ID A0A0N4YIR8_NIPBR Unreviewed; 492 AA.
AC A0A0N4YIR8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=NBR_LOCUS16821 {ECO:0000313|EMBL:VDL80416.1};
OS Nippostrongylus brasiliensis (Rat hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Heligmosomidae; Nippostrongylus.
OX NCBI_TaxID=27835 {ECO:0000313|Proteomes:UP000038043, ECO:0000313|WBParaSite:NBR_0001682001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:NBR_0001682001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL80416.1, ECO:0000313|Proteomes:UP000271162}
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,
CC ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP14/UBP6 subfamily.
CC {ECO:0000256|ARBA:ARBA00008739}.
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DR EMBL; UYSL01022412; VDL80416.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4YIR8; -.
DR STRING; 27835.A0A0N4YIR8; -.
DR WBParaSite; NBR_0001682001-mRNA-1; NBR_0001682001-mRNA-1; NBR_0001682001.
DR OMA; FKSDAEY; -.
DR Proteomes; UP000038043; Unplaced.
DR Proteomes; UP000271162; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
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; IPR019954; Ubiquitin_CS.
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; PF00240; ubiquitin; 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; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000271162};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 2..69
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 100..464
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 72..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 55978 MW; 21E3DC4D00588EF5 CRC64;
MPNVNVKWGK EKYEVLADLN EPPLVFKSQL FALTGVPPDR QKVVVKGKTL GDESWTGISI
SDGAMIMMMG SADAVPAPPK PEEQRAEAER ENEKTLKLPS GLKNLGNTCY MNSVLQSFKT
IPELKDGLRC LRQEGQSTNA DKKMALAVKS VYEMLDNPRR TDEPLVPFFM LQALHGILPQ
FSSRDEHGHL EQQDANECFS EIQRMLLNAL SSNKDAVGKD VREFFRGRYQ VTQKCLESEE
EPKQITSEEF YQLSCFLSAE VRYIQSGIKE KLSGEIEKNS SVLGRNAKWE RNVLIDRLPA
YVSVQMVRFF YKESSQVNAK ILKDVKFPMI LDLCDICTPE LQERLRPQRA AVKKEEDAKI
ERMRKHKMEG TTPKEGEDDG KPLPFSFPDD EGSNNSGFYE LKAVITHKGR SSNSGHYVAW
VRLEEDKWAM CDDEHVSPVT SDQVLKLSGG GDWHCAYVLL YGPRIVKEYP EMKEEKENIV
EQTKEMESMQ TN
//
