ID A0C651_PARTE Unreviewed; 515 AA.
AC A0C651;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Chromosome undetermined scaffold_151, whole genome shotgun sequence {ECO:0000313|EMBL:CAK66268.1};
GN ORFNames=GSPATT00035397001 {ECO:0000313|EMBL:CAK66268.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK66268.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK66268.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK66268.1,
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).
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DR EMBL; CT868043; CAK66268.1; -; Genomic_DNA.
DR RefSeq; XP_001433665.1; XM_001433628.1.
DR AlphaFoldDB; A0C651; -.
DR STRING; 5888.A0C651; -.
DR EnsemblProtists; CAK66268; CAK66268; GSPATT00035397001.
DR GeneID; 5019450; -.
DR KEGG; ptm:GSPATT00035397001; -.
DR eggNOG; KOG1868; Eukaryota.
DR HOGENOM; CLU_030851_0_0_1; -.
DR InParanoid; A0C651; -.
DR OMA; PPIAEYF; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR CDD; cd02257; Peptidase_C19; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
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; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF888; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 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; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 66..165
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 209..513
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 24..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 515 AA; 60277 MW; 4216D539F2E2FE89 CRC64;
MFICCASNKK PKVVQTQTQI PPLQAQTKQP KYQIRTSNDQ DQHSTNLTNM EGTNDKINLS
LQEVEKFILH DKKTLEQERE LVTKLIELPE KSHLIEFNWA IAYTNYIKNA GLHPGEISNK
ILYDKYKAKE ELVLDKDYVL VNDQVWNVLV NIYKGGPMMT INDLDRKSEI NILDQSLKVF
ASPSMNDLDI KQAKIRHLKQ MSIKELQIVG LENEIYFCYL NSVLQCLMGI PQLNSYFLIS
SQSECKLFSY AYSLLLRKAS KVHYKARIVA KELIKVLQKH FSIYEMHDSS ELLLFILDKF
KEEIFINNAL QLNQLQQCQF KQSITFIDEL FHGQLTSFIK CSDCNKISQH QDPFYDLSLP
LVGKNFMQRK LTIQECLSNY FKEEMIDGGW TCSFCNQKFR TIKRRVKISF APNILVLQLK
RFQVYPLQKK IKEPVVADME LNIKNFCVSE VVDTKYELHS MIVHSGTIDQ GHYVAVVKRN
QNFYLFNDDE IERLSLNQIN RIDSAYLFMY HRKSD
//
