ID A0A095C9V9_SCHHA Unreviewed; 517 AA.
AC A0A095C9V9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE Flags: Fragment;
GN ORFNames=MS3_07513 {ECO:0000313|EMBL:KGB39098.1};
OS Schistosoma haematobium (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6185 {ECO:0000313|EMBL:KGB39098.1};
RN [1] {ECO:0000313|EMBL:KGB39098.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22246508; DOI=10.1038/ng.1065;
RA Young N.D., Jex A.R., Li B., Liu S., Yang L., Xiong Z., Li Y.,
RA Cantacessi C., Hall R.S., Xu X., Chen F., Wu X., Zerlotini A., Oliveira G.,
RA Hofmann A., Zhang G., Fang X., Kang Y., Campbell B.E., Loukas A.,
RA Ranganathan S., Rollinson D., Rinaldi G., Brindley P.J., Yang H., Wang J.,
RA Wang J., Gasser R.B.;
RT "Whole-genome sequence of Schistosoma haematobium.";
RL Nat. Genet. 44:221-225(2012).
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: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KL251133; KGB39098.1; -; Genomic_DNA.
DR RefSeq; XP_012798858.1; XM_012943404.1.
DR AlphaFoldDB; A0A095C9V9; -.
DR STRING; 6185.A0A095C9V9; -.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000245; P:spliceosomal complex assembly; IEA:InterPro.
DR CDD; cd02669; Peptidase_C19M; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR033809; USP39.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646:SF16; U4_U6.U5 TRI-SNRNP-ASSOCIATED PROTEIN 2; 1.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 1..98
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 123..464
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 484..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGB39098.1"
SQ SEQUENCE 517 AA; 59660 MW; BC35991F822252D9 CRC64;
RSCPYLDTIR RNMLDFDFEK LCSVSLSHLN VYACLICGKY FQGRGNSTHA YTHSVSESHH
VFLNLETRRF YCLPDDYEIL DGSLEDITYL LNPTFSTPEI LALDSYSKMV RAYNGLTYYP
GVVGLNNIKA NDYCNVILQM LSHISPLRNY FLDIKKFENL PSVSGDQMML LVQRFSELIR
KLWNPRNFKT HVSPHEFLQA VVLCSKKRFQ ITEQGDAIEF LSWLVNAIDK ALRIKKIPCP
RGAVNKTYKS IVSSTLRGKM RMYSRKIMPV NMTDEEKASL ADSPEYMTSI SDINFFYLTC
DLPPPPLYLD EFKENIIPQV SLATLLSKFN GVTEKEYKTH RDSTLRRFEL RRLPPYLILY
MKRFVKNIFT LEKNPTIVNF PIRSIDFGEL LAPEFRAKHR HTTYDLIANI VHDGPPTPGS
GTHRIHLVHR GTGKWFELQD LHVSEVLPQM IPLSETLIQV WAVNKSIPNP SFVEPVKVID
EEIGEETKPE VKTDENEECG EIKKEDTIDT VNNKPQN
//
