ID A0CFU2_PARTE Unreviewed; 946 AA.
AC A0CFU2;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=GSPATT00038101001 {ECO:0000313|EMBL:CAK69659.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK69659.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK69659.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK69659.1,
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}.
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DR EMBL; CT868071; CAK69659.1; -; Genomic_DNA.
DR RefSeq; XP_001437056.1; XM_001437019.1.
DR AlphaFoldDB; A0CFU2; -.
DR STRING; 5888.A0CFU2; -.
DR MEROPS; C19.022; -.
DR EnsemblProtists; CAK69659; CAK69659; GSPATT00038101001.
DR GeneID; 5022841; -.
DR KEGG; ptm:GSPATT00038101001; -.
DR eggNOG; KOG1870; Eukaryota.
DR HOGENOM; CLU_001060_7_1_1; -.
DR InParanoid; A0CFU2; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 InterPro; IPR002893; Znf_MYND.
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; PS50235; USP_3; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1..115
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 334..946
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 785..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 946 AA; 110923 MW; B6B95DDDD4CED4C2 CRC64;
MSDLVQFKEL RQKGIDEFHT SNDMVYNIIS KKWLEEWLES KEKDHPIDNY SCVNSDLLQS
KSSTIFKYDP IQSHMWNKIM LPNLQEGVDY EILDKASWEF IAKKYHTTAI ERDATIVNGK
KQVNVNLVPL NFGAVFPSSL RKYNGGKTAS LIKGDQYVSR TCKLQSFIEL LASTLQTVSG
YEFLRRDGIR LYKAPIGMTI SEIEKHISEE IKNLGTYDDV VFDFKDGDYL DPTKYETIDD
CQIAPGQVIL GDFKEVQKNW VIKHPFFPME GKCEGCYNFK VLQFPCECKK VSYCTEECKK
KDEAYHLPRC EKTDSDDETM DKLQRIEKSM DGKVGLQNLG NTCFMNSGIQ CIGNTFPIRE
YLLSNQYKQD INELNTLGTK GELAQKFAHL LRRMWYAERT PIPPFSLKRA IGKFQPQFQG
FQQHDSQELI TYLLDGLNED LCRIKQKPYV ERKDYDGRPD FEVAKESWEQ FKLRNDSIIV
DNLYGQYKST LRCPNCNKIS ITFDPYLMVN VSIPQNTTKK LEIQFIDPNL LWDCQTLIYN
YEKTQDPTLG QILQSPEIQD KIQQINPTDL IYICTSAYQH DDTDENDKMS SLRKKLKYKK
LYIRKALQSE LNIEKDNKIC IMIHESFKQN AQYQWKREIT PAFNFYFDKT KTTHADIHKF
IFDIHVGVLA TFEDLPKYQG NNWSEYYEEN ILDKVYYLEF KSNQNWQVEC AYCNAKSCND
CVCAYVQDTC IEKYIQKEPK LEIEVFVVWK RGFKSASSVD ELYNDWLKHH QRKQTDVEEL
PKQLTDQEQT QEVVDDAKQQ ENISDEQSAQ KQNFTTCLVP IEPAIPTIQP TNVQGATEKS
MKLTECLKFS EQPEQLDEEN TWYCNQCKDH VRAFKVMEIY KTPKILIFHL KRFKNSNKFF
KSKLETLIDF PIENFDIREF VQNHHLPSDF ANENPQNSKI NDPYLL
//
