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Q92TE4 (Q92TE4_RHIME) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length811 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings By similarity. RuleBase RU003363 HAMAP MF_01898

Catalytic activity

ATP-dependent breakage, passage and rejoining of double-stranded DNA. RuleBase RU003363 SAAS SAAS002288 HAMAP MF_01898

Subunit structure

Made up of two chains. The A chain is responsible for DNA breakage and rejoining; the B chain catalyzes ATP hydrolysis. The enzyme forms an A2B2 tetramer By similarity. HAMAP MF_01898

Subcellular location

Cytoplasm By similarity HAMAP MF_01898.

Sequence similarities

Belongs to the type II topoisomerase family. HAMAP MF_01898 RuleBase RU000380

Contains 1 Toprim domain. SAAS SAAS002288 HAMAP MF_01898

Sequences

Sequence LengthMass (Da)Tools
Q92TE4 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: D7B9E477673F27C5

FASTA81188,781
        10         20         30         40         50         60 
MTDISETEAG AIAEYGADSI KVLKGLDAVR KRPGMYIGDT DDGSGLHHMV YEVVDNAIDE 

        70         80         90        100        110        120 
ALAGHADIVT VTLNPDGSVT VTDNGRGIPT DIHREEGVSA AEVIMTQLHA GGKFDQNSYK 

       130        140        150        160        170        180 
VSGGLHGVGV SVVNALSVSL KLKIRRAGKI HEMSFTHGVA DGPLKVTGDA GGETGTEVTF 

       190        200        210        220        230        240 
TPSEQTFSNI EFEFGTLEHR LRELAFLNSG VRIVLTDKRH SDIRREEMMY DGGLEAFVAY 

       250        260        270        280        290        300 
LDRAKKPLVQ KPVSIRGEKD GITVEVAMWW NDSYHENVLC FTNNIPQRDG GTHMAGFRGA 

       310        320        330        340        350        360 
LTRQITSYAD TSGITKKEKV SLTGDDCREG LTAVLSVKVP DPKFSSQTKD KLVSSEVRPV 

       370        380        390        400        410        420 
VESLVNEALS VWLEEHPSDA KILVGKVVEA AAAREAARKA RELTRRKGAL DISSLPGKLA 

       430        440        450        460        470        480 
DCSERDPAKS ELFLVEGDSA GGSAKQGRSR ENQAILPLRG KILNVERARF DKMLSSQEIG 

       490        500        510        520        530        540 
TLITALGTSI GKDEFNADKL RYHKIIIMTD ADVDGAHIRT LLLTFFFRQM PELIERGHLY 

       550        560        570        580        590        600 
IAQPPLYKVA RGKSVQYLKD EKALEDYLIS MGLEEASLEL ASGEVRVGQD LREVINDALR 

       610        620        630        640        650        660 
LRSLMEGLHS RYNRSVVEQA AIAGALNVEL NGERDEYQLI AAEVARRLDV IAEETERGWE 

       670        680        690        700        710        720 
AAVTAEGGLK LERMVRGVKE AAVLDMALIG SSDARHIDQL KARLKEVYGA PPVLRRRDGT 

       730        740        750        760        770        780 
QEISGPRALL DAIFAAGRKG LTMQRYKGLG EMNAEQLWET TLDPNVRSLL QVKVTDATDA 

       790        800        810 
DGLFSRLMGD EVEPRRDFIQ ENALSVANLD I 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL591688 Genomic DNA. Translation: CAC41399.1.
RefSeqNP_384118.1. NC_003047.1.

3D structure databases

HSSPHSSP built from PDB template 1AJ6 based on UniProtKB P06982.
ProteinModelPortalQ92TE4.
SMRQ92TE4. Positions 20-389.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1231637.
GenomeReviewsGene locus R00012 in contig AL591688_GR.
KEGGsme:SMc02782.
NMPDRfig|266834.1.peg.1306.
PATRIC23629173. VBISinMel96828_1364.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG304889.
OMADCSSRDP.
ProtClustDBPRK14939.

Enzyme and pathway databases

BioCycSMEL266834:SMC02782-MONOMER.

Family and domain databases

HAMAPMF_01898. GyrB.
[Tree]
InterProIPR003594. ATPase-like_ATP-bd.
IPR011557. GyrB.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR001241. Topo_IIA.
IPR013759. Topo_IIA_B/N_ab.
IPR002288. Topo_IIA_B_C.
IPR013506. Topo_IIA_bsu_dom2.
IPR013760. Topo_IIA_cen.
IPR018522. TopoIIA_CS.
IPR006171. Toprim_domain.
[Graphical view]
Gene3DG3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.
G3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit.
G3DSA:3.40.50.670. Topo_IIA_B/N_ab. 2 hits.
KOK02470.
PfamPF00204. DNA_gyraseB. 1 hit.
PF00986. DNA_gyraseB_C. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01751. Toprim. 1 hit.
[Graphical view]
PRINTSPR00418. TPI2FAMILY.
SMARTSM00387. HATPase_c. 1 hit.
SM00433. TOP2c. 1 hit.
[Graphical view]
SUPFAMSSF55874. ATP_bd_ATPase. 1 hit.
SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.
SSF56719. Topo_IIA_cen. 1 hit.
TIGRFAMsTIGR01059. GyrB. 1 hit.
PROSITEPS00177. TOPOISOMERASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ92TE4_RHIME
AccessionPrimary (citable) accession number: Q92TE4
Entry history
Integrated into UniProtKB/TrEMBL: December 1, 2001
Last sequence update: December 1, 2001
Last modified: January 25, 2012
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)