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Protein

Pre-mRNA-splicing factor ATP-dependent RNA helicase-like protein cdc28

Gene

cdc28

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Involved in pre-mRNA splicing. Is required together with ATP and at least one other factor, for the first cleavage-ligation reaction. Functions as a molecular motor in the activation of the precatalytic spliceosome for the first transesterification reaction of pre-mRNA splicing by hydrolyzing ATP to cause the activation of the spliceosome without the occurrence of splicing (By similarity).By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi441 – 4488ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent RNA helicase activity Source: PomBase
  3. poly(A) RNA binding Source: GO_Central

GO - Biological processi

  1. mRNA 3'-splice site recognition Source: PomBase
  2. mRNA splicing, via spliceosome Source: GO_Central
  3. spliceosomal tri-snRNP complex assembly Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA-splicing factor ATP-dependent RNA helicase-like protein cdc28 (EC:3.6.4.13)
Alternative name(s):
Pre-mRNA-processing protein 8
Gene namesi
Name:cdc28
Synonyms:prp8
ORF Names:SPBC19C2.01, SPBC21B10.01c, SPBC874.01
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

PomBaseiSPBC19C2.01.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: GO_Central
  2. spliceosomal complex Source: GO_Central
  3. U4/U6 x U5 tri-snRNP complex Source: PomBase
  4. U5 snRNP Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Cells show pre-mRNA splicing defects. Cdc28-P8 temperature-sensitive mutant causes cell-cycle arrest in G2 and exhibits a splicing defect that leads to accumulation of unspliced precursors at the restrictive temperature. Temperature-sensitive pre-mRNA splicing mutant Prp8-1 exhibits a cell-cycle phenotype identical to cdc28-p8. Prp8-1 mutant produces elongated cells, accumulates U6 snRNA precursor and has defects in an early step of TFIID pre-mRNA splicing at the nonpermissive temperature.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10551055Pre-mRNA-splicing factor ATP-dependent RNA helicase-like protein cdc28PRO_0000055154Add
BLAST

Proteomic databases

MaxQBiQ10752.

Interactioni

Protein-protein interaction databases

BioGridi277230. 11 interactions.
STRINGi4896.SPBC19C2.01-1.

Structurei

3D structure databases

ProteinModelPortaliQ10752.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini428 – 592165Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini617 – 790174Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi539 – 5424DEAH box

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1643.
HOGENOMiHOG000175261.
InParanoidiQ10752.
KOiK12813.
OMAiGYFYHIA.
OrthoDBiEOG7M98QW.
PhylomeDBiQ10752.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR011709. DUF1605.
IPR007502. Helicase-assoc_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q10752-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLEQYVSDK AISLLGMSEP SVVEYLIAEA KGSSSSNNLY QKLVSFGMDG
60 70 80 90 100
DDPAVKEFAH TLYARIPREG SRPKENYNAR KKKEQGILQM ERLNSSYDLL
110 120 130 140 150
IEPQSHETPG KPLKKKSRSK TPKREIARRQ RDEDEWESDE YEEVVDGSAS
160 170 180 190 200
HPIEEDSVST DFQNHDYEKS SDPETERLND LREREEFEER LRRKDLEAAT
210 220 230 240 250
NEFVEDYSSK FSSEELALRK LADDPESWRK LASELRKKSR QQYLKPRAQQ
260 270 280 290 300
QLEILRREIR DEEQLFAGEK LTQAEIRELE KKKELLRIAE ERQRLEKQAT
310 320 330 340 350
EYQMPEDYFT EQGKLDRKRK EEVLYQRYKD SNEGEQNEVT MGAAEQQRWE
360 370 380 390 400
AQQINKALLF DQNEWLPPGE KQFDFVFDES QQIDFLLDTK LSAENPVDTD
410 420 430 440 450
KMTDVKVEKS LESSRKSLPV YQYKDDLLKA INEYQVLLIV AETGSGKTTQ
460 470 480 490 500
LPQFLHEAGY TKGNKKICCT QPRRVAAMSV AARVAKEMDV RLGQEVGYSI
510 520 530 540 550
RFENATSEKT VIKYLTDGML LREFLTEPDL ASYSVIIIDE AHERTLHTDI
560 570 580 590 600
LFGLVKDIAR FRPDLKVLIS SATIDAEKFS AYFDEAPVFY VPGRRYPVDI
610 620 630 640 650
YYTPQPEANY IQAAITTILQ IHTTQPAGDI LVFLTGQDEI ELMSENMQEL
660 670 680 690 700
CRILGKRIPE IILCPIYANL PSELQAKIFD PTPPGARKVV LATNIAETSI
710 720 730 740 750
TIDGVNFVID SGFVKQNMYN PRTGMESLVS VPCSRASADQ RAGRAGRVGP
760 770 780 790 800
GKCFRLYTRR TYNNELDMVT SPEIQRTNLT NIVLLLKSLG INNLLDFDFM
810 820 830 840 850
DAPPPETLMR SLELLYALGA LNNRGELTKL GRQMAEFPTD PMLSKSLIAS
860 870 880 890 900
SKYGCVEEVL SIVSMLGEAS SLFYRPKDKI MEADKARANF TQPGGDHLTL
910 920 930 940 950
LHIWNEWVDT DFSYNWAREN FLQYKSLCRA RDVRDQLANL CERVEIELVT
960 970 980 990 1000
NSSESLDPIK KAITAGYFSN AARLDRSGDS YRTVKSNQTV YIHPSSSVAE
1010 1020 1030 1040 1050
KKPKVIIYFE LVLTTKEYCR QITEIQPEWL LEISPHYFKP ENIEELQKTQ

