ID   A0A452HM52_9SAUR        Unreviewed;       890 AA.
AC   A0A452HM52;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
OS   Gopherus agassizii (Agassiz's desert tortoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Gopherus.
OX   NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000016019.1, ECO:0000313|Proteomes:UP000291020};
RN   [1] {ECO:0000313|Proteomes:UP000291020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28562605;
RA   Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA   Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT   "The Agassiz's desert tortoise genome provides a resource for the
RT   conservation of a threatened species.";
RL   PLoS ONE 12:e0177708-e0177708(2017).
RN   [2] {ECO:0000313|Ensembl:ENSGAGP00000016019.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A452HM52; -.
DR   STRING; 38772.ENSGAGP00000016019; -.
DR   Ensembl; ENSGAGT00000018301.1; ENSGAGP00000016019.1; ENSGAGG00000012044.1.
DR   Proteomes; UP000291020; 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; 2.
DR   Gene3D; 3.30.2230.10; DUSP-like; 1.
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; IPR028135; Ub_USP-typ.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF29; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 11; 1.
DR   Pfam; PF06337; DUSP; 1.
DR   Pfam; PF14836; Ubiquitin_3; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00695; DUSP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 1.
DR   PROSITE; PS51283; DUSP; 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|RuleBase:RU366025};
KW   Protease {ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT   DOMAIN          1..114
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   DOMAIN          238..861
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          572..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          867..890
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   890 AA;  100885 MW;  95B108704D66B42E CRC64;
     MRLNSALDVA LGRGAGIRGW GPELQLGPSP PRYLLENHWY QQWKEYVESG DQNSSSFPGH
     INNSELFEDL ESFRLKERLV ESEEYVLVPE DVWNKLVSWY GLEHDQPPIE RKVVELPSTQ
     KVEVYPVELY LCQHNDLDSP VTAQFSRVNT IDSVLQEARR QFEVPPEDET RLWVKNSDGS
     CERLRNIHMT VLDACLSMGQ VVIMETRNKD GTWPSSRPHV MRNSVEDEEL YRGQPGVCGL
     TNLGNTCFMN SAFQCLSNVP PLTEYFLNNH YLGELNFSNP LGMKGEIAEA YADLVKQAWS
     GHHRAIVPRM FKTKVGHFAS QFLGYQQHDA QELLSFLLDG LHEDLNRVKR KEYVELRDAA
     GRPDEEVAEE AWRNHKRRND SIIVDIFHGL FKSTLVCPAC GKVSVTFDPF CYLSVPLPVS
     QERAMELFFV YMDPSRKPQQ HRVVVPKAGK VLDLCLALAK HTGVPAEQMM VADVFSHRFY
     KLYQVDEALS CILDRDDIFV YEVAGGLAEP GGALVLPVYL RERAPPRDGD PGYGVVLFGH
     PLLVSVPQAQ LSWDALYGLL LERLSRYVRC PESGSEEEEE SEEEDLYGPQ ANGLSEGEEE
     EEMLGEGPAS QAEGSSGGSG GPPTLSPPPT ANRRKRKCRH RRPLFTVRPV NANGTSERPA
     LPGEGFALHA QPYIAIDWDS NMKKQYYDEE EAEGYVKHEC MGHVQRRQPV KLRECVELFT
     TVETLEEENP WYCPTCKRHQ LATKKLDLWA LPEVLIIHLK RFSYTRLARE KLDTLVEFPI
     RDLDFSDFII KPRADVAPAP HKYDLIAVSN HYGSLRDGHY TTFARNKDSG HWFYFDDSSV
     SPVAEAQIES KAAYVLFYQR QDRICPPGTT PCPRPPDAGG GCCSDSMEVD
//