RRP5_SCHPO
ID RRP5_SCHPO Reviewed; 1690 AA.
AC O74835;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=rRNA biogenesis protein rrp5;
DE AltName: Full=Ribosomal RNA-processing protein 5;
DE AltName: Full=U3 small nucleolar RNA-associated protein rrp5;
DE Short=U3 snoRNA-associated protein rrp5;
GN Name=rrp5 {ECO:0000250|UniProtKB:Q05022}; ORFNames=SPCC1183.07;
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] {ECO:0000312|EMBL:CAA21087.1}
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] {ECO:0000305}
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1391; SER-1394; SER-1684 AND
RP SER-1686, AND IDENTIFICATION BY 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: Involved in the biogenesis of rRNA. Required for the
CC formation of 18S and 5.8S rRNA (By similarity).
CC {ECO:0000250|UniProtKB:Q05022}.
CC -!- SUBUNIT: Component of the ribosomal small subunit (SSU) processome.
CC {ECO:0000250|UniProtKB:Q05022}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329672; CAA21087.1; -; Genomic_DNA.
DR PIR; T40847; T40847.
DR RefSeq; NP_587890.1; NM_001022882.2.
DR AlphaFoldDB; O74835; -.
DR SMR; O74835; -.
DR BioGRID; 275475; 14.
DR IntAct; O74835; 1.
DR STRING; 4896.SPCC1183.07.1; -.
DR iPTMnet; O74835; -.
DR MaxQB; O74835; -.
DR PaxDb; O74835; -.
DR PRIDE; O74835; -.
DR EnsemblFungi; SPCC1183.07.1; SPCC1183.07.1:pep; SPCC1183.07.
DR GeneID; 2538897; -.
DR KEGG; spo:SPCC1183.07; -.
DR PomBase; SPCC1183.07; rrp5.
DR VEuPathDB; FungiDB:SPCC1183.07; -.
DR eggNOG; KOG1070; Eukaryota.
DR HOGENOM; CLU_000845_0_0_1; -.
DR InParanoid; O74835; -.
DR OMA; GQYLRAY; -.
DR PhylomeDB; O74835; -.
DR Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:O74835; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0032040; C:small-subunit processome; ISO:PomBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0042134; F:rRNA primary transcript binding; ISO:PomBase.
DR GO; GO:0030515; F:snoRNA binding; ISO:PomBase.
DR GO; GO:0006364; P:rRNA processing; ISO:PomBase.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 2.40.50.140; -; 11.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR045209; Rrp5.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR008847; Suf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR23270; PTHR23270; 3.
DR Pfam; PF00575; S1; 4.
DR Pfam; PF05843; Suf; 1.
DR SMART; SM00386; HAT; 6.
DR SMART; SM00316; S1; 13.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF50249; SSF50249; 12.
DR PROSITE; PS50126; S1; 12.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
KW Ribosome biogenesis; rRNA processing.
