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Database: UniProt
Entry: I7LUY7_TETTS
LinkDB: I7LUY7_TETTS
Original site: I7LUY7_TETTS 
ID   I7LUY7_TETTS            Unreviewed;       853 AA.
AC   I7LUY7;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 2.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   ORFNames=TTHERM_00188880 {ECO:0000313|EMBL:EAR96319.2};
OS   Tetrahymena thermophila (strain SB210).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=312017 {ECO:0000313|EMBL:EAR96319.2, ECO:0000313|Proteomes:UP000009168};
RN   [1] {ECO:0000313|Proteomes:UP000009168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX   PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA   Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA   Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA   Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA   Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA   Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA   Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA   Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA   Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA   Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA   Hamilton E.P., Orias E.;
RT   "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT   model eukaryote.";
RL   PLoS Biol. 4:1620-1642(2006).
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; Evidence={ECO:0000256|ARBA:ARBA00000707};
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DR   EMBL; GG662693; EAR96319.2; -; Genomic_DNA.
DR   RefSeq; XP_001016564.2; XM_001016564.2.
DR   AlphaFoldDB; I7LUY7; -.
DR   STRING; 312017.I7LUY7; -.
DR   GeneID; 7844665; -.
DR   KEGG; tet:TTHERM_00188880; -.
DR   eggNOG; KOG1868; Eukaryota.
DR   InParanoid; I7LUY7; -.
DR   OrthoDB; 227085at2759; -.
DR   Proteomes; UP000009168; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR035927; DUSP-like_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR006615; Pept_C19_DUSP.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR24006:SF733; RE52890P; 1.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF06337; DUSP; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 1.
DR   PROSITE; PS51283; DUSP; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:EAR96319.2};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009168};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          331..435
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   DOMAIN          523..839
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          95..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          447..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..128
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..150
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..181
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..265
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   853 AA;  98181 MW;  349EAC3EBAA89B85 CRC64;
     MDSPNIKSNY YTSSPIQNFI TQATEPDRLI TEFCDFSGLK NSNCEEEIID DDDELVPQVP
     QTLEKKIPLM NKYFRDRTRS DKLFTQTSLQ SLATLKTENE KEKKQSNQNQ EHLESIEQKE
     EEDQILSQQK QQKNEAAEEI GSKIEKSQSK QIKNQEGPNT LEDKQSQQQL EKQEEVEEQK
     QQGRNFSFSN HPQTPKRDSN SSSINLSEQK NSIFDTPKLN SQSPQQLENQ TPSRINQEKN
     QKEQQQPQLI SQRISTESTS TSSSSQIVTV FQMPNFSNSN NYNQCTSLSN TSFSSTQNDN
     NISQTSTKQS DISINETISM LEINEIASKL KRLPAKERKM KELVLIKEWN QDKYYSHIID
     ISWAVQYTKW LSDPHSTASF SLPISNSNLI DYENKTVKKG IKEKINFDIV SSKVYFLMRC
     LYGGGPDIPL SRQSSSTSSK SITEAIKSAQ NVKQPSSGGI GENLFSKQSS STSTAATTNP
     SMLEYHNRAQ KQMIPSQFDN QVIQTADVVR PSQLFKKQAL GVRGLHNQSN YCYLNASVQC
     LLSIPELNSY FLSEEYRRVV KIQGTRKALK IVPVYADMIK LYEKTSENNI LDMNLLKKVI
     KKPFIPHEQH DAQEFIRYIL SEIQDELNPI LPSKNPTQFK DSEEAYQYYL RFQNSIIDYI
     FSGQLSSNVN CSKCGYISRT YDPFLDLSLG MDSKTTSVQD CLNKFFSEEI LSDDYKCEKC
     NQNNKAKKQV LISKTPYILT LHLKRFKIYP KKRKITDFIK YPIQNLSIKQ YVKNSSTSGG
     YYYNLIGIIV HSGSQDSGHY ISYVKRENRW FCCDDGKYQE VSEKTVIKQE VYLLFYQRIE
     ESPEVNQQKK IAQ
//
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