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Protein

Helicase required for RNAi-mediated heterochromatin assembly 1

Gene

hrr1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has a role in the RNA interference (RNAi) pathway which is important for heterochromatin formation and accurate chromosome segregation. A member of the RNA-directed RNA polymerase complex (RDRC) which is involved in the generation of small interfering RNAs (siRNAs) and mediate their association with the RNA-induced transcriptional silencing (RITS) complex. RITS acts as a priming complex for dsRNA synthesis at the site of non-coding centromeric RNA.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi393 – 4008ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • chromatin remodeling Source: PomBase
  • chromatin silencing at centromere Source: PomBase
  • chromatin silencing by small RNA Source: PomBase
  • chromosome segregation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Cell cycle, Chromosome partition, RNA-mediated gene silencing

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Helicase required for RNAi-mediated heterochromatin assembly 1 (EC:3.6.4.13)
Gene namesi
Name:hrr1
ORF Names:SPCC1739.03
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC1739.03.
PomBaseiSPCC1739.03. hrr1.

Subcellular locationi

GO - Cellular componenti

  • chromosome, centromeric region Source: GOC
  • cytosol Source: PomBase
  • nuclear RNA-directed RNA polymerase complex Source: PomBase
  • nucleus Source: PomBase
  • RNA-directed RNA polymerase complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 999999Helicase required for RNAi-mediated heterochromatin assembly 1PRO_0000256155Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei94 – 941Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO74465.

PTM databases

iPTMnetiO74465.

Interactioni

Subunit structurei

Cid12, hrr1 and rdp1 interact forming the RNA-directed RNA polymerase complex (RDRC). The RDRC complex interacts with the RITS complex via interaction between ago1 and hrr1. Clr4 has a role in mediating this interaction.1 Publication

Protein-protein interaction databases

BioGridi275818. 288 interactions.
DIPiDIP-29303N.
MINTiMINT-4679301.

Family & Domainsi

Phylogenomic databases

InParanoidiO74465.
KOiK11701.
OMAiTVLTFYN.
OrthoDBiEOG7VX948.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027417. P-loop_NTPase.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.

Sequencei

Sequence statusi: Complete.

O74465-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQVQDEIWK LSTLDAWEMV NKNTEVVFDE IPEPETLSEM KRHPLYSNIF
60 70 80 90 100
NADNNTTSFT EQIETSETSK TQDSEGNKVD KNLKENKSIR RKRSIDNDYE
110 120 130 140 150
LSNVKRNDIT SGKNREFENE HHPASDTSSW RELPSIPTLE ELTSKSVELP
160 170 180 190 200
SNNIYGGYKS FEDYLSIHYR LLREDAVSPL RESVLRYKVN PNYITGSSLA
210 220 230 240 250
VYDHVRIDGY TISSSVIAAK LSFSVRAKKK IKWATSRRLI SGSLVLLSND
260 270 280 290 300
DFQTFRIGTV CARPLSGLNK HPHEIDVKFE DISISLDPRE EYVMIEATSG
310 320 330 340 350
YWEAYKHVLR SLQRLSASTF PMKDYLVHCK SNQETAKHIQ NNPRIRINSI
360 370 380 390 400
LKNNSQKIVN ALEPFGPGEY ILDSSQLKAY QSMLTKRLSI IQGPPGTGKS
410 420 430 440 450
FVTLKAIETL LENTHSHVLP ILVACQTNHA VDQILIRLLH QGASVMRLGS
460 470 480 490 500
RTKDPEIAAV TIFQKAKHTK HSFKAAYNEI RHKKQRLIKQ ITNIMHNFNL
510 520 530 540 550
EFVTLSYLHS KGIITTSQLE SLRNNTEWIS SVAENGEKTE EELISIWLGD
560 570 580 590 600
AKVELITPSE ITDGFEEELQ IDPEKLEEIQ KEAEDSGALM EEELRGKFIN
610 620 630 640 650
LRCKYLFSKL TTLHEKEIDT LLTIPNIWDI PEYSRGIIYC RWLESAYAAA
660 670 680 690 700
EKELNRLYRF YLKVDRERIG FSNKRAAILL RGANVIGMTT TGLNKYRDIL
710 720 730 740 750
ERINPKICFI EEAADVLEGP IIPAVFPSLE QLVLIGDHKQ LRPGCSTYAL
760 770 780 790 800
RQDPFNLSIS MFERLVENDM EYTRLTMQRR MHPQIRRLVS SVYEDLSDYE
810 820 830 840 850
ITKYWPSIPG MGEIRRFFLT HSRIEDNDGF ASKINLFEAQ MLVQFAVYLI
860 870 880 890 900
NNGVEPQKIT CLTFYAAQKD LIERLLSESL NREKHFIKVA TVDGYQGEEN
910 920 930 940 950
DVVLLSLVRN NDRTEVGFLS SPHRVCVSLS RARRGLFIFG NAQLVAESNP
960 970 980 990
LWWDAINTLM NDETIQGLGD HLPLFTKDGT IYVNDPVELL DVNMRLTRK
Length:999
Mass (Da):114,625
Last modified:July 11, 2012 - v2
Checksum:i8CBE21AF974D56CC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA20777.2.
PIRiT41111.
RefSeqiNP_588411.2. NM_001023402.2.

Genome annotation databases

EnsemblFungiiSPCC1739.03.1; SPCC1739.03.1:pep; SPCC1739.03.
GeneIDi2539248.
KEGGispo:SPCC1739.03.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA20777.2.
PIRiT41111.
RefSeqiNP_588411.2. NM_001023402.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275818. 288 interactions.
DIPiDIP-29303N.
MINTiMINT-4679301.

PTM databases

iPTMnetiO74465.

Proteomic databases

MaxQBiO74465.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC1739.03.1; SPCC1739.03.1:pep; SPCC1739.03.
GeneIDi2539248.
KEGGispo:SPCC1739.03.

Organism-specific databases

EuPathDBiFungiDB:SPCC1739.03.
PomBaseiSPCC1739.03. hrr1.

Phylogenomic databases

InParanoidiO74465.
KOiK11701.
OMAiTVLTFYN.
OrthoDBiEOG7VX948.

Miscellaneous databases

PROiO74465.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027417. P-loop_NTPase.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "Comparative functional genomics of the fission yeasts."
    Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.
    , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
    Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVISION OF GENE MODEL.
  3. "Two RNAi complexes, RITS and RDRC, physically interact and localize to noncoding centromeric RNAs."
    Motamedi M.R., Verdel A., Colmenares S.U., Gerber S.A., Gygi S.P., Moazed D.
    Cell 119:789-802(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COMPOSITION OF THE RDRC AND RITS COMPLEXES, INTERACTION WITH AGO1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  4. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiHRR1_SCHPO
AccessioniPrimary (citable) accession number: O74465
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: July 11, 2012
Last modified: July 6, 2016
This is version 94 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

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.