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Protein

ATP-dependent DNA helicase Ta0057

Gene

Ta0057

Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

ATP-dependent 5'-3' DNA helicase involved in nucleotide excision repair (NER) of DNA.By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Cofactori

[4Fe-4S] clusterNote: Binds 1 [4Fe-4S] cluster.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi74 – 741Iron-sulfur (4Fe-4S)
Metal bindingi95 – 951Iron-sulfur (4Fe-4S)
Metal bindingi110 – 1101Iron-sulfur (4Fe-4S)
Metal bindingi146 – 1461Iron-sulfur (4Fe-4S)

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 188ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Keywords - Ligandi

4Fe-4S, ATP-binding, DNA-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent DNA helicase Ta0057 (EC:3.6.4.12)
Gene namesi
Ordered Locus Names:Ta0057
OrganismiThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Taxonomic identifieri273075 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
Proteomesi
  • UP000001024 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 602602ATP-dependent DNA helicase Ta0057PRO_0000352310Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi273075.Ta0057m.

Structurei

Secondary structure

1
602
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107Combined sources
Beta strandi13 – 164Combined sources
Helixi17 – 3216Combined sources
Beta strandi35 – 428Combined sources
Helixi43 – 5917Combined sources
Beta strandi64 – 663Combined sources
Helixi70 – 734Combined sources
Helixi77 – 804Combined sources
Helixi88 – 10316Combined sources
Helixi107 – 1093Combined sources
Helixi115 – 1184Combined sources
Helixi120 – 12910Combined sources
Helixi133 – 14210Combined sources
Helixi147 – 1548Combined sources
Helixi155 – 1573Combined sources
Beta strandi159 – 1646Combined sources
Helixi165 – 1684Combined sources
Helixi171 – 18111Combined sources
Helixi185 – 1873Combined sources
Beta strandi188 – 1925Combined sources
Helixi195 – 1973Combined sources
Helixi198 – 2069Combined sources
Beta strandi208 – 2114Combined sources
Helixi212 – 22413Combined sources
Beta strandi229 – 2313Combined sources
Helixi236 – 25419Combined sources
Beta strandi256 – 2583Combined sources
Beta strandi260 – 2623Combined sources
Helixi265 – 27511Combined sources
Helixi279 – 30224Combined sources
Helixi310 – 32213Combined sources
Turni326 – 3283Combined sources
Beta strandi329 – 3346Combined sources
Helixi336 – 3383Combined sources
Beta strandi340 – 3456Combined sources
Helixi349 – 3524Combined sources
Helixi353 – 3575Combined sources
Beta strandi358 – 3669Combined sources
Helixi370 – 3778Combined sources
Beta strandi383 – 3853Combined sources
Helixi392 – 3943Combined sources
Beta strandi395 – 4006Combined sources
Helixi407 – 4093Combined sources
Helixi412 – 42918Combined sources
Beta strandi433 – 4386Combined sources
Helixi440 – 4467Combined sources
Helixi464 – 47310Combined sources
Beta strandi479 – 4835Combined sources
Beta strandi489 – 4913Combined sources
Helixi496 – 4983Combined sources
Beta strandi501 – 5066Combined sources
Helixi514 – 52714Combined sources
Helixi530 – 5345Combined sources
Helixi536 – 54813Combined sources
Beta strandi553 – 5553Combined sources
Beta strandi558 – 5636Combined sources
Helixi565 – 5739Combined sources
Beta strandi578 – 5814Combined sources
Helixi583 – 59513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VSFX-ray2.90A1-602[»]
4A15X-ray2.20A2-602[»]
5H8WX-ray2.20A1-597[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HM14.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 247247Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini421 – 602182Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi193 – 1964DEAH box

Sequence similaritiesi

Belongs to the helicase family. RAD3/XPD subfamily.Curated
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiarCOG00770. Archaea.
COG1199. LUCA.
OMAiRENYLTI.

