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Protein

ATP-dependent DNA helicase Hel308

Gene

hel308

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks. Unwinds the lagging strand from forked DNA structures in a 3'-5' direction. PCNA, the DNA polymerase sliding clamp subunit, stimulates the helicase activity, and may alter substrate specificity. Unwinds branched DNA (Holliday junctions) in an ATP-dependent fashion; ss- and dsDNA stimulate ATPase to the greatest extent, although it preferentially binds DNA with a single-stranded region. Processes a RecA-mediated recombination intermediate between gapped circular and homologus linear dsDNA.UniRule annotation2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.UniRule annotation

Cofactori

Mg2+1 Publication, Zn2+1 PublicationNote: Divalent cations, Mg2+ and Zn2+ are best.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei28 – 281ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi46 – 538ATP

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.4.12. 5243.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent DNA helicase Hel308UniRule annotation (EC:3.6.4.12UniRule annotation)
Alternative name(s):
ATP-dependent Holliday junction unwindase Hjm
Holliday junction migration DNA helicase
Gene namesi
Name:hel308UniRule annotation
Synonyms:hjm
Ordered Locus Names:PF0677
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000001013 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi52 – 521K → A: No ATPase activity. 1 Publication
Mutagenesisi145 – 1451D → A: No ATPase activity. 1 Publication
Mutagenesisi146 – 1461E → A: No ATPase activity. 1 Publication
Mutagenesisi701 – 72020Missing : No binding to PCNA. 1 PublicationAdd
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 720720ATP-dependent DNA helicase Hel308PRO_0000102110Add
BLAST

Proteomic databases

PRIDEiO73946.

Expressioni

Inductioni

Constitutively expressed (at protein level).1 Publication

Interactioni

Subunit structurei

Monomer. Interacts with PCNA.UniRule annotation2 Publications

Protein-protein interaction databases

STRINGi186497.PF0677.

Structurei

Secondary structure

1
720
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Helixi10 – 189Combined sources
Helixi26 – 327Combined sources
Turni33 – 353Combined sources
Helixi36 – 383Combined sources
Beta strandi41 – 455Combined sources
Helixi48 – 503Combined sources
Helixi52 – 6716Combined sources
Beta strandi69 – 746Combined sources
Helixi78 – 803Combined sources
Helixi81 – 877Combined sources
Helixi89 – 946Combined sources
Beta strandi98 – 1014Combined sources
Helixi110 – 1145Combined sources
Beta strandi116 – 1205Combined sources
Helixi122 – 13110Combined sources
Helixi136 – 1383Combined sources
Beta strandi139 – 1457Combined sources
Helixi147 – 1515Combined sources
Turni153 – 1553Combined sources
Helixi156 – 16611Combined sources
Beta strandi170 – 1767Combined sources
Helixi182 – 1887Combined sources
Beta strandi191 – 1955Combined sources
Beta strandi200 – 20910Combined sources
Beta strandi212 – 2154Combined sources
Beta strandi220 – 2223Combined sources
Helixi228 – 2358Combined sources
Beta strandi240 – 2434Combined sources
Helixi247 – 26115Combined sources
Helixi262 – 2643Combined sources
Helixi267 – 27812Combined sources
Helixi284 – 29310Combined sources
Turni294 – 2963Combined sources
Beta strandi297 – 3004Combined sources
Helixi306 – 31712Combined sources
Beta strandi323 – 3264Combined sources
Beta strandi328 – 3303Combined sources
Helixi331 – 3333Combined sources
Beta strandi338 – 3436Combined sources
Beta strandi346 – 3483Combined sources
Beta strandi351 – 3533Combined sources
Helixi359 – 3668Combined sources
Turni372 – 3743Combined sources
Beta strandi376 – 3838Combined sources
Beta strandi385 – 3873Combined sources
Helixi389 – 3968Combined sources
Helixi411 – 42414Combined sources
Helixi430 – 4389Combined sources
Helixi441 – 4455Combined sources
Helixi450 – 46516Combined sources
Beta strandi468 – 4714Combined sources
Beta strandi477 – 4793Combined sources
Helixi481 – 4899Combined sources
Helixi493 – 50816Combined sources
Helixi512 – 5209Combined sources
Helixi532 – 5343Combined sources
Helixi535 – 54511Combined sources
Helixi546 – 5483Combined sources
Turni554 – 5574Combined sources
Helixi561 – 58121Combined sources
Helixi586 – 5938Combined sources
Helixi597 – 62125Combined sources
Helixi624 – 6263Combined sources
Helixi627 – 63913Combined sources
Helixi643 – 6486Combined sources
Beta strandi651 – 6533Combined sources
Helixi656 – 6638Combined sources
Turni664 – 6663Combined sources
Helixi670 – 6745Combined sources
Helixi678 – 6825Combined sources
Helixi689 – 69911Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZJ2X-ray2.40A1-720[»]
2ZJ5X-ray2.40A1-720[»]
2ZJ8X-ray2.00A1-720[»]
2ZJAX-ray2.70A1-720[»]
ProteinModelPortaliO73946.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO73946.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 197165Helicase ATP-bindingUniRule annotationAdd
BLAST
Domaini229 – 422194Helicase C-terminalUniRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi145 – 1484DEAH box

Sequence similaritiesi

Belongs to the helicase family. Hel308 subfamily.UniRule annotation
Contains 1 helicase ATP-binding domain.UniRule annotation
Contains 1 helicase C-terminal domain.UniRule annotation

