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Centromere DNA-binding protein complex CBF3 subunit B (Centromere protein 3)

 CBF3B_YEAST             Reviewed;         608 AA.
P40969; D6VZZ0;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
28-MAR-2018, entry version 143.
RecName: Full=Centromere DNA-binding protein complex CBF3 subunit B;
Short=Centromere protein 3;
Name=CEP3; Synonyms=CBF3, CBF3B, CSL1; OrderedLocusNames=YMR168C;
ORFNames=YM8520.17C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=AC 502;
PubMed=7957085;
Lechner J.;
"A zinc finger protein, essential for chromosome segregation,
constitutes a putative DNA binding subunit of the Saccharomyces
cerevisiae kinetochore complex, Cbf3.";
EMBO J. 13:5203-5211(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7876302; DOI=10.1083/jcb.128.5.749;
Strunnikov A.V., Kingsbury J., Koshland D.;
"CEP3 encodes a centromere protein of Saccharomyces cerevisiae.";
J. Cell Biol. 128:749-760(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169872;
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S.,
Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome
XIII.";
Nature 387:90-93(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
ASSEMBLY OF THE CBF3 COMPLEX.
PubMed=15090617; DOI=10.1091/mbc.E03-12-0887;
Rodrigo-Brenni M.C., Thomas S., Bouck D.C., Kaplan K.B.;
"Sgt1p and Skp1p modulate the assembly and turnover of CBF3 complexes
required for proper kinetochore function.";
Mol. Biol. Cell 15:3366-3378(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
-!- FUNCTION: Acts as a component of the centromere DNA-binding
protein complex CBF3, which is essential for chromosome
segregation and movement of centromeres along microtubules. CBF3
is required for the recruitment of other kinetochore complexes to
CEN DNA. It plays a role in the attachment of chromosomes to the
spindle and binds selectively to a highly conserved DNA sequence
called CDEIII, found in centromers and in several promoters.
-!- SUBUNIT: Component of the CBF3 copmplex, which is formed of
CBF3A/CBF2, CBF3B/CEP3, CBF3C/CTF13 and CBF3D.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-4077, EBI-4077;
P35203:CTF13; NbExp=2; IntAct=EBI-4077, EBI-4085;
P22216:RAD53; NbExp=2; IntAct=EBI-4077, EBI-17843;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome,
centromere.
-!- MISCELLANEOUS: Present with 1900 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-----------------------------------------------------------------------
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EMBL; X81396; CAA57159.1; -; Genomic_DNA.
EMBL; U12339; AAA57074.1; -; Genomic_DNA.
EMBL; Z49705; CAA89804.1; -; Genomic_DNA.
EMBL; BK006946; DAA10064.1; -; Genomic_DNA.
PIR; S51790; S51790.
RefSeq; NP_013891.1; NM_001182672.1.
PDB; 2QUQ; X-ray; 2.80 A; A=47-608.
PDB; 2VEQ; X-ray; 2.49 A; A=48-608.
PDB; 6F07; EM; 3.60 A; A/B=1-608.
PDBsum; 2QUQ; -.
PDBsum; 2VEQ; -.
PDBsum; 6F07; -.
ProteinModelPortal; P40969; -.
SMR; P40969; -.
BioGrid; 35346; 599.
DIP; DIP-5956N; -.
IntAct; P40969; 12.
MINT; P40969; -.
STRING; 4932.YMR168C; -.
iPTMnet; P40969; -.
MaxQB; P40969; -.
PaxDb; P40969; -.
PRIDE; P40969; -.
EnsemblFungi; YMR168C; YMR168C; YMR168C.
GeneID; 855204; -.
KEGG; sce:YMR168C; -.
EuPathDB; FungiDB:YMR168C; -.
SGD; S000004778; CEP3.
HOGENOM; HOG000111345; -.
InParanoid; P40969; -.
KO; K11575; -.
OMA; DYLQSGP; -.
OrthoDB; EOG092C1C0B; -.
BioCyc; YEAST:G3O-32858-MONOMER; -.
EvolutionaryTrace; P40969; -.
PRO; PR:P40969; -.
Proteomes; UP000002311; Chromosome XIII.
GO; GO:0031518; C:CBF3 complex; IDA:SGD.
GO; GO:0000778; C:condensed nuclear chromosome kinetochore; IDA:SGD.
GO; GO:0019237; F:centromeric DNA binding; IDA:SGD.
GO; GO:0008301; F:DNA binding, bending; IDA:SGD.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007094; P:mitotic spindle assembly checkpoint; IMP:SGD.
GO; GO:0000921; P:septin ring assembly; IMP:SGD.
CDD; cd00067; GAL4; 1.
Gene3D; 4.10.240.10; -; 1.
InterPro; IPR031760; Cep3_C.
InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
Pfam; PF16846; Cep3; 1.
Pfam; PF00172; Zn_clus; 1.
SMART; SM00066; GAL4; 1.