Family and domain databases

Gene3Di3.40.50.300. 4 hits.
InterProiIPR006555. ATP-dep_Helicase_C.
IPR010614. DEAD_2.
IPR010643. HBB.
IPR014013. Helic_SF1/SF2_ATP-bd_DinG/Rad3.
IPR006554. Helicase-like_DEXD_c2.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF06733. DEAD_2. 1 hit.
PF06777. HBB. 1 hit.
PF13307. Helicase_C_2. 1 hit.
[Graphical view]
SMARTiSM00488. DEXDc2. 1 hit.
SM00491. HELICc2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 4 hits.
PROSITEiPS51193. HELICASE_ATP_BIND_2. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9HM14-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQKSYGVALE SPTGSGKTIM ALKSALQYSS ERKLKVLYLV RTNSQEEQVI
60 70 80 90 100
KELRSLSSTM KIRAIPMQGR VNMCILYRMV DDLHEINAES LAKFCNMKKR
110 120 130 140 150
EVMAGNEAAC PYFNFKIRSD ETKRFLFDEL PTAEEFYDYG ERNNVCPYES
160 170 180 190 200
MKAALPDADI VIAPYAYFLN RSVAEKFLSH WGVSRNQIVI ILDEAHNLPD
210 220 230 240 250
IGRSIGSFRI SVESLNRADR EAQAYGDPEL SQKIHVSDLI EMIRSALQSM
260 270 280 290 300
VSERCGKGDV RIRFQEFMEY MRIMNKRSER EIRSLLNYLY LFGEYVENEK
310 320 330 340 350
EKVGKVPFSY CSSVASRIIA FSDQDEEKYA AILSPEDGGY MQAACLDPSG
360 370 380 390 400
ILEVLKESKT IHMSGTLDPF DFYSDITGFE IPFKKIGEIF PPENRYIAYY
410 420 430 440 450
DGVSSKYDTL DEKELDRMAT VIEDIILKVK KNTIVYFPSY SLMDRVENRV
460 470 480 490 500
SFEHMKEYRG IDQKELYSML KKFRRDHGTI FAVSGGRLSE GINFPGNELE
510 520 530 540 550
MIILAGLPFP RPDAINRSLF DYYERKYGKG WEYSVVYPTA IKIRQEIGRL
560 570 580 590 600
IRSAEDTGAC VILDKRAGQF RKFIPDMKKT SDPASDIYNF FISAQAREKY

GA
Length:602
Mass (Da):69,169
Last modified:March 1, 2001 - v1
Checksum:iCE13FA7D1F3A0DD8
GO

Sequence cautioni

The sequence CAC11205 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL445063 Genomic DNA. Translation: CAC11205.1. Different initiation.

Genome annotation databases

EnsemblBacteriaiCAC11205; CAC11205; CAC11205.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL445063 Genomic DNA. Translation: CAC11205.1. Different initiation.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VSFX-ray2.90A1-602[»]
4A15X-ray2.20A2-602[»]
5H8WX-ray2.20A1-597[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273075.Ta0057m.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC11205; CAC11205; CAC11205.

Phylogenomic databases

eggNOGiarCOG00770. Archaea.
COG1199. LUCA.
OMAiRENYLTI.

Miscellaneous databases

EvolutionaryTraceiQ9HM14.

Family and domain databases

Gene3Di3.40.50.300. 4 hits.
InterProiIPR006555. ATP-dep_Helicase_C.
IPR010614. DEAD_2.
IPR010643. HBB.
IPR014013. Helic_SF1/SF2_ATP-bd_DinG/Rad3.
IPR006554. Helicase-like_DEXD_c2.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF06733. DEAD_2. 1 hit.
PF06777. HBB. 1 hit.
PF13307. Helicase_C_2. 1 hit.
[Graphical view]
SMARTiSM00488. DEXDc2. 1 hit.
SM00491. HELICc2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 4 hits.
PROSITEiPS51193. HELICASE_ATP_BIND_2. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiXPD_THEAC
AccessioniPrimary (citable) accession number: Q9HM14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: March 1, 2001
Last modified: May 11, 2016
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.