ID   BCD1_YEAST              Reviewed;         366 AA.
AC   P38772; D3DKY8;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Box C/D snoRNA protein 1;
GN   Name=BCD1; OrderedLocusNames=YHR040W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   FUNCTION.
RX   PubMed=12837249; DOI=10.1016/s0092-8674(03)00466-5;
RA   Peng W.-T., Robinson M.D., Mnaimneh S., Krogan N.J., Cagney G.,
RA   Morris Q.D., Davierwala A.P., Grigull J., Yang X., Zhang W., Mitsakakis N.,
RA   Ryan O.W., Datta N., Jojic V., Pal C., Canadien V., Richards D.P.,
RA   Beattie B., Wu L.F., Altschuler S.J., Roweis S., Frey B.J., Emili A.,
RA   Greenblatt J.F., Hughes T.R.;
RT   "A panoramic view of yeast noncoding RNA processing.";
RL   Cell 113:919-933(2003).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA   Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA   Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA   Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT   "Assigning function to yeast proteins by integration of technologies.";
RL   Mol. Cell 12:1353-1365(2003).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Required for box C/D snoRNAs accumulation involved in snoRNA
CC       processing, snoRNA transport to the nucleolus and ribosome biogenesis.
CC       {ECO:0000269|PubMed:12837249}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:14690591}.
CC   -!- MISCELLANEOUS: Present with 2800 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the BCD1 family. {ECO:0000305}.
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DR   EMBL; U00062; AAB68905.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06732.1; -; Genomic_DNA.
DR   PIR; S46736; S46736.
DR   RefSeq; NP_011906.1; NM_001179170.1.
DR   PDB; 2N94; NMR; -; A=1-45.
DR   PDB; 6NZ2; NMR; -; A=120-303.
DR   PDB; 6THL; X-ray; 2.80 A; B=120-303.
DR   PDBsum; 2N94; -.
DR   PDBsum; 6NZ2; -.
DR   PDBsum; 6THL; -.
DR   AlphaFoldDB; P38772; -.
DR   SMR; P38772; -.
DR   BioGRID; 36472; 212.
DR   DIP; DIP-3862N; -.
DR   IntAct; P38772; 7.
DR   STRING; 4932.YHR040W; -.
DR   iPTMnet; P38772; -.
DR   MaxQB; P38772; -.
DR   PaxDb; 4932-YHR040W; -.
DR   PeptideAtlas; P38772; -.
DR   EnsemblFungi; YHR040W_mRNA; YHR040W; YHR040W.
DR   GeneID; 856436; -.
DR   KEGG; sce:YHR040W; -.
DR   AGR; SGD:S000001082; -.
DR   SGD; S000001082; BCD1.
DR   VEuPathDB; FungiDB:YHR040W; -.
DR   eggNOG; KOG2858; Eukaryota.
DR   GeneTree; ENSGT00390000017201; -.
DR   HOGENOM; CLU_025524_3_0_1; -.
DR   InParanoid; P38772; -.
DR   OMA; LGNCEVC; -.
DR   OrthoDB; 162842at2759; -.
DR   BioCyc; YEAST:G3O-31099-MONOMER; -.
DR   BioGRID-ORCS; 856436; 4 hits in 10 CRISPR screens.
DR   PRO; PR:P38772; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38772; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0070761; C:pre-snoRNP complex; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030515; F:snoRNA binding; IDA:SGD.
DR   GO; GO:0000492; P:box C/D snoRNP assembly; IDA:SGD.
DR   GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0042254; P:ribosome biogenesis; IDA:SGD.
DR   GO; GO:0016074; P:sno(s)RNA metabolic process; IMP:SGD.
DR   GO; GO:0048254; P:snoRNA localization; IBA:GO_Central.
DR   Gene3D; 3.30.60.190; -; 1.
DR   InterPro; IPR007529; Znf_HIT.
DR   PANTHER; PTHR13483:SF3; BOX C_D SNORNA PROTEIN 1; 1.
DR   PANTHER; PTHR13483; UNCHARACTERIZED; 1.
DR   Pfam; PF04438; zf-HIT; 1.
DR   SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR   PROSITE; PS51083; ZF_HIT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Ribosome biogenesis; Zinc; Zinc-finger.
FT   CHAIN           1..366
FT                   /note="Box C/D snoRNA protein 1"
FT                   /id="PRO_0000173558"
FT   ZN_FING         5..39
FT                   /note="HIT-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT   REGION          318..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         5
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT   BINDING         8
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT   BINDING         17
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT   BINDING         20
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT   BINDING         25
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT   BINDING         29
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT   BINDING         33
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT   BINDING         39
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT   MOD_RES         330
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   STRAND          6..8
FT                   /evidence="ECO:0007829|PDB:2N94"
FT   TURN            18..20
FT                   /evidence="ECO:0007829|PDB:2N94"
FT   HELIX           27..37
FT                   /evidence="ECO:0007829|PDB:2N94"
FT   STRAND          41..43
FT                   /evidence="ECO:0007829|PDB:2N94"
FT   STRAND          127..130
FT                   /evidence="ECO:0007829|PDB:6NZ2"
FT   STRAND          133..136
FT                   /evidence="ECO:0007829|PDB:6THL"
FT   HELIX           143..147
FT                   /evidence="ECO:0007829|PDB:6THL"
FT   STRAND          151..153
FT                   /evidence="ECO:0007829|PDB:6THL"
FT   TURN            154..157
FT                   /evidence="ECO:0007829|PDB:6THL"
FT   STRAND          158..167
FT                   /evidence="ECO:0007829|PDB:6THL"
FT   STRAND          180..191
FT                   /evidence="ECO:0007829|PDB:6THL"
FT   HELIX           194..196
FT                   /evidence="ECO:0007829|PDB:6THL"
FT   HELIX           199..208
FT                   /evidence="ECO:0007829|PDB:6THL"
FT   TURN            218..220
FT                   /evidence="ECO:0007829|PDB:6NZ2"
FT   HELIX           227..235
FT                   /evidence="ECO:0007829|PDB:6THL"
FT   STRAND          240..244
FT                   /evidence="ECO:0007829|PDB:6THL"
FT   STRAND          258..261
FT                   /evidence="ECO:0007829|PDB:6THL"
FT   HELIX           264..266
FT                   /evidence="ECO:0007829|PDB:6THL"
FT   HELIX           269..273
FT                   /evidence="ECO:0007829|PDB:6THL"
FT   STRAND          277..281
FT                   /evidence="ECO:0007829|PDB:6THL"
FT   STRAND          283..290
FT                   /evidence="ECO:0007829|PDB:6THL"
SQ   SEQUENCE   366 AA;  42334 MW;  EE8BDAF489EC1F12 CRC64;
     MAVLCGVCGI KEFKYKCPRC LVQTCSLECS KKHKTRDNCS GQTHDPKEYI SSEALKQADD
     DKHERNAYVQ RDYNYLTQLK RMVHVQKMDA RMKNKRVLGP VGGHNSNFKK RRYDIDEDDR
     DSTECQRIIR RGVNCLMLPK GMQRSSQNRS KWDKTMDLFV WSVEWILCPM QEKGEKKELF
     KHVSHRIKET DFLVQGMGKN VFQKCCEFYR LAGTSSCIEG EDGSETKEER TQILQKSGLK
     FYTKTFPYNT THIMDSKKLV ELAIHEKCIG ELLKNTTVIE FPTIFVAMTE ADLPEGYEVL
     HQEPRPLEHT STLNKFIDNA REEEDAEEDS QPTEEPVQKE TQDASDSDSD SDDDYNPGLS
     MDFLTA
//