ID A5DYC8_LODEL Unreviewed; 1370 AA.
AC A5DYC8;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=LELG_02365 {ECO:0000313|EMBL:EDK44186.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK44186.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK44186.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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}.
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DR EMBL; CH981526; EDK44186.1; -; Genomic_DNA.
DR RefSeq; XP_001525807.1; XM_001525757.1.
DR STRING; 379508.A5DYC8; -.
DR GeneID; 5232993; -.
DR KEGG; lel:LELG_02365; -.
DR eggNOG; KOG1863; Eukaryota.
DR HOGENOM; CLU_003532_2_1_1; -.
DR InParanoid; A5DYC8; -.
DR OMA; DTDWGFA; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000001996; 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; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 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:UP000001996};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 164..308
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 335..661
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 31..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1036
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1370 AA; 158048 MW; 8CA19DE1CA44AF5A CRC64;
MISDDSHPST KRRALYDDTV VDIEDDSQEY AAANNEKGEL NQDINTQHKA DSPPEYNNDS
SSPEVIDITG DVNQEGNIEI DPNDLDSEEE EEVELVDESG EDYIDIDQEN QLQQQQQQQL
LLIQLIQLIQ LLQKAQNKIP MANEFDKLAK YLMKPIPDYP VKEEIHFVWE VTDWALLSKE
EKIRSPKFKC GDYEWNILLF PNGNNTNANI SAYMEPHPLT NETTADSNLN GKDSDWYVCA
QFAIDVWNPE APESHSPSQS SHRFSKTDAD WGFSALIDKR SLSLKKFANK LFEVPILENN
KLNFTGFVRV IDDSLTGVLW HNFNNYDSKT KSGYVGLNNQ GATCYLNSLL QSYFTTKIFR
KLVYQIPTQQ EKNAGVALAL QRIFYLLSTS KDPVGTMELT KSFGWDSSDA FTQHDVQELN
RILMDKLEHA MKGSAIEKGL NDIFVGKMKS YIKCVNVPYE SSRVEDFWDI QLNVKGFRNL
EESFKNYIEI EMLEGENKYQ AGDDYGYQDA KKGVVFESFP PVLHLQLKRF EYDFMVDDLV
KIDDFYEFPD RIDLKPYLDE DLPQDVKNQN WNYKLHGVLV HQGTISNGHY YAMIKPNASG
KTWLRFDDDR VWKVTQLQVF QENFGASDLS KEELSKLTRA EQQEHLIKRV TSAYMLVYYR
ESELDQIVPI EDDAIEAAIP DHVSNQIKYE MEERERIERE RREALFYTNV KIVTTSTINN
HLGFDLALDP TVENYYESAL AGTACDAKTL RVRKDSAYAD LVSKIAESLG YEDASKIRLV
VLSHRENHTN RLDVPVEDDL QKTTIGNVIA KSFNRRHDEH VFFVEELNKD IRNINKLVGE
TEIIDPTKFD FDKVFYKIQS VGTATSTSED EMKFQSTVPY SGYSTIFIKY FDPVSQELRC
LSYITVRRND KIETIVEPVK QLLGFSNDVE LEAFEELCPT MIEPIDLDAT FDKQELNSGD
IITFQVTNVR DIAGDKQFQS AKAYYKFMAT RVHIRVKPFN ANMEDEDSDY VENDKEDTKL
DGETEGDNIN GQENDKVTQR EIELAKKLSK SFDLWISKTK SYHDLAEAIS KVVGCDPEFL
KIFLVGNQGQ KYPLKTIHML SQVFSPKSHV DDIYEFEYEI LNIKLKDYES LRPFKVYWLS
NLLQFQVFEL LVKRSETVRE LVSKLLHKVK VSESQLKFLL CWSGVNHSFS EILKFDFPIN
EIAEHSEIYC GLFPAEVKAL CDHDIYKCYI GDGEKTWSDA EKDITNEAEK AEYTQTKTAS
KSLNLITVFH FHKSSSNHHG IPFMFIVFPG ESFKSTRERL RLKLGLGKQA FDKIRFALAD
LNNKGQYLDD EDENLVLFDK VSIERSFLAL DHPDRNSKRV NPFDKGISIK
//
