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
//