SUPFAM; SSF57701; SSF57701; 1.
PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
1: Evidence at protein level;
3D-structure; Centromere; Chromosome; Complete proteome; DNA-binding;
Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Zinc.
CHAIN 1 608 Centromere DNA-binding protein complex
CBF3 subunit B.
/FTId=PRO_0000114941.
DNA_BIND 14 42 Zn(2)-C6 fungal-type.
{ECO:0000255|PROSITE-ProRule:PRU00227}.
MOD_RES 575 575 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
HELIX 58 71 {ECO:0000244|PDB:2VEQ}.
TURN 72 74 {ECO:0000244|PDB:2VEQ}.
HELIX 75 79 {ECO:0000244|PDB:2VEQ}.
HELIX 85 87 {ECO:0000244|PDB:2VEQ}.
TURN 92 95 {ECO:0000244|PDB:2VEQ}.
HELIX 96 105 {ECO:0000244|PDB:2VEQ}.
HELIX 108 121 {ECO:0000244|PDB:2VEQ}.
HELIX 123 130 {ECO:0000244|PDB:2VEQ}.
HELIX 134 146 {ECO:0000244|PDB:2VEQ}.
HELIX 154 173 {ECO:0000244|PDB:2VEQ}.
HELIX 176 182 {ECO:0000244|PDB:2VEQ}.
HELIX 186 192 {ECO:0000244|PDB:2VEQ}.
HELIX 200 202 {ECO:0000244|PDB:2VEQ}.
HELIX 204 222 {ECO:0000244|PDB:2VEQ}.
TURN 223 227 {ECO:0000244|PDB:2VEQ}.
HELIX 231 240 {ECO:0000244|PDB:2VEQ}.
TURN 241 244 {ECO:0000244|PDB:2VEQ}.
HELIX 245 248 {ECO:0000244|PDB:2VEQ}.
HELIX 250 265 {ECO:0000244|PDB:2VEQ}.
HELIX 280 302 {ECO:0000244|PDB:2VEQ}.
HELIX 313 315 {ECO:0000244|PDB:2QUQ}.
HELIX 338 356 {ECO:0000244|PDB:2VEQ}.
TURN 357 360 {ECO:0000244|PDB:2VEQ}.
HELIX 367 385 {ECO:0000244|PDB:2VEQ}.
HELIX 394 422 {ECO:0000244|PDB:2VEQ}.
HELIX 427 443 {ECO:0000244|PDB:2VEQ}.
HELIX 444 446 {ECO:0000244|PDB:2VEQ}.
TURN 447 449 {ECO:0000244|PDB:2VEQ}.
HELIX 451 455 {ECO:0000244|PDB:2VEQ}.
HELIX 457 476 {ECO:0000244|PDB:2VEQ}.
HELIX 480 495 {ECO:0000244|PDB:2VEQ}.
HELIX 498 500 {ECO:0000244|PDB:2VEQ}.
HELIX 501 522 {ECO:0000244|PDB:2VEQ}.
STRAND 530 534 {ECO:0000244|PDB:2VEQ}.
HELIX 536 550 {ECO:0000244|PDB:2VEQ}.
HELIX 555 562 {ECO:0000244|PDB:2VEQ}.
HELIX 589 600 {ECO:0000244|PDB:2VEQ}.
HELIX 603 606 {ECO:0000244|PDB:2VEQ}.
SEQUENCE 608 AA; 71358 MW; 2E24A0508080A09B CRC64;
MFNRTTQLKS KHPCSVCTRR KVKCDRMIPC GNCRKRGQDS ECMKSTKLIT ASSSKEYLPD
LLLFWQNYEY WITNIGLYKT KQRDLTRTPA NLDTDTEECM FWMNYLQKDQ SFQLMNFAME
NLGALYFGSI GDISELYLRV EQYWDRRADK NHSVDGKYWD ALIWSVFTMC IYYMPVEKLA
EIFSVYPLHE YLGSNKRLNW EDGMQLVMCQ NFARCSLFQL KQCDFMAHPD IRLVQAYLIL
ATTTFPYDEP LLANSLLTQC IHTFKNFHVD DFRPLLNDDP VESIAKVTLG RIFYRLCGCD
YLQSGPRKPI ALHTEVSSLL QHAAYLQDLP NVDVYREENS TEVLYWKIIS LDRDLDQYLN
KSSKPPLKTL DAIRRELDIF QYKVDSLEED FRSNNSRFQK FIALFQISTV SWKLFKMYLI
YYDTADSLLK VIHYSKVIIS LIVNNFHAKS EFFNRHPMVM QTITRVVSFI SFYQIFVESA
AVKQLLVDLT ELTANLPTIF GSKLDKLVYL TERLSKLKLL WDKVQLLDSG DSFYHPVFKI
LQNDIKIIEL KNDEMFSLIK GLGSLVPLNK LRQESLLEEE DENNTEPSDF RTIVEEFQSE
YNISDILS


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