ID I7M5W9_TETTS Unreviewed; 1170 AA.
AC I7M5W9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 2.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=TTHERM_00825230 {ECO:0000313|EMBL:EAR83728.2};
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:EAR83728.2, 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};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; GG662507; EAR83728.2; -; Genomic_DNA.
DR RefSeq; XP_001031391.2; XM_001031391.3.
DR AlphaFoldDB; I7M5W9; -.
DR STRING; 312017.I7M5W9; -.
DR GeneID; 7830905; -.
DR KEGG; tet:TTHERM_00825230; -.
DR eggNOG; KOG1870; Eukaryota.
DR InParanoid; I7M5W9; -.
DR OrthoDB; 653068at2759; -.
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; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 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; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF24; USP DOMAIN-CONTAINING PROTEIN; 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; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:EAR83728.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000009168}.
FT DOMAIN 149..286
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 507..1169
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 428..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1170 AA; 135887 MW; 030C742A5862B39D CRC64;
MDKQTQISLG TYKICYEESK NQKDYQKALK YILQVTGQKA EYEKQWHSEI IECLLALKLY
NQCVKKIDSA LKSISKQDYT AQLENYEALV VSYLGLYNLP KANECIKHMD SLLSKLSSSS
EQKQGQKDFS QIIQDLKFKV DGFNIISQDQ RLKQAEEYRK LELSDEDSQF FKKAGQEVYL
IPTQWLNKWK EFSSYKEKFE QSDNMEDEED SKKTIDQIYP GPIDASNLVE TYVKNHLIDA
NQDQFFENYV LKSDKAEKHD FEIVSKQIGD FLYEKYGGFK VKRMTILNPI TNEVNVELFF
KKINFIPIPT LSPDQKEDSY YTIYISKFAS LKQLNDKIKR SLEFLPQKKN QILNRQYFKL
WKLSTDLMKN YQNVYKTMAQ KYREPTIQLD VKDIVIGEDE CIDDMQLTDS EIILYELSET
NNFKIVPCPQ RKQSSKKESE NKEDYQQQSI NQNSQSTEII DESDEIEGFP TGKIKIRRID
ESHVRNMMQK YRIQNGQKGF SGKKGLCGLQ NLGNTCFMNS ALQCLSNVEE LTTFMVNNEY
VNDLNPDNPL GANGHLAVSY ADLVRDIWQG GDSSVSPHYL KKVIGKFAPQ FYGYSQQDSQ
ELLSYLLDGL HEDLNRIKKK PVVEAIDYSG GKDQEMSLEF FKNYKKRNDS VISDLMVGQF
KSTLVCPDKN CGKISITFDP FLTLSVPIPR VTKEDVSFYI IFKDPRKTPY KIETQIRSDS
SLGELKKQIS DNLNIPCQSL IFANNAQSKI EEFLKDDERG VHIKEISGIC FVYEVEKVGT
SIKDINQKSQ QDMEEEEQEQ DKEESPQNKK TSPITQNDGD QIDVEEEEEQ KVQNSKKSVS
HDFVYTEIEF CQIMESDVKL NSNVSNTDIH NVSYSRLVSL KYNSKVQDLY LQIYRIVRVY
LHTYQQANGQ PEVKIDIDIA NDSRENLLKE LSDLENNPQQ KCLFRIFNKD MTPIDYKSQE
PLISLRVKTQ NRLKVKMVLD HKIEVKLMRT KRCESYNFES QKTSKEVSSG SADLYDCIDA
FVKKEQLEKG NEWYCSKCKR HVLATKQMEI YNTPKILIIH LKRFKSGNVR NFGRYYFESG
GKKINDLIDF PIENLDMTKY VLGSNGKPQI YDLFAVSQHY GGMGGGHYTA CAQNFLNKRW
YNFNDSHVSQ SSAEQAVCSA AYVLFYRRRD
//
