(data stored in SCRATCH zone)

SWISSPROT: D5EA31_METMS

ID   D5EA31_METMS            Unreviewed;       367 AA.
AC   D5EA31;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 56.
DE   RecName: Full=Type 2 DNA topoisomerase 6 subunit A {ECO:0000256|HAMAP-Rule:MF_00132};
DE            EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_00132};
DE   AltName: Full=Type II DNA topoisomerase VI subunit A {ECO:0000256|HAMAP-Rule:MF_00132};
GN   Name=top6A {ECO:0000256|HAMAP-Rule:MF_00132};
GN   OrderedLocusNames=Mmah_0505 {ECO:0000313|EMBL:ADE36032.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE36032.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE36032.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Relaxes both positive and negative superturns and exhibits a
CC       strong decatenase activity. {ECO:0000256|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:0000256|HAMAP-
CC         Rule:MF_00132};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00132};
CC   -!- SUBUNIT: Homodimer. Heterotetramer of two Top6A and two Top6B chains.
CC       {ECO:0000256|HAMAP-Rule:MF_00132}.
CC   -!- SIMILARITY: Belongs to the TOP6A family. {ECO:0000256|HAMAP-
CC       Rule:MF_00132}.
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DR   EMBL; CP001994; ADE36032.1; -; Genomic_DNA.
DR   RefSeq; WP_013036975.1; NC_014002.1.
DR   EnsemblBacteria; ADE36032; ADE36032; Mmah_0505.
DR   GeneID; 8982646; -.
DR   KEGG; mmh:Mmah_0505; -.
DR   eggNOG; arCOG04143; Archaea.
DR   eggNOG; COG1697; LUCA.
DR   HOGENOM; HOG000225930; -.
DR   KO; K03166; -.
DR   OMA; FTDGDPY; -.
DR   OrthoDB; 22842at2157; -.
DR   BioCyc; MMAH547558:G1GHT-507-MONOMER; -.
DR   Proteomes; UP000001059; 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:0016889; F:endodeoxyribonuclease activity, producing 3'-phosphomonoesters; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IEA:InterPro.
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;
DR   PRODOM; D5EA31.
DR   SWISS-2DPAGE; D5EA31.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00132};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00132};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00132, ECO:0000313|EMBL:ADE36032.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00132};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00132};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00132};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00132}.
FT   DOMAIN          77..139
FT                   /note="TP6A_N"
FT                   /evidence="ECO:0000259|Pfam:PF04406"
FT   ACT_SITE        104
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00132"
FT   METAL           200
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00132"
FT   METAL           252
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00132"
SQ   SEQUENCE   367 AA;  42094 MW;  C82FD74183619942 CRC64;
     MAKNEHRKEH DRLAEQRLTG LASELYSHFV DGRIPYVNMP SRTKNNIEFN EISDVWVYGG
     RESERSAKTV KGAFQLLKTS HVLDFLLNNH IGNNRGSTLR ELYYISENWD IAKFKEQPES
     DRLIEDLEII SSLQREYFHM RPEEDGATLF GPLQLREETK RGDRDIHCQE DVGESGYQIP
     FNVENIDFID HDAKFIIAIE TGGMYARLIE NGFDELNDAI LVHLKGQPAR STRRMIKRMN
     EELGIPVVVF TDGDPWSYRI YASVAYGAIK SAHLSEFMAT PAAKFVGVQP SDIVEYELST
     DKLTDKDVDA LRSELTDPRF ETDYWKEQIN LQLDIGKKAE QQAFAGKGLD FVTKTYLPDR
     LSDMGII
//

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