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Protein

H/ACA ribonucleoprotein complex subunit 4

Gene

CBF5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a central role in ribosomal RNA processing. Probable catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs. May function as a pseudouridine synthase. Binds in vitro to centromeres and microtubules. It is a centromeric DNA-CBF3-binding factor which is involved in mitotic chromosome segregation. Essential for cell growth.5 Publications

Catalytic activityi

RNA uridine = RNA pseudouridine.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei95 – 951NucleophileBy similarity

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • pseudouridine synthase activity Source: SGD
  • RNA binding Source: UniProtKB-KW

GO - Biological processi

  • box H/ACA snoRNA 3'-end processing Source: SGD
  • cell division Source: UniProtKB-KW
  • mitotic nuclear division Source: UniProtKB-KW
  • mRNA pseudouridine synthesis Source: SGD
  • rRNA modification Source: UniProtKB
  • rRNA processing Source: SGD
  • rRNA pseudouridine synthesis Source: SGD
  • snRNA pseudouridine synthesis Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Ribonucleoprotein

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ribosome biogenesis, rRNA processing

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

BioCyciYEAST:YLR175W-MONOMER.
ReactomeiR-SCE-171319. Telomere Extension By Telomerase.

Names & Taxonomyi

Protein namesi
Recommended name:
H/ACA ribonucleoprotein complex subunit 4 (EC:5.4.99.-)
Alternative name(s):
Centromere-binding factor 5
Centromere/microtubule-binding protein CBF5
H/ACA snoRNP protein CBF5
Small nucleolar RNP protein CBF5
p64'
Gene namesi
Name:CBF5
Ordered Locus Names:YLR175W
ORF Names:L9470.11
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR175W.
SGDiS000004165. CBF5.

Subcellular locationi

GO - Cellular componenti

  • box H/ACA snoRNP complex Source: SGD
  • chromosome, centromeric region Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB-KW
  • microtubule Source: UniProtKB-KW
  • nucleolus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Microtubule, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi65 – 651D → A: Reduced pseudouridylation of rRNA and reduced snoRNA levels. 1 Publication
Mutagenesisi94 – 941L → A: Reduced pseudouridylation of rRNA. 1 Publication
Mutagenesisi95 – 951D → A: Reduced pseudouridylation of rRNA. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 483483H/ACA ribonucleoprotein complex subunit 4PRO_0000121982Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki9 – 9Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei47 – 471PhosphoserineCombined sources
Cross-linki267 – 267Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei378 – 3781PhosphothreonineCombined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP33322.

PTM databases

iPTMnetiP33322.

Interactioni

Subunit structurei

Component of the small nucleolar ribonucleoprotein particles containing H/ACA-type snoRNAs (H/ACA snoRNPs). The protein component of the H/ACA snoRNP contains CBF5, GAR1, NHP2 and NOP10. The complex contains a stable core composed of CBF5 and NOP10, to which GAR1 and NHP2 subsequently bind. Also interacts with NAF1 and SHQ1, which may be required for assembly of H/ACA snoRNP complexes. May also associate with the CBF3 110 kDa subunit (CBF2). Interacts with the trimethylguanosine synthase (TGS1) and with NOP53.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NAF1P539196EBI-4105,EBI-28887
NHP2P3249511EBI-4105,EBI-12014

Protein-protein interaction databases

BioGridi31446. 166 interactions.
DIPiDIP-4472N.
IntActiP33322. 74 interactions.
MINTiMINT-501145.

Structurei

Secondary structure

1
483
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 263Combined sources
Helixi29 – 313Combined sources
Beta strandi32 – 354Combined sources
Helixi48 – 503Combined sources
Helixi53 – 586Combined sources
Beta strandi60 – 667Combined sources
Beta strandi68 – 703Combined sources
Helixi72 – 8312Combined sources
Beta strandi88 – 925Combined sources
Beta strandi94 – 974Combined sources
Beta strandi99 – 1068Combined sources
Helixi107 – 1126Combined sources
Helixi113 – 1186Combined sources
Beta strandi121 – 13111Combined sources
Helixi138 – 1458Combined sources
Beta strandi148 – 1525Combined sources
Beta strandi165 – 17814Combined sources
Turni179 – 1824Combined sources
Beta strandi183 – 1908Combined sources
Helixi196 – 20712Combined sources
Beta strandi211 – 22111Combined sources
Helixi233 – 24614Combined sources
Helixi250 – 2556Combined sources
Beta strandi256 – 2583Combined sources
Helixi259 – 2635Combined sources
Beta strandi268 – 2714Combined sources
Helixi273 – 2753Combined sources
Helixi276 – 2827Combined sources
Beta strandi283 – 2864Combined sources
Helixi287 – 2893Combined sources
Beta strandi290 – 2934Combined sources
Beta strandi302 – 3065Combined sources
Beta strandi312 – 3209Combined sources
Helixi322 – 3276Combined sources
Beta strandi329 – 33911Combined sources
Helixi355 – 36511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3U28X-ray1.90A3-394[»]
3UAIX-ray3.06A3-394[»]
3ZV0X-ray2.80C/D1-386[»]
ProteinModelPortaliP33322.
SMRiP33322. Positions 18-378.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini266 – 34176PUAPROSITE-ProRule annotationAdd
BLAST
Repeati434 – 43631
Repeati437 – 43932
Repeati440 – 44233
Repeati443 – 44534
Repeati446 – 44835
Repeati449 – 45136
Repeati452 – 45437
Repeati455 – 45738
Repeati458 – 46039
Repeati461 – 463310

