ID A0E2I4_PARTE Unreviewed; 1029 AA.
AC A0E2I4;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=GSPATT00022673001 {ECO:0000313|EMBL:CAK89501.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK89501.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK89501.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK89501.1,
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; CT868655; CAK89501.1; -; Genomic_DNA.
DR RefSeq; XP_001456898.1; XM_001456861.1.
DR AlphaFoldDB; A0E2I4; -.
DR STRING; 5888.A0E2I4; -.
DR EnsemblProtists; CAK89501; CAK89501; GSPATT00022673001.
DR GeneID; 5042683; -.
DR KEGG; ptm:GSPATT00022673001; -.
DR eggNOG; KOG1870; Eukaryota.
DR HOGENOM; CLU_001060_7_1_1; -.
DR InParanoid; A0E2I4; -.
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; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 1..129
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 280..317
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT DOMAIN 341..940
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 974..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 585..620
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 984..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1029 AA; 121993 MW; 2DFA5E98421DB464 CRC64;
MISEEVQKYK EMEEKFLQEF NSRSGSFFLI SSQWLNNWKK KVGYDGEPNT SISLGNINSD
IGHKPKQVLK YDPIELNPWN TQLKPNLVEG VDYYVIDSNM WQSLKGQQQM CEFRNNKYRS
DFTIERESFL DNEGKRQIQA YLQCIKFVPI FPSAMSKLQA SMIEGEQYIS PIAQISEVVT
ILSKTLKTVT SFKFVSKDNV RLYKLGSSWN LDNLKAFLLQ AQKEKKQFME FTDIEFLDPT
QNKQIKDYNF EKDQILLMDT KEIHSTFLIS NNIFGQEEKC TNCSQYYNLT FNCACKKVKY
CSEACLQQHS YQHTQVCEKQ DDTDEILVNL LPTPQSKLGL TGFRNLGNTC YMNSALQCLS
NTTELSRYFL DNSFKFDINT QNALGTKGEF ASLFSYLLKR LWFDKQTTIS PFQFKRLVGK
LSPNFAGNAQ HDAQEFITFT LDLLNEDLNR VKVKPYVEIP DNNNRPDDEV SQEQWECFKK
RNDSLIVDQL YGQYRSKLQC PNCNKISITF DPYLMVNVTI PQEKKKVLEF YIIDPENFWL
SQPVTHYYEP ELRLKEVLQF KSQEWLNCEW DQIILTLSST FSIEEVFLDQ RLEQLKKQLK
QEKKLQLRKL TEQEQLIQND QQVHVLIHNQ ILTMNNWKKD IVPTMYFILS QNYKYKEIHM
FFFNCFKNVL KNFADFDQSW LNSENLEETY QQHILDKYWK IMFKSNQRFQ VNCSYCYKAY
CNDCPLEFTD KIFGDCFQRE DKLLQPEIQI IWLKPCREKI DDMYTEYQKI FDPNYKAPVV
NINWDNNQKS NKYKQTYTLE HCLEYSTKPE QLQVDNSWYC SGCKDHVQAY KTLQIYKTSK
ILIFHLKRFK DSYKLFKSKL QTNIIYPEKL DMTNFVLHQD NNNLYELYAI CNHIGESGSG
HYTAFCKNNG DWYKFDDSIV TKETNNIVTP NAYVLFYRRI EQNYVEYDLE AKLKQNIDLL
LADEVFKQHL QKFQKENDES VDTQKQEQPA PPKQQEENNQ QLVKLDINLV NNQSSSDTND
GDEENEDEH
//
