ID   SPO6_SCHPO              Reviewed;         474 AA.
AC   Q9Y7J1;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Sporulation-specific protein 6;
GN   Name=spo6; ORFNames=SPBC1778.04;
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10886372; DOI=10.1046/j.1365-2443.2000.00343.x;
RA   Nakamura T., Kishida M., Shimoda C.;
RT   "The Schizosaccharomyces pombe spo6+ gene encoding a nuclear protein with
RT   sequence similarity to budding yeast Dbf4 is required for meiotic second
RT   division and sporulation.";
RL   Genes Cells 5:463-479(2000).
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).
CC   -!- FUNCTION: May act as a kinase regulator. Essential for progression of
CC       meiosis II and sporulation. {ECO:0000269|PubMed:10886372}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10886372}.
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DR   EMBL; CU329671; CAB39799.1; -; Genomic_DNA.
DR   EMBL; AB020809; BAA82783.1; -; Genomic_DNA.
DR   PIR; T43504; T43504.
DR   RefSeq; NP_596287.1; NM_001022209.2.
DR   AlphaFoldDB; Q9Y7J1; -.
DR   SMR; Q9Y7J1; -.
DR   BioGRID; 276582; 15.
DR   STRING; 4896.SPBC1778.04.1; -.
DR   PaxDb; Q9Y7J1; -.
DR   PRIDE; Q9Y7J1; -.
DR   EnsemblFungi; SPBC1778.04.1; SPBC1778.04.1:pep; SPBC1778.04.
DR   GeneID; 2540044; -.
DR   KEGG; spo:SPBC1778.04; -.
DR   PomBase; SPBC1778.04; spo6.
DR   VEuPathDB; FungiDB:SPBC1778.04; -.
DR   eggNOG; KOG4139; Eukaryota.
DR   HOGENOM; CLU_576409_0_0_1; -.
DR   InParanoid; Q9Y7J1; -.
DR   OMA; GYCENCC; -.
DR   PhylomeDB; Q9Y7J1; -.
DR   PRO; PR:Q9Y7J1; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005654; C:nucleoplasm; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0043539; F:protein serine/threonine kinase activator activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030437; P:ascospore formation; IMP:PomBase.
DR   GO; GO:0007135; P:meiosis II; IMP:PomBase.
DR   GO; GO:0007165; P:signal transduction; IC:PomBase.
DR   Gene3D; 3.40.50.10190; -; 1.
DR   Gene3D; 6.10.250.3410; -; 1.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR013939; Regulatory_Dfp1/Him1.
DR   InterPro; IPR006572; Znf_DBF.
DR   InterPro; IPR038545; Znf_DBF_sf.
DR   Pfam; PF08630; Dfp1_Him1_M; 1.
DR   Pfam; PF07535; zf-DBF; 1.
DR   SMART; SM00586; ZnF_DBF; 1.
DR   SUPFAM; SSF52113; SSF52113; 1.
DR   PROSITE; PS51265; ZF_DBF4; 1.
PE   4: Predicted;
KW   Meiosis; Metal-binding; Nucleus; Reference proteome; Sporulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..474
FT                   /note="Sporulation-specific protein 6"
FT                   /id="PRO_0000072139"
FT   DOMAIN          125..178
FT                   /note="BRCT"
FT   ZN_FING         421..470
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT   BINDING         428
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT   BINDING         431
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT   BINDING         441
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT   BINDING         447
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
SQ   SEQUENCE   474 AA;  54749 MW;  0E14F84C068EC419 CRC64;
     MDFYSVKSQP FVRSPLVDQN PSIQNINEEV KRDIQNPLSY KTETSDKELC QTAACATSCS
     DWYPQQQTHM PHQNAFDSAK ATAKMALPPT AFSNYCVKPS LTRNKDIPRT SIRVSKLRYW
     QRDYRLAFPN FIFYFDNVDE EIKRRVTQKI NNLGAKVATL FTFEVTHFIT TRTTDPEMCQ
     PNDVLYLSKT ANMKIWLLDK LLNRILFTLL NSDSLVNTSA SCLQSLLDGE KVYGTSDKDF
     YVPSKNVEYF REYFLCIRDL SQYYKPIAVR EWEKTLDSGE ILWPSLAITA QGRCPFNTGR
     RRELKITKHN HPAHEIRKQL LSCTNQTNQN NVVKNSASVL VRQIMGDYNI TESAVDGAKQ
     MPTEFPKPEN LLPVEKRAAM SPLNLLEPRL INKQNTLANQ SPRQPPNAFD ADPLAHKKVK
     IETKSGYCEN CCERYKDLER HLGGKHHRRF AEKDENFQGL DDLFLLIRRP IRTN