ID A0A0M9VQA3_9BASI Unreviewed; 558 AA.
AC A0A0M9VQA3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=Malapachy_2671 {ECO:0000313|EMBL:KOS15319.1};
OS Malassezia pachydermatis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS15319.1, ECO:0000313|Proteomes:UP000037751};
RN [1] {ECO:0000313|EMBL:KOS15319.1, ECO:0000313|Proteomes:UP000037751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS15319.1,
RC ECO:0000313|Proteomes:UP000037751};
RA Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT pachydermatis CBS1879.";
RL Submitted (JUL-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOS15319.1}.
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DR EMBL; LGAV01000002; KOS15319.1; -; Genomic_DNA.
DR RefSeq; XP_017992951.1; XM_018137159.1.
DR AlphaFoldDB; A0A0M9VQA3; -.
DR STRING; 77020.A0A0M9VQA3; -.
DR GeneID; 28729034; -.
DR VEuPathDB; FungiDB:Malapachy_2671; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000037751; 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 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:SF758; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 36; 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:UP000037751};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 123..455
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..558
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 558 AA; 61692 MW; 36E8DBEA960E8454 CRC64;
MAKGSLRSPK KSEARRVRTD MAVAAAASTS RSVPDAIKPG ALLKSLLDDP VRYVGSSRDE
LKASMSLEAA RASHFEVVNE TTTADNNEAD IPPPTAKDAA ASSLPLYTPR IVPQFPRAHM
RAAGLHNRGN TCYMNSVMQA LLHTPPLAHA MLTQSVPTLL GRYGMPRTKK QALKAANAFN
AVAALKEFFE RAYSGASAVT PSQFIANLRK FARPLRPGRQ EDAHEYLRLL LESMQHACTC
FARKSVAPND PVLMTTLIQK IFGGRLRSRV TCHSCRHNSD TFDPVLDLSL DVRKGIASVK
QALDAFTAPE MLSDKYRCDH CHRHVDATKR FTIDATPLAL TVHLKRFTIF GNKINKTVSY
GERLHLGRYM SERQKGLGAD QTMDEESLST IGAAQQYRLY AVVHHYGSGP NVGHYVASVR
SSDGTWLRMD DSYVSPLSHC PLDDPSAYLL LYVREPVALD ATTTTPMASP RKGPMHPPPS
PKKRKVAPLR RDRPEELSAE EDEGLGQPLS RAEYQHSRTS GDSSDEASID QELTLPPPLS
KKDVRRRKRR KLARRSLA
//