KRHKR
Length:1,055
Mass (Da):121,217
Last modified:August 28, 2001 - v2
Checksum:i223694BD85404DCC
GO

Sequence cautioni

The sequence AAC49377.1 differs from that shown. Reason: Frameshift at positions 80 and 1012. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti760 – 7601R → W in AAC49377 (PubMed:8862522).Curated
Sequence conflicti969 – 9691S → P in AAC49377 (PubMed:8862522).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48733 Genomic DNA. Translation: AAC49377.1. Frameshift.
CU329671 Genomic DNA. Translation: CAB57929.2.
PIRiT46568.
T50372.
RefSeqiNP_595686.2. NM_001021581.3.

Genome annotation databases

EnsemblFungiiSPBC19C2.01.1; SPBC19C2.01.1:pep; SPBC19C2.01.
GeneIDi2540707.
KEGGispo:SPBC19C2.01.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48733 Genomic DNA. Translation: AAC49377.1. Frameshift.
CU329671 Genomic DNA. Translation: CAB57929.2.
PIRiT46568.
T50372.
RefSeqiNP_595686.2. NM_001021581.3.

3D structure databases

ProteinModelPortaliQ10752.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277230. 11 interactions.
STRINGi4896.SPBC19C2.01-1.

Proteomic databases

MaxQBiQ10752.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC19C2.01.1; SPBC19C2.01.1:pep; SPBC19C2.01.
GeneIDi2540707.
KEGGispo:SPBC19C2.01.

Organism-specific databases

PomBaseiSPBC19C2.01.

Phylogenomic databases

eggNOGiCOG1643.
HOGENOMiHOG000175261.
InParanoidiQ10752.
KOiK12813.
OMAiGYFYHIA.
OrthoDBiEOG7M98QW.
PhylomeDBiQ10752.

Miscellaneous databases

NextBioi20801829.
PROiQ10752.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR011709. DUF1605.
IPR007502. Helicase-assoc_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A connection between pre-mRNA splicing and the cell cycle in fission yeast: cdc28+ is allelic with prp8+ and encodes an RNA-dependent ATPase/helicase."
    Lundgren K., Allan S., Urushiyama S., Tani T., Ohshima Y., Frendewey D., Beach D.
    Mol. Biol. Cell 7:1083-1094(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE.
  2. "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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Isolation of novel pre-mRNA splicing mutants of Schizosaccharomyces pombe."
    Urushiyama S., Tani T., Ohshima Y.
    Mol. Gen. Genet. 253:118-127(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiCDC28_SCHPO
AccessioniPrimary (citable) accession number: Q10752
Secondary accession number(s): Q9URU1, Q9USV9, Q9UUD7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 14, 1998
Last sequence update: August 28, 2001
Last modified: March 31, 2015
This is version 122 of the entry and version 2 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

External Data

Dasty 3

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 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.