HRR1_SCHPO
ID HRR1_SCHPO Reviewed; 999 AA.
AC O74465;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Helicase required for RNAi-mediated heterochromatin assembly 1;
DE EC=3.6.4.13;
GN Name=hrr1; ORFNames=SPCC1739.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP FUNCTION, COMPOSITION OF THE RDRC AND RITS COMPLEXES, INTERACTION WITH
RP AGO1, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15607976; DOI=10.1016/j.cell.2004.11.034;
RA Motamedi M.R., Verdel A., Colmenares S.U., Gerber S.A., Gygi S.P.,
RA Moazed D.;
RT "Two RNAi complexes, RITS and RDRC, physically interact and localize to
RT noncoding centromeric RNAs.";
RL Cell 119:789-802(2004).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Has a role in the RNA interference (RNAi) pathway which is
CC important for heterochromatin formation and accurate chromosome
CC segregation. A member of the RNA-directed RNA polymerase complex (RDRC)
CC which is involved in the generation of small interfering RNAs (siRNAs)
CC and mediate their association with the RNA-induced transcriptional
CC silencing (RITS) complex. RITS acts as a priming complex for dsRNA
CC synthesis at the site of non-coding centromeric RNA.
CC {ECO:0000269|PubMed:15607976}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- SUBUNIT: Cid12, hrr1 and rdp1 interact forming the RNA-directed RNA
CC polymerase complex (RDRC). The RDRC complex interacts with the RITS
CC complex via interaction between ago1 and hrr1. Clr4 has a role in
CC mediating this interaction. {ECO:0000269|PubMed:15607976}.
CC -!- INTERACTION:
CC O74465; O94717: ers1; NbExp=4; IntAct=EBI-15624169, EBI-15977565;
CC O74465; O94687: tas3; NbExp=2; IntAct=EBI-15624169, EBI-423002;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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DR EMBL; CU329672; CAA20777.2; -; Genomic_DNA.
DR PIR; T41111; T41111.
DR RefSeq; NP_588411.2; NM_001023402.2.
DR AlphaFoldDB; O74465; -.
DR BioGRID; 275818; 288.
DR DIP; DIP-29303N; -.
DR IntAct; O74465; 3.
DR STRING; 4896.SPCC1739.03.1; -.
DR iPTMnet; O74465; -.
DR MaxQB; O74465; -.
DR PaxDb; O74465; -.
DR PRIDE; O74465; -.
DR EnsemblFungi; SPCC1739.03.1; SPCC1739.03.1:pep; SPCC1739.03.
DR GeneID; 2539248; -.
DR KEGG; spo:SPCC1739.03; -.
DR PomBase; SPCC1739.03; hrr1.
DR VEuPathDB; FungiDB:SPCC1739.03; -.
DR eggNOG; KOG1807; Eukaryota.
DR HOGENOM; CLU_001066_2_0_1; -.
DR InParanoid; O74465; -.
DR OMA; IGKWERD; -.
DR PRO; PR:O74465; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0031380; C:nuclear RNA-directed RNA polymerase complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0031379; C:RNA-directed RNA polymerase complex; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; IMP:PomBase.
DR GO; GO:0031508; P:pericentric heterochromatin assembly; IMP:PomBase.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10887; PTHR10887; 1.
DR Pfam; PF13086; AAA_11; 2.
DR Pfam; PF13087; AAA_12; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Chromosome partition; Cytoplasm; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; RNA-mediated gene silencing.
FT CHAIN 1..999
FT /note="Helicase required for RNAi-mediated heterochromatin
FT assembly 1"
FT /id="PRO_0000256155"
FT REGION 61..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 393..400
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 999 AA; 114625 MW; 8CBE21AF974D56CC CRC64;
MEQVQDEIWK LSTLDAWEMV NKNTEVVFDE IPEPETLSEM KRHPLYSNIF NADNNTTSFT
EQIETSETSK TQDSEGNKVD KNLKENKSIR RKRSIDNDYE LSNVKRNDIT SGKNREFENE
HHPASDTSSW RELPSIPTLE ELTSKSVELP SNNIYGGYKS FEDYLSIHYR LLREDAVSPL
RESVLRYKVN PNYITGSSLA VYDHVRIDGY TISSSVIAAK LSFSVRAKKK IKWATSRRLI
SGSLVLLSND DFQTFRIGTV CARPLSGLNK HPHEIDVKFE DISISLDPRE EYVMIEATSG
YWEAYKHVLR SLQRLSASTF PMKDYLVHCK SNQETAKHIQ NNPRIRINSI LKNNSQKIVN
ALEPFGPGEY ILDSSQLKAY QSMLTKRLSI IQGPPGTGKS FVTLKAIETL LENTHSHVLP
ILVACQTNHA VDQILIRLLH QGASVMRLGS RTKDPEIAAV TIFQKAKHTK HSFKAAYNEI
RHKKQRLIKQ ITNIMHNFNL EFVTLSYLHS KGIITTSQLE SLRNNTEWIS SVAENGEKTE
EELISIWLGD AKVELITPSE ITDGFEEELQ IDPEKLEEIQ KEAEDSGALM EEELRGKFIN
LRCKYLFSKL TTLHEKEIDT LLTIPNIWDI PEYSRGIIYC RWLESAYAAA EKELNRLYRF
YLKVDRERIG FSNKRAAILL RGANVIGMTT TGLNKYRDIL ERINPKICFI EEAADVLEGP
IIPAVFPSLE QLVLIGDHKQ LRPGCSTYAL RQDPFNLSIS MFERLVENDM EYTRLTMQRR
MHPQIRRLVS SVYEDLSDYE ITKYWPSIPG MGEIRRFFLT HSRIEDNDGF ASKINLFEAQ
MLVQFAVYLI NNGVEPQKIT CLTFYAAQKD LIERLLSESL NREKHFIKVA TVDGYQGEEN
DVVLLSLVRN NDRTEVGFLS SPHRVCVSLS RARRGLFIFG NAQLVAESNP LWWDAINTLM
NDETIQGLGD HLPLFTKDGT IYVNDPVELL DVNMRLTRK