FT CHAIN 1..1690
FT /note="rRNA biogenesis protein rrp5"
FT /id="PRO_0000314629"
FT DOMAIN 109..209
FT /note="S1 motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 226..289
FT /note="S1 motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 306..376
FT /note="S1 motif 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 398..473
FT /note="S1 motif 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 490..559
FT /note="S1 motif 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 579..648
FT /note="S1 motif 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 666..739
FT /note="S1 motif 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 761..830
FT /note="S1 motif 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 866..942
FT /note="S1 motif 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 973..1044
FT /note="S1 motif 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 1053..1122
FT /note="S1 motif 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 1147..1216
FT /note="S1 motif 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 1236..1307
FT /note="S1 motif 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT REPEAT 1420..1452
FT /note="HAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 1526..1558
FT /note="HAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 1596..1628
FT /note="HAT 3"
FT /evidence="ECO:0000255"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1313..1424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1317..1331
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1369
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1391
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1394
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1684
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1686
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1690 AA; 187524 MW; 42629B8347DACCD6 CRC64;
MAGNKRKRSN ASEGSDSQGN ERISSLSANE ATQDFPRGGA SSLTPLEYKE AVLEAKKDFM
ESASGTAELS KKTRPKKKGS KKSSKSELDN EENLKVHIQS LRYKNITPGS LILGQIAQIN
TLDLAVSLPN CLTGYVPITN ISDKLSDRLD SIDNHAEDNA ATEEEDGLNQ IPDLMDLYKV
GQWVRVSVTA LGSENTTKTG KRHIELSLKP QDANGSAPEA ADFVAGSMIQ AVVSSIEDHG
IVFDIGINNY TGFLSKKHIN DFPFVEGQSL LCSVISKEDR IFHLSLTATS TKALEVMPSV
QAILPGDYIN VLVTDIKESG VIAKYMGVVD VTSDIYHSSP VKGEDLEDKF QLAKSVPARV
LFVIPGDPPK IAVSFLPHVL TFNFATPNTP HPDQLDIGFI VNAAKVTYVS SSLGVFCDVG
VPEISGFAHI SRLSDKKVAG ISPNSGPYKV DSTHEARIIN YSYVDNLYIL SFQQSVLNQQ
FLRIEDIEVG QFVDGTIAKL IPQGIVVTIS EGINGLVPST HMADIALQFP ERRFKVGSSV
KCRVLSTNVL RKRVLLTLKK SLLNTDLPLI YDYEQATPGT QTVGTLARIF EDGAIVEFYN
SVRAFLPVSE MSEAYIRDAR EHFKVGQTLS VTIVSCDPEN RKMRVGCREQ SWDAKRLERF
ENIKAGSVLS GIVLQKTEDS VIVDLGDKVT GVITLGQLCD GDLNKCSKVM NKLRASTKLA
EVLVLRKDTS KKLISLSLKK SLVEAAKENR MPINITDLKE GIKYFGFVRN ATTFGVFVEF
CDGLVALVPK AYISEEYVPV PSAVYKPQQS VTCVCLSVEL SQEKAFMSFK PLAQKQEKAV
EFMESKYDID NPVDETIKKT YDYVAGKITW AVVTSAKASQ LNVDLAANVH GRVDVSEVFD
NFGEIVDPNK PLKRFHKGDK IRVRVLGIHD SRNHKFLPIS HRVSPKQFLE LSVRPSILNM
EPFSMKEPQF KKGDEVTGFV NNVSKECVWV SLTPSVNGRI PILDLTTDVK ELNSLQKHFF
LGKAIKCYVV NAEDSITLSA IGPLQGFENL TPGSRLVGKV TNVNEAGAIL QLPGHMSGRV
SRIDMFDDYD ILPETKFTRN NLVGVCVLSV DVPNRKVALS ARNSRTQSQP VEIKDKEINS
VDDLKIGDIC RGFVCNVANQ GLFVTIGHNL IARVKIGELF DTFIKDWKPH FHVNQLVKGS
IVGIDNDSKR IEMSLKQSKI KDSSEITKTF ADIAVGSNLD GTVVKVGDYG VLIRIDGTDN
IVGLCHKSEI ADAVVLNISK LYSSGDKVRA HVLDVDSEKR RIALGLKSSY FDSDSDISMS
DNEEDVEMRS EDQSDTSESE VGSKDDVQSE EVENLESAGD EDEEEEPSAL QANGFDWTDG
STVFDKLADD TEDSEDEEDE EPKRKKSKSD RFDDEEKDLD EIPSTAADFE RQLLSSPNSS
LLWISYMAYH LNLNELQEAR EVGKRALSTI NYREEDEKLN VWMALLNLEV AYGTEDSLKE
VFKEACAYCD ALIVYEKLCG ILIKGGKVDL ADEYMQLMLK NFKQVPSVWI QYATFLLNND
KAEKAHGLLE RSLQSLPKSE HVGIIEKFAI LEFKNGDPER GRTIFEGLLS SYPKRLDLWN
VLIDMEMKQD DPSIVRRLFQ RLLALNLSTK KAKFAFKKWL AYEKNIGDDE GAEQVKRRAI
EYVSESHSEN