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni434 – 4633010 X 3 AA tandem repeats of K-K-[DE]Add
BLAST

Sequence similaritiesi

Belongs to the pseudouridine synthase TruB family.Curated
Contains 1 PUA domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00510000047092.
HOGENOMiHOG000231224.
InParanoidiP33322.
KOiK11131.
OMAiYVDYNAK.
OrthoDBiEOG7QNVWW.

Family and domain databases

Gene3Di2.30.130.10. 1 hit.
InterProiIPR012960. Dyskerin-like.
IPR020103. PsdUridine_synth_cat_dom.
IPR002501. PsdUridine_synth_N.
IPR002478. PUA.
IPR015947. PUA-like_domain.
IPR004802. tRNA_PsdUridine_synth_B_fam.
IPR032819. TruB_C.
IPR004521. Uncharacterised_CHP00451.
[Graphical view]
PANTHERiPTHR23127. PTHR23127. 1 hit.
PfamiPF08068. DKCLD. 1 hit.
PF01472. PUA. 1 hit.
PF16198. TruB_C_2. 1 hit.
PF01509. TruB_N. 1 hit.
[Graphical view]
SMARTiSM01136. DKCLD. 1 hit.
SM00359. PUA. 1 hit.
[Graphical view]
SUPFAMiSSF55120. SSF55120. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR00425. CBF5. 1 hit.
TIGR00451. unchar_dom_2. 1 hit.
PROSITEiPS50890. PUA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P33322-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKEDFVIKP EAAGASTDTS EWPLLLKNFD KLLVRSGHYT PIPAGSSPLK
60 70 80 90 100
RDLKSYISSG VINLDKPSNP SSHEVVAWIK RILRCEKTGH SGTLDPKVTG
110 120 130 140 150
CLIVCIDRAT RLVKSQQGAG KEYVCIVRLH DALKDEKDLG RSLENLTGAL
160 170 180 190 200
FQRPPLISAV KRQLRVRTIY ESNLIEFDNK RNLGVFWASC EAGTYMRTLC
210 220 230 240 250
VHLGMLLGVG GHMQELRRVR SGALSENDNM VTLHDVMDAQ WVYDNTRDES
260 270 280 290 300
YLRSIIQPLE TLLVGYKRIV VKDSAVNAVC YGAKLMIPGL LRYEEGIELY
310 320 330 340 350
DEIVLITTKG EAIAVAIAQM STVDLASCDH GVVASVKRCI MERDLYPRRW
360 370 380 390 400
GLGPVAQKKK QMKADGKLDK YGRVNENTPE QWKKEYVPLD NAEQSTSSSQ
410 420 430 440 450
ETKETEEEPK KAKEDSLIKE VETEKEEVKE DDSKKEKKEK KDKKEKKEKK
460 470 480
EKKDKKEKKE KKEKKRKSED GDSEEKKSKK SKK
Length:483
Mass (Da):54,705
Last modified:February 1, 1994 - v1
Checksum:iD356B39FDCC32E2D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L12351 Genomic DNA. Translation: AAA34473.1.
U17246 Genomic DNA. Translation: AAB67463.1.
BK006945 Genomic DNA. Translation: DAA09495.1.
PIRiS41853.
RefSeqiNP_013276.1. NM_001182062.1.

Genome annotation databases

EnsemblFungiiYLR175W; YLR175W; YLR175W.
GeneIDi850872.
KEGGisce:YLR175W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L12351 Genomic DNA. Translation: AAA34473.1.
U17246 Genomic DNA. Translation: AAB67463.1.
BK006945 Genomic DNA. Translation: DAA09495.1.
PIRiS41853.
RefSeqiNP_013276.1. NM_001182062.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3U28X-ray1.90A3-394[»]
3UAIX-ray3.06A3-394[»]
3ZV0X-ray2.80C/D1-386[»]
ProteinModelPortaliP33322.
SMRiP33322. Positions 18-378.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31446. 166 interactions.
DIPiDIP-4472N.
IntActiP33322. 74 interactions.
MINTiMINT-501145.

PTM databases

iPTMnetiP33322.

Proteomic databases

MaxQBiP33322.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR175W; YLR175W; YLR175W.
GeneIDi850872.
KEGGisce:YLR175W.

