ID A0A0M8MIW7_9BASI Unreviewed; 1120 AA.
AC A0A0M8MIW7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=Malapachy_0284 {ECO:0000313|EMBL:KOS12438.1};
OS Malassezia pachydermatis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS12438.1, ECO:0000313|Proteomes:UP000037751};
RN [1] {ECO:0000313|EMBL:KOS12438.1, ECO:0000313|Proteomes:UP000037751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS12438.1,
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 -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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:KOS12438.1}.
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DR EMBL; LGAV01000014; KOS12438.1; -; Genomic_DNA.
DR RefSeq; XP_017990070.1; XM_018134809.1.
DR AlphaFoldDB; A0A0M8MIW7; -.
DR STRING; 77020.A0A0M8MIW7; -.
DR GeneID; 28726684; -.
DR VEuPathDB; FungiDB:Malapachy_0284; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000037751; 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; cd02659; peptidase_C19C; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF644; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7; 1.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50144; MATH; 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|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000037751};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 49..181
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 207..528
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 1120 AA; 129839 MW; 7CE3A5D5B1597413 CRC64;
MDTQDVGMSV ADPLTADEGV HALARISVMD HKAFADKYLA DLGQEEADFQ VCHWPIKSWH
ALDKRITGPE FECGGHRWRI LLFPFGNSNG QPYDMVSVYL DYADNQNTPE GWHACAQFAL
VISNPNDPTL FSTSQAHHRF TAEEMDWGFT RFNEFRKLAV PLDNRTRPII EDDQAVVSAY
VRVLKDPTGV LWHNFINYDS KKETGYVGMK NQGATCYMNS LLQSLYFTNY YRRAVYQIPT
ENDVPTDSVA YALQRVFYQL QTSNLPVGTT ELTKSFGWKS LDSFLQHDVQ EFNRVLQEKL
EEKMKGTAAD GAITNLFVGK MKSFLRCVNV DFESSRSEDF YDIQLNVKGM SNLEQSFWDY
IQTEMLEGDN KYFAEGYGLQ DAEKGVIFEK FPPVLHLQLK RFEYDMEKDM MVKINDRHEF
PLEIDLKPFL IKEAQSEPWV YKLHGVLVHS GDLHGGHYFA LIKPERDSNW FKFDDDRVTP
ATLKEVLEDN FGGEMMPTNG AQRQFAATAP VRAMKRFTNA YMLVYVRESK MDSVLKPIQE
VDTPMHLRNR LEEERVEMEA RRREREEQHL YLTTKVVTEE LIRQHQGFDL ATFDDRMGRP
TELPTFRVLK NEPFVSFKTR LAQHFNVPDH LMRLWVLVNR QNKTVRPDAV VPENDPNLTL
EMVRDRMASR QHDLRLFVEM LDPDSLAMTH FDASTPGNSI MIFLKYFDTS RQTLLGVSRM
YVQRQMKVAD LVPTINELMR WPPTTQVKLF EEIKPGMIEL LKPKATFVQS EIQDGDVICF
QIELSEKDAN DYEMQQLYSN PIQFYDFLQN QVRLLLKPRY EDAPCQTEFE LTLSKKMTYD
MLATKVSERL KQDPLKLRFT AANGPNGTPK TVLKRSANQT VNEIIQTSYL QGSASLLYYE
MLDVSIIELE TKRSLKVVWM GAFNKEEAQP HSFLLPKTAT IHELSDQLAK LVTLRPEETG
KIRIFESAAL GKQQRELHSF DTINSIPDGT ELFAEEIWPE ELALGEDKKL VQVCHFTKDI
ARTHSVPFRF VLKQGERFAE TAQRLQQRMD VPEKEFAKYR FALIQLSQFK QPTYLEDDDV
LFEHKFQPDD ILGVDHIDKT GRSNRYNTSA AQDRGIRIRS
//
