位置:首页 > 蛋白库 > TOP6A_NATPD
TOP6A_NATPD
ID   TOP6A_NATPD             Reviewed;         368 AA.
AC   Q3IPW7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=NP_3480A;
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC   2260 / Gabara;
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
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}.
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; CR936257; CAI49831.1; -; Genomic_DNA.
DR   RefSeq; WP_011323451.1; NC_007426.1.
DR   AlphaFoldDB; Q3IPW7; -.
DR   SMR; Q3IPW7; -.
DR   STRING; 348780.NP_3480A; -.
DR   EnsemblBacteria; CAI49831; CAI49831; NP_3480A.
DR   GeneID; 3703275; -.
DR   KEGG; nph:NP_3480A; -.
DR   eggNOG; arCOG04143; Archaea.
DR   HOGENOM; CLU_037229_1_0_2; -.
DR   OMA; NWGEARF; -.
DR   OrthoDB; 22842at2157; -.
DR   Proteomes; UP000002698; 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; Reference proteome; Topoisomerase.
FT   CHAIN           1..368
FT                   /note="Type 2 DNA topoisomerase 6 subunit A"
FT                   /id="PRO_1000018316"
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;  42118 MW;  3E7A61D8D7A000EE CRC64;
     MSSESDTDTE DEIARERLIE LASDFYDQFA EGEVPTMEIP TRTKSNIVFD EDKDVWVYGD
     RTSTRSANSV RGAQKLLKAI YTIEFLADQL EQGRSSTLRE LYYLSESWDE ERAQFNDQDE
     SNQLVEDLEI VSKVTREDFH MRPEESGATI MGPLYLREQT RRGEREIHCQ KDVGEGGYQI
     PNNPDTIEFL DNDADFVLCV ETGGMRDRLV ENGFDEEHNV IIVHLKGQPA RATRRITKRL
     HDDLDLPVVV FCDGDPWSYR IYASVAYGSI KSAHLSEYLA TPEAEYIGIQ PADIVEYDLP
     TDPLSDSDIN ALESELDDPR FQDDYWREQI ELQLDIGKKA EQQALASRGL DFVTETYLPE
     RLGEMGVL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024