ID A6ZVC0_YEAS7 Unreviewed; 1072 AA.
AC A6ZVC0;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=UBP7 {ECO:0000313|EMBL:EDN61345.1};
GN ORFNames=SCY_2636 {ECO:0000313|EMBL:EDN61345.1};
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796 {ECO:0000313|EMBL:EDN61345.1, ECO:0000313|Proteomes:UP000007060};
RN [1] {ECO:0000313|EMBL:EDN61345.1, ECO:0000313|Proteomes:UP000007060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789 {ECO:0000313|EMBL:EDN61345.1,
RC ECO:0000313|Proteomes:UP000007060};
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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:EDN61345.1}.
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DR EMBL; AAFW02000124; EDN61345.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZVC0; -.
DR HOGENOM; CLU_004122_0_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF24; USP DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 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:0000313|EMBL:EDN61345.1};
KW Protease {ECO:0000313|EMBL:EDN61345.1}.
FT DOMAIN 610..1070
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 467..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..537
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1072 AA; 123260 MW; DE0C86CA1A8A70C1 CRC64;
MLDDDKGTAM HPHITPFTPE YSNELLRRVQ DLYHEDIKHY YPQLKLEKLL DLLEHTEYLF
ELYLDSIHHD RPNDALTAFI IGCYYVFLII PQSLQFQTRN KSYSIYTDLK KMYENEMNMT
NVVLMVKKEI GVVLDESVKH GAGIEHRITK KRAFSVPADD LSGQVASLSL DTAAPQDHDL
KGTFTEDDAE QSSPVWTAPN LEPNDQLKLA LLPEVIPTPA FREPERKTSV PVRPSVLLED
VPSIYHEDDT SFASLNPPFR EITADRSVTH RKDSYHSVYM VDSGNLKEDN DDLFNVENDG
FIQSLDILQK QSIITAPELF SILSNRVERE KVLLIDLRIP QRSAINHIVA PNLVNVDPNL
LWDKQTNTPI YKDDILEHLL KENENFINRN KFDYIVYYTD VKTFMTINFD YAFIFFYLML
TSQKTPLTTV PTTLLGGYEK WKKTLHSYAQ EYHISIEDYL YRPYSQKARL QQEQQQQQQQ
QPDSQDSSSA KESSTKVPEP PSWKPPDLPI RLRKRPPPPP PVSMPTTPEI PPPLPPKIMV
HSQVSSISRK PPIPAKQHVK KEQLNSNEII QRKRQHQHQH YDQQILQPQR AYNIPTIERS
PNVYVSLSIT GLRNLGNTCY INSMIQCLFA AKTFRTLFIS SKYKSYLQPI RSNGSHYSPK
LSNSLSMLFN KMYLNGGCSV VPTGFLKVIN QLRPDLKIPD DQQDTQEFLM ILLDRLHDEL
SDQQHVANDY PNLLLYNADA LKVSNNEYKH WFDKNVIGNG ISPIDDIFQG QMENSLQCKR
CGYTTFNYST FYVLSLAIPR RSMKLSKLGR STEKRVKLED CINMFTSDEV LSGENAWDCP
RCGPTASVST SVSALENEPS IVKSKKKKSR FFTLHTGTKR RHLDFFGDGI TEGHNSNNNN
TTIFERERSR SPFRMLGGSG KRSSSSTPFS TGGNDSNNSS DYKNKKLTTV KTINFVTLPK
ILVIHLSRFY YDLTKKNNTV VTYPLILNII LKNNDTMKYK LFGVVNHTGT LISGHYTSLV
NKDLEHNVNI GRSKWYYFDD EVVKADRKHG SDKNLKISSS DVYVLFYERV YD
//
