ID A0A183DPD4_9BILA Unreviewed; 484 AA.
AC A0A183DPD4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=GPUH_LOCUS10575 {ECO:0000313|EMBL:VDN17632.1};
OS Gongylonema pulchrum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Spiruroidea; Gongylonematidae; Gongylonema.
OX NCBI_TaxID=637853 {ECO:0000313|Proteomes:UP000050760, ECO:0000313|WBParaSite:GPUH_0001058801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:GPUH_0001058801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN17632.1, ECO:0000313|Proteomes:UP000271098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-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; UYRT01078042; VDN17632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A183DPD4; -.
DR WBParaSite; GPUH_0001058801-mRNA-1; GPUH_0001058801-mRNA-1; GPUH_0001058801.
DR Proteomes; UP000050760; Unplaced.
DR Proteomes; UP000271098; 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 Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF644; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7; 1.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50144; MATH; 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:UP000271098};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 96..215
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 234..484
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 70..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 54761 MW; 607272DE798A6E42 CRC64;
MGVWTLTFFF FQMTNDLGRG DHVREIRGND VEDDSDLGIC VAEEENKENA RVRVAYVRAP
TQRMIQEEIM DTTDSNGGQQ SPMAGESEED DPYKSEGMLH LDIDHFSDFA RGSSETHQRL
SNPFQNERRS AGRAFGFFLQ CNGEAEAISW SCTASAVLTV RAQKPGVESH VRRINHTFYH
KENDWGYSQF LPCDTLLNPD SGFIKDDTIK LEVIVMADAP HGVQWDSKKH AGFIGLKNQG
ATCYMNSILQ TFFFTNQLRK AVYQMPTEND DPETSVALAM QRVFYELQNS DKPVGTKKLT
KSFGWDSVES FHQHDVQELC RVLLDNLENK MSETKVKNTI PSLFEGKMKS YVRFMESFAD
YTAAEVLDGD NKYDAGEFGL QPAVKGVKFL SFPPILHLQL MRFQYDALQD ANVKINDRFE
FPAVLNLDPF IESSDKKEPQ DFLLHAVLVH SGDFHGGHYV VFINTNLGGP AKVSSLQKFC
LLGN
//
