| Tag |
Content |
| dbPAF ID |
dbPAF-0004895 |
| Uniprot Accession |
P09232; PRTB_YEAST; D3DLJ0;
|
| Genbank Protein ID |
NP_010854.1;
|
| Genbank Nucleotide ID |
NM_001178875.1;
|
| Protein Name |
Cerevisin |
| Protein Synonyms/Alias |
Proteinase YSCB;Vacuolar protease B;PrB; |
| Gene Name |
PRB1 |
| Gene Synonyms/Alias |
YEL060C; |
| Organism |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)(Baker's yeast) |
| NCBI Taxa ID |
559292 |
Functional Description
(View all) |
Vacuolar proteinase B involved in protein degradation in the vacuole. Among other substrates, acts on carboxypeptidase Y (cpY/PRC1) to activate it by processing its Pro-peptide. Required for meiosis and spore formation, and for optimal survival in stationary phase.Functional Description
Vacuolar proteinase B involved in protein degradation in the vacuole. Among other substrates, acts on carboxypeptidase Y (cpY/PRC1) to activate it by processing its Pro-peptide. Required for meiosis and spore formation, and for optimal survival in stationary phase. |
Phosphorylation Sites
|
dbPAF PTMs: 3 |
Sequence
(Fasta) | MKLENTLFTL GALGSISAAL VIPNLENAAD HHELINKEDH HERPRKVEFT KDDDEEPSDS 60
EDKEHGKFHK KGRKGQDKES PEFNGKRASG SHGSAHEGGK GMKPKHESSN DDDNDDKKKK 120
PHHKGGCHEN KVEEKKMKGK KVKGKKHHEK TLEKGRHHNR LAPLVSTAQF NPDAISKIIP 180
NRYIIVFKRG APQEEIDFHK ENVQQAQLQS VENLSAEDAF FISTKDTSLS TSEAGGIQDS 240
FNIDNLFSGY IGYFTQEIVD LIRQNPLVDF VERDSIVEAT EFDTQNSAPW GLARISHRER 300
LNLGSFNKYL YDDDAGRGVT SYVIDTGVNI NHKDFEKRAI WGKTIPLNDE DLDGNGHGTH 360
CAGTIASKHY GVAKNANVVA VKVLRSNGSG TMSDVVKGVE YAAKAHQKEA QEKKKGFKGS 420
TANMSLGGGK SPALDLAVNA AVEVGIHFAV AAGNENQDAC NTSPASADKA ITVGASTLSD 480
DRAYFSNWGK CVDVFAPGLN ILSTYIGSDD ATATLSGTSM ASPHVAGLLT YFLSLQPGSD 540
SEFFELGQDS LTPQQLKKKL IHYSTKDILF DIPEDTPNVL IYNGGGQDLS AFWNDTKKSH 600
SSGFKQELNM DEFIGSKTDL IFDQVRDILD KLNII
636Fasta Sequence
>P09232|PRB1|Saccharomyces cerevisiae (strain ATCC 204508 / S288c)(Baker's yeast)
MKLENTLFTLGALGSISAALVIPNLENAADHHELINKEDHHERPRKVEFTKDDDEEPSDSEDKEHGKFHKKGRKGQDKESPEFNGKRASGSHGSAHEGGKGMKPKHESSNDDDNDDKKKKPHHKGGCHENKVEEKKMKGKKVKGKKHHEKTLEKGRHHNRLAPLVSTAQFNPDAISKIIPNRYIIVFKRGAPQEEIDFHKENVQQAQLQSVENLSAEDAFFISTKDTSLSTSEAGGIQDSFNIDNLFSGYIGYFTQEIVDLIRQNPLVDFVERDSIVEATEFDTQNSAPWGLARISHRERLNLGSFNKYLYDDDAGRGVTSYVIDTGVNINHKDFEKRAIWGKTIPLNDEDLDGNGHGTHCAGTIASKHYGVAKNANVVAVKVLRSNGSGTMSDVVKGVEYAAKAHQKEAQEKKKGFKGSTANMSLGGGKSPALDLAVNAAVEVGIHFAVAAGNENQDACNTSPASADKAITVGASTLSDDRAYFSNWGKCVDVFAPGLNILSTYIGSDDATATLSGTSMASPHVAGLLTYFLSLQPGSDSEFFELGQDSLTPQQLKKKLIHYSTKDILFDIPEDTPNVLIYNGGGQDLSAFWNDTKKSHSSGFKQELNMDEFIGSKTDLIFDQVRDILDKLNII
|
| Keyword |
KW-0034--Amyloid
KW-0181--Complete proteome
KW-0903--Direct protein sequencing
KW-1015--Disulfide bond
KW-0325--Glycoprotein
KW-0378--Hydrolase
KW-0640--Prion
KW-0645--Protease
KW-1185--Reference proteome
KW-0720--Serine protease
KW-0732--Signal
KW-0926--Vacuole
KW-0865--Zymogen
|
| Interpro |
IPR000209--Peptidase_S8/S53_dom
IPR023827--Peptidase_S8_Asp-AS
IPR022398--Peptidase_S8_His-AS
IPR023828--Peptidase_S8_Ser-AS
IPR015500--Peptidase_S8_subtilisin-rel
IPR009020--Prot_inh_propept
IPR010259--S8pro/Inhibitor_I9
|
| PROSITE |
PS00136--SUBTILASE_ASP
PS00137--SUBTILASE_HIS
PS00138--SUBTILASE_SER
|
| Pfam |
PF05922--Inhibitor_I9
PF00082--Peptidase_S8
|
| Gene Ontology |
GO:0000324--C:fungal-type vacuole
GO:0000328--C:fungal-type vacuole lumen
GO:0004252--F:serine-type endopeptidase activity
GO:0009267--P:cellular response to starvation
GO:0007039--P:protein catabolic process in the vacuole
GO:0030435--P:sporulation resulting in formation of a cellular spore
|
