ID C5LMS0_PERM5 Unreviewed; 507 AA.
AC C5LMS0;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=Pmar_PMAR007654 {ECO:0000313|EMBL:EER01961.1};
OS Perkinsus marinus (strain ATCC 50983 / TXsc).
OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC Perkinsus.
OX NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN [1] {ECO:0000313|EMBL:EER01961.1, ECO:0000313|Proteomes:UP000007800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL Submitted (JUL-2008) 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; GG683573; EER01961.1; -; Genomic_DNA.
DR RefSeq; XP_002769243.1; XM_002769197.1.
DR AlphaFoldDB; C5LMS0; -.
DR EnsemblProtists; EER01961; EER01961; Pmar_PMAR007654.
DR GeneID; 9054589; -.
DR InParanoid; C5LMS0; -.
DR OMA; HTECKIS; -.
DR OrthoDB; 160664at2759; -.
DR Proteomes; UP000007800; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd16104; Ubl_USP14_like; 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; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR044635; UBP14-like.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR43982; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR43982:SF1; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000007800};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 5..74
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 114..479
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 365..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 507 AA; 57127 MW; C12C84CCA1336AA0 CRC64;
MSTNIPVVVK WGKATYNIEV NTAESVAVLK TQLENLTSVP HDKQKIMGLP GGLLKDSDDL
SKKITKPNQK ITLLGTAVAQ QLKAPTASTV FVEDLSDEER RKVLKEREVE TLPIGLVNLG
NSCYMNATLQ ALYAVPPLRQ ALLKYYDSSA HSEGSNQERS LSALIHQTFK DLGTKADAVE
PASLFMLLRV MYPETFGKTT QGGIPQQQDA DEFLRALMLN LSDTVKTPHS NVIDDLFGFT
MKTRMRCLEA EAEPESVSEE RHRVLLCHMG TPTDPVGHLY QGVQLSLKET ITKQASVLGR
DAEFEKSSAM DSLPEYLIVE FARFQWKGES TSAGHFPQVL DVYDFCTEDV RKQLTRGRQR
RRVYMDEQER KRIQAKEANR KDSDVEMDAT EEDSSVAQIP TGNYRCVSIV SHEGRSAEGG
HYMGWAKFKE ADGDVFKEDQ WVRFNDDKVT QHDWKYVVDQ LVGGRADTQI AYIVIYQKDK
VPDGSIEEIV DEEMEMESNP DKKKAKQ
//
