Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Nucleotide bindingi65 – 72ATPPROSITE-ProRule annotation8

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000549671 – 394ATP-dependent RNA helicase fal1Add BLAST394

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei67Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ10055.
PRIDEiQ10055.

PTM databases

iPTMnetiQ10055.
SwissPalmiQ10055.

Interactioni

Protein-protein interaction databases

BioGridi278099. 2 interactors.
MINTiMINT-4696561.

Structurei

3D structure databases

ProteinModelPortaliQ10055.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini52 – 222Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST171
Domaini233 – 394Helicase C-terminalPROSITE-ProRule annotationAdd BLAST162

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi21 – 49Q motifAdd BLAST29
Motifi170 – 173DEAD box4

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.
OrthoDBiEOG092C2B1L.
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278099. 2 interactors.
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.
OrthoDBiEOG092C2B1L.
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...

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: November 30, 2016
This is version 131 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.