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Database: UniProt
Entry: M7BQV0_CHEMY
LinkDB: M7BQV0_CHEMY
Original site: M7BQV0_CHEMY 
ID   M7BQV0_CHEMY            Unreviewed;       677 AA.
AC   M7BQV0;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=UY3_02434 {ECO:0000313|EMBL:EMP40271.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP40271.1, ECO:0000313|Proteomes:UP000031443};
RN   [1] {ECO:0000313|Proteomes:UP000031443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
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}.
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DR   EMBL; KB514175; EMP40271.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7BQV0; -.
DR   STRING; 8469.M7BQV0; -.
DR   eggNOG; KOG1957; Eukaryota.
DR   Proteomes; UP000031443; 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   Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 2.
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; IPR013826; Topo_IA_cen_sub3.
DR   InterPro; IPR023405; Topo_IA_core_domain.
DR   InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR   PANTHER; PTHR11390:SF20; DNA TOPOISOMERASE 3-BETA-1; 1.
DR   PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR   Pfam; PF01131; Topoisom_bac; 2.
DR   PRINTS; PR00417; PRTPISMRASEI.
DR   SMART; SM00437; TOP1Ac; 1.
DR   SMART; SM00436; TOP1Bc; 1.
DR   SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR   PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|RuleBase:RU362092};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362092};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW   Topoisomerase {ECO:0000256|RuleBase:RU362092}.
FT   DOMAIN          10..106
FT                   /note="DNA topoisomerase type IA"
FT                   /evidence="ECO:0000259|SMART:SM00436"
FT   DOMAIN          153..360
FT                   /note="DNA topoisomerase type IA DNA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00437"
FT   REGION          632..670
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        635..659
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   677 AA;  76420 MW;  1E93345EFEC632AA CRC64;
     MNKPRGTEKT VYRAKFSSIT DTDICNAMNS LGEPNRNEAL SVDARQELDL RIGCAFTRFQ
     TKYFQGKYGN LDSSLISFGP CQTPTLGFCV ERHDKIQSFK PETYWVLQAK VNHEKESSLT
     LEWDRVRVFD REIAQMFLNI TKMAREAKVE SVSKKEKAKQ RPLALNTVEM LRVASAALGM
     GPQHTMQIAE RLYTQGYISY PRTETTHYPE NFDLKEPLRQ QANNPYWAET VKALLSEGVN
     RPRKGHDAGD HPPITPMRAA TEAELGFTEI MPWQSIPLEE SLPNCEKGDI FPVSEVKLLE
     KQTNPPDYLT EAELITLMEK HGIGTDASIP VHINNICQRN YVTVESGRRL KPTNLGIVLV
     HGYYKIDAEL VLPTIRSAVE KQLNLIAQGK ANYQQVLEHT LDIFKRKFHY FVDSIAGMDE
     LMEVSFSPLA ATGKPLSRCG KCHRFMKYIQ AKPSRLHCSH CDETYSLPQN GTIKLYKELR
     CPLDDFELVL WSSGSRGKSY PLCPYCYNHP PFRDMKKGMG CNECTHPTCQ HSLSMLGIGQ
     CVECENGVLV LDPTSGPKWK MACNKCNVIV HFFENAHKVR VSPETCESCD AALVDVDFNK
     AKSPLPGDET QHSGCVFCDP VFQDLVELKH AATRHPMHRG GQGKRQGRGR GKGRRPGGRP
     NPKRPKDKMA DLAAYFV
//
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