Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9YCB6 (RGYR1_AERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Reverse gyrase 1

Including the following 2 domains:

  1. Helicase
    EC=3.6.4.12
  2. Topoisomerase
    EC=5.99.1.3
Gene names
Name:rgy1
Ordered Locus Names:APE_1340.1
OrganismAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) [Complete proteome] [HAMAP]
Taxonomic identifier272557 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Aeropyrum ›

Protein attributes

Sequence length1370 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. It cleaves transiently a single DNA strand and remains covalently bound to the 5' DNA end through a tyrosine residue. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication By similarity. HAMAP-Rule MF_01125

Catalytic activity

ATP + H2O = ADP + phosphate. HAMAP-Rule MF_01125

ATP-dependent breakage, passage and rejoining of double-stranded DNA. HAMAP-Rule MF_01125

Cofactor

Magnesium. Binds two Mg2+ per subunit By similarity.

Subunit structure

Monomer By similarity.

Domain

Both the DNA unwinding and positive supercoiling activities require the cooperation of both domains. The cooperative action between the helicase-like and the topoisomerase domains is specific. The helicase-like domain probably does not directly unwind DNA but acts more likely by driving ATP-dependent conformational changes within the whole enzyme, functioning more like a protein motor. The "latch" region of the N-terminal domain plays a regulatory role in the enzyme, repressing topoisomerase activity in the absence of ATP and therefore preventing the enzyme from acting as an ATP-independent relaxing enzyme; it also helps to coordinate nucleotide hydrolysis by the ATPase domain with the supercoiling activity of the topoisomerase domain By similarity. HAMAP-Rule MF_01125

Miscellaneous

This enzyme is the only unique feature of hyperthermophilic bacteria/archaea discovered so far. It appears to be essential for adaptation to life at high temperatures. HAMAP-Rule MF_01125

Sequence similarities

In the N-terminal section; belongs to the DEAD box helicase family. DDVD subfamily.

In the C-terminal section; belongs to the prokaryotic type I/III topoisomerase family.

Contains 1 helicase ATP-binding domain.

Contains 1 Toprim domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13701370Reverse gyrase 1 HAMAP-Rule MF_01125
PRO_0000158084

Regions

Domain99 – 287189Helicase ATP-binding
Domain647 – 825179Toprim
Zinc finger16 – 3722C4-type 1 By similarity
Nucleotide binding112 – 1198ATP By similarity
Zinc finger747 – 76418C4-type 2 By similarity
Region653 – 1370718Topoisomerase I HAMAP-Rule MF_01125
Motif220 – 2234DEAD box HAMAP-Rule MF_01125

Sites

Active site10281For DNA cleavage activity By similarity
Metal binding6531Magnesium 1; catalytic By similarity
Metal binding7941Magnesium 1; catalytic By similarity
Metal binding7941Magnesium 2 By similarity
Metal binding7961Magnesium 2 By similarity
Binding site951ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9YCB6 [UniParc].

Last modified June 26, 2007. Version 2.
Checksum: 03F731FB2EA80936

FASTA1,370154,734
        10         20         30         40         50         60 
MASARAASRG VYRYLCPNCG GPNSEERLSR GLPCPRCLPR LPRKGVSGWT GLARLLRREG 

        70         80         90        100        110        120 
TLGAGVKAMA SLEEEARSLW RFFEKAVGSP PWGAQRTWAK RLARGDSFSI IAPTGVGKTT 

       130        140        150        160        170        180 
FGAAASLFYA CKKGMRSYIV LPTTTLAANV ARKLESMVES TGCGRVRLLV IHSKLKTSER 

       190        200        210        220        230        240 
REAMERFEKG DFDILVTTAA FARKYADRLS GYRFRLVFVD DVDAVLRSAR SVDAILKIVG 

       250        260        270        280        290        300 
FDEEAIEKGL EVLRLQREQA RLVGLLQSQR EEVREEARKK LLEVKRRLER LEAEIEARRG 

       310        320        330        340        350        360 
RTASLIVSSA TGRPRGARVR LFRVLLNFEA GGRGDIGLRR VIDSYTHPTD GVAEKVVELV 

       370        380        390        400        410        420 
RRLGTGGLVY VPIDMGVEYA ERLAEELRRA GVKAEAYHAK KPLELLDRFA EGEIDVLVGV 

       430        440        450        460        470        480 
ANYYGTLVRG LDLPARVRYA VFAGVPRHKF GSDIGDPHPS RLLRLLSILA ESRIEEVASA 

       490        500        510        520        530        540 
ARSHMGRLRR MLRVLSPAAL QMIAERVARG EVEGGYDRQV LEAYQFLREA LARDDVWESL 

