ID A0A061H8E3_9BASI Unreviewed; 972 AA.
AC A0A061H8E3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=PFL1_04117 {ECO:0000313|EMBL:EPQ28290.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ28290.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ28290.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ28290.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
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; KE361635; EPQ28290.1; -; Genomic_DNA.
DR RefSeq; XP_007879832.1; XM_007881641.1.
DR AlphaFoldDB; A0A061H8E3; -.
DR GeneID; 19318224; -.
DR KEGG; pfp:PFL1_04117; -.
DR eggNOG; KOG1871; Eukaryota.
DR HOGENOM; CLU_008279_7_2_1; -.
DR OrthoDB; 55585at2759; -.
DR Proteomes; UP000053664; Unassembled WGS sequence.
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; 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:UP000053664};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 430..874
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 972 AA; 100168 MW; E652CDDFF66359B1 CRC64;
MSAAHLPSSH SSIPAASFSS PGVSSSRHAA QAQASTSSLA SHSYASLSLL PESSEGGLVF
STEFSPAASP RRSSFKLAAT APSLSTSGEA ASSGSASSHA AVFTAAATAD GKPPPSARPR
ASRAASSSSS SSKRAERDPL FQSIPDSTSF GSGGADGKSW GVALHPPSPR TAPALTLSYR
SSPDPSQFPS FASLLRSMPR QSSSRRAPIA SKSASVTSSA TPPPPSATAA TITSSSPSAD
PSRLKSSSTA THTASTTPAE ATPAPSLIST HPSSPATADA PDLAASVLTE ATSVADLDSQ
AKSEAAASTA STPQAAASPA PKKAAWGAPK SWAELASRSG AASSRQGAVG ISVNFGETAA
GSQADASETG SPSRSPRPAA NGRRKSGVGA GEAGSRHHAA SGPAKPAVMS LERMLADSHK
SFKAPLTHPR GLVNTGNFCF ANAILQMLVY CAPFYNLFTL IGREVPADFG NATPLMEAVI
HFLREFVLVD TAAQVNGAGG EHDDSGEHEA VSSFAPGASE PFVPEFVYEA MRLNKRFDQM
RRGHQEDAEE FLGFFLDTLH EELIGAIRRS AAKLAQSGSG ANSLLSRMSE EEKRLNGVTD
ADLKRLGVKV GGARDGSGAN GSASTDGSML GLGLDDEVEE REVTRPVSPS EEGWMEVGQK
GKTAFTRTTS TSDSPITRIF GGKLRSVLRC PGAKDSVTLE PYQPLQLDIQ PPHVQSIEDA
LVNLTVPEVI PGVYSPAKGA HIDATKQVFI ESLPPILIVH LKRFVYDEVG GVQKSQKPLA
YGTTLEIAGE ALSPAMRAQG RPKYKLFGVV YHHGRYASGG HYTVDVLRQD SRSWLHIDDT
TFSTIPTEHV VRMAGKNAPV GHDGLAYLLF YKRDDGSSDA KIASSTAPAS TSGFATGGHG
AATPPLRKPT RPATTATASP SSGKKKADAT VAAAAERQAG GRHEAATATA GAGAGAGAGA
EKKKRVVPGW SK
//
