YN8E_SCHPO
ID YN8E_SCHPO Reviewed; 1065 AA.
AC Q9P789;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 2.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Pumilio domain-containing protein P35G2.14;
GN ORFNames=SPBP35G2.14;
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 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-260; SER-506; SER-511;
RP SER-515 AND THR-554, 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329671; CAB87376.2; -; Genomic_DNA.
DR RefSeq; NP_595389.2; NM_001021296.2.
DR AlphaFoldDB; Q9P789; -.
DR SMR; Q9P789; -.
DR BioGRID; 277835; 68.
DR STRING; 4896.SPBP35G2.14.1; -.
DR iPTMnet; Q9P789; -.
DR MaxQB; Q9P789; -.
DR PaxDb; Q9P789; -.
DR PRIDE; Q9P789; -.
DR EnsemblFungi; SPBP35G2.14.1; SPBP35G2.14.1:pep; SPBP35G2.14.
DR GeneID; 2541323; -.
DR KEGG; spo:SPBP35G2.14; -.
DR PomBase; SPBP35G2.14; -.
DR VEuPathDB; FungiDB:SPBP35G2.14; -.
DR eggNOG; KOG4574; Eukaryota.
DR HOGENOM; CLU_290869_0_0_1; -.
DR InParanoid; Q9P789; -.
DR OMA; IVRVCTH; -.
DR PRO; PR:Q9P789; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0010494; C:cytoplasmic stress granule; EXP:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000932; C:P-body; EXP:PomBase.
DR GO; GO:0003729; F:mRNA binding; ISO:PomBase.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISO:PomBase.
DR GO; GO:0034063; P:stress granule assembly; IMP:PomBase.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR033133; PUM-HD.
DR InterPro; IPR001313; Pumilio_RNA-bd_rpt.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00806; PUF; 4.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00025; Pumilio; 5.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50302; PUM; 6.
DR PROSITE; PS50303; PUM_HD; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..1065
FT /note="Pumilio domain-containing protein P35G2.14"
FT /id="PRO_0000310366"
FT DOMAIN 592..666
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 712..1065
FT /note="PUM-HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00318"
FT REPEAT 771..808
FT /note="Pumilio 1"
FT REPEAT 809..844
FT /note="Pumilio 2"
FT REPEAT 846..884
FT /note="Pumilio 3"
FT REPEAT 886..917
FT /note="Pumilio 4"
FT REPEAT 919..954
FT /note="Pumilio 5"
FT REPEAT 956..993
FT /note="Pumilio 6"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 260
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 554
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1065 AA; 114230 MW; 046038A978EE99BE CRC64;
MHQDAMQGSI YEGSRRNTIS KPSNNNPPLD MSSLNNDFGQ QLDSLATGVG SGSLNGTTNP
SSNFNDSNRS NISSSLRSEM EMSNNLLKNT QNDTWTSTVG LSVPENQEAM NFNEGPTGIS
SIASKNNSSI TSKLQNNSNL SVTSSANRGR TSSVSSSYDP SFPWGPRMSS VSSGKQHLSS
LSLHTHFNPS SSSTVSSDSL ESSQQKAPSS SSTATPASAA SEIISNKDPV VEPTHSASNA
ANSGSNTIRA RQTTRTRSNT LPWSPRVFGP TLGYNTPPFG YPPTTSSALP NASGSSSSFF
GLPTAVSASA GTSFSDISPA APKASLENNI ASNASSLLNP VGLDHFSAAS GWSRDFNHLP
ASSLATARSS LTGNAKSGID SSVTGMPSDN YARVVESSTA EFFDPSLASS FGLTNYRTKP
LTTGFNHPRP QGHGLNTSLF NTSSGGSLKS PTFEVSNRLG DVDTVPDLPP LGSLSSRPKP
SSSSRRRSQS LSAMLKTSNP YMPSPSLLSG SLANSSEHSS SPRLRGSPIH NQPVSSSKST
ASLNTNNNGL RASTPEMANI STRSSSESNN TNSWPTVGDA TIENLTQHEP THALWVGNLP
SGVSATTVAT TFSAYGTVSS IRMLSHKHSA FLNFDSVETA KHVLEELNGK RIFFGSDPVC
ISFAKVASSS SESSHSAVDG LNKAFSNVSF VPSLREVYDD LINVVQSFGF KDLSKIYQIL
NAACELTDFA AQIPSISKAF SSRRLNAPKL RQVRKRIDNG LCTQEEVEDI AINWLDEVSD
LSSDHLGNTV VQKLFDYCSD PVKEMMLERI APHLAQIGIH KNGTWAAQKI VDVASTEAQM
RLIAKHLQPY IPLLFADQFG NYVVQTCLKF GAPMNDFVFE AILNQFWVIA QSRYGSRAVR
ACLESPDVTE EQRVLVAAAI TVYSVHLAMN GNGTLLLTYL VENMNYPHIP ILLTRRFVQD
IVRVCTHRLA YNSLLKIISI SQGDTACGDL VVDAILDTQN DLNPNSLEKI LFEQTYGPSF
ICKLLTHENI SASHRQQLQS AVRNVLGTME DRGSSELKKL AEVCA
