ID   C4R3L1_KOMPG            Unreviewed;      1280 AA.
AC   C4R3L1;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   OrderedLocusNames=PAS_chr3_0117 {ECO:0000313|EMBL:CAY70048.1};
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY70048.1, ECO:0000313|Proteomes:UP000000314};
RN   [1] {ECO:0000313|EMBL:CAY70048.1, ECO:0000313|Proteomes:UP000000314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314};
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(2009).
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};
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DR   EMBL; FN392321; CAY70048.1; -; Genomic_DNA.
DR   RefSeq; XP_002492326.1; XM_002492281.1.
DR   AlphaFoldDB; C4R3L1; -.
DR   STRING; 644223.C4R3L1; -.
DR   EnsemblFungi; CAY70048; CAY70048; PAS_chr3_0117.
DR   GeneID; 8199397; -.
DR   KEGG; ppa:PAS_chr3_0117; -.
DR   eggNOG; KOG1863; Eukaryota.
DR   HOGENOM; CLU_003155_1_0_1; -.
DR   InParanoid; C4R3L1; -.
DR   OMA; HHLVYKS; -.
DR   OrthoDB; 1423057at2759; -.
DR   Proteomes; UP000000314; Chromosome 3.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd02666; Peptidase_C19J; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR044635; UBP14-like.
DR   InterPro; IPR025305; UCH_repeat_domain.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR43982; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR43982:SF6; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 2-RELATED; 1.
DR   Pfam; PF13446; RPT; 3.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:CAY70048.1};
KW   Protease {ECO:0000313|EMBL:CAY70048.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000314}.
FT   DOMAIN          693..1250
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          808..900
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1139..1180
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        839..900
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1280 AA;  147077 MW;  BB82033A3BE4A38E CRC64;
     MPDQVPSAST NVNNPFAQLE AYDFSKSKIF KTSNRLIDDI KNSVLFLEQF SILNLPAVDY
     ATQLSLQYQN RQINESFKLV LLNNQLDFAP TVSTEQLPNG TRTVFRGLIV QDTVHGIPIS
     DIPIYHCRIL FKSLENEILC SKHQFFHFSD DSLSPSDRSD LVTDYAKISK GELTDCEDDL
     KPSIVQSCPK LLDSTNYICR KCYKVLRIEI FEKDLSNEEY KQFELNEIQF RYSKTVSADP
     SLNISNENDV NKIPSQSECL WTLFKVLRGP LSRDPEELEV KTLDVNHKIL NIHLDMDIFE
     KCLFFHKSAD GSYLTPPLFS EYGVFENLVR ESYIRKLLEV VYLGTICPNN PGLKRLNQFA
     QAYWFNDTGS KIFHFLKEFD STAAIEWFGG LRYDVLERYN PALTTLVSAN YFNNKLICGS
     YSLLCESDPQ NTPKYFDALR DIGLLRQAPV VQEFVAKEAS KNVFSFRDTM RNYQILGIDT
     SSADFPTLSD DEILKFYKYE LILANSESSY DRLRNALSSI ADYRKSEALQ NYLRIEPIHN
     IDQAYKHFDT PQSIEDDVLI TAFQFKKDDF PQAVALYDRA LLTIAIQRKS LFLWSYITHN
     LDYLFKVIVA SSSKTITGVE DAYKYLGCDP LATDFQVVTI FQERLIKDPG IDVILFFYSL
     VVIEKSRSSK LIGKFLQNGV VDASFLPLES SPVGLNNIGN TCYLNSLLQY YFVIKPLRTA
     IQNFKDILPS SEEEFNSIED YSKRRIGGRT VGYKETERSF QFVYQLRDLF DELIHSRRIA
     ITPTKELAYL AFSPSTDEVQ FHLPEVQKPR PSITESETGM SDAPVPELSP VAMDWSSSIA
     YPEPSSSHHE ESAALNSPDE SSELIHSPTK RKLSPQPSTE DLNEIDTKVS VTNAEPPTTT
     LPKRATTAVA LIGNDQLENA LELGRQQDVT ECIENVLFQL ESASKPTSLD SDDQEQNDLV
     KELFYGRTKQ ILQPVDKETK ENITDSSVRT KVERFVSLLV NIGDHPKDLY DALDTYFTED
     LIDLDDGQVK RSLTITELPK FLQIQVQRVQ FDRERGIPFK ALDPLPFHEK LYMDRYLETD
     NEELILKRKE IFQWKNEISK LNRRKDEILV PSSHSMTPRN ALIATKEFLE AQKELPGDIQ
     ATESTLITLQ KEIDILNSEL QTINSRLSEL EEKCQHQFDQ FKNTGYSIFA IFIHRGEASY
     GHYWVYIRDP TRNIYRKYND ETITEVPISE VFNFSESNTA TPYFLVFVRE DLEDEVEPLK
     RELDSSPTTE DFRISVEELD
//