ID A0A3P6S0G3_LITSI Unreviewed; 855 AA.
AC A0A3P6S0G3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=NLS_LOCUS684 {ECO:0000313|EMBL:VDK69172.1};
OS Litomosoides sigmodontis (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Litomosoides.
OX NCBI_TaxID=42156 {ECO:0000313|EMBL:VDK69172.1, ECO:0000313|Proteomes:UP000277928};
RN [1] {ECO:0000313|EMBL:VDK69172.1, ECO:0000313|Proteomes:UP000277928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR EMBL; UYRX01000018; VDK69172.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P6S0G3; -.
DR STRING; 42156.A0A3P6S0G3; -.
DR Proteomes; UP000277928; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd22755; OTU_CeDUB-like; 1.
DR CDD; cd02257; Peptidase_C19; 2.
DR Gene3D; 3.90.70.80; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
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:SF733; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE-RELATED; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 2.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000277928};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 286..854
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 643..783
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT REGION 199..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 855 AA; 97061 MW; 372475B159DE427A CRC64;
MLANGSLINV EKDEVLLTDN MHRGFVELCN DGETSLLRIF YLKDGEGRLE WECTQISDLE
RAEDCSSLVF RICRLKSGID CNEHVLIKPE RSKDCHTIYY AFRYLQQKSI DCYCVPLPKL
FKSLFPILGD GKSAIQQKSA VQKRTLVKQL STFHQISVKN QAYVDSNQKK NKKAVPLHVK
NGSQKRKPIT STDIYLDSPN KRLAHKPPKD TTGTLAGPFA VHHPDELLKE DRMLAINSVI
TKGNNPKKEI TNLDDAFLCT HNRNSAPNFS ARFQRLSAGT DGASLKGFLN LGNSCYMNAV
LQGLFHVEAF KDLLNVVPES SECSILSALK ALQKNYEKAA SAMKRCLLEN VFKFLGDERL
EMTEQEDAQE FLTIILEKIN FELESLSNNK NAEENSLSES VMSLSSIFGF ELKHEITCNR
NSVSPSLQML LENCLRSEVV EHICPRCNEK FATMSHEFRS LSKCLIIFLK RYDFKQSASK
RGQRKLKDAI SLSMCIHLVS CNRKQSELKN CFNSLLPISD IVNDDQVSFV LETPPNELVL
SSSSSSDNII EDARQAAQED ALKTIQEIDG FDDEKFSKKI KHSTKSSVIA YDSTTNESLD
YLTLFCLPRL DFCERSCAEL NIRCHFSTVR QEPKPLFCKS IPSSTAPIVA DGNCLFRSIA
LYLSGSDEEH SVVRKNVVEF EEKYDDELRE VNNFSLADWK EHIRKMTNDG EWATEIELLA
LAALLDADIW TFLNGKWLRY RPLYTVGKDG ISHKLPIQKY DDNGKDAIFL INENFHYKPV
FDIISNGTVR DYHLAAVISH KGIGPSNGHY VCDVKNLNRN IWMHFDDSHV EERTEAEVIA
ECAEDGYIFF YVAEN
//
