ID D2VIY7_NAEGR Unreviewed; 473 AA.
AC D2VIY7;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=NAEGRDRAFT_83194 {ECO:0000313|EMBL:EFC43106.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC43106.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC43106.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
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; GG738875; EFC43106.1; -; Genomic_DNA.
DR RefSeq; XP_002675850.1; XM_002675804.1.
DR AlphaFoldDB; D2VIY7; -.
DR STRING; 5762.D2VIY7; -.
DR EnsemblProtists; EFC43106; EFC43106; NAEGRDRAFT_83194.
DR GeneID; 8853245; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_83194; -.
DR eggNOG; KOG1872; Eukaryota.
DR InParanoid; D2VIY7; -.
DR OrthoDB; 160664at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
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; 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; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:EFC43106.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 3..73
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 107..468
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 361..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 473 AA; 54155 MW; F61E0E0E630CCC4D CRC64;
MSTTITLKWN KSTFDNVEIG DLKTGLDFKK KCQELTGVHP DRQKIMGLGA GILKDNQELS
AVKVKAGQLV RMMGSADELP EPPKEKTVFI EDTAKENGDG EVQYYPAGLE NLGNTCYMNS
ALESFRYVPE LREAIEHFDG SSVSELLEKD KEIASELKSL YKRLDTANDS ISPITFLEAF
RKAYPQFAEK ERTELGEFYS QQDSDEFITN LLGSLENMLK TSDRNVVNLI TCYLYCFYRL
QCTECEEAPT VTKEAWKKLS CFISQQVSNL PYGLQKSLDG TLEKESPTLG KTAVYTKTQR
ISKLPNYLVV NFVRFFWKQK QQVKAKVLRD VAFPSVLDTF ELCTDEYKNK LKETREKMRL
DREEEMKKKK EEQLNNLGQQ AKKQKTEETD KTPLYQVNDS GWFELCAVVT HKGRAANEGH
YVAWVKNDAG QWLQFNDDDV TAVTEEEVKK LSGGGDWHTA YLCLYRKARK LNL
//
