ID J9IEA3_9SPIT Unreviewed; 1418 AA.
AC J9IEA3;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=OXYTRI_06384 {ECO:0000313|EMBL:EJY72618.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY72618.1};
RN [1] {ECO:0000313|EMBL:EJY72618.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY72618.1};
RX PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT with 16,000 Tiny Chromosomes.";
RL PLoS Biol. 11:E1001473-E1001473(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJY72618.1}.
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DR EMBL; AMCR01014965; EJY72618.1; -; Genomic_DNA.
DR EnsemblProtists; EJY72618; EJY72618; OXYTRI_06384.
DR OrthoDB; 653068at2759; -.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:InterPro.
DR CDD; cd00756; MoaE; 1.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR Gene3D; 3.90.1170.40; Molybdopterin biosynthesis MoaE subunit; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR036563; MoaE_sf.
DR InterPro; IPR003448; Mopterin_biosynth_MoaE.
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; PF02391; MoaE; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR SUPFAM; SSF54690; Molybdopterin synthase subunit MoaE; 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:EJY72618.1}.
FT DOMAIN 398..564
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 788..1415
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 167..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1418 AA; 165837 MW; 470EF18917E8EF37 CRC64;
MSIKCQIFKD EKLPDLQSMT DDLKLPECGA VAAFSGITRN NFNGKKVKTL YYECYESMAL
KEMHKLSEKA IIDYNLSGIA VYHRVGECPI SEASVNIVAV SPHRKEALQA VAWAIDELKM
KVPIWKKEYY EDGEIKESPH CHRCEESKHD HGDNSQHNHD KVVDQQLQQD DQSNSGSSVQ
GTNIKGRSIN NESQPPKTQQ TTQNGDQQDT LPKDFATFAQ QYQDKLRDNF LQKQKDGDFD
SFMSITNDEA QQTLRQIHEQ YKSGKVNEQI FRGLMQLYLS MKHKLSKQLK EGLRRSVEQN
LMYSLWYIFI YLTISESEVF NSYSDQVLLI LFKLQEEESD DEDINSKDLS ISIEEQQKQK
LHKQLIQVQK YKKQKLGEMH EDFPLLKKHK KIIYLSCEEL REQATRVKQM IMKMPSIPKQ
AGEEYFIVAI DWWKKWKEYT QYDTIEATDD SDLSPQFSNS VNLENSSNNH DTSSNSKQQK
KPKHNMNQDK ETLQLLYPGE INQTDGFSEM QTDLSYLKHS QQEGDIYHIK TSCKEDEHFA
ILPKDAFEYL IEIYDGIRVP RYSIELTTED DEEQEEEQTI DKPESSKQEE NKSSKNLKTK
KQRQFMIEIF LKPVLLYILP KLRTHPNLKK PAYVFISRRA KVLDLRIKLA EILSHSKKDQ
TTAEQLMNIA RIWRLEVGEN VLQIEKEFDM ETRDNLPMPL SGKVLLNEEI IEEINVADND
VLLYEVQSLP YLKNNNMFAF IPKDLVQKEK RSKNSVIKSL KAEDLNEEQL MKIPLEKCME
RESRGGLVGL QNLGNTCFMN SVIQCLANTE PLVKYLVYGC YEDHINKRNT LGTRGRLASV
FSDLLTEMYI GTNSYVAPWD VKNVISRRAI QFQGFAQHDS QEMLSFLLET LHEDLNDVSA
KPYVEYKDFD GRKDDIISTE YWEGFKKREK SLFVDLFYGQ LKSRVQCTVC NKISISFDPF
NMLSVPIPQT KEQKVTIKYF PYKFEEEHKE FTLVVGEQFN LREIRQKILE NQSPESQCKE
LFLTKVKNKS AIYLLDNDRA TRNNLEKGEE FCAFENPNNS DLSDNYFLIE LKINQHKRSY
FVMSGIQTLT YSRLLVLDKR MTVREVKLAI FKQLRFLIKT PDIPTISKER RKNMNEQKLL
EEEFNWYFNN KDNQSGSFEA GNPLYSIYVN NNLPMSEGYI YSSQAECDLC NKSHKGQNCL
FDFKDQMTLR QIVDKLKYDR DLELVVQFNS NPQANLKPLE NLQFKQVNLS FGASNQVMKK
SGISIYDCIS WFSQEETLTG NDKWYCSQCK QHQNALKKME LYRAPEFLII HLKRFSHQRA
SFFSSRKIQE LIDFPVEGLD LRNYCLQSSS NKEQYIYDLY AVSNHYGSLN GGHYTAFAQN
PINKRWYEFD DSDVSRIDSS KIATKASYVL FYRRRQKK
//
