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TOP6B_NATPD
ID   TOP6B_NATPD             Reviewed;         798 AA.
AC   Q3IPW6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Type 2 DNA topoisomerase 6 subunit B {ECO:0000255|HAMAP-Rule:MF_00322};
DE            EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_00322};
DE   AltName: Full=Type II DNA topoisomerase VI subunit B {ECO:0000255|HAMAP-Rule:MF_00322};
DE            Short=TopoVI-B {ECO:0000255|HAMAP-Rule:MF_00322};
GN   Name=top6B {ECO:0000255|HAMAP-Rule:MF_00322}; OrderedLocusNames=NP_3482A;
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_00322}.
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_00322};
CC   -!- SUBUNIT: Homodimer. Heterotetramer of two Top6A and two Top6B chains.
CC       {ECO:0000255|HAMAP-Rule:MF_00322}.
CC   -!- SIMILARITY: Belongs to the TOP6B family. {ECO:0000255|HAMAP-
CC       Rule:MF_00322}.
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DR   EMBL; CR936257; CAI49832.1; -; Genomic_DNA.
DR   RefSeq; WP_011323452.1; NC_007426.1.
DR   AlphaFoldDB; Q3IPW6; -.
DR   SMR; Q3IPW6; -.
DR   STRING; 348780.NP_3482A; -.
DR   EnsemblBacteria; CAI49832; CAI49832; NP_3482A.
DR   GeneID; 3703276; -.
DR   KEGG; nph:NP_3482A; -.
DR   eggNOG; arCOG01165; Archaea.
DR   HOGENOM; CLU_006403_0_0_2; -.
DR   OMA; TRIELEM; -.
DR   OrthoDB; 13565at2157; -.
DR   Proteomes; UP000002698; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd00823; TopoIIB_Trans; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   HAMAP; MF_00322; Top6B; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR040494; Top6b_C.
DR   InterPro; IPR005734; TopoVI_B.
DR   InterPro; IPR015320; TopoVI_B_transducer.
DR   PANTHER; PTHR10871:SF4; PTHR10871:SF4; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF18000; Top6b_C; 1.
DR   Pfam; PF09239; Topo-VIb_trans; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR01052; top6b; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Isomerase; Nucleotide-binding;
KW   Reference proteome; Topoisomerase.
FT   CHAIN           1..798
FT                   /note="Type 2 DNA topoisomerase 6 subunit B"
FT                   /id="PRO_1000005872"
FT   REGION          221..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT   BINDING         91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT   BINDING         112..113
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT   BINDING         122..129
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT   BINDING         629
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
SQ   SEQUENCE   798 AA;  87363 MW;  82DF9847312DB62A CRC64;
     MTSYQSQLGD GGGGEPIAEE LAESQQSISI AEFFEKNKQM LGFDSDAKAL VTAVKEAVDN
     ALDAAEEAGI LPDIYVEIED RGDYYRLTVE DNGPGITKEQ IPKVFGKLLY GSRFHAREQT
     RGQQGIGISA AVLYSQLTSG KPAKITSKTD SHSSAQYFEL TIDTDTNEPE IDHEREATWE
     RPHGTRIELE MEGNMRARKQ LHDYIKYTAV VNPHARVEFH EPEDSFKSER ATEELPPETE
     EIRPHPHGVE LGTLLKMLDA TDSYSLSGFL QAEFTRVGNK TADGVIDSFR DRHFGREMAW
     SPPQPHEDVD IETAVSDAVA NKSAEATAAF ARAVADEVTD MAALSHAELS AVVASVADDI
     EAEHDETFGE TVRENAVEAA WKSVTDDVSA DCYALVDGAT TTRKDDAAVE GLSRRLAEKF
     TDQEDARNRF RRSTLREFVD RAADATEEYD DATFGETARE NVVEAVWERA VTVPDEPPTV
     TEVADNRDAA ARLLEAMRST DILSPPTDCL APISEDLVKA GLKKEYDAEF YTSVTRDASV
     HGGDPFVVEV GIAHGGDIAV DGSVETLRFA NRVPLVYQRG ACATVDVLKG VNWRNYGLDQ
     PGGSGMPSGP AVIMVHVAST SVPFTSESKD AVANIPEIED ELRLALQQAG RDLQSHLKKQ
     RSLEKRRRKQ DVIADILPDM AAKLSEVTDR EPLDVEDSLA RIMNNVLVER TVEESTVQLS
     VHNYGDTNVG PEVTDIVSQE PDGAESATVV EMDGEWFLKW SPTVGGGETA TLEYEVDGDA
     EFDISVEGIE AEKLTVDA
 
 
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