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Database: UniProt
Entry: A0A0M0JRG2_9EUKA
LinkDB: A0A0M0JRG2_9EUKA
Original site: A0A0M0JRG2_9EUKA 
ID   A0A0M0JRG2_9EUKA        Unreviewed;       837 AA.
AC   A0A0M0JRG2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Ubiquitin carboxyl-terminal hydrolase 26-like protein {ECO:0000313|EMBL:KOO28887.1};
GN   ORFNames=Ctob_004573 {ECO:0000313|EMBL:KOO28887.1};
OS   Chrysochromulina tobinii.
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC   Chrysochromulinaceae; Chrysochromulina.
OX   NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO28887.1, 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|ARBA:ARBA00000707};
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:KOO28887.1}.
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DR   EMBL; JWZX01002498; KOO28887.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M0JRG2; -.
DR   OrthoDB; 307371at2759; -.
DR   Proteomes; UP000037460; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd01795; Ubl_USP48; 1.
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; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR044743; Ubl_USP48.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF722; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 48; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KOO28887.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037460};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          83..429
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   DOMAIN          716..775
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   REGION          118..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   837 AA;  90685 MW;  7B4BADF900BDE5CC CRC64;
     MSGKKVRRDA MPMPQLSDAK ARQQYIYGLA TQAAAKKQKS AADPTDLQAV EAAAKKAAKD
     ADAKLLFGLE PRDKVRTDAT AGTGLRNLGA TCYMNSLLQC LHMNVGFRRG IYKWAGGAGA
     GGGSSGQPPP PEAAAAAAST GSSRRPEEVR ADEVCRQLQL LFANLQHSDS ACYDPAALTS
     ALSLDVSVQQ DASEFCKLLL SFLEEQLKLS PEPAIQTLVQ DHFRGSFCYH TQCCTCRTPS
     DSSSICFPFY ELDLNVRPTL QQALDEYIAV EHLDGSNQYE CIHCKGRRDA TRQIAIRQLP
     PVLCLQLKRF VYDPNKDAKK KSPAARWLTV NDELVTEEDF DPAKAATKPK PNGVTLLKQS
     APCDGRLFAS HEAYMLMYTR DDVIAEAQAT HAEVQAPATV REAVHAANVA LRAATEKYQD
     ALCAHTERLT ARQTLIDELR PILRSDGHDG RWIESRWLQA CLTLGPRGTT DELGPIRNQF
     IECCHGGAAD PKHVSTGAMK LISVAAWQKL LGLFGGGPEL LATGCVECAD AEWERRQLEM
     AKEAHKAALA VALNSASSSL TKHASVEANG GDGGVPHDDY YYVPRLTGSK WVRWLSEGQR
     DATRELFCPH DKLLRLEAHA RTIGAEAWGH LFALFPDSIP ILVEAVGRGD GDGRLVECAA
     CLVSECEREA AKADEKMSAK LSAKSEIASR SAQRQRLGRL LQEDGRLDPD VLRSKLSVRA
     SSSINVLNLK LRIYQATEWS PSQQRLFIDG DELLNDEQTL SDAGVLPNSF IHVYIDTSRV
     AEMPAIEEAF GSASGGKPRA PEDGFAGSAL VSASLGASRS AAAAGESDAS ANVMDLT
//
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