ID C5KE86_PERM5 Unreviewed; 462 AA.
AC C5KE86;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=Pmar_PMAR020947 {ECO:0000313|EMBL:EER17206.1};
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:EER17206.1, 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; GG672253; EER17206.1; -; Genomic_DNA.
DR RefSeq; XP_002785410.1; XM_002785364.1.
DR AlphaFoldDB; C5KE86; -.
DR MEROPS; C19.001; -.
DR EnsemblProtists; EER17206; EER17206; Pmar_PMAR020947.
DR GeneID; 9053431; -.
DR InParanoid; C5KE86; -.
DR OMA; HINTKLI; -.
DR OrthoDB; 166948at2759; -.
DR Proteomes; UP000007800; 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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR041432; UBP13_Znf-UBP_var.
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 Pfam; PF17807; zf-UBP_var; 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 Hydrolase {ECO:0000313|EMBL:EER17206.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:EER17206.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007800};
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 184..302
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 344..462
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 443..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 462 AA; 51230 MW; 6757D323C68D10BC CRC64;
MSRAVELVKQ YASTGRIKVP QFGDTVHNDS CVLSMDTPLY PVEGLYVSLE EGWKGYGRPF
LDVDINNHDI SSASGAVVYL HINTKLIPKK KEDDDEEKEP TKLAIGVQGG FDGGKDYEEE
KDYRIAVVPY CNGKADTEWL YLSLDDLSDL PEIVGEAVFA IIDHKGAEDD AAVMAWEAGE
EERPVSKYAA ELVQEVPVKR ISPNSADWYC EKSGDRENLW LNLSDGYIGG GRRNWDGSGG
SNGALEHYLE MKDQGKMYPL VVKLGTITPK GVADVFSYAE DEDTMVSDPK LAQHLEHWGI
DVMKMSKTDK SMAEMEVELN KEFAFDRITE AGKELDRVRG PGLVGLRNLG NSCYINSFLQ
LIFSGSVEAL KRRYVDENGV LRRSMAQKGA LDNEGSPQRT VLEVAKLTNA LNGTRYCPPI
PQGEEERKLD PFNGMLAPVS LRKHFGKGHP DFSTSSQQDA AE
//
