ID A0A1A0HEE8_9ASCO Unreviewed; 803 AA.
AC A0A1A0HEE8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=METBIDRAFT_31202 {ECO:0000313|EMBL:OBA22278.1};
OS Metschnikowia bicuspidata var. bicuspidata NRRL YB-4993.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowia.
OX NCBI_TaxID=869754 {ECO:0000313|EMBL:OBA22278.1, ECO:0000313|Proteomes:UP000092555};
RN [1] {ECO:0000313|EMBL:OBA22278.1, ECO:0000313|Proteomes:UP000092555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL YB-4993 {ECO:0000313|EMBL:OBA22278.1,
RC ECO:0000313|Proteomes:UP000092555};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., LaButti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) 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,
CC ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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:OBA22278.1}.
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DR EMBL; LXTC01000002; OBA22278.1; -; Genomic_DNA.
DR RefSeq; XP_018712774.1; XM_018855807.1.
DR AlphaFoldDB; A0A1A0HEE8; -.
DR STRING; 869754.A0A1A0HEE8; -.
DR GeneID; 30028783; -.
DR OrthoDB; 55585at2759; -.
DR Proteomes; UP000092555; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02257; Peptidase_C19; 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; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF687; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 10; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 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 Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000092555};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 374..798
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..44
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 803 AA; 87127 MW; D67C26F4CF32F15C CRC64;
MPAGQFPAQQ AYVPVNMATG AGGYVPGRKK HFKSHNHHHN GHHQSSHGQG GLHHPYSKHA
SPTPSPNVAP DSGGAAKPRG ADVNNSELVP RIDDSATSTS ASITAPTSPR PTPPPSHSSP
KQGRGSRPED SMPAPTAPAL KQVSSPAAAS SSAAPSSAAP FSPAASSSVA SSQPVELPAT
LPATLPATLS FSGQASHPDR SLKDVLPLLL NITRDELISS RNAIHQSTKQ LLESRSRHTE
SLVAADPNRD YLVDIRRRIQ IIDHTKGSEY ETSLGAGLPP RPSKPNDNET NDSNASKPPL
NWASLLQSAV QKPAKLKAHT PLNGQYASKP LPPSVSVAPT LTDRCQSLGL LVMSMLYDPA
FNLNAHEPYT LKPRGLTNTG NICYMNAVLQ CLIYCAPFNK TLRLVEEKSL GILGKSSTPV
LDATIKFVND FATVTATSKS GGSSTNSEGI VVGRPLSPES LYMKLVENPK FQHLKWGQQE
DAEEFLVYLL DGLHEDFVTA EASVTADQME QLISLYGLKL DAPHAQDLKT RMKNALRLVK
HVENDAAEDH EGSQDEQSEN GWSEVGGRRK VSSKRVSEVE PSPITSIFGG RFRSVLTVPK
SKESHSITVD PYRCILLDIS LCDVQTIEDA LWKLNEVENL PYKTEGGLEV VAQKQTYIED
LPEVLTLQLK RFSFQQKQEQ LLGNGLEPTV NELSHFHGVG KIEKVLKNIS YGLDLAIPLE
SLSTAARHTQ NRNYLLTGVI YHHGRNAEGG HYTCDVLRGD KKWLRIDDTA VEPINADAVT
EKPEATDKSA YILIYQRKQA SDT
//
