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TOP6A_AERPE
ID   TOP6A_AERPE             Reviewed;         389 AA.
AC   Q9YE67;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   03-AUG-2022, entry version 120.
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=APE_0703.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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; BA000002; BAA79679.2; -; Genomic_DNA.
DR   PIR; G72659; G72659.
DR   AlphaFoldDB; Q9YE67; -.
DR   SMR; Q9YE67; -.
DR   STRING; 272557.APE_0703.1; -.
DR   EnsemblBacteria; BAA79679; BAA79679; APE_0703.1.
DR   KEGG; ape:APE_0703.1; -.
DR   PATRIC; fig|272557.25.peg.504; -.
DR   eggNOG; arCOG04143; Archaea.
DR   Proteomes; UP000002518; 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..389
FT                   /note="Type 2 DNA topoisomerase 6 subunit A"
FT                   /id="PRO_0000145444"
FT   ACT_SITE        107
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
FT   BINDING         208
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
FT   BINDING         260
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
SQ   SEQUENCE   389 AA;  45416 MW;  AC7865AAD473A7BB CRC64;
     MSGEMFGDEV DIKARLRAAE VMYKKFHRLI SDVIKGRPPK LEIPKRTLSN TIFDPERGIL
     VIGEEKLERE FLNVGESRRF MQTLLMASII YQSLIENEYP TIRDLYYKGK HTIVYRDYSG
     RKREENTWDE QKESDSVIQD IEVYTGLFRE DMLILSKEKG KVVGNMRIRS GGDVIDLSKL
     GHGAYAIEPT PDLIEFLDVD AEFVLVVEKD AVFQQLHRAG FWKKYKALLV TGSGQPDRAT
     RRFVRRLHEE LKLPVYIITD SDPYGWYIYS VYKVGSITLS YESERLATPK AKFLGVQMTD
     IFGYRGKKPY LSEAERKKFM IKATDKDIKR AKELLNYSWI GKNRRWNVEI RLFLKHLVKL
     EIEAIASKGL KFFAYQYIPE KIETGDWID
 
 
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