ID   PCC1_SCHPO              Reviewed;          88 AA.
AC   Q10220;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=EKC/KEOPS complex subunit SPAC4H3.13;
DE   AltName: Full=Protein PCC1 homolog;
GN   ORFNames=SPAC4H3.13;
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   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).
CC   -!- FUNCTION: Component of the EKC/KEOPS complex that is required for the
CC       formation of a threonylcarbamoyl group on adenosine at position 37
CC       (t(6)A37) in tRNAs that read codons beginning with adenine. The complex
CC       is probably involved in the transfer of the threonylcarbamoyl moiety of
CC       threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. SPAC4H3.13/PCC1
CC       functions as a dimerization module for the complex. The EKC/KEOPS
CC       complex also promotes both telomere uncapping and telomere elongation.
CC       The complex is required for efficient recruitment of transcriptional
CC       coactivators (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the EKC/KEOPS complex composed of at least of
CC       SPAP27G11.07c/BUD32, cgi121, gon7, pgp2 and SPAC4H3.13/PCC1; the whole
CC       complex dimerizes. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}. Chromosome, telomere {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CTAG/PCC1 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA93352.1; -; Genomic_DNA.
DR   PIR; T38893; T38893.
DR   RefSeq; NP_594349.1; NM_001019770.2.
DR   AlphaFoldDB; Q10220; -.
DR   SMR; Q10220; -.
DR   BioGRID; 279837; 1.
DR   STRING; 4896.SPAC4H3.13.1; -.
DR   MaxQB; Q10220; -.
DR   PaxDb; Q10220; -.
DR   EnsemblFungi; SPAC4H3.13.1; SPAC4H3.13.1:pep; SPAC4H3.13.
DR   GeneID; 2543415; -.
DR   KEGG; spo:SPAC4H3.13; -.
DR   PomBase; SPAC4H3.13; -.
DR   VEuPathDB; FungiDB:SPAC4H3.13; -.
DR   HOGENOM; CLU_113770_4_1_1; -.
DR   InParanoid; Q10220; -.
DR   OMA; YFCSSAR; -.
DR   PhylomeDB; Q10220; -.
DR   PRO; PR:Q10220; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0000408; C:EKC/KEOPS complex; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0070525; P:tRNA threonylcarbamoyladenosine metabolic process; IBA:GO_Central.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; ISO:PomBase.
DR   InterPro; IPR015419; CTAG/Pcc1.
DR   PANTHER; PTHR31283; PTHR31283; 1.
DR   Pfam; PF09341; Pcc1; 1.
PE   3: Inferred from homology;
KW   Activator; Chromosome; Cytoplasm; Nucleus; Reference proteome; Telomere;
KW   Transcription; Transcription regulation; tRNA processing.
FT   CHAIN           1..88
FT                   /note="EKC/KEOPS complex subunit SPAC4H3.13"
FT                   /id="PRO_0000218926"
SQ   SEQUENCE   88 AA;  10112 MW;  1588AC8F5CA7C899 CRC64;
     MSEMIVLPHK VTVKVPLASR VDAERCLQVL APDRELKEEL VQRNLFVDDN YLVVNYSCSS
     ARMTRVTVNS LFENLYLIID TMHELSSL