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
//