ID A0A2P6VSC6_9CHLO Unreviewed; 914 AA.
AC A0A2P6VSC6;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=g22 {ECO:0000313|EMBL:PSC77008.1};
GN ORFNames=C2E20_0022 {ECO:0000313|EMBL:PSC77008.1};
OS Micractinium conductrix.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Micractinium.
OX NCBI_TaxID=554055 {ECO:0000313|EMBL:PSC77008.1, ECO:0000313|Proteomes:UP000239649};
RN [1] {ECO:0000313|EMBL:PSC77008.1, ECO:0000313|Proteomes:UP000239649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 241.80 {ECO:0000313|EMBL:PSC77008.1,
RC ECO:0000313|Proteomes:UP000239649};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
CC -!- FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-terminal
CC Gly of ubiquitin. Involved in the processing of poly-ubiquitin
CC precursors as well as that of ubiquitinated proteins.
CC {ECO:0000256|RuleBase:RU366025}.
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|ARBA:ARBA00009085, 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:PSC77008.1}.
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DR EMBL; LHPF02000001; PSC77008.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6VSC6; -.
DR STRING; 554055.A0A2P6VSC6; -.
DR Proteomes; UP000239649; 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; cd02663; Peptidase_C19G; 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; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF733; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE-RELATED; 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:PSC77008.1};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000239649};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 22..418
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 139..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 98633 MW; 793BB9453165BDF1 CRC64;
MGASGSKPDK AVQELPDDEH YFGLENFGNT CYCNSVLQTL YFCRPFRERV LQYAAKLQAV
AAASKQPPPE NMLTCLADLF LQVSSQKKKC GFVSPRRFVS RVKAENALFS SYMHQDAHEF
WIWLLNDIGE VLEKEERAAQ AAARRASRDP SRASSRASSR ATSPTKGRSP TKGAGAGTGA
GAGAGRSPSL QLLSAAAAKA AAARNRPVRT WVHELFQGKL VNETRCLQCE TVTCREEDFY
DLSLEIDQNC SLTSCLRNFS STETLEGEEK FFCDKCGRLQ EAQKRMRLAR LPPVLCLHLK
RFKYIESIGR LKKLMHRVTF PWELKMINTT DDCPDADSSY ELFAVVVHMG AHPNHGHYVA
LVRTPGGQWV CFDDEQVNAV TEAQVQSVFG HTQDWQPVRE DQQGPHADHG YLLLYLRKED
AAAAAAVAAA VVKQQQQQQQ QQQQHRAAAS WEATERLASD ADELWDACDA QEIKASEREA
VLREAEALSQ CLIKLDAVLT EHMRPWAANA LPCDVLGVHD AMQAACIAIT ACARVAERLH
TSRREHYVIA SAATLLFDAG GHLLAAAQRF LQGGAVAADQ ATTQLRAAGF LLCHVLRPQP
EAAAAFAAST GKPEALLPWL QTVTHVLAKH TGCPPGEAEG EAASNLPFID YLRFVRHLLF
EPAYSRHAAA LAGPDRADQI AAFLLECCLP ALLRRAQQEP EAAVAAGQPV SKALLALRDV
FASSSLSAAL LRLIAQPRGA AVVPCLASLA RALPLHLPAV SSADLLLQSV QAEATVEKAR
LELRAVAVRH WHAWQAATSA LLAAAAPRGC DSTPVEVAAV NARLLGLRSL LATAEICPMM
VGRHFLEPCQ LLLQASVPGG PPATLLVSVL STSAGAAVRT KNARLAAAVA GSGMLRDGLE
AALQAGEAGA EALP
//
