GenomeNet

Database: UniProt
Entry: A0A482WCJ2_9CUCU
LinkDB: A0A482WCJ2_9CUCU
Original site: A0A482WCJ2_9CUCU 
ID   A0A482WCJ2_9CUCU        Unreviewed;       852 AA.
AC   A0A482WCJ2;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   22-FEB-2023, entry version 12.
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=BDFB_010613 {ECO:0000313|EMBL:RZC42173.1};
OS   Asbolus verrucosus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Pimeliinae; Asbolus.
OX   NCBI_TaxID=1661398 {ECO:0000313|EMBL:RZC42173.1, ECO:0000313|Proteomes:UP000292052};
RN   [1] {ECO:0000313|EMBL:RZC42173.1, ECO:0000313|Proteomes:UP000292052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Butters {ECO:0000313|EMBL:RZC42173.1};
RC   TISSUE=Head and leg muscle {ECO:0000313|EMBL:RZC42173.1};
RA   Rider S.D.;
RT   "Genome of the blue death feigning beetle - Asbolus verrucosus.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:RZC42173.1}.
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; QDEB01010189; RZC42173.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A482WCJ2; -.
DR   STRING; 1661398.A0A482WCJ2; -.
DR   Proteomes; UP000292052; Unassembled WGS sequence.
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: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; 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; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034144; TOPRIM_TopoIII.
DR   PANTHER; PTHR11390:SF20; DNA TOPOISOMERASE 3-BETA-1; 1.
DR   PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   Pfam; PF01751; Toprim; 1.
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   PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000292052};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW   ECO:0000256|RuleBase:RU362092}.
FT   DOMAIN          3..156
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          822..841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   852 AA;  95609 MW;  99C10B19643B3E7B CRC64;
     MKTVLMVAEK PSLAASLANI LSNGSNSTRK GSNGICSVHE WNGTFRGTPA RLKMTSVCGH
     VMGVDFISKY NNWDRVDPVE LFSCPIEKKE ATPKFKMPMF LSHEAKGCDN LVLWLDCDKE
     GENICFEVMQ CVARSMSGDV FSNSVTYRAK FSAITEQDIK AAFNNLSHPN ENEAKSVDAR
     QELDLRIGCA FTRFQTKFFQ GRYGDLDSSL ISYGPCQTPT LGFCVQRHDQ IQTFKPESYW
     VIKVTIKTKD GDDVNLEWKR IRCFDKEVAN MFLQQIKNQT EAKVVSVVAK EKSKPRPVAL
     NTVELMRVAS SGLGMGPHHA MQIAEKLYTQ GYISYPRTET TRYPENFDLV GVLRQQQNSS
     EWGEDVREIL SKGVNRPKQG HDAGDHPPIT PMKLASRNEL DSESWKLYDY IARHFIATLA
     RDCKYLSTTA TVVINDETFT VTGKTLLDPG YTTVMTWQAF DKNEIVPNLS ENELVPIKDM
     RLSEHQTSPP DYLTEAELIT LMETHGIGTD ASIPVHINNI SQRNYVTVTS GRRLKPTTLG
     IVLVHGYQKI DAELVLPTMR SAVEEQLNLI AIGKANFQAV LRHTVDIFRL KFQYFVKNID
     GMDQLFEVSF SPLSASGKAH SRCGKCRRYM KYIQAKPPRL HCPQCDDTYS LPQNGTVKLF
     KELKCPLDDF ELLCWTMGNK GKSFVFCPYC YNHPPFKDMK KGNGCNSCSH PTCPYSLNSN
     GVCSCVECDA GVLVLDPSSG PKWKLGCTRC DTIINFFDDA QKITVLSDVC DCGAQLVNVE
     YKSEKTKLPN SSSEMKGCVF CTAEFGKLVD KPKTAVYVRS RPFRGGKAPN RGRGRSRAKP
     KDKMAQLAAY FV
//
DBGET integrated database retrieval system