ID G8YKW9_PICSO Unreviewed; 868 AA.
AC G8YKW9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=Piso0_001480 {ECO:0000313|EMBL:CCE88703.1};
GN ORFNames=GNLVRS01_PISO0F07331g {ECO:0000313|EMBL:CCE88703.1};
OS Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS 10061 / NRRL Y-12695) (Hybrid yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE88703.1, ECO:0000313|Proteomes:UP000005222};
RN [1] {ECO:0000313|Proteomes:UP000005222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
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|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR EMBL; FO082054; CCE88703.1; -; Genomic_DNA.
DR AlphaFoldDB; G8YKW9; -.
DR STRING; 559304.G8YKW9; -.
DR MEROPS; C19.004; -.
DR eggNOG; KOG1871; Eukaryota.
DR HOGENOM; CLU_008279_4_0_1; -.
DR InParanoid; G8YKW9; -.
DR OMA; HLKWFVY; -.
DR Proteomes; UP000005222; Chromosome F.
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; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF104; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 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:UP000005222};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 436..866
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 868 AA; 96300 MW; 1825F8CAA255CC24 CRC64;
MSASSSNTTN SGPNRFRGDA ASFSPSQTSP SMIHQQYQQH IYPDYLYGSP SMVPNQYYPY
MPYMIHPSAP YAEFNPYGQA YQAYPVQIPQ YPGQPYPVIP GGVGANGMNM AAMNMNMNMN
MNMGMGMGMG MMNRPKSAHA RSKNHHHSSG SVGYNTSNGS KDSFSNDVSA SSSTDNFKQP
PPSAKRQSDT KNGLSDETKQ AESNRQNTST EKQGSKSDSK ASTEQGSKVN EALHFPLYFN
SNLDSFINAQ KTSIKKRTEK VNEKKERLAK ALTNRGVENQ SLIINRVDGV KIIDHNESNA
IESVENDSYN KYLQSARRSS NAREGDKIAF AANGNNDDNK ASGKPSNWAA ILQNTPATVP
RKPKAPSKSG GSVSHSKSPS ISTQTVSPQQ PASVEKSDTP AATFPLGVLL LNIMFDKKFS
LISARSNTPV YKIKKRGLTN TGNICYMNAI LQILLYCEPF NKMLKLVETK TVGNLGNKSS
TPLLDLVIKF FNEFSSSQRN SNGTIKPFAV ENFYLSLIAN EKFQHLKWGQ QEDAEEFLGY
LLDGLHEEFV NATKSLTTPQ IDGLIQDFQK MHDGSDDYTV REFKANVKNT MKILKKYTEP
ASEREDTESD NDGWAEVGSN HRKVSAKRTV EIEPSPITSI FGGQFRSVLQ IPKSKESESI
TLDPYQCIQL DISDPSIGTI EEAFKHMNEP EKIPYKAANK EVIAKKQTFI DQLPNVLVIH
LKRFSYQQGA RDGSDAGDDS TQPRSNGGLG GIEKLRKKIT YSHTLTIPNE VLSPITQKQS
ANGYHYKLFG VVYHHGIGAE GGHYTCDVLR KSSLHDSQEE SNDKKIDNEW IRIDDTQVES
IDKNEVLDSG SEESSKNAYI LFYQKILI
//
