RSD1_SCHPO
ID RSD1_SCHPO Reviewed; 603 AA.
AC O13845;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=RNA-binding protein rsd1;
GN Name=rsd1; ORFNames=SPAC19G12.07c;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-174 AND SER-465, AND
RP 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).
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DR EMBL; CU329670; CAB10118.2; -; Genomic_DNA.
DR PIR; T37994; T37994.
DR RefSeq; NP_594422.2; NM_001019851.2.
DR AlphaFoldDB; O13845; -.
DR SMR; O13845; -.
DR BioGRID; 279002; 13.
DR STRING; 4896.SPAC19G12.07c.1; -.
DR iPTMnet; O13845; -.
DR MaxQB; O13845; -.
DR PaxDb; O13845; -.
DR PRIDE; O13845; -.
DR EnsemblFungi; SPAC19G12.07c.1; SPAC19G12.07c.1:pep; SPAC19G12.07c.
DR GeneID; 2542545; -.
DR KEGG; spo:SPAC19G12.07c; -.
DR PomBase; SPAC19G12.07c; rsd1.
DR VEuPathDB; FungiDB:SPAC19G12.07c; -.
DR eggNOG; KOG0147; Eukaryota.
DR HOGENOM; CLU_020551_4_1_1; -.
DR InParanoid; O13845; -.
DR OMA; GRDNDKG; -.
DR PRO; PR:O13845; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005681; C:spliceosomal complex; ISS:PomBase.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:1990446; F:U1 snRNP binding; IDA:PomBase.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISS:PomBase.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR029123; RBM39_linker.
DR InterPro; IPR006509; RBM39_SF.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF15519; RBM39linker; 1.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR SMART; SM00361; RRM_1; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR TIGRFAMs; TIGR01622; SF-CC1; 1.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..603
FT /note="RNA-binding protein rsd1"
FT /id="PRO_0000081876"
FT DOMAIN 240..317
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 340..417
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 506..590
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 603 AA; 69362 MW; 10094A172F1956F2 CRC64;
MQLDAEALAE APFRKQEVPQ NQENQQKASS SFHESSLTSS THSHPSNPPP PPTRLHDRSF
KPVSKNYESE GRLTPPPVSM GYRYARSSKQ SFQREDSGYN DDVVTNSSSH RTPRHHRRSY
SPRSDYGSRS PSPHSSVDSH QSRSPVRSRD RDRSSRSSRS RHPSSRSRHR YDDYSRSPPY
SSRHSRSRRR YEERSSRSSR AHDYDYEDLR DDDRSHERKR SRSRPRERSS KLSEEERDRR
TVFVSQLANR LTSRELYDFF EQAGPVRDAQ IVRDKISGRS KGVAYVEFCH EDSVQAAIAL
SGKRLLGLPV IVQLTEAEKN RKAREAAELA RAASAEIPFH RLCVSNIHFN LTDEDVKAIF
EPFGDIEFVH LQRDDQNRSK GFGYIQYRNP ISARNALEKM NGFDLAGRNM RVCLGNDKFT
TETTSSMLKR FDETLARQER SQPSQRNGGS STYESQDYRE AAPLSPTEEE SRPITRDELM
KKLARSEDIS DNSKLVSEPE PPIRSRCALL ENMFNPAEET SPNWVQELEQ DVKEECDEKY
GKVVHIAVVP NELGQIFVKF ENADFAEKAI TGLHQRWFGG RTIKASILPE TDYYFKFPNA
KTA
