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Protein

ATP-dependent RNA helicase fal1

Gene

tif412

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 (By similarity).By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi65 – 728ATPPROSITE-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

Enzyme and pathway databases

ReactomeiR-SPO-429947. Deadenylation of mRNA.
R-SPO-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase fal1 (EC:3.6.4.13)
Gene namesi
Name:tif412
Synonyms:fal1
ORF Names:SPAC1F5.10
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1F5.10.
PomBaseiSPAC1F5.10.

Subcellular locationi

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: GO_Central
  • cytosol Source: PomBase
  • nucleolus Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 394394ATP-dependent RNA helicase fal1PRO_0000054967Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei67 – 671Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ10055.
PRIDEiQ10055.

PTM databases

iPTMnetiQ10055.
SwissPalmiQ10055.

Interactioni

Protein-protein interaction databases

BioGridi278099. 2 interactions.
MINTiMINT-4696561.

Structurei

3D structure databases

ProteinModelPortaliQ10055.
SMRiQ10055. Positions 22-394.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini52 – 222171Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini233 – 394162Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi21 – 4929Q motifAdd
BLAST
Motifi170 – 1734DEAD box

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

HOGENOMiHOG000268797.
InParanoidiQ10055.
KOiK13025.
OMAiTATFCIS.
OrthoDBiEOG7FNCJ0.
PhylomeDBiQ10055.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
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.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
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.

Q10055-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADEIMENVE LTTSEDVNAV SSFEEMNLKE DLLRGIYAYG YETPSAVQSR
60 70 80 90 100
AIIQICKGRD VIAQAQSGTG KTATFSIGIL QSIDLSVRDT QALILSPTRE
110 120 130 140 150
LAVQIQNVVL ALGDHMNVQC HACIGGTSVG NDIKKLDYGQ HVVSGTPGRV
160 170 180 190 200
TDMIRRRNLR TRNVKMLILD EADELLNQGF KEQIYDIYRY LPPGTQVVVV
210 220 230 240 250
SATLPQDVLE MTNKFTTNPV RILVKRDELT LEGLKQYFIA VEKEEWKFDT
260 270 280 290 300
LCDLYDTLTI TQAVIFCNSR RKVDWLTEKM REANFTVTSM HGEMPQKERD
310 320 330 340 350
AIMQDFRQGN SRVLICTDIW ARGIDVQQVS LVINYDLPAN RENYIHRIGR
360 370 380 390
SGRFGRKGVA INFVTNEDVR ILRDIEQYYS TVIDEMPMNI GDMV
Length:394
Mass (Da):44,706
Last modified:February 1, 1996 - v1
Checksum:i499EBC2DC6442349
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA92238.1.
PIRiT38085.
RefSeqiNP_592863.1. NM_001018263.2.

Genome annotation databases

EnsemblFungiiSPAC1F5.10.1; SPAC1F5.10.1:pep; SPAC1F5.10.
GeneIDi2541602.
KEGGispo:SPAC1F5.10.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA92238.1.
PIRiT38085.
RefSeqiNP_592863.1. NM_001018263.2.

3D structure databases

ProteinModelPortaliQ10055.
SMRiQ10055. Positions 22-394.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278099. 2 interactions.
MINTiMINT-4696561.

PTM databases

iPTMnetiQ10055.
SwissPalmiQ10055.

Proteomic databases

MaxQBiQ10055.
PRIDEiQ10055.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1F5.10.1; SPAC1F5.10.1:pep; SPAC1F5.10.
GeneIDi2541602.
KEGGispo:SPAC1F5.10.

Organism-specific databases

EuPathDBiFungiDB:SPAC1F5.10.
PomBaseiSPAC1F5.10.

Phylogenomic databases

HOGENOMiHOG000268797.
InParanoidiQ10055.
KOiK13025.
OMAiTATFCIS.
OrthoDBiEOG7FNCJ0.
PhylomeDBiQ10055.

Enzyme and pathway databases

ReactomeiR-SPO-429947. Deadenylation of mRNA.
R-SPO-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

PROiQ10055.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
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.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
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-67, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiFAL1_SCHPO
AccessioniPrimary (citable) accession number: Q10055
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 6, 2016
This is version 128 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.