Reviewed, UniProtKB/Swiss-Prot Q10171 (UBLH1_SCHPO)

Names and origin

Protein names

Recommended name:
    Probable ubiquitin carboxyl-terminal hydrolase 1
    EC=3.1.2.15

Gene names

Name:	uch1
ORF Names:	SPAC27F1.03c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	222 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Ubiquitin-protein hydrolase is involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin By similarity.
Catalytic activity	Ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol.
Sequence similarities	Belongs to the peptidase C12 family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Proteasome
Molecular function	Hydrolase Protease Thiol protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe nucleus Inferred from direct assay. Source: GeneDB_SPombe protein complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin thiolesterase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 222	222	Probable ubiquitin carboxyl-terminal hydrolase 1		PRO_0000211074
Regions
	Region	44 – 61	18	Ubiquitin binding 1 Potential
	Region	171 – 179	9	Ubiquitin binding 2 Potential
Sites
	Active site	83	1	By similarity
	Active site	158	1	By similarity
	Active site	177	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q10171-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 218317B99BEC35B0	FASTA	222	24,913
	10 20 30 40 50 60 MWRPLENTPE VLEPYLQKIG VQDASVFDLF SLEEIPEYIP RPVHALLFVF PSSGTKTIYK 70 80 90 100 110 120 GSRILPKDSD KVLWYPQTIP NACGTIGLLH AVSNGELRRK VNENDFIKSL IRTAEGSSIE 130 140 150 160 170 180 ERAKLIEDSK ELEALHAAFA GPPLEVEGSE EDVETDLHFI CFVKGKSKDD NHFYELDGRQ 190 200 210 220 EGPVQHSEIE SDLLNAEVLS VIKNYIQSID SPFFSLVAIT TP

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAA93292.1.
PIR	T38461.
RefSeq	NP_594531.1.
3D structure databases
HSSP	HSSP built from PDB template 1CMX based on UniProtKB P35127.
ModBase	Search...
Genome annotation databases
GeneID	2541733.
KEGG	spo:SPAC27F1.03c.
NMPDR	fig|4896.1.peg.4501.
Organism-specific databases
GeneDB_Spombe	SPAC27F1.03c.
Phylogenomic databases
OMA	Q10171. RRPFARE.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-002628-MON.
BRENDA	3.1.2.15. 653.
Gene expression databases
ArrayExpress	Q10171.
Family and domain databases
InterPro	IPR001578. Peptidase_C12. [Graphical view]
Gene3D	G3DSA:3.40.532.10. Peptidase_C12. 1 hit.
PANTHER	PTHR10589. Peptidase_C12. 1 hit.
Pfam	PF01088. Peptidase_C12. 1 hit. [Graphical view]
PRINTS	PR00707. UBCTHYDRLASE.
ProDom	PD350662. Peptidase_C12. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00140. UCH_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UBLH1_SCHPO

Accession

Primary (citable) accession number: Q10171

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)