ID A0A0L0DBR3_THETB Unreviewed; 486 AA.
AC A0A0L0DBR3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=AMSG_00520 {ECO:0000313|EMBL:KNC48743.1};
OS Thecamonas trahens ATCC 50062.
OC Eukaryota; Apusozoa; Apusomonadida; Apusomonadidae; Thecamonas.
OX NCBI_TaxID=461836 {ECO:0000313|EMBL:KNC48743.1, ECO:0000313|Proteomes:UP000054408};
RN [1] {ECO:0000313|EMBL:KNC48743.1, ECO:0000313|Proteomes:UP000054408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50062 {ECO:0000313|EMBL:KNC48743.1,
RC ECO:0000313|Proteomes:UP000054408};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA Borenstein D., Chapman S., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA Burger G., Gray M.W., Holland P.W.H., King N., Lang F.B.F., Roger A.J.,
RA Ruiz-Trillo I., Lander E., Nusbaum C.;
RT "The Genome Sequence of Thecamonas trahens ATCC 50062.";
RL Submitted (MAY-2010) 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};
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DR EMBL; GL349434; KNC48743.1; -; Genomic_DNA.
DR RefSeq; XP_013762794.1; XM_013907340.1.
DR AlphaFoldDB; A0A0L0DBR3; -.
DR STRING; 461836.A0A0L0DBR3; -.
DR EnsemblProtists; KNC48743; KNC48743; AMSG_00520.
DR GeneID; 25560323; -.
DR eggNOG; KOG1867; Eukaryota.
DR OMA; HCKGDEV; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000054408; 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 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; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF33; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 22; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KNC48743.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054408}.
FT DOMAIN 121..444
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 464..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 486 AA; 52544 MW; 7581003F36038167 CRC64;
MSCSRAHAAA HAATHPDHSL AVVIDFDAVF CFACARFVYD NAIDAALAAG TLAARARIRS
WAVPAAHLRV HSAEWLVSAE DMAAASQRVG VKRALGEPSS AEASEVDDVG MRIKKRRRGL
RGLNNFGNSC FMSCVLQTLL HNPLLRAYFL SHLHDPTKCT VAKKRCLGCN MVSLFTQTLS
GSSLPMNPSE FLHSIWVHSK YLAGYEQQDA HEFLISVLDG IHTHSRNQVP LPVASVPLPA
RPAPRCSCVV HSVFSGILSS KLVCLSCGAS SPSYDPFVDV SLQISSEVKA LEQCLLNFTS
SERLSVELPC RACAPEGKRP FTKRLQFQEL PLTLAIHLKR FESHGGTATG SSVKLSDFVS
FPLVLDMAPY VARESQSAFA VVVHIGSIDA GHYIAYVRVP APTVGAAAVP ASQLWFRCDD
AVVTLATVKE VLASEAYLLF YVKREIDYHD LGKTEIISAS SSTPRAARSS VLSPTASSPR
TFPPQA
//
