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
//