ID A0E8K9_PARTE Unreviewed; 1128 AA.
AC A0E8K9;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=GSPATT00024355001 {ECO:0000313|EMBL:CAK91626.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK91626.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK91626.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK91626.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CT868664; CAK91626.1; -; Genomic_DNA.
DR RefSeq; XP_001459023.1; XM_001458986.1.
DR AlphaFoldDB; A0E8K9; -.
DR STRING; 5888.A0E8K9; -.
DR EnsemblProtists; CAK91626; CAK91626; GSPATT00024355001.
DR GeneID; 5044808; -.
DR KEGG; ptm:GSPATT00024355001; -.
DR eggNOG; KOG1870; Eukaryota.
DR HOGENOM; CLU_273471_0_0_1; -.
DR InParanoid; A0E8K9; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
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 SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Reference proteome {ECO:0000313|Proteomes:UP000000600}.
FT DOMAIN 100..135
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 171..296
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 477..1114
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 1128 AA; 134154 MW; 64FF97A7E82AF514 CRC64;
MGVCCQKNKK SEFTQYQHME EDIWKSKAIF PDQYLKVLEQ RYYALQPEYG LNLEKLSRLI
PNIKSKHLLN RLLKYFNMKM EDQIDFNGIC LLISKFLNAG QTGKIEILFQ LYDLDNDQML
DSKEFNLFIQ ENDNLLDQST RRNQNFTRSK FKTWAEGNLK LDKTMSFKIF LRPDQEKQMI
EQLKDQIKND KVYIISSKWW DNWKQYVNMA TANPGQQIDD VTQKPQQEFI EISSQLWLAR
PGPIDNRDIA GEYEGELKLQ AKQKCDFQEV GEDAWKELLS WYGITDKRLE FKRRGKFDKD
GFKIEVHPTI IQAFETDANG IVQYKKWFKL KMSEDSTMHD VRRKLFQKFQ IKTINGSEYL
LYKMKINEDW ELILDLDDNI SSLNITSGTY FTLTKLKQKP KSKVGNWQLG QKSLIEDPSQ
RVEKMCLAQR FTEDLKYVIL HIEGQSFFDD FQLEIKENHG AQFNSYIQGR SYNIKYPGLQ
NLGNTCYMNA ALQCLINTKY FFNFLFNEGY KNKVKVNNSL VQHLSSLAKE MTQTAELSIS
PSVFQNALVR ICPRFKMYEA QDADEFLDYL LTQISDELKG YDTQQDTVIE TLFQGDYLTQ
KQCSSCQYEM NEPEKNKIFR LKIQEEAGVF KLRLLIFMKL KFIYDRDEQF VVNQKDLLKK
TIILTKNDGS FTMRDLYEKI NSILGLAQNE YEFARSYKKE FIKIFINIDE NQELTKLGIN
QNKTLNLYQL GSIHQAEREF ETISQMFNYP SQDFKLNDLI NFLDPNNQWK QGKIVQVIQS
NPIKYKILYR LQQQNNNQKQ FEYIMDKQKI VKFREKIKHH THEKVPLLHY YFNTFKKQYN
LTLKPIILLL PIQSLSLLEL KVYIYKQVSR FINITHFNVQ SPFKSSNVSQ QEICNFFSNP
SFPYKIRVLD QNRKCLFCEN IRPHNNITQS HCMGCEEDPI LLNFDQFTKP SIILEWKEIK
FAKILEKRKD ELEERSLIHL RLQKCLEKSA EDTFITQECF SCRQNTQIRN NSYLNKPPIM
LIINLQKYKS NGEQIERYID FPLNSLDIKD CRRSKQPVLY DLYAVINNKR GRDITHYTAY
VKKKDEWYEF DDSNVQKVRE VQTKNAYLLF YTIQEIPEDS DISLLNFK
//
