ID   RRN9_SCHPO              Reviewed;         250 AA.
AC   Q10204;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=RNA polymerase I-specific transcription initiation factor RRN9 homolog;
DE   AltName: Full=Accumulation of condensin at rDNA protein 1;
GN   Name=acr1; ORFNames=SPBC17D1.04;
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   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RRN5; RRN7; RRN11 AND
RP   SSP27, AND MUTAGENESIS OF CYS-58.
RX   PubMed=18362178; DOI=10.1083/jcb.200708170;
RA   Nakazawa N., Nakamura T., Kokubu A., Ebe M., Nagao K., Yanagida M.;
RT   "Dissection of the essential steps for condensin accumulation at
RT   kinetochores and rDNAs during fission yeast mitosis.";
RL   J. Cell Biol. 180:1115-1131(2008).
CC   -!- FUNCTION: Component of the UAF (upstream activation factor) complex
CC       which interacts with the upstream element of the RNA polymerase I
CC       promoter and is required for the proper accumulation of rpa1/nuc1 at
CC       rDNAs. Required for nucleolar localization of condensin.
CC       {ECO:0000269|PubMed:18362178}.
CC   -!- SUBUNIT: Component of the UAF (upstream activation factor) complex.
CC       Interacts with rrn5, rrn7, rrn11 and ssp27.
CC       {ECO:0000269|PubMed:18362178}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:18362178}.
CC   -!- SIMILARITY: Belongs to the RRN9 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA20428.1; -; Genomic_DNA.
DR   PIR; T39707; S67388.
DR   RefSeq; NP_596386.1; NM_001022307.2.
DR   AlphaFoldDB; Q10204; -.
DR   BioGRID; 276379; 2.
DR   STRING; 4896.SPBC17D1.04.1; -.
DR   MaxQB; Q10204; -.
DR   PaxDb; Q10204; -.
DR   PRIDE; Q10204; -.
DR   EnsemblFungi; SPBC17D1.04.1; SPBC17D1.04.1:pep; SPBC17D1.04.
DR   GeneID; 2539830; -.
DR   KEGG; spo:SPBC17D1.04; -.
DR   PomBase; SPBC17D1.04; acr1.
DR   VEuPathDB; FungiDB:SPBC17D1.04; -.
DR   eggNOG; ENOG502SYCY; Eukaryota.
DR   HOGENOM; CLU_1012503_0_0_1; -.
DR   InParanoid; Q10204; -.
DR   OMA; MDWQVVY; -.
DR   PRO; PR:Q10204; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR   GO; GO:0000500; C:RNA polymerase I upstream activating factor complex; IDA:PomBase.
DR   GO; GO:0001181; F:RNA polymerase I general transcription initiation factor activity; IC:PomBase.
PE   1: Evidence at protein level;
KW   Nucleus; Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..250
FT                   /note="RNA polymerase I-specific transcription initiation
FT                   factor RRN9 homolog"
FT                   /id="PRO_0000116529"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         58
FT                   /note="C->Y: In acr1-936; defects in accumulation of
FT                   condensin at rDNAs. Mitotic and interphase defects."
FT                   /evidence="ECO:0000269|PubMed:18362178"
SQ   SEQUENCE   250 AA;  28714 MW;  41F287186536409B CRC64;
     MNDSEEELEQ QGSQEDISSS QDTSDEKEMR KQDALYAQLI EYREIVSELR RSEMKNLCIQ
     LYCSYKAGIT RRNELQSDLD GYERRIPPRL RAVWPTIHSI PDESFFDGTS ASRFRQEAAY
     LAVRLASKKL HKLGRMASSE ELPNPDGLRY LVERLQIKLE RLFDSVDTFR QEQGSKSMQS
     RVKPMDWKIL YGLARVTNGS FSSSQKADVL ALGNGTRACQ SLFKEMSLQP SIDIEKVSHS
     NPEISIEFED