ID A0A0V0YD74_TRIPS Unreviewed; 693 AA.
AC A0A0V0YD74;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=Usp37 {ECO:0000313|EMBL:KRX97922.1};
GN ORFNames=T4E_9451 {ECO:0000313|EMBL:KRX97922.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX97922.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX97922.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX97922.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX97922.1}.
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DR EMBL; JYDU01000026; KRX97922.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0YD74; -.
DR STRING; 6337.A0A0V0YD74; -.
DR Proteomes; UP000054815; 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; cd02257; Peptidase_C19; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
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; 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, ECO:0000313|EMBL:KRX97922.1};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 208..679
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 519..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 693 AA; 79285 MW; 6B4DE7C6CCE3D233 CRC64;
MFKGLVRMTG CFFATQWTPG DWTFFTKASS SHYYLRVRIE SSHAFREYPL CSVQDVPDEV
LETTAYYRLR FVNEICAFIQ LSYDQLLKLH NFVIAAMKDN NNSNAPLLKI EAVEHSNLNK
LEEQLPNSEV NHKDNGLNNE FNTSLVDVIS TMTQDTNEKE NMPILIAETP PSHSKRSRCP
SVSKSEKRPY YITRRTSRRL ANEEQSPYGF SNLGNTCYMN AILQALLHQK PFAQELWRAY
EKSRLLLQPD SLLSHLSNLL RGSSGDLSVN KKDVLLSVKN KIASTARQFH GDSEHDAQEF
ILQLINQLDD EVRALNKSYP ENQISNPVFR NFSFAICSYR KCTKCGHTTC SEEEFVDLPL
DLHSKLQSFS LQKLVEAFFA DGTVNRHCEK CNCDEAFAQS RISRLPRILV INVKRHYFNG
LSSEIRKAEN VISIPLFITL RDFCVSDAVD SADLTLSAKK AYPFHQTDDH EKGKQSRMIL
RNSKVLFRGE DSNCNSEKAA VEDEFDMFAL SPKDDVVEYK QEDEELSSSS SGSSSKRRRS
EKSVLSESLI IGNDARFEED LTEAIRLSII ESQQRDQPKE NCVEVDGPSL NGLNNSLSPG
EEELLRNEQE GFLPRSYKLC AVVNHIGLSC QTGHYITDVY DWKENEWFCF DDSKAKLTSL
REVQQQRKKT GYIFFYVDKK LLTDSVCDFV ETT
//
