ID A0A183H8V9_9BILA Unreviewed; 455 AA.
AC A0A183H8V9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=OFLC_LOCUS3921 {ECO:0000313|EMBL:VDO38233.1};
OS Onchocerca flexuosa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=387005 {ECO:0000313|Proteomes:UP000050787, ECO:0000313|WBParaSite:OFLC_0000392001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:OFLC_0000392001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO38233.1, ECO:0000313|Proteomes:UP000267606}
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|ARBA:ARBA00000707};
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DR EMBL; UZAJ01002791; VDO38233.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A183H8V9; -.
DR STRING; 387005.A0A183H8V9; -.
DR WBParaSite; OFLC_0000392001-mRNA-1; OFLC_0000392001-mRNA-1; OFLC_0000392001.
DR Proteomes; UP000050787; Unplaced.
DR Proteomes; UP000267606; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF10; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 77..191
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 233..455
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 455 AA; 51739 MW; 79C10C1E0E5F77E4 CRC64;
MDGILAIGVE GGFCSGPKYD ITNEYAVVLA PDFDKKIPLD RLASKLAQVC QKIIENEGVQ
RQEILEAGVQ VWEGEARVNT RHLNLEQIDN GKRIPPWGWK CEEEGCDLKE NLWLNLTDGA
IMCGRSQYIQ EGVMSKGQNH ARLHFDLTGY PLVVKLGTIT KDDADVFSYD EDDSVRDPNL
KQHLLHFGID MDKTEKTEKS TLEMELDLNQ KWEWEMCQED GANLELVYGP GFTGIINIGS
SCYISATLQM LLQIPDFVQA YGIECEKHFL NVSIFNSHYD FNCQTAKVFS SLLSGEFSQK
DGDCNGIKPV QFRKIVARGN AEFSTTRQQD ADEYIRILFD RIDQFLKKPK PVDAVRFKLE
HRLEDQATNR VRYSYSEEVV LSLNVPEKNA YKQPEQTVET DAPVRPTISF ADCLSATFGR
QEIADFRSPI TNEVQGAIEQ YRIATFPDYL IIQLK
//