       550        560        570        580        590        600 
RELDVGIVRE GGRTYILVPD PATYLQASGR TSRLYAGGIT LGLSVVVVDN EPVMRGLMKR 

       610        620        630        640        650        660 
VSWMAEVDWR RFEDLDLQSI LREIDEDREK VRRVVKGLYR GVELVRTALL VVESPNKART 

       670        680        690        700        710        720 
IARFFGQPSV RLLPGGGRVY EVATGDKILM IMASGGHVFD LVVRVDGRDL EAAGGEPEHA 

       730        740        750        760        770        780 
IFGVLRYRLG GNGAAAYTPV YTSIKRCLDC GYQFVDEASR CPRCGSELIR NSLSTVEDLR 

       790        800        810        820        830        840 
RVAWEADEVY VGTDPDTEGE KIGWDVALAL RPYAPDIKRL EFHEVTKKAI LEALSNPRSF 

       850        860        870        880        890        900 
DDNLVDAQVV RRVEDRWIGF TLSPLLWCDF WPRYCKRVLE EYGEKRPHMD RERCAKYKAY 

       910        920        930        940        950        960 
YNLSAGRVQT PTLGWVVDRT LAYRKKVWLY RVVHDSQLLF AVRSDDPEVP ESVKRVLDNW 

       970        980        990       1000       1010       1020 
VKHHKKTGIE PWLDVKAVVE KEEWTALPPP PPYTTDTMLR DANRLLGLGS AEAMRIAQDL 

      1030       1040       1050       1060       1070       1080 
FEWGLITYHR TDSTRVSDRG MQVAREWLET RFGGLAGQLY RPRRWGEGGA HEAIRPVRPI 

      1090       1100       1110       1120       1130       1140 
DVERLQLLVE EGVIELPGTL TRRHLRLYDL IFRRFMASQM READALRVVY RLRVPELDGY 

      1150       1160       1170       1180       1190       1200 
TLTLERVVEI GRPGDAEGVT RGFTLVWPYV RPQPRLVEGR EAWIRARVEG RQVPKAYPYT 

      1210       1220       1230       1240       1250       1260 
EGEIVEEMKT RGIGRPSTYA KIVETLFRRR YVIEVSREEG RGAGFVVATS RGINVYNYLT 

      1270       1280       1290       1300       1310       1320 
EELRSADEEE YGGRIAGILR RVPSLVSEDR TRELERQMDM VEKGDASRDD VLESVFNEIS 

      1330       1340       1350       1360       1370 
DLALLLNIEH PIKHRSRAEG NTQGNTWVSN FVACAVKSPE VSRVWGAGVG

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000002 Genomic DNA. Translation: BAA80332.2.
PIRF72609.
RefSeqNP_147880.2. NC_000854.2.

3D structure databases

ProteinModelPortalQ9YCB6.
ModBaseSearch...

Protein-protein interaction databases

STRING272557.APE_1340.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA80332; BAA80332; APE_1340.1.
GeneID1445950.
KEGGape:APE_1340.1.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1110.
HOGENOMHOG000222775.
KOK03170.
ProtClustDBPRK09401.

Enzyme and pathway databases

BioCycAPER272557:GJD6-916-MONOMER.

Family and domain databases

Gene3D1.10.290.10. 1 hit.
1.10.460.10. 2 hits.
HAMAPMF_01125. Reverse_gyrase.
InterProIPR003593. AAA+_ATPase.
IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR005736. Reverse_gyrase.
IPR000380. Topo_IA.
IPR003601. Topo_IA_2.
IPR013497. Topo_IA_cen.
IPR013824. Topo_IA_cen_sub1.
IPR013826. Topo_IA_cen_sub3.
IPR023405. Topo_IA_core_domain.
IPR003602. Topo_IA_DNA-bd.
IPR006171. Toprim_domain.
[Graphical view]
PANTHERPTHR11390. PTHR11390. 1 hit.
PfamPF00270. DEAD. 1 hit.
PF01131. Topoisom_bac. 1 hit.
PF01751. Toprim. 1 hit.
[Graphical view]
PRINTSPR00417. PRTPISMRASEI.
SMARTSM00382. AAA. 1 hit.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00437. TOP1Ac. 1 hit.
SM00436. TOP1Bc. 1 hit.
SM00493. TOPRIM. 1 hit.
[Graphical view]
SUPFAMSSF56712. Topo_IA_core. 1 hit.
TIGRFAMsTIGR01054. rgy. 1 hit.
PROSITEPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRGYR1_AERPE
AccessionPrimary (citable) accession number: Q9YCB6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: June 26, 2007
Last modified: May 1, 2013
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents