ID A0A421JA58_9ASCO Unreviewed; 484 AA.
AC A0A421JA58;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=JA9_001845 {ECO:0000313|EMBL:RLV85705.1};
OS Meyerozyma sp. JA9.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=2028340 {ECO:0000313|EMBL:RLV85705.1, ECO:0000313|Proteomes:UP000286412};
RN [1] {ECO:0000313|EMBL:RLV85705.1, ECO:0000313|Proteomes:UP000286412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA9 {ECO:0000313|EMBL:RLV85705.1,
RC ECO:0000313|Proteomes:UP000286412};
RA Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT "Physiological and comparative genomic analysis of newly identified yeasts
RT Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT production.";
RL Submitted (AUG-2017) 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:RLV85705.1}.
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DR EMBL; NSDU01000013; RLV85705.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A421JA58; -.
DR STRING; 2028340.A0A421JA58; -.
DR Proteomes; UP000286412; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd02657; Peptidase_C19A; 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; 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, ECO:0000313|EMBL:RLV85705.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000286412};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 4..60
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 106..482
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 484 AA; 54560 MW; 5AD7A298664F76E1 CRC64;
MGTNTVSIKN SGKVYEVDVD SSTSGSQFKE KIFGITNIPV DRQKILIKGG KIDDSKPIEE
QISSQKQPIM VLGNPAPAVP SGPVEKQVFL EDLNPNSLIK VSNEPSGLVN LGNTCYLNSS
LQALFQIDDI ATKVANYKSP NGINSTSNES LTASLRATFD QMSKKQEKVN PMLFLTLFRN
VFPQFAEQDH GFYKQQDAEE AFSQLLTILD QTLKVGDHFR LSYKKEQKCL ALPDEAATID
YEDSLKLNCH IDIKTNFLRD GILSGLKETI QKYNDTLQSN TEYEITRTIT RLPKYLTIHF
MRFFWRRDTQ KKSKILRRVQ FPFELDLAEM LDPSIKNDKV AVRDKIRQIE KDQDELIRDF
KKSKKSSGLN PTEQEEEDQM KIESIKSKFR DDLTSALPGI SLDSTTENPS SVYQLGAVIT
HAGSSADSGH YQAYVRDPKD IEGIRWWKFN DDKVSEVSRE KVETLAGGGE ADSALILIYK
GIGL
//
