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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)DescriptionActionsGraphical viewLength
Nucleotide bindingi166 – 173ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHelicase, Hydrolase, RNA-binding
Biological processRibosome biogenesis, rRNA processing
LigandATP-binding, Nucleotide-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. mak5.

Subcellular locationi

GO - Cellular componenti

  • nucleolus Source: PomBase
  • nucleus Source: PomBase

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002322391 – 648ATP-dependent RNA helicase mak5Add BLAST648

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei85Phosphoserine1 Publication1
Modified residuei566Phosphoserine1 Publication1
Modified residuei567Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO74393.
PRIDEiO74393.

PTM databases

iPTMnetiO74393.

Interactioni

Protein-protein interaction databases

BioGridi277391. 1 interactor.
MINTiMINT-4678705.

Structurei

3D structure databases

ProteinModelPortaliO74393.
SMRiO74393.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini153 – 331Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST179
Domaini378 – 523Helicase C-terminalPROSITE-ProRule annotationAdd BLAST146

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi122 – 150Q motifAdd BLAST29
Motifi275 – 278DEAD box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi59 – 82Lys-richAdd BLAST24

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

Phylogenomic databases

HOGENOMiHOG000290702.
InParanoidiO74393.
KOiK14805.
OMAiIECGAME.
OrthoDBiEOG092C1I7Y.
PhylomeDBiO74393.

Family and domain databases

InterProiView protein in InterPro
IPR011545. 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.
PfamiView protein in Pfam
PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
SMARTiView protein in SMART
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiView protein in PROSITE
PS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.

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.
SMRiO74393.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277391. 1 interactor.
MINTiMINT-4678705.

PTM databases

iPTMnetiO74393.

Proteomic databases

MaxQBiO74393.
PRIDEiO74393.

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. mak5.

Phylogenomic databases

HOGENOMiHOG000290702.
InParanoidiO74393.
KOiK14805.
OMAiIECGAME.
OrthoDBiEOG092C1I7Y.
PhylomeDBiO74393.

Miscellaneous databases

PROiPR:O74393.

Family and domain databases

InterProiView protein in InterPro
IPR011545. 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.
PfamiView protein in Pfam
PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
SMARTiView protein in SMART
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiView protein in PROSITE
PS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMAK5_SCHPO
AccessioniPrimary (citable) accession number: O74393
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 1, 1998
Last modified: April 12, 2017
This is version 115 of the entry and version 1 of the sequence. See 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.