ID   NHP2_SCHPO              Reviewed;         154 AA.
AC   Q9P7H0; O94239;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=H/ACA ribonucleoprotein complex subunit nhp2;
DE   AltName: Full=H/ACA snoRNP protein NHP2;
DE   AltName: Full=High mobility group-like nuclear protein 2;
DE   AltName: Full=P17-nhp2;
GN   Name=nhp2; ORFNames=SPAC1782.10c;
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:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10502409; DOI=10.1006/excr.1999.4607;
RA   Maiorano D., Brimage L.J., Leroy D., Kearsey S.E.;
RT   "Functional conservation and cell cycle localization of the Nhp2 core
RT   component of H+ACA snoRNPs in fission and budding yeasts.";
RL   Exp. Cell Res. 252:165-174(1999).
RN   [2]
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, 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: Non-catalytic component of the H/ACA small nucleolar
CC       ribonucleoprotein (H/ACA snoRNP), which catalyzes pseudouridylation of
CC       rRNA and is required for ribosome biogenesis (PubMed:10502409). This
CC       involves the isomerization of uridine such that the ribose is
CC       subsequently attached to C5, instead of the normal N1 (By similarity).
CC       Pseudouridine ('psi') residues may serve to stabilize the conformation
CC       of rRNAs (By similarity). The H/ACA snoRNP complex also mediates
CC       pseudouridylation of other types of RNAs (By similarity). The H/ACA
CC       snoRNP complex mediates pseudouridylation at position 93 in U2 snRNA
CC       (By similarity). Directly binds H/ACA snoRNAs (By similarity).
CC       {ECO:0000250|UniProtKB:P32495, ECO:0000269|PubMed:10502409}.
CC   -!- SUBUNIT: Component of the small nucleolar ribonucleoprotein particles
CC       containing H/ACA-type snoRNAs (H/ACA snoRNPs).
CC       {ECO:0000250|UniProtKB:P32495}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10502409}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ010068; CAA08990.1; -; mRNA.
DR   EMBL; CU329670; CAB76272.1; -; Genomic_DNA.
DR   PIR; T43644; T43644.
DR   PIR; T50100; T50100.
DR   RefSeq; NP_594717.1; NM_001020144.2.
DR   AlphaFoldDB; Q9P7H0; -.
DR   SMR; Q9P7H0; -.
DR   BioGRID; 278833; 12.
DR   STRING; 4896.SPAC1782.10c.1; -.
DR   iPTMnet; Q9P7H0; -.
DR   MaxQB; Q9P7H0; -.
DR   PaxDb; Q9P7H0; -.
DR   PRIDE; Q9P7H0; -.
DR   EnsemblFungi; SPAC1782.10c.1; SPAC1782.10c.1:pep; SPAC1782.10c.
DR   GeneID; 2542369; -.
DR   KEGG; spo:SPAC1782.10c; -.
DR   PomBase; SPAC1782.10c; nhp2.
DR   VEuPathDB; FungiDB:SPAC1782.10c; -.
DR   eggNOG; KOG3167; Eukaryota.
DR   HOGENOM; CLU_084513_1_1_1; -.
DR   InParanoid; Q9P7H0; -.
DR   OMA; IDVYSHI; -.
DR   PhylomeDB; Q9P7H0; -.
DR   PRO; PR:Q9P7H0; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0031429; C:box H/ACA snoRNP complex; IGI:PomBase.
DR   GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0034513; F:box H/ACA snoRNA binding; IGI:PomBase.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0019843; F:rRNA binding; IC:PomBase.
DR   GO; GO:0000469; P:cleavage involved in rRNA processing; IBA:GO_Central.
DR   GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR   GO; GO:0031118; P:rRNA pseudouridine synthesis; IGI:PomBase.
DR   GO; GO:0031120; P:snRNA pseudouridine synthesis; IGI:PomBase.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   InterPro; IPR002415; H/ACA_rnp_Nhp2-like.
DR   InterPro; IPR029064; L30e-like.
DR   InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
DR   InterPro; IPR018492; Ribosomal_L7Ae/L8/Nhp2.
DR   Pfam; PF01248; Ribosomal_L7Ae; 1.
DR   PRINTS; PR00881; L7ARS6FAMILY.
DR   PRINTS; PR00883; NUCLEARHMG.
DR   SUPFAM; SSF55315; SSF55315; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW   Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..154
FT                   /note="H/ACA ribonucleoprotein complex subunit nhp2"
FT                   /id="PRO_0000136775"
FT   MOD_RES         119
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   CONFLICT        76
FT                   /note="A -> P (in Ref. 1; CAA08990)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   154 AA;  17178 MW;  9E5E8FE5E88B6055 CRC64;
     MAKDKKDHKH SGSTEDEYDS YLPALMPIAK PLAPKKLNKK MMKTVKKASK QKHILRGVKE
     VVKAVRKGEK GLVILAGDIS PMDVISHIPV LCEDNNVPYL YTVSKELLGE ASNTKRPTSC
     VMIVPGGKKK DMSKVEEYKE SYEEIIKEVP ALEV