ID A0A0C7MZA8_9SACH Unreviewed; 862 AA.
AC A0A0C7MZA8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=LALA0_S07e01662g {ECO:0000313|EMBL:CEP63067.1};
OS Lachancea lanzarotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP63067.1, ECO:0000313|Proteomes:UP000054304};
RN [1] {ECO:0000313|EMBL:CEP63067.1, ECO:0000313|Proteomes:UP000054304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP63067.1,
RC ECO:0000313|Proteomes:UP000054304};
RA Neuveglise Cecile;
RL Submitted (DEC-2014) 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|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
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DR EMBL; LN736366; CEP63067.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C7MZA8; -.
DR STRING; 1245769.A0A0C7MZA8; -.
DR HOGENOM; CLU_005922_1_0_1; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000054304; 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; 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; IPR001763; Rhodanese-like_dom.
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:SF95; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 4-RELATED; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000054304};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 179..303
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 490..857
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 327..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 32..59
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 329..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 97342 MW; 6918F13E59113377 CRC64;
MPHKKIAQPT CKSTTQLIHI ADEFVKQDDG KNQDMETLLQ ECIDTLVNYQ EECKKLRRKG
SQNSPQSLGS RDENIFETYE AAYVYYKIVS QLVLNKIPEL PEFLHAKNNA ETQREKGLID
LYNMLVKTLL TDEKFAEIRK FIKEHSTAEK KPAAIKSYTE STWTNGQRIS PSRLSTLSNE
HRVLLIDLRP RLKFIESHIK SETITCIEPI SFKDSYSDIE LTRRSLITSP AREVSLFKER
DSFDYIVIYT DELDKTGFSQ QQQVSLLELL VQRSFERPLN NVKVLILQGG FEGWVNNGGP
CDSSHHKEDR EYALEYSIPP LIPQKASVMK PAPSSSTFAN FPETNGSVSH EDRPNSPLLF
PQQRPSGLQR SSSFRDRLSS MSPISRTISP SPTHESIVHR DSTSYPETPQ LGPSPNGNKL
PSQVKHEREI FNSHLNGFSP PRINGGMVEN GLDKALMRPA ADTNGKGLAR AADESADHVL
LNKPVSGFCV GLVNLGNSCY MNCIIQCLLG TNELAQIFLD DSYKNHINLN SKLGSKGVLA
KYFSQLIHTM RQKAVSAPPG TPKNHNKGDE KSAVQPINFK VASGSINSLF KGSSQQDCQE
FCQFLLDGLH EDLNQCGGNP SLKELSEEAE KIREKLCMRI ASSIEWERYL TTDFSVIVDL
FQGQYASQLK CKVCGRTSTT YQPFSVLSVP VPSGSRCGII DCFEEFTKIE TLERDERWSC
PQCKVKQPST KKITITRLPR NLIIHLKRFD NQLNKNNILV SYPNVLDLTP FWADDFDGKL
PPGVTELPTR GQVPPFNYDL YGVACHFGTL YGGHYTAYVN KGSPYGWCYF DDTSWRKVKN
QHEYITTNAY VLFYHRASMS SL
//