Phylogenomic databases

eggNOGiarCOG00553. Archaea.
COG1204. LUCA.
HOGENOMiHOG000227028.
KOiK03726.
OMAiDEIHYLG.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
HAMAPiMF_00442. Helicase_Hel308.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR022965. Helicase_Hel308.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR027417. P-loop_NTPase.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00278. HhH1. 2 hits.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O73946-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVDELRVDE RIKSTLKERG IESFYPPQAE ALKSGILEGK NALISIPTAS
60 70 80 90 100
GKTLIAEIAM VHRILTQGGK AVYIVPLKAL AEEKFQEFQD WEKIGLRVAM
110 120 130 140 150
ATGDYDSKDE WLGKYDIIIA TAEKFDSLLR HGSSWIKDVK ILVADEIHLI
160 170 180 190 200
GSRDRGATLE VILAHMLGKA QIIGLSATIG NPEELAEWLN AELIVSDWRP
210 220 230 240 250
VKLRRGVFYQ GFVTWEDGSI DRFSSWEELV YDAIRKKKGA LIFVNMRRKA
260 270 280 290 300
ERVALELSKK VKSLLTKPEI RALNELADSL EENPTNEKLA KAIRGGVAFH
310 320 330 340 350
HAGLGRDERV LVEENFRKGI IKAVVATPTL SAGINTPAFR VIIRDIWRYS
360 370 380 390 400
DFGMERIPII EVHQMLGRAG RPKYDEVGEG IIVSTSDDPR EVMNHYIFGK
410 420 430 440 450
PEKLFSQLSN ESNLRSQVLA LIATFGYSTV EEILKFISNT FYAYQRKDTY
460 470 480 490 500
SLEEKIRNIL YFLLENEFIE ISLEDKIRPL SLGIRTAKLY IDPYTAKMFK
510 520 530 540 550
DKMEEVVKDP NPIGIFHLIS LTPDITPFNY SKREFERLEE EYYEFKDRLY
560 570 580 590 600
FDDPYISGYD PYLERKFFRA FKTALVLLAW INEVPEGEIV EKYSVEPGDI
610 620 630 640 650
YRIVETAEWL VYSLKEIAKV LGAYEIVDYL ETLRVRVKYG IREELIPLMQ
660 670 680 690 700
LPLVGRRRAR ALYNSGFRSI EDISQARPEE LLKIEGIGVK TVEAIFKFLG
710 720
KNVKISEKPR KSTLDYFLKS
Length:720
Mass (Da):82,631
Last modified:November 1, 1998 - v1
Checksum:iBA17FCE53F615688
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016521 Genomic DNA. Translation: BAA32016.1.
AE009950 Genomic DNA. Translation: AAL80801.1.
PIRiT43854.
RefSeqiWP_011011799.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL80801; AAL80801; PF0677.
GeneIDi1468523.
KEGGipfu:PF0677.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016521 Genomic DNA. Translation: BAA32016.1.
AE009950 Genomic DNA. Translation: AAL80801.1.
PIRiT43854.
RefSeqiWP_011011799.1. NC_003413.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZJ2X-ray2.40A1-720[»]
2ZJ5X-ray2.40A1-720[»]
2ZJ8X-ray2.00A1-720[»]
2ZJAX-ray2.70A1-720[»]
ProteinModelPortaliO73946.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi186497.PF0677.

Proteomic databases

PRIDEiO73946.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL80801; AAL80801; PF0677.
GeneIDi1468523.
KEGGipfu:PF0677.

Phylogenomic databases

eggNOGiarCOG00553. Archaea.
COG1204. LUCA.
HOGENOMiHOG000227028.
KOiK03726.
OMAiDEIHYLG.

Enzyme and pathway databases

BRENDAi3.6.4.12. 5243.

Miscellaneous databases

EvolutionaryTraceiO73946.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
HAMAPiMF_00442. Helicase_Hel308.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR022965. Helicase_Hel308.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR027417. P-loop_NTPase.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00278. HhH1. 2 hits.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Pfu helicase locus."
    Kanai A., Oida H., Yabe T., Hihara S., Doi H.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  2. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
    Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
    Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  3. "Identification of a novel helicase activity unwinding branched DNAs from the hyperthermophilic archaeon, Pyrococcus furiosus."
    Fujikane R., Komori K., Shinagawa H., Ishino Y.
    J. Biol. Chem. 280:12351-12358(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, FUNCTION, ATP-DEPENDENCE, COFACTOR, SUBUNIT, INDUCTION.
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  4. "The archaeal Hjm helicase has recQ-like functions, and may be involved in repair of stalled replication fork."
    Fujikane R., Shinagawa H., Ishino Y.
    Genes Cells 11:99-110(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN ATPASE, FUNCTION AS A HELICASE, INTERACTION WITH PCNA, SUBUNIT, DNA-BINDING, MUTAGENESIS OF LYS-52; ASP-145; GLU-146 AND 701-LYS--SER-720.
  5. "Atomic structures and functional implications of the archaeal RecQ-like helicase Hjm."
    Oyama T., Oka H., Mayanagi K., Shirai T., Matoba K., Fujikane R., Ishino Y., Morikawa K.
    BMC Struct. Biol. 9:2-2(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) WITH AND WITHOUT ATP.

Entry informationi

Entry nameiHELS_PYRFU
AccessioniPrimary (citable) accession number: O73946
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: November 1, 1998
Last modified: December 9, 2015
This is version 105 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.