ID A0A1D8PP95_CANAL Unreviewed; 660 AA.
AC A0A1D8PP95;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN OrderedLocusNames=CAALFM_C600170CA {ECO:0000313|EMBL:AOW29967.1},
GN orf19.8766 {ECO:0000313|CGD:CAL0000199093};
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561 {ECO:0000313|EMBL:AOW29967.1, ECO:0000313|Proteomes:UP000000559};
RN [1] {ECO:0000313|EMBL:AOW29967.1, ECO:0000313|Proteomes:UP000000559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2] {ECO:0000313|EMBL:AOW29967.1, ECO:0000313|Proteomes:UP000000559}
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=17419877; DOI=.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3] {ECO:0000313|EMBL:AOW29967.1, ECO:0000313|Proteomes:UP000000559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=24025428; DOI=.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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}.
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DR EMBL; CP017628; AOW29967.1; -; Genomic_DNA.
DR RefSeq; XP_710490.2; XM_705398.2.
DR AlphaFoldDB; A0A1D8PP95; -.
DR SMR; A0A1D8PP95; -.
DR STRING; 237561.A0A1D8PP95; -.
DR EnsemblFungi; C6_00170C_A-T; C6_00170C_A-T-p1; C6_00170C_A.
DR GeneID; 3647903; -.
DR KEGG; cal:CAALFM_C600170CA; -.
DR CGD; CAL0000199093; orf19.8766.
DR VEuPathDB; FungiDB:C6_00170C_A; -.
DR InParanoid; A0A1D8PP95; -.
DR OrthoDB; 55585at2759; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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, ECO:0000313|EMBL:AOW29967.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000559};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 289..660
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..119
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..242
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 660 AA; 75143 MW; 2CCEE1B7B1227E6D CRC64;
MTSSSSNSGS SRFRGDAASF SPSQYPNYHQ QQFHPQQYMA QQIPAQQQFY YQFPQTYPMM
MNQMYPVFPY PPDPFFQQQQ QQQQQQQQQQ QFVMQPQYIY HPPPKPPKTN KPPKVNGSAP
PPKIELVDLP LYINTSKTEF LQRYSITQES RSIDELQRAN TLEEYNENTN RLIISTNVMK
IIDENDHKTT ITNGQPEEPK PAAKAVAPPV PISNWASFLQ STAPPTPKKI AKPKPPPTPP
TPVQAVTPVP QFDMSNESAQ PLGTLLLKIM FDSNYSVFSS LPTFDIKPRG LTNTGNICYM
NSILQILIHC EPFNRLLKLI ETKSIGSLGP SSTPLLDATI IFFNQFQENV KGAISPESFY
ASLTKLDKFS HLKWGQQEDA EEFLGYYLDG LNEEFLGAIK QLNTPQIDSL IQVYAQDHDA
EATAKFKFNV KSTIKRIKND AEADDGEWNQ VNKKKNSTTT KIEIDPTPLN MIFGGEFKSV
VTIPKQSSSF QKSITLDPFQ HVQLDVSSAD TIEDAIKHLN ESESISYTNN NKEIQVKKQT
FIEKLPNVLI IHLKRFSYLK DQEIGVEKLR KKVDYNHDLI IPKEVMARDT GMPIKYQLVS
VVYHHGSSAD AGHYTSDIYN AGQWWRIDDT AVKQIQNEEV LNAGTEENIK NAYILLYRRI
//