Organism-specific databases

EuPathDBiFungiDB:YLR175W.
SGDiS000004165. CBF5.

Phylogenomic databases

GeneTreeiENSGT00510000047092.
HOGENOMiHOG000231224.
InParanoidiP33322.
KOiK11131.
OMAiYVDYNAK.
OrthoDBiEOG7QNVWW.

Enzyme and pathway databases

BioCyciYEAST:YLR175W-MONOMER.
ReactomeiR-SCE-171319. Telomere Extension By Telomerase.

Miscellaneous databases

PROiP33322.

Family and domain databases

Gene3Di2.30.130.10. 1 hit.
InterProiIPR012960. Dyskerin-like.
IPR020103. PsdUridine_synth_cat_dom.
IPR002501. PsdUridine_synth_N.
IPR002478. PUA.
IPR015947. PUA-like_domain.
IPR004802. tRNA_PsdUridine_synth_B_fam.
IPR032819. TruB_C.
IPR004521. Uncharacterised_CHP00451.
[Graphical view]
PANTHERiPTHR23127. PTHR23127. 1 hit.
PfamiPF08068. DKCLD. 1 hit.
PF01472. PUA. 1 hit.
PF16198. TruB_C_2. 1 hit.
PF01509. TruB_N. 1 hit.
[Graphical view]
SMARTiSM01136. DKCLD. 1 hit.
SM00359. PUA. 1 hit.
[Graphical view]
SUPFAMiSSF55120. SSF55120. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR00425. CBF5. 1 hit.
TIGR00451. unchar_dom_2. 1 hit.
PROSITEiPS50890. PUA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An essential yeast protein, CBF5p, binds in vitro to centromeres and microtubules."
    Jiang W., Middleton K., Yoon H.-J., Fouquet C., Carbon J.
    Mol. Cell. Biol. 13:4884-4893(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "The yeast nucleolar protein Cbf5p is involved in rRNA biosynthesis and interacts genetically with the RNA polymerase I transcription factor RRN3."
    Cadwell C., Yoon H.-J., Zebarjadian Y., Carbon J.
    Mol. Cell. Biol. 17:6175-6183(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "The box H + ACA snoRNAs carry Cbf5p, the putative rRNA pseudouridine synthase."
    Lafontaine D.L., Bousquet-Antonelli C., Henry Y., Caizergues-Ferrer M., Tollervey D.
    Genes Dev. 12:527-537(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN H/ACA SNORNP COMPLEXES.
  6. "Cbf5p, a potential pseudouridine synthase, and Nhp2p, a putative RNA-binding protein, are present together with Gar1p in all H BOX/ACA-motif snoRNPs and constitute a common bipartite structure."
    Watkins N.J., Gottschalk A., Neubauer G., Kastner B., Fabrizio P., Mann M., Luehrmann R.
    RNA 4:1549-1568(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN H/ACA SNORNP COMPLEX.
  7. "Point mutations in yeast CBF5 can abolish in vivo pseudouridylation of rRNA."
    Zebarjadian Y., King T., Fournier M.J., Clarke L., Carbon J.
    Mol. Cell. Biol. 19:7461-7472(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-65; LEU-94 AND ASP-95.
  8. "The Shq1p.Naf1p complex is required for box H/ACA small nucleolar ribonucleoprotein particle biogenesis."
    Yang P.K., Rotondo G., Porras T., Legrain P., Chanfreau G.
    J. Biol. Chem. 277:45235-45242(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SHQ1.
  9. "Hypermethylation of the cap structure of both yeast snRNAs and snoRNAs requires a conserved methyltransferase that is localized to the nucleolus."
    Mouaikel J., Verheggen C., Bertrand E., Tazi J., Bordonne R.
    Mol. Cell 9:891-901(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TGS1.
  10. "Naf1 p is a box H/ACA snoRNP assembly factor."
    Fatica A., Dlakic M., Tollervey D.
    RNA 8:1502-1514(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NAF1.
  11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  13. "Cbf5p, the putative pseudouridine synthase of H/ACA-type snoRNPs, can form a complex with Gar1p and Nop10p in absence of Nhp2p and box H/ACA snoRNAs."
    Henras A.K., Capeyrou R., Henry Y., Caizergues-Ferrer M.
    RNA 10:1704-1712(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF THE H/ACA SNORNP COMPLEX.
  14. "Nop53p is a novel nucleolar 60S ribosomal subunit biogenesis protein."
    Sydorskyy Y., Dilworth D.J., Halloran B., Yi E.C., Makhnevych T., Wozniak R.W., Aitchison J.D.
    Biochem. J. 388:819-826(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOP53, IDENTIFICATION BY MASS SPECTROMETRY.
  15. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  16. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND THR-378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-9 AND LYS-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCBF5_YEAST
AccessioniPrimary (citable) accession number: P33322
Secondary accession number(s): D6VYH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 6, 2016
This is version 158 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 33600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.