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Database: UniProt
Entry: A0A109FEU9_9BASI
LinkDB: A0A109FEU9_9BASI
Original site: A0A109FEU9_9BASI 
ID   A0A109FEU9_9BASI        Unreviewed;       976 AA.
AC   A0A109FEU9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN   ORFNames=RHOSPDRAFT_35321 {ECO:0000313|EMBL:KWU43181.1};
OS   Rhodotorula sp. JG-1b.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU43181.1, ECO:0000313|Proteomes:UP000062823};
RN   [1] {ECO:0000313|EMBL:KWU43181.1, ECO:0000313|Proteomes:UP000062823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JG-1b {ECO:0000313|EMBL:KWU43181.1,
RC   ECO:0000313|Proteomes:UP000062823};
RG   DOE Joint Genome Institute;
RA   Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA   Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT   "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT   permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT   Antarctica.";
RL   Submitted (DEC-2015) 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}.
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DR   EMBL; KQ954494; KWU43181.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A109FEU9; -.
DR   STRING; 1305733.A0A109FEU9; -.
DR   OrthoDB; 55585at2759; -.
DR   Proteomes; UP000062823; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062823};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT   DOMAIN          539..974
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          99..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          613..674
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          717..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..172
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..265
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..386
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..473
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..656
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   976 AA;  102502 MW;  E6F9690F01C2B6ED CRC64;
     MVTPSPGPSR GPTPTSSTHA SASSSRASNA SKLNPNSATF SYLQQHEPVP SRASPPLHPG
     QAMPYASFSP PPPPSRNGMY GMPMPVSYSP YPISSATTMP GVGPTATQAS APSGSWSAPR
     VGGWPGPSTY GPGPIHHSGP HHHSQPPYYT QSQLPPPAQN RMTPPVPPPT ANGILLPLSN
     GPPPNLAATM AAAGYPHHMP NSAMPPNLPM QSVPHPGLLP PFSPPQPLPP SAASAPRLVP
     APSLPVSPAT PLPPQSVPPP PSRTSTSATN PTRPDNLTPA FGAAMSPPPP AAAATRSAHG
     PRGYGIRRKK DHLPAPKDAK PLDFAPNLRM PGGFAGIFRT PSSLGSPGSA SGRSRTVTAP
     SEQKASAATA SAPATSPTNS PAALAVRDSS ESAALASKDV NPPSASGQAP EAAINGETAE
     SPVPPLSPTR SREQSAAPPL SPTPSGGPAA STPISPVAAS TTSQTTSPRI APSSFKRSWA
     DLVRPAAGSQ PAKGVNGVLP ISASIGPDPS AAPRAGDTLL STVHRAPPHE HMPHAPTPRG
     LINNGNLCFA NSTLQALVYC GSFWNLMNIV ERGTKKNLRD EMTGVAAAEK NASERSAVEA
     TIAFLAEFRT DETPAPAFDP SVNRKSAASA STSGTTTPKP PFNNSAHSHM PSSPSMSTPT
     TPGPLSPTPI HDALRHNPRF DAMRRGTQED AEEFLGFFLE TLHEEILKLA EIEEAQEEKR
     KGKGKAPVSG AEEGWEEVGS KGRVATTRTT ATKESPITRI FGGKLRSVLR CPGQKDSVTI
     EPFQRLQLDI QPDHVLSIAD ALLHLTTPES LPDFMSSRGV RTQDASKQVF VDALPPVLLL
     HLKRFLYDEV GGVQKSTKKV AYGTELTIDE RVMSAPLRAQ VGKDGAKYEL FGVVYHHGLQ
     ASGGHYTVAV RRGYRSPAWL ELDDTHMRSL TEDEVAVSAT APSRRWESVS EGRRRFEDDD
     ADQKVAYLLL YAQVKQ
//
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