 AA; 120246 MW; 646D200CB070E380 CRC64;
MELEQAATQS NSDSEKKIKE NSNVTGNHSD THINGMSNGF DKKREHKSEH RDRDKERSHK
SDHKDRSKEK DRNHKSEHRD KEKDRHKHSS SSIKEKDKHD TSNSNKDKDK DRKSSSSSKD
KEHKSSSSSS KDKEKDKSKD KEHHHKSSSS SSSKDKDRHH SSSKDKESKE KDKDKSKDKY
KHSLSSSSRD KDKDKDKEKN ISKDKEKERK LEKDKERHST SHTNDKEKHR SSEKDKDKHN
LSNKDKHRHD KEKDRHRHDK EKSKHREDKD KKDKEKEEIK VKEEIMDIKS NHIGNEEFHY
DIGQTIKHEV KEESVSQIEP EDDDDSGGEQ PLYIKEEEDE EEPVNEEEGS MDSTDGNDTR
LSDLHNTTIK TEEESDEDVP LSARSMAPTS IKRSLDSEEE EDVPLSARKK SKKSDTKTKK
KKRKYEDDED EDEIEQKPKK KGARTSKGEN SSPRKKKQEE EQEVWKWWEE EKKNDGTKWT
FLEHKGPVFA PPYEPLPPDV NFYYNGKEMK LSQDAEEVAT FYARMLDHDY TTKPAFNSNF
FHDWREVMTE SERTKIVDLS KCNFKEIHAY FIQKSEERKA MTKEEKQKIK EKNEEIQKEY
GYCIIDGHKE KIGNFKIEPP GLFRGRGEHP KMGKLKKRVM PEDILINCSK DSNIPKPPPG
HKWKEIRHDP NVTWLASWTE NIQGQVKYVM LNPSSKLKGE KDWQKYEIAR KLAQLIDKIR
AEYREDWKSK EMRIRQRAVA LYFIDKLALR AGNEKDEDQA DTVGCCSLRV EHITLHEQKD
GKEYVVVFDF LGKDSIRYYN EVPVEKRVFK NLQLFMENKS PSDDLFDRLN TTVMNKHLNE
LMEGLTAKVF RTYNASWTLQ QQLDKLTNPD DTEAEKILSY NRANRAVAIL CNHQRSVPKT
HAKSMENLKA KIEAKKQAIN DAELAVKDAK RDAKHGSVKE KVTYEKKKKA LDRLKEQLTK
LEVQATDKEE NKEIALGTSK LNYLDPRITV AWCKKHNVPI EKIYNKTQRD KFRWAIDMAG
PDYIF
//
