ID A0A2A2JEX8_9BILA Unreviewed; 825 AA.
AC A0A2A2JEX8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=WR25_19548 {ECO:0000313|EMBL:PAV60062.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV60062.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV60062.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV60062.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm,
CC perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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:PAV60062.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LIAE01010489; PAV60062.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2JEX8; -.
DR STRING; 2018661.A0A2A2JEX8; -.
DR Proteomes; UP000218231; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR11830; 40S RIBOSOMAL PROTEIN S3A; 1.
DR PANTHER; PTHR11830:SF3; CYLINDROMATOSIS, ISOFORM D; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF74924; Cap-Gly domain; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 223..266
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 444..756
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 825 AA; 93087 MW; 59BBB5CDCFBC58B7 CRC64;
MSTDFHRSHA PKPIHYYSPH NVYPPQISTK SPISNFDRAA PSRTRVIPIE RKDSPKSLSN
SNSSFSPASS SHASLQPYYD RPNNGFDLLT NDGIPNPRTG GEQFENDIRN WNGGSSLRRR
PSAEPEHSSF GRRDHSDNRS KEDIVRERRI SGPGDQRRSR EDEKSTNRET MLRSQSKSRL
TASQLRDISY TTISVDDPML TQRVSVGDRC IWSGHPCTVR FIGYLKGHAS IYAGVEFDDK
VGKGTGAFEG ETVFRAPDGH AGFVILSALE KLNDVPNSHD SRPPPPYHQV APSKPEDFLI
NGLDIGSRVS ANYVGAIRSG TVKWIGDSMS DERDRIMKCA VVQLDSEPPS GWRLASDDPD
LSINFSEPRC VILPYNPQTL KACPTGSGSN GSNGDVEMAD ASSNPFSSHH QEPERVDFGN
LDSDVQLTKV YPTRNKEDLI GRMRGIQGHR NSCYLDSMLF AMFSQTTVYD HLLDRIPRSD
DVPQLKELQR ILATEIVYPL RKSHYVRADH VMKVRELLQS ILPNMKGLTT EEKDPEEIIN
EVFGKIFKAP PAVRFIKDNK IDSMHICPII VEEWSQGIVT TQHLLERHMV ASNVRFAEPP
KTLIIQLPRY GQQKLFDKIL PLESINITPL VDRATVKCGF CDSPAVVHCP ECYLCNRVFL
SEVSYCKSCF HKHIEHKEFA DHLPHPYKSS SKKPHNYRMS LTAVLCIETS HYVSFVRTLS
GEWVFFDSMA DREGYSNGYN VPIVKQCEGI SYWLSNDAWK RLRNADEQQV KQIFGRGSTE
ADPLVCRMLS DSYFCFYEEE PYSPKSMASS SSSNSLLSVF KKNSS
//
