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TOP6A_PYRAB
ID   TOP6A_PYRAB             Reviewed;         382 AA.
AC   Q9V134; G8ZJ60;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Type 2 DNA topoisomerase 6 subunit A {ECO:0000255|HAMAP-Rule:MF_00132};
DE            EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_00132};
DE   AltName: Full=Type II DNA topoisomerase VI subunit A {ECO:0000255|HAMAP-Rule:MF_00132};
GN   Name=top6A {ECO:0000255|HAMAP-Rule:MF_00132}; OrderedLocusNames=PYRAB05950;
GN   ORFNames=PAB2411;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
CC   -!- FUNCTION: Relaxes both positive and negative superturns and exhibits a
CC       strong decatenase activity. {ECO:0000255|HAMAP-Rule:MF_00132}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00132};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00132};
CC   -!- SUBUNIT: Homodimer. Heterotetramer of two Top6A and two Top6B chains.
CC       {ECO:0000255|HAMAP-Rule:MF_00132}.
CC   -!- SIMILARITY: Belongs to the TOP6A family. {ECO:0000255|HAMAP-
CC       Rule:MF_00132}.
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DR   EMBL; AJ248284; CAB49517.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE69987.1; -; Genomic_DNA.
DR   PIR; F75179; F75179.
DR   RefSeq; WP_010867719.1; NC_000868.1.
DR   AlphaFoldDB; Q9V134; -.
DR   SMR; Q9V134; -.
DR   IntAct; Q9V134; 1.
DR   MINT; Q9V134; -.
DR   STRING; 272844.PAB2411; -.
DR   EnsemblBacteria; CAB49517; CAB49517; PAB2411.
DR   GeneID; 1495500; -.
DR   KEGG; pab:PAB2411; -.
DR   PATRIC; fig|272844.11.peg.633; -.
DR   eggNOG; arCOG04143; Archaea.
DR   HOGENOM; CLU_037229_1_0_2; -.
DR   OMA; NWGEARF; -.
DR   OrthoDB; 22842at2157; -.
DR   PhylomeDB; Q9V134; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd00223; TOPRIM_TopoIIB_SPO; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   HAMAP; MF_00132; Top6A; 1.
DR   InterPro; IPR002815; Spo11/TopoVI_A.
DR   InterPro; IPR013049; Spo11/TopoVI_A_N.
DR   InterPro; IPR036078; Spo11/TopoVI_A_sf.
DR   InterPro; IPR004085; TopoVI_A.
DR   InterPro; IPR034136; TOPRIM_Topo6A/Spo11.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR10848; PTHR10848; 1.
DR   Pfam; PF04406; TP6A_N; 1.
DR   PRINTS; PR01550; TOP6AFAMILY.
DR   PRINTS; PR01552; TPISMRASE6A.
DR   SUPFAM; SSF56726; SSF56726; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Isomerase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Topoisomerase.
FT   CHAIN           1..382
FT                   /note="Type 2 DNA topoisomerase 6 subunit A"
FT                   /id="PRO_0000145452"
FT   ACT_SITE        108
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
FT   BINDING         202
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
FT   BINDING         254
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
SQ   SEQUENCE   382 AA;  44188 MW;  6462F819FDEBD6BD CRC64;
     MKLKRQKPKE KFSYDPQKVL KKLEDLAWKI LEEVKSGKNP YFDVPTRGLN NVYFDEEARL
     IKLGDKLSRR YFLNVAHARK FTQTLILMAY IKRLVSEGKH ASLREAYYAN KHTIPGTREN
     TFEDQSESDP IIEDLERMLG VLREEMHITA DRRGYIYGDI VIKDGEDEFN ASKLGTGGWA
     VPGTVEHIQF PEVNVDYVLV VETAAMADRL IEEKYPKKEN CLIVATQGQA SRGVRRLIHR
     LHYEEGLPII VFTDGDPYGW YIYSTIKQGS INLAYLSEKL ATPDAKFVGM TMDDIKEYNL
     EHVTEKLKGI PPDKKGGPTG DYKRLIEELN YPWFQNKEWQ RQLKLALKWG VRIEQQALAN
     KSLEFVAKEY LPEKIREGKL LP
 
 
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