ID A0A0N4ZNK9_PARTI Unreviewed; 851 AA.
AC A0A0N4ZNK9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS Parastrongyloides trichosuri (Possum-specific nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Parastrongyloides.
OX NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0001012200.1};
RN [1] {ECO:0000313|WBParaSite:PTRK_0001012200.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A0N4ZNK9; -.
DR STRING; 131310.A0A0N4ZNK9; -.
DR WBParaSite; PTRK_0001012200.1; PTRK_0001012200.1; PTRK_0001012200.
DR Proteomes; UP000038045; Unplaced.
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 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; 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 SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF74924; Cap-Gly domain; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 463..792
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 851 AA; 97478 MW; D67D9FCD1A8765F1 CRC64;
MYKNVYGNSQ FHPPTNGSRT YYVGPDKLYS SYASPCISPN IVKNGDRIQI RQRASSQNAL
RNPQYTSSNF ERYQNNISTS NSMQFPQSRN GEIYNGQYIQ LSPKNNTYND NYSSSNSVIV
SSNTYDGISQ QYYNSTKPLI NGGPVVKKKE DHSIRKAIGK GINKGIDLIK PKSHTKSSKV
IPYLPNNVIS DYSRTSFDLS ERILFCDEEG GKRFGTVTYS ALLSSPSLDN FIGIQCDDDE
IGYGNGELNG KRYFLCEDGK AAFVHSQTCW KMSDYEYQRT KNEEKKAREI AENELKRRLK
PDDQVLVKYL EYKKDAIFEY SFISNDNRNY AIVTIINDRT PPTWKKISRS LASIIPERIM
TKIEKNHNST AVVPLSALTI KTPLHSSPKR IIDYPMPIEP SGAPPSYVES FQHEPIMVQQ
SNSHYQQQNH QGSIKHFGNI DSGIEERPCD PCKNYDSLIG RFKGIQGHNN SCYLDATLYS
MFLQSTEFDS LILEKKKTSE DIKEFSEVQR ILKNEIVYPL RKFHFVRADH ILKLRVLLGK
ILNDQIGMTE NEKDPEEFMN ALFEKVFKIK PLLRLRNNND GKIHDTFFCP LIADDSWTFQ
QSKLMNLQYL FDRSIFSSTI ELAEIPNLLI IQLPRSGEVK IFERILPTIT LDISNVVNTN
TKLCRLCRRN VATEKCPECF LTKECYLKDV FYCSRCFKDS HSDGNSSTHV PCEVITKNPS
SQPKKILLKL SAVLCIETSH YVSFVNCNVN SATPENDRWV FFDSMADREG LSEGYNVPTV
KQVPNLSKWL TDEGGRKIYE LLSQSGWSLP EHGDYDPLLK RLLADCYICI YQYTDELNDS
ERGYIKSSSR V
//
