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Database: UniProt
Entry: A0A0M0J9G5_9EUKA
LinkDB: A0A0M0J9G5_9EUKA
Original site: A0A0M0J9G5_9EUKA 
ID   A0A0M0J9G5_9EUKA        Unreviewed;       635 AA.
AC   A0A0M0J9G5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
DE   Flags: Fragment;
GN   ORFNames=Ctob_002036 {ECO:0000313|EMBL:KOO22868.1};
OS   Chrysochromulina tobinii.
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC   Chrysochromulinaceae; Chrysochromulina.
OX   NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO22868.1, ECO:0000313|Proteomes:UP000037460};
RN   [1] {ECO:0000313|Proteomes:UP000037460}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX   PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA   Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA   Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA   Cattolico R.A.;
RT   "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT   Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT   Prymnesiales (Haptophyceae).";
RL   PLoS Genet. 11:e1005469-e1005469(2015).
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|RuleBase:RU366025};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|RuleBase:RU366025}.
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:KOO22868.1}.
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DR   EMBL; JWZX01003243; KOO22868.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M0J9G5; -.
DR   OrthoDB; 51419at2759; -.
DR   Proteomes; UP000037460; 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   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF702; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 47; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 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, ECO:0000313|EMBL:KOO22868.1};
KW   Protease {ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037460};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT   DOMAIN          109..517
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          354..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          566..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          613..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..589
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KOO22868.1"
SQ   SEQUENCE   635 AA;  65728 MW;  E918CD5EF440635B CRC64;
     VAEECNLVVG TFALCSNSFT LKLDDPGADA TKLLEIGCTQ KQRLRVEGIN GRIPEAAAST
     AGSGSSVAAQ ALGTVALWSA GRADGQQHVY GPLARGIASS AEVNADGFIG LINQGATCYL
     SSLVQSLFMT PQFRAAMYDL GAPTAGSGVI SRELQRVFVQ LQTSKAQAVD TKALTGSFGW
     TQADAFMQHD VQELLRVLFD ALETELEGSA QYEHIRRIYR GEWCDYVRCK TCGTTSSRPS
     AFDDVNLAIR TFDAAQTPIR SLAAAIEAFI EPETLEGDNA YHCEHCASKQ PALKGLRFTM
     LPPVLCLGLK RFDFDFAELR RVKLHHSVAV PAMLSASTFL EDRAVRQAKR KLAGDNFEAD
     SGEGGSSTDA VSSPEPEVSL ECNDGAAGGD ISNGDGGLTE GGAGDDGEPA SGEAAGGQAA
     SGKAASAVAS GEAASGEGGN STSSAADQYE LFSMLMHSGS ALAGHYFCFI KDLSSGTWYK
     FNDSSVSLAT DSQLQAAMGA TENGSAGSTY MVFYRRVDSA EPLVPPVNVP PGLQEASLAG
     PIEGFGHQSS SSSDAMMVGA AESSSTAYTS DAPGSAGTSS TSASSTDPVC GPSLIGPMPQ
     GVVWPEIGAC SSLATTSTNS GSSSEKGVVI GRRAR
//
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