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TOP6A_HALMA
ID   TOP6A_HALMA             Reviewed;         368 AA.
AC   Q5V4R4;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=rrnAC0459;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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; AY596297; AAV45488.1; -; Genomic_DNA.
DR   RefSeq; WP_004962323.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5V4R4; -.
DR   SMR; Q5V4R4; -.
DR   STRING; 272569.rrnAC0459; -.
DR   EnsemblBacteria; AAV45488; AAV45488; rrnAC0459.
DR   GeneID; 40154726; -.
DR   GeneID; 64822811; -.
DR   KEGG; hma:rrnAC0459; -.
DR   PATRIC; fig|272569.17.peg.1231; -.
DR   eggNOG; arCOG04143; Archaea.
DR   HOGENOM; CLU_037229_1_0_2; -.
DR   OMA; NWGEARF; -.
DR   Proteomes; UP000001169; Chromosome I.
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; Reference proteome; Topoisomerase.
FT   CHAIN           1..368
FT                   /note="Type 2 DNA topoisomerase 6 subunit A"
FT                   /id="PRO_0000145446"
FT   ACT_SITE        103
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
FT   BINDING         201
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
FT   BINDING         253
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
SQ   SEQUENCE   368 AA;  41965 MW;  4ED984D5C6D9C7FD CRC64;
     MSTDSDTTPD TEEAREQLID LAADFYDQFA DGEVPTMTIP TRTKSNIVFD EDEQVWVYGD
     RNSTRSAKTI SGAEKILKAV YTIDFLSQQL EEDRSSTLRE LYYLSESWDL DEAQFNTQDE
     SNNLIEDLEI VSDVKREDFH MRPEESGAKV MGPLLLREQT NRGDREIHCQ DDVGQGGYQI
     PNNPDTIEFL DNDAKFVLCV ETGGMRDRLV ENGFDDEYDA LVVHLGGQPA RATRRLIKRL
     HDELDLPVTV FTDGDPWSYR IFGSVSYGSI KSAHLSEYLA TPEAQFIGIR PEDIVEYELP
     TDPLSDSDVN ALESELEDPR FQTDFWEEQI ELQLDINKKA EQQALASRGL DFVTETYLPE
     RLDEMGIL
 
 
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