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Protein

ATP-dependent RNA helicase mak5

Gene

mak5

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-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi166 – 1738ATPPROSITE-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 mak5 (EC:3.6.4.13)
Gene namesi
Name:mak5
ORF Names:SPBC4F6.07c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC4F6.07c.
PomBaseiSPBC4F6.07c.

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 – 648648ATP-dependent RNA helicase mak5PRO_0000232239Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei85 – 851Phosphoserine1 Publication
Modified residuei566 – 5661Phosphoserine1 Publication
Modified residuei567 – 5671Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO74393.

PTM databases

iPTMnetiO74393.

Interactioni

Protein-protein interaction databases

BioGridi277391. 1 interaction.
MINTiMINT-4678705.

Structurei

3D structure databases

ProteinModelPortaliO74393.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini153 – 331179Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini378 – 523146Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi122 – 15029Q motifAdd
BLAST
Motifi275 – 2784DEAD box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi59 – 8224Lys-richAdd
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

HOGENOMiHOG000290702.
InParanoidiO74393.
KOiK14805.
OMAiIECGAME.
OrthoDBiEOG7NW6JS.
PhylomeDBiO74393.

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. 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.

O74393-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKKAALDEL KWKEVKLPDH LDDFDGFMGL EEIEGVDIKY QPKGAMKEVI
60 70 80 90 100
YELPEVHEKK DKKPEKRKKD QKEASEKKKK GKRTSPTIEM TSLGSKVTSK
110 120 130 140 150
NYNEFSTLEE EDEHNSHGVD VSAWAHFSLS PEMLGSLSKA GFSKPMPIQS
160 170 180 190 200
LVIPEASIGF DIIGKADTGS GKTLAFGIPI LEHCLRNVDA KYVQALVVAP
210 220 230 240 250
TRELAHQICQ HFELIKPSPN IRVMSITGGL AVQKQQRLLN KHPHVVVATP
260 270 280 290 300
GRLWSVINEN NLTGNFKKIK CLVLDEADRL LQKSHFEELS KLLEILGNPM
310 320 330 340 350
HTQRQTFIFS ATFDEGLQQR LKKNMKGNIT EKYNSPMENM LKEVRFFGKP
360 370 380 390 400
KFLDANPQSA VASRVLEGLI ECAPAEKDLY LYYLIMRYPG KTMVFANGIE
410 420 430 440 450
DIKRITPFLN ELKVPSYPLH AQLDQKKRLQ SLEKFKNNPK GVLVCTDVAA
460 470 480 490 500
RGIDIPSVTH VIHYHVPHTA DMYVHRSGRT ARANEDGVSI LMCGPKELSQ
510 520 530 540 550
LKRLCYRLKK KIETFINFPV DMSILDILKT RVVLAHKIVN LTRKDGRVGR
560 570 580 590 600
EEAWLKSMAQ ELGVESSDDE DPDLPKKSES SKNKKQIAHL RSELAPLLHE
610 620 630 640
KIRTGFSGRY LTSGLVNMAE KLANEEVHDN IIGMDSISAL EVLQKRKK
Length:648
Mass (Da):73,250
Last modified:November 1, 1998 - v1
Checksum:i07CA3668698B426A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA20727.1.
PIRiT40504.
RefSeqiNP_596107.1. NM_001022024.2.

Genome annotation databases

EnsemblFungiiSPBC4F6.07c.1; SPBC4F6.07c.1:pep; SPBC4F6.07c.
GeneIDi2540874.
KEGGispo:SPBC4F6.07c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA20727.1.
PIRiT40504.
RefSeqiNP_596107.1. NM_001022024.2.

3D structure databases

ProteinModelPortaliO74393.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277391. 1 interaction.
MINTiMINT-4678705.

PTM databases

iPTMnetiO74393.

Proteomic databases

MaxQBiO74393.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC4F6.07c.1; SPBC4F6.07c.1:pep; SPBC4F6.07c.
GeneIDi2540874.
KEGGispo:SPBC4F6.07c.

Organism-specific databases

EuPathDBiFungiDB:SPBC4F6.07c.
PomBaseiSPBC4F6.07c.

Phylogenomic databases

HOGENOMiHOG000290702.
InParanoidiO74393.
KOiK14805.
OMAiIECGAME.
OrthoDBiEOG7NW6JS.
PhylomeDBiO74393.

Miscellaneous databases

PROiO74393.

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. 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-85; SER-566 AND SER-567, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiMAK5_SCHPO
AccessioniPrimary (citable) accession number: O74393
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 1, 1998
Last modified: June 8, 2016
This is version 109 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.