ID Q5KIZ8_CRYNJ Unreviewed; 327 AA.
AC Q5KIZ8; Q55TE0;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|PIRNR:PIRNR038120, ECO:0000256|RuleBase:RU361215};
DE EC=3.4.19.12 {ECO:0000256|PIRNR:PIRNR038120, ECO:0000256|RuleBase:RU361215};
GN OrderedLocusNames=CND01170 {ECO:0000313|EMBL:AAW42987.1};
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684 {ECO:0000313|EMBL:AAW42987.1, ECO:0000313|Proteomes:UP000002149};
RN [1] {ECO:0000313|EMBL:AAW42987.1, ECO:0000313|Proteomes:UP000002149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565 {ECO:0000313|Proteomes:UP000002149};
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J., Koo H.L., Krzywinski M.I., Kwon-Chung J.K.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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|PIRNR:PIRNR038120, ECO:0000256|RuleBase:RU361215};
CC -!- SIMILARITY: Belongs to the peptidase C12 family.
CC {ECO:0000256|ARBA:ARBA00009326, ECO:0000256|PIRNR:PIRNR038120,
CC ECO:0000256|RuleBase:RU361215}.
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DR EMBL; AE017344; AAW42987.1; -; Genomic_DNA.
DR RefSeq; XP_570294.1; XM_570294.1.
DR AlphaFoldDB; Q5KIZ8; -.
DR STRING; 214684.Q5KIZ8; -.
DR PaxDb; 214684-Q5KIZ8; -.
DR EnsemblFungi; AAW42987; AAW42987; CND01170.
DR GeneID; 3256953; -.
DR KEGG; cne:CND01170; -.
DR VEuPathDB; FungiDB:CND01170; -.
DR eggNOG; KOG2778; Eukaryota.
DR HOGENOM; CLU_018316_0_1_1; -.
DR InParanoid; Q5KIZ8; -.
DR OMA; YIQYEIQ; -.
DR OrthoDB; 276003at2759; -.
DR Proteomes; UP000002149; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0019784; F:deNEDDylase activity; IEA:EnsemblFungi.
DR GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IEA:EnsemblFungi.
DR GO; GO:0000338; P:protein deneddylation; IEA:EnsemblFungi.
DR Gene3D; 1.20.58.860; -; 1.
DR Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001578; Peptidase_C12_UCH.
DR InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR InterPro; IPR017390; Ubiquitinyl_hydrolase_UCH37.
DR InterPro; IPR041507; UCH_C.
DR PANTHER; PTHR10589; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR10589:SF16; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L5; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR Pfam; PF18031; UCH_C; 1.
DR PIRSF; PIRSF038120; Ubiquitinyl_hydrolase_UCH37; 1.
DR PRINTS; PR00707; UBCTHYDRLASE.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR038120};
KW Protease {ECO:0000256|PIRNR:PIRNR038120, ECO:0000256|RuleBase:RU361215};
KW Reference proteome {ECO:0000313|Proteomes:UP000002149};
KW Thiol protease {ECO:0000256|PIRNR:PIRNR038120,
KW ECO:0000256|RuleBase:RU361215};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR038120}.
FT DOMAIN 8..221
FT /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT cysteine active-site"
FT /evidence="ECO:0000259|Pfam:PF01088"
FT DOMAIN 261..301
FT /note="Peptidase C12 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18031"
FT REGION 304..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 92
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR038120-1"
FT ACT_SITE 177
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038120-1"
FT SITE 192
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR038120-2"
SQ SEQUENCE 327 AA; 36520 MW; 4A8EB1728947A5A9 CRC64;
MADDPSGWSL TESDPQVFTQ LLKDLGVNGL QVDDLYSLDA ETLATLKPIH ALIFLFKYVA
PDAESAQESA GVEVDPLDNG VWFANQVINN SCGTLAALNA VMNIKPQQSV HERESIKLGS
ELENLREFGA GMQSLDLGHV LSSSDHIREV HNSFSKSSPF AMDPSAFPER EKEDAYHFVA
YLPINDILYE LDGLRRFPIM HAPVDGDWLD TARETIEQRI ATYPPGSLMF NLLCVRSDAI
PRLERLLNDP STPAEQKFVI QDQLEHERNK SQKGAMENSL RRHNLLPVVF QLFKSLGESG
MAAKAVEDAR TKGKERRERM QAKGEAE
//
