UBP11_SCHPO
ID UBP11_SCHPO Reviewed; 350 AA.
AC Q9UUD6;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 11;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 11;
DE AltName: Full=Ubiquitin thioesterase 11;
DE AltName: Full=Ubiquitin-specific-processing protease 11;
GN Name=ubp11; ORFNames=SPBC19C2.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12;
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; CU329671; CAB52031.1; -; Genomic_DNA.
DR PIR; T39795; T39795.
DR RefSeq; NP_595689.1; NM_001021586.2.
DR AlphaFoldDB; Q9UUD6; -.
DR SMR; Q9UUD6; -.
DR BioGRID; 277237; 25.
DR STRING; 4896.SPBC19C2.04c.1; -.
DR MEROPS; C19.A63; -.
DR PaxDb; Q9UUD6; -.
DR PRIDE; Q9UUD6; -.
DR EnsemblFungi; SPBC19C2.04c.1; SPBC19C2.04c.1:pep; SPBC19C2.04c.
DR GeneID; 2540714; -.
DR KEGG; spo:SPBC19C2.04c; -.
DR PomBase; SPBC19C2.04c; ubp11.
DR VEuPathDB; FungiDB:SPBC19C2.04c; -.
DR eggNOG; KOG1867; Eukaryota.
DR HOGENOM; CLU_008279_11_3_1; -.
DR InParanoid; Q9UUD6; -.
DR OMA; SWWSAND; -.
DR PhylomeDB; Q9UUD6; -.
DR Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR PRO; PR:Q9UUD6; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; HDA:PomBase.
DR GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..350
FT /note="Ubiquitin carboxyl-terminal hydrolase 11"
FT /id="PRO_0000080611"
FT DOMAIN 49..344
FT /note="USP"
FT ACT_SITE 59
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 302
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 350 AA; 39169 MW; 53986D30F9552DA4 CRC64;
MSTTPLSISR AKKYKTVFKG AAILTTFAAL YIVTSPSTGK RLVKNASIKG LYNVSGNDCF
LNCVLQSLAS QESLLEILKL RCSSSTLYAT LYELLQKLNS GPGNPITPGS FLNSLEIATN
KKLVRSIQQD AQEFLQHLVE TLELQKPHTY KWSKVLSFPV DSPFIGTMEQ KVQCCQCLAI
SISYSTATSI QLCLPPEYSG NSNVSLLSLM EADREQHISD YKCDSCFKSS PKHSKTSCIR
TVDWKNPPTI LQIQLERTSY TCQGLTRNNV SISFPSKLIL KNKHHYILRS LITHSGSVTY
GHYLCYRLQD DIWWKANDSL ITKSSLNEAL SQTRSACLLF YEMESPLALD
