ID   H2ZYD5_LATCH            Unreviewed;       818 AA.
AC   H2ZYD5;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000002406.1, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Proteomes:UP000008672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT   "The draft genome of Latimeria chalumnae.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000002406.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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DR   EMBL; AFYH01174458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H2ZYD5; -.
DR   STRING; 7897.ENSLACP00000002406; -.
DR   Ensembl; ENSLACT00000002426.1; ENSLACP00000002406.1; ENSLACG00000002150.1.
DR   eggNOG; KOG1870; Eukaryota.
DR   GeneTree; ENSGT00940000157311; -.
DR   HOGENOM; CLU_004896_0_0_1; -.
DR   InParanoid; H2ZYD5; -.
DR   OMA; VIRISYP; -.
DR   TreeFam; TF352179; -.
DR   Proteomes; UP000008672; 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; 3.30.2230.10; DUSP-like; 2.
DR   InterPro; IPR035927; DUSP-like_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR006615; Pept_C19_DUSP.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF32; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 33; 1.
DR   Pfam; PF06337; DUSP; 2.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00695; DUSP; 2.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 2.
DR   PROSITE; PS51283; DUSP; 2.
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:UP000008672};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT   DOMAIN          146..623
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   DOMAIN          621..714
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   DOMAIN          723..818
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   REGION          70..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   818 AA;  92900 MW;  CB579FDCCA643276 CRC64;
     QMPIVSSICL HVEAGREIKM EEPVQIPEAS GPISTDRVNL RACVEKKCYY VGCGDSHKDL
     CAFHLEDTKQ SPSTNPITQQ NSYNEGTVDR EQTQNSLKLL RSQEMLGPLT KDLHICGGST
     LKIPKFTVLE LDMDMEDGEK EVKGLTGLMN VGNTCYMNAA LQALANCPPL RKFFFNFSSL
     LQALKKPAIS ELYQKLLFNI WHKRKSGYIV PITMVQGIQT MNPTFQGYYQ HDVQEFLRFL
     ISQLHKELKE TILEIEEPLS IMTDESNSHQ KDSGFKITES CSNSNKGGNT DDLLLLLNEG
     NNQTLPTDGQ QEKNLLNKHH NACAMENLDK DDANFSSSNS AELHKQEALN EGFDSNLTSS
     PPRVSTIGYA MTSTIKKSVP LSFPKKKTEK TYRSIISDVF DGTIMSSVQC LACDSLSQRL
     ESFQDLSLPI PKRKNLAKLR QGVQMSQMKK GLFGIARQKA AYIKECIKSW FGISGVTLQD
     CLASYFRTEK LKGGNMYSCG ECKKLRKGVR FSKIKMLPEV LSLHMMRFRH NLKESTKINT
     HVSFPLEGLE LRPFLTKHSP CQVTTYDLIS LICHRGNVNS GHYIAYCRKD ANTWYQYDDH
     KVSEVSEATI QKEHAYILLY KKSSEAAHQV SNLLNLAEPN AQEVYISKQW LSKFQTFAEP
     GPISNTDFMC IHGGIPPHKV NYIEDLVVSV PQNTWAHLQK TYRGGPEVNH LHVCEVCHTE
     AEDLQNRRKL ELETFFRLNK EFQKKSPEVL HCINMQWMRR WERFVKAKDN DPPGLINNHN
     LTVKKSGRFS LIKGPNFAHI SKETRKYFHS IYGGGPQI
//