ID A0A132A6J7_SARSC Unreviewed; 687 AA.
AC A0A132A6J7;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Ubiquitin carboxyl-terminal hydrolase 48-like protein 2 {ECO:0000313|EMBL:KPM06509.1};
GN ORFNames=QR98_0049860 {ECO:0000313|EMBL:KPM06509.1};
OS Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC Sarcoptidae; Sarcoptinae; Sarcoptes.
OX NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM06509.1, ECO:0000313|Proteomes:UP000616769};
RN [1] {ECO:0000313|EMBL:KPM06509.1, ECO:0000313|Proteomes:UP000616769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM06509.1};
RX PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT "Draft genome of the scabies mite.";
RL Parasit. Vectors 8:585-585(2015).
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 -!- 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:KPM06509.1}.
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DR EMBL; JXLN01010911; KPM06509.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A132A6J7; -.
DR VEuPathDB; VectorBase:SSCA003407; -.
DR OMA; AWAWIES; -.
DR OrthoDB; 307371at2759; -.
DR Proteomes; UP000616769; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
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; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF722; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 48; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KPM06509.1}.
FT DOMAIN 89..417
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 687 AA; 81247 MW; BE64F6A5177BB283 CRC64;
MSECIDGPEI SIDQRQDSIK SSLEDFDRIL LRYYKLDIGN CKAKKNRNCI SNARCLRGLG
QPQWLIKPRK NSDEIETSDS KSTVHPSYRG LKNLGATCYI NTFLQLWFHN INLRKSIYEW
RPEAISDQVQ NNPIVCLQIV LSMMQFSLRN FVDPSPFIKC LLLNESQEQD THEFLNLFNN
YIQNQLKYEN SIQTTINDQY QMKLAYIIQY DLLSFENFKF SLLLSRCNEC SFVSEKVSES
YELILRVKGF KDLDECIENY FIEERLEGSN KYACQVCDCF REARRCIELR KLPPFLNLQL
MRFESANGLN KKINSFLKFP DKLNMKKFLK SDITDEDIIY HLYAVVIHEG QTANSGHYIT
YIKKNNFWFK FNDENVEKLK DISLKMDNDS EFDGKKNQCE KGFHRSKNAY ILVYRDNRVN
EVESPYSLLD YRLPDYIIEH IEKDNRRYQE EQEKIEQLKN LQLKDERNHQ EKLRQIYESM
ETIEEQTTNL DAIDKNWLVS LFNAKIENDI DSINNEKLLC SHRKLNPNSD FKVIAKKSAD
LIYSFYSFDI RLELPLNYCS KCIFNKITLA NLKQEIDFDS KAIITHSKHK SDLNETMFWV
GKESFKKWKT MRLNLMDSKN DSNEAEGEIG HFNQDLQCPH GNLCSNPNKR RLVREIIWKI
FKKHFPQAKE FTQDSPICPN CQVDLAK
//
