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Protein

ATP-dependent RNA helicase has1

Gene

has1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

ATP-dependent RNA helicase involved in 40S ribosomal subunit biogenesis. Required for the processing and cleavage of 35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA.

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi133 – 1408ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Ribosome biogenesis, rRNA processing

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase has1 (EC:3.6.4.13)
Gene namesi
Name:has1
ORF Names:SPAC1F7.02c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1F7.02c.
PomBaseiSPAC1F7.02c. has1.

Subcellular locationi

GO - Cellular componenti

  • nucleolus Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 578578ATP-dependent RNA helicase has1PRO_0000055087Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601Phosphoserine1 Publication
Modified residuei62 – 621Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ09916.

PTM databases

iPTMnetiQ09916.

Interactioni

Subunit structurei

Associates in the nucleolus with the 60S and pre-60S ribosomal subunits.By similarity

Protein-protein interaction databases

BioGridi278164. 7 interactions.
MINTiMINT-4696367.

Structurei

3D structure databases

ProteinModelPortaliQ09916.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini120 – 296177Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini310 – 480171Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi89 – 11729Q motifAdd
BLAST
Motifi243 – 2464DEAD box
Motifi322 – 33817Bipartite nuclear localization signalBy similarityAdd
BLAST

Domaini

The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000268799.
InParanoidiQ09916.
KOiK13179.
OMAiTKGFVFR.
OrthoDBiEOG7FR7R5.
PhylomeDBiQ09916.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR025313. DUF4217.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF13959. DUF4217. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM01178. DUF4217. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q09916-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKSELKRKK HQSGNEEVKE KRQKPLKNDK KIAEELPQDE DDYEQEEENE
60 70 80 90 100
DADQNTSVES ESEELDNENE DERVQKSVNL NASSTSDIEK FSDLQLSENI
110 120 130 140 150
QKAIKEMGFE TMTEIQKRSI PPLLAGRDVL GAAKTGSGKT LAFLIPTIEM
160 170 180 190 200
LYALKFKPRN GTGVIIISPT RELALQIFGV AKELLKYHHQ TFGIVIGGAN
210 220 230 240 250
RRAEADKLVK GVNLLVATPG RLLDHLQNTK GFVFRNLRSL VIDEADRILE
260 270 280 290 300
IGFEDEMRQI MKILPSENRQ TLLFSATQTT KVEDLARISL KPGPLYVNVD
310 320 330 340 350
SGKPTSTVEG LEQGYVVVDS DKRFLLLFSF LKRNLKKKVI VFMSSCASVK
360 370 380 390 400
YMAELLNYID LPVLDLHGKQ KQQRRTNTFF EFCNAEKGIL LCTNVAARGL
410 420 430 440 450
DIPAVDWIVQ YDPPDDPRDY IHRVGRTARG TKGTGKSLMF LAPSELGFLR
460 470 480 490 500
YLKTAKVSLN EFEFPANKVA NVQSQLEKLV SKNYYLQQSA KDGYRSYLQA
510 520 530 540 550
YASYSLKSIF DINKLDLAKV AKSFGFAHPP NVNITIGASG RTDKKERRAG
560 570
YNKKNHVDVY SKQRSSAISQ DKERGWSR
Length:578
Mass (Da):65,261
Last modified:February 1, 1996 - v1
Checksum:i37E8FDB4081901E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA91949.1.
PIRiS62574.
RefSeqiNP_594488.1. NM_001019917.2.

Genome annotation databases

EnsemblFungiiSPAC1F7.02c.1; SPAC1F7.02c.1:pep; SPAC1F7.02c.
GeneIDi2541668.
KEGGispo:SPAC1F7.02c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA91949.1.
PIRiS62574.
RefSeqiNP_594488.1. NM_001019917.2.

3D structure databases

ProteinModelPortaliQ09916.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278164. 7 interactions.
MINTiMINT-4696367.

PTM databases

iPTMnetiQ09916.

Proteomic databases

MaxQBiQ09916.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1F7.02c.1; SPAC1F7.02c.1:pep; SPAC1F7.02c.
GeneIDi2541668.
KEGGispo:SPAC1F7.02c.

Organism-specific databases

EuPathDBiFungiDB:SPAC1F7.02c.
PomBaseiSPAC1F7.02c. has1.

Phylogenomic databases

HOGENOMiHOG000268799.
InParanoidiQ09916.
KOiK13179.
OMAiTKGFVFR.
OrthoDBiEOG7FR7R5.
PhylomeDBiQ09916.

Miscellaneous databases

PROiQ09916.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR025313. DUF4217.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF13959. DUF4217. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM01178. DUF4217. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-62, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiHAS1_SCHPO
AccessioniPrimary (citable) accession number: Q09916
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 6, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  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.