ID A0DMZ0_PARTE Unreviewed; 482 AA.
AC A0DMZ0;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Chromosome undetermined scaffold_57, whole genome shotgun sequence {ECO:0000313|EMBL:CAK84407.1};
GN ORFNames=GSPATT00018612001 {ECO:0000313|EMBL:CAK84407.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK84407.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK84407.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK84407.1,
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; CT868507; CAK84407.1; -; Genomic_DNA.
DR RefSeq; XP_001451804.1; XM_001451767.1.
DR AlphaFoldDB; A0DMZ0; -.
DR STRING; 5888.A0DMZ0; -.
DR EnsemblProtists; CAK84407; CAK84407; GSPATT00018612001.
DR GeneID; 5037589; -.
DR KEGG; ptm:GSPATT00018612001; -.
DR eggNOG; KOG1865; Eukaryota.
DR HOGENOM; CLU_030851_0_0_1; -.
DR InParanoid; A0DMZ0; -.
DR OMA; CYAISCV; -.
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; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF104; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 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 PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000600}.
FT DOMAIN 67..160
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 197..481
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 482 AA; 56425 MW; CA6D26874B07A374 CRC64;
MQSYKDTDNN SENLNEEDKQ CNKDYKLSSS INKQVPQFPQ KKAPSYSNEV PQILKLQNQF
RNAQGNTRRE LECQLIKRLV DLKKNSDSDW YRLNGAWAQK YTTYLYDNSS TLPGPIDNTD
LLQKKNLVMN ADFYVVNETV WKFLLEEYSG GPEILDEKIP PSPSSNASST TDRAKSVDIS
IVSYISQLDI NPEIPIKGLK NELYFCYMHS SLQCMMCIQE LNNFILNNIN RQHIQSMPLC
TNYQELLRQL KDTQQDYIKI NSLRNSIAKK FNPKYQHDAQ EFLLFLLSSF EDEIINFNKK
NGQQQTILPN VIDQYLKGKM VSEIHCKNCS KKSQILEDFL SLSLALLKIN SINQSFDEFL
KDELIQDYKC DSCHKKKTAI KKTRITKLPQ YLILHLKRFK FFPKQNKIIQ HIKFSLESSF
CGIKYSLVGI IVHSGSLEQG HYYSFCKRQN KWWLFNDQKI KLVNNNDVLQ QQGYILFYQQ
LL
//
