ID A0A3Q0KQ07_SCHMA Unreviewed; 893 AA.
AC A0A3Q0KQ07;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183 {ECO:0000313|Proteomes:UP000008854, ECO:0000313|WBParaSite:Smp_152000.1};
RN [1] {ECO:0000313|Proteomes:UP000008854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Puerto Rican {ECO:0000313|Proteomes:UP000008854};
RX PubMed=22253936; DOI=10.1371/journal.pntd.0001455;
RA Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A.,
RA De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C.,
RA Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J.,
RA Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A.,
RA Zerlotini A., Dunne D.W., Berriman M.;
RT "A systematically improved high quality genome and transcriptome of the
RT human blood fluke Schistosoma mansoni.";
RL PLoS Negl. Trop. Dis. 6:E1455-E1455(2012).
RN [2] {ECO:0000313|WBParaSite:Smp_152000.1}
RP IDENTIFICATION.
RC STRAIN=Puerto Rican {ECO:0000313|WBParaSite:Smp_152000.1};
RG WormBaseParasite;
RL Submitted (DEC-2018) 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|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR AlphaFoldDB; A0A3Q0KQ07; -.
DR STRING; 6183.A0A3Q0KQ07; -.
DR EnsemblMetazoa; Smp_152000.1; Smp_152000.1; Smp_152000.
DR WBParaSite; Smp_152000.1; Smp_152000.1; Smp_152000.
DR InParanoid; A0A3Q0KQ07; -.
DR Proteomes; UP000008854; Unassembled WGS sequence.
DR ExpressionAtlas; A0A3Q0KQ07; baseline and differential.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
DR CDD; cd00158; RHOD; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR015063; USP8_dimer.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF104; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF08969; USP8_dimer; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR SUPFAM; SSF140856; USP8 N-terminal domain-like; 1.
DR PROSITE; PS50206; RHODANESE_3; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000008854};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 147..272
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 540..878
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 326..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 80..107
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 326..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 893 AA; 103076 MW; 34CFF1376653E070 CRC64;
MNKKQLYLAH SVDELKKLSK INIRSTVPAV LQREMSLLKC QANEVWEHDE ERAYVLFMKY
FEYYDKLKRL TGNKCSALLK NELLSSIERA EILRDSLKAR YEDLSRQTLP DVKRTIEPQQ
NHKPDKPQNV ISSFWIQTNE LAELIKKQHK FLLIDARSKI EFEQCRIAFD NTINLPYDII
KRGTTVNNIS DYLQKNDFFK KLWDNRSKFD DIILLDENGF DSDQSVLNKN HPLQILKDAM
LKWDAEQVLT AEPRILFKGM KDFRMRYPPL LIQTTISFNQ KDSRQINPQL EAPKFQYPDL
NIREEQLPTV NLADLLASQS KDPTLSFKTI QNGRTGMNDG TSSVFKRPLA PKPSTFNNRV
QYTPKMMSSQ SPEISLNNIR QTNSPVDHRL GVVSSGLSNL SVGKSDLYST NISSNLTLPY
GSIKGDEDMK DNVWKLSDDN LDEEPLAYCD YHDKLHPDST LNKLSGQIIE NTINRSNGPY
ANPWKASLSM SPSSVSLQSV PSIPPSETKP TNILHSHSSL TSFNQSDVPN NQAIHQTRTN
GLRNLGNTCY INSVVQSLSH TRALVHYFLD GFHERQAVVS NRLGYGGEIV KHFEMLLSAL
YNQPNQDAEL YKFRSAVAKH QSKFSSNDQQ DSLEFLLFLL DGLHEDLNEA RSEKNNNSTK
LKHNESMIEY TSSNEQAEAA WIQHKDFNNS IIVSSFQGLL RSTVKCNSCH VTSTTFDVFM
VLSLPIEQNK CQLTDCLKLF LEKEEMVGQC RWHCPSCNTR RDASKWIELW KLPTYLIIHL
KRFRYEYGNW RKQTTNVDFP IECLDMSSFI VGPKLHSSEY ALYSVLNHRG TMESGHYTTF
CRNIRDGRWY EYDDENVSLL DKNEIQNDNA YILFYELLPR VGVFFENTHN MVR
//
