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Protein

Ubiquitin carboxyl-terminal hydrolase 4

Gene

DOA4

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Ubiquitin thioesterase that acts at the late endosome/prevacuolar compartment to recover ubiquitin from ubiquitinated membrane proteins en route to the vacuole. Removes also ubiquitin from soluble proteins targeted to proteasomes. Is essential to maintain a normal level of free ubiquitin. Required for promoting coordination of DNA replication and avoids DNA overreplication (By similarity).By similarity

Catalytic activityi

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

Enzyme regulationi

RFU1 is an inhibitor of deubiquitination activity.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei441 – 4411NucleophilePROSITE-ProRule annotation
Active sitei752 – 7521Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. cysteine-type peptidase activity Source: UniProtKB-KW
  2. ubiquitinyl hydrolase activity Source: InterPro

GO - Biological processi

  1. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Protein family/group databases

MEROPSiC19.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 4 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme 4
Ubiquitin thioesterase 4
Ubiquitin-specific-processing protease 4
Gene namesi
Name:DOA4
Synonyms:UBP4
Ordered Locus Names:KLLA0E10275g
OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic identifieri284590 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
ProteomesiUP000000598: Chromosome E

Subcellular locationi

Cytoplasm By similarity. Late endosome membrane By similarity; Peripheral membrane protein By similarity

GO - Cellular componenti

  1. late endosome membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 796796Ubiquitin carboxyl-terminal hydrolase 4PRO_0000376820Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ9HFS7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini170 – 294125RhodanesePROSITE-ProRule annotationAdd
BLAST
Domaini432 – 794363USPAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C19 family.Curated
Contains 1 rhodanese domain.PROSITE-ProRule annotation
Contains 1 USP domain.Curated

Phylogenomic databases

eggNOGiCOG5533.
HOGENOMiHOG000248489.
InParanoidiQ9HFS7.
KOiK11839.
OMAiEDLNQCG.
OrthoDBiEOG7R2BSX.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
InterProiIPR001394. Peptidase_C19_UCH.
IPR001763. Rhodanese-like_dom.
IPR018200. USP_CS.
IPR028889. USP_dom.
[Graphical view]
PfamiPF00581. Rhodanese. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]
SMARTiSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9HFS7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLEHNSKLFC KSLSQLSAVA SKVVAEDVEG EHFKQLLAKC IDTLSIYKSE
60 70 80 90 100
LRKLSCASKD TPPSQIYQLN ETLYVYYKIV SQIASQVIPG LAEFQQIKMN
110 120 130 140 150
SKKDSKDKEL LEIYSRLVSA LANDKQIGEV KRFIKNHSEE AAHDGTQHSY
160 170 180 190 200
ENGEFVSISQ LHSLIRHDND SSGILLVDIR PRMDFNDGHI KHNNVICIEP
210 220 230 240 250
ISFKESYTDS DILRKSLITA SDREVDLFKN RDKFRLIVLY TDTDEHTKYY
260 270 280 290 300
WQQLEVLQDI LCNRSFDKPL HHTKVIVLQN GVNAWKEKYP MELKKIMESA
310 320 330 340 350
ISDIRTKPVE HNFHPMALSN NNNIEKANSP SHSQTTSFTH YPDAPFLTNG
360 370 380 390 400
ASIKTAGLVP NQLLPSTSNL TKALQQNDEG NSEPYKLQPN GIKNHRQESN
410 420 430 440 450
NHANGTNCIV SSNGNNSVAK SGHPSINLDF AIGLVNLGNS CYLNCIIQCL
460 470 480 490 500
LGCHELSYIF LTNSYRKHVN VNSRLGSKGL LANYFSQLVQ KMYQQGKLQA
510 520 530 540 550
YNNTNMESTA VHPTQFKLAC GSINSLFKGK QQQDCQEFCQ FLLDGLHEDL
560 570 580 590 600
NQCGTNPPLK ELSPEAEKMR ETMPMRIASA IEWERYLTTD FSVIVDLFQG
610 620 630 640 650
QYASQLRCKI CAHTSTTYQA FSVLSVPVPR ARSCTIYDCF KEFTKLETLE
660 670 680 690 700
KDELWYCPYC KQRQPSTKQI IITRLPNNLI IHLKRFDNMM NKNNVFVNYP
710 720 730 740 750
NELDLTGFWI DDYNGEMPKD NGVSLPLRGQ KPPFNYRLFA VASHSGTLYG
760 770 780 790
GHYTSFVDKG RVGWCSFDDV SWRKIRRKDE YITPNAYVLF YRRVNM
Length:796
Mass (Da):90,929
Last modified:March 1, 2001 - v1
Checksum:i09A9F905579C14B2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF303215 Genomic DNA. Translation: AAG17929.1.
CR382125 Genomic DNA. Translation: CAG99500.1.
RefSeqiXP_454413.1. XM_454413.1.

Genome annotation databases

GeneIDi2894137.
KEGGikla:KLLA0E10275g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF303215 Genomic DNA. Translation: AAG17929.1.
CR382125 Genomic DNA. Translation: CAG99500.1.
RefSeqiXP_454413.1. XM_454413.1.

3D structure databases

ProteinModelPortaliQ9HFS7.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC19.005.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2894137.
KEGGikla:KLLA0E10275g.

Phylogenomic databases

eggNOGiCOG5533.
HOGENOMiHOG000248489.
InParanoidiQ9HFS7.
KOiK11839.
OMAiEDLNQCG.
OrthoDBiEOG7R2BSX.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
InterProiIPR001394. Peptidase_C19_UCH.
IPR001763. Rhodanese-like_dom.
IPR018200. USP_CS.
IPR028889. USP_dom.
[Graphical view]
PfamiPF00581. Rhodanese. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]
SMARTiSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the deubiquitinating enzymes of the yeast Saccharomyces cerevisiae."
    Amerik A.Y., Li S.J., Hochstrasser M.
    Biol. Chem. 381:981-992(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Genome evolution in yeasts."
    Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.
    , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
    Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

Entry informationi

Entry nameiUBP4_KLULA
AccessioniPrimary (citable) accession number: Q9HFS7
Secondary accession number(s): Q6CNS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: March 1, 2001
Last modified: January 7, 2015
